Entry
stringlengths 6
10
| Entry Name
stringlengths 5
11
| Sequence
stringlengths 2
35.2k
| EC number
stringlengths 7
118
⌀ | Cofactor
stringlengths 38
1.77k
⌀ | Gene Ontology (biological process)
stringlengths 18
11.3k
⌀ | Gene Ontology (cellular component)
stringlengths 17
1.75k
⌀ | Gene Ontology (molecular function)
stringlengths 24
2.09k
⌀ | Pfam
stringlengths 8
232
⌀ | Gene3D
stringlengths 10
250
⌀ | Protein families
stringlengths 9
237
⌀ | Post-translational modification
stringlengths 16
8.52k
⌀ | Subcellular location [CC]
stringlengths 29
6.18k
⌀ | Catalytic activity
stringlengths 64
35.7k
⌀ | Kinetics
stringlengths 69
11.7k
⌀ | Pathway
stringlengths 27
908
⌀ | pH dependence
stringlengths 64
955
⌀ | Temperature dependence
stringlengths 70
1.16k
⌀ | Function [CC]
stringlengths 17
15.3k
⌀ | Organism
stringlengths 8
196
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G2IQQ5 | LIGJ_SPHSK | MMMIIDCHGHYTVLPKAHDEWREQQKAAFKAGQPAPPYPEISDDEIRETIEANQLRLIKERGADMTIFSPRASAMAPHVGDQSVAVPWAQACNNLIARVVDLFPETFAGVCMLPQSPEADMTSSIAELERCVNELGFIGCNLNPDPGGGHFKHPPLTDRFWYPFYEKMVELDVPAMIHVSGSCNPAMHATGAYYLAADTIAFMQLLQGNLFADFPTLRFIIPHGGGAVPYHWGRFRGLADMLKQPSLDTLLMNNVFFDTCVYHQPGINLLADVIDNKNILFGSEMVGAVRGIDPTTGHYFDDTKRYIDALDISDQERHAIFEGNTRRVFPRLDAKLKARGL | 4.2.1.- | COFACTOR: Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000269|PubMed:30207699}; Note=Binds 1 zinc ion per subunit. The metal center contained within the active site of LigJ is not used to activate the water molecule but is utilized to activate the substrate via polarization of the carbonyl oxygen. {ECO:0000269|PubMed:30207699}; | heterocycle metabolic process [GO:0046483]; lignin catabolic process [GO:0046274] | cytosol [GO:0005829] | carboxy-lyase activity [GO:0016831]; hydrolase activity [GO:0016787]; metal ion binding [GO:0046872] | PF04909; | 3.20.20.140; | Metallo-dependent hydrolases superfamily | null | null | CATALYTIC ACTIVITY: Reaction=(3Z)-2-oxo-4-carboxy-3-hexenedioate + H2O = (2S)-2-hydroxy-4-oxobutane-1,2,4-tricarboxylate; Xref=Rhea:RHEA:58508, ChEBI:CHEBI:15377, ChEBI:CHEBI:142690, ChEBI:CHEBI:142706; Evidence={ECO:0000269|PubMed:29658701, ECO:0000269|PubMed:30207699}; | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=9.8 uM for (3Z)-2-keto-4-carboxy-3-hexenedioate (at pH 8.0) {ECO:0000269|PubMed:30207699}; Note=kcat is 25.6 sec(-1) (at pH 8.0). {ECO:0000269|PubMed:30207699}; | PATHWAY: Secondary metabolite metabolism; lignin degradation. {ECO:0000269|PubMed:11092855, ECO:0000305|PubMed:29658701}. | null | null | FUNCTION: Contributes to the degradation of lignin at the level of the protocatechuate 4,5-cleavage pathway. Catalyzes the hydration of the double bond of (3Z)-2-keto-4-carboxy-3-hexenedioate (KCH) to (4S)-4-carboxy-4-hydroxy-2-oxoadipate (CHA, also named (2S)-2-hydroxy-4-oxobutane-1,2,4-tricarboxylate) (PubMed:29658701, PubMed:30207699). Is involved in the catabolism of both vanillate and syringate (PubMed:11092855). {ECO:0000269|PubMed:11092855, ECO:0000269|PubMed:29658701, ECO:0000269|PubMed:30207699}. | Sphingobium sp. (strain NBRC 103272 / SYK-6) |
G2IQQ8 | LIGK_SPHSK | MRGAAMGVVVQNIERAPLEVIDGLAACGVATVHEAQGRTGLLASYMRPIYRGARVAGSALTISAPPGDNWMVHVAIEQLKAGDILLLAPTSPCEDGYFGDLLATSAQARGCRGLVIDAGVRDVRDLTEMNFPVWSKAIYAQGTVKNTLGSVNVPVVCANALVNPGDVIVADDDGVCVVPLANAEKVLEAARAREANEGDKREKMANGVLGLDLYKMRERLEKEGLKYV | 4.1.1.112; 4.1.3.17 | COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000269|PubMed:12486039}; | lignin catabolic process [GO:0046274]; protocatechuate catabolic process, meta-cleavage [GO:0019617] | null | 4-hydroxy-4-methyl-2-oxoglutarate aldolase activity [GO:0047443]; metal ion binding [GO:0046872]; oxaloacetate decarboxylase activity [GO:0008948] | PF03737; | 3.50.30.40; | LigK/PcmE family | null | null | CATALYTIC ACTIVITY: Reaction=4-hydroxy-4-methyl-2-oxoglutarate = 2 pyruvate; Xref=Rhea:RHEA:22748, ChEBI:CHEBI:15361, ChEBI:CHEBI:58276; EC=4.1.3.17; Evidence={ECO:0000269|PubMed:29658701}; CATALYTIC ACTIVITY: Reaction=2-hydroxy-4-oxobutane-1,2,4-tricarboxylate = oxaloacetate + pyruvate; Xref=Rhea:RHEA:28935, ChEBI:CHEBI:15361, ChEBI:CHEBI:16452, ChEBI:CHEBI:58075; EC=4.1.3.17; Evidence={ECO:0000269|PubMed:12486039}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:28936; Evidence={ECO:0000269|PubMed:12486039}; CATALYTIC ACTIVITY: Reaction=H(+) + oxaloacetate = CO2 + pyruvate; Xref=Rhea:RHEA:15641, ChEBI:CHEBI:15361, ChEBI:CHEBI:15378, ChEBI:CHEBI:16452, ChEBI:CHEBI:16526; EC=4.1.1.112; Evidence={ECO:0000269|PubMed:12486039}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:15642; Evidence={ECO:0000269|PubMed:12486039}; | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=11.2 uM for 2-hydroxy-4-oxobutane-1,2,4-tricarboxylate {ECO:0000269|PubMed:12486039}; KM=136 uM for oxaloacetate {ECO:0000269|PubMed:12486039}; Vmax=265 umol/min/mg enzyme for CHA aldol cleavage {ECO:0000269|PubMed:12486039}; Vmax=13.2 umol/min/mg enzyme for oxaloacetate decarboxylation {ECO:0000269|PubMed:12486039}; | PATHWAY: Secondary metabolite metabolism; lignin degradation. {ECO:0000305|PubMed:12486039}. | BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 8.0 for CHA aldolase activity, and 7.0 for oxaloacetate decarboxylase activity. {ECO:0000269|PubMed:12486039}; | null | FUNCTION: Contributes to the degradation of lignin, being involved in the final step of the protocatechuate 4,5-cleavage pathway. Catalyzes the conversion of 4-carboxy-4-hydroxy-2-oxoadipate (CHA, also named 2-hydroxy-4-oxobutane-1,2,4-tricarboxylate) to pyruvate and oxaloacetate but also the decarboxylation of oxaloacetate to pyruvate and CO2. Is essential for catabolism and utilization of vanillate and syringate (PubMed:12486039). Is also able to catalyze the formation of 4-hydroxy-4-methyl-2-oxoglutarate (HMG) from two molecules of pyruvate (PubMed:29658701). {ECO:0000269|PubMed:12486039, ECO:0000269|PubMed:29658701}. | Sphingobium sp. (strain NBRC 103272 / SYK-6) |
G2IQS7 | LIGM_SPHSK | MSAPTNLEQVLAAGGNTVEMLRNSQIGAYVYPVVAPEFSNWRTEQWAWRNSAVLFDQTHHMVDLYIRGKDALKLLSDTMINSPKGWEPNKAKQYVPVTPYGHVIGDGIIFYLAEEEFVYVGRAPAANWLMYHAQTGGYNVDIVHDDRSPSRPMGKPVQRISWRFQIQGPKAWDVIEKLHGGTLEKLKFFNMAEMNIAGMKIRTLRHGMAGAPGLEIWGPYETQEKARNAILEAGKEFGLIPVGSRAYPSNTLESGWIPSPLPAIYTGDKLKAYREWLPANSYEASGAIGGSFVSSNIEDYYVNPYEIGYGPFVKFDHDFIGRDALEAIDPATQRKKVTLAWNGDDMAKIYASLFDTEADAHYKFFDLPLANYANTNADAVLDAAGNVVGMSMFTGYSYNEKRALSLATIDHEIPVGTELTVLWGEENGGTRKTTVEPHKQMAVRAVVSPVPYSVTARETYEGGWRKAAVTA | 2.1.1.341 | null | lignin catabolic process [GO:0046274]; methylation [GO:0032259] | cytosol [GO:0005829] | methyltransferase activity [GO:0008168] | PF01571; | null | GcvT family | null | null | CATALYTIC ACTIVITY: Reaction=(6S)-5,6,7,8-tetrahydrofolate + vanillate = (6S)-5-methyl-5,6,7,8-tetrahydrofolate + 3,4-dihydroxybenzoate; Xref=Rhea:RHEA:52276, ChEBI:CHEBI:16632, ChEBI:CHEBI:18608, ChEBI:CHEBI:36241, ChEBI:CHEBI:57453; EC=2.1.1.341; Evidence={ECO:0000269|PubMed:15743951, ECO:0000269|PubMed:28373573, ECO:0000269|PubMed:28429420}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:52277; Evidence={ECO:0000269|PubMed:15743951, ECO:0000269|PubMed:28373573, ECO:0000269|PubMed:28429420}; CATALYTIC ACTIVITY: Reaction=(6S)-5,6,7,8-tetrahydrofolate + 3-O-methylgallate = (6S)-5-methyl-5,6,7,8-tetrahydrofolate + 3,4,5-trihydroxybenzoate; Xref=Rhea:RHEA:52280, ChEBI:CHEBI:16918, ChEBI:CHEBI:18608, ChEBI:CHEBI:19950, ChEBI:CHEBI:57453; EC=2.1.1.341; Evidence={ECO:0000269|PubMed:15743951}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:52281; Evidence={ECO:0000269|PubMed:15743951}; | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=0.63 mM for vanillate {ECO:0000269|PubMed:28373573}; KM=0.72 mM for tetrahydrofolate {ECO:0000269|PubMed:28373573}; Note=kcat is 5.76 sec(-1) with vanillate as substrate. {ECO:0000269|PubMed:28373573}; | PATHWAY: Secondary metabolite metabolism; lignin degradation. {ECO:0000305|PubMed:15743951}. | BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 8 with vanillate as substrate. {ECO:0000269|PubMed:28373573}; | BIOPHYSICOCHEMICAL PROPERTIES: Temperature dependence: Optimum temperature is 30 degrees Celsius with vanillate as substrate. {ECO:0000269|PubMed:28373573}; | FUNCTION: Involved in the catabolism of vanillate and syringate. Catalyzes the transfer of a methyl moiety from vanillate or 3-O-methylgallate (3MGA) to tetrahydrofolate, forming protocatechuate (PCA) or gallate, respectively, and methyl-tetrahydrofolate. Has similar activities with both substrates (PubMed:15743951). Cannot use syringate (PubMed:15743951). Uses an ordered, sequential kinetic mechanism (PubMed:28373573). {ECO:0000269|PubMed:15743951, ECO:0000269|PubMed:28373573}. | Sphingobium sp. (strain NBRC 103272 / SYK-6) |
G2NFJ9 | LAM55_STREK | MHVPPTDPARSAPPASPHRRRRPKALGLTALAAAMLMAVPTTQAAFGSDVRPAAAQEVVGGGDLGPNVLVFDPSTPDIQGKVDEVFRKQESNQFGTDRYALMFKPGTYNDINAQIGFYTSIAGLGLNPDDTTFNGDVTVDAGWFDGNATQNFWRSAENLALNPVNGTNRWAVSQAAPFRRMHVKGGLNLAPDGYGWASGGYIADSKIDGEVGPYSQQQWYTRDSSVGGWGNGVWNMTFSGVEGAPAQSFPEPPYTTLETTPVSREKPFLYLDGDDYKVFVPAKRTNARGTSWGNGTPEGESLPLDQFYVVKPGATAETINAAVDQGLHLLFTPGVYHVDQPIEIDRANTVALGLGLATIIPDNGVTALKVGDVDGVKVAGLLVDAGPVNSETLVEVGSDGASGDHAANPTSLQDVFVRIGGAGPGKATTSIVVNSNDTIIDHTWVWRADHGEGVGWETNRADYGVHVKGDNVLATGLFVEHFNKYDVQWSGENGKTIFYQNEKAYDAPDQAAIQNGDIKGYAAYKVDDSVTTHEGWGMGSYCYFNVNPDIRQQHGFQAPVKPGVKFHDLLVVSLGGKGQYEHVINDIGDPTSGDTTIPSQVVSFP | 3.2.1.58 | null | glucan catabolic process [GO:0009251] | extracellular region [GO:0005576] | glucan exo-1,3-beta-glucosidase activity [GO:0004338] | null | 2.160.20.10; | Glycosyl hydrolase 55 family | null | SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:23301151}. | CATALYTIC ACTIVITY: Reaction=Successive hydrolysis of beta-D-glucose units from the non-reducing ends of (1->3)-beta-D-glucans, releasing alpha-glucose.; EC=3.2.1.58; Evidence={ECO:0000269|PubMed:25752603}; | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=0.93 mg/ml for L.digitata soluble laminarin (at pH 6 and 40 degrees Celsius) {ECO:0000269|PubMed:25752603}; Vmax=128 umol/min/mg enzyme with L.digitata soluble laminarin as substrate (at pH 6 and 40 degrees Celsius) {ECO:0000269|PubMed:25752603}; Note=kcat is 138 sec(-1) with L.digitata soluble laminarin as substrate (at pH 6 and 40 degrees Celsius). {ECO:0000269|PubMed:25752603}; | null | BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 6. Maintains 70% or more of the maximal activity from pH 6.0 to 9.0. {ECO:0000269|PubMed:25752603}; | BIOPHYSICOCHEMICAL PROPERTIES: Temperature dependence: Optimum temperature is 50 degrees Celsius. Maintains 70% or more of the maximal activity from 35 to 65 degrees Celsius. {ECO:0000269|PubMed:25752603}; | FUNCTION: Exo-beta-1,3-glucanase that specifically hydrolyzes laminarin and laminarioligosaccharides, producing glucose and laminaribiose as end products. {ECO:0000269|PubMed:25752603}. | Streptomyces sp. (strain SirexAA-E / ActE) |
G2Q0E2 | PEX10_THET4 | MATQPPPARPPPPLTSSPYPYAAAPDIIRAHQKDAYFQGVLANRLSDLHRRLRGARSAHAWAAETRTFAAALYLCLTTLLGNRTLGEEYCDLVQVEEAPSKLFASSSSKAADDHIYENGLGGGGDGGPLLPSLPRRAGYILTAIVLPHLASRALPSVRSAIRKRLQSRLATLSRRRQQTGTKSGSGRGGRGGGGGITEYRVLRYLLTHLTPLTSGAHFRAATLAVFYFTGAYYELSKWVWGLRYVFTTRAGRVVDDDHNRHHHSPQHGGGNGGRAGYEVLGVLLVVQMAVRAWLHVREQLSSGSVAGGGGEEEEDGEDGFRERTAFGPGTNVDVSLDEHAFTSNNELLGGGGGGGGSSSQRSLGEIGAMAHTPVLKAGRARYDLGTSDKVMGWIKGAQQRKCTLCLEELKDPAATQCGHVFCWACIGDWVREKPECPLCRREAMVQHILPLRAA | 2.3.2.27 | null | protein import into peroxisome matrix, receptor recycling [GO:0016562]; protein ubiquitination [GO:0016567] | peroxisomal membrane [GO:0005778] | transferase activity [GO:0016740]; zinc ion binding [GO:0008270] | PF04757;PF13923; | 3.30.40.10; | Pex2/pex10/pex12 family | null | SUBCELLULAR LOCATION: Peroxisome membrane {ECO:0000250|UniProtKB:Q05568}; Multi-pass membrane protein {ECO:0000269|PubMed:35768507}. | CATALYTIC ACTIVITY: Reaction=S-ubiquitinyl-[E2 ubiquitin-conjugating enzyme]-L-cysteine + [acceptor protein]-L-lysine = [E2 ubiquitin-conjugating enzyme]-L-cysteine + N(6)-ubiquitinyl-[acceptor protein]-L-lysine.; EC=2.3.2.27; Evidence={ECO:0000250|UniProtKB:Q05568}; | null | PATHWAY: Protein modification; protein ubiquitination. {ECO:0000250|UniProtKB:Q05568}. | null | null | FUNCTION: E3 ubiquitin-protein ligase component of a retrotranslocation channel required for peroxisome organization by mediating export of the PEX5 receptor from peroxisomes to the cytosol, thereby promoting PEX5 recycling (By similarity). The retrotranslocation channel is composed of PEX2, PEX10 and PEX12; each subunit contributing transmembrane segments that coassemble into an open channel that specifically allows the passage of PEX5 through the peroxisomal membrane (By similarity). PEX10 also regulates PEX5 recycling by acting as a E3 ubiquitin-protein ligase (By similarity). When PEX5 recycling is compromised, PEX10 catalyzes polyubiquitination of PEX5 during its passage through the retrotranslocation channel, leading to its degradation (By similarity). {ECO:0000250|UniProtKB:Q05568}. | Thermothelomyces thermophilus (strain ATCC 42464 / BCRC 31852 / DSM 1799) (Sporotrichum thermophile) |
G2Q1C9 | PEX2_THET4 | MSDSDPKPTAAKGAAPTSIPNSTRNPNPTPPNPNPNPNPISTPAPTPTATPSPPIASSSNNGNNSTRSTNIDTNNNTNNAFFQAQQRIAARREAREAAAAARQATQQSASRLRARIAASQSPLLRRLGTSTLSLWDTLTSREGTRPAFRVGQVDAELLDEELVELLRGQVREALRYVGGGGGGGGGGGGGGVGSGVAQDWEAEISLALRAVLFKLTVWDHDATYGAALQNLKYTDARRDGPALAPPSRWQKALYGLVTVGGRYLWAKWEDWLLEQDDGFEGPSPRVKRLARWTSALSTLHASAALVSFLVFLLHGRYRTLLDRLLRMRLAPPTSQVSREVSFEYLNRQLVWHAFTEFLLFVLPLVGINRWRRWLARTWRRTKKIMTADADGGAGDKKGEYSFLPERTCAICYRDQNSASSETELLAAASGGVVGSAQTDITNPYEAIPCGCTYCFVCLATRIEREEGEGWPCLRCGELIKECKPWNGDVLEEPQVKSSPATTKTVVFADDVKAPSDHEEEENEEEEEQQGELGENEGESSQVLVEADPDGGLNDLRPETPSVSSDQADDSRGSESEDYEAEEDGLDEDPES | 2.3.2.36 | null | protein import into peroxisome matrix, receptor recycling [GO:0016562]; protein ubiquitination [GO:0016567] | peroxisomal membrane [GO:0005778] | transferase activity [GO:0016740]; zinc ion binding [GO:0008270] | PF04757; | null | Pex2/pex10/pex12 family | null | SUBCELLULAR LOCATION: Peroxisome membrane {ECO:0000250|UniProtKB:P32800}; Multi-pass membrane protein {ECO:0000269|PubMed:35768507}. | CATALYTIC ACTIVITY: Reaction=[E2 ubiquitin-conjugating enzyme]-S-ubiquitinyl-L-cysteine + [acceptor protein]-L-cysteine = [E2 ubiquitin-conjugating enzyme]-L-cysteine + [acceptor protein]-S-ubiquitinyl-L-cysteine.; EC=2.3.2.36; Evidence={ECO:0000250|UniProtKB:P32800}; | null | PATHWAY: Protein modification; protein ubiquitination. {ECO:0000250|UniProtKB:P32800}. | null | null | FUNCTION: E3 ubiquitin-protein ligase component of a retrotranslocation channel required for peroxisome organization by mediating export of the PEX5 receptor from peroxisomes to the cytosol, thereby promoting PEX5 recycling (By similarity). The retrotranslocation channel is composed of PEX2, PEX10 and PEX12; each subunit contributing transmembrane segments that coassemble into an open channel that specifically allows the passage of PEX5 through the peroxisomal membrane (By similarity). PEX2 also regulates peroxisome organization by acting as a E3 ubiquitin-protein ligase (By similarity). PEX2 ubiquitinates PEX5 during its passage through the retrotranslocation channel: catalyzes monoubiquitination of PEX5 at 'Cys-6', a modification that acts as a signal for PEX5 extraction into the cytosol (By similarity). {ECO:0000250|UniProtKB:P32800}. | Thermothelomyces thermophilus (strain ATCC 42464 / BCRC 31852 / DSM 1799) (Sporotrichum thermophile) |
G2Q9A5 | MYCA_THET4 | MVQTPRQKKFGNEPIAIIGSACRFPGAASTPSKLWELLRKPKDLLTKIPPNRFNADSFYHPDGAHHGASNVTESYFLEEDPRLFDAAFFNVKPVEAHSIDPQHRMLLEVVYESLEAAGQSIEGLAKSQTGVFVGLMCADFSDHILRDLDAIPTYMATGTARSLISNRISYFFDWHGPSMTIDTACSSSLFAVHQAVQLLRSGDSDLAVAAGSNLILGPELYIGESKLKMLSPTGRSRMWDADADGYARGEGVAAVILKRLSDAIRDGDHIESIIRESGINSDGRTKGLTMPNELAQADLIVRTYQKAGLDPTKEEERCQYFEAHGTGTEAGDCREAEGISRAFFGYQGGNEGPAPPSQSEKLYVGSIKTVVGHTEGTAGLAGLLKASLAIQHSTIPPNMLFERLSPKVAPFYKGVEIATEAKPWPKASDVRRASVNSFGFGGANAHVILENYEPPAVAAAGTGAGAGDAASQTSFTPFVFSAASETALEGVLEAYAAHLRENPDLPLRDLSYTLHSRRSALGVRAALPAVASTQQLANSISDHLELARAGRNDKSAGQGASIGSRPIAATPRLLGVFTGQGAQWAAMGKELIQGSAFVRDRIKSLESALSDLPASARASWSLTDELLADAASSRLGEALLAQPLCTAVQIVLVDLLREAGIEFAAVVGHSSGEIAAAYAARIISAEEAIKIAYYRGLCVEEHVKTEGAMMAVGTSYEDATELCNLDAFSGRLGIAACNSPSSVTLSGDAAAIREAKDILDDEKKFARPLKVNKAYHSHHMAACSAPYKQALEACNIEPRQLAEEEGGCVWYSSVYPGTAMGTTAAHIEDLKGEYWKDNMLRPVLFAQALETAIERNEDSPFNLVIEVGPHPALKGPASETLTALYGKKQLPLPPYTGTLSRGSGDIAALSVTLGTAWSRFGSPFVNFAQYEALLTGEPRSARKVVPNLPTYKWDHDKVFWHDTRLSRAMRNRKELPNPLLGRRIPDGVTDEMRWRNIIRPSELPWISGHQLQGQMVYPAAAYLSTAIEACAFLAEGSVVESVEIRDFDLGKALVFDGNTEQTGVETLFSLSNIVKKGPKQITANFAFHAALGADADVLSRLGSGRVIVTLAGTGTGAGTGRLLLPPQRAPEPADTAEVREDEFYASLEKLGYEYTNDFRALSGMRRKLDHGSAYVRVPGHELAADAVLVHPALLDCALQAIFLAYWYPNDGSLDQLQVPTGIASLTVNTSLCRQDLAEGVRLPLESFLTEDPLSTATIGGDVEVYGRDGRTPLIQVQGVRITPLATRTGQADRQLFMENVWGPGAPDGTLAADNRAGAADFELASDLERLTIYFMRKLVRDIPPSQRQGLEWHHEALFDFVEHVLEQTANGRQRFCKPEWLDDTWESISHIRAKHPDSIEVELTHAVGENLAAAVRGETQILQHMFKDNLLNRYYVEALGIRETTAFLARTVAQIVHRYPHMDILEIGAGTGGATKAIFREIGRTFSSYTYTDISTGFFEKAQEVFAATADKMIFRALDIEKDVVEQGYREGAYDLIIGSLVLHATKSLDKTMRATRRLLKPGGYLVLLELTNLDVLRTGFAMSGLPGWWLGRDDGRRYSPCATSARWHQVLLGAGFSGIDTITPEVDVLPRPFSVIVSQAVEPRVNLLREPLSHPAESNASAADGGELVIVGGQSLATVILIDSVLDLTRHFGFAVTRLSSLDEFDAAAVSPTALVLNLAELDQPVFSNLTGETMRGLQSMLDYQRTILWVTQGCRAEQPYMSMSVGLGRTVALEAPGVKLQFLDLDISRKPNSKLVAEALIRLRFTRDEGSTRGILYSTEQELVEDDGRILVPRLLPIRPANERYNSSKRKITKLTEVGAESPALVLASTDAGYAVYEGASDDARAGASDDTAIIRVTASTLLPVIGNLYGVLGQEKDSGSWVLGLSSTNGSHVAVPRGQVRLVGDAILKEEAQQQQRLLLLALLAVEAQSSQILSAVPRDSKLLVNEPPAGLAGSLVRRAAERGTTVVFTASTTDAADLGLPHGHPVVSLSPLSSKRAVRAALPADVALFLDCSAEPEGVGLGSLIAACVPPSGQSIKLAELGEKLRQQPTLVDAPPSDTELASLPTLVDWSSGDKVPVSLQSVDSLIRFDGAKTYVLFGLTSDLGRSLVDWMASHGARNVVMTSRRPNIDPKWLEERRARGIRIQAFANDITDPAAVEDLVNSIRRSFPPIAGIMHGAMVLEDVPFSEMSLEIMNKVVRPKVMGTIHLDRLFQDEQLDFFVFFSSLASASGNRGQSNYSAANMYMTAKTFERRRKGLAASVLHLGAVMGIGYVMREASEIVFPAIRRAGFQWMDERAFRQCVAEAILAGRPDSGRSPEIVTGLRVINVDEEEPAPWMDNPRFQHCIVRGGTDSGAKKNQGGAAAGVKTRLLEAATPEEVLDIIRDSFLQKLQIMLQTELQTDDERANILAANAEDTGIDSLVAVEIRSWFQKEMDVDVPVLKILGGATMADLVAFAHEKLPEGLTPNLGNESAAAAAAAAAERSQSRVEITPAPDAVDTSRTSTTVFSAPPTLDPASSSTGSDHPTSVTSSGHTTPAHELETGLSPPSAPPCAPREQDVERTAPMSLGQSRFWFLRSYIEDQTTFNISFSVRLKGPLQVDKLESAIQTLGHRHQALRTAFVARPGQLLPDQAVLKRSLLRLEKRQIKEAAEASEAFEAMKNYVFAIERGESMRLVLLSLSPSDHFLVVGYHHINMDGASLEVFMADLMKLYTGRPLAPRPFQYPDFAAQQQLEVQQGKMDRDIAWWQDQLAGAALFRLLGTGDLCIGMADANRFEGDLASSVGMYLNLLPLRFRPSGDRTFRDTLKDVRRTAYAAMAHSHVPFDLVLNNLKIQRSTLHSPLFQAFINYRAGVAEKRSLGAVEGEGEQYHFGRSAYDISLDIMENPNSDPRLMFLVQEQLYSEHEANILADTYMHLLDLFARKPDSTLGSAPAFAPETAEEAIRLGRGNPVVSDWPQTIVHRVDDIIQRNPDTIAVREALGGRVWNYRQLRDRVGAIARALLAAGVTGGSRVALFQEPGFDWVSSLLAVMRVGAVFVPIDPGTPVERLAVIAAAARPAVALSHDATESAQEAALAVIRDAGGARVVNVSRGEGEGEGDVAGAGAPANLAQPDEAAVIFFTSGTTGVPKGAIVPHRGITNFMEHTCDIRGPEVVLFHSALGFDLAMWQCFSGLAHGGTLVVAPRSMRGDPVAITGLMAKEKITCTGATPSEYHTWIQYGFSKLAQSTSWRIAMTGGEQCTPKLVDDFRSLRLPGLRLWNCYGPSEVTVGSNQAEIPLSEPPQAPVTVGKAMPNRSVYILDDRLEPVCAGAPGEVVIGGVGVGLGYLGNDHLTAEKFVPDPFAPAGGSAKMYRTGDRGRLTRDGELEILGRIDGDSQIKLRGIRIEMQDVEQAILRSADGALASVCVTARGEPPTLVAHAVFRPDAPVPRRDRDAFLRRLASSLPLPQYMHPAVIVEIPSMPLNLHGKLDRRAVQELPTRVVAAKEEEEEKRPNGSSAAPLTQQELQLRSRVWERVIPEDVLSLYTVDRDTDFFHVGGNSMLLVEVQRRVKDEFGANLTIMRLFENSTLGAMAAAVHDAALESAGVDAAIDWEDETALTKDLADAVPSPEERAAAGRRRLDNNGPGGKVVVILTGATGFIGRELLARLLSSPDVAEVRCIAVRDPSRLADVVESNPGRVSVHAGDLTSVEETVGEEDEQRLFADAHAVIHCGADVSFLKTYATLRRANVGSTKALARLALRHGLDFHYVSTAATGRLLLVADPSSSPTARGDVFGEESVAAYPPPPGWLDHYVASKWASEAFLERAAARLGLRVWVHRPTSVTGPGAGETDVMSTVMRFAKKLRAVPVSSRWRGSLDFVPVETVADGIVGAVIRGGREHQQQQQQQETTPEEAGSVVPVKFLHHSGGLVIPIERLQSHLEEEDGVEYRTVPLGQWIEMAVAEGLNVLVAAYLASVDEMDTDIVFQAYVKG | 2.3.1.-; 6.3.2.- | null | amide biosynthetic process [GO:0043604]; fatty acid biosynthetic process [GO:0006633]; heterocycle biosynthetic process [GO:0018130]; methylation [GO:0032259]; organic cyclic compound biosynthetic process [GO:1901362]; organonitrogen compound biosynthetic process [GO:1901566]; toxin biosynthetic process [GO:0009403] | null | 3-oxoacyl-[acyl-carrier-protein] synthase activity [GO:0004315]; fatty acid synthase activity [GO:0004312]; isomerase activity [GO:0016853]; ligase activity [GO:0016874]; methyltransferase activity [GO:0008168]; oxidoreductase activity [GO:0016491]; phosphopantetheine binding [GO:0031177] | PF00698;PF00501;PF00668;PF16197;PF00109;PF02801;PF08659;PF08242;PF07993;PF21089;PF00550;PF14765; | 3.30.300.30;3.40.47.10;1.10.1200.10;3.30.559.10;3.40.366.10;3.40.50.12780;3.40.50.720;3.30.559.30;3.10.129.110;3.40.50.150; | NRP synthetase family | null | null | CATALYTIC ACTIVITY: Reaction=ATP + 12 H(+) + L-leucine + 8 malonyl-CoA + 9 NADPH + 4 S-adenosyl-L-methionine = (5S)-5-(2-methylpropyl)-3-[(2E,6R,8E,10E,12E)-6,8,10,12-tetramethyltetradeca-2,8,10,12-tetraenoyl]-2,5-dihydro-1H-pyrrol-2-one + AMP + 8 CO2 + 8 CoA + diphosphate + 7 H2O + 9 NADP(+) + 4 S-adenosyl-L-homocysteine; Xref=Rhea:RHEA:67288, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:16526, ChEBI:CHEBI:30616, ChEBI:CHEBI:33019, ChEBI:CHEBI:57287, ChEBI:CHEBI:57384, ChEBI:CHEBI:57427, ChEBI:CHEBI:57783, ChEBI:CHEBI:57856, ChEBI:CHEBI:58349, ChEBI:CHEBI:59789, ChEBI:CHEBI:169930, ChEBI:CHEBI:456215; Evidence={ECO:0000269|PubMed:27960349}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:67289; Evidence={ECO:0000269|PubMed:27960349}; | null | PATHWAY: Mycotoxin biosynthesis. {ECO:0000269|PubMed:27960349}. | null | null | FUNCTION: Hybrid PKS-NRPS synthetase; part of the gene cluster that mediates the biosynthesis of myceliothermophins, mycotoxins that contain a trans-fused decalin ring system connected to a conjugated 3-pyrrolin-2-one moiety and that have potential anti-tumor properties (PubMed:27960349). The polyketide synthase module (PKS) of the PKS-NRPS mycA is responsible for the synthesis of the octaketide backbone (PubMed:27960349). The downstream nonribosomal peptide synthetase (NRPS) module then amidates the carboxyl end of the octaketide with a leucine (PubMed:27960349). A reductase-like domain (R) at the C-terminus catalyzes the reductive release of the polyketide-amino acid intermediate (PubMed:27960349). Because mycA lacks a designated enoylreductase (ER) domain, the required activity is provided the enoyl reductase mycC (PubMed:27960349). Following mycA-catalyzed construction and release of aminoacyl polyketide aldehyde, Knoevenagel condensation yields the expected ketone (PubMed:27960349). This C18 keto acyclic precursor is the substrate of the Diels-Alderase mycB, that catalyzes the Diels-Alder cycloaddition to produce myceliothermophin E (PubMed:27960349). A yet unknown oxygenase involved in the production of myceliothermophin A, via substitution with a hydroxyl group at the C21, has still to be identified (PubMed:27960349). {ECO:0000269|PubMed:27960349}. | Thermothelomyces thermophilus (strain ATCC 42464 / BCRC 31852 / DSM 1799) (Sporotrichum thermophile) |
G2Q9T3 | LP9H_THET4 | MSKASALLAGLTGAALVAAHGHVSHIVVNGVYYRNYDPTTDWYQPNPPTVIGWTAADQDNGFVEPNSFGTPDIICHKSATPGGGHATVAAGDKINIVWTPEWPESHIGPVIDYLAACNGDCETVDKSSLRWFKIDGAGYDKAAGRWAADALRANGNSWLVQIPSDLKAGNYVLRHEIIALHGAQSPNGAQAYPQCINLRVTGGGSNLPSGVAGTSLYKATDPGILFNPYVSSPDYTVPGPALIAGAASSIAQSTSVATATGTATVPGGGGANPTATTTAATSAAPSTTLRTTTTSAAQTTAPPSGDVQTKYGQCGGNGWTGPTVCAPGSSCSVLNEWYSQCL | 3.2.1.4 | COFACTOR: Name=Cu(2+); Xref=ChEBI:CHEBI:29036; Evidence={ECO:0000250|UniProtKB:Q4WP32}; Note=Binds 1 copper ion per subunit. {ECO:0000250|UniProtKB:Q4WP32}; | cellulose catabolic process [GO:0030245] | extracellular region [GO:0005576] | cellulose binding [GO:0030248]; hydrolase activity, acting on glycosyl bonds [GO:0016798]; metal ion binding [GO:0046872]; oxidoreductase activity [GO:0016491] | PF03443;PF00734; | 2.70.50.70; | Polysaccharide monooxygenase AA9 family | null | SUBCELLULAR LOCATION: Secreted {ECO:0000305|PubMed:22342036}. | CATALYTIC ACTIVITY: Reaction=Endohydrolysis of (1->4)-beta-D-glucosidic linkages in cellulose, lichenin and cereal beta-D-glucans.; EC=3.2.1.4; Evidence={ECO:0000269|PubMed:22342036, ECO:0000269|PubMed:35450635}; | null | null | BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 8.0. {ECO:0000269|PubMed:22342036}; | BIOPHYSICOCHEMICAL PROPERTIES: Temperature dependence: Optimum temperature is 65 degrees Celsius. {ECO:0000269|PubMed:22342036}; | FUNCTION: Lytic polysaccharide monooxygenase (LMPO) that depolymerizes crystalline and amorphous polysaccharides via the oxidation of scissile alpha- or beta-(1-4)-glycosidic bonds, yielding C1 or C4 oxidation products (PubMed:22342036, PubMed:35450635). Catalysis by LPMOs requires the reduction of the active-site copper from Cu(II) to Cu(I) by a reducing agent and H(2)O(2) or O(2) as a cosubstrate (Probable). Hydrolyzes weakly barley beta-glucan, carboxymethyl cellulose, lichenan, wheat arabinoxylan and birchwood xylan (PubMed:22342036, PubMed:35450635). Stimulates the hydrolysis of lignocellulosic substrates (such as hydrothermal pretreated wheat straw or steam-pretreated spruce), when combined with other cellulolytic enzymes (PubMed:22342036). {ECO:0000269|PubMed:22342036, ECO:0000269|PubMed:35450635, ECO:0000305|PubMed:35450635}. | Thermothelomyces thermophilus (strain ATCC 42464 / BCRC 31852 / DSM 1799) (Sporotrichum thermophile) |
G2QAB5 | LP9D_THET4 | MYRTLGSIALLAGGAAAHGAVTSYNIAGKDYPGYSGFAPTGQDVIQWQWPDYNPVLSASDPKLRCNGGTGAALYAEAAPGDTITATWAQWTHSQGPILVWMYKCPGDFSSCDGSGAGWFKIDEAGFHGDGTTVFLDTETPSGWDIAKLVGGNKSWSSKIPDGLAPGNYLVRHELIALHQANNPQFYPECAQIKVTGSGTAEPAASYKAAIPGYCQQSDPNISFNINDHSLPQEYKIPGPPVFKGTASAKARAFQA | 3.2.1.4 | COFACTOR: Name=Cu(2+); Xref=ChEBI:CHEBI:29036; Evidence={ECO:0000269|PubMed:28257189}; Note=Binds 1 copper ion per subunit. {ECO:0000269|PubMed:28257189}; | cellulose catabolic process [GO:0030245] | extracellular region [GO:0005576] | hydrolase activity [GO:0016787]; metal ion binding [GO:0046872] | PF03443; | 2.70.50.70; | Polysaccharide monooxygenase AA9 family | null | SUBCELLULAR LOCATION: Secreted {ECO:0000305|PubMed:29196788}. | CATALYTIC ACTIVITY: Reaction=Endohydrolysis of (1->4)-beta-D-glucosidic linkages in cellulose, lichenin and cereal beta-D-glucans.; EC=3.2.1.4; Evidence={ECO:0000269|PubMed:28257189, ECO:0000269|PubMed:29196788}; | null | null | null | null | FUNCTION: Lytic polysaccharide monooxygenase that depolymerizes crystalline and amorphous polysaccharides via the oxidation of scissile alpha- or beta-(1-4)-glycosidic bonds, yielding specifically C1 oxidation product (PubMed:28257189, PubMed:29196788). Catalysis by LPMOs requires the reduction of the active-site copper from Cu(II) to Cu(I) by a reducing agent and H(2)O(2) or O(2) as a cosubstrate (PubMed:28257189). Is active on regenerated amorphous cellulose (RAC) in the presence of ascorbic acid or 3-methylcatechol (PubMed:29196788). Acts also on phosphoric acid swollen cellulose (PASC) as a substrate (PubMed:28257189). {ECO:0000269|PubMed:28257189, ECO:0000269|PubMed:29196788}. | Thermothelomyces thermophilus (strain ATCC 42464 / BCRC 31852 / DSM 1799) (Sporotrichum thermophile) |
G2QFD0 | LMCO1_THET4 | MLLSKLSILLAKWLSVAVYAGTLVHDEQFIPDHILRVSVAQVPSACENREDVVVNGTSPGPAIHLLPGARTWIRVYNDMNDRNLSMHWHGLSQRFAPFSDGTPSATQWPIPPGHFFDYEILTEPEDAGTYFYHSHVGMQALSCTGPLIVEDCGSSPYHYDDERILLFQDHFQKSDLEMIQGLTSTQFTWTGETRGILLNGRGVSPNQAAVQGRPGEASGFFGSHRFSNFRAGDGTSNSWDGIRGDDQIEPPTDCTLPVIDVEPGKTYRLRFIGATGLSLLTMGFEDHNDLTIVQVDGSEYNAPVTVDHIQLGGGQRFDVLLRTKTAEELRCNGDKTTYFLQFETRDRPDPYRGYGVLRYNLGTPVPAAPTTPALTLPAEVNNWLEYTFQPLHPSSSLSPTAEEVTRRVILEAEQKIDPATGRLVWKLAHMTWTDMSRDKPVLVDIYERGEAAMPDYAAALTNYGWDPATKLFPAKKDEVLEIVIQNTGSHYSGASGIVETHPFHAHGQHFYDVGSGPGKYDPEANNAKLASLGYRPIKRDTTMVYRYGEGKVAPGEPAGWRAWRMKMNNPGVWMVHCHILAHMIMGMETIWVVGDAEDIVTIPLSVSQNYFTYGGSVYGNDTHAPEVYHYFDDTNKCCAAGAGDSEDSGH | 1.-.-.- | null | null | null | copper ion binding [GO:0005507]; ferroxidase activity [GO:0004322] | PF00394;PF07731;PF07732; | 2.60.40.420; | Multicopper oxidase family | PTM: N-glycosylation Asn-55 and Asn-83 is involved in folding, conformational stability and laccase activity. {ECO:0000269|PubMed:37326583}. | null | CATALYTIC ACTIVITY: Reaction=2 2',3,4-trihydroxy-trans-chalcone + 2 H(+) + O2 = 2 3',4'-dihydroxyaurone + 2 H2O; Xref=Rhea:RHEA:63848, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, ChEBI:CHEBI:144744, ChEBI:CHEBI:144745; Evidence={ECO:0000269|PubMed:30529567}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:63849; Evidence={ECO:0000269|PubMed:30529567}; | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=2.37 mM for ABTS {ECO:0000269|PubMed:30529567}; KM=2.41 mM for 2,6-dimethoxyphenol {ECO:0000269|PubMed:30529567}; | null | BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 4.0. {ECO:0000269|PubMed:30529567}; | BIOPHYSICOCHEMICAL PROPERTIES: Temperature dependence: Optimum temperature is 50 degrees Celsius. {ECO:0000269|PubMed:30529567}; | FUNCTION: Yellow laccase-like multicopper oxidase that is able to oxidize a variety of phenolic compounds including standard laccase substrates such as 2'-azino-bis(3-ethylbenzothiazoline-6-sulphonic acid) (ABTS) and 2,6-dimethoxyphenol (2,6-DMP) (PubMed:30529567, PubMed:37326583). The existence of an ortho-hydroxy group is crucial for oxidation since pyrogallol and catechol, which contain ortho-hydroxy groups, are readily oxidized, which is not the case for resorcinol and hydroquinone, that contain meta- and para-hydroxy groups, respectively (PubMed:37326583). The same is also true for the existence of a methoxy group in an ortho-position, since 2,6-DMP, guaiacol and ferulic and caffeic acids are also rather easily oxidized compared with the corresponding unsubstituted compound (PubMed:37326583). Can be used for the bioconversion of 2',3,4-trihy-droxychalcone to 3',4'-dihydroxy-aurone, a bioactive aurone recently shown to possess inhibitory activity against several isoforms of the histone deacetylase complex (HDAC) (PubMed:30529567). {ECO:0000269|PubMed:30529567, ECO:0000269|PubMed:37326583}. | Thermothelomyces thermophilus (strain ATCC 42464 / BCRC 31852 / DSM 1799) (Sporotrichum thermophile) |
G2QG48 | XYLO_THET4 | MHLLPLTVSATAVVSAASSPHAKRAAIDECLKNAKVPVTARNSTEWKTDASPFNDRLPYTPAAIAKPATVEHIQAAVLCAAEVGVKANPKSGGHSYASFGLGGEDGHLVVELDRMYNVTLDPETHIATVQPGARLGHIATVLYEEGKRAFSHGTCPGVGVGGHSLHGGFGFSSHSHGLAVDWITSADVVLANGSLVTASETENPDLFWALRGAGSNFGIVASFRFKTFAAPPNVTSYEINLPWTNSSNVVKGWGALQEWLLNGGMPEEMNMRVLGNAFQTQLQGLYHGNASALKTAIQPLLALLDANLSSVQEHDWMEGFRHYAYSGEIDITDPGYDQSETFYSKSLVTSALPPDVLERVAEYWIETANKVRRSWYIIIDMYGGPNSAVTRVPPGAGSYAFRDPERHLFLYELYDRSFGPYPDDGFAFLDGWVHAFTGGLDSSDWGMYINYADPGLDRAEAQEVYYRQNLDRLRRIKQQLDPTELFYYPQAVEPAEV | 1.1.3.- | COFACTOR: Name=FAD; Xref=ChEBI:CHEBI:57692; Evidence={ECO:0000269|PubMed:27629413}; Note=Binds 1 FAD per subunit in a bicovalent manner. {ECO:0000269|PubMed:27629413}; | null | extracellular region [GO:0005576] | FAD binding [GO:0071949]; oxidoreductase activity [GO:0016491] | PF08031;PF01565; | 3.30.465.10;3.40.462.20; | Oxygen-dependent FAD-linked oxidoreductase family | PTM: The FAD cofactor is bound via a bicovalent 6-S-cysteinyl, 8alpha-N1-histidyl FAD linkage. {ECO:0000269|PubMed:27629413}. | SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:27629413}. | CATALYTIC ACTIVITY: Reaction=D-xylobiose + O2 = D-xylobiono-1,5-lactone + H2O2; Xref=Rhea:RHEA:59632, ChEBI:CHEBI:15379, ChEBI:CHEBI:16240, ChEBI:CHEBI:28309, ChEBI:CHEBI:143156; Evidence={ECO:0000269|PubMed:27629413}; CATALYTIC ACTIVITY: Reaction=D-xylotriose + O2 = D-xylotriono-1,5-lactone + H2O2; Xref=Rhea:RHEA:59636, ChEBI:CHEBI:15379, ChEBI:CHEBI:16240, ChEBI:CHEBI:62783, ChEBI:CHEBI:143164; Evidence={ECO:0000269|PubMed:27629413}; CATALYTIC ACTIVITY: Reaction=D-xylotetraose + O2 = D-xylotetraono-1,5-lactone + H2O2; Xref=Rhea:RHEA:59640, ChEBI:CHEBI:15379, ChEBI:CHEBI:16240, ChEBI:CHEBI:62972, ChEBI:CHEBI:143165; Evidence={ECO:0000269|PubMed:27629413}; | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=0.13 mM for oxygen {ECO:0000269|PubMed:27629413}; KM=342 mM for cellobiose {ECO:0000269|PubMed:27629413}; KM=532 mM for lactose {ECO:0000269|PubMed:27629413}; KM=359 mM for xylose {ECO:0000269|PubMed:27629413}; KM=1.15 mM for xylobiose {ECO:0000269|PubMed:27629413}; KM=0.69 mM for xylotriose {ECO:0000269|PubMed:27629413}; KM=0.43 mM for xylotetraose {ECO:0000269|PubMed:27629413}; | null | BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 7. {ECO:0000269|PubMed:27629413}; | BIOPHYSICOCHEMICAL PROPERTIES: Temperature dependence: Optimum temperature is 30 degrees Celsius. Stable up to 60 degrees Celsius. {ECO:0000269|PubMed:27629413}; | FUNCTION: Catalyzes the selective oxidation of C1 hydroxyl moieties on mono-, oligo- and polysaccharides with concomitant reduction of molecular oxygen to hydrogen peroxide. This results in the formation of the corresponding lactones, which typically undergo spontaneous hydrolysis. Xylooligosaccharide oxidase is able to oxidize a variety of substrates including D-xylose, D-cellobiose, lactose and arabinose. The enzyme acts primarily on xylooligosaccharides, indicating that it prefers pentose-based oligosaccharides over hexose-based oligosaccharides. {ECO:0000269|PubMed:27629413}. | Thermothelomyces thermophilus (strain ATCC 42464 / BCRC 31852 / DSM 1799) (Sporotrichum thermophile) |
G2QND5 | FAEB_THET4 | MLVRSFLGFAVLAATCLAASLQEVTEFGDNPTNIQMYIYVPDQLDTNPPVIVALHPCGGSAQQWFSGTQLPSYADDNGFILIYPSTPHMSNCWDIQNPDTLTHGQGGDALGIVSMVNYTLDKHSGDSSRVYAMGFSSGGMMTNQLAGSYPDVFEAGAVYSGVAFGCAAGAESATPFSPNQTCAQGLQKTAQEWGDFVRNAYAGYTGRRPRMQIFHGLEDTLVRPQCAEEALKQWSNVLGVELTQEVSGVPSPGWTQKIYGDGTQLQGFFGQGIGHQSTVNEQQLLQWFGLI | 3.1.1.73 | null | xylan catabolic process [GO:0045493] | extracellular region [GO:0005576] | feruloyl esterase activity [GO:0030600] | PF10503; | 3.40.50.1820; | Carbohydrate esterase 1 (CE1) family, Feruloyl esterase type B subfamily | null | SUBCELLULAR LOCATION: Secreted {ECO:0000250}. | CATALYTIC ACTIVITY: Reaction=feruloyl-polysaccharide + H2O = ferulate + polysaccharide.; EC=3.1.1.73; Evidence={ECO:0000269|PubMed:22012339}; | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=0.27 mM for methyl ferulate (MFA) {ECO:0000269|PubMed:22012339}; KM=0.26 mM for methyl p-coumarate (MpCA) {ECO:0000269|PubMed:22012339}; KM=0.18 mM for methyl caffeate (MCA) {ECO:0000269|PubMed:22012339}; KM=0.21 mM for methyl sinapate (MSA) {ECO:0000269|PubMed:22012339}; KM=2.29 mM for nitrophenyl-5-O-trans-feruloyl-alpha-L-arabinofuranoside {ECO:0000269|PubMed:22012339}; KM=2.79 mM for nitrophenyl-2-O-trans-feruloyl-alpha-L-arabinofuranoside {ECO:0000269|PubMed:22012339}; KM=2.33 mM for ethyl ferulate {ECO:0000269|PubMed:22012339}; KM=1.14 mM for n-propyl ferulate {ECO:0000269|PubMed:22012339}; KM=1.4 mM for iso-propyl ferulate {ECO:0000269|PubMed:22012339}; KM=0.74 mM for n-butyl ferulate {ECO:0000269|PubMed:22012339}; KM=0.65 mM for iso-butyl ferulate {ECO:0000269|PubMed:22012339}; KM=0.74 mM for 2-butyl ferulate {ECO:0000269|PubMed:22012339}; | null | BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 7.0. {ECO:0000269|PubMed:22012339}; | BIOPHYSICOCHEMICAL PROPERTIES: Temperature dependence: Optimum temperature is 50 degrees Celsius. {ECO:0000269|PubMed:22012339}; | FUNCTION: Feruloyl esterase which acts in synergy with xylanases in degradation of plant cell walls. Hydrolyzes the ester linkage of hydroxycinnamic acids (ferulic acid (FA) and p-coumaric acid) and diferulates present in plant cell walls. Is active on substrates containing ferulic acid ester linked to the C-5 and C-2 linkages of arabinofuranose, while it was found capable of de-esterifying acetylated glucuronoxylans. Efficiently releases ferulic acid (FA) from destarched wheat bran when incubated with an M3 xylanase. {ECO:0000269|PubMed:22012339}. | Thermothelomyces thermophilus (strain ATCC 42464 / BCRC 31852 / DSM 1799) (Sporotrichum thermophile) |
G2QNH0 | ADT_THET4 | MSNKQETKILGMPPFVVDFLMGGVSAAVSKTAAAPIERIKLLVQNQDEMIKAGRLDRRYNGIIDCFRRTTADEGLMALWRGNTANVIRYFPTQALNFAFRDKFKAMFGYKKDKDGYAKWMAGNLASGGAAGATSLLFVYSLDYARTRLANDAKSAKGGGARQFNGLIDVYRKTLASDGIAGLYRGFGPSVAGIVVYRGLYFGMYDSIKPVVLVGPLANNFLASFLLGWCVTTGAGIASYPLDTVRRRMMMTSGEAVKYKSSIDAFRQIIAKEGVKSLFKGAGANILRGVAGAGVLSIYDQLQILLFGKAFKGGSG | null | null | mitochondrial ADP transmembrane transport [GO:0140021]; mitochondrial ATP transmembrane transport [GO:1990544]; negative regulation of mitochondrial outer membrane permeabilization involved in apoptotic signaling pathway [GO:1901029] | mitochondrial inner membrane [GO:0005743] | ATP:ADP antiporter activity [GO:0005471] | PF00153; | 1.50.40.10; | Mitochondrial carrier (TC 2.A.29) family | null | SUBCELLULAR LOCATION: Mitochondrion inner membrane {ECO:0000250|UniProtKB:P18239}; Multi-pass membrane protein {ECO:0000269|PubMed:30611538}. | CATALYTIC ACTIVITY: Reaction=ADP(in) + ATP(out) = ADP(out) + ATP(in); Xref=Rhea:RHEA:34999, ChEBI:CHEBI:30616, ChEBI:CHEBI:456216; Evidence={ECO:0000269|PubMed:30611538}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:35000; Evidence={ECO:0000269|PubMed:30611538}; | null | null | null | null | FUNCTION: ADP:ATP antiporter that mediates import of ADP into the mitochondrial matrix for ATP synthesis, and export of ATP out to fuel the cell (PubMed:30611538). Cycles between the cytoplasmic-open state (c-state) and the matrix-open state (m-state): operates by the alternating access mechanism with a single substrate-binding site intermittently exposed to either the cytosolic (c-state) or matrix (m-state) side of the inner mitochondrial membrane (PubMed:30611538). {ECO:0000269|PubMed:30611538}. | Thermothelomyces thermophilus (strain ATCC 42464 / BCRC 31852 / DSM 1799) (Sporotrichum thermophile) |
G2TRN4 | ERH_SCHPO | MSPPPAESHIILLIQQGSDPKTRIWSDHCSLRSAIEYIVGVYQTNQAVSEKESIDVSRFFNFFDEIYDCVPLVYDRHFRAYIPHEKQWLLHHAQEYLTAARQIP | null | null | nuclear-transcribed mRNA catabolic process, meiosis-specific transcripts [GO:0033621]; regulation of siRNA-independent facultative heterochromatin formation [GO:1902801]; regulatory ncRNA 3'-end processing [GO:0043628] | ascospore-type prospore nucleus [GO:1905754]; cytoplasm [GO:0005737]; heterochromatin island [GO:1990342]; nuclear exosome focus [GO:1990251]; nucleoplasm [GO:0005654]; nucleus [GO:0005634]; rDNA heterochromatin [GO:0033553] | molecular function inhibitor activity [GO:0140678] | PF01133; | 3.30.2260.10; | E(R) family | null | SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:23145069, ECO:0000269|PubMed:26942678}. Cytoplasm {ECO:0000269|PubMed:23145069}. Note=Localizes to chromatin regions during vegetative growth, localizes to mei2 nuclear dots during meiosis. {ECO:0000269|PubMed:26942678}. | null | null | null | null | null | FUNCTION: Forms part of the erh1-mmi1 complex that recruits the CCR4-NOT complex and the NURS complex to target RNAs (PubMed:26942678, PubMed:30651569, PubMed:31974447). Suppresses the meiotic program during vegetative growth and promotes the meiotic program during mating (PubMed:31974447). Recruitment of the NURS complex to target mRNAs promotes mRNA decay by engagement of the nuclear exosome, and formation of heterochromatin islands at meiotic genes silenced by the exosome (PubMed:26942678). Recruitment of the CCR4-NOT complex to target RNAs promotes heterochromatin formation at RNAi-dependent heterochromatin domains (HOODs), including a subset of meiotic genes, lncRNAs and retrotransposons (PubMed:26942678). Recruitment of the CCR4-NOT complex to rDNA promotes rDNA heterochromatin assembly (PubMed:26942678). {ECO:0000269|PubMed:26942678, ECO:0000269|PubMed:30651569, ECO:0000269|PubMed:31974447}. | Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast) |
G2WR64 | DMT5_VERDV | MAQKPQQFDVLGDTGARVDRPRDSLALIFKRALELGLDDVSQDGGVRFTVGTMCSGTDAPILALRELQDAALAMGYNHLFDFDHQFSVEIEAYKQAFIERNSKPSGEIYRDVIQVSDPSRKDAITAHGSLAPIPAAPDLLVAGSSCVDFSKLNNKRDILAKHSVLSRLYEEAKNTKNGLDFGTVTPQSQSHDVRMALQDVRDSFHTEGESVKTFGSILQFIYDQRPKLIILENVSHAPWRAFTHFWLPLVGYVALSMKVDSKNFLVPQTRTRGYLVAVDQWHYGTELSTRMARLWSSMMESSNWFPNQYPEVHKFLLSSMDQRILEARAIEERKIAENMTRDVEARMCAYDHAKVRRQQGLGPDRPFTQRDGRGNLLPRDTSWQAYIRGTSSRVQDLLDITWLSERKKGGRDLNYKAKYLDLGEGVERLKTQIGIVGCVLPDGDLFATDQGRPILGVEALSLQGLPIDRIRTSVETQADLHDMAGNAMTTTVVGAATLCILIAERQVTRSSGFHDGLPLLDNGASTRTQHLKHLFAIRQSDRNGAADGAFALLQHCPSYSTAQKDQAAVAHLIMIHQKGRRYCPCAGYRKHNPATGLMICTLCNQVRCVTCAGNPAHAFETLLTGPLWSWDETIHALRGILPNRFALTGGHGIPQDDKDVKSLCSSLYTTEKENGNITTRLRELRKCLGAVYYLDHFDNSQVIVATYVSTCGRIELSIGLDQVVWYLYLPEPLEPGSFNQQPAPPIARAILDKSADNVFPSCLSWEIFFLQPVPVVLSLEPQSDSTFRCFVTEFNGQPIKSYPIIPMAATELMVGVEGVYEFSQTCGTPFDLLYSRRTAGSEPSSAPCYLFLDTKHTTEPEEDSWVMSQSVSKLEPGTHREVLCKFSSSWKEQEQKLRQHGTPQTVQCEIPGLWRSVHQTNGALMNISMSDVHLAPDRMTAETSEDLHVIIPGALNFPDVAQAPIPVLQLRIDIPDLPFPVHLLPQLWKTDGEIFKECAKETDSGEKWMRVSDHHHKDALSLISFALGALKANHLPREFTVGILERAGAVCQSLDADFPNPKVHLLWEGFKVKKLFDDSEAAQQLAESYSKRPLPLELDVQIVRADQPRHTGDLYSGRAGGNIAQEPELIIRILFNPTALAHRAWLHIPRDGLIRGIRRDVMQDGHIGFAVDVEFVDPSLKMIEPFEACLSQDVISSATYASAIQLPSFDSCGVQLRPDQIQSVQWMIEKESSNSCFVEREVEEFLVPSSSIRLRSHAEVVNRARGGVLAHDVGFGKTIATLALIDHQRNQSNERSVTERYAWTQERHCHLKATLIVCPPQIVDQWRDEIERFLGSENWNVVVINAKTPFHRGILEMADIVILSTAFIHSTAFVQALTRVAGAANFHDASSASSREFNIWYREAVTDLEDSCQCYADNNRNNGALAKHISLRTQERKASFEKARAACIVESRRKDQKSKATARTQRAKKKSKKPRRTAAAAAESDHSAESDSDSAMDDRKRKVATSHVVSDFKDATVLQMYSFDRVVLDEFSYENKSTAAFVANCVASSKWILSGTPPMADLSQVCAIADLVNMHVARPEASVPRSFPSITRGPRLDKTTRGEAMRQYADPKSAQFALERHEQARTFLEHKMTRRETDISHIGVTEQVVVCRLDPVSSVVYAQLQQVLYDARWDIEEVPGDMRAIIDWLLQQTGNNKASKARENLRMSWHNTIQSLLVQSSTNLSAYGENMKKLGMDVRAGAVSGITVLTSMRTIYQRLQARSKAMIKSQFDMLMYVVDQVQMSGLLTMTNAKGRDKTKQDKAMYYQDHLDDFIQRFTAARPWSFGDAEIRDDFWKGGNGVYGAIDWWKLTEEDVEAMDEDELKHVETKLVCFKASYNPESQMEATGQQLEESVCDLLNANVLDQYHEAEPEKVAANIGLASATLLDVYWKDTAKSKDFEFGNKFRPYRPKLNEEETDRGTSHDQATNRMAMALQSVQAGIEEYIRQARRLRVLGIVQDLFAFAQALEAGHQPNAPTCSVCGSQDNTEMKDLSLFITCGHLLCSGCVAAHEHQHGQAESTTGEVLCPVDSCSAMARSALVPCTQLISATAASTLDFEGKSAKVMKILDVIRTDVKDDEKVLLFVSNKKLKAQLSDALEEDDNVDVYMTTGTHHDTDAIRSFKEPNEDGRKKVLVQSLMSEESAGTNLTEANHVMFAAPLHTDRRNHYMYMRQARGRAIRFGQTRPVRVYHFVTAHTMEVDVLEHRLGHKLLIPEGGDRMPLDDLDYKLYALDTRAASRGPPSATKEASAAPTISSTLRRIRPYIDEVETRKLLDSQEYDEWQDRLDVSPSAATKQTPWFRSQVVEQSADEVYDDDVEVGN | 3.6.4.- | null | methylation [GO:0032259]; nucleotide-excision repair [GO:0006289] | chromosome [GO:0005694]; nucleus [GO:0005634] | ATP binding [GO:0005524]; ATP-dependent chromatin remodeler activity [GO:0140658]; DNA binding [GO:0003677]; hydrolase activity [GO:0016787]; metal ion binding [GO:0046872]; methyltransferase activity [GO:0008168] | PF00271;PF00176; | 3.40.50.300;3.40.50.10810;3.40.50.150; | Class I-like SAM-binding methyltransferase superfamily, C5-methyltransferase family; SNF2/RAD54 helicase family | null | SUBCELLULAR LOCATION: Nucleus {ECO:0000305|PubMed:33941240}. Chromosome {ECO:0000305|PubMed:33941240}. | CATALYTIC ACTIVITY: Reaction=a 2'-deoxycytidine in DNA + ATP + H2O + S-adenosyl-L-methionine = a 5-methyl-2'-deoxycytidine in DNA + ADP + 2 H(+) + phosphate + S-adenosyl-L-homocysteine; Xref=Rhea:RHEA:68984, Rhea:RHEA-COMP:11369, Rhea:RHEA-COMP:11370, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:57856, ChEBI:CHEBI:59789, ChEBI:CHEBI:85452, ChEBI:CHEBI:85454, ChEBI:CHEBI:456216; Evidence={ECO:0000250|UniProtKB:J9VI03}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:68985; Evidence={ECO:0000250|UniProtKB:J9VI03}; | null | null | null | null | FUNCTION: May play a role in cytosine methylation at palindromic 5'-CG-3' and 5'-C[ACT]G-3' sites in DNA. {ECO:0000269|PubMed:33941240}. | Verticillium dahliae (strain VdLs.17 / ATCC MYA-4575 / FGSC 10137) (Verticillium wilt) |
G2X4G0 | 424Y_VERDV | MVSFTSLLAAFSVVSGVLTSPIAVVPEVNTALAKRTPSSTGTSGGFYYSFWTDTPNSVTYTNGDAGKFSVSWKNNNGNHVGGKGWRTGSARTIKYSGSYKPNGNSYLAIYGWTRSPLIEYYIVESFGTYNPSTGATSKGQFTVDGSVYDLYTSTRTNAPSIEGTRTFTQFWSVRRTKRTSGSVNTGAHFAAWKKAGMNLGSHDYQILAVEGYKSSGSATMTVS | 3.2.1.8 | null | effector-mediated perturbation of host innate immune response by symbiont [GO:0140404]; xylan catabolic process [GO:0045493] | extracellular region [GO:0005576]; host cell nucleus [GO:0042025] | endo-1,4-beta-xylanase activity [GO:0031176] | PF00457; | 2.60.120.180; | Glycosyl hydrolase 11 (cellulase G) family | null | SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:34233072}. Host nucleus {ECO:0000269|PubMed:34233072}. | CATALYTIC ACTIVITY: Reaction=Endohydrolysis of (1->4)-beta-D-xylosidic linkages in xylans.; EC=3.2.1.8; Evidence={ECO:0000255|PROSITE-ProRule:PRU01097}; | null | PATHWAY: Glycan degradation; xylan degradation. {ECO:0000255|PROSITE-ProRule:PRU01097}. | null | null | FUNCTION: Secreted effector that localizes to the host nucleus to contribute to the virulence process (PubMed:34233072). Induces host innate immunity responses; triggers BAK1-and SOBIR1-dependent cell death, salicylic acid signaling and jasmonic acid signaling (PubMed:34233072). {ECO:0000269|PubMed:34233072}. | Verticillium dahliae (strain VdLs.17 / ATCC MYA-4575 / FGSC 10137) (Verticillium wilt) |
G2X4M1 | ISC1_VERDV | MSSFRSMLGVPPSTASTQDSVLVIIDAQGEYAEGKLKISNIEASRPNISSLLEKYRAANAPIVHVVHETPAGAPLFTQGTKLAEIFDELTPKEGEAVVTKHHPGSFADTNLQEILEKSGKKKIVLVGYMAHVCVSTTARQGAQRGWDVIVAEDAVGDRDIPGVDAAQLVKVALAEIADVFGTLVSSKDIN | 3.3.2.1 | null | effector-mediated suppression of host innate immune response [GO:0140403] | extracellular region [GO:0005576]; host cell cytoplasm [GO:0030430]; host cell nucleus [GO:0042025] | isochorismatase activity [GO:0008908] | PF00857; | 3.40.50.850; | Isochorismatase family | null | SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:25156390}. Host cytoplasm {ECO:0000269|PubMed:25156390}. Host nucleus {ECO:0000269|PubMed:25156390}. Note=Lacks a signal peptide and uses an unconventional secretion pathway for delivering effectors which plays an important role in host-pathogen interactions. {ECO:0000269|PubMed:25156390}. | CATALYTIC ACTIVITY: Reaction=H2O + isochorismate = (2S,3S)-2,3-dihydroxy-2,3-dihydrobenzoate + pyruvate; Xref=Rhea:RHEA:11112, ChEBI:CHEBI:15361, ChEBI:CHEBI:15377, ChEBI:CHEBI:29780, ChEBI:CHEBI:58764; EC=3.3.2.1; Evidence={ECO:0000269|PubMed:25156390}; | null | null | null | null | FUNCTION: Secreted isochorismatase required for full virulence of V.dahliae (PubMed:25156390). Suppresses salicylate-mediated innate immunity of the host by disrupting the plant salicylate metabolism pathway via hydrolysis of its isochorismate precursor (PubMed:25156390). {ECO:0000269|PubMed:25156390}. | Verticillium dahliae (strain VdLs.17 / ATCC MYA-4575 / FGSC 10137) (Verticillium wilt) |
G2X7W6 | ATC3_VERDV | MAGRPTGGPQGAPSHDLLLDLENDQPVYGGGQRSTLNDDDLMRTYTRDQESGQDQGRPSVSYDDFIGAGQSRQHGTGSQPGGPGQSSSSNNNNNNNVSAPYSRSGRQYSQTSDLGNYQRYADDFDDYPADGDSFYQQGGALNGGGADAAARHNARNRNSVLTMGGGFFGKMKNRLGMGQGYSEMDLPLTEPGGGGGGAGGGGHSRADSSGIDPPKRDKKFDMGNFKFGFGRSKPDPSTLGPRIIHLNNPPANAANKYVNNHVSTAKYNIATFLPKFLLEQFSKIANVFFLFTAALQQIPGLSPTNRFTTIIPLVAVLMVSAGKELVEDYRRKQADAALNTSRAQVLRGSTFEETKWINVAVGDIVRVESEEPFPADIVLLASSEPEGLCYIETANLDGETNLKIKQALPETSQMVSSSELSRLGGRMKSEQPNSSLYTYEATLTMQTGGGEKELPLNPEQLLLRGATLRNTPWIHGVVVFTGHETKLMRNATAAPIKRTKVEKKLNTLVLLLVGILMVLSIISTVGDLIIRRVEGDAISYLMLDQPDTAGKIAETFFKDMVTYWVLFSSLVPISLFVTVEMVKYWHGILINDDLDMYYDRNDTPANCRTSNLVEELGMVEFVFSDKTGTLTCNMMEFKQASIAGIQYADEVPEDRRATIQDGVEVGLHDYKRLKENRKNHSSAPAIDHFLALLATCHTVIPEKGDEKGGKIKYQAASPDEGALVDGAATLGYTFTDRKPKAVFIEVDGQTLEYELLAVCEFNSTRKRMSTIYRCPDGVIRVYCKGADTVILERLNENNPHVEQTLTHLEEYASEGLRTLCLAMREVSEQEFQEWNQVYEKAATTVGGNRAEELDKASEMIEHDFFLLGATAIEDRLQDGVPETIHTLQEANIKVWVLTGDRQETAINIGMSCKLLSEEMMLLIINEESAAATRDNIEKKLEAIRAQGDRTIELETLALVIDGKSLTYALEKDLEKMFLDLAIMCKAVICCRVSPLQKALVVKLVKKYQKESILLAIGDGANDVSMIQAAHIGVGISGEEGLQAARSADVSIAQFRFLKKLLLVHGAWSYQRVAKTILYSFYKNITLYMTQFWYTFRNVFSGAVIYESWTLTFYNVFYTVLPPLALGILDQFISARLLDRYPQLYSMGQQNQFFRMKVFIEWLLNAVYHSIILYVFGELIWHGDLILENGQIAGHWMWGTALYAPVLLTVLGKAGLVTSNWTKYHVIAIPGSMAIWWIFIAVYGTVAPMIPFSPEFHGIVPKLYSSPIFWLQSFALAILCLLRDFAWKYAKRMYRPESYHHIQEIQKYNIQDYRPRMEQFQKAIRKVRQVQRMRKQRGYAFSQADESQARVLQAYDTTQNRGRYGEMTSSRPQGQGT | 7.6.2.1 | COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250|UniProtKB:P39524}; | endocytic recycling [GO:0032456]; phospholipid translocation [GO:0045332]; post-Golgi vesicle-mediated transport [GO:0006892] | plasma membrane [GO:0005886]; trans-Golgi network membrane [GO:0032588] | ATP binding [GO:0005524]; ATP hydrolysis activity [GO:0016887]; magnesium ion binding [GO:0000287]; phosphatidylethanolamine flippase activity [GO:0090555]; phosphatidylserine floppase activity [GO:0090556] | PF13246;PF00122;PF16212;PF16209; | 3.40.1110.10;2.70.150.10;3.40.50.1000; | Cation transport ATPase (P-type) (TC 3.A.3) family, Type IV subfamily | null | SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:36072318}; Multi-pass membrane protein {ECO:0000255}. Golgi apparatus, trans-Golgi network membrane {ECO:0000269|PubMed:36072318}; Multi-pass membrane protein {ECO:0000255}. | CATALYTIC ACTIVITY: Reaction=ATP + H2O + phospholipidSide 1 = ADP + phosphate + phospholipidSide 2.; EC=7.6.2.1; Evidence={ECO:0000250|UniProtKB:P39524}; CATALYTIC ACTIVITY: Reaction=a 1,2-diacyl-sn-glycero-3-phospho-L-serine(out) + ATP + H2O = a 1,2-diacyl-sn-glycero-3-phospho-L-serine(in) + ADP + H(+) + phosphate; Xref=Rhea:RHEA:38567, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:57262, ChEBI:CHEBI:456216; Evidence={ECO:0000250|UniProtKB:P39524}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:38568; Evidence={ECO:0000250|UniProtKB:P39524}; CATALYTIC ACTIVITY: Reaction=a 1,2-diacyl-sn-glycero-3-phosphoethanolamine(out) + ATP + H2O = a 1,2-diacyl-sn-glycero-3-phosphoethanolamine(in) + ADP + H(+) + phosphate; Xref=Rhea:RHEA:66132, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:64612, ChEBI:CHEBI:456216; Evidence={ECO:0000250|UniProtKB:P39524}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:66133; Evidence={ECO:0000250|UniProtKB:P39524}; | null | null | null | null | FUNCTION: Catalytic component of a P4-ATPase flippase complex which catalyzes the hydrolysis of ATP coupled to the transport of phosphatidylserine and small amounts of ethanolamine from the lumen to the cytosolic leaflet of the trans-Golgi network and cell membrane and ensures the maintenance of asymmetric distribution of phospholipids (By similarity). Required for efficient vesicle transport during toxin secretion (PubMed:36072318). {ECO:0000250|UniProtKB:P39524, ECO:0000269|PubMed:36072318}. | Verticillium dahliae (strain VdLs.17 / ATCC MYA-4575 / FGSC 10137) (Verticillium wilt) |
G2XDH0 | SCP41_VERDV | MRTETASLLLLAALSVAEELTPNDVPLACANMCGPIVELSYKCDVDGTDELRKLKRRKLFSPQQQQQQQQQQQQSAPKAKRQADPEPQAPAPVPSSTNNQQAADVIFIPGSIGKFKTIPTPLPPADTGVPSMAVTPAAPAPTLPVLDLRPTTTPTNLNPNLPILATPILPSVPASTPLATASSTQVPLPVGNEADAGDGVDAGPAPSNSLNGNVGDMVDDAGNLWPGQKGRQAASDLETACICSNTSFNVRRVAGLCGDCLEQVSGDQGPMRAILASCNFTTERYEPEKESLVANVRVEATKPSFTQTAAASYSWRVSGPTWAVVVGAGMLLGMGW | null | null | effector-mediated suppression of host innate immune response [GO:0140403] | extracellular region [GO:0005576]; host cell nucleus [GO:0042025] | transcription regulator inhibitor activity [GO:0140416] | null | null | null | null | SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:29757140}. Host nucleus {ECO:0000269|PubMed:29757140}. | null | null | null | null | null | FUNCTION: Effector that binds transcription regulators in the host plant to suppress the host's innate immune response (PubMed:29757140). Inhibits the host plant transcription regulators CBP60G and SARD1 (PubMed:29757140). {ECO:0000269|PubMed:29757140}. | Verticillium dahliae (strain VdLs.17 / ATCC MYA-4575 / FGSC 10137) (Verticillium wilt) |
G2XKQ0 | SUMO5_HUMAN | MSDLEAKPSTEHLGDKIKDEDIKLRVIGQDSSEIHFKVKMTTPLKKLKKSYCQRQGVPVNSLRFLFEGQRIADNHTPEELGMEEEDVIEVYQEQIGGHSTV | null | null | PML body organization [GO:0030578]; protein sumoylation [GO:0016925] | nucleus [GO:0005634]; PML body [GO:0016605] | identical protein binding [GO:0042802]; protein tag activity [GO:0031386]; transcription factor binding [GO:0008134]; ubiquitin-like protein ligase binding [GO:0044389] | PF11976; | null | Ubiquitin family, SUMO subfamily | PTM: Cleavage of precursor form is necessary for function. {ECO:0000250|UniProtKB:P63165}.; PTM: Autosumoylated at Lys-18. {ECO:0000269|PubMed:27211601}. | SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:27211601}. Note=Forms prominent non-membrane-bound structures in the nucleus. {ECO:0000269|PubMed:27211601}. | null | null | null | null | null | FUNCTION: Ubiquitin-like protein that can be covalently attached to proteins as a monomer or as a lysine-linked polymer. Regulates the life cycle of promyelocytic leukemia nuclear bodies (PML-NBs). PolySUMO1P1/SUMO5 conjugation on 'Lys-160' of PML facilitates recruitment of PML-NB components, which enlarges PML-NB. SUMO1P1/SUMO5 also increases polySUMO2/3 conjugation of PML, resulting in RNF4-mediated disruption of PML-NBs. {ECO:0000269|PubMed:27211601}. | Homo sapiens (Human) |
G3C7W6 | S2611_CAVPO | MPSSLKGLGQAWLSSSSMALSACCSVSAWQKRLPVLAWLPRYSLQWLKMDFIAGLSVGLTVIPQALAYAEVAGLPPQYGLYSAFTGCFVYVFLGTSRDVTLGPTAIMSLLVSFYTFHEPAYAVLLTFLSGCIQLAMGLLHLGFLLDFISCPVIKGFTSAAAIIIGFGQIKNLLGLHNIPRQFFLQVYHTFLSVGETRLGDAILGLVCMVLLLVLKLMRDRIPPVHPEMPLCVRLSCGLVWTTATARNALVVSFAALVAYSFEVTGYQPFILTGEIAKGLPPVRVPPFSVTMANGTVSFTRMVQDLGAGLAVVPLIGLLESIAVAKAFASQNDYHVDANQELLAIGLTNMLGSFVSSYPITGSFGRTAVNAQSGVCTPAGGLVTGALVLLSLDYLTSLFYYIPKAALAAVIIMAVVPLFDTKIFGMLWRVKRLDLLPLCATFLLCFWEVQYGILAGTLVSTLFLLHFVARPKTQVSEGPVLILQLASGLHFPAIETLRDIVLSRALEVTSPRPAVLECSHVCSIDYTVVLGLAGLLEDFRKQGVSLVFSGLQAPVLHTLLAADLKGFQNFPTLEKAEQYVRQELGMEPYNVCEDSVPEHKVTLLTA | null | null | oxalate transport [GO:0019532]; sulfate transport [GO:0008272] | apical plasma membrane [GO:0016324]; basolateral plasma membrane [GO:0016323]; endoplasmic reticulum [GO:0005783]; Golgi apparatus [GO:0005794]; lysosomal membrane [GO:0005765]; nucleoplasm [GO:0005654]; plasma membrane [GO:0005886] | chloride channel activity [GO:0005254]; chloride:bicarbonate antiporter activity [GO:0140900]; secondary active sulfate transmembrane transporter activity [GO:0008271] | PF01740;PF00916; | 3.30.750.24; | SLC26A/SulP transporter (TC 2.A.53) family | null | SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:Q86WA9}; Multi-pass membrane protein {ECO:0000255}. Lysosome membrane {ECO:0000250|UniProtKB:Q86WA9}; Multi-pass membrane protein {ECO:0000255}. Apical cell membrane {ECO:0000250|UniProtKB:Q80ZD3}; Multi-pass membrane protein {ECO:0000255}. Basolateral cell membrane {ECO:0000250|UniProtKB:Q80ZD3}; Multi-pass membrane protein {ECO:0000255}. | CATALYTIC ACTIVITY: Reaction=chloride(out) + hydrogencarbonate(in) = chloride(in) + hydrogencarbonate(out); Xref=Rhea:RHEA:72363, ChEBI:CHEBI:17544, ChEBI:CHEBI:17996; Evidence={ECO:0000269|PubMed:21593449}; CATALYTIC ACTIVITY: Reaction=H(+)(in) + sulfate(in) = H(+)(out) + sulfate(out); Xref=Rhea:RHEA:28574, ChEBI:CHEBI:15378, ChEBI:CHEBI:16189; Evidence={ECO:0000269|PubMed:21593449}; CATALYTIC ACTIVITY: Reaction=chloride(out) + oxalate(in) = chloride(in) + oxalate(out); Xref=Rhea:RHEA:72263, ChEBI:CHEBI:17996, ChEBI:CHEBI:30623; Evidence={ECO:0000269|PubMed:21593449}; | null | null | null | null | FUNCTION: Sodium-independent anion exchanger mediating bicarbonate, chloride, sulfate and oxalate transport (PubMed:21593449). Exhibits sodium-independent sulfate anion transporter activity that may cooperate with SLC26A2 to mediate DIDS-sensitive sulfate uptake into high endothelial venules endothelial cells (HEVEC) (By similarity). In the kidney, mediates chloride-bicarbonate exchange, facilitating V-ATPase-mediated acid secretion (By similarity). May function as a chloride channel, playing an important role in moderating chloride homeostasis and neuronal activity in the cerebellum (By similarity). {ECO:0000250|UniProtKB:Q80ZD3, ECO:0000250|UniProtKB:Q86WA9, ECO:0000269|PubMed:21593449}. | Cavia porcellus (Guinea pig) |
G3ECR1 | CAS9_STRTR | MLFNKCIIISINLDFSNKEKCMTKPYSIGLDIGTNSVGWAVITDNYKVPSKKMKVLGNTSKKYIKKNLLGVLLFDSGITAEGRRLKRTARRRYTRRRNRILYLQEIFSTEMATLDDAFFQRLDDSFLVPDDKRDSKYPIFGNLVEEKVYHDEFPTIYHLRKYLADSTKKADLRLVYLALAHMIKYRGHFLIEGEFNSKNNDIQKNFQDFLDTYNAIFESDLSLENSKQLEEIVKDKISKLEKKDRILKLFPGEKNSGIFSEFLKLIVGNQADFRKCFNLDEKASLHFSKESYDEDLETLLGYIGDDYSDVFLKAKKLYDAILLSGFLTVTDNETEAPLSSAMIKRYNEHKEDLALLKEYIRNISLKTYNEVFKDDTKNGYAGYIDGKTNQEDFYVYLKNLLAEFEGADYFLEKIDREDFLRKQRTFDNGSIPYQIHLQEMRAILDKQAKFYPFLAKNKERIEKILTFRIPYYVGPLARGNSDFAWSIRKRNEKITPWNFEDVIDKESSAEAFINRMTSFDLYLPEEKVLPKHSLLYETFNVYNELTKVRFIAESMRDYQFLDSKQKKDIVRLYFKDKRKVTDKDIIEYLHAIYGYDGIELKGIEKQFNSSLSTYHDLLNIINDKEFLDDSSNEAIIEEIIHTLTIFEDREMIKQRLSKFENIFDKSVLKKLSRRHYTGWGKLSAKLINGIRDEKSGNTILDYLIDDGISNRNFMQLIHDDALSFKKKIQKAQIIGDEDKGNIKEVVKSLPGSPAIKKGILQSIKIVDELVKVMGGRKPESIVVEMARENQYTNQGKSNSQQRLKRLEKSLKELGSKILKENIPAKLSKIDNNALQNDRLYLYYLQNGKDMYTGDDLDIDRLSNYDIDHIIPQAFLKDNSIDNKVLVSSASNRGKSDDFPSLEVVKKRKTFWYQLLKSKLISQRKFDNLTKAERGGLLPEDKAGFIQRQLVETRQITKHVARLLDEKFNNKKDENNRAVRTVKIITLKSTLVSQFRKDFELYKVREINDFHHAHDAYLNAVIASALLKKYPKLEPEFVYGDYPKYNSFRERKSATEKVYFYSNIMNIFKKSISLADGRVIERPLIEVNEETGESVWNKESDLATVRRVLSYPQVNVVKKVEEQNHGLDRGKPKGLFNANLSSKPKPNSNENLVGAKEYLDPKKYGGYAGISNSFAVLVKGTIEKGAKKKITNVLEFQGISILDRINYRKDKLNFLLEKGYKDIELIIELPKYSLFELSDGSRRMLASILSTNNKRGEIHKGNQIFLSQKFVKLLYHAKRISNTINENHRKYVENHKKEFEELFYYILEFNENYVGAKKNGKLLNSAFQSWQNHSIDELCSSFIGPTGSERKGLFELTSRGSAADFEFLGVKIPRYRDYTPSSLLKDATLIHQSVTGLYETRIDLAKLGEG | 3.1.-.- | COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000269|PubMed:22949671}; Note=Endonuclease activity on target DNA requires Mg(2+). {ECO:0000269|PubMed:22949671}; | defense response to virus [GO:0051607]; maintenance of CRISPR repeat elements [GO:0043571] | null | DNA binding [GO:0003677]; endonuclease activity [GO:0004519]; metal ion binding [GO:0046872]; RNA binding [GO:0003723] | PF16593;PF16595;PF16592;PF13395; | 1.10.30.50;3.30.420.10; | CRISPR-associated protein Cas9 family, Subtype II-A subfamily | null | null | null | null | null | null | null | FUNCTION: CRISPR (clustered regularly interspaced short palindromic repeat) is an adaptive immune system that provides protection against mobile genetic elements (viruses, transposable elements and conjugative plasmids). CRISPR clusters contain spacers, sequences complementary to antecedent mobile elements, and target invading nucleic acids. CRISPR clusters are transcribed and processed into CRISPR RNA (crRNA). In type II CRISPR systems correct processing of pre-crRNA requires a trans-encoded small RNA (tracrRNA), endogenous ribonuclease 3 (rnc) and Cas9. The tracrRNA serves as a guide for ribonuclease 3-aided processing of pre-crRNA (Probable). Cas9/crRNA/tracrRNA endonucleolytically cleaves linear or circular dsDNA target complementary to the spacer yielding blunt ends; Cas9 is inactive in the absence of the 2 guide RNAs (gRNA). Cas9 recognizes a 3'-G-rich protospacer adjacent motif (PAM, TGGTG in this organism) in the CRISPR repeat sequences to help distinguish self versus nonself, as targets within the bacterial CRISPR locus do not have PAMs. PAM recognition is also required for catalytic activity. When the CRISPR3/cas system consisting of cas9-cas1-cas2-csn2-CRISPR3 or just cas9-CRISPR3 is expressed in E.coli it prevents plasmids homologous to spacers 1 or 2 from transforming. {ECO:0000269|PubMed:21813460, ECO:0000269|PubMed:22949671, ECO:0000269|PubMed:23535272, ECO:0000305}. | Streptococcus thermophilus |
G3FEX6 | POLG_JAEVM | MTKKPGGPGKNRAINMLKRGLPRVFPLVGVKRVVMSLLDGRGPVRFVLALITFFKFTALAPTKALLGRWRAVEKSVAMKHLTSFKRELGTLIDAVNKRGKKQNKRGGNESSIMWLASLAIVIACAGAMKLSNFQGKLLMTINNTDIADVIVIPTSKGENRCWVRAIDVGYMCEDTITYECPKLAVGNDPEDVDCWCDNQEVYVQYGRCTRTRHSKRSRRSVSVQTHGESSLVNKKEAWLDSTKATRYLMKTENWIIRNPGYAFLAAALGWMLGSNSGQRVVFTILLLLVAPAYSFNCLGMGNRDFIEGASGATWVDLVLEGDSCLTIMANDKPTLDVRMINIEASQLAEVRSYCYHASVTDISTVARCPTTGEAHNEKRADSSYVCKQGFTDRGWGNGCGLFGKGSIDTCAKFSCTSKAIGRTIQPENIKYEVGVFVHGTTTSENHGNYSAQVGASQAAKFTVTPNAPSITLKLGDYGEVTLDCEPRSGLNTEAFYVMTVGSKSFLVHREWFHDLSLPWTSPSSTAWRNRELLMEFEEAHATKQSVVALGSQEGGLHQALAGAIVVEYSSSVKLTSGHLKCRLKMDKLALKGTTYGMCTEKFSFAKNPADTGHGTVVIELTYSGSDGPCKIPIVSVASLNDMTPVGRLVTVNPFVATSSSNSKVLVEMEPPFGDSYIVVGRGDKQINHHWYKAGSTLGKAFSTTLKGAQRLAALGDTAWDFGSIGGVFNSIGKAVHQVFGGAFRTLFGGMSWITQGLMGALLLWMGVNARDRSIALAFLATGGVLVFLATNVHADTGCAIDITRKEMRCGSGIFVHNDVEAWVDRYKYLPETPRSLAKIVHKAHQEGVCGVRSVTRLEHQMWESVRDELNVLLKENAVDLSVVVNKPVGRYRSAPKRLSMTQEKFEMGWKAWGKSILFAPELANSTFVVDGPETKECPDERRAWNSMQIEDFGFGITSTRVWLKIREENTDECDGAIIGTAVKGHVAVHSDLSYWIESRLNDTWKLERAVFGEVKSCTWPETHTLWGDGVEESELIIPHTIAGPRSKHNRREGYKTQNQGPWDENGIVLDFDYCPGTKVTITEDCGKRGPSIRTTTDSGKLITDWCCRSCSLPPLRFRTENGCWYGMEIRPVRHDETTLVRSQVDAFNGEMIDPFQLGLLVMFLATQEVLRKRWTARLTIPAVLGALLVLMLGGITYIDLARYVVLVAAAFAEANSGGDVLHLALIAVFKIQPAFLVMNMLSARWTNQENMVLVLGAAFFQLASVDLQIGVHGILNAAAIAWMIVRAITFPTTSTVAMPVLALLTPGMRALYLDTYRIILLVIGICSLLQERRKTMAKKKGAVLLGLALTSTGWFSPTTIAAGLMVCNPNKKRGWPATEFLSAVGLMFAIVGGLAELDIESMSIPFMLAGLMAVSYVISGKATDMWLDRAADISWEMEAAITGSSRRLDVKLDDDGDFHLIDDPGVPWKVWLLRMSCIGLAALTPWAIVPAAFGYWLTLKTTKRGGVFWDTPSPKPCLKGDTTTGVYRIMARGILGTYQAGVGVMYENVFHTLWHTTRGAAIMSGEGKLTPYWGSVKEDRISYGGPWRFDRKWNGTDDVQVIVVEPGKPAVNIQTKPGVFRTPFGEIGAVSLDYPRGTSGSPILDSNGDIIGLYGNGVELGDGSYVSAIVQGDRQEEPVPDAYTPSMLKKRQMTVLDLHPGSGKTRKILPQIIKDAIQQRLRTAVLAPTRVVAAEMAEALRGLPVRYQTSAVQREHQGNEIVDVMCHATLTHRLMSPNRVPNYNLFVMDEAHFTDPASIAARGYIATKVELGEAAAIFMTATPPGTTDPFPDSNAPIHDLQDEIPDRAWSSGYEWITEYAGKTVWFVASVKMGNEIAMCLQRAGKKVIQLNRKSYDTEYPKCKNGDWDFVITTDISEMGANFGASRVIDCRKSVKPTILEEGEGRVILGNPSPITSASAAQRRGRVGRNPNQVGDEYHYGGATSEDDSNLAHWTEAKIMLDNIHMPNGLVAQLYGPEREKAFTMDGEYRLRGEEKKNFLELLRTADLPVWLAYKVASNGIQYTDRKWCFDGPRTNAILEDNTEVEIVTRMGERKILKPRWLDARVYADHQALKWFKDFAAGKRSAVSFIEVLGRMPEHFMGKTREALDTMYLVATAEKGGKAHRMALEELPDALETITLIVAITVMTGGFFLLMMQRKGIGKMGLGALVLTLATFFLWAAEVPGTKIAGTLLVALLLMVVLIPEPEKQRSQTDNQLAVFLICVLTVVGVVAANEYGMLEKTKADLKSMFGGRTQAPGLTGLPSMALDLRPATAWALYGGSTVVLTPLLKHLITSEYVTTSLASISSQAGSLFVLPRGVPFTDLDLTVGLVFLGCWGQITLTTFLTAMVLVTLHYGYMLPGWQAEALRAAQRRTAAGIMKNAVVDGMVATDVPELERTTPLMQKKVGQVLLIGVSVAAFLVNPNVTTVREAGVLVTAATLTLWDNGASAVWNSTTATGLCHVMRGSYLAGGSIAWTLIKNADKPSLKRGRPGGRTLGEQWKEKLNAMSRDEFFKYRREAIIEVDRTEARRARRENNIVGGHPVSRGSAKLRWLVEKGFVSPIGKVIDLGCGRGGWSYYAATLKKVQEVKGYTKGGAGHEEPMLMQSYGWNLVSLKSGVDVFYKPSEPSDTLFCDIGESSPSPEVEEQRTLRVLEMTSDWLHRGPREFCIKVLCPYMPKVIEKMEVLQRRFGGGLVRLPLSRNSNHEMYWVSGAAGNVVHAVNMTSQVLLGRMDRTVWRGPKYEEDVNLGSGTRAVGKGEVHSNQEKIRKRIQKLREEFATTWHQDPEHPYRTWTYHGSYEVKATGSASSLVNGVVKLMSKPWDAIANVTTMAMTDTTPFGQQRVFKEKVDTKAPEPPAGVKEVLNETTNWLWAHLSREKRPRLCTKEEFIKKVNSNAALGAVFAEQNQWSTAREAVGDPLFWEMVDEERENHLRGECHTCIYNMMGKREKKPGEFGKAKGSRAIWFMWLGARYLEFEALGFLNEDHWLSRENSGGGVEGSGVQKLGYILRDIAGKQGGKMYADDTAGWDTRITRTDLENEAKVLELLDGEHRMLARAIIELTYRHKVVKVMRPAAGGKTVMDVISREDQRGSGQVVTYALNTFTNIAVQLVRLMEAEGVIGPQHLEQLPRKNKIAVRTWLFENGEERVTRMAISGDDCVVKPLDDRFATALHFLNAMSKVRKDIQEWKPSHGWHDWQQVPFCSNHFQEIVMKDGRSIVVPCRGQDELIGRARISPGAGWNVKDTACLAKAYAQMWLLLYFHRRDLRLMANAICSAVPVDWVPTGRTSWSIHSKGEWMTTEDMLQVWNRVWIEENEWMMDKTPITSWTDVPYVGKREDIWCGSLIGTRSRATWAENIYAAINQVRAVIGKENYVDYMSSLRRYEDVLIQEDRVI | 2.1.1.56; 2.1.1.57; 2.7.7.48; 3.4.21.91; 3.6.1.15; 3.6.4.13 | COFACTOR: Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Note=For RNA-directed RNA polymerase NS5 activity; Mn(2+) is more effective than Mg(2+). {ECO:0000250|UniProtKB:P27395}; | clathrin-dependent endocytosis of virus by host cell [GO:0075512]; fusion of virus membrane with host endosome membrane [GO:0039654]; induction by virus of host autophagy [GO:0039520]; proteolysis [GO:0006508]; symbiont-mediated suppression of host JAK-STAT cascade via inhibition of host TYK2 activity [GO:0039574]; symbiont-mediated suppression of host JAK-STAT cascade via inhibition of STAT1 activity [GO:0039563]; symbiont-mediated suppression of host JAK-STAT cascade via inhibition of STAT2 activity [GO:0039564]; symbiont-mediated suppression of host type I interferon-mediated signaling pathway [GO:0039502]; viral RNA genome replication [GO:0039694]; virion attachment to host cell [GO:0019062]; virus-mediated perturbation of host defense response [GO:0019049] | extracellular region [GO:0005576]; host cell endoplasmic reticulum membrane [GO:0044167]; host cell nucleus [GO:0042025]; host cell perinuclear region of cytoplasm [GO:0044220]; host cell surface [GO:0044228]; membrane [GO:0016020]; viral capsid [GO:0019028]; viral envelope [GO:0019031]; virion membrane [GO:0055036] | ATP binding [GO:0005524]; ATP hydrolysis activity [GO:0016887]; double-stranded RNA binding [GO:0003725]; metal ion binding [GO:0046872]; mRNA (nucleoside-2'-O-)-methyltransferase activity [GO:0004483]; mRNA 5'-cap (guanine-N7-)-methyltransferase activity [GO:0004482]; protein dimerization activity [GO:0046983]; RNA helicase activity [GO:0003724]; RNA-dependent RNA polymerase activity [GO:0003968]; serine-type endopeptidase activity [GO:0004252]; structural molecule activity [GO:0005198] | PF20907;PF01003;PF07652;PF21659;PF02832;PF00869;PF01004;PF00948;PF01005;PF01002;PF01350;PF01349;PF00972;PF20483;PF01570;PF01728;PF00949; | 1.10.10.930;1.10.260.90;1.20.1280.260;2.40.10.120;2.60.40.350;1.10.8.970;2.60.260.50;3.30.70.2840;3.40.50.300;2.60.98.10;3.40.50.150;3.30.67.10;3.30.387.10; | Class I-like SAM-binding methyltransferase superfamily, mRNA cap 0-1 NS5-type methyltransferase family | PTM: [Genome polyprotein]: Specific enzymatic cleavages in vivo yield mature proteins (By similarity). Cleavages in the lumen of endoplasmic reticulum are performed by host signal peptidase, whereas cleavages in the cytoplasmic side are performed by serine protease NS3. Signal cleavage at the 2K-4B site requires a prior NS3 protease-mediated cleavage at the 4A-2K site. {ECO:0000250|UniProtKB:P17763, ECO:0000250|UniProtKB:P27395}.; PTM: [Protein prM]: Cleaved in post-Golgi vesicles by a host furin, releasing the mature small envelope protein M, and peptide pr. This cleavage is incomplete as up to 30% of viral particles still carry uncleaved prM. {ECO:0000250|UniProtKB:P17763}.; PTM: [Envelope protein E]: N-glycosylated. {ECO:0000250|UniProtKB:P17763}.; PTM: [Non-structural protein 1]: N-glycosylated. The excreted form is glycosylated and this is required for efficient secretion of the protein from infected cells. {ECO:0000250|UniProtKB:P17763}.; PTM: [Serine protease NS3]: Acetylated by host KAT5. Acetylation modulates NS3 RNA-binding and unwinding activities and plays an important positive role for viral replication. {ECO:0000250|UniProtKB:Q32ZE1}.; PTM: [RNA-directed RNA polymerase NS5]: Phosphorylated on serines residues. This phosphorylation may trigger NS5 nuclear localization. {ECO:0000250|UniProtKB:P17763}. | SUBCELLULAR LOCATION: [Genome polyprotein]: Host endoplasmic reticulum membrane {ECO:0000255}; Multi-pass membrane protein {ECO:0000255}.; SUBCELLULAR LOCATION: [Capsid protein C]: Virion {ECO:0000250|UniProtKB:P17763}. Host nucleus {ECO:0000250|UniProtKB:P17763}. Host cytoplasm {ECO:0000250|UniProtKB:P06935}. Host cytoplasm, host perinuclear region {ECO:0000250|UniProtKB:P06935}.; SUBCELLULAR LOCATION: [Peptide pr]: Secreted {ECO:0000250|UniProtKB:P17763}.; SUBCELLULAR LOCATION: [Small envelope protein M]: Virion membrane {ECO:0000250|UniProtKB:P03314}; Multi-pass membrane protein {ECO:0000250|UniProtKB:P03314}. Host endoplasmic reticulum membrane {ECO:0000250|UniProtKB:P03314}; Multi-pass membrane protein {ECO:0000255}. Note=ER membrane retention is mediated by the transmembrane domains. {ECO:0000250|UniProtKB:P03314}.; SUBCELLULAR LOCATION: [Envelope protein E]: Virion membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000250|UniProtKB:P03314}. Host endoplasmic reticulum membrane {ECO:0000250|UniProtKB:P03314}; Multi-pass membrane protein {ECO:0000255}. Host cell surface {ECO:0000250|UniProtKB:P03314}. Note=ER membrane retention is mediated by the transmembrane domains. {ECO:0000250|UniProtKB:P03314}.; SUBCELLULAR LOCATION: [Non-structural protein 1]: Secreted {ECO:0000250|UniProtKB:P17763}. Host endoplasmic reticulum membrane; Peripheral membrane protein; Lumenal side {ECO:0000250|UniProtKB:P17763}. Note=Located in RE-derived vesicles hosting the replication complex. {ECO:0000250|UniProtKB:Q9Q6P4}.; SUBCELLULAR LOCATION: [Non-structural protein 2A]: Host endoplasmic reticulum membrane {ECO:0000250|UniProtKB:P14335}; Multi-pass membrane protein {ECO:0000250|UniProtKB:P17763}.; SUBCELLULAR LOCATION: [Serine protease subunit NS2B]: Host endoplasmic reticulum membrane; Multi-pass membrane protein {ECO:0000250|UniProtKB:P17763}.; SUBCELLULAR LOCATION: [Serine protease NS3]: Host endoplasmic reticulum membrane {ECO:0000255|PROSITE-ProRule:PRU00860}; Peripheral membrane protein {ECO:0000255|PROSITE-ProRule:PRU00860}; Cytoplasmic side {ECO:0000255|PROSITE-ProRule:PRU00860}. Note=Remains non-covalently associated to serine protease subunit NS2B. {ECO:0000255|PROSITE-ProRule:PRU00860}.; SUBCELLULAR LOCATION: [Non-structural protein 4A]: Host endoplasmic reticulum membrane {ECO:0000250|UniProtKB:P14335}; Multi-pass membrane protein {ECO:0000250|UniProtKB:P17763}. Note=Located in RE-associated vesicles hosting the replication complex. {ECO:0000250|UniProtKB:P17763}.; SUBCELLULAR LOCATION: [Non-structural protein 4B]: Host endoplasmic reticulum membrane {ECO:0000250|UniProtKB:P17763}; Multi-pass membrane protein {ECO:0000250|UniProtKB:P17763}. Note=Located in RE-derived vesicles hosting the replication complex. {ECO:0000250|UniProtKB:Q9Q6P4}.; SUBCELLULAR LOCATION: [RNA-directed RNA polymerase NS5]: Host endoplasmic reticulum membrane; Peripheral membrane protein; Cytoplasmic side {ECO:0000250|UniProtKB:P17763}. Host nucleus {ECO:0000250|UniProtKB:P27395}. Note=Located in RE-associated vesicles hosting the replication complex. NS5 protein is mainly localized in the nucleus rather than in ER vesicles. {ECO:0000250|UniProtKB:P17763}. | CATALYTIC ACTIVITY: Reaction=Selective hydrolysis of -Xaa-Xaa-|-Yaa- bonds in which each of the Xaa can be either Arg or Lys and Yaa can be either Ser or Ala.; EC=3.4.21.91; Evidence={ECO:0000250|UniProtKB:P27395}; CATALYTIC ACTIVITY: Reaction=a ribonucleoside 5'-triphosphate + H2O = a ribonucleoside 5'-diphosphate + H(+) + phosphate; Xref=Rhea:RHEA:23680, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:43474, ChEBI:CHEBI:57930, ChEBI:CHEBI:61557; EC=3.6.1.15; Evidence={ECO:0000250|UniProtKB:P27395}; CATALYTIC ACTIVITY: Reaction=a ribonucleoside 5'-triphosphate + RNA(n) = diphosphate + RNA(n+1); Xref=Rhea:RHEA:21248, Rhea:RHEA-COMP:14527, Rhea:RHEA-COMP:17342, ChEBI:CHEBI:33019, ChEBI:CHEBI:61557, ChEBI:CHEBI:140395; EC=2.7.7.48; Evidence={ECO:0000255|PROSITE-ProRule:PRU00539}; CATALYTIC ACTIVITY: Reaction=ATP + H2O = ADP + H(+) + phosphate; Xref=Rhea:RHEA:13065, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:456216; EC=3.6.4.13; Evidence={ECO:0000250|UniProtKB:P27395}; CATALYTIC ACTIVITY: Reaction=a 5'-end (5'-triphosphoguanosine)-ribonucleoside in mRNA + S-adenosyl-L-methionine = a 5'-end (N(7)-methyl 5'-triphosphoguanosine)-ribonucleoside in mRNA + S-adenosyl-L-homocysteine; Xref=Rhea:RHEA:67008, Rhea:RHEA-COMP:17166, Rhea:RHEA-COMP:17167, ChEBI:CHEBI:57856, ChEBI:CHEBI:59789, ChEBI:CHEBI:156461, ChEBI:CHEBI:167617; EC=2.1.1.56; Evidence={ECO:0000255|PROSITE-ProRule:PRU00924}; CATALYTIC ACTIVITY: Reaction=a 5'-end (N(7)-methyl 5'-triphosphoguanosine)-ribonucleoside in mRNA + S-adenosyl-L-methionine = a 5'-end (N(7)-methyl 5'-triphosphoguanosine)-(2'-O-methyl-ribonucleoside) in mRNA + H(+) + S-adenosyl-L-homocysteine; Xref=Rhea:RHEA:67020, Rhea:RHEA-COMP:17167, Rhea:RHEA-COMP:17168, ChEBI:CHEBI:15378, ChEBI:CHEBI:57856, ChEBI:CHEBI:59789, ChEBI:CHEBI:156461, ChEBI:CHEBI:167609; EC=2.1.1.57; Evidence={ECO:0000255|PROSITE-ProRule:PRU00924}; | null | null | null | null | FUNCTION: [Capsid protein C]: Plays a role in virus budding by binding to the cell membrane and gathering the viral RNA into a nucleocapsid that forms the core of a mature virus particle. During virus entry, may induce genome penetration into the host cytoplasm after hemifusion induced by the surface proteins. Can migrate to the cell nucleus where it modulates host functions. Overcomes the anti-viral effects of host EXOC1 by sequestering and degrading the latter through the proteasome degradation pathway. {ECO:0000250|UniProtKB:P17763}.; FUNCTION: [Capsid protein C]: Inhibits RNA silencing by interfering with host Dicer. {ECO:0000250|UniProtKB:P03314}.; FUNCTION: [Peptide pr]: Prevents premature fusion activity of envelope proteins in trans-Golgi by binding to envelope protein E at pH6.0. After virion release in extracellular space, gets dissociated from E dimers. {ECO:0000250|UniProtKB:P17763}.; FUNCTION: [Protein prM]: Acts as a chaperone for envelope protein E during intracellular virion assembly by masking and inactivating envelope protein E fusion peptide. prM is the only viral peptide matured by host furin in the trans-Golgi network probably to avoid catastrophic activation of the viral fusion activity in acidic Golgi compartment prior to virion release. prM-E cleavage is inefficient, and many virions are only partially matured. These uncleaved prM would play a role in immune evasion. {ECO:0000250|UniProtKB:P17763}.; FUNCTION: [Small envelope protein M]: May play a role in virus budding. Exerts cytotoxic effects by activating a mitochondrial apoptotic pathway through M ectodomain. May display a viroporin activity. {ECO:0000250|UniProtKB:P17763}.; FUNCTION: [Envelope protein E]: Binds to host cell surface receptor and mediates fusion between viral and cellular membranes. Efficient virus attachment to cell is, at least in part, mediated by host HSPA5. Envelope protein is synthesized in the endoplasmic reticulum in the form of heterodimer with protein prM. They play a role in virion budding in the ER, and the newly formed immature particle is covered with 60 spikes composed of heterodimer between precursor prM and envelope protein E. The virion is transported to the Golgi apparatus where the low pH causes dissociation of PrM-E heterodimers and formation of E homodimers. prM-E cleavage is inefficient, and many virions are only partially matured. These uncleaved prM would play a role in immune evasion. {ECO:0000250|UniProtKB:P17763}.; FUNCTION: [Non-structural protein 1]: Involved in immune evasion, pathogenesis and viral replication. Once cleaved off the polyprotein, is targeted to three destinations: the viral replication cycle, the plasma membrane and the extracellular compartment. Essential for viral replication. Required for formation of the replication complex and recruitment of other non-structural proteins to the ER-derived membrane structures. Excreted as a hexameric lipoparticle that plays a role against host immune response. Antagonizing the complement function. Binds to the host macrophages and dendritic cells. Inhibits signal transduction originating from Toll-like receptor 3 (TLR3). {ECO:0000250|UniProtKB:Q9Q6P4}.; FUNCTION: [Non-structural protein 2A]: Component of the viral RNA replication complex that functions in virion assembly and antagonizes the host alpha/beta interferon antiviral response. {ECO:0000250|UniProtKB:P14335}.; FUNCTION: [Serine protease subunit NS2B]: Required cofactor for the serine protease function of NS3 (By similarity). May have membrane-destabilizing activity and form viroporins (By similarity). {ECO:0000250|UniProtKB:P17763, ECO:0000250|UniProtKB:P27395}.; FUNCTION: [Serine protease NS3]: Displays three enzymatic activities: serine protease, NTPase and RNA helicase. NS3 serine protease, in association with NS2B, performs its autocleavage and cleaves the polyprotein at dibasic sites in the cytoplasm: C-prM, NS2A-NS2B, NS2B-NS3, NS3-NS4A, NS4A-2K and NS4B-NS5. NS3 RNA helicase binds RNA and unwinds dsRNA in the 3' to 5' direction. {ECO:0000255|PROSITE-ProRule:PRU00860}.; FUNCTION: [Non-structural protein 4A]: Regulates the ATPase activity of the NS3 helicase activity (By similarity). NS4A allows NS3 helicase to conserve energy during unwinding (By similarity). {ECO:0000250|UniProtKB:Q9Q6P4}.; FUNCTION: [Peptide 2k]: Functions as a signal peptide for NS4B and is required for the interferon antagonism activity of the latter. {ECO:0000250|UniProtKB:P17763}.; FUNCTION: [Non-structural protein 4B]: Induces the formation of ER-derived membrane vesicles where the viral replication takes place (By similarity). Inhibits interferon (IFN)-induced host STAT1 phosphorylation and nuclear translocation, thereby preventing the establishment of cellular antiviral state by blocking the IFN-alpha/beta pathway (By similarity). Inhibits STAT2 translocation in the nucleus after IFN-alpha treatment (By similarity). {ECO:0000250|UniProtKB:Q9Q6P4}.; FUNCTION: [RNA-directed RNA polymerase NS5]: Replicates the viral (+) and (-) RNA genome (By similarity). Performs the capping of genomes in the cytoplasm. NS5 methylates viral RNA cap at guanine N-7 and ribose 2'-O positions (By similarity). Besides its role in RNA genome replication, also prevents the establishment of cellular antiviral state by blocking the interferon-alpha/beta (IFN-alpha/beta) signaling pathway (By similarity). Inhibits host TYK2 and STAT2 phosphorylation, thereby preventing activation of JAK-STAT signaling pathway (By similarity). {ECO:0000250|UniProtKB:P27395, ECO:0000250|UniProtKB:Q9Q6P4}. | Japanese encephalitis virus (strain M28) (JEV) |
G3FNQ9 | SPAZ_ORBOL | MLTNGLISLLAIAGLATNAFAGPIRKVSNAGAAGAIADKYIVVLKKGLSDSAVSKHTNRISSFHSNVARDLTGARAHGVGRKFRFSSTGFNGYVGGFDKATLQEILNSPEVDYVEQDTVVTTYAEQTDSTWGLDRISHEDYSAPYTYEYDETAAGAGTTVYVIDTGIRISHDEFQTVNGSSRATWGFNSVDKTDSDGNGHGTHCAGTIAGKTYGVSKKAKVVAVKVLSAGGSGSTAGVVSGMNWVAENATPNFSVASMSLGGSKSTALNAAVDCIFNAGITIVVAAGNENQDAKNVSPASAPNAITVGAIDSSNKIASLSNWGTLIDVFAPGVGVLSSWATSDKETKTISGTSMACPHVAGLAAYYISASEGGADPATITDKITSSRRQWSGHREHPWLPKQDRLQRICLSTHSPKTNHQVTIVAS | 3.4.21.- | null | collagen catabolic process [GO:0030574]; proteolysis [GO:0006508] | extracellular space [GO:0005615] | serine-type endopeptidase activity [GO:0004252] | PF05922;PF00082; | 3.30.70.80;3.40.50.200; | Peptidase S8 family | null | SUBCELLULAR LOCATION: Secreted {ECO:0000250}. | null | null | null | BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 6-8. {ECO:0000269|Ref.1}; | BIOPHYSICOCHEMICAL PROPERTIES: Temperature dependence: Optimum temperature is 45 degrees Celsius. {ECO:0000269|Ref.1}; | FUNCTION: Hydrolyzes gelatin, casein, the chromogenic substrate azocoll and the cuticle of the nematode P.redivivus. Immobilizes P.redivivus. {ECO:0000269|Ref.1}. | Orbilia oligospora (Nematode-trapping fungus) (Arthrobotrys oligospora) |
G3GTP0 | DNLI4_CRIGR | MATSQTSQTVAAHVPFADLCSTLERIQKSKERAEKIRHFKEFLDSWRKFHDALHKNKKDVTDSFYPAMRLILPQLERERMAYGIKETMLAKLYIELLNLPREGKDALKLLNYRTPSGARTDAGDFAVIAYFVLKPRCLQKGSLTIQQVNELLDLVASNNSGKRKDLVKKSLLQLITQSSALEQKWLIRMIIKDLKLGVSQQTILNIFHNDAVELHNVTTDLEKVCRQLHDPAVGLSDISITLFSAFKPMLAAVADVERVEKDMKQQSFYIETKLDGERMQMHKDGSVYQYFSRNGYNYTDQFGASPQEGTLTPFIHDAFRTDVQVCILDGEMMAYNPTTQTFMQKGVKFDIKRMVEDSDLQTCYCVFDVLMVNNKKLGRETLRKRYDILNSTFTPIQGRIEIVQKKLAQTKNEVVDALNEAIDKREEGIMIKHPLSIYKPDKRGEGWLKIKPEYVSGLMDELDLLIVGGYWGKGSRGGMMSHFLCAVAEKPPHGEKPSVFHTLCRVGSGYTMKELYDLGLKLAKYWKPFHKKSPPSSILCGTEKPEVYIEPCNSVIVQIKAAEIVPSDMYKTGTTLRFPRIEKIRDDKEWHECMTLGDLEELRGKASGKLATKHLHVGDDDEPREKRRKPVSKMKKTIGIIEHLKAPNLSNISKVSNVFEDVEFCVMSGLDGYPKSDLENRIAEFGGYIVQNPGPDTYCVIAGCENIRVKNIISSDQHDVVKPEWLLECFKTKTCVPWQPRFMIHMCPSTKQHFAREYDCYGDSYFVDTDLDQLKEVFLGIKKAGEHQTPEEMAPVIADLEYRYSWDHSPLCMFRHCTVYLDLYAVINDSSSKIKATRLDVTALELRFHGAKVVSHLSEGVSHVIIGENQSRVSDFKVFRRTLKKKFKILQERWVTDSVDKGELQEENQYLL | 6.5.1.1 | COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250|UniProtKB:P49917}; | cell cycle [GO:0007049]; cell division [GO:0051301]; cellular response to ionizing radiation [GO:0071479]; central nervous system development [GO:0007417]; chromosome organization [GO:0051276]; DN2 thymocyte differentiation [GO:1904155]; DNA biosynthetic process [GO:0071897]; DNA ligation involved in DNA recombination [GO:0051102]; DNA ligation involved in DNA repair [GO:0051103]; double-strand break repair via classical nonhomologous end joining [GO:0097680]; fibroblast proliferation [GO:0048144]; immunoglobulin V(D)J recombination [GO:0033152]; in utero embryonic development [GO:0001701]; isotype switching [GO:0045190]; negative regulation of neuron apoptotic process [GO:0043524]; neurogenesis [GO:0022008]; neuron apoptotic process [GO:0051402]; nucleotide-excision repair, DNA gap filling [GO:0006297]; positive regulation of chromosome organization [GO:2001252]; positive regulation of fibroblast proliferation [GO:0048146]; positive regulation of neurogenesis [GO:0050769]; pro-B cell differentiation [GO:0002328]; response to gamma radiation [GO:0010332]; response to X-ray [GO:0010165]; single strand break repair [GO:0000012]; somatic stem cell population maintenance [GO:0035019]; stem cell proliferation [GO:0072089]; T cell receptor V(D)J recombination [GO:0033153] | condensed chromosome [GO:0000793]; DNA ligase IV complex [GO:0032807]; DNA-dependent protein kinase-DNA ligase 4 complex [GO:0005958]; nucleoplasm [GO:0005654] | ATP binding [GO:0005524]; DNA binding [GO:0003677]; DNA ligase (ATP) activity [GO:0003910]; magnesium ion binding [GO:0000287] | PF00533;PF04679;PF01068;PF04675;PF11411; | 6.10.250.520;3.40.50.10190;1.10.3260.10;3.30.470.30;2.40.50.140; | ATP-dependent DNA ligase family | null | SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:P49917}. | CATALYTIC ACTIVITY: Reaction=ATP + (deoxyribonucleotide)n-3'-hydroxyl + 5'-phospho-(deoxyribonucleotide)m = (deoxyribonucleotide)n+m + AMP + diphosphate.; EC=6.5.1.1; Evidence={ECO:0000255|PROSITE-ProRule:PRU10135}; | null | null | null | null | FUNCTION: DNA ligase involved in DNA non-homologous end joining (NHEJ); required for double-strand break (DSB) repair and V(D)J recombination. Catalyzes the NHEJ ligation step of the broken DNA during DSB repair by resealing the DNA breaks after the gap filling is completed. Joins single-strand breaks in a double-stranded polydeoxynucleotide in an ATP-dependent reaction. LIG4 is mechanistically flexible: it can ligate nicks as well as compatible DNA overhangs alone, while in the presence of XRCC4, it can ligate ends with 2-nucleotides (nt) microhomology and 1-nt gaps. Forms a subcomplex with XRCC4; the LIG4-XRCC4 subcomplex is responsible for the NHEJ ligation step and XRCC4 enhances the joining activity of LIG4. Binding of the LIG4-XRCC4 complex to DNA ends is dependent on the assembly of the DNA-dependent protein kinase complex DNA-PK to these DNA ends. LIG4 regulates nuclear localization of XRCC4. {ECO:0000250|UniProtKB:P49917}. | Cricetulus griseus (Chinese hamster) (Cricetulus barabensis griseus) |
G3HIK4 | CETP_CRIGR | MLAVTLLSLALLGSTCACSTSTSYEAGIVCRITKAALLVLNQETAKVIQTAFQRASYPDIKGERSMMLLGRVTYGLHNIQISHLSIASSQVELVEAKSVDVSIQNASVIFKGTLNYGYKGAWGLNIEQSVDFEIESAIDLQINTKLTCDSGHVRTDAPDCSISFHKLLLHLQGEREPGWTKQLFTNIISFTLKMVLKGQVCKEINVISNIMADFVQTRAANIISDRDIEVDISLTRSPIITATYLESHHKGHFIYKNISEVLPLPAFSPTLLGDTRMLYFWFSEQVLDSLAKAAFQDGRLQLNLAETELKVVLETWHFNPNQEIIPEVITGFPSPGQVTVHCPRRPTISCQNKGVVVSSPVVMEFLFPHKDGQDSVTHTFEEDIVATIQASYSKKKLFLSLVDFQIKPKTTSNMAESSESIQNFLQLMITTVGIPEIMSRLEVALTTLMNSKGLDLFDIINPEIITRDGFLLLQMDFGFPEHLLVDFLQSLN | null | null | cholesterol homeostasis [GO:0042632]; cholesterol metabolic process [GO:0008203]; cholesterol transport [GO:0030301]; high-density lipoprotein particle remodeling [GO:0034375]; low-density lipoprotein particle remodeling [GO:0034374]; phosphatidylcholine metabolic process [GO:0046470]; phospholipid homeostasis [GO:0055091]; reverse cholesterol transport [GO:0043691]; triglyceride homeostasis [GO:0070328]; triglyceride metabolic process [GO:0006641]; triglyceride transport [GO:0034197]; very-low-density lipoprotein particle remodeling [GO:0034372] | extracellular space [GO:0005615]; high-density lipoprotein particle [GO:0034364] | cholesterol binding [GO:0015485]; cholesterol transfer activity [GO:0120020]; phosphatidylcholine binding [GO:0031210]; phospholipid transporter activity [GO:0005548]; triglyceride binding [GO:0017129] | PF01273;PF02886; | null | BPI/LBP/Plunc superfamily, BPI/LBP family | null | SUBCELLULAR LOCATION: Secreted {ECO:0000250|UniProtKB:P11597}. Note=Secreted in plasma. {ECO:0000250|UniProtKB:P11597}. | CATALYTIC ACTIVITY: Reaction=cholesteryl (9Z-octadecenoate)(in) = cholesteryl (9Z-octadecenoate)(out); Xref=Rhea:RHEA:43348, ChEBI:CHEBI:46898; Evidence={ECO:0000250|UniProtKB:P11597}; CATALYTIC ACTIVITY: Reaction=1,2,3-tri-(9Z-octadecenoyl)-glycerol(in) = 1,2,3-tri-(9Z-octadecenoyl)-glycerol(out); Xref=Rhea:RHEA:43352, ChEBI:CHEBI:53753; Evidence={ECO:0000250|UniProtKB:P11597}; CATALYTIC ACTIVITY: Reaction=cholesteryl (9Z,12Z)-octadecadienoate(in) = cholesteryl (9Z,12Z)-octadecadienoate(out); Xref=Rhea:RHEA:43356, ChEBI:CHEBI:41509; Evidence={ECO:0000250|UniProtKB:P11597}; | null | null | null | null | FUNCTION: Involved in the transfer of neutral lipids, including cholesteryl ester and triglyceride, among lipoprotein particles. Allows the net movement of cholesteryl ester from high density lipoproteins/HDL to triglyceride-rich very low density lipoproteins/VLDL, and the equimolar transport of triglyceride from VLDL to HDL (PubMed:24293641). Regulates the reverse cholesterol transport, by which excess cholesterol is removed from peripheral tissues and returned to the liver for elimination (By similarity). {ECO:0000250|UniProtKB:P11597, ECO:0000269|PubMed:24293641}. | Cricetulus griseus (Chinese hamster) (Cricetulus barabensis griseus) |
G3HKI1 | XRCC4_CRIGR | MERKVSRISLASEPNITYFLQVSWEETVGSGFVITLTDGHSAWTATVSESEISQEADDMAMEKEKYADELRKALVSGSGSDTYKFIFSRESCHFSLEKELKDVSFRLGSFNLDKVPNSTEVIRELICYCLDTIAEKQAKNEHLQKENDRLLRDWNDVQGRFEKCVIAKEALEADLYQRFILVLNEKKTKIRSLHKLLDEIQQLEKNLKPERETKCSEKTTDQDAIYDGSTDEEAGASVLAEAAVCKEDSLFSSPDVTDIAPSRKRRHHMQKNLGTEPKMAPQEQQLQGKERLASSLPHTLKEEHEHTSAGNMSLETLRNSSPEDIFD | null | null | DNA ligation involved in DNA repair [GO:0051103]; double-strand break repair via nonhomologous end joining [GO:0006303]; immunoglobulin V(D)J recombination [GO:0033152]; response to X-ray [GO:0010165] | cytoplasm [GO:0005737]; DNA ligase IV complex [GO:0032807]; DNA-dependent protein kinase-DNA ligase 4 complex [GO:0005958]; nucleus [GO:0005634]; site of double-strand break [GO:0035861] | DNA binding [GO:0003677] | PF06632; | 1.20.5.370;2.170.210.10; | XRCC4-XLF family, XRCC4 subfamily | PTM: Phosphorylated by PRKDC at the C-terminus in response to DNA damage; Ser-253 constitutes the main phosphorylation sites. Phosphorylations by PRKDC at the C-terminus of XRCC4 and NHEJ1/XLF are highly redundant and regulate ability of the XRCC4-NHEJ1/XLF subcomplex to bridge DNA. Phosphorylation by PRKDC does not prevent interaction with NHEJ1/XLF but disrupts ability to bridge DNA and promotes detachment from DNA. Phosphorylation at Ser-320 and Ser-321 by PRKDC promotes recognition by the SCF(FBXW7) complex and subsequent ubiquitination via 'Lys-63'-linked ubiquitin. Phosphorylation at Thr-230 by CK2 promotes interaction with PNKP; regulating PNKP activity and localization to DNA damage sites. Phosphorylation by CK2 promotes interaction with APTX. {ECO:0000250|UniProtKB:Q13426}.; PTM: Ubiquitinated at Lys-289 by the SCF(FBXW7) complex via 'Lys-63'-linked ubiquitination, thereby promoting double-strand break repair: the SCF(FBXW7) complex specifically recognizes XRCC4 when phosphorylated at Ser-320 and Ser-321 by PRKDC, and 'Lys-63'-linked ubiquitination facilitates DNA non-homologous end joining (NHEJ) by enhancing association with XRCC5/Ku80 and XRCC6/Ku70. Monoubiquitinated. {ECO:0000250|UniProtKB:Q13426}.; PTM: [DNA repair protein XRCC4]: Undergoes proteolytic processing by caspase-3 (CASP3). This generates the protein XRCC4, C-terminus (XRCC4/C), which translocates to the cytoplasm and activates phospholipid scramblase activity of XKR4, thereby promoting phosphatidylserine exposure on apoptotic cell surface. {ECO:0000250|UniProtKB:Q13426}. | SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q13426}. Chromosome {ECO:0000250|UniProtKB:Q13426}. Note=Localizes to site of double-strand breaks. {ECO:0000250|UniProtKB:Q13426}.; SUBCELLULAR LOCATION: [Protein XRCC4, C-terminus]: Cytoplasm {ECO:0000250|UniProtKB:Q13426}. Note=Translocates from the nucleus to the cytoplasm following cleavage by caspase-3 (CASP3). {ECO:0000250|UniProtKB:Q13426}. | null | null | null | null | null | FUNCTION: [DNA repair protein XRCC4]: DNA non-homologous end joining (NHEJ) core factor, required for double-strand break repair and V(D)J recombination (PubMed:18093953). Acts as a scaffold protein that regulates recruitment of other proteins to DNA double-strand breaks (DSBs). Associates with NHEJ1/XLF to form alternating helical filaments that bridge DNA and act like a bandage, holding together the broken DNA until it is repaired. The XRCC4-NHEJ1/XLF subcomplex binds to the DNA fragments of a DSB in a highly diffusive manner and robustly bridges two independent DNA molecules, holding the broken DNA fragments in close proximity to one other. The mobility of the bridges ensures that the ends remain accessible for further processing by other repair factors. Plays a key role in the NHEJ ligation step of the broken DNA during DSB repair via direct interaction with DNA ligase IV (LIG4): the LIG4-XRCC4 subcomplex reseals the DNA breaks after the gap filling is completed. XRCC4 stabilizes LIG4, regulates its subcellular localization and enhances LIG4's joining activity. Binding of the LIG4-XRCC4 subcomplex to DNA ends is dependent on the assembly of the DNA-dependent protein kinase complex DNA-PK to these DNA ends. Promotes displacement of PNKP from processed strand break termini (By similarity). {ECO:0000250|UniProtKB:Q13426, ECO:0000269|PubMed:18093953}.; FUNCTION: [Protein XRCC4, C-terminus]: Acts as an activator of the phospholipid scramblase activity of XKR4. This form, which is generated upon caspase-3 (CASP3) cleavage, translocates into the cytoplasm and interacts with XKR4, thereby promoting phosphatidylserine scramblase activity of XKR4 and leading to phosphatidylserine exposure on apoptotic cell surface. {ECO:0000250|UniProtKB:Q13426}. | Cricetulus griseus (Chinese hamster) (Cricetulus barabensis griseus) |
G3I6Z6 | NOTC1_CRIGR | MGRSDSRAGALLEGGCEQNIDPRRAAHCHHPRLATSSLRCSQPSGTCLNGGRCEVANGTEACVCSGPFVGQRCQDPNPCLSTPCKNAGTCHVVEHGGTVNYACSCPLGFSGPLCLTPLDNACLANPCRNGGTCDLLTLTEYKCRCPPGWSGKSCQQADPCASNPCANGGQCLPFESSYICGCPPGFHGPTCRQDVNECSQNPGLCRHGGTCHNEIGSYRCVCRATHTGPHCELPYVPCSPSPCQNGGTCRPTGDTTHECACLPGFAGQNCEENVDDCPGNNCKNGGACVDGVNTYNCRCPPEWTGQYCTEDVDECQLMPNACQNGGTCHNTHGGYNCVCVNGWTGEDCSENIDDCASAACFQGATCHDRVASFYCECPHGRTGLLCHLNDACISNPCNEGSNCDTNPVNGKAICTCPSGYTGPACSQDVDECALGANPCEHAGKCLNTLGSFECQCLQGYTGPRCEIDVNECISNPCQNDATCLDQIGEFQCICMPGYEGVYCEINTDECASSPCLHNGHCMDKINEFLCQCPKGFSGHLCQYDVDECASTPCKNGAKCLDGPNTYTCVCTEGYTGTHCEVDIDECDPDPCHYGFCKDGVATFTCLCQPGYTGHHCETNINECHSQPCRHGGTCQDRDNSYLCLCLKGTTGPNCEINLDDCASNPCDSGTCLDKIDGYECACEPGYTGSMCNVNIDECAGSPCHNGGTCEDGIAGFTCRCPEGYHDPTCLSEVNECNSNPCIHGACRDGLNGYKCDCAPGWSGTNCDINNNECESNPCVNGGTCKDMTSGYVCTCREGFSGPNCQTNINECASNPCLNQGTCIDDVAGYKCNCPLPYTGATCEVVLAPCATSPCKNSGVCKESEDYESFSCVCPTGWQGQTCEIDINECVKSPCRHGASCQNTNGSYRCLCQAGYTGRNCESDIDDCRPNPCHNGGSCTDGINMAFCDCLPGFQGAFCEEDINECASNPCRNGANCTDCVDSYTCTCPAGFNGIHCENNTPDCTESSCFNGGTCVDGINSFTCLCPPGFTGSYCQYDVNECDSRPCLHGGTCQDSYGTYKCTCPQGYTGLNCQNLVHWCDSAPCKNGGKCWQTNTQYHCECRSGWTGFNCDVLSVSCEVAAQKRGIDVTLLCQHGGLCVDEEDKHYCHCQAGYTGSYCEDEVDECSPNPCQNGATCTDYLGGFSCKCVAGYHGSNCSEEINECLSQPCQNGGTCIDLTNTYKCSCPRGTQGVHCEINVDDCHPHLDPASRSPKCFNNGTCVDQVGGYSCTCPPGFVGERCEGDINECLSNPCDPRGTQDCVQRVNDFHCECRAGHTGRRCESVINGCRGKPCKNGGVCAVASNTARGFICRCPAGFEGATCENDARTCGSLRCLNGGTCISGPRSPTCLCLGSFTGPECQFPASSPCVGSNPCYNQGTCEPTSESPFYRCLCPAKFNGLLCHILDYSFTGGAGRDIPPPQIEEACELPECQEDAGNKVCNLQCNNHACGWDGGDCSLNFNDPWKNCTQSLQCWKYFSDGHCDSQCNSASCLFDGFDCQRTEGQCNPLYDQYCKDHFSDGHCDQGCNSAECDWDGLDCADHVPERLAAGTLVLVVLLPPEQLRNNSFHFLRELSHVLHTNVVFKRDAEGQQMIFPYYGHEEELRKHPIKRSAVGWTTSSLLPSTNGGRQRRELDPMDIRGSIVYLEIDNRQCVQSSSQCFQSATDVAAFLGALASLGNLNIPYKIEAVKSETVEPPLPSQLHLMYLAAAAFVLLFFVGCGVLLSRKRRRQHGQLWFPEGFKVSEASKKKRREPLGEDSVGLKPLKNASDGALMDDNQNEWGDEDLETKKFRFEEPVVVPDLDDQTDHRQWTQQHLDAADLRMSAMAPTPPQGEVDADCMDVNVRGPDGFTPLMIASCSGGGLETGNSEEEEDAPAVISDFIYQGASLHNQTDRTGETALHLAARYSRSDAAKRLLEASADANIQDNMGRTPLHAAVSADAQGVFQILLRNRATDLDARMHDGTTPLILAARLAVEGMLEDLINSHADVNAVDDLGKSALHWAAAVNNVDAAVVLLKNGANKDMQNNKEETPLFLAAREGSYETAKVLLDHFANRDITDHMDRLPRDIAQERMHHDIVRLLDEYNLVRSPQLHGTALGGTPTLSPTLCSPNGYLGNLKSATQGKKARKPSTKGLACGSKEAKDLKARRKKSQDGKGCLLDSSSMLSPVDSLESPHGYLSDVASPPLLPSPFQQSPSMPLSHLPGMPDTHLGISHLNVAAKPEMAALAGSSRLAFEPPPPRLPHLPVASSASTVLSTNGSXGEEEWLAPSQYNPLRPGVASGTLSTQAAGLQHGMMGPLHSSLSTNTLSPMIYQGLPNTRLATQPHLVQTQQVQPQNLQIQPQNLQPPSQPHLSVSSAANGHLGRSFLGGEHSQADVQPLGPSSLPVHTILPQESQALPTSLPSSMVPPMTTTQFLTPPSQHSYSSSPVDNTPSHQLQVPEHPFLTPSPESPDQWSSSSPHSNISDWSEGISSPPTSMPSQITHIPEAFK | null | null | angiogenesis [GO:0001525]; cell differentiation [GO:0030154]; cilium assembly [GO:0060271]; Notch signaling involved in heart development [GO:0061314]; regulation of developmental process [GO:0050793]; regulation of DNA-templated transcription [GO:0006355] | adherens junction [GO:0005912]; apical plasma membrane [GO:0016324]; Golgi lumen [GO:0005796]; Golgi membrane [GO:0000139]; nucleus [GO:0005634] | calcium ion binding [GO:0005509]; signaling receptor activity [GO:0038023] | PF00023;PF12796;PF00008;PF07645;PF12661;PF06816;PF07684;PF00066; | 3.30.300.320;3.30.70.3310;1.25.40.20;2.10.25.10; | NOTCH family | PTM: Synthesized in the endoplasmic reticulum as an inactive form which is proteolytically cleaved by a furin-like convertase in the trans-Golgi network before it reaches the plasma membrane to yield an active, ligand-accessible form. Cleavage results in a C-terminal fragment N(TM) and a N-terminal fragment N(EC). Following ligand binding, it is cleaved by ADAM17 to yield a membrane-associated intermediate fragment called notch extracellular truncation (NEXT). Following endocytosis, this fragment is then cleaved by one of the catalytic subunits of gamma-secretase (PSEN1 or PSEN2) to release a Notch-derived peptide containing the intracellular domain (NICD) from the membrane. {ECO:0000250|UniProtKB:Q01705}.; PTM: Phosphorylated. {ECO:0000250}.; PTM: O-linked glycosylation by GALNT11 is involved in determination of left/right symmetry: glycosylation promotes activation of NOTCH1, possibly by promoting cleavage by ADAM17, modulating the balance between motile and immotile (sensory) cilia at the left-right organiser (LRO) (By similarity). O-glycosylated on the EGF-like domains (PubMed:10734111). O-glucosylated at Ser-451 by KDELC1 and KDELC2 (By similarity). Contains both O-linked fucose and O-linked glucose in the EGF-like domains 11, 12 and 13, which are interacting with the residues on DLL4. MFNG-, RFNG- and LFNG-mediated modification of O-fucose residues at specific EGF-like domains results in inhibition of its activation by JAG1 and enhancement of its activation by DLL1 via an increased binding to DLL1 (By similarity). {ECO:0000250|UniProtKB:P46531, ECO:0000250|UniProtKB:Q01705, ECO:0000250|UniProtKB:Q07008, ECO:0000269|PubMed:10734111}.; PTM: Ubiquitinated. Undergoes 'Lys-29'-linked polyubiquitination by ITCH; promotes the lysosomal degradation of non-activated internalized NOTCH1. Monoubiquitination at Lys-1765 is required for activation by gamma-secretase cleavage, it promotes interaction with AAK1, which stabilizes it. Deubiquitination by EIF3F is necessary for nuclear import of activated Notch. {ECO:0000250|UniProtKB:Q01705}.; PTM: Hydroxylated at Asn-1961 by HIF1AN. Hydroxylated at Asn-2028 by HIF1AN (By similarity). Hydroxylation reduces affinity for HI1AN and may thus indirectly modulate negative regulation of NICD (By similarity). {ECO:0000250}. | SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:Q01705}; Single-pass type I membrane protein {ECO:0000250|UniProtKB:Q01705}.; SUBCELLULAR LOCATION: [Notch 1 intracellular domain]: Nucleus {ECO:0000250|UniProtKB:Q01705}. Note=Following proteolytical processing NICD is translocated to the nucleus. Nuclear location may require MEGF10. {ECO:0000250|UniProtKB:Q01705}. | null | null | null | null | null | FUNCTION: Functions as a receptor for membrane-bound ligands Jagged-1 (JAG1), Jagged-2 (JAG2) and Delta-1 (DLL1) to regulate cell-fate determination. Upon ligand activation through the released notch intracellular domain (NICD) it forms a transcriptional activator complex with RBPJ/RBPSUH and activates genes of the enhancer of split locus. Affects the implementation of differentiation, proliferation and apoptotic programs. Involved in angiogenesis; negatively regulates endothelial cell proliferation and migration and angiogenic sprouting. Involved in the maturation of both CD4(+) and CD8(+) cells in the thymus. Important for follicular differentiation and possibly cell fate selection within the follicle. During cerebellar development, functions as a receptor for neuronal DNER and is involved in the differentiation of Bergmann glia. Represses neuronal and myogenic differentiation. May play an essential role in postimplantation development, probably in some aspect of cell specification and/or differentiation. May be involved in mesoderm development, somite formation and neurogenesis. May enhance HIF1A function by sequestering HIF1AN away from HIF1A (By similarity). Required for the THBS4 function in regulating protective astrogenesis from the subventricular zone (SVZ) niche after injury. Involved in determination of left/right symmetry by modulating the balance between motile and immotile (sensory) cilia at the left-right organiser (LRO) (By similarity). {ECO:0000250|UniProtKB:Q01705}. | Cricetulus griseus (Chinese hamster) (Cricetulus barabensis griseus) |
G3I8R9 | BIP_CRIGR | MKFPMVAAALLLLCAVRAEEEDKKEDVGTVVGIDLGTTYSCVGVFKNGRVEIIANDQGNRITPSYVAFTPEGERLIGDAAKNQLTSNPENTVFDAKRLIGRTWNDPSVQQDIKFLPFKVVEKKTKPYIQVDIGGGQTKTFAPEEISAMVLTKMKETAEAYLGKKVTHAVVTVPAYFNDAQRQATKDAGTIAGLNVMRIINEPTAAAIAYGLDKREGEKNILVFDLGGGTFDVSLLTIDNGVFEVVATNGDTHLGGEDFDQRVMEHFIKLYKKKTGKDVRKDNRAVQKLRREVEKAKRALSSQHQARIEIESFFEGEDFSETLTRAKFEELNMDLFRSTMKPVQKVLEDSDLKKSDIDEIVLVGGSTRIPKIQQLVKEFFNGKEPSRGINPDEAVAYGAAVQAGVLSGDQDTGDLVLLDVCPLTLGIETVGGVMTKLIPRNTVVPTKKSQIFSTASDNQPTVTIKVYEGERPLTKDNHLLGTFDLTGIPPAPRGVPQIEVTFEIDVNGILRVTAEDKGTGNKNKITITNDQNRLTPEEIERMVNDAEKFAEEDKKLKERIDTRNELESYAYSLKNQIGDKEKLGGKLSSEDKETMEKAVEEKIEWLESHQDADIEDFKAKKKELEEIVQPIISKLYGSAGPPPTGEEDTSEKDEL | 3.6.4.10 | null | endoplasmic reticulum unfolded protein response [GO:0030968]; negative regulation of apoptotic process [GO:0043066]; negative regulation of cysteine-type endopeptidase activity involved in apoptotic process [GO:0043154]; negative regulation of IRE1-mediated unfolded protein response [GO:1903895]; negative regulation of protein-containing complex assembly [GO:0031333]; post-translational protein targeting to membrane, translocation [GO:0031204] | cell surface [GO:0009986]; cytosol [GO:0005829]; endoplasmic reticulum chaperone complex [GO:0034663]; endoplasmic reticulum lumen [GO:0005788]; endoplasmic reticulum membrane [GO:0005789]; melanosome [GO:0042470]; mitochondrion [GO:0005739]; nucleus [GO:0005634]; perinuclear region of cytoplasm [GO:0048471] | ATP binding [GO:0005524]; ATP hydrolysis activity [GO:0016887]; ATP-dependent protein folding chaperone [GO:0140662] | PF00012; | 1.20.1270.10;3.30.420.40; | Heat shock protein 70 family | PTM: In unstressed cells, AMPylation at Thr-518 by FICD inactivates the chaperome activity: AMPylated form is locked in a relatively inert state and only weakly stimulated by J domain-containing proteins (PubMed:26673894, PubMed:27918543, PubMed:29064369, PubMed:29198525). In response to endoplasmic reticulum stress, de-AMPylation by the same protein, FICD, restores the chaperone activity (PubMed:27918543). {ECO:0000269|PubMed:26673894, ECO:0000269|PubMed:27918543, ECO:0000269|PubMed:29064369, ECO:0000269|PubMed:29198525}. | SUBCELLULAR LOCATION: Endoplasmic reticulum lumen {ECO:0000250|UniProtKB:P11021}. Melanosome {ECO:0000250|UniProtKB:P11021}. Cytoplasm {ECO:0000250|UniProtKB:P20029}. Cell surface. Note=Identified by mass spectrometry in melanosome fractions from stage I to stage IV (By similarity). Localizes to the cell surface in epithelial cells; high levels of free iron promotes cell surface localization (By similarity). {ECO:0000250|UniProtKB:P11021}. | CATALYTIC ACTIVITY: Reaction=ATP + H2O = ADP + H(+) + phosphate; Xref=Rhea:RHEA:13065, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:456216; EC=3.6.4.10; Evidence={ECO:0000269|PubMed:29198525}; | null | null | null | null | FUNCTION: Endoplasmic reticulum chaperone that plays a key role in protein folding and quality control in the endoplasmic reticulum lumen (By similarity). Involved in the correct folding of proteins and degradation of misfolded proteins via its interaction with DNAJC10/ERdj5, probably to facilitate the release of DNAJC10/ERdj5 from its substrate (By similarity). Acts as a key repressor of the ERN1/IRE1-mediated unfolded protein response (UPR) (PubMed:29198525). In the unstressed endoplasmic reticulum, recruited by DNAJB9/ERdj4 to the luminal region of ERN1/IRE1, leading to disrupt the dimerization of ERN1/IRE1, thereby inactivating ERN1/IRE1 (PubMed:29198525). Accumulation of misfolded protein in the endoplasmic reticulum causes release of HSPA5/BiP from ERN1/IRE1, allowing homodimerization and subsequent activation of ERN1/IRE1 (PubMed:29198525). Plays an auxiliary role in post-translational transport of small presecretory proteins across endoplasmic reticulum (ER). May function as an allosteric modulator for SEC61 channel-forming translocon complex, likely cooperating with SEC62 to enable the productive insertion of these precursors into SEC61 channel. Appears to specifically regulate translocation of precursors having inhibitory residues in their mature region that weaken channel gating. May also play a role in apoptosis and cell proliferation (By similarity). {ECO:0000250|UniProtKB:P11021, ECO:0000250|UniProtKB:P20029, ECO:0000269|PubMed:29198525}. | Cricetulus griseus (Chinese hamster) (Cricetulus barabensis griseus) |
G3J3K0 | FKS1_CORMM | MSGYQGGHHDQYDQGYGQAGHGDGYYQDDQYYDQGHGDHAAQGDHAAQGDHGAQGTQGDGYYDESGYYHADANNPYHQDGGYYDGHDQYQDDYYNNNQGYYDGEYNQGYAQGGRHPSEEESETFSDFTMRSDMARAAEMDYYGRGDEQYNGYGEGGRGYRPPSSQLSYGGNRSSGASTPNYGMEYGNGLASQRSKEPYPAWTSDAQIPLSKEEIEDIFLDLTSKFGFQRDSMRNMYDHLMTLLDSRASRMTPNQALLSLHADYIGGDNANYRKWYFAAHLDLDDAVGFANASTKNRKRKAKKGKKKGGEAGNEAETLQELEGDDSLEAAEYRWKTRMNRMSQYDRVRQIALYLLCWGEANQVRFMPECLCFIFKCADDYLNSPACQALVEPVEEFTFLNNVITPLYQYCRDQGYEILNGVYVRRERDHKHIIGYDDCNQLFWYPEGIERIVLEDKSKLVDLPPAERYLKLKEVNWKKCFFKTYKESRSWFHLLLNFNRIWVIHLTMFWFYTSHNAPSLITYQYEQQKDNQPPASKQFSIVGFGGAIASLIQIFATLAEWVYVPRRWAGAQHLTKRLLFLIVILVLNVAPGVKVFMFHGNKDGKDADQKNKDTPIDKAIGIVHFVIAVFTFLFFSVMPLGGLLGSYLTKKSRRYVASQTFTASYPRLTGNDMAMSFGLWLTVFGAKFGESYVYLTLSFRDPIRYLSIMKIDCLGDAMFGSTAATQQILCKHQPTIVLILMTFTDLIFFFLDTYLFYVILNTVFSIARSFYIGSSIWTPWRNIFSRLPKRIYSKVLATTDMEIKYKPKVLISQVWNAIVISMYREHLLAIDHVQKLLYHQVPSEQEGKRTLRAPTFFVSQEDHSFKTEFFPSHSEAERRISFFAQSLSTPIPEPVPVDNMPTFTVMIPHYSEKILLSLREIIREDEPYSRVTLLEYLKQLHPHEWECFVKDTKILADETAQMNGEPEKSEKDTAKSKIDDLPFYCIGFKSSAPEYTLRTRIWASLRSQTLYRTVSGFMNYSRAIKLLYRVENPEVVQMFGGNSEKLERELERMARRKFKLVVSMQRYSKFKKEEMENAEFLLRAYPDLQIAYLDEEPPLAEGEEPRLYSALIDGHSELMENGMRRPKFRVQLSGNPVLGDGKSDNQNHAIIFYRGEYIQLIDANQDNYLEECLKIRSVLAEFEEMKPDNHSPYTPGVKNDVHTPVAILGAREYIFSENIGILGDVAAGKEQTFGTLFARTMAQVGGKLHYGHPDFLNGIFMTTRGGVSKAQKGLHLNEDIFAGMNALVRGGRIKHCEYYQCGKGRDLGFGSILNFTTKIGTGMGEQWLSREYYYLGTQLPLDRFLSFYYAHAGFHVNNMFIMLSVQSFMLTLMSIGALRHETIRCDYNPQKPITDPLYPTKCSNTDELMGWVYRCIISIFFVFFISFVPLIVQELTERGVWRAALRFIKQFCSLSPFFEVFVCQIYANSVQSDLAFGGARYIGTGRGFATARIPFGVLYSRFAGQSIYFGARLLMMLLFATSTAWQPALTYFWIVLLGLIISPFLYNPHQFAWTDFFIDYRDFLRWLSRGNSRAHASSWIMFCRLSRTRITGYKRKVMGDASAKMSADVPRAAVANIFLTEILTPLLLAATTTVAYLFVNAQTGVTDNDKNSSSSPGFKIGPSGALIRLAVVAFAPIGINAGVLAAMFGMACCMGPVLNMCCKKFGPVLAGIAHGAAAVFMIIFFEVMYVLEGFNFARALAGIIAAMCIQRFIFKLIVSLALTREFKTDQSNIAFWNGKWYSMGWHSVSQPAREFLCKITELSMFSADFILGHWILFMMAPLILIPQIDKIHSMMLFWLLPSRQIRPPIYSMKQSKLRRRRVIRFAILYFVLFIIFLALVVAPGVIGKKFLGDTIFKALDNGNGGPANLHLLQPWGLDNNNTEGKTETGTKAGGADASATDASKLRLF | 2.4.1.34 | null | (1->3)-beta-D-glucan biosynthetic process [GO:0006075]; cell wall organization [GO:0071555]; fungal-type cell wall polysaccharide biosynthetic process [GO:0051278] | 1,3-beta-D-glucan synthase complex [GO:0000148] | 1,3-beta-D-glucan synthase activity [GO:0003843] | PF14288;PF02364; | null | Glycosyltransferase 48 family | null | SUBCELLULAR LOCATION: Membrane {ECO:0000269|PubMed:35816703}; Multi-pass membrane protein {ECO:0000255}. Cell membrane {ECO:0000250|UniProtKB:P38631}; Multi-pass membrane protein {ECO:0000255}. | CATALYTIC ACTIVITY: Reaction=[(1->3)-beta-D-glucosyl](n) + UDP-alpha-D-glucose = [(1->3)-beta-D-glucosyl](n+1) + H(+) + UDP; Xref=Rhea:RHEA:21476, Rhea:RHEA-COMP:11146, Rhea:RHEA-COMP:14303, ChEBI:CHEBI:15378, ChEBI:CHEBI:37671, ChEBI:CHEBI:58223, ChEBI:CHEBI:58885; EC=2.4.1.34; Evidence={ECO:0000269|PubMed:35816703}; | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=84.3 uM for UDP-glucose (at 37 degrees Celsius and pH 7) {ECO:0000269|PubMed:35816703}; Note=kcat is 1.42 min(-1) for UDP-glucose (at 37 degrees Celsius and pH 7). {ECO:0000269|PubMed:35816703}; | null | BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 7. {ECO:0000269|PubMed:35816703}; | BIOPHYSICOCHEMICAL PROPERTIES: Temperature dependence: Optimum temperature is 37 degrees Celsius. {ECO:0000269|PubMed:35816703}; | FUNCTION: Catalytic subunit of the 1,3-beta-glucan synthase (GS) (PubMed:35816703). Synthesizes 1,3-beta-glucan, a major structural component of the fungal cell wall (PubMed:35816703). Involved in cell wall synthesis, maintenance and remodeling (By similarity). {ECO:0000250|UniProtKB:P38631, ECO:0000269|PubMed:35816703}. | Cordyceps militaris (strain CM01) (Caterpillar fungus) |
G3KIM8 | ACRC_ANAPI | MFLLKIKKERMKRMDFSLTREQEMLKKLARQFAEIELEPVAEEIDREHVFPAENFKKMAEIGLTGIGIPKEFGGSGGGTLEKVIAVSEFGKKCMASASILSIHLIAPQAIYKYGTKEQKETYLPRLTKGGELGAFALTEPNAGSDAGAVKTTAILDSQTNEYVLNGTKCFISGGGRAGVLVIFALTEPKKGLKGMSAIIVEKGTPGFSIGKVESKMGIAGSETAELIFEDCRVPAANLLGKEGKGFKIAMEALDGARIGVGAQAIGIAEGAIDLSVKYVHERIQFGKPIANLQGIQWYIADMATKTAAARALVEFAAYLEDAGKPFTKESAMCKLNASENARFVTNLALQIHGGYGYMKDYPLERMYRDAKITEIYEGTSEIHKVVIAREVMKR | 1.3.1.95 | COFACTOR: Name=FAD; Xref=ChEBI:CHEBI:57692; Evidence={ECO:0000269|PubMed:12603323}; | leucine catabolic process [GO:0006552] | cytoplasm [GO:0005737] | acryloyl-CoA reductase (NADH) activity [GO:0043958]; FAD binding [GO:0071949]; isovaleryl-CoA dehydrogenase activity [GO:0008470]; oxidoreductase activity, acting on the CH-CH group of donors, NAD or NADP as acceptor [GO:0016628] | PF00441;PF02770;PF02771; | 1.10.540.10;2.40.110.10;1.20.140.10; | Acyl-CoA dehydrogenase family | null | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:12603323}. | CATALYTIC ACTIVITY: Reaction=NAD(+) + propanoyl-CoA = acryloyl-CoA + H(+) + NADH; Xref=Rhea:RHEA:34471, ChEBI:CHEBI:15378, ChEBI:CHEBI:57367, ChEBI:CHEBI:57392, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945; EC=1.3.1.95; Evidence={ECO:0000269|PubMed:12603323}; | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=2 uM for acryloyl-CoA (with NADH as electron acceptor at pH 7.5 and 25 degrees Celsius) {ECO:0000269|PubMed:12603323}; KM=8 uM for NADH (at pH 7.5 and 25 degrees Celsius) {ECO:0000269|PubMed:12603323}; KM=50 uM for propionyl-CoA (with of ferricenium hexafluorophosphate as electron acceptor at pH 7.5 and 25 degrees Celsius) {ECO:0000269|PubMed:12603323}; KM=100 uM for butyryl-CoA (with of ferricenium hexafluorophosphate as electron acceptor at pH 7.5 and 25 degrees Celsius) {ECO:0000269|PubMed:12603323}; KM=1800 uM for 3-buten-2-one (with NADH as electron acceptor at pH 7.5 and 25 degrees Celsius) {ECO:0000269|PubMed:12603323}; Vmax=0.8 umol/min/mg enzyme with propionyl-CoA as substrate (with ferricenium hexafluorophosphate as electron acceptor at pH 7.5 and 25 degrees Celsius) {ECO:0000269|PubMed:12603323}; Vmax=1.4 umol/min/mg enzyme with butyryl-CoA as substrate (with ferricenium hexafluorophosphate as electron acceptor at pH 7.5 and 25 degrees Celsius) {ECO:0000269|PubMed:12603323}; Vmax=1.4 umol/min/mg enzyme with NADH as substrate (at pH 7.5 and 25 degrees Celsius) {ECO:0000269|PubMed:12603323}; Vmax=1.8 umol/min/mg enzyme with acryloyl-CoA as substrate (with NADH as electron acceptor at pH 7.5 and 25 degrees Celsius) {ECO:0000269|PubMed:12603323}; Vmax=11.6 umol/min/mg enzyme with 3-buten-2-one as substrate (with NADH as electron acceptor at pH 7.5 and 25 degrees Celsius) {ECO:0000269|PubMed:12603323}; Note=kcat is 4.5 sec(-1), 29 sec(-1), 2 sec(-1) and 3.5 sec(-1) for acryloyl-CoA, 3-buten-2-one, propionyl-CoA and butyryl-CoA, respectively (at pH 7.5 and 25 degrees Celsius).; | null | BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is between 6.5 and 7. {ECO:0000269|PubMed:12603323}; | BIOPHYSICOCHEMICAL PROPERTIES: Temperature dependence: In the range between 25 and 55 degrees Celsius, the activity increases with rising temperature. Above 55 degrees Celsius, it decreases and becomes almost zero at 65 degrees Celsius. {ECO:0000269|PubMed:12603323}; | FUNCTION: Probable catalytic subunit of the acryloyl-CoA reductase complex involved in the pathway of L-alanine fermentation. Catalyzes the irreversible NADH-dependent formation of propionyl-CoA from acryloyl-CoA. It can also use 3-buten-2-one as substrate. {ECO:0000269|PubMed:12603323}. | Anaerotignum propionicum (Clostridium propionicum) |
G3LSH3 | NBCL_LOTJA | MSLEDSLRSLSLDYLNLLINGQAFSDVTFSVEGRLVHAHRCILAARSLFFRKFFCGPDPPPPSGNLDSPGGPRVNSPRPGGVIPVNSVGYEVFLLMLQFLYSGQVSIVPQKHEPRPNCGERACWHTHCTSAVDLALDTLAAARYFGVEQLALLTQKQLASMVEKASIEDVMKVLLASRKQDMHQLWTTCSHLVAKSGLPPEVLAKHLPIDIVAKIEELRLKSTLARRSLIPHHHHHHHHHGHHDMGAAADLEDQKIRRMRRALDSSDVELVKLMVMGEGLNLDEALALPYAVENCSREVVKALLELGAADVNYPSGPSGKTPLHIAAEMVSPDMVAVLLDHHADPNVRTVDGVTPLDILRTLTSDFLFKGAVPGLTHIEPNKLRLCLELVQSAALVMSREEGNANANSSNNNNAPCSAATPIYPPMNEDHNSSSSNANLNLDSRLVYLNLGAAQMSGDDDSSHGSHREAMNQAMYHHHHSHDY | null | null | induced systemic resistance, jasmonic acid mediated signaling pathway [GO:0009864]; plant organ development [GO:0099402]; regulation of DNA-templated transcription [GO:0006355] | nucleus [GO:0005634] | transcription cis-regulatory region binding [GO:0000976] | PF12796;PF00651;PF11900; | 1.25.40.20; | Plant 'ANKYRIN-BTB/POZ' family, 'NOOT-BOP-COCH-like' (NBCL) subfamily | null | SUBCELLULAR LOCATION: Nucleus {ECO:0000269|Ref.2}. Cytoplasm {ECO:0000269|Ref.2}. Cell membrane {ECO:0000269|Ref.2}; Peripheral membrane protein {ECO:0000269|Ref.2}; Cytoplasmic side {ECO:0000269|Ref.2}. | null | null | PATHWAY: Protein modification; protein ubiquitination. {ECO:0000250|UniProtKB:O22286}. | null | null | FUNCTION: May act as a substrate-specific adapter of an E3 ubiquitin-protein ligase complex (CUL3-RBX1-BTB) which mediates the ubiquitination and subsequent proteasomal degradation of target proteins (By similarity). Transcriptional co-regulator involved in the promotion of leaf and floral meristem fate and determinacy (PubMed:26390061, Ref.2). Required for the abscission of senescent organs, probably by regulating the cell wall disorganization in abscission zones (AZs, e.g. pulvini at the base of leaves) (PubMed:26390061). Involved in the coordination of the symbiotic nodule developmental program; promotes the formation of root nodules by interacting directly with APP1 to modulate the expression of the nuclear transcription factor Y subunit (NF-YA1), a key nodulin (Ref.2). Necessary for the robust maintenance of nodule identity throughout the nodule developmental program (By similarity). {ECO:0000250|UniProtKB:O22286, ECO:0000250|UniProtKB:Q2HW56, ECO:0000269|PubMed:26390061, ECO:0000269|Ref.2}. | Lotus japonicus (Lotus corniculatus var. japonicus) |
G3MZR2 | FUT7_BOVIN | MQNAGLSPTPSLRALGGLAMAALLSTVWLWWRLGAAPGGAPAPQPTTTILVWHWPFASQPPELPGDTCTRYGVARCRLTVNRSLLAGADAVVFHHRELQTQQARLPLAERPRGQPWVWASMESPSHTRGLGRLRGVFNWVLSYRRDSDIFVPYGRLEPREGPAPPLPAKRGLAAWVVSNFQKRQRRVQLYRQLALHLRVDVFGRAAGQPLCASCLLRAVAGYRFYLSFENSEHRDYITEKFWRNALLAGAVPVVLGPPRAAYEAVAPPDAFVHVDDFGSARELAAFLTSMNESCYRRYFAWRDRFRVRLFSDWRERFCAICARFPQLPRGQVYQDLEGWFQA | 2.4.1.- | null | fucosylation [GO:0036065]; inflammatory response [GO:0006954]; leukocyte migration involved in inflammatory response [GO:0002523]; lymphocyte migration into lymph node [GO:0097022]; positive regulation of cell adhesion [GO:0045785]; positive regulation of cell-cell adhesion [GO:0022409]; positive regulation of leukocyte adhesion to vascular endothelial cell [GO:1904996]; positive regulation of leukocyte tethering or rolling [GO:1903238]; positive regulation of neutrophil migration [GO:1902624]; protein glycosylation [GO:0006486]; regulation of cell-cell adhesion [GO:0022407]; regulation of insulin receptor signaling pathway [GO:0046626]; regulation of type IV hypersensitivity [GO:0001807] | membrane [GO:0016020] | 4-galactosyl-N-acetylglucosaminide 3-alpha-L-fucosyltransferase activity [GO:0017083]; alpha-(1->3)-fucosyltransferase activity [GO:0046920] | PF17039;PF00852; | 3.40.50.11660; | Glycosyltransferase 10 family | PTM: N-glycosylated. {ECO:0000250|UniProtKB:Q11130}. | SUBCELLULAR LOCATION: Membrane {ECO:0000255}; Single-pass membrane protein {ECO:0000255}. | CATALYTIC ACTIVITY: Reaction=an N-acetyl-alpha-neuraminyl-(2->3)-beta-D-galactosyl-(1->4)-N-acetyl-beta-D-glucosaminyl derivative + GDP-beta-L-fucose = an alpha-Neu5Ac-(2->3)-beta-D-Gal-(1->4)-[alpha-L-Fuc-(1->3)]-beta-D-GlcNAc derivative + GDP + H(+); Xref=Rhea:RHEA:56076, ChEBI:CHEBI:15378, ChEBI:CHEBI:57273, ChEBI:CHEBI:58189, ChEBI:CHEBI:136545, ChEBI:CHEBI:139509; Evidence={ECO:0000269|PubMed:22909383}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:56077; Evidence={ECO:0000305|PubMed:22909383}; CATALYTIC ACTIVITY: Reaction=a neolactoside IV(3)-alpha-NeuAc-nLc4Cer + GDP-beta-L-fucose = a neolactoside IV(3)-alpha-NeuNAc,III(3)-alpha-Fuc-nLc4Cer + GDP + H(+); Xref=Rhea:RHEA:48392, ChEBI:CHEBI:15378, ChEBI:CHEBI:57273, ChEBI:CHEBI:58189, ChEBI:CHEBI:90390, ChEBI:CHEBI:90392; Evidence={ECO:0000250|UniProtKB:Q11130}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:48393; Evidence={ECO:0000250|UniProtKB:Q11130}; CATALYTIC ACTIVITY: Reaction=GDP-beta-L-fucose + N-acetyl-alpha-neuraminosyl-(2->3)-beta-D-galactosyl-(1->4)-N-acetyl-beta-D-glucosaminyl-(1->3)-beta-D-galactosyl-(1->4)-N-acetyl-beta-D-glucosaminyl-(1->3)-beta-D-galactosyl-(1->4)-beta-D-glucosyl-(1<->1')-ceramide = GDP + H(+) + N-acetyl-alpha-neuraminosyl-(2->3)-beta-D-galactosyl-(1->4)-[alpha-L-fucosyl-(1->3)]-N-acetyl-beta-D-glucosaminyl-(1->3)-beta-D-galactosyl-(1->4)-N-acetyl-beta-D-glucosaminyl-(1->3)-beta-D-galactosyl-(1->4)-beta-D-glucosyl-(1<->1')-ceramide; Xref=Rhea:RHEA:48356, ChEBI:CHEBI:15378, ChEBI:CHEBI:57273, ChEBI:CHEBI:58189, ChEBI:CHEBI:90336, ChEBI:CHEBI:90339; Evidence={ECO:0000250|UniProtKB:Q11130}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:48357; Evidence={ECO:0000250|UniProtKB:Q11130}; CATALYTIC ACTIVITY: Reaction=an alpha-Neu5Ac-(2->3)-beta-D-Gal-(1->4)-beta-D-GlcNAc-(1->3)-beta-D-Gal-(1->4)-[alpha-L-Fuc-(1->3)]-beta-D-GlcNAc derivative + GDP-beta-L-fucose = an alpha-Neu5Ac-(2->3)-beta-D-Gal-(1->4)-[alpha-L-Fuc-(1->3)]-beta-D-GlcNAc-(1->3)-beta-D-Gal-(1->4)-[alpha-L-Fuc-(1->3)]-beta-D-GlcNAc derivative + GDP + H(+); Xref=Rhea:RHEA:52864, ChEBI:CHEBI:15378, ChEBI:CHEBI:57273, ChEBI:CHEBI:58189, ChEBI:CHEBI:145342, ChEBI:CHEBI:145343; Evidence={ECO:0000250|UniProtKB:Q11130}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:52865; Evidence={ECO:0000250|UniProtKB:Q11130}; CATALYTIC ACTIVITY: Reaction=an alpha-Neu5Ac-(2->3)-beta-D-Gal-(1->4)-beta-D-GlcNAc6S derivative + GDP-beta-L-fucose = an alpha-Neu5Ac-(2->3)-beta-D-Gal-(1->4)-[alpha-L-Fuc-(1->3)]-beta-D-GlcNAc6S derivative + GDP + H(+); Xref=Rhea:RHEA:62004, ChEBI:CHEBI:15378, ChEBI:CHEBI:57273, ChEBI:CHEBI:58189, ChEBI:CHEBI:145344, ChEBI:CHEBI:145345; Evidence={ECO:0000250|UniProtKB:Q11130}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:62005; Evidence={ECO:0000250|UniProtKB:Q11130}; CATALYTIC ACTIVITY: Reaction=alpha-Neu5Ac-(2->3)-beta-D-Gal-(1->4)-beta-D-GlcNAc-(1->3)-beta-D-Gal-(1->4)-D-Glc + GDP-beta-L-fucose = alpha-Neu5Ac-(2->3)-beta-D-Gal-(1->4)-[alpha-L-Fuc-(1->3)]-beta-D-GlcNAc-(1->3)-beta-D-Gal-(1->4)-D-Glc + GDP + H(+); Xref=Rhea:RHEA:62008, ChEBI:CHEBI:15378, ChEBI:CHEBI:57273, ChEBI:CHEBI:58189, ChEBI:CHEBI:145346, ChEBI:CHEBI:145347; Evidence={ECO:0000250|UniProtKB:Q11130}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:62009; Evidence={ECO:0000250|UniProtKB:Q11130}; CATALYTIC ACTIVITY: Reaction=alpha-Neu5Ac-(2->3)-beta-D-Gal-(1->4)-beta-D-GlcNAc-(1->3)-beta-D-Gal-(1->4)-[alpha-L-Fuc-(1->3)]-beta-D-GlcNAc-(1->3)-beta-D-Gal-(1->4)-beta-D-GlcNAc + GDP-beta-L-fucose = alpha-Neu5Ac-(2->3)-beta-D-Gal-(1->4)-[alpha-L-Fuc-(1->3)]-beta-D-GlcNAc-(1->3)-beta-D-Gal-(1->4)-[alpha-L-Fuc-(1->3)]-beta-D-GlcNAc-(1->3)-beta-D-Gal-(1->4)-beta-D-GlcNAc + GDP + H(+); Xref=Rhea:RHEA:62060, ChEBI:CHEBI:15378, ChEBI:CHEBI:57273, ChEBI:CHEBI:58189, ChEBI:CHEBI:145400, ChEBI:CHEBI:145401; Evidence={ECO:0000250|UniProtKB:Q11130}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:62061; Evidence={ECO:0000250|UniProtKB:Q11130}; CATALYTIC ACTIVITY: Reaction=alpha-Neu5Ac-(2->3)-beta-D-Gal-(1->4)-beta-D-GlcNAc-(1->3)-beta-D-Gal-(1->4)-beta-D-GlcNAc-(1->3)-beta-D-Gal-(1->4)-beta-D-GlcNAc + GDP-beta-L-fucose = alpha-Neu5Ac-(2->3)-beta-D-Gal-(1->4)-[alpha-L-Fuc-(1->3)]-beta-D-GlcNAc-(1->3)-beta-D-Gal-(1->4)-beta-D-GlcNAc-(1->3)-beta-D-Gal-(1->4)-beta-D-GlcNAc + GDP + H(+); Xref=Rhea:RHEA:62056, ChEBI:CHEBI:15378, ChEBI:CHEBI:57273, ChEBI:CHEBI:58189, ChEBI:CHEBI:145398, ChEBI:CHEBI:145399; Evidence={ECO:0000250|UniProtKB:Q11130}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:62057; Evidence={ECO:0000250|UniProtKB:Q11130}; | null | PATHWAY: Protein modification; protein glycosylation. {ECO:0000250|UniProtKB:Q11130}. | null | null | FUNCTION: Catalyzes the transfer of L-fucose, from a guanosine diphosphate-beta-L-fucose, to the N-acetyl glucosamine (GlcNAc) of a distal alpha2,3 sialylated lactosamine unit of a glycoprotein or a glycolipid-linked sialopolylactosamines chain through an alpha-1,3 glycosidic linkage and participates in the final fucosylation step in the biosynthesis of the sialyl Lewis X (sLe(x)), a carbohydrate involved in cell and matrix adhesion during leukocyte trafficking and fertilization (PubMed:22909383). In vitro, also synthesizes sialyl-dimeric-Lex structures, from VIM-2 structures and both di-fucosylated and trifucosylated structures from mono-fucosylated precursors. However does not catalyze alpha 1-3 fucosylation when an internal alpha 1-3 fucosylation is present in polylactosamine chain and the fucosylation rate of the internal GlcNAc residues is reduced once fucose has been added to the distal GlcNAc. Also catalyzes the transfer of a fucose from GDP-beta-fucose to the 6-sulfated a(2,3)sialylated substrate to produce 6-sulfo sLex mediating significant L-selectin-dependent cell adhesion. Through sialyl-Lewis(x) biosynthesis, can control SELE- and SELP-mediated cell adhesion with leukocytes and allows leukocytes tethering and rolling along the endothelial tissue thereby enabling the leukocytes to accumulate at a site of inflammation. May enhance embryo implantation through sialyl Lewis X (sLeX)-mediated adhesion of embryo cells to endometrium. May affect insulin signaling by up-regulating the phosphorylation and expression of some signaling molecules involved in the insulin-signaling pathway through SLe(x) which is present on the glycans of the INSRR alpha subunit (By similarity). {ECO:0000250|UniProtKB:Q11130, ECO:0000269|PubMed:22909383}. | Bos taurus (Bovine) |
G3MZY8 | RPB1_BOVIN | MHGGGPPSGDSACPLRTIKRVQFGVLSPDELKRMSVTEGGIKYPETTEGGRPKLGGLMDPRQGVIERTGRCQTCAGNMTECPGHFGHIELAKPVFHVGFLVKTMKVLRCVCFFCSKLLVDSNNPKIKDILAKSKGQPKKRLTHVYDLCKGKNICEGGEEMDNKFGVEQPEGDEDLTKEKGHGGCGRYQPRIRRSGLELYAEWKHVNEDSQEKKILLSPERVHEIFKRISDEECFVLGMEPRYARPEWMIVTVLPVPPLSVRPAVVMQGSARNQDDLTHKLADIVKINNQLRRNEQNGAAAHVIAEDVKLLQFHVATMVDNELPGLPRAMQKSGRPLKSLKQRLKGKEGRVRGNLMGKRVDFSARTVITPDPNLSIDQVGVPRSIAANMTFAEIVTPFNIDRLQELVRRGNSQYPGAKYIIRDNGDRIDLRFHPKPSDLHLQTGYKVERHMCDGDIVIFNRQPTLHKMSMMGHRVRILPWSTFRLNLSVTTPYNADFDGDEMNLHLPQSLETRAEIQELAMVPRMIVTPQSNRPVMGIVQDTLTAVRKFTKRDVFLERGEVMNLLMFLSTWDGKVPQPAILKPRPLWTGKQIFSLIIPGHINCIRTHSTHPDDEDSGPYKHISPGDTKVVVENGELIMGILCKKSLGTSAGSLVHISYLEMGHDITRLFYSNIQTVINNWLLIEGHTIGIGDSIADSKTYQDIQNTIKKAKQDVIEVIEKAHNNELEPTPGNTLRQTFENQVNRILNDARDKTGSSAQKSLSEYNNFKSMVVSGAKGSKINISQVIAVVGQQNVEGKRIPFGFKHRTLPHFIKDDYGPESRGFVENSYLAGLTPTEFFFHAMGGREGLIDTAVKTAETGYIQRRLIKSMESVMVKYDATVRNSINQVVQLRYGEDGLAGESVEFQNLATLKPSNKAFEKKFRFDYTNERALRRTLQEDLVKDVLSNAHIQNELEREFERMREDREVLRVIFPTGDSKVVLPCNLLRMIWNAQKIFHINPRLPSDLHPIKVVEGVKELSKKLVIVNGDDPLSRQAQENATLLFNIHLRSTLCSRRMAEEFRLSGEAFDWLLGEIESKFNQAIAHPGEMVGALAAQSLGEPATQMTLNTFHYAGVSAKNVTLGVPRLKELINISKKPKTPSLTVFLLGQSARDAERAKDILCRLEHTTLRKVTANTAIYYDPNPQSTVVAEDQEWVNVYYEMPDFDVARISPWLLRVELDRKHMTDRKLTMEQIAEKINAGFGDDLNCIFNDDNAEKLVLRIRIMNSDENKMQEEEEVVDKMDDDVFLRCIESNMLTDMTLQGIEQISKVYMHLPQTDNKKKIIITEDGEFKALQEWILETDGVSLMRVLSEKDVDPVRTTSNDIVEIFTVLGIEAVRKALERELYHVISFDGSYVNYRHLALLCDTMTCRGHLMAITRHGVNRQDTGPLMKCSFEETVDVLMEAAAHGESDPMKGVSENIMLGQLAPAGTGCFDLLLDAEKCKYGMEIPTNIPGLGAAGPTGMFFGSAPSPMGGISPAMTPWNQGATPAYGAWSPSVGSGMTPGAAGFSPSAASDASGFSPGYSPAWSPTPGSPGSPGPSSPYIPSPGGAMSPSYSPTSPAYEPRSPGGYTPQSPSYSPTSPSYSPTSPSYSPTSPNYSPTSPSYSPTSPSYSPTSPSYSPTSPSYSPTSPSYSPTSPSYSPTSPSYSPTSPSYSPTSPSYSPTSPSYSPTSPSYSPTSPSYSPTSPSYSPTSPSYSPTSPSYSPTSPNYSPTSPNYTPTSPSYSPTSPSYSPTSPNYTPTSPNYSPTSPSYSPTSPSYSPTSPSYSPSSPRYTPQSPTYTPSSPSYSPSSPSYSPTSPKYTPTSPSYSPSSPEYTPTSPKYSPTSPKYSPTSPKYSPTSPTYSPTTPKYSPTSPTYSPTSPVYTPTSPKYSPTSPTYSPTSPKYSPTSPTYSPTSPKGSTYSPTSPGYSPTSPTYSLTSPAISPDDSDDEN | 2.7.7.48; 2.7.7.6; 3.1.13.- | COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000269|PubMed:26789250, ECO:0000269|PubMed:28892040}; Note=Two Mg(2+) ions are coordinated by both the catalytic residues and the nucleic acid substrate to enhance substrate recognition and catalytic efficiency. {ECO:0000250|UniProtKB:P24928, ECO:0000269|PubMed:26789250, ECO:0000269|PubMed:28892040}; | null | cytoplasm [GO:0005737]; euchromatin [GO:0000791]; RNA polymerase II, core complex [GO:0005665] | core promoter sequence-specific DNA binding [GO:0001046]; DNA-directed 5'-3' RNA polymerase activity [GO:0003899]; DNA/RNA hybrid binding [GO:0071667]; hydrolase activity [GO:0016787]; magnesium ion binding [GO:0000287]; RNA polymerase II activity [GO:0001055]; RNA-dependent RNA polymerase activity [GO:0003968]; zinc ion binding [GO:0008270] | PF04997;PF00623;PF04983;PF05000;PF04998;PF04992;PF04990;PF05001; | 1.10.132.30;1.10.150.390;2.40.40.20;3.30.1360.140;6.10.250.2940;6.20.50.80;3.30.1490.180;4.10.860.120;1.10.274.100; | RNA polymerase beta' chain family | PTM: The tandem heptapeptide repeats in the C-terminal domain (CTD) can be highly phosphorylated. The phosphorylation activates Pol II. Phosphorylation occurs mainly at residues 'Ser-2' and 'Ser-5' of the heptapeptide repeat and is mediated, at least, by CDK7 and CDK9. CDK7 phosphorylation of POLR2A associated with DNA promotes transcription initiation by triggering dissociation from DNA. Phosphorylation also takes place at 'Ser-7' of the heptapeptide repeat, which is required for efficient transcription of snRNA genes and processing of the transcripts. The phosphorylation state is believed to result from the balanced action of site-specific CTD kinases and phosphatases, and a 'CTD code' that specifies the position of Pol II within the transcription cycle has been proposed. Dephosphorylated by the protein phosphatase CTDSP1. Dephosphorylated at 'Ser-2' following UV irradiation. {ECO:0000250|UniProtKB:P24928}.; PTM: Among tandem heptapeptide repeats of the C-terminal domain (CTD) some do not match the Y-S-P-T-S-P-S consensus, the seventh serine residue 'Ser-7' being replaced by a lysine. 'Lys-7' in these non-consensus heptapeptide repeats can be alternatively acetylated, methylated and dimethylated. EP300 is one of the enzyme able to acetylate 'Lys-7'. Acetylation at 'Lys-7' of non-consensus heptapeptide repeats is associated with 'Ser-2' phosphorylation and active transcription. Regulates initiation or early elongation steps of transcription specially for inducible genes. {ECO:0000250|UniProtKB:P24928}.; PTM: Methylated at Arg-1810 prior to transcription initiation when the CTD is hypophosphorylated, phosphorylation at Ser-1805 and Ser-1808 preventing this methylation. Symmetrically or asymmetrically dimethylated at Arg-1810 by PRMT5 and CARM1 respectively. Symmetric or asymmetric dimethylation modulates interactions with CTD-binding proteins like SMN1/SMN2 and TDRD3. SMN1/SMN2 interacts preferentially with the symmetrically dimethylated form while TDRD3 interacts with the asymmetric form. Through the recruitment of SMN1/SMN2, symmetric dimethylation is required for resolving RNA-DNA hybrids created by RNA polymerase II, that form R-loop in transcription terminal regions, an important step in proper transcription termination. CTD dimethylation may also facilitate the expression of select RNAs. Among tandem heptapeptide repeats of the C-terminal domain (CTD) some do not match the Y-S-P-T-S-P-S consensus, the seventh serine residue 'Ser-7' being replaced by a lysine. 'Lys-7' in these non-consensus heptapeptide repeats can be alternatively acetylated, methylated, dimethylated and trimethylated. Methylation occurs in the earliest transcription stages and precedes or is concomitant to 'Ser-5' and 'Ser-7' phosphorylation. Dimethylation and trimehtylation at 'Lys-7' of non-consensus heptapeptide repeats are exclusively associated with phosphorylated CTD. {ECO:0000250|UniProtKB:P24928}.; PTM: Ubiquitinated by WWP2 leading to proteasomal degradation (By similarity). Following transcription stress, the elongating form of RNA polymerase II (RNA pol IIo) is ubiquitinated by NEDD4 on Lys-1268 at DNA damage sites without leading to degradation: ubiquitination promotes RNA pol IIo backtracking to allow access by the transcription-coupled nucleotide excision repair (TC-NER) machinery. At stalled RNA pol II where TC-NER has failed, RBX1-mediated polybiquitination at Lys-1268 may lead to proteasome-mediated degradation in a UBAP2- and UBAP2L-dependent manner; presumably to halt global transcription and enable 'last resort' DNA repair pathways (By similarity). {ECO:0000250|UniProtKB:P08775, ECO:0000250|UniProtKB:P24928}. | SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:P24928}. Cytoplasm {ECO:0000250|UniProtKB:P24928}. Chromosome {ECO:0000250|UniProtKB:P24928}. Note=Hypophosphorylated form is mainly found in the cytoplasm, while the hyperphosphorylated and active form is nuclear. Co-localizes with kinase SRPK2 and helicase DDX23 at chromatin loci where unscheduled R-loops form. {ECO:0000250|UniProtKB:P24928}. | CATALYTIC ACTIVITY: Reaction=a ribonucleoside 5'-triphosphate + RNA(n) = diphosphate + RNA(n+1); Xref=Rhea:RHEA:21248, Rhea:RHEA-COMP:14527, Rhea:RHEA-COMP:17342, ChEBI:CHEBI:33019, ChEBI:CHEBI:61557, ChEBI:CHEBI:140395; EC=2.7.7.6; Evidence={ECO:0000269|PubMed:16769904, ECO:0000269|PubMed:26789250}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:21249; Evidence={ECO:0000269|PubMed:16769904, ECO:0000269|PubMed:26789250}; PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:21250; Evidence={ECO:0000250|UniProtKB:P24928}; CATALYTIC ACTIVITY: Reaction=a ribonucleoside 5'-triphosphate + RNA(n) = diphosphate + RNA(n+1); Xref=Rhea:RHEA:21248, Rhea:RHEA-COMP:14527, Rhea:RHEA-COMP:17342, ChEBI:CHEBI:33019, ChEBI:CHEBI:61557, ChEBI:CHEBI:140395; EC=2.7.7.48; Evidence={ECO:0000250|UniProtKB:P24928}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:21249; Evidence={ECO:0000250|UniProtKB:P24928}; CATALYTIC ACTIVITY: Reaction=a 3'-end ribonucleotidyl-ribonucleotide-RNA + H2O = a 3'-end ribonucleotide-RNA + a ribonucleoside 5'-phosphate + H(+); Xref=Rhea:RHEA:77763, Rhea:RHEA-COMP:17428, Rhea:RHEA-COMP:18982, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:58043, ChEBI:CHEBI:74896, ChEBI:CHEBI:197502; Evidence={ECO:0000250|UniProtKB:P24928, ECO:0000305|PubMed:9604937}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:77764; Evidence={ECO:0000250|UniProtKB:P24928, ECO:0000305|PubMed:9604937}; | null | null | null | null | FUNCTION: Catalytic core component of RNA polymerase II (Pol II), a DNA-dependent RNA polymerase which synthesizes mRNA precursors and many functional non-coding RNAs using the four ribonucleoside triphosphates as substrates (PubMed:16769904, PubMed:26789250). Pol II-mediated transcription cycle proceeds through transcription initiation, transcription elongation and transcription termination stages. During transcription initiation, Pol II pre-initiation complex (PIC) is recruited to DNA promoters, with focused-type promoters containing either the initiator (Inr) element, or the TATA-box found in cell-type specific genes and dispersed-type promoters that often contain hypomethylated CpG islands usually found in housekeeping genes. Once the polymerase has escaped from the promoter it enters the elongation phase during which RNA is actively polymerized, based on complementarity with the template DNA strand. Transcription termination involves the release of the RNA transcript and polymerase from the DNA (By similarity) (PubMed:16769904, PubMed:26789250). Forms Pol II active center together with the second largest subunit POLR2B/RPB2. Appends one nucleotide at a time to the 3' end of the nascent RNA, with POLR2A/RPB1 most likely contributing a Mg(2+)-coordinating DxDGD motif, and POLR2B/RPB2 participating in the coordination of a second Mg(2+) ion and providing lysine residues believed to facilitate Watson-Crick base pairing between the incoming nucleotide and template base. Typically, Mg(2+) ions direct a 5' nucleoside triphosphate to form a phosphodiester bond with the 3' hydroxyl of the preceding nucleotide of the nascent RNA, with the elimination of pyrophosphate. The reversible pyrophosphorolysis can occur at high pyrophosphate concentrations (PubMed:16769904, PubMed:26789250). Can proofread the nascent RNA transcript by means of a 3' -> 5' exonuclease activity. If a ribonucleotide is mis-incorporated, backtracks along the template DNA and cleaves the phosphodiester bond releasing the mis-incorporated 5'-ribonucleotide (By similarity) (PubMed:9604937). Through its unique C-terminal domain (CTD, 52 heptapeptide tandem repeats) serves as a platform for assembly of factors that regulate transcription initiation, elongation and termination. CTD phosphorylation on Ser-5 mediates Pol II promoter escape, whereas phosphorylation on Ser-2 is required for Pol II pause release during transcription elongation and further pre-mRNA processing. Additionally, the regulation of gene expression levels depends on the balance between methylation and acetylation levels of the CTD-lysines. Initiation or early elongation steps of transcription of growth-factor-induced immediate early genes are regulated by the acetylation status of the CTD. Methylation and dimethylation have a repressive effect on target genes expression. Cooperates with mRNA splicing machinery in co-transcriptional 5'-end capping and co-transcriptional splicing of pre-mRNA (By similarity). {ECO:0000250|UniProtKB:P24928, ECO:0000269|PubMed:16769904, ECO:0000269|PubMed:26789250, ECO:0000269|PubMed:9604937}.; FUNCTION: RNA-dependent RNA polymerase that catalyzes the extension of a non-coding RNA (ncRNA) at the 3'-end using the four ribonucleoside triphosphates as substrates. An internal ncRNA sequence near the 3'-end serves as a template in a single-round Pol II-mediated RNA polymerization reaction. May decrease the stability of ncRNAs that repress Pol II-mediated gene transcription. {ECO:0000250|UniProtKB:P24928}. | Bos taurus (Bovine) |
G3QY98 | APOA1_GORGO | MKAAVLTLAVLFLTGSQARHFWQQDEPPQSPWDRVKDLATVYVDVLKDSGRDYVSQFEGSALGKQLNLKLLDNWDSVTSTFSKLREQLGPVTQEFWDNLEKETEGLRQEMSKDLEEVKAKVQPYLDDFQKKWQEEMELYRQKVEPLRAELQEGARQKLHELQEKLSPLGEEMRDRARAHVDALRTHLAPYSDELRQRLAARLEALKENGGARLAEYHAKATEHLSTLSEKAKPALEDLRQGLLPVLESFKVSFLSALEEYTKKLNTQ | null | null | acylglycerol homeostasis [GO:0055090]; adrenal gland development [GO:0030325]; blood vessel endothelial cell migration [GO:0043534]; cholesterol biosynthetic process [GO:0006695]; cholesterol efflux [GO:0033344]; cholesterol homeostasis [GO:0042632]; cholesterol import [GO:0070508]; cholesterol metabolic process [GO:0008203]; endothelial cell proliferation [GO:0001935]; G protein-coupled receptor signaling pathway [GO:0007186]; glucocorticoid metabolic process [GO:0008211]; high-density lipoprotein particle assembly [GO:0034380]; high-density lipoprotein particle remodeling [GO:0034375]; integrin-mediated signaling pathway [GO:0007229]; lipid storage [GO:0019915]; lipoprotein biosynthetic process [GO:0042158]; negative regulation of cell adhesion molecule production [GO:0060354]; negative regulation of cytokine production involved in immune response [GO:0002719]; negative regulation of heterotypic cell-cell adhesion [GO:0034115]; negative regulation of inflammatory response [GO:0050728]; negative regulation of interleukin-1 beta production [GO:0032691]; negative regulation of tumor necrosis factor-mediated signaling pathway [GO:0010804]; negative regulation of very-low-density lipoprotein particle remodeling [GO:0010903]; peptidyl-methionine modification [GO:0018206]; phosphatidylcholine biosynthetic process [GO:0006656]; phospholipid efflux [GO:0033700]; phospholipid homeostasis [GO:0055091]; positive regulation of cholesterol efflux [GO:0010875]; positive regulation of cholesterol metabolic process [GO:0090205]; positive regulation of phagocytosis [GO:0050766]; positive regulation of phospholipid efflux [GO:1902995]; positive regulation of Rho protein signal transduction [GO:0035025]; positive regulation of stress fiber assembly [GO:0051496]; positive regulation of substrate adhesion-dependent cell spreading [GO:1900026]; protein oxidation [GO:0018158]; protein stabilization [GO:0050821]; regulation of Cdc42 protein signal transduction [GO:0032489]; regulation of intestinal cholesterol absorption [GO:0030300]; regulation of protein phosphorylation [GO:0001932]; reverse cholesterol transport [GO:0043691]; triglyceride homeostasis [GO:0070328]; vitamin transport [GO:0051180] | chylomicron [GO:0042627]; endocytic vesicle [GO:0030139]; extracellular vesicle [GO:1903561]; high-density lipoprotein particle [GO:0034364]; low-density lipoprotein particle [GO:0034362]; spherical high-density lipoprotein particle [GO:0034366]; very-low-density lipoprotein particle [GO:0034361] | amyloid-beta binding [GO:0001540]; apolipoprotein A-I receptor binding [GO:0034191]; chemorepellent activity [GO:0045499]; cholesterol binding [GO:0015485]; cholesterol transfer activity [GO:0120020]; enzyme binding [GO:0019899]; heat shock protein binding [GO:0031072]; high-density lipoprotein particle binding [GO:0008035]; high-density lipoprotein particle receptor binding [GO:0070653]; phosphatidylcholine-sterol O-acyltransferase activator activity [GO:0060228]; phospholipid binding [GO:0005543]; protein homodimerization activity [GO:0042803] | PF01442; | 1.20.5.20;6.10.140.380;1.20.120.20; | Apolipoprotein A1/A4/E family | PTM: Glycosylated. {ECO:0000250}.; PTM: Palmitoylated. {ECO:0000250}.; PTM: Phosphorylation sites are present in the extracellular medium. {ECO:0000250}. | SUBCELLULAR LOCATION: Secreted. | null | null | null | null | null | FUNCTION: Participates in the reverse transport of cholesterol from tissues to the liver for excretion by promoting cholesterol efflux from tissues and by acting as a cofactor for the lecithin cholesterol acyltransferase (LCAT). As part of the SPAP complex, activates spermatozoa motility (By similarity). {ECO:0000250}. | Gorilla gorilla gorilla (Western lowland gorilla) |
G3UXB3 | NKX11_MOUSE | MSTSGPAAPGDVPALPPPPPGPGSGPAPPAPAATARDTMDGRAELPIFPRAGVPPLAASDTVPAVPEGAGAARPAAPPRPTSFSVLDILDPNKFNSRRRRCVLLGPVVPATCAPCAPAACVAVPAASGRSPRAELERRALSAATGVAAAAGAEPTSAGDSYRADEAEANGYSSGSGRSPTADSEDEAPEDEDEEEAPEVQDAQGTEEPRGGSGGLGARGSGCPGAAEVEASPVDDTAAPGPRGNSPGAPGPPATATGAGSAGSTPQGAAVTTKPKRKRTGSDSKSGKPRRARTAFTYEQLVALENKFKATRYLSVCERLNLALSLSLTETQVKIWFQNRRTKWKKQNPGADTSAPTGGGGGPGPGAGPGAGLPGGLSPLSPSPPMGAPLALHGPAGYPAHSPGGLVCAAQLPFLSSPAVLSPFVLGSQTYGAPAFYAPHL | null | null | cell differentiation [GO:0030154]; lipid metabolic process [GO:0006629]; nervous system process [GO:0050877]; regulation of generation of precursor metabolites and energy [GO:0043467]; regulation of glucose metabolic process [GO:0010906]; regulation of transcription by RNA polymerase II [GO:0006357] | nucleus [GO:0005634] | DNA-binding transcription factor activity, RNA polymerase II-specific [GO:0000981]; RNA polymerase II cis-regulatory region sequence-specific DNA binding [GO:0000978] | PF00046; | 1.10.10.60; | NK-1 homeobox family | null | SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00108}. | null | null | null | null | null | FUNCTION: May be required for the coordinated crosstalk of factors involved in the maintenance of energy homeostasis, possibly by regulating the transcription of specific factors involved in energy balance. {ECO:0000269|PubMed:17879320, ECO:0000269|PubMed:21126319}. | Mus musculus (Mouse) |
G3UZ78 | ADGB_MOUSE | MASKQAKRKEVHRINSAHGSDKSKDLYHFGSNVPPGSFEQKKGKFPIWPEWSEADINAEKWDAGKGGKEKDKTAKSPIFHFFEDPEGKIELPQSLKVFSWKRPQDFIFSRTPVVVKNEITFDLFSPNEHLLCSELMRWIISEIYAVWKIFNGGILSNYHKGNLGELPILPWKPWEHIYSLCKAVKGHVPLFNSYGKYVVKLYWMGCWRKITVDDFLPFDEENNLLLPATSYEFELWPMLLSKAIIKLANVDVHVAHRRELGELTVIHALTGWLPEVIPLHPAYVDRVWELLKEILPEFKLTEEPSSESKITTIDNKLKEATKENKDGKDGKNGKDLKDGKDMKDGKDGKDGKDGKDGKDGKDEKADARDLGKKNKKDGEKEKEKFKFSLHGSRPSSDVQYSMQSLSECSSAIQLPHMVVYATFTPLYLFENKIFSLEKMANSAEKLREYGLSHICSHPVLVTRSRSCPLVSPPKPPPLPAWKLIRHKKETVITDEAQDAVPKKPEQFLEISSPFLNYRMTPFTIPTETHFVQSVIKKGTPLGSSLPPLVENDLVASTSQGEMSIVNGNQSQGNIALQITLGKDEPSEPALADFHQLEATSLDRDLISLTTATLDKSQEELAINEGVAKEIWLDFEDFCVCFHHIYIFHKPHSYCLNFQKSEFKFVEERVPYYLFVDSLKPIELLVCFSALVRWGESGALTKDSPPVEPGLLTAEAITWKSLKPLSVVLRIHTYATKASVVRLPAGRHMLLFNAYSPVGHAIHVCSMTTFVIGDEDIVLPNFEPESYRFTEQSIIIMKAIGNVIANFKDKGKLPAALRDLQAAHYPIPLNNKELTAQHFRVFHISLWRLMKKSQVAKPPSNFKFAFRAMVFDTDLLDSFSEDVSLAEWVDLKYSTPINEKEYTSEEIAAAVKIQSMWKGCYVRLLMKARKPETKENVTVADTLQKIWAVLEMNLEQYALSLLRLMFKSKCKSMESYPCYQDEETKLAFADHTVNYADQPPNSWFIVFREIFLVPQDMIILPKVYTTLPICILHVINNDTLEQVPKVFQKVVPFLYTKNKKGYTFVAEAYTGDTFVSGARWKLRLIGSYNPLPFLARDSPCNTFSIKEIRDYYIPNDRKILFRYSIKVTVAQSITIQVRTSKPDTFIKLQVLESEEVITSTVGKGQAVIPAFYFLGNEKALSSQSSKQVLLSHPSPKKDPEVLTKKKSGQPGQKSFKGRSGGGLTDTGMPLLEEEILNIPTLEENSSTPQQCYKYIIQCLVLFNSWPLNETQLTFVQALKDMEKMDIKEKHEEPAPMGSPDSHAVSEGQKSVGVPKTTRKGKEKSAEKEKLAKEKQAPRFEPQQVQMPTAVHSQQEDPNKPYWILRLVSEHTDSDYVDVKKDTERADEIRAMKQAWETTEPGRAIKAAQARLKYLTQFIKKPVTTDTTTSAPSPETLSVSQSQTKSSEEGELDTGKYADIKELPPNAAGSVLWKKWQMTKTITSLTKFTSSESVPKEEPPQKEIPVVRQRSPTILETSPQQIRKALEFLDFSHYVRKTAAEAVLQTEELNKQQAMQKAEEIHQFRQHRSRILSIRDIDQEERFKQKDEVLEMYGEMRDSVDEARQKILDIREVYRNKLLEAERLRMEALAAQEAAVKIEIEKKSPASDSQKKKKVGKKK | null | null | proteolysis [GO:0006508]; spermatid development [GO:0007286]; spermatogenesis [GO:0007283] | sperm annulus [GO:0097227]; sperm flagellum [GO:0036126]; sperm midpiece [GO:0097225] | calcium-dependent cysteine-type endopeptidase activity [GO:0004198]; heme binding [GO:0020037]; metal ion binding [GO:0046872]; oxygen binding [GO:0019825] | PF00648; | 1.10.490.10; | Globin family; Peptidase C2 family | null | SUBCELLULAR LOCATION: Cell projection, cilium, flagellum {ECO:0000269|PubMed:35700329}. Note=Expressed within the midpiece and along the whole sperm flagellum (PubMed:35700329). Detected in the annulus of the sperm flagellum in S12 and S15 spermatids and mature sperm (PubMed:35700329). {ECO:0000269|PubMed:35700329}. | null | null | null | null | null | FUNCTION: Probable chimeric globin with a bis-histidyl six-coordinate heme-iron atom through which it could bind dioxygen, carbon monoxide and nitric oxide (By similarity). Required for sperm flagellum formation and maturation of elongating spermatids, thus playing an essential role in male fertility (PubMed:35700329, PubMed:36995441). {ECO:0000250|UniProtKB:Q8N7X0, ECO:0000269|PubMed:35700329, ECO:0000269|PubMed:36995441}. | Mus musculus (Mouse) |
G3V6S8 | SRSF6_RAT | MPRVYIGRLSYNVREKDIQRFFSGYGRLLEIDLKNGYGFVEFEDSRDADDAVYELNSKELCGERVIVEHARGPRRDRDGYSYGSRSGGGGYSSRRTSGRDKYGPPVRTEYRLIVENLSSRCSWQDLKDFMRQAGEVTYADAHKERTNEGVIEFRSYSDMKRALDKLDGTEINGRNIRLIEDKPRTSHRRSYSGSRSRSRSRRRSRSRSRRSSRSRSRSISKSRSRSRSRSKGRSRSRSKGRKSRSKSKSKPKSDRGSHSHSRSRSKDKYGKSRSRSRSRSPKENGKGDIKSKSRSRSQSRSHSPLPAPPSKARSMSPPPKRASRSRSRSRSRSRSSSRD | null | null | alternative mRNA splicing, via spliceosome [GO:0000380]; mRNA splice site recognition [GO:0006376]; negative regulation of gene expression [GO:0010629]; negative regulation of keratinocyte differentiation [GO:0045617]; negative regulation of mRNA splicing, via spliceosome [GO:0048025]; negative regulation of type B pancreatic cell apoptotic process [GO:2000675]; positive regulation of epithelial cell proliferation involved in lung morphogenesis [GO:0060501]; regulation of alternative mRNA splicing, via spliceosome [GO:0000381]; regulation of keratinocyte proliferation [GO:0010837]; regulation of wound healing [GO:0061041]; response to insulin [GO:0032868] | cytoplasm [GO:0005737]; nuclear speck [GO:0016607]; nucleus [GO:0005634]; ribonucleoprotein complex [GO:1990904] | mRNA binding [GO:0003729]; pre-mRNA binding [GO:0036002]; RNA binding [GO:0003723] | PF00076; | 3.30.70.330; | Splicing factor SR family | PTM: Extensively phosphorylated on serine residues in the RS domain. Phosphorylated by DYRK1A, probably in the RS domain. Phosphorylation by DYRK1A modulates alternative splice site selection and inhibits the expression of MAPT/Tau exon 10 (By similarity). {ECO:0000250}. | SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:12549914}. Nucleus speckle {ECO:0000250|UniProtKB:Q13247}. | null | null | null | null | null | FUNCTION: Plays a role in constitutive splicing and modulates the selection of alternative splice sites. Plays a role in the alternative splicing of MAPT/Tau exon 10. Binds to alternative exons of TNC pre-mRNA and promotes the expression of alternatively spliced TNC. Plays a role in wound healing and in the regulation of keratinocyte differentiation and proliferation via its role in alternative splicing (By similarity). {ECO:0000250}. | Rattus norvegicus (Rat) |
G3V6U9 | SETD3_RAT | MGKKSRVKTQKSGTGATATVSPKEILNLTSELLQKCSSPAPGPGKEWEEYTQIRALVEKIRKKQKGLSVTFDGKREDYFPDLMKWASENGASVEGFEMVNFKEEGFGLRATRDIKAEELFLWVPRKLLMTVESAKNSILGPLYSQDRILQAMGNIALAFHLLCERASPNSFWQPYIQTLPSEYDTPLYFEEEEVRCLQSTQAIHDVFSQYKNTARQYAYFYKVIQTHPHANKLPLKDSFTYEDYRWAVSSVMTRQNQIPTEDGSRVTLALIPLWDMCNHTNGLITTGYNLEDDRCECVALQDFQAGDQIYIFYGTRSNAEFVIHSGFFFDNNSHDRVKIKLGVSKSDRLYAMKAEVLARAGIPTSSVFALHFTEPPISAQLLAFLRVFCMTEEELKEHLLGDSAIDRIFTLGNSEFPVSWDNEVKLWTFLEDRASLLLKTYKTTIEEDKTVLKNPDLSVRATMAIKLRLGEKEILEKAVKSAAMNREYYRKHMEERAPLPRYEESDLGLLEGGVGDSRLPLVLRKLEEEAGVQESLSLTETVSKVKAAENGLVNGESLIPNGTRSENESLSPEESENTTGDTEESSGSMDAVKERL | 2.1.1.85 | null | actin modification [GO:0030047]; bioluminescence [GO:0008218]; peptidyl-histidine methylation [GO:0018021]; positive regulation of muscle cell differentiation [GO:0051149]; positive regulation of transcription by RNA polymerase II [GO:0045944]; regulation of uterine smooth muscle contraction [GO:0070472] | chromatin [GO:0000785]; cytoplasm [GO:0005737]; nucleus [GO:0005634] | actin binding [GO:0003779]; histone H3K36 methyltransferase activity [GO:0046975]; histone H3K4 methyltransferase activity [GO:0042800]; protein-L-histidine N-tele-methyltransferase activity [GO:0018064]; RNA polymerase II-specific DNA-binding transcription factor binding [GO:0061629]; transcription coactivator activity [GO:0003713] | PF09273;PF00856; | 3.90.1420.10;3.90.1410.10; | Class V-like SAM-binding methyltransferase superfamily, SETD3 actin-histidine methyltransferase family | PTM: Phosphorylated by GSK3B, which is required for recognition by the SCF(FBXW7) complex and subsequent degradation. {ECO:0000250|UniProtKB:Q86TU7}.; PTM: Ubiquitinated by the SCF(FBXW7) complex following phosphorylation by GSK3B, leading to its degradation by the proteasome. {ECO:0000250|UniProtKB:Q86TU7}. | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q86TU7}. Nucleus {ECO:0000250|UniProtKB:Q91WC0}. Note=Localizes mainly in the cytoplasm. {ECO:0000250|UniProtKB:Q86TU7}. | CATALYTIC ACTIVITY: Reaction=L-histidyl-[protein] + S-adenosyl-L-methionine = H(+) + N(tele)-methyl-L-histidyl-[protein] + S-adenosyl-L-homocysteine; Xref=Rhea:RHEA:19369, Rhea:RHEA-COMP:9745, Rhea:RHEA-COMP:11600, ChEBI:CHEBI:15378, ChEBI:CHEBI:16367, ChEBI:CHEBI:29979, ChEBI:CHEBI:57856, ChEBI:CHEBI:59789; EC=2.1.1.85; Evidence={ECO:0000269|PubMed:30526847}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:19370; Evidence={ECO:0000269|PubMed:30526847}; | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=2.996 uM for beta-actin {ECO:0000269|PubMed:30526847}; KM=0.109 uM for S-adenosyl-L-methionine {ECO:0000269|PubMed:30526847}; Vmax=11.28 nmol/min/mg enzyme with beta-actin as substrate {ECO:0000269|PubMed:30526847}; Vmax=8.053 nmol/min/mg enzyme with S-adenosyl-L-methionine as substrate {ECO:0000269|PubMed:30526847}; Note=kcat is 0.8 min(-1) with beta-actin as substrate (PubMed:30526847). kcat is 0.57 min(-1) with S-adenosyl-L-methionine as substrate (PubMed:30526847). {ECO:0000269|PubMed:30526847}; | null | null | null | FUNCTION: Protein-histidine N-methyltransferase that specifically mediates 3-methylhistidine (tele-methylhistidine) methylation of actin at 'His-73' (PubMed:30526847). Histidine methylation of actin is required for smooth muscle contraction of the laboring uterus during delivery (By similarity). Does not have protein-lysine N-methyltransferase activity and probably only catalyzes histidine methylation of actin (By similarity). {ECO:0000250|UniProtKB:Q86TU7, ECO:0000269|PubMed:30526847}. | Rattus norvegicus (Rat) |
G3V7L1 | UTRN_RAT | MAKYGHLEASPDDGQNQFSDIIKSRSDEHNDVQKKTFTKWINARFSKSGKPPINDMFSDLKDGRKLLDLLEGLTGTSLPKERGSTRVHALNNVNRVLQVLHQNNVELVNIGGTDIVDGNPKLTLGLLWSIILHWQVKDVMKDIMSDLQQTNSEKILLSWVRQTTRPYSQVNVLNFTTSWTDGLAFNAVLHRHKPDLFSWDRVVKMSPTERLEHAFSKAHTYLGIEKLLDPEDVAVQLPDKKSIIMYLTSLFEVLPQQVTIDAIREVETLPRKYKKECEGEEINIQSAVLTEEGQSPRAETPSTVTEVDMDLDSYQIALEEVLTWLLSAEDTFQEQDDISDDVEDVKEQFATHETFMMELTAHQSSVGSVLQAGNQLMTQGTLSDEEEFEIQEQMTLLNARWEALRVESMERQSRLHDALMELQKKQLQQLSGWLTLTEERIQKMESLPVGDDLPSLQNLLEEHKSLQSDLEAEQVKVNSLTHMVVIVDENSGESATAVLEDQLQKLGERWTAVCRWTEERWNRLQEINILWQELLEEQCLLEAWLTEKEEALNKVQTGNFKDQKELGVSVRRLAILKEDMEMKRQTLDQLSEIGQDVGQLLSNPKASEKMNSDSEELTQRWDSLVQRLEDSSNQVTQAVAKLGMSQIPQKDLLETVHVREQGMIKKPKQELPPPPPPKKRQIHVDVEAKKKFDATSAELQSWILRSKAALQNTEMNEYKKSQETSGVRKKWKGLEKEQKEKIPQLDELNQTGQILQEQMGKEGLLAEEINDVLERVLLEWKMISQQLEDLGRKIQLQEDINAYFRQLDALEKTIRAKEEWLRDASFSESPQRSLPSLKDSCQRELTDLLGLHPRIEILCASCSALRSQPSVPGFVQQGFDDLRRHYQAVQKALEEYQQQLENELKSQPEPAYLDTLNTLKKMLSESEKAAQASLSALNDPSAVEQALQEKKALDETLENQKPTLHKLSEETKALEKNMLPDVGKTYRQEFDDAQGKWNKVKTKVSRDLRSLEEIIPRLRDFKADSEVIEKWTNGVKDFLMKEQAAQGDTTALQRQLDQCTTFANEIETIESSLKNLRDIETSLQRCPVTGVKTWVQTRLADYQSQLEKFSQEIDIQKSRLSDSQEKAMNLKKDLAEMQEWMAQAEEDYLERDFEYKSPEELESAVEEMKRAKEDVLQKEVRVKILKDSIKLVAARVPSGGQELTSEFNEVLESYQLLCNRIRGKCHTLEEVWSCWVELLHYLDLETSWLNTLEERMQSTEALPERAEAVHDALESLESVLRHPADNRTQIRELGQTLIDGGILDDIISEKLEAFNSRYEELSHLAESKQISLEKQLQVLRETDHMLQVLKESLGELDKQLTTYLTDRIDAFQLPQEAQKIQAEISAHELTLEELKKNVRPQPPTSPEGRTTRGGSQMDLLQRKLREVSTKFQLFQKPANFEQRMLDCKRVLDGVKAELHVLSVKDVDPDVIQTHLDKCMKLYKTLSEVKLEVETVIKTGRHIVQKQQTDNPKGMDEQLTSLKVLYNDLGAQVTEGKQDLERASQLSRKLKKEAAILSEWLSTTEAELVQKSTSEGVIGDLDTEISWAKNILKDLERRKVDLNAITESSAALQHLVVGSESVLEDTLCVLNAGWSRVRTWTEDWRNTLLNHQNQLEVFDGHVAHISTWLYQAEALLDEIEKKPASKQEEIVKRLLSELSDASIQVENVREQAIVLVNARGSSSRELVEPKLAELSKNFEKVSQHINSAQMLIGQDPAGTVEAVGPFSDLESLESDIENMLKVVEKHLDPSNDEKMDEERAQIEEVLQRGEHLLHEPMEDSKKEKIRLQLLLLHTRYNKIKAIPQRKTIPLSSGIMSSALPADYLVEINKILLTLDDIELSLNIPELNTTVYEDFSFQEDSLKRIKDQLDRLGEQLAAVHEKQPDVILEASGPEAIQIRDMLSQLNAKWDRVNRLYSDRRGSFARAVEEWKQFHCDLDDLTQWLSEAEDLLVGTCAPDGSLDLEKARTHQLELEDGLSSHQPCLIDVNQKGEDIVQRLRPSDASFLKDKLASLNQRWSALVAEVKDLQPRLKGESKQVSGYRKRLDEVVCWLTKVENAVQKRSTPDPEENPWELTDLAQEMDAQAENIKWLNRAELEMLSDKNLSLCERDNLSESLRNVNTMWTKICREVPSLLKTRTQDPCSAPQTRIAAHPNVQKVALVSSASDAPLRGPEISVPADLDKTITELADWLVLIDQMLKSNIVTVGDVKEINKTVSRMKITKADLEQRHPQLDFVFTLAQNLKNKASSSDLRTAITEKLEKLKTQWESTQHGVELRRQQLEDMVVDSLQWDDHREETEELMRKHEARFYMLQQARRDPLSKQVSDNQLLLQELGSGDGVIMAFDNVLQKLLEEYSSDDTRNVEETTEYLKTSWINLKQSIADRQSALEAELRTVQTSRRDLENFVKWLQEAETTANVLADASQRENALQDSVLARQLRQQMLDIQAEIDAHNDIFKSIDGNRQKMVKALGNSEEATMLQHRLDDMNQRWNDLKAKSASIRAHLEASAEKWNRLLASLEELIKWLNMKDEELKKQMPIGGDVPALQLQYDHCKVLRRELKEKEYSVLNAVDQARVFLADQPIEAPEEPRRNPQSKTELTPEERAQKIAKAMRKQSSEVREKWESLNAVTSTWQKQVGKALEKLRDLQGAVDDLDADMKEVEAVRNGWKPVGDLLIDSLQDHIEKTLAFREEIAPINLKVKTMNDLSSQLSPLDLHPSPKMSRQLDDLNMRWKLLQVSVEDRLKQLQEAHRDFGPSSQHFLSTSVQLPWQRSISHNKVPYYINHQTQTTCWDHPKMTELFQSLGDLNNVRFSAYRTAIKIRRLQKALCLDLLELNTTNEVFKQHKLNQNDQLLSVPDVINCLTTTYDGLEQLHKDLVNVPLCVDMCLNWLLNVYDTGRTGKIRVQSLKIGLMSLSKGLLEEKYRCLFKEVAGPTEMCDQRQLGLLLHDAIQIPRQLGEVAAFGGSNIEPSVRSCFQQNNNKPEISVKEFIDWMRLEPQSMVWLPVLHRVAAAETAKHQAKCNICKECPIVGFRYRSLKHFNYDVCQSCFFSGRTAKGHKLHYPMVEYCIPTTSGEDVRDFTKVLKNKFRSKKYFAKHPRLGYLPVQTVLEGDNLETPITLISMWPEHYDPSQSPQLFHDDTHSRIEQYATRLAQMERTNGSFLTDSSSTTGSVEDEHALIQQYCQTLGGESPVSQPQSPAQILKSVEKEERGELERIIADLEEEQRNLQVEYEQLKEQHLRRGLPLGSPPDSIVSPYHTSEDSELIAEAKLLRQHKGRLEARMQILEDHNKQLESQLHRLRQLLEQPDSDSRINGVSPWASPQHPSLSYSLDPDPGPQSHQAASEDLLAPPHDTSTDLTDVMEQLNSTFPSCSPNVPSRPQAI | null | null | neuromuscular junction development [GO:0007528]; positive regulation of cell-matrix adhesion [GO:0001954]; response to denervation involved in regulation of muscle adaptation [GO:0014894]; synaptic signaling [GO:0099536] | cortical actin cytoskeleton [GO:0030864]; cytoplasm [GO:0005737]; dystrophin-associated glycoprotein complex [GO:0016010]; filopodium [GO:0030175]; filopodium membrane [GO:0031527]; growth cone [GO:0030426]; neuromuscular junction [GO:0031594]; plasma membrane [GO:0005886]; postsynaptic membrane [GO:0045211]; protein-containing complex [GO:0032991]; sarcolemma [GO:0042383]; synapse [GO:0045202] | actin binding [GO:0003779]; actin filament binding [GO:0051015]; integrin binding [GO:0005178]; protein kinase binding [GO:0019901]; vinculin binding [GO:0017166]; zinc ion binding [GO:0008270] | PF00307;PF09068;PF09069;PF00435;PF00569; | 1.20.58.60;2.20.70.10;3.30.60.90;1.10.418.10;1.10.238.10; | null | null | SUBCELLULAR LOCATION: Postsynaptic cell membrane {ECO:0000250|UniProtKB:P46939}; Peripheral membrane protein {ECO:0000250|UniProtKB:P46939}; Cytoplasmic side {ECO:0000250|UniProtKB:P46939}. Cytoplasm, cytoskeleton {ECO:0000250|UniProtKB:P46939}. Note=Neuromuscular junction. {ECO:0000250|UniProtKB:P46939}. | null | null | null | null | null | FUNCTION: May play a role in anchoring the cytoskeleton to the plasma membrane. {ECO:0000250}. | Rattus norvegicus (Rat) |
G3V7L5 | PO4F2_RAT | MMMMSLNSKQAFSMPHAGSLHVEPKYSALHSASPGSSAPAAPSASSPSSSSNAGSGGGGGGGGGGGGGGRSSSSSSSGSGGGGGGGSEAMRRACLPTPPSNIFGGLDESLLARAEALAAVDIVSQSKSHHHHPPHHSPFKPDATYHTMNTIPCTSAASSSSVPISHPSALAGTHHHHHHHHHHHHQPHQALEGELLEHLSPGLALGAMAGPDGTVVSTPAHAPHMATMNPMHQAALSMAHAHGLPSHMGCMSDVDADPRDLEAFAERFKQRRIKLGVTQADVGSALANLKIPGVGSLSQSTICRFESLTLSHNNMIALKPILQAWLEEAEKSHREKLTKPELFNGAEKKRKRTSIAAPEKRSLEAYFAIQPRPSSEKIAAIAEKLDLKKNVVRVWFCNQRQKQKRMKYSAGI | null | null | axon extension [GO:0048675]; axon guidance [GO:0007411]; axonogenesis [GO:0007409]; cellular response to cytokine stimulus [GO:0071345]; cellular response to estradiol stimulus [GO:0071392]; cellular response to insulin stimulus [GO:0032869]; cellular response to oxygen levels [GO:0071453]; dorsal root ganglion development [GO:1990791]; heart development [GO:0007507]; intracellular estrogen receptor signaling pathway [GO:0030520]; intrinsic apoptotic signaling pathway by p53 class mediator [GO:0072332]; MAPK cascade [GO:0000165]; negative regulation of adipose tissue development [GO:1904178]; negative regulation of amacrine cell differentiation [GO:1902870]; negative regulation of cell differentiation [GO:0045596]; negative regulation of DNA-binding transcription factor activity [GO:0043433]; negative regulation of transcription by RNA polymerase II [GO:0000122]; neuromuscular process controlling balance [GO:0050885]; neuron differentiation [GO:0030182]; positive regulation of axon extension [GO:0045773]; positive regulation of cardiac muscle cell apoptotic process [GO:0010666]; positive regulation of cell differentiation [GO:0045597]; positive regulation of glucose import [GO:0046326]; positive regulation of osteoclast differentiation [GO:0045672]; positive regulation of programmed cell death [GO:0043068]; positive regulation of transcription by RNA polymerase II [GO:0045944]; positive regulation of transcription regulatory region DNA binding [GO:2000679]; regulation of DNA-binding transcription factor activity [GO:0051090]; regulation of gene expression [GO:0010468]; regulation of retinal ganglion cell axon guidance [GO:0090259]; regulation of transcription by RNA polymerase II [GO:0006357]; retina development in camera-type eye [GO:0060041]; retinal ganglion cell axon guidance [GO:0031290]; sensory perception of sound [GO:0007605]; spermatogenesis [GO:0007283] | cytoplasm [GO:0005737]; euchromatin [GO:0000791]; nuclear speck [GO:0016607]; nucleus [GO:0005634]; transcription regulator complex [GO:0005667] | chromatin binding [GO:0003682]; DNA-binding transcription activator activity, RNA polymerase II-specific [GO:0001228]; DNA-binding transcription factor activity, RNA polymerase II-specific [GO:0000981]; DNA-binding transcription repressor activity, RNA polymerase II-specific [GO:0001227]; p53 binding [GO:0002039]; promoter-specific chromatin binding [GO:1990841]; RNA polymerase II cis-regulatory region sequence-specific DNA binding [GO:0000978]; RNA polymerase II transcription regulatory region sequence-specific DNA binding [GO:0000977]; sequence-specific DNA binding [GO:0043565] | PF00046;PF00157; | 1.10.10.60;1.10.260.40; | POU transcription factor family, Class-4 subfamily | null | SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:18368538}. Nucleus speckle {ECO:0000250|UniProtKB:Q12837}. Cytoplasm {ECO:0000250|UniProtKB:Q63934}. | null | null | null | null | null | FUNCTION: Tissue-specific DNA-binding transcription factor involved in the development and differentiation of target cells. Functions either as activator or repressor modulating the rate of target gene transcription through RNA polymerase II enzyme in a promoter-dependent manner. Binds to the consensus octamer motif 5'-AT[A/T]A[T/A]T[A/T]A-3' of promoter of target genes. Plays a fundamental role in the gene regulatory network essential for retinal ganglion cell (RGC) differentiation. Binds to an octamer site to form a ternary complex with ISL1; cooperates positively with ISL1 and ISL2 to potentiate transcriptional activation of RGC target genes being involved in RGC fate commitment in the developing retina and RGC axon formation and pathfinding. Inhibits DLX1 and DLX2 transcriptional activities preventing DLX1- and DLX2-mediated ability to promote amacrine cell fate specification. In cooperation with TP53 potentiates transcriptional activation of BAX promoter activity increasing neuronal cell apoptosis. Negatively regulates BAX promoter activity in the absence of TP53. Acts as a transcriptional coactivator via its interaction with the transcription factor ESR1 by enhancing its effect on estrogen response element (ERE)-containing promoter. Antagonizes the transcriptional stimulatory activity of POU4F1 by preventing its binding to an octamer motif. Involved in TNFSF11-mediated terminal osteoclast differentiation. {ECO:0000250|UniProtKB:Q63934}. | Rattus norvegicus (Rat) |
G3V7P1 | STX12_RAT | MSYGPLDMYRNPGPSGPQPRDFNSIIQTCSGNIQRISQATAQIKNLMSQLGTKQDSSKLQENLQQFQHSTNQLAKETNELLKELGSLPLPLSASEQRQQKLQKERLMNDFSSALNNFQVVQRKVSEKEKESIARARAGSRLSAEDRQREEQLVSFDSHEEWNQMQSQEEEAAITEQDLELIKERETAIQQLEADILDVNQIFKDLAMMIHDQGDLIDSIEANVESSEVHVERASDQLQRAAYYQKKSRKKMCILVLVLSVIVTVLVVVIWVASK | null | null | autophagosome assembly [GO:0000045]; cholesterol efflux [GO:0033344]; endocytic recycling [GO:0032456]; intracellular protein transport [GO:0006886]; protein stabilization [GO:0050821]; regulation of postsynaptic membrane neurotransmitter receptor levels [GO:0099072]; synaptic vesicle to endosome fusion [GO:0016189]; vesicle docking [GO:0048278]; vesicle fusion [GO:0006906] | BLOC-1 complex [GO:0031083]; early endosome membrane [GO:0031901]; endomembrane system [GO:0012505]; Golgi membrane [GO:0000139]; membrane raft [GO:0045121]; phagocytic vesicle [GO:0045335]; phagophore assembly site [GO:0000407]; postsynaptic endosome membrane [GO:0098895]; postsynaptic recycling endosome [GO:0098837]; recycling endosome [GO:0055037]; recycling endosome membrane [GO:0055038]; SNARE complex [GO:0031201]; synaptic vesicle [GO:0008021]; synaptic vesicle membrane [GO:0030672]; vesicle [GO:0031982] | SNAP receptor activity [GO:0005484]; SNARE binding [GO:0000149] | PF05739;PF14523; | 1.20.5.110;1.20.58.70; | Syntaxin family | null | SUBCELLULAR LOCATION: Endosome membrane; Single-pass type IV membrane protein {ECO:0000269|PubMed:9553086}. Golgi apparatus membrane; Single-pass type IV membrane protein {ECO:0000269|PubMed:9553086}. Endomembrane system {ECO:0000305}; Single-pass type IV membrane protein {ECO:0000305}; Cytoplasmic side {ECO:0000305}. Early endosome membrane {ECO:0000269|PubMed:20098723}; Single-pass type IV membrane protein {ECO:0000305}. Recycling endosome membrane {ECO:0000269|PubMed:20098723, ECO:0000269|PubMed:30962439, ECO:0000269|PubMed:9553086}; Single-pass type IV membrane protein {ECO:0000305}. | null | null | null | null | null | FUNCTION: SNARE promoting fusion of transport vesicles with target membranes (PubMed:17159904, PubMed:30962439). Together with SNARE STX6, promotes movement of vesicles from endosomes to the cell membrane, and may therefore function in the endocytic recycling pathway (PubMed:30962439). Through complex formation with GRIP1, GRIA2 and NSG1 controls the intracellular fate of AMPAR and the endosomal sorting of the GRIA2 subunit toward recycling and membrane targeting (PubMed:16037816). {ECO:0000269|PubMed:16037816, ECO:0000269|PubMed:17159904, ECO:0000269|PubMed:30962439}. | Rattus norvegicus (Rat) |
G3V7R4 | FOXO1_RAT | MAEAPQVVETDPDFEPLPRQRSCTWPLPRPEFNQSNSTTSSPAPSGSTAANPDATASLASASAVSTDFMSNLSLLEESEDFARAPGCVAVAAAAAASRGLCGDFQGPEAGCVHSAPPQPPPTGPLSQPPPVPPAAAGPLAGQPRKTSSSRRNAWGNLSYADLITKAIESSAEKRLTLSQIYEWMVKSVPYFKDKGDSNSSAGWKNSIRHNLSLHSKFIRVQNEGTGKSSWWMLNPEGGKSGKSPRRRAASMDNNSKFAKSRGRAAKKKASLQSGQEGPGDSPGSQFSKWPASPGSHSNDDFDNWSTFRPRTSSNASTISGRLSPIMTEQDDLGDGDVHSLVYPPSAAKMASTLPSLSEISNPENMENLLDNLNLLSSPTSLTVSTQSSPGSMMQQTPCYSFAPPNTSLNSPSPNYAKYTYGQSSMSPVPQMPMQTLQDSKSSYGGLNQYNCAPGLLKELLTSDSPPHNDIMSPVDPGVAQPNSRVLGQNVLMGPNSVMPAYGSQAPHNKMMNPSSHTHPGHAQQTSSVNGRALPHVVNTMPHTSAMNRLTPVKTPLQVPLSHPMQMSALGNYSSVSSCNGYGRMGVLHQEKLPSDLDGMFIERLDCDMESIIRNDLMDGDTLDFNFDNVLPNQSFPHSVKTTTHSWVSG | null | null | apoptotic process [GO:0006915]; autophagy [GO:0006914]; blood vessel development [GO:0001568]; canonical Wnt signaling pathway [GO:0060070]; cell differentiation [GO:0030154]; cellular response to dexamethasone stimulus [GO:0071549]; cellular response to hydrogen peroxide [GO:0070301]; cellular response to hyperoxia [GO:0071455]; cellular response to insulin stimulus [GO:0032869]; cellular response to nitric oxide [GO:0071732]; cellular response to oxidative stress [GO:0034599]; cellular response to starvation [GO:0009267]; DNA damage response [GO:0006974]; enamel mineralization [GO:0070166]; gene expression [GO:0010467]; glucose homeostasis [GO:0042593]; insulin receptor signaling pathway [GO:0008286]; negative regulation of apoptotic process [GO:0043066]; negative regulation of canonical Wnt signaling pathway [GO:0090090]; negative regulation of cardiac muscle hypertrophy in response to stress [GO:1903243]; negative regulation of fat cell differentiation [GO:0045599]; negative regulation of insulin secretion [GO:0046676]; negative regulation of stress-activated MAPK cascade [GO:0032873]; neuronal stem cell population maintenance [GO:0097150]; positive regulation of apoptotic process [GO:0043065]; positive regulation of autophagy [GO:0010508]; positive regulation of DNA-templated transcription [GO:0045893]; positive regulation of gluconeogenesis [GO:0045722]; positive regulation of protein catabolic process [GO:0045732]; positive regulation of smooth muscle cell apoptotic process [GO:0034393]; positive regulation of transcription by RNA polymerase II [GO:0045944]; regulation of cell population proliferation [GO:0042127]; regulation of DNA-templated transcription [GO:0006355]; regulation of gluconeogenesis [GO:0006111]; regulation of neural precursor cell proliferation [GO:2000177]; regulation of reactive oxygen species metabolic process [GO:2000377]; regulation of transcription by RNA polymerase II [GO:0006357]; regulation of transcription initiation by RNA polymerase II [GO:0060260]; response to fatty acid [GO:0070542]; response to fluoride [GO:1902617]; response to insulin [GO:0032868] | cytoplasm [GO:0005737]; nucleoplasm [GO:0005654]; nucleus [GO:0005634] | beta-catenin binding [GO:0008013]; chromatin DNA binding [GO:0031490]; DNA binding [GO:0003677]; DNA-binding transcription activator activity, RNA polymerase II-specific [GO:0001228]; DNA-binding transcription factor activity [GO:0003700]; DNA-binding transcription factor activity, RNA polymerase II-specific [GO:0000981]; DNA-binding transcription repressor activity, RNA polymerase II-specific [GO:0001227]; nucleic acid binding [GO:0003676]; promoter-specific chromatin binding [GO:1990841]; protein phosphatase 2A binding [GO:0051721]; RNA polymerase II cis-regulatory region sequence-specific DNA binding [GO:0000978]; sequence-specific DNA binding [GO:0043565]; transcription coactivator binding [GO:0001223]; ubiquitin protein ligase binding [GO:0031625] | PF00250;PF16676;PF16675; | 1.10.10.10; | null | PTM: Phosphorylation by NLK promotes nuclear export and inhibits the transcriptional activity. In response to growth factors, phosphorylation on Thr-24, Ser-250 and Ser-313 by PKB/AKT1 promotes nuclear export and inactivation of transactivational activity (PubMed:19483080). Phosphorylation on Thr-24 is required for binding 14-3-3 proteins. Phosphorylation of Ser-250 decreases DNA-binding activity and promotes the phosphorylation of Thr-24 and Ser-313, permitting phosphorylation of Ser-316 and Ser-319, probably by CDK1, leading to nuclear exclusion and loss of function. Stress signals, such as response to oxygen or nitric oxide, attenuate the PKB/AKT1-mediated phosphorylation leading to nuclear retention. Phosphorylation of Ser-323 is independent of IGF1 and leads to reduced function. Dephosphorylated on Thr-24 and Ser-250 by PP2A in beta-cells under oxidative stress leading to nuclear retention. Phosphorylation of Ser-243 by CDK1 disrupts binding of 14-3-3 proteins leading to nuclear accumulation and has no effect on DNA binding nor transcriptional activity. Phosphorylation by STK4/MST1 on Ser-206, upon oxidative stress, inhibits binding to 14-3-3 proteins and nuclear export (By similarity). PPIA/CYPA promotes its dephosphorylation on Ser-250 (By similarity). {ECO:0000250|UniProtKB:Q12778, ECO:0000250|UniProtKB:Q9R1E0, ECO:0000269|PubMed:19483080}.; PTM: Ubiquitinated by SKP2 (By similarity). Ubiquitination leads to proteasomal degradation (By similarity). Ubiquitinated by STUB1/CHIP; when Ser-250 is phosphorylated (By similarity). {ECO:0000250|UniProtKB:Q12778, ECO:0000250|UniProtKB:Q9R1E0}.; PTM: Methylation inhibits AKT1-mediated phosphorylation at Ser-250 and is increased by oxidative stress. {ECO:0000250|UniProtKB:Q9R1E0}.; PTM: Acetylated. Acetylation at Lys-256 and Lys-268 are necessary for autophagic cell death induction. Deacetylated by SIRT2 in response to oxidative stress or serum deprivation, thereby negatively regulating FOXO1-mediated autophagic cell death. Once in the nucleus, acetylated by CREBBP/EP300. Acetylation diminishes the interaction with target DNA and attenuates the transcriptional activity. It increases the phosphorylation at Ser-250. Deacetylation by SIRT1 results in reactivation of the transcriptional activity. Oxidative stress by hydrogen peroxide treatment appears to promote deacetylation and uncoupling of insulin-induced phosphorylation. By contrast, resveratrol acts independently of acetylation. Acetylated at Lys-417, promoting its localization to the nucleus and transcription factor activity. Deacetylation at Lys-417 by SIRT6, promotes its translocation into the cytoplasm, preventing its transcription factor activity. Deacetylation and subsequent inhibition by SIRT6 has different effects depending on cell types: it inhibits gluconeogenesis in hepatocytes, promotes glucose sensing in pancreatic beta-cells and regulates lipid catabolism in brown adipocytes. {ECO:0000250|UniProtKB:Q12778}. | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:19483080}. Nucleus {ECO:0000250|UniProtKB:Q9R1E0}. Note=Shuttles between the cytoplasm and nucleus (By similarity). Largely nuclear in unstimulated cells (By similarity). In osteoblasts, colocalizes with ATF4 and RUNX2 in the nucleus. Serum deprivation increases localization to the nucleus, leading to activate expression of SOX9 and subsequent chondrogenesis (By similarity). Insulin-induced phosphorylation at Ser-253 by PKB/AKT1 leads, via stimulation of Thr-24 phosphorylation, to binding of 14-3-3 proteins and nuclear export to the cytoplasm where it is degraded by the ubiquitin-proteasomal pathway (By similarity). Phosphorylation at Ser-249 by CDK1 disrupts binding of 14-3-3 proteins and promotes nuclear accumulation (By similarity). Phosphorylation by NLK results in nuclear export (By similarity). Translocates to the nucleus upon oxidative stress-induced phosphorylation at Ser-212 by STK4/MST1 (By similarity). SGK1-mediated phosphorylation also results in nuclear translocation. Retained in the nucleus under stress stimuli including oxidative stress, nutrient deprivation or nitric oxide. Methylated form is nuclear (By similarity). PPIA/CYPA stimulates its nuclear accumulation (By similarity). Deacetylation by SIRT6, promotes its translocation into the cytoplasm (By similarity). {ECO:0000250|UniProtKB:Q12778, ECO:0000250|UniProtKB:Q9R1E0}. | null | null | null | null | null | FUNCTION: Transcription factor that is the main target of insulin signaling and regulates metabolic homeostasis in response to oxidative stress (By similarity). Binds to the insulin response element (IRE) with consensus sequence 5'-TT[G/A]TTTTG-3' and the related Daf-16 family binding element (DBE) with consensus sequence 5'-TT[G/A]TTTAC-3'. Activity suppressed by insulin (By similarity). Main regulator of redox balance and osteoblast numbers and controls bone mass (By similarity). Orchestrates the endocrine function of the skeleton in regulating glucose metabolism (By similarity). Also acts as a key regulator of chondrogenic commitment of skeletal progenitor cells in response to lipid availability: when lipids levels are low, translocates to the nucleus and promotes expression of SOX9, which induces chondrogenic commitment and suppresses fatty acid oxidation (By similarity). Acts synergistically with ATF4 to suppress osteocalcin/BGLAP activity, increasing glucose levels and triggering glucose intolerance and insulin insensitivity (By similarity). Also suppresses the transcriptional activity of RUNX2, an upstream activator of osteocalcin/BGLAP (By similarity). Acts as an inhibitor of glucose sensing in pancreatic beta cells by acting as a transcription repressor and suppressing expression of PDX1 (By similarity). In hepatocytes, promotes gluconeogenesis by acting together with PPARGC1A and CEBPA to activate the expression of genes such as IGFBP1, G6PC1 and PCK1 (By similarity). Also promotes gluconeogenesis by directly promoting expression of PPARGC1A and G6PC1 (By similarity). Important regulator of cell death acting downstream of CDK1, PKB/AKT1 and STK4/MST1 (By similarity). Promotes neural cell death (By similarity). Mediates insulin action on adipose tissue (By similarity). Regulates the expression of adipogenic genes such as PPARG during preadipocyte differentiation and, adipocyte size and adipose tissue-specific gene expression in response to excessive calorie intake (By similarity). Regulates the transcriptional activity of GADD45A and repair of nitric oxide-damaged DNA in beta-cells (By similarity). Required for the autophagic cell death induction in response to starvation or oxidative stress in a transcription-independent manner (By similarity). Mediates the function of MLIP in cardiomyocytes hypertrophy and cardiac remodeling (PubMed:26436652). Positive regulator of apoptosis in cardiac smooth muscle cells as a result of its transcriptional activation of pro-apoptotic genes (PubMed:19483080). Regulates endothelial cell (EC) viability and apoptosis in a PPIA/CYPA-dependent manner via transcription of CCL2 and BCL2L11 which are involved in EC chemotaxis and apoptosis (By similarity). {ECO:0000250|UniProtKB:Q12778, ECO:0000250|UniProtKB:Q9R1E0, ECO:0000269|PubMed:19483080, ECO:0000269|PubMed:26436652}. | Rattus norvegicus (Rat) |
G3V7W1 | PDCD6_RAT | MAAYSYRPGPGAGPGPAAGAALPDQSFLWNVFQRVDKDRSGVISDNELQQALSNGTWTPFNPVTVRSIISMFDRENKAGVNFSEFTGVWKYITDWQNVFRTYDRDNSGMIDKHELKQALSGFGYRLSDQFHDILIRKFDRQGRGQIAFDDFIQGCIVLQRLTDIFRRYDTDQDGWIQVSYEQYLSMVFSIV | null | null | angiogenesis [GO:0001525]; apoptotic process [GO:0006915]; cellular response to heat [GO:0034605]; COPII vesicle coating [GO:0048208]; endoplasmic reticulum to Golgi vesicle-mediated transport [GO:0006888]; intracellular protein transport [GO:0006886]; negative regulation of phosphatidylinositol 3-kinase/protein kinase B signal transduction [GO:0051898]; negative regulation of TOR signaling [GO:0032007]; negative regulation of vascular endothelial growth factor receptor signaling pathway [GO:0030948]; neural crest cell development [GO:0014032]; neural crest formation [GO:0014029]; positive regulation of angiogenesis [GO:0045766]; positive regulation of endothelial cell migration [GO:0010595]; positive regulation of endothelial cell proliferation [GO:0001938]; positive regulation of protein monoubiquitination [GO:1902527]; response to calcium ion [GO:0051592]; vascular endothelial growth factor receptor-2 signaling pathway [GO:0036324] | COPII vesicle coat [GO:0030127]; Cul3-RING ubiquitin ligase complex [GO:0031463]; cytoplasm [GO:0005737]; cytoplasmic vesicle [GO:0031410]; cytosol [GO:0005829]; endoplasmic reticulum [GO:0005783]; endoplasmic reticulum exit site [GO:0070971]; endoplasmic reticulum membrane [GO:0005789]; endosome [GO:0005768]; nucleoplasm [GO:0005654]; nucleus [GO:0005634] | calcium ion binding [GO:0005509]; calcium-dependent protein binding [GO:0048306]; identical protein binding [GO:0042802]; magnesium ion binding [GO:0000287]; protein dimerization activity [GO:0046983]; protein homodimerization activity [GO:0042803]; protein-macromolecule adaptor activity [GO:0030674]; protein-membrane adaptor activity [GO:0043495]; ubiquitin ligase-substrate adaptor activity [GO:1990756] | PF13499; | 1.10.238.10; | null | null | SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000269|PubMed:27276012}; Peripheral membrane protein {ECO:0000250|UniProtKB:O75340}. Cytoplasmic vesicle, COPII-coated vesicle membrane {ECO:0000250|UniProtKB:O75340}. Cytoplasm {ECO:0000250|UniProtKB:O75340}. Nucleus {ECO:0000250|UniProtKB:O75340}. Endosome {ECO:0000250|UniProtKB:O75340}. Note=Interaction with RBM22 induces relocalization from the cytoplasm to the nucleus (By similarity). Translocated from the cytoplasm to the nucleus after heat shock cell treatment (By similarity). Accumulates in cytoplasmic vesicle-like organelles after heat shock treatment, which may represent stress granules (By similarity). In response to calcium increase, relocates from cytoplasm to COPII vesicle coat (By similarity). Localizes to endoplasmic reticulum exit site (ERES) (PubMed:27276012). {ECO:0000250|UniProtKB:O75340, ECO:0000269|PubMed:27276012}. | null | null | null | null | null | FUNCTION: Calcium sensor that plays a key role in processes such as endoplasmic reticulum (ER)-Golgi vesicular transport, endosomal biogenesis or membrane repair (By similarity). Acts as an adapter that bridges unrelated proteins or stabilizes weak protein-protein complexes in response to calcium: calcium-binding triggers exposure of apolar surface, promoting interaction with different sets of proteins thanks to 3 different hydrophobic pockets, leading to translocation to membranes (By similarity). Involved in ER-Golgi transport (PubMed:27276012). Regulates ER-Golgi transport by promoting the association between PDCD6IP and TSG101, thereby bridging together the ESCRT-III and ESCRT-I complexes (By similarity). Together with PEF1, acts as a calcium-dependent adapter for the BCR(KLHL12) complex, a complex involved in ER-Golgi transport by regulating the size of COPII coats (By similarity). In response to cytosolic calcium increase, the heterodimer formed with PEF1 interacts with, and bridges together the BCR(KLHL12) complex and SEC31 (SEC31A or SEC31B), promoting monoubiquitination of SEC31 and subsequent collagen export, which is required for neural crest specification (By similarity). Involved in the regulation of the distribution and function of MCOLN1 in the endosomal pathway (By similarity). Promotes localization and polymerization of TFG at endoplasmic reticulum exit site (By similarity). Required for T-cell receptor-, Fas-, and glucocorticoid-induced apoptosis (By similarity). May mediate Ca(2+)-regulated signals along the death pathway: interaction with DAPK1 can accelerate apoptotic cell death by increasing caspase-3 activity (By similarity). Its role in apoptosis may however be indirect, as suggested by knockout experiments (By similarity). May inhibit KDR/VEGFR2-dependent angiogenesis; the function involves inhibition of VEGF-induced phosphorylation of the Akt signaling pathway (By similarity). {ECO:0000250|UniProtKB:O75340, ECO:0000250|UniProtKB:P12815, ECO:0000269|PubMed:27276012}.; FUNCTION: [Isoform 2]: Has a lower Ca(2+) affinity than isoform 1 (By similarity). {ECO:0000250|UniProtKB:P12815}. | Rattus norvegicus (Rat) |
G3V7X8 | CP26B_RAT | MLFEGLELVSALATLAACLVSVTLLLAVSQQLWQLRWAATRDKSCKLPIPKGSMGFPLIGETGHWLLQGSGFQSSRREKYGNVFKTHLLGRPLIRVTGAENVRKILLGEHQLVSTEWPRSARVLLGPNTVANSIGDIHRNKRKVFSKIFSHEALESYLPKIQLVIQDTLRAWSSQPEAINVYQEAQRLTFRMAVRVLLGFSIPEEDLGNLFEVYQQFVENVFSLPVDLPFSGYRRGIQARQILQKGLEKAIREKLQCTQGKDYSDALDILIESSKEHGKEMTMQELKDGTLELIFAAYATTASASTSLIMQLLKHPAVLEKLREELRAQGLLHGGGCPCEGTLRLDMLSGLRYLDCVIKEVMRLFTPVSGGYRTVLQTFELDGFQIPKGWSVMYSIRDTHDTAPVFKDVNVFDPDRFSQARSEDKDGRFHYLPFGGGVRTCLGKHLAKLFLKVLAVELASTSRFELATRTFPRITLVPVLHPVDGLSVKFFGLDSNQNEILPETEAMLSATV | 1.14.13.- | COFACTOR: Name=heme; Xref=ChEBI:CHEBI:30413; Evidence={ECO:0000250|UniProtKB:Q9Y6A2}; | bone morphogenesis [GO:0060349]; cell fate determination [GO:0001709]; cellular response to retinoic acid [GO:0071300]; cornification [GO:0070268]; embryonic limb morphogenesis [GO:0030326]; establishment of skin barrier [GO:0061436]; establishment of T cell polarity [GO:0001768]; inflammatory response [GO:0006954]; kidney development [GO:0001822]; male meiotic nuclear division [GO:0007140]; negative regulation of retinoic acid receptor signaling pathway [GO:0048387]; positive regulation of gene expression [GO:0010628]; positive regulation of tongue muscle cell differentiation [GO:2001037]; proximal/distal pattern formation [GO:0009954]; regulation of retinoic acid receptor signaling pathway [GO:0048385]; regulation of T cell differentiation [GO:0045580]; response to retinoic acid [GO:0032526]; response to vitamin A [GO:0033189]; retinoic acid catabolic process [GO:0034653]; retinoic acid metabolic process [GO:0042573]; retinoic acid receptor signaling pathway [GO:0048384]; spermatogenesis [GO:0007283]; sterol metabolic process [GO:0016125]; tongue morphogenesis [GO:0043587]; xenobiotic metabolic process [GO:0006805] | cytoplasm [GO:0005737]; endoplasmic reticulum membrane [GO:0005789] | all-trans retinoic acid 18-hydroxylase activity [GO:0062183]; heme binding [GO:0020037]; iron ion binding [GO:0005506]; monooxygenase activity [GO:0004497]; oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen, NAD(P)H as one donor, and incorporation of one atom of oxygen [GO:0016709]; retinoic acid 4-hydroxylase activity [GO:0008401]; retinoic acid binding [GO:0001972] | PF00067; | 1.10.630.10; | Cytochrome P450 family | null | SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000250|UniProtKB:O43174}; Peripheral membrane protein {ECO:0000250|UniProtKB:O43174}. Microsome membrane {ECO:0000250|UniProtKB:O43174}; Peripheral membrane protein {ECO:0000250|UniProtKB:O43174}. | CATALYTIC ACTIVITY: Reaction=all-trans-retinoate + O2 + reduced [NADPH--hemoprotein reductase] = all-trans-4-hydroxyretinoate + H(+) + H2O + oxidized [NADPH--hemoprotein reductase]; Xref=Rhea:RHEA:51984, Rhea:RHEA-COMP:11964, Rhea:RHEA-COMP:11965, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, ChEBI:CHEBI:35291, ChEBI:CHEBI:57618, ChEBI:CHEBI:58210, ChEBI:CHEBI:134178; Evidence={ECO:0000250|UniProtKB:Q811W2}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:51985; Evidence={ECO:0000250|UniProtKB:Q811W2}; CATALYTIC ACTIVITY: Reaction=all-trans-retinoate + O2 + reduced [NADPH--hemoprotein reductase] = all-trans-18-hydroxyretinoate + H(+) + H2O + oxidized [NADPH--hemoprotein reductase]; Xref=Rhea:RHEA:55856, Rhea:RHEA-COMP:11964, Rhea:RHEA-COMP:11965, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, ChEBI:CHEBI:35291, ChEBI:CHEBI:57618, ChEBI:CHEBI:58210, ChEBI:CHEBI:139258; Evidence={ECO:0000250|UniProtKB:Q811W2}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:55857; Evidence={ECO:0000250|UniProtKB:Q811W2}; | null | null | null | null | FUNCTION: A cytochrome P450 monooxygenase involved in the metabolism of retinoates (RAs), the active metabolites of vitamin A, and critical signaling molecules in animals (By similarity). RAs exist as at least four different isomers: all-trans-RA (atRA), 9-cis-RA, 13-cis-RA, and 9,13-dicis-RA, where atRA is considered to be the biologically active isomer, although 9-cis-RA and 13-cis-RA also have activity (By similarity). Catalyzes the hydroxylation of atRA primarily at C-4 and C-18, thereby contributing to the regulation of atRA homeostasis and signaling (By similarity). Hydroxylation of atRA limits its biological activity and initiates a degradative process leading to its eventual elimination (By similarity). Involved in the convertion of atRA to all-trans-4-oxo-RA. Can oxidize all-trans-13,14-dihydroretinoate (DRA) to metabolites which could include all-trans-4-oxo-DRA, all-trans-4-hydroxy-DRA, all-trans-5,8-epoxy-DRA, and all-trans-18-hydroxy-DRA (By similarity). Shows preference for the following substrates: atRA > 9-cis-RA > 13-cis-RA (By similarity). Plays a central role in germ cell development: acts by degrading RAs in the developing testis, preventing STRA8 expression, thereby leading to delay of meiosis. Required for the maintenance of the undifferentiated state of male germ cells during embryonic development in Sertoli cells, inducing arrest in G0 phase of the cell cycle and preventing meiotic entry. Plays a role in skeletal development, both at the level of patterning and in the ossification of bone and the establishment of some synovial joints. Essential for postnatal survival (By similarity). {ECO:0000250|UniProtKB:Q811W2, ECO:0000250|UniProtKB:Q9NR63}.; FUNCTION: Has also a significant activity in oxidation of tazarotenic acid and may therefore metabolize that xenobiotic in vivo. {ECO:0000250|UniProtKB:Q9NR63}. | Rattus norvegicus (Rat) |
G3V893 | ZN335_RAT | MEENEVESSSDAAPRPGQPEEPSESGLGVGTSEAVSADSTDAATAPGLTEADDSGVGQSSDSGSRSVEEVSESISTEPLPQGYLPDSSSVSRGPVAEVPGGPPALVHSSALPDPSMLVSDCTASSSDLGSAIDKIIESTIGPDLIQSCITVTSGEEGGAETTQYLILQGPDDGAPMASSMSTSTLANSLAAIEALADGPTSTSTCLEPAEQPPGEPSSLAQPPAPVVEELDLQGLEAMMEVVVVQQFKCKMCQYRSSTKATLLRHMRERHFRPALAVAAAAAGKRGRVRKWGTSTKTTEEEGPEEEEEDDDIVDAGAIDDLEEDSDYNPAEDEPRGRQLRLQRPTPSTLRPRRRPGRPRKLPRLETSDLHDGIGEPLVSSQSTQSPPELQDLEAPSSSDLRALGKVGRGLVETGVSQSDAENAAPSCQDEADVPPRRRGRPSRRFLGKKYRKYYYKSPKPLLRPYLCRICGSRFLSHEDLRFHVNSHEAGDPQLFKCLQCSYRSRRWSSLKEHMFNHVGSKPYKCDECSYTSVYRKDVIRHAAVHSQDRKKRPDPTPKLSSFPCPVCGRVYPMQKRLTQHMKTHSTEKPHMCDKCGKSFKKRYTFKMHLLTHIQAVANRRFKCEFCEFVCEDKKALLNHQLSHVSDKPFKCSFCPYRTFREDFLLSHVAVKHTGAKPFACEYCHFSTRHKKNLRLHVRCRHANSFEEWGRRHPEEPPSRRRPFFSLQQIEELKQQHSAAPGPPLSSAGPEAPQEPAPFQPPETPPLLCPDALGGATIIYQQGAEESTAMATQTALDLLLNMSAQRELGATALQVAVVKSEDVEAELTSTARQPSSEDTTPRVVTLHVAESGSSVAAESQLGPSDLQQIALPPGPFSGASYSVITAPPVEGRASASGPPYREEPPGEAAQAVVVNDTLKEAGTHYIMAADGTQLHHIELTADGSISFPSPDTLAPGTKWPLLQCGGPPRDGPEVLSPTKTHHTGGSQGSSTPPPATSHALGLLVPHSPPSAAASSTKKFSCKVCSEAFPSRAEMESHKRAHAGPAAFKCPDCPFSARQWPEVRAHMAQHSSLRPHQCNQCSFASKNKKDLRRHMLTHTNEKPFSCHVCGQRFNRNGHLKFHIQRLHSIDGRKTGTSTARAPAQTIILNSEEETLATLHTAFQSNHGTLGTERLQQALSQEHIIVAQEQTVANQEEATYIQEITADGQTVQHLVTSDNQVQYIISQDGVQHLLPQEYVVVPDGHHIQVQEGQITHIQYEQGTPFLQESQIQYVPVSPSQQLVTQAQLEAAAHSAVTAVADAAMAQAQGLFGTEEAVPEHIQQLQHQGIEYDVITLSDD | null | null | brain development [GO:0007420]; brain morphogenesis [GO:0048854]; cerebral cortex neuron differentiation [GO:0021895]; epigenetic regulation of gene expression [GO:0040029]; in utero embryonic development [GO:0001701]; neuron projection morphogenesis [GO:0048812]; positive regulation of lymphocyte proliferation [GO:0050671]; positive regulation of neuroblast proliferation [GO:0002052]; positive regulation of neurogenesis [GO:0050769]; positive regulation of transcription by RNA polymerase II [GO:0045944]; regulation of gene expression [GO:0010468]; regulation of neurogenesis [GO:0050767] | histone methyltransferase complex [GO:0035097]; nucleus [GO:0005634] | histone methyltransferase binding [GO:1990226]; metal ion binding [GO:0046872]; nuclear receptor coactivator activity [GO:0030374]; RNA polymerase II cis-regulatory region sequence-specific DNA binding [GO:0000978]; transcription cis-regulatory region binding [GO:0000976] | PF00096;PF13912;PF13909; | 3.30.160.60; | Krueppel C2H2-type zinc-finger protein family | null | SUBCELLULAR LOCATION: Nucleus {ECO:0000250}. | null | null | null | null | null | FUNCTION: Component or associated component of some histone methyltransferase complexes may regulate transcription through recruitment of those complexes on gene promoters (By similarity). Enhances ligand-dependent transcriptional activation by nuclear hormone receptors (By similarity). Plays an important role in neural progenitor cell proliferation and self-renewal through the regulation of specific genes involved brain development, including REST (By similarity). Also controls the expression of genes involved in somatic development and regulates, for instance, lymphoblast proliferation (By similarity). {ECO:0000250|UniProtKB:Q9H4Z2}. | Rattus norvegicus (Rat) |
G3V8D4 | APOC2_RAT | MGSRFFLALFLALLVLGNEVQGTEEDDPGSSALLDTVQEHLFSYWNSAKAAAGELYQKTYLTSVDEKLRDMYSKSSAAMTTYAGIFTDQLLTLLKGE | null | null | cholesterol efflux [GO:0033344]; chylomicron remnant clearance [GO:0034382]; high-density lipoprotein particle clearance [GO:0034384]; lipid catabolic process [GO:0016042]; lipoprotein transport [GO:0042953]; negative regulation of cholesterol transport [GO:0032375]; negative regulation of lipid metabolic process [GO:0045833]; negative regulation of receptor-mediated endocytosis [GO:0048261]; negative regulation of very-low-density lipoprotein particle clearance [GO:0010916]; phospholipid efflux [GO:0033700]; positive regulation of fatty acid biosynthetic process [GO:0045723]; positive regulation of phospholipid catabolic process [GO:0060697]; positive regulation of triglyceride catabolic process [GO:0010898]; response to xenobiotic stimulus [GO:0009410]; triglyceride homeostasis [GO:0070328] | chylomicron [GO:0042627]; extracellular space [GO:0005615]; intermediate-density lipoprotein particle [GO:0034363]; low-density lipoprotein particle [GO:0034362]; spherical high-density lipoprotein particle [GO:0034366]; very-low-density lipoprotein particle [GO:0034361] | lipase inhibitor activity [GO:0055102]; lipid binding [GO:0008289]; lipoprotein lipase activator activity [GO:0060230]; molecular function activator activity [GO:0140677]; phospholipase activator activity [GO:0016004]; phospholipase binding [GO:0043274] | PF05355; | 1.10.1440.10; | Apolipoprotein C2 family | PTM: Proapolipoprotein C-II is synthesized as a sialic acid containing glycoprotein which is subsequently desialylated prior to its proteolytic processing. {ECO:0000250|UniProtKB:P02655}.; PTM: Proapolipoprotein C-II, the major form found in plasma undergoes proteolytic cleavage of its N-terminal hexapeptide to generate the mature form apolipoprotein C-II, which occurs as the minor form in plasma. {ECO:0000250|UniProtKB:P02655}. | SUBCELLULAR LOCATION: Secreted {ECO:0000250|UniProtKB:P02655}. | null | null | null | null | null | FUNCTION: Component of chylomicrons, very low-density lipoproteins (VLDL), low-density lipoproteins (LDL), and high-density lipoproteins (HDL) in plasma. Plays an important role in lipoprotein metabolism as an activator of lipoprotein lipase. {ECO:0000250|UniProtKB:P02655}. | Rattus norvegicus (Rat) |
G3V8H4 | CBLC_RAT | MAAATAPQGWQWGEPRALGRAVKLLQRLEEQCRDLRLFVGPPSLRDLLPRTAQLLREVAKARSDKTRGDPEGPGGAGDFLVIYLTNLEAKGRQVAELLPHRGKKDANQDVFPEGSRFRRQLAKLALIFSHMHAELSALFPEGKYCGHLYQITKGSANTFWRENCGVRCVLPWAEFQSLLCSCHPVEPGPIMQALRSTLDLTCSGHVSVFEFDIFTRLFQPWPTLLKNWQLLAVNHPGYMAFLTYDEVQTRLQAYRDKPGSYIFRPSCTRLGQWAIGYVSSNGSILQTIPLNKPLLQVLLKGQKDGIFLYPDGKNHNPDLTELCRAVLNQCIQVSQEQLQLYQAMNSTFELCKICTERDKDVRIEPCGHLLCSCCLAAWQHSDSQTCPFCRCEIKGREAVSICQAQERSMEVRTTAGDSGDNCHQEAAEWKLESVTPSAPPLPPEVPCPQRPQNKGWLTLAPFTLPRLRPPLPLPKMASVLWEVTSRPQVREGATESS | 2.3.2.27 | null | cell surface receptor signaling pathway [GO:0007166]; negative regulation of epidermal growth factor receptor signaling pathway [GO:0042059]; negative regulation of neuron apoptotic process [GO:0043524]; protein catabolic process [GO:0030163]; protein stabilization [GO:0050821]; protein ubiquitination [GO:0016567]; response to glial cell derived neurotrophic factor [GO:1990790]; signal transduction [GO:0007165]; ubiquitin-dependent protein catabolic process [GO:0006511] | membrane raft [GO:0045121]; plasma membrane [GO:0005886] | calcium ion binding [GO:0005509]; epidermal growth factor receptor binding [GO:0005154]; phosphotyrosine residue binding [GO:0001784]; receptor tyrosine kinase binding [GO:0030971]; SH3 domain binding [GO:0017124]; ubiquitin protein ligase activity [GO:0061630] | PF02262;PF02761;PF02762;PF13920; | 1.20.930.20;1.10.238.10;3.30.505.10;3.30.40.10; | null | PTM: Phosphorylated on multiple tyrosine residues by SRC. {ECO:0000250}.; PTM: Autoubiquitinated, when phosphorylated at Tyr-341. | null | CATALYTIC ACTIVITY: Reaction=S-ubiquitinyl-[E2 ubiquitin-conjugating enzyme]-L-cysteine + [acceptor protein]-L-lysine = [E2 ubiquitin-conjugating enzyme]-L-cysteine + N(6)-ubiquitinyl-[acceptor protein]-L-lysine.; EC=2.3.2.27; Evidence={ECO:0000250|UniProtKB:Q9ULV8}; | null | null | null | null | FUNCTION: Acts as an E3 ubiquitin-protein ligase, which accepts ubiquitin from specific E2 ubiquitin-conjugating enzymes, and then transfers it to substrates promoting their degradation by the proteasome. Functionally coupled with the E2 ubiquitin-protein ligases UB2D1, UB2D2 and UB2D3. Regulator of EGFR mediated signal transduction; upon EGF activation, ubiquitinates EGFR. Inhibits EGF stimulated MAPK1 activation. Promotes ubiquitination of SRC phosphorylated at 'Tyr-419', has the highest ubiquitin ligase activity among CBL family proteins. In collaboration with CD2AP may act as regulatory checkpoint for Ret signaling by modulating the rate of RET degradation after ligand activation; CD2AP converts it from an inhibitor to a promoter of RET degradation; the function limits the potency of GDNF on neuronal survival. {ECO:0000269|PubMed:18753381}. | Rattus norvegicus (Rat) |
G3V8V5 | KCNK4_RAT | MRSTTLLALLALVLLYLVSGALVFQALEQPHEQQVQKDLEDGRDQFLKDHPCVSQKNLEGFIKLVAEALGGGANPETSWTNSSNHSSAWNLGSAFFFSGTIITTIGYGNIALHTDAGRLFCIFYALVGIPLFGMLLAGVGDRLGSSLRRGIGHIEAVFLKWHVPPGLVRMLSAVLFLLIGCLLFVLTPTFVFSYMESWSKLEAIYFVIVTLTTVGFGDYVPGDGTGQNSPAYQPLVWFWILFGLAYFASVLTTIGNWLRAVSRRTRAEMGGLTAQAASWTGTVTARVTQRTGPSAPPPEKEQPLLPSSLPAPPAVAEPAHRPGSPAPAEKVETPPPTASALDYPSENLAFIDESSDTQSERGCALPRAPRGRRRPNPTKKPSRPRGPGRLRDKAVPV | null | null | cellular response to alkaline pH [GO:0071469]; cellular response to fatty acid [GO:0071398]; cellular response to mechanical stimulus [GO:0071260]; cellular response to temperature stimulus [GO:0071502]; detection of mechanical stimulus involved in sensory perception of touch [GO:0050976]; memory [GO:0007613]; potassium ion transmembrane transport [GO:0071805]; sensory perception of pain [GO:0019233]; sensory perception of temperature stimulus [GO:0050951]; stabilization of membrane potential [GO:0030322] | plasma membrane [GO:0005886]; potassium channel complex [GO:0034705] | mechanosensitived potassium channel activity [GO:0098782]; outward rectifier potassium channel activity [GO:0015271]; potassium channel activity [GO:0005267]; potassium ion leak channel activity [GO:0022841]; temperature-gated cation channel activity [GO:0097604] | PF07885; | 1.10.287.70; | Two pore domain potassium channel (TC 1.A.1.8) family | null | SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:11374070}; Multi-pass membrane protein {ECO:0000305}. | null | null | null | null | null | FUNCTION: Voltage-insensitive potassium channel (PubMed:11374070, PubMed:15677687). Channel opening is triggered by mechanical forces that deform the membrane, and by raising the intracellular pH to basic levels (PubMed:11374070, PubMed:15677687). The channel is inactive at 24 degrees Celsius (in vitro); raising the temperature to 37 degrees Celsius increases the frequency of channel opening, with a further increase in channel activity when the temperature is raised to 42 degrees Celsius (PubMed:15677687). Plays a role in the perception of pain caused by heat (By similarity). Plays a role in the sensory perception of pain caused by pressure (By similarity). {ECO:0000250|UniProtKB:O88454, ECO:0000269|PubMed:11374070, ECO:0000269|PubMed:15677687}. | Rattus norvegicus (Rat) |
G3V909 | ATF6A_RAT | MESPFSPVLPHGPGEDWESTLFAELGYFTDTDDVQFDAAHETYENNFDHLNFDLDLMPWESDIWSPSSHFCSDIKAEPQPLSPASSSCSVSSPRSTDSCSSTQHVPEELDLLSSSQSPLSLYGDSCHSPSSAEPLKEEKPVTGPGNKTEHGLTPKKKIQMSSKPSVQPKPLLLPAAPKTPANASVPAKTIIIQTLPALMPLAKQQSIISIQPAPTKGQTVLLSQPAVVQLQTPGVLPSAQPVLAVTGGATQLPNHVVNVVPAPVVNSPVNGKLCVTKPVLQSSTRSTGSDIAVLRRQQRMIKNRESACQSRKKKKEYMLGLEARLKAALSENEQLKKENGSLKRQLDQVVSENQRLKVPSPKRRAVCVMIVLAFIMLNYGPMSMLEQDSRRVKPSVSPANQRRHLLEFSAKEVKDTSDGDNQKNSYRYDHSVSNDKALMVLSEEPLLYIPPPPCQPLINTTESLRLNHELRGWVHRHEVERTKSRRMTNSQQKTRILQGALEQGSNSQLMAVQYTETTSISRNSGSELQVYYASPGSYQGFFDAIRRRGDTFYVVSFRRDHLLLPATTHNKTTRPKMSIVLPAININDNVINGQDYEVMMQIDCQVMDTRILHIKSSSVPPYLRDHQRNQTSTFFGSPPTATETTHVVSTLPESVQ | null | null | endoplasmic reticulum unfolded protein response [GO:0030968]; eye development [GO:0001654]; positive regulation of apoptotic process [GO:0043065]; positive regulation of ATF6-mediated unfolded protein response [GO:1903893]; positive regulation of autophagy [GO:0010508]; positive regulation of transcription by RNA polymerase II [GO:0045944]; regulation of transcription by RNA polymerase II [GO:0006357]; response to endoplasmic reticulum stress [GO:0034976]; visual perception [GO:0007601] | endoplasmic reticulum [GO:0005783]; endoplasmic reticulum membrane [GO:0005789]; Golgi apparatus [GO:0005794]; Golgi membrane [GO:0000139]; membrane [GO:0016020]; nucleus [GO:0005634]; RNA polymerase II transcription regulator complex [GO:0090575] | DNA-binding transcription activator activity, RNA polymerase II-specific [GO:0001228]; DNA-binding transcription factor activity [GO:0003700]; DNA-binding transcription factor activity, RNA polymerase II-specific [GO:0000981]; enzyme binding [GO:0019899]; identical protein binding [GO:0042802]; protein heterodimerization activity [GO:0046982]; RNA polymerase II cis-regulatory region sequence-specific DNA binding [GO:0000978]; RNA polymerase II transcription regulatory region sequence-specific DNA binding [GO:0000977]; sequence-specific DNA binding [GO:0043565]; sequence-specific double-stranded DNA binding [GO:1990837]; transcription cis-regulatory region binding [GO:0000976]; ubiquitin protein ligase binding [GO:0031625] | PF00170; | 1.20.5.170; | BZIP family, ATF subfamily | PTM: During unfolded protein response, a fragment of approximately 50 kDa containing the cytoplasmic transcription factor domain is released by proteolysis. The cleavage seems to be performed sequentially by site-1 (MBTPS1, S1P) and site-2 (MBTPS2, S2P) proteases (By similarity). {ECO:0000250|UniProtKB:P18850}.; PTM: N-glycosylated. The glycosylation status may serve as a sensor for ER homeostasis, resulting in ATF6 activation to trigger the unfolded protein response (UPR) (By similarity). {ECO:0000250|UniProtKB:P18850}.; PTM: Ubiquitinated by RNF186 at Lys-139, which is required for pattern recognition receptor-induced unfolded protein response-associated outcomes. {ECO:0000250|UniProtKB:P18850}. | SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000269|PubMed:22682248}; Single-pass type II membrane protein {ECO:0000255}. Golgi apparatus membrane {ECO:0000250|UniProtKB:P18850}; Single-pass type II membrane protein {ECO:0000255}. Note=Translocates from the endoplasmic reticulum to the Golgi, where it is processed. {ECO:0000250|UniProtKB:P18850}.; SUBCELLULAR LOCATION: [Processed cyclic AMP-dependent transcription factor ATF-6 alpha]: Nucleus {ECO:0000269|PubMed:22682248}. Note=Under ER stress the cleaved N-terminal cytoplasmic domain translocates into the nucleus (PubMed:22682248). THBS4 promotes its nuclear shuttling (By similarity). {ECO:0000250|UniProtKB:F6VAN0, ECO:0000269|PubMed:22682248}. | null | null | null | null | null | FUNCTION: [Cyclic AMP-dependent transcription factor ATF-6 alpha]: Precursor of the transcription factor form (Processed cyclic AMP-dependent transcription factor ATF-6 alpha), which is embedded in the endoplasmic reticulum membrane. Endoplasmic reticulum stress promotes processing of this form, releasing the transcription factor form that translocates into the nucleus, where it activates transcription of genes involved in the unfolded protein response (UPR). {ECO:0000250|UniProtKB:P18850}.; FUNCTION: [Processed cyclic AMP-dependent transcription factor ATF-6 alpha]: Transcription factor that initiates the unfolded protein response (UPR) during endoplasmic reticulum stress by activating transcription of genes involved in the UPR. Binds DNA on the 5'-CCAC[GA]-3'half of the ER stress response element (ERSE) (5'-CCAAT-N(9)-CCAC[GA]-3') and of ERSE II (5'-ATTGG-N-CCACG-3'). Binding to ERSE requires binding of NF-Y to ERSE. Could also be involved in activation of transcription by the serum response factor. May play a role in foveal development and cone function in the retina. {ECO:0000250|UniProtKB:P18850}. | Rattus norvegicus (Rat) |
G3V928 | LRP1_RAT | MLTPPLLLLLPLLSALVAGATMDAPKTCSPKQFACRDQITCISKGWRCDGERDCPDGSDEAPEICPQSKAQRCPPNEHSCLGTELCVPMSRLCNGIQDCMDGSDEGAHCRELRVNCSRMGCQHHCVPTPSGPTCYCNNSFQLQADGKTCKDFDECSVYGTCSQLCTNTDGSFTCGCVEGYLLQPDNRSCKAKNEPVDRPPVLLIANSQNILATYLSGAQVSTITPTSTRQTTAMDFSYANETVCWVHVGDSAAQTQLKCARMPSLKGFVDEHTINISLSLHHVEQMAIDWLTGNFYFVDDIDDRIFVCNRNGDTCVTLLDLELYNPKGIALDPAMGKVFFTDYGQIPKVERCDMDGQNRTKLVDSKIVFPHGITLDLVSRLVYWADAYLDYIEVVDYEGKGRQTIIQGILIEHLYGLTVFENYLYATNSDNANTQQKTSVIRVNRFNSTEYQVVTRVDKGGALHIYHQRRQPRVRSHACENDQYGKPGGCSDICLLANSHKARTCRCRSGFSLGSDGKSCKKPEHELFLVYGKGRPGIIRGMDMGAKVPDEHMIPIENLMNPRALDFHAETGFIYFADTTSYLIGRQKIDGTERETILKDGIHNVEGVAVDWMGDNLYWTDDGPKKTISVARLEKAAQTRKTLIEGKMTHPRAIVVDPLNGWMYWTDWEEDPKDSRRGRLERAWMDGSHRDIFVTSKTVLWPNGLSLDIPAGRLYWVDAFYDRIETILLNGTDRKIVYEGPELNHAFGLCHHGNYLFWTEYRSGSVYRLERGVAGAQPTVTLLRSERPPIFEIRMYDAQQQQVGTNKCRVNNGGCSSLCLATPGSRQCACAEDQVLDADGVTCLANPSYVPPPQCQPGEFACANNRCIQERWKCDGDNDCLDNSDEAPALCHQHTCPSDRFKCENNRCIPNRWLCDGDNDCGNSEDESNATCSARTCPPNQFSCASGRCIPISWTCDLDDDCGDRSDESASCAYPTCFPLTQFTCNNGRCININWRCDNDNDCGDNSDEAGCSHSCSSTQFKCNSGRCIPEHWTCDGDNDCGDYSDETHANCTNQATRPPGGCHSDEFQCRLDGLCIPLRWRCDGDTDCMDSSDEKGCEGVTHVCDPNVKFGCKDSARCISKAWVCDGDSDCEDNSDEENCEALACRPPSHPCANNTSVCLSPDKLCDGKDDCGDGSDEGELCDQCSLNNGGCSHNCSVAPGEGIVCSCPLGMELGPDNHTCQIQSYCAKHLKCSQKCDQNKFSVKCSCYEGWVLEPDGESCRSLDPFKPFIIFSNRHEIRRIDLHKGDYSVLVPGLRNTIALDFHLSQSALYWTDVVEDKIYRGKLLDNGALTSFEVVIQYGLATPEGLAVDWIAGNIYWVESNLDQIEVAKLDGTLRTTLLAGDIEHPRAIALDPRDGILFWTDWDASLPRIEAASMSGAGRRTIHRETGSGGWPNGLTVDYLEKRILWIDARSDAIYSARYDGSGHMEVLRGHEFLSHPFAVTLYGGEVYWTDWRTNTLAKANKWTGHNVTVVQRTNTQPFDLQVYHPSRQPMAPNPCEANGGRGPCSHLCLINYNRTVSCACPHLMKLHNDNTTCYEFKKFLLYARQMEIRGVDLDAPYYNYIISFTVPDIDNVTVLDYDAREQRVYWSDVRTQAIKRAFINGTGVETVVSADLPNAHGLAVDWVSRNLFWTSYDTNKKQINVARLDGSFKNAVVQGLEQPHGLVVHPLRGKLYWTDGDNISMVNMDGSNRTLLFSGQKGPVGLAIDFPESKLYWISSGNHTINRCNLDGSELEVIDTMRSQLGKATALAIMGDKLWWADQVSEKMGTCNKADGSGSVVLRNSTTLVMHMKVYDESIQLEHEGTNPCSVNNGDCSQLCLPTSETTRSCMCTAGYSLRSGQQACEGVGSFLLYSVHEGIRGIPLDPNDKSDALVPVSGTSLAVGIDFHAENDTIYWVDMGLSTISRAKRDQTWREDVVTNGIGRVEGIAVDWIAGNIYWTDQGFDVIEVARLNGSFRYVVISQGLDKPRAITVHPEKGYLFWTEWGHYPRIERSRLDGTERVVLVNVSISWPNGISVDYQGGKLYWCDARMDKIERIDLETGENREVVLSSNNMDMFSVSVFEDFIYWSDRTHANGSIKRGCKDNATDSVPLRTGIGVQLKDIKVFNRDRQKGTNVCAVANGGCQQLCLYRGGGQRACACAHGMLAEDGASCREYAGYLLYSERTILKSIHLSDERNLNAPVQPFEDPEHMKNVIALAFDYRAGTSPGTPNRIFFSDIHFGNIQQINDDGSGRTTIVENVGSVEGLAYHRGWDTLYWTSYTTSTITRHTVDQTRPGAFERETVITMSGDDHPRAFVLDECQNLMFWTNWNELHPSIMRAALSGANVLTLIEKDIRTPNGLAIDHRAEKLYFSDATLDKIERCEYDGSHRYVILKSEPVHPFGLAVYGEHIFWTDWVRRAVQRANKYVGSDMKLLRVDIPQQPMGIIAVANDTNSCELSPCRINNGGCQDLCLLTHQGHVNCSCRGGRILQEDFTCRAMNSSCRAQDEFECANGECISFSLTCDGVSHCKDKSDEKPSYCNSRRCKKTFRQCNNGRCVSNMLWCNGVDDCGDGSDEIPCNKTACGVGEFRCRDGSCIGNSSRCNQFVDCEDASDEMNCSATDCSSYFRLGVKGVLFQPCERTSLCYAPSWVCDGANDCGDYSDERDCPGVKRPRCPLNYFACPSGRCIPMSWTCDKEDDCENGEDETHCNKFCSEAQFECQNHRCISKQWLCDGSDDCGDGSDEAAHCEGKTCGPSSFSCPGTHVCVPERWLCDGDKDCADGADESISAGCLYNSTCDDREFMCQNRLCIPKHFVCDHDRDCADGSDESPECEYPTCGPNEFRCANGRCLSSRQWECDGENDCHDHSDEAPKNPHCTSPEHKCNASSQFLCSSGRCVAEALLCNGQDDCGDGSDERGCHVNECLSRKLSGCSQDCEDLKIGFKCRCRPGFRLKDDGRTCADVDECSTTFPCSQLCINTHGSYKCLCVEGYAPRGGDPHSCKAVTDEEPFLIFANRYYLRKLNLDGSNYTLLKQGLNNAVALDFDYRGQMIYWTDVTTQGSMIRRMHLNGSNVQVLHRTGLSNPDGLAVDWVGGNLYWCDKGRDTIEVSKLNGAYRTVLVSSGLREPRALVVDVQNGYLYWTDWGDHSLIGRIGMDGSGRSIIVDTKITWPNGLTVDYVTERIYWADAREDYIEFASLDGSNRHVVLSQDIPHIFALTLFEDYVYWTDWETKSINRAHKTTGANKTLLISTLHRPMDLHVFHALRQPDVPNHPCKVNNGGCSNLCLLSPGGGHKCACPTNFYLGGDGRTCVSNCTASQFVCKNDKCIPFWWKCDTEDDCGDHSDEPPDCPEFKCRPGQFQCSTGICTNPAFICDGDNDCQDNSDEANCDIHVCLPSQFKCTNTNRCIPGIFRCNGQDNCGDGEDERDCPEVTCAPNQFQCSITKRCIPRVWVCDRDNDCVDGSDEPANCTQMTCGVDEFRCKDSGRCIPARWKCDGEDDCGDGSDEPKEECDERTCEPYQFRCKNNRCVPGRWQCDYDNDCGDNSDEESCTPRPCSESEFSCANGRCIAGRWKCDGDHDCADGSDEKDCTPRCDMDQFQCKSGHCIPLRWRCDADADCMDGSDEEACGTGVRTCPLDEFQCNNTLCKPLAWKCDGEDDCGDNSDENPEECTRFQCPPNRPFRCKNDRVCLWIGRQCDGTDNCGDGTDEEDCEPPTAQNPHCKDKKEFLCRNQRCLSSSLRCNMFDDCGDGSDEEDCSIDPKLTSCATNASMCGDEARCVRTEKAAYCACRPGFHTVPGQPGCQDINECLRFGTCSQLCNNTKGGHLCSCARNFMKTHNTCKAEGSEYQVLYIADDNEIRSLFPGHPHSAYEQAFQGDESVRIDAMDVHVKAGRVYWTNWHTGTISYRSLPPAAPPTTSNRHRRQIDRGVTHLNISGLKMPRGIAIDWVAGNVYWTDSGRDVIEVAQMKGENRKTLISGMIDEPHAIVVDPLRGTMYWSDWGNHPKIETAAMDGTLRETLVQDNIQWPTGLAVDYHNERLYWADAKLSVIGSIRLNGTDPIVAVDSKRGLSHPFSIDVFEDYIYGVTYINNRVFKIHKFGHSPLINLTGGLSHASDVVLYHQHKQPEVTNPCDRKKCEWLCLLSPSGPVCTCPNGKRLDNGTCVPVPSPTPPPDAPRPGTCTLQCFNGGSCFLNARRQPKCRCQPRYTGDKCELDQCWEYCHNGGTCAASPSGMPTCRCPTGFTGPRCTQQVCAGYCANNSTCTVNQGNQPQCRCLPGFLGDRCQYRQCSGFCENFGTCQMAADGSRQCRCTVYFEGTRCEVNKCSRCLQGACVVNKQTGDVTCNCTDGRVAPSCLTCIDHCSNGGSCTMNSKMMPECQCPPHMTGPRCEEQVVSQQQPGHMTSILIPLLLLLLLLLVAGVVFWYKRRVRGAKGFQHQRMTNGAMNVEIGNPTYKMYEGGEPDDVGGLLDADFALDPDKPTNFTNPVYATLYMGGHGSRHSLASTDEKRELLGRGPEDEIGDPLA | null | null | amyloid-beta clearance [GO:0097242]; amyloid-beta clearance by cellular catabolic process [GO:0150094]; amyloid-beta clearance by transcytosis [GO:0150093]; aorta morphogenesis [GO:0035909]; apoptotic cell clearance [GO:0043277]; astrocyte activation involved in immune response [GO:0002265]; cardiac septum development [GO:0003279]; cellular lipid catabolic process [GO:0044242]; cellular response to amyloid-beta [GO:1904646]; cerebral cortex development [GO:0021987]; chemoattraction of axon [GO:0061642]; cholesterol metabolic process [GO:0008203]; coronary vasculature development [GO:0060976]; enzyme-linked receptor protein signaling pathway [GO:0007167]; lysosomal transport [GO:0007041]; negative regulation of apoptotic process [GO:0043066]; negative regulation of cell-substrate adhesion [GO:0010812]; negative regulation of cytosolic calcium ion concentration [GO:0051481]; negative regulation of endopeptidase activity [GO:0010951]; negative regulation of focal adhesion assembly [GO:0051895]; negative regulation of gene expression [GO:0010629]; negative regulation of neuron apoptotic process [GO:0043524]; negative regulation of neuron projection development [GO:0010977]; negative regulation of platelet-derived growth factor receptor-beta signaling pathway [GO:2000587]; negative regulation of SMAD protein signal transduction [GO:0060392]; negative regulation of smooth muscle cell migration [GO:0014912]; negative regulation of transforming growth factor beta receptor signaling pathway [GO:0030512]; negative regulation of Wnt signaling pathway [GO:0030178]; phagocytosis [GO:0006909]; positive regulation of amyloid-beta clearance [GO:1900223]; positive regulation of axon extension [GO:0045773]; positive regulation of axon extension involved in regeneration [GO:0048691]; positive regulation of chemokine (C-X-C motif) ligand 2 production [GO:2000343]; positive regulation of cholesterol efflux [GO:0010875]; positive regulation of cholesterol import [GO:1904109]; positive regulation of cholesterol transport [GO:0032376]; positive regulation of collateral sprouting of injured axon [GO:0048694]; positive regulation of cytosolic calcium ion concentration [GO:0007204]; positive regulation of endocytosis [GO:0045807]; positive regulation of ERK1 and ERK2 cascade [GO:0070374]; positive regulation of insulin secretion involved in cellular response to glucose stimulus [GO:0035774]; positive regulation of lipid transport [GO:0032370]; positive regulation of lysosomal protein catabolic process [GO:1905167]; positive regulation of neuron projection development [GO:0010976]; positive regulation of phagocytosis [GO:0050766]; positive regulation of protein localization to plasma membrane [GO:1903078]; positive regulation of protein transport [GO:0051222]; positive regulation of Schwann cell migration [GO:1900149]; positive regulation of transcytosis [GO:1904300]; positive regulation of vascular associated smooth muscle cell migration [GO:1904754]; protein kinase C-activating G protein-coupled receptor signaling pathway [GO:0007205]; receptor internalization [GO:0031623]; receptor-mediated endocytosis [GO:0006898]; regulation of actin cytoskeleton organization [GO:0032956]; regulation of cholesterol transport [GO:0032374]; regulation of pulmonary blood vessel remodeling [GO:1905109]; transport across blood-brain barrier [GO:0150104] | apical part of cell [GO:0045177]; axonal growth cone [GO:0044295]; basolateral plasma membrane [GO:0016323]; clathrin-coated pit [GO:0005905]; clathrin-coated vesicle [GO:0030136]; dendrite [GO:0030425]; early endosome [GO:0005769]; endosome [GO:0005768]; external side of plasma membrane [GO:0009897]; Golgi apparatus [GO:0005794]; insulin-responsive compartment [GO:0032593]; low-density lipoprotein receptor complex [GO:0062136]; membrane [GO:0016020]; microtubule organizing center [GO:0005815]; neuronal cell body [GO:0043025]; nucleus [GO:0005634]; plasma membrane [GO:0005886]; receptor complex [GO:0043235] | alpha-2 macroglobulin receptor activity [GO:0016964]; apolipoprotein binding [GO:0034185]; calcium ion binding [GO:0005509]; cargo receptor activity [GO:0038024]; clathrin heavy chain binding [GO:0032050]; coreceptor activity [GO:0015026]; low-density lipoprotein particle receptor activity [GO:0005041]; protease binding [GO:0002020]; protein-containing complex binding [GO:0044877]; signaling receptor binding [GO:0005102] | PF12662;PF16472;PF00008;PF07645;PF14670;PF00057;PF00058; | 4.10.1220.10;2.10.25.10;4.10.400.10;2.120.10.30; | LDLR family | PTM: Cleaved into a 85 kDa membrane-spanning subunit (LRP-85) and a 515 kDa large extracellular domain (LRP-515) that remains non-covalently associated. Gamma-secretase-dependent cleavage of LRP-85 releases the intracellular domain from the membrane. {ECO:0000250|UniProtKB:Q07954}.; PTM: Phosphorylated on serine and threonine residues. {ECO:0000250|UniProtKB:Q07954}.; PTM: Phosphorylated on tyrosine residues upon stimulation with PDGF. Tyrosine phosphorylation promotes interaction with SHC1. {ECO:0000250|UniProtKB:Q07954}. | SUBCELLULAR LOCATION: [Low-density lipoprotein receptor-related protein 1 85 kDa subunit]: Cell membrane {ECO:0000250|UniProtKB:Q07954}; Single-pass type I membrane protein {ECO:0000250|UniProtKB:Q07954}. Membrane, coated pit {ECO:0000250|UniProtKB:Q07954}.; SUBCELLULAR LOCATION: [Low-density lipoprotein receptor-related protein 1 515 kDa subunit]: Cell membrane {ECO:0000250|UniProtKB:Q07954}; Peripheral membrane protein {ECO:0000250|UniProtKB:Q07954}; Extracellular side {ECO:0000250|UniProtKB:Q07954}. Membrane, coated pit {ECO:0000250|UniProtKB:Q07954}.; SUBCELLULAR LOCATION: Golgi outpost {ECO:0000269|PubMed:31522887}. Cytoplasm, cytoskeleton, microtubule organizing center {ECO:0000269|PubMed:31522887}. Note=Localizes to the postsynaptic Golgi apparatus region, also named Golgi outpost, which shapes dendrite morphology by functioning as sites of acentrosomal microtubule nucleation. {ECO:0000269|PubMed:31522887}.; SUBCELLULAR LOCATION: [Low-density lipoprotein receptor-related protein 1 intracellular domain]: Cytoplasm {ECO:0000250|UniProtKB:Q07954}. Nucleus {ECO:0000250|UniProtKB:Q07954}. Note=After cleavage, the intracellular domain (LRPICD) is detected both in the cytoplasm and in the nucleus. {ECO:0000250|UniProtKB:Q07954}. | null | null | null | null | null | FUNCTION: Endocytic receptor involved in endocytosis and in phagocytosis of apoptotic cells (By similarity). Required for early embryonic development (By similarity). Involved in cellular lipid homeostasis. Involved in the plasma clearance of chylomicron remnants and activated LRPAP1 (alpha 2-macroglobulin), as well as the local metabolism of complexes between plasminogen activators and their endogenous inhibitors. Acts as an LRPAP1 alpha-2-macroglobulin receptor. Acts as a TAU/MAPT receptor and controls the endocytosis of TAU/MAPT as well as its subsequent spread. May modulate cellular events, such as APP metabolism, kinase-dependent intracellular signaling, neuronal calcium signaling as well as neurotransmission (By similarity). {ECO:0000250|UniProtKB:Q07954, ECO:0000250|UniProtKB:Q91ZX7}. | Rattus norvegicus (Rat) |
G3V9D0 | PGLT1_RAT | MERLSGCRLRPWMLLLLLFPVQGRQKDSGSKWKVFIDQINRALENYEPCSSQNCSCYHGVIEEDLTPFRGGISRKMMAEVVRRRLGTHYQIIKHRLFREDDCMFPSRCSGVEHFILEVIRRLPDMEMVINVRDYPQVPKWMEPTIPVFSFSKTSEYHDIMYPAWTFWEGGPAVWPLYPTGLGRWDLFREDLLRSAAQWPWEKKNSTAYFRGSRTSPERDPLILLSRKNPKLVDAEYTKNQAWKSMKDTLGKPAAKDVHLIDHCKYKYLFNFRGVAASFRFKHLFLCGSLVFHVGDEWVEFFYPQLKPWVHYIPVKTDLSDVQELLQFVKANDDLAQEIAKRGSQFIINHLQMDDITCYWENLLTEYSKFLSYNVTRRKDYYQIIPRRLKTEL | 2.4.1.376; 2.4.2.63 | null | axial mesoderm development [GO:0048318]; circulatory system development [GO:0072359]; gastrulation [GO:0007369]; muscle tissue development [GO:0060537]; paraxial mesoderm development [GO:0048339]; positive regulation of Notch signaling pathway [GO:0045747]; protein O-linked glycosylation [GO:0006493]; protein O-linked glycosylation via serine [GO:0018242]; regulation of gastrulation [GO:0010470]; regulation of Notch signaling pathway [GO:0008593]; somitogenesis [GO:0001756] | endomembrane system [GO:0012505]; endoplasmic reticulum lumen [GO:0005788] | EGF-domain serine glucosyltransferase activity [GO:0140561]; EGF-domain serine xylosyltransferase activity [GO:0140562]; glucosyltransferase activity [GO:0046527]; UDP-glucosyltransferase activity [GO:0035251]; UDP-xylosyltransferase activity [GO:0035252] | PF05686; | null | Glycosyltransferase 90 family | null | SUBCELLULAR LOCATION: Endoplasmic reticulum lumen {ECO:0000269|PubMed:21949356}. | CATALYTIC ACTIVITY: Reaction=L-seryl-[EGF-like domain protein] + UDP-alpha-D-xylose = 3-O-(beta-D-xylosyl)-L-seryl-[EGF-like domain protein] + H(+) + UDP; Xref=Rhea:RHEA:62016, Rhea:RHEA-COMP:16010, Rhea:RHEA-COMP:16011, ChEBI:CHEBI:15378, ChEBI:CHEBI:29999, ChEBI:CHEBI:57632, ChEBI:CHEBI:58223, ChEBI:CHEBI:132085; EC=2.4.2.63; Evidence={ECO:0000250|UniProtKB:Q8NBL1}; CATALYTIC ACTIVITY: Reaction=L-seryl-[EGF-like domain protein] + UDP-alpha-D-glucose = 3-O-(beta-D-glucosyl)-L-seryl-[EGF-like domain protein] + H(+) + UDP; Xref=Rhea:RHEA:58116, Rhea:RHEA-COMP:14610, Rhea:RHEA-COMP:16010, ChEBI:CHEBI:15378, ChEBI:CHEBI:29999, ChEBI:CHEBI:58223, ChEBI:CHEBI:58885, ChEBI:CHEBI:140576; EC=2.4.1.376; Evidence={ECO:0000250|UniProtKB:Q8NBL1}; | null | PATHWAY: Protein modification; protein glycosylation. {ECO:0000250|UniProtKB:Q8BYB9}. | null | null | FUNCTION: Dual specificity glycosyltransferase that catalyzes the transfer of glucose and xylose from UDP-glucose and UDP-xylose, respectively, to a serine residue found in the consensus sequence of C-X-S-X-P-C. Specifically targets extracellular EGF repeats of protein such as CRB2, F7, F9 and NOTCH2 (By similarity). Acts as a positive regulator of Notch signaling by mediating O-glucosylation of Notch, leading to regulate muscle development (By similarity). Notch glucosylation does not affect Notch ligand binding (By similarity). Required during early development to promote gastrulation: acts by mediating O-glucosylation of CRB2, which is required for CRB2 localization to the cell membrane (By similarity). {ECO:0000250|UniProtKB:Q8BYB9, ECO:0000250|UniProtKB:Q8NBL1}. | Rattus norvegicus (Rat) |
G3V9H8 | RET_RAT | MAKARSGAAGLGLKLFLLLPLLGEAPLGLYFSRDAYWERLYVDQPAGTPLLYVHALRDAPGEVPSFRLGQYLYGVYRTRLHENDWIHIDSGTGLLYLNQSLDHSSWEQLSIRNGGFPLLTVFLQVFLGSTAQREGECHWPGCARVYFSFINDTFPNCSSFKARDLCTPETGVSFRIRENRPPGTFYQFRMLPVQFLCPNISVKYKLLEGDGLPFRCDPDCLEVSTRWALDRELQEKYVLEAECAVAGPGANKEKVAVSFPVTVYDEDDSPPTFSGGVGTASAVVEFKRKEGTVVATLQVFDADVVPASGELVRRYTSTLLSGDSWAQQTFRVEHTPNETLVQSNNNSVRATMHNYKLVLNRSLSISESRVLQLVVLVNDSDFQGPGSGVLFLHFNVSVLPVTLNLPMAYSFPVNRRARRYAQIGKVCVENCQEFSGVSIQYKLQPSSTNCSALGVVTSTEDTSGTLYVNDTEALRRPECTELQYTVVATDRQTRRQTQASLVVTVEGTYIAEEVGCPKSCAVNKRRPECEECGGLGSPTGRCEWRQGDGKGITRNFSTCSPSTRTCPDGHCDALESRDINICPQDCLRGPIVGGHERGERQGIKAGYGICNCFPDEKKCFCEPEDSQGPLCDELCRTVITAAVLFSFIISVLLSTFCIHRYHKHAHKPPIASAEMTFCRPAQGFPISYSSSGTRRPSLDSMENQVSVDSFKIPEDPKWEFPRKNLVLGKTLGEGEFGKVVKATAFRLKGRAGYTTVAVKMLKENASQSELRDLLSEFNLLKQVNHPHVIKLYGACSQDGPLLLIVEYAKYGSLRGFLRDSRKIGPAYVSSGGSRNSSSLDHPDERVLTMGDLISFAWQISRGMQYLAEMKLVHRDLAARNILVAEGRKMKISDFGLSRDVYEEDSYVKKSKGRIPVKWMAIESLFDHIYTTQSDVWSFGVLLWEIVTLGGNPYPGIPPERLFNLLKTGHRMERPDNCSEEMYRLMLQCWKQEPDKRPVFADISKDLEKMMVKSRDYLDLAASTPSDSLLYDDGLSEEETPLVDCNSAPLPRSLPSTWIENKLYGMSDPNWPGESPVPLTRADGTSTGFPRYANDSVYANWMVSPSAAKLMDTFDS | 2.7.10.1 | COFACTOR: Name=Ca(2+); Xref=ChEBI:CHEBI:29108; Evidence={ECO:0000250|UniProtKB:P07949}; | cellular response to retinoic acid [GO:0071300]; embryonic epithelial tube formation [GO:0001838]; enteric nervous system development [GO:0048484]; glial cell-derived neurotrophic factor receptor signaling pathway [GO:0035860]; homophilic cell adhesion via plasma membrane adhesion molecules [GO:0007156]; innervation [GO:0060384]; MAPK cascade [GO:0000165]; membrane protein proteolysis [GO:0033619]; nervous system development [GO:0007399]; neural crest cell migration [GO:0001755]; neuron cell-cell adhesion [GO:0007158]; neuron differentiation [GO:0030182]; neuron maturation [GO:0042551]; Peyer's patch morphogenesis [GO:0061146]; phosphorylation [GO:0016310]; positive regulation of cell adhesion mediated by integrin [GO:0033630]; positive regulation of cell migration [GO:0030335]; positive regulation of cell size [GO:0045793]; positive regulation of DNA-templated transcription [GO:0045893]; positive regulation of gene expression [GO:0010628]; positive regulation of MAPK cascade [GO:0043410]; positive regulation of metanephric glomerulus development [GO:0072300]; positive regulation of neuron maturation [GO:0014042]; positive regulation of neuron projection development [GO:0010976]; positive regulation of peptidyl-serine phosphorylation of STAT protein [GO:0033141]; positive regulation of phosphatidylinositol 3-kinase/protein kinase B signal transduction [GO:0051897]; regulation of axonogenesis [GO:0050770]; regulation of cell adhesion [GO:0030155]; response to pain [GO:0048265]; response to xenobiotic stimulus [GO:0009410]; retina development in camera-type eye [GO:0060041]; transmembrane receptor protein tyrosine kinase signaling pathway [GO:0007169]; ureter maturation [GO:0035799]; ureteric bud development [GO:0001657] | axon [GO:0030424]; dendrite [GO:0030425]; early endosome [GO:0005769]; endosome membrane [GO:0010008]; neuronal cell body [GO:0043025]; plasma membrane [GO:0005886]; plasma membrane protein complex [GO:0098797]; receptor complex [GO:0043235] | ATP binding [GO:0005524]; calcium ion binding [GO:0005509]; transmembrane receptor protein tyrosine kinase activity [GO:0004714] | PF00028;PF07714;PF17756;PF17812;PF17813; | 2.60.40.60;1.10.510.10; | Protein kinase superfamily, Tyr protein kinase family | PTM: Autophosphorylated on C-terminal tyrosine residues upon ligand stimulation. {ECO:0000250|UniProtKB:P07949}.; PTM: Proteolytically cleaved by caspase-3. The soluble RET kinase fragment is able to induce cell death. The extracellular cell-membrane anchored RET cadherin fragment accelerates cell adhesion in sympathetic neurons (By similarity). {ECO:0000250|UniProtKB:P07949}. | SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:P07949}; Single-pass type I membrane protein {ECO:0000250|UniProtKB:P07949}. Endosome membrane {ECO:0000250|UniProtKB:P07949}; Single-pass type I membrane protein {ECO:0000250|UniProtKB:P07949}. Note=Predominantly located on the plasma membrane. In the presence of SORL1 and GFRA1, directed to endosomes. {ECO:0000250|UniProtKB:P07949}. | CATALYTIC ACTIVITY: Reaction=ATP + L-tyrosyl-[protein] = ADP + H(+) + O-phospho-L-tyrosyl-[protein]; Xref=Rhea:RHEA:10596, Rhea:RHEA-COMP:10136, Rhea:RHEA-COMP:10137, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:46858, ChEBI:CHEBI:82620, ChEBI:CHEBI:456216; EC=2.7.10.1; Evidence={ECO:0000255|PROSITE-ProRule:PRU10028}; | null | null | null | null | FUNCTION: Receptor tyrosine-protein kinase involved in numerous cellular mechanisms including cell proliferation, neuronal navigation, cell migration, and cell differentiation in response to glia cell line-derived growth family factors (GDNF, NRTN, ARTN, PSPN and GDF15) (By similarity). In contrast to most receptor tyrosine kinases, RET requires not only its cognate ligands but also coreceptors, for activation (By similarity). GDNF ligands (GDNF, NRTN, ARTN, PSPN and GDF15) first bind their corresponding GDNFR coreceptors (GFRA1, GFRA2, GFRA3, GFRA4 and GFRAL, respectively), triggering RET autophosphorylation and activation, leading to activation of downstream signaling pathways, including the MAPK- and AKT-signaling pathways (PubMed:23333276). Acts as a dependence receptor via the GDNF-GFRA1 signaling: in the presence of the ligand GDNF in somatotrophs within pituitary, promotes survival and down regulates growth hormone (GH) production, but triggers apoptosis in absence of GDNF (By similarity). Required for the molecular mechanisms orchestration during intestine organogenesis via the ARTN-GFRA3 signaling: involved in the development of enteric nervous system and renal organogenesis during embryonic life, and promotes the formation of Peyer's patch-like structures, a major component of the gut-associated lymphoid tissue (By similarity). Mediates, through interaction with GDF15-receptor GFRAL, GDF15-induced cell-signaling in the brainstem which triggers an aversive response, characterized by nausea, vomitting, and/or loss of appetite in response to various stresses (By similarity). Modulates cell adhesion via its cleavage by caspase in sympathetic neurons and mediates cell migration in an integrin (e.g. ITGB1 and ITGB3)-dependent manner (By similarity). Also active in the absence of ligand, triggering apoptosis through a mechanism that requires receptor intracellular caspase cleavage (By similarity). Triggers the differentiation of rapidly adapting (RA) mechanoreceptors (By similarity). Involved in the development of the neural crest (By similarity). Regulates nociceptor survival and size (By similarity). Phosphorylates PTK2/FAK1 (By similarity). {ECO:0000250|UniProtKB:P07949, ECO:0000250|UniProtKB:P35546, ECO:0000269|PubMed:23333276}. | Rattus norvegicus (Rat) |
G3V9M2 | JIP2_RAT | MADRAEMFSLSTFHSLSPPGCRPPQDISLEEFDDEDLSEITDDCGLGLSYDSDHCEKDSLSLGRSEQPHPICSFQDDFQEFEMIDDNEEEEDEEEEEEEEEEEDGDGDGRAGGGSGSQELSGESLIPSPSIEESHKLRPTTLHLTTLGAQDSLNNNSNGGFTSAPPSSWQETVLRSPVQEPLKELPAPLLPAEEEHHEVQSLARPGCDCEGNQPPEPPASGGASPSSDPGIEADLRSHSSGGHEGRRSSQELSSPGSDSEEAGGARLGRMISSISETELELSSDSGSSSGRSSHLTNSIEEASSPASEPEPEPEPEPLHEPPRRPAFLPVGQDDTNSEYESGSESEPDLSEDADSPWLLSNLVSRMISEGSSPIRCPGQCLSPPAPRPPEEAASQANPVPQDCPDPEAVAGPHVELVDMDTLCGPPPPAPAAPRLGPAQSGPCLFLSNPTRDTITPLWAPPGRTARPGRSCSAACSEEEEEDEEEDEEDEEDAEDSVIPPGSRTTGSTAPLDASLVYDAVKYTLVVDEHTQLELVSLRRCAGLDNDSEEDSSCEASEEEAGATLLGSDQVPEDASPDSPDLTFSKKFLNVFVNSTSRSSSTESFGLFSCVVNGEEREQTHRAVFRFIPRHPDELELDVDDPVLVEAEEDDFWFRGFNMRTGERGVFPAFYAHAVPGPAKDLLGSKRSPCWVDRFDVQFLGSVEVPCHQGNGILCAAMQKIATARKLTVHLRPPASCDLEISLRGVKLSLSGGGPEFQRCSHFFQMKNISFCGCHPRNSCYFGFITKHPLLSRFACHVFVSQESMRPVARSVGRAFLEYYQEHLAFACPTEDIYLE | null | null | behavioral fear response [GO:0001662]; dendrite morphogenesis [GO:0048813]; excitatory postsynaptic potential [GO:0060079]; JNK cascade [GO:0007254]; mating behavior [GO:0007617]; negative regulation of apoptotic signaling pathway [GO:2001234]; nonassociative learning [GO:0046958]; positive regulation of stress-activated MAPK cascade [GO:0032874]; regulation of JNK cascade [GO:0046328]; regulation of synaptic transmission, glutamatergic [GO:0051966]; social behavior [GO:0035176] | cytoplasm [GO:0005737]; neuronal cell body [GO:0043025]; postsynaptic density [GO:0014069]; protein-containing complex [GO:0032991] | JUN kinase binding [GO:0008432]; kinesin binding [GO:0019894]; MAP-kinase scaffold activity [GO:0005078]; protein kinase binding [GO:0019901]; protein-containing complex binding [GO:0044877] | PF00640;PF14604; | 2.30.29.30;2.30.30.40; | JIP scaffold family | null | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q13387}. Note=Accumulates in cell surface projections. {ECO:0000250|UniProtKB:Q13387}. | null | null | null | null | null | FUNCTION: The JNK-interacting protein (JIP) group of scaffold proteins selectively mediates JNK signaling by aggregating specific components of the MAPK cascade to form a functional JNK signaling module. JIP2 inhibits IL1 beta-induced apoptosis in insulin-secreting cells. {ECO:0000250}. | Rattus norvegicus (Rat) |
G3V9R8 | HNRPC_RAT | MASNVTNKTDPRSMNSRVFIGNLNTLVVKKSDVEAIFSKYGKIVGCSVHKGFAFVQYVNERNARAAVAGEDGRMIAGQVLDINLAAEPKVNRGKAGVKRSAAEMYGSSFDLDYDFQRDYYDRMYSYPARVPPPPPIARAVVPSKRQRVSGNTSRRGKSGFNSKSGQRGSSSKSVKGDDLQAIKKELTQIKQKVDSLLESLEKIEKEQSKQADLSFSSPVEMKNEKSEEEQSSASVKKDETNVKMESEAGADDSAEEGDLLDDDDNEDRGDDQLELKDDEKEPEEGEDDRDSANGEDDS | null | null | 3'-UTR-mediated mRNA stabilization [GO:0070935]; mRNA splicing, via spliceosome [GO:0000398]; negative regulation of mRNA modification [GO:0090367]; negative regulation of telomere maintenance via telomerase [GO:0032211] | actin cytoskeleton [GO:0015629]; catalytic step 2 spliceosome [GO:0071013]; cytosol [GO:0005829]; nucleoplasmic periphery of the nuclear pore complex [GO:1990826]; nucleus [GO:0005634]; pronucleus [GO:0045120]; protein-containing complex [GO:0032991]; spliceosomal complex [GO:0005681]; telomerase holoenzyme complex [GO:0005697] | deaminase binding [GO:1990827]; enzyme inhibitor activity [GO:0004857]; identical protein binding [GO:0042802]; mRNA 3'-UTR binding [GO:0003730]; mRNA binding [GO:0003729]; N6-methyladenosine-containing RNA reader activity [GO:1990247]; poly(U) RNA binding [GO:0008266]; protein domain specific binding [GO:0019904]; ribonucleoprotein complex binding [GO:0043021]; RNA binding [GO:0003723]; telomerase RNA binding [GO:0070034] | PF00076; | 3.30.70.330; | RRM HNRPC family, RALY subfamily | PTM: Phosphorylated on Ser-253 and Ser-291 in resting cells. {ECO:0000250|UniProtKB:P07910}.; PTM: Sumoylated. Sumoylation reduces affinity for mRNA. {ECO:0000250|UniProtKB:P07910}.; PTM: Ubiquitinated and degraded after nucleo-cytoplasmic transport by YWHAE. {ECO:0000250|UniProtKB:P07910}. | SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:P07910}. Note=Component of ribonucleosomes. {ECO:0000250|UniProtKB:P07910}. | null | null | null | null | null | FUNCTION: Binds pre-mRNA and nucleates the assembly of 40S hnRNP particles. Interacts with poly-U tracts in the 3'-UTR or 5'-UTR of mRNA and modulates the stability and the level of translation of bound mRNA molecules. Single HNRNPC tetramers bind 230-240 nucleotides. Trimers of HNRNPC tetramers bind 700 nucleotides. May play a role in the early steps of spliceosome assembly and pre-mRNA splicing. N6-methyladenosine (m6A) has been shown to alter the local structure in mRNAs and long non-coding RNAs (lncRNAs) via a mechanism named 'm(6)A-switch', facilitating binding of HNRNPC, leading to regulation of mRNA splicing. {ECO:0000250|UniProtKB:P07910}. | Rattus norvegicus (Rat) |
G3V9T7 | GET3_RAT | MAAGVAGWGVEAEEFEDAPDVEPLEPTLSNIIEQRSLKWIFVGGKGGVGKTTCSCSLAVQLSKGRESVLIISTDPAHNISDAFDQKFSKVPTKVKGYDNLFAMEIDPSLGVAELPDEFFEEDNMLSMGKKMMQEAMSAFPGIDEAMSYAEVMRLVKGMNFSVVVFDTAPTGHTLRLLNFPTIVERGLGRLMQIKNQISPFISQMCNMLGLGDMNADQLASKLEETLPVIRSVSEQFKDPEQTTFICVCIAEFLSLYETERLIQELAKCKIDTHNIIVNQLVFPDPEKPCKMCEARHKIQAKYLDQMEDLYEDFHIVKLPLLPHEVRGADKVNTFSALLLEPYKPPSTQ | 3.6.-.- | null | post-translational protein targeting to endoplasmic reticulum membrane [GO:0006620]; tail-anchored membrane protein insertion into ER membrane [GO:0071816] | endoplasmic reticulum membrane [GO:0005789]; GET complex [GO:0043529]; nucleolus [GO:0005730]; nucleoplasm [GO:0005654] | ATP binding [GO:0005524]; ATP hydrolysis activity [GO:0016887]; membrane insertase activity [GO:0032977]; metal ion binding [GO:0046872] | PF02374; | 3.40.50.300; | ArsA ATPase family | null | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_03112}. Endoplasmic reticulum {ECO:0000255|HAMAP-Rule:MF_03112}. Nucleus, nucleolus {ECO:0000255|HAMAP-Rule:MF_03112}. | null | null | null | null | null | FUNCTION: ATPase required for the post-translational delivery of tail-anchored (TA) proteins to the endoplasmic reticulum. Recognizes and selectively binds the transmembrane domain of TA proteins in the cytosol. This complex then targets to the endoplasmic reticulum by membrane-bound receptors GET1/WRB and CAMLG/GET2, where the tail-anchored protein is released for insertion. This process is regulated by ATP binding and hydrolysis. ATP binding drives the homodimer towards the closed dimer state, facilitating recognition of newly synthesized TA membrane proteins. ATP hydrolysis is required for insertion. Subsequently, the homodimer reverts towards the open dimer state, lowering its affinity for the GET1-CAMLG receptor, and returning it to the cytosol to initiate a new round of targeting. {ECO:0000255|HAMAP-Rule:MF_03112, ECO:0000269|PubMed:23041287, ECO:0000269|PubMed:27226539}. | Rattus norvegicus (Rat) |
G3X745 | GPC1_BOVIN | MELRARGWWLLYAAAVLVACARGDPASKSRSCGEVRQIYGAKGFSLSDVPQAEISGEHLRICPQGYTCCTSEMEENLANRSRAELETALLEGTRALQATLAAQQRGFDDHFQRLLNDSERALQEAFPGAFGELYTQNAKAFRDLYAELRLYYGGANLHLQETLAEFWARLLERLFRQLHPQLLLPDDYLDCLGKQAEPLRPFGEAPRELRLRATRAFVAARTFVQGLGVAGDVVRKVAKVPLSPECSRAVMKLVYCAHCLGVPGARPCPDYCRNVLKGCLANQADLDAEWRNLLDSMVLITDKFWGPSGAESVVGGVHYWLAEAINALQDNSDTLTAKVIQGCGNPKVNPQGPGTEEKWPRGKLALQERPPAGTLQKLVSEAKAQLRDAQDFWISLPGTLCSEKLAMSSASDERCWNGMAKGRYLPEVMGDGLANQINNPEVEVDITKPDMTIRQQIMQLKIMTNRLRGAYNGNDLDFQDASDDGSGSGSGEGCPDEMCGRKVGRKSASSRTPLTHALPGLSEREGQQTSAAAPTPPQASPLLLLGLALALPAVAPRGR | null | null | cell migration [GO:0016477]; heparan sulfate proteoglycan catabolic process [GO:0030200]; negative regulation of fibroblast growth factor receptor signaling pathway [GO:0040037]; positive regulation of skeletal muscle cell differentiation [GO:2001016]; regulation of protein localization to membrane [GO:1905475] | cell surface [GO:0009986]; collagen-containing extracellular matrix [GO:0062023]; endosome [GO:0005768]; extracellular matrix [GO:0031012]; extracellular region [GO:0005576]; membrane raft [GO:0045121]; plasma membrane [GO:0005886]; side of membrane [GO:0098552]; synapse [GO:0045202] | copper ion binding [GO:0005507]; fibroblast growth factor binding [GO:0017134]; laminin binding [GO:0043236] | PF01153; | null | Glypican family | PTM: S-nitrosylated in a Cu(2+)-dependent manner. Nitric acid (NO) is released from the nitrosylated cysteines by ascorbate or by some other reducing agent, in a Cu(2+) or Zn(2+) dependent manner. This free nitric oxide is then capable of cleaving the heparan sulfate side chains (By similarity). {ECO:0000250}.; PTM: N- and O-glycosylated (By similarity). N-glycosylation is mainly of the complex type containing sialic acid. O-glycosylated with heparan sulfate. The heparan sulfate chains can be cleaved either by the action of heparanase or, degraded by a deaminative process that uses nitric oxide (NO) released from the S-nitrosylated cysteines. This process is triggered by ascorbate, or by some other reducing agent, in a Cu(2+)- or Zn(2+) dependent manner. Cu(2+) ions are provided by ceruloproteins such as APP, PRNP or CP which associate with GCP1 in intracellular compartments or lipid rafts (By similarity). {ECO:0000250}.; PTM: Shed from the cell surface probably by further cleavage. {ECO:0000250}. | SUBCELLULAR LOCATION: Cell membrane {ECO:0000250}; Lipid-anchor, GPI-anchor {ECO:0000250}; Extracellular side {ECO:0000250}. Endosome {ECO:0000250}. Note=S-nitrosylated form recycled in endosomes. Localizes to CAV1-containing vesicles close to the cell surface. Cleavage of heparan sulfate side chains takes place mainly in late endosomes. Associates with both forms of PRNP in lipid rafts. Colocalizes with APP in perinuclear compartments and with CP in intracellular compartments (By similarity). {ECO:0000250}.; SUBCELLULAR LOCATION: [Secreted glypican-1]: Secreted, extracellular space {ECO:0000250}. | null | null | null | null | null | FUNCTION: Cell surface proteoglycan that bears heparan sulfate. Binds, via the heparan sulfate side chains, alpha-4 (V) collagen and participates in Schwann cell myelination (By similarity). May act as a catalyst in increasing the rate of conversion of prion protein PRPN (C) to PRNP (Sc) via associating (via the heparan sulfate side chains) with both forms of PRPN, targeting them to lipid rafts and facilitating their interaction. Required for proper skeletal muscle differentiation by sequestering FGF2 in lipid rafts preventing its binding to receptors (FGFRs) and inhibiting the FGF-mediated signaling (By similarity). {ECO:0000250}. | Bos taurus (Bovine) |
G3X8Y1 | TRI55_MOUSE | MSTSLNYKSFSKEQQTMDNLEKQLICPICLEMFTKPVVILPCQHNLCRKCASDIFQASNPYLPTRGGTTVASGGRFRCPSCRHEVVLDRHGVYGLQRNLLVENIIDIYKQESTRPEKKLDQPMCEEHEEERINIYCLNCEVPTCSLCKVFGAHKDCQVAPLTHVFQRQKSELSDGIAVLVGSNDRVQGVISQLEDTCKTIEECCRKQKQDLCEKFDHLYGILEERKTEMTQAITRTQEEKLEHVRTLIRKYSDHLENVSKLVESGIQFMDEPEMAVFLQNAKTLLQKIVEASKAFQMEKLEQGYEIMSNFTVNLNREEKIIREIDFSREEEEEEDAGEIDEEGEGEDAVEVEEAENVQIASSGEEESLEKAAEPSQLPAELQVAPEPLPASSPEPFSSMPPAADVLVTQGEVVPIGSQQTTQSETSGPSAAETADPLFYPSWYKGQSRKTSSNPPCTHGSEGLGQIGPLGIEDSSVQSAEVAEAATNEQAAVSGKESSSTAATSQIGFEAPSPQGQSAALGSGGGADPEPARHVFSFSWLNSLNE | 2.3.2.27 | null | diapedesis [GO:0050904]; leukocyte migration involved in inflammatory response [GO:0002523]; macrophage migration [GO:1905517]; positive regulation of non-canonical NF-kappaB signal transduction [GO:1901224]; protein K48-linked ubiquitination [GO:0070936]; protein ubiquitination [GO:0016567] | cytoplasm [GO:0005737]; nucleus [GO:0005634] | identical protein binding [GO:0042802]; protein-macromolecule adaptor activity [GO:0030674]; ubiquitin protein ligase activity [GO:0061630]; zinc ion binding [GO:0008270] | PF00643;PF13445; | 1.20.5.170;3.30.160.60;3.30.40.10; | null | PTM: Targeted for degradation through the proteasomal and lysosomal pathways in the presence of SUMO3. {ECO:0000250|UniProtKB:Q9BYV6}. | SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:29435413}. Cytoplasm {ECO:0000269|PubMed:29435413}. Note=TLR4 signaling pathway promotes nuclear translocation. {ECO:0000269|PubMed:29435413}. | CATALYTIC ACTIVITY: Reaction=S-ubiquitinyl-[E2 ubiquitin-conjugating enzyme]-L-cysteine + [acceptor protein]-L-lysine = [E2 ubiquitin-conjugating enzyme]-L-cysteine + N(6)-ubiquitinyl-[acceptor protein]-L-lysine.; EC=2.3.2.27; Evidence={ECO:0000250|UniProtKB:Q9BYV6}; | null | null | null | null | FUNCTION: E3 ubiquitin ligase that plays an important role in regulating cardiac development and contractility, muscle growth, metabolism, and fiber-type differentiation. Acts as a critical factor that regulates cardiomyocyte size during development in concert with TRIM63 by regulating E2F1-mediated gene expression (PubMed:23512667). Plays a role in apoptosis induction in cardiomyocytes by promoting ubiquitination of the DUSP1 phosphatase (PubMed:32463795). Promotes non-canonical NF-kappa-B signaling and B-cell-mediated immune responses by mediating NFKB2 'Lys-48'-linked ubiquitination and processing. In turn, NFKB2 is further processed by valosin-containing protein/VCP, an ATPase that mediates ubiquitin-dependent protein degradation by the proteasome (PubMed:37816088). May play a role in preventing macrophages from producing inflammatory factors and migrating by downregulating the level of nuclear NF-kappa-B subunit RELA (PubMed:29435413). Modifies also PPARG via polyubiquitination and accelerates PPARG proteasomal degradation to inhibit its activity (By similarity). {ECO:0000250|UniProtKB:Q9BYV6, ECO:0000269|PubMed:23512667, ECO:0000269|PubMed:29435413, ECO:0000269|PubMed:32463795, ECO:0000269|PubMed:37816088}. | Mus musculus (Mouse) |
G3X912 | SPRTN_MOUSE | MDEDLVVALRLQEEWDVQMARRAAAAREPVSLVDASWELVDPTPDLQALFLQFNDRFFWGQLEAVEVKWSVRMTLCAGICTYEGRGGMCSIRLSEPLLKLRPRKDLVETLLHEMIHAYLFVTNNDKDREGHGPEFCKHMHRINQLTGANITVYHTFHDEVDEYRRHWWRCNGPCQHRQPYYGYVKRATNRAPSVHDYWWADHQKTCGGTYIKIKEPENYSKKGRGKTKADKQPASAVENKDKLCRGEAQLLIPFSGKGYVLGDASTCPSAGKLNTSYMVNEAKGLSSQDHSVSGLRLNSNAEVKCEQNCLPKKPHLVSPLPTASHQSVLSSYFPRVSVANQKAFRNVNGSPVKNGTTGDGTKRPASGGSQRKVPPSRASLRNTSKVTAPASATVTSAAGTSATISREESGSEDQFLNKRPRLEDRTALDTIKEQTQSGGDLRSSSQPTAASAPQSLSSQRRLVNCPVCQGVVVESQINEHLDRCLEGNKTNLRPRRV | 3.4.24.- | COFACTOR: Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000250|UniProtKB:Q9H040}; | DNA damage response [GO:0006974]; positive regulation of protein ubiquitination [GO:0031398]; protein autoprocessing [GO:0016540]; protein-DNA covalent cross-linking repair [GO:0106300]; proteolysis [GO:0006508]; response to UV [GO:0009411]; translesion synthesis [GO:0019985] | chromatin [GO:0000785]; nuclear speck [GO:0016607]; nucleus [GO:0005634] | double-stranded DNA binding [GO:0003690]; K63-linked polyubiquitin modification-dependent protein binding [GO:0070530]; metal ion binding [GO:0046872]; metalloendopeptidase activity [GO:0004222]; polyubiquitin modification-dependent protein binding [GO:0031593]; single-stranded DNA binding [GO:0003697]; ubiquitin binding [GO:0043130] | PF10263; | 3.30.160.60; | Spartan family | PTM: Autocatalytically cleaved in response to double-stranded DNA-binding: autocatalytic cleavage takes place in trans and leads to inactivation. {ECO:0000250|UniProtKB:Q9H040}.; PTM: Monoubiquitinated; monoubiquitination promotes exclusion from chromatin. Deubiquitinated by VCPIP1: deubiquitination is required for subsequent acetylation and recruitment to chromatin and DNA damage sites. {ECO:0000250|UniProtKB:Q9H040}.; PTM: Acetylated following deubiquitination by VCPIP1, leading to recruitment to chromatin and DNA damage sites. {ECO:0000250|UniProtKB:Q9H040}.; PTM: Phosphorylation by CHEK1 promotes recruitment to chromatin. {ECO:0000250|UniProtKB:Q9H040}. | SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q9H040}. Chromosome {ECO:0000250|UniProtKB:Q9H040}. Note=Localizes to sites of UV damage via the PIP-box. Recruited to stalled replication forks at sites of replication stress following deubiquitination. CHEK1 stimulates recruitment to chromatin. {ECO:0000250|UniProtKB:Q9H040}. | null | null | null | null | null | FUNCTION: DNA-dependent metalloendopeptidase that mediates the proteolytic cleavage of covalent DNA-protein cross-links (DPCs) during DNA synthesis, thereby playing a key role in maintaining genomic integrity (PubMed:27871365, PubMed:28199696). DPCs are highly toxic DNA lesions that interfere with essential chromatin transactions, such as replication and transcription, and which are induced by reactive agents, such as UV light or formaldehyde (PubMed:27871365, PubMed:28199696). Associates with the DNA replication machinery and specifically removes DPCs during DNA synthesis (By similarity). Catalyzes proteolytic cleavage of the HMCES DNA-protein cross-link following unfolding by the BRIP1/FANCJ helicase (By similarity). Acts as a pleiotropic protease for DNA-binding proteins cross-linked with DNA, such as TOP1, TOP2A, histones H3 and H4 (By similarity). Mediates degradation of DPCs that are not ubiquitinated, while it is not able to degrade ubiquitinated DPCs. SPRTN activation requires polymerase collision with DPCs followed by helicase bypass of DPCs (By similarity). Involved in recruitment of VCP/p97 to sites of DNA damage. Also acts as an activator of CHEK1 during normal DNA replication by mediating proteolytic cleavage of CHEK1, thereby promoting CHEK1 removal from chromatin and subsequent activation. Does not activate CHEK1 in response to DNA damage. May also act as a 'reader' of ubiquitinated PCNA: recruited to sites of UV damage and interacts with ubiquitinated PCNA and RAD18, the E3 ubiquitin ligase that monoubiquitinates PCNA. Facilitates chromatin association of RAD18 and is required for efficient PCNA monoubiquitination, promoting a feed-forward loop to enhance PCNA ubiquitination and translesion DNA synthesis (By similarity). {ECO:0000250|UniProtKB:A0A1L8G2K9, ECO:0000250|UniProtKB:Q9H040, ECO:0000269|PubMed:27871365, ECO:0000269|PubMed:28199696}. | Mus musculus (Mouse) |
G3X939 | SL9A3_MOUSE | MWHRALGPGWKLLLALALTSLQGARGAEEEPSSDGSFQVVTFKWHHVQDPYIIALWILVASLAKIVFHLSHKVTSIVPESALLIVLGLVLGGIVWAADHIASFTLTPTLFFFYLLPPIVLDAGYFMPNRLFFGNLGTILLYAVIGTIWNAATTGLSLYGVFLSGLMGELKIGLLDFLLFGSLIAAVDPVAVLAVFEEVHVNEVLFIIVFGESLLNDAVTVVLYNVFESFVTLGGDAVTGVDCVKGIVSFFVVSLGGTLVGVIFAFLLSLVTRFTKHVRIIEPGFVFVISYLSYLTSEMLSLSSILAITFCGICCQKYVKANISEQSATTVRYTMKMLASGAETIIFMFLGISAVNPDIWTWNTAFVLLTLVFISVYRAIGVVLQTWILNRYRMVQLETIDQVVMSYGGLRGAVAYALVVLLDEKKVKEKNLFVSTTLIVVFFTVIFQGLTIKPLVQWLKVKRSEHREPKLNEKLHGRAFDHILSAIEDISGQIGHNYLRDKWSNFDRKFLSKVLMRRSAQKSRDRILNVFHELNLKDAISYVAEGERRGSLAFIRSPSTDNMVNVDFNTPRPSTVEASVSYFLRENVSAVCLDMQSLEQRRRSIRDTEDMVTHHTLQQYLYKPRQEYKHLYSRHELTPNEDEKQDKEIFHRTMRKRLESFKSAKLGINQNKKAAKLYKRERAQKRRNSSIPNGKLPMENLAHNYTIKEKDLELSEHEEATNYEEISGGIEFLASVTQDVASDSGAGIDNPVFSPDEDLDPSILSRVPPWLSPGETVVPSQRARVQIPNSPSNFRRLTPFRLSNKSVDSFLQADGHEEQLQPAAPESTHM | null | null | potassium ion transmembrane transport [GO:0071805]; receptor-mediated endocytosis [GO:0006898]; regulation of intracellular pH [GO:0051453]; regulation of pH [GO:0006885]; regulation of sodium ion transport [GO:0002028]; sodium ion import across plasma membrane [GO:0098719]; sodium ion transport [GO:0006814] | apical plasma membrane [GO:0016324]; brush border [GO:0005903]; brush border membrane [GO:0031526]; early endosome membrane [GO:0031901]; plasma membrane [GO:0005886]; recycling endosome membrane [GO:0055038]; vesicle [GO:0031982] | identical protein binding [GO:0042802]; PDZ domain binding [GO:0030165]; phosphatidylinositol binding [GO:0035091]; potassium:proton antiporter activity [GO:0015386]; sodium:proton antiporter activity [GO:0015385] | PF00999; | 6.10.140.1330; | Monovalent cation:proton antiporter 1 (CPA1) transporter (TC 2.A.36) family | PTM: Phosphorylated by PKA, which inhibits activity. Phosphorylation at Ser-659 by SGK1 is associated with increased abundance at the cell membrane. Phosphorylation at Ser-714 by CSNK2A1 regulates SLC9A3 activity through the formation of multiple signaling complexes (By similarity). {ECO:0000250|UniProtKB:P26432, ECO:0000250|UniProtKB:P26433}. | SUBCELLULAR LOCATION: Apical cell membrane {ECO:0000250|UniProtKB:P48764}; Multi-pass membrane protein {ECO:0000250|UniProtKB:P48764}. Cell membrane {ECO:0000250|UniProtKB:P48764}; Multi-pass membrane protein {ECO:0000250|UniProtKB:P48764}. Recycling endosome membrane {ECO:0000250|UniProtKB:P48764}; Multi-pass membrane protein {ECO:0000250|UniProtKB:P48764}. Early endosome membrane {ECO:0000250|UniProtKB:P48764}; Multi-pass membrane protein {ECO:0000250|UniProtKB:P48764}. Note=In intestinal epithelial cells, localizes to the ileal brush border. Phosphorylation at Ser-663 by SGK1 is associated with increased abundance at the cell membrane. Angiotensin-2 enhances apical expression (By similarity). {ECO:0000250|UniProtKB:Q28362}. | CATALYTIC ACTIVITY: Reaction=H(+)(out) + Na(+)(in) = H(+)(in) + Na(+)(out); Xref=Rhea:RHEA:29419, ChEBI:CHEBI:15378, ChEBI:CHEBI:29101; Evidence={ECO:0000250|UniProtKB:P48764}; | null | null | null | null | FUNCTION: Plasma membrane Na(+)/H(+) antiporter. Exchanges intracellular H(+) ions for extracellular Na(+) in 1:1 stoichiometry, playing a key role in salt and fluid absorption and pH homeostasis (By similarity). Major apical Na(+)/H(+) exchanger in kidney and intestine playing an important role in renal and intestine Na(+) absorption and blood pressure regulation (PubMed:9662405). {ECO:0000250|UniProtKB:P48764, ECO:0000269|PubMed:9662405}. | Mus musculus (Mouse) |
G3X943 | S39A2_MOUSE | MEVLLGVKIGCLLALLVLTLGCGLTPIYVKWFQMDAATGHHHRVLSLLGCTSAGVFLGAGLMHMTAEALEGIESEIQKFVEQNSTGSKGNSSRDAASSYVEYPYGELVISLGFFFVFLLESLALQCCHGAAGGSTVQEEEWGGTHAFGFHKHPAVPSPSRGPLRALVLLLSLSFHSVFEGLAVGLQATVAATIQLCVAVLAHKGLVVFSVGLRLGKIGTGPRWATFCILSLALMSPVGLALGLTVAGGASGQTQGLAQAVLEGIAAGTFLYVTFLEILPRELACPEAPLAKYSCVAAGFAFMALIALWA | null | null | cadmium ion transmembrane transport [GO:0070574]; keratinocyte differentiation [GO:0030216]; zinc ion transmembrane transport [GO:0071577]; zinc ion transport [GO:0006829] | cytoplasmic ribonucleoprotein granule [GO:0036464]; cytoplasmic vesicle [GO:0031410]; plasma membrane [GO:0005886] | metal ion binding [GO:0046872]; zinc ion transmembrane transporter activity [GO:0005385] | PF02535; | null | ZIP transporter (TC 2.A.5) family | null | SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:Q9NP94}; Multi-pass membrane protein {ECO:0000255}. | CATALYTIC ACTIVITY: Reaction=Zn(2+)(in) = Zn(2+)(out); Xref=Rhea:RHEA:29351, ChEBI:CHEBI:29105; Evidence={ECO:0000269|PubMed:14525987}; PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:29353; Evidence={ECO:0000305|PubMed:14525987}; CATALYTIC ACTIVITY: Reaction=Cd(2+)(in) = Cd(2+)(out); Xref=Rhea:RHEA:28707, ChEBI:CHEBI:48775; Evidence={ECO:0000250|UniProtKB:Q9NP94}; | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=1.6 uM for Zn(2+) {ECO:0000269|PubMed:14525987}; | null | null | null | FUNCTION: Transporter for the divalent cation Zn(2+). Mediates the influx of Zn(2+) into cells from extracellular space (PubMed:14525987). The Zn(2+) uniporter activity is independent of H(+)-driving force, but is modulated by extracellular pH and membrane potential. Transports also other divalent cations Zn(2+), Cd2(+), Cu2(+), Co2(+) in the order of decreasing affinity, respectively (By similarity). In the skin, aids in the differentiation of keratinocytes in the epidermis (PubMed:24936057). {ECO:0000250|UniProtKB:Q9NP94, ECO:0000269|PubMed:14525987, ECO:0000269|PubMed:24936057}. | Mus musculus (Mouse) |
G3X982 | AOXC_MOUSE | MSPSKESDELIFFVNGKKVTERNADPEVNLLFYLRKVIRLTGTKYGCGGGDCGACTVMISRYDPISKRISHFSATACLVPICSLHGAAVTTVEGIGSTKTRIHPVQERIAKGHGTQCGFCTPGMVMSIYTLLRNHPEPSTEQIMETLGGNLCRCTGYRPIVESAKSFCPSSTCCQMNGEGKCCLDEEKNEPERKNSVCTKLYEKKEFQPLDPTQELIFPPELMRMAEESQNTVLTFRGERTTWIAPGTLNDLLELKMKHPSAPLVIGNTYLGLHMKFTDVSYPIIISPARILELFVVTNTKQGLTLGAGLSLTQVKNVLSDVVSRLPKEKTQIYCALLKQLKTLAGQQIRNVASLGGHIISRLPTSDLNPILGIGNCILNVASTEGIQQIPLNDHFLAGVPDAILKPEQVLISVFVPRSSKWEFVSAFRQAPRQQNAFATVNAGMKVVFKEDTNTITDLGILYGGIGATVISADKSCRQLIGRCWDEEMLDDAGKMICEEVSLLMAAPGGMEEYRKTLAISFLFMFYLDVLKQLKTRDPHKYPDISQKLLHILEDFPLTMPYGMQSFQDVDFQQPLQDPIGRPIMHQSGIKHATGEAVFCDDMSVLPGELFLAVVTSSKSHAKIISLDASEALASLGVVDVVTARDVPGDNGREEESLYAQDEVICVGQIVCAVAADSYAHAQQAAKKVKIVYQDIEPMIVTVQDALQYESFIGPERKLEQGNVEEAFQCADQILEGEVHLGGQEHFYMETQSVRVVPKGEDKEMDIYVSSQDAAFTQEMVARTLGIPKNRINCHVKRVGGAFGGKASKPGLLASVAAVAAQKTGRPIRFILERRDDMLITGGRHPLLGKYKIGFMNNGKIKAADIQLYINGGCTPDDSELVIEYALLKLENAYKIPNLRVRGRVCKTNLPSNTAFRGFGFPQGAFVTETCMSAVAAKCRLPPEKVRELNMYRTIDRTIHNQEFDPTNLLQCWEACVENSSYYNRKKAVDEFNQQRFWKKRGIAIIPMKFSVGFPKTFYYQAAALVQIYTDGSVLVAHGGVELGQGINTKMIQVASRELKIPMSYIHLDEMSTVTVPNTVTTGASTGADVNGRAVQNACQILMKRLEPIIKQNPSGTWEEWVKEAFVQSISLSATGYFRGYQADMDWEKGEGDIFPYFVFGAACSEVEIDCLTGAHKNIRTDIVMDGSFSINPAVDIGQIEGAFVQGLGLYTLEELKYSPEGVLYTRGPHQYKIASVTDIPEEFHVSLLTPTPNPKAIYSSKGLGEAGTFLGCSVFFAIAAAVAAAREERGLSPIWAINSPATAEVIRMACEDQFTNLVPQTDSKCCKPWSIPVA | 1.17.3.-; 1.2.3.1 | COFACTOR: Name=[2Fe-2S] cluster; Xref=ChEBI:CHEBI:190135; Evidence={ECO:0000269|PubMed:11562361}; Note=Binds 2 [2Fe-2S] clusters per subunit. {ECO:0000269|PubMed:11562361}; COFACTOR: Name=FAD; Xref=ChEBI:CHEBI:57692; Evidence={ECO:0000269|PubMed:11562361}; Note=Binds 1 FAD per subunit. {ECO:0000269|PubMed:11562361}; COFACTOR: Name=Mo-molybdopterin; Xref=ChEBI:CHEBI:71302; Evidence={ECO:0000269|PubMed:11562361}; Note=Binds 1 Mo-molybdopterin (Mo-MPT) cofactor per subunit. {ECO:0000269|PubMed:11562361}; | xenobiotic metabolic process [GO:0006805] | cytosol [GO:0005829] | 2 iron, 2 sulfur cluster binding [GO:0051537]; aldehyde oxidase activity [GO:0004031]; electron transfer activity [GO:0009055]; FAD binding [GO:0071949]; flavin adenine dinucleotide binding [GO:0050660]; iron ion binding [GO:0005506]; molybdenum ion binding [GO:0030151]; molybdopterin cofactor binding [GO:0043546]; NAD binding [GO:0051287]; protein homodimerization activity [GO:0042803] | PF01315;PF03450;PF00941;PF00111;PF01799;PF02738;PF20256; | 3.10.20.30;3.30.465.10;1.10.150.120;3.90.1170.50;3.30.365.10;3.30.390.50;3.30.43.10; | Xanthine dehydrogenase family | null | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:11562361, ECO:0000269|PubMed:15383531}. | CATALYTIC ACTIVITY: Reaction=an aldehyde + H2O + O2 = a carboxylate + H(+) + H2O2; Xref=Rhea:RHEA:16829, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, ChEBI:CHEBI:16240, ChEBI:CHEBI:17478, ChEBI:CHEBI:29067; EC=1.2.3.1; Evidence={ECO:0000269|PubMed:11562361, ECO:0000269|PubMed:21705476, ECO:0000269|PubMed:23019336}; | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=2.3 uM for phthalazine {ECO:0000269|PubMed:11562361, ECO:0000269|PubMed:21705476, ECO:0000269|PubMed:23019336}; KM=1.4 uM for phthalazine (at 37 degrees Celsius and pH 8) {ECO:0000269|PubMed:11562361, ECO:0000269|PubMed:21705476, ECO:0000269|PubMed:23019336}; KM=2.5 uM for benzaldehyde (at 37 degrees Celsius and pH 8) {ECO:0000269|PubMed:11562361, ECO:0000269|PubMed:21705476, ECO:0000269|PubMed:23019336}; KM=128.5 uM for N1-methylnicotinamide (at 37 degrees Celsius and pH 8) {ECO:0000269|PubMed:11562361, ECO:0000269|PubMed:21705476, ECO:0000269|PubMed:23019336}; KM=32.3 uM for phenanthridine (at 37 degrees Celsius and pH 8) {ECO:0000269|PubMed:11562361, ECO:0000269|PubMed:21705476, ECO:0000269|PubMed:23019336}; KM=13 uM for benzaldehyde (at 37 degrees Celsius and pH 7.4) {ECO:0000269|PubMed:11562361, ECO:0000269|PubMed:21705476, ECO:0000269|PubMed:23019336}; KM=29 uM for butyraldehyde (at 37 degrees Celsius and pH 8) {ECO:0000269|PubMed:11562361, ECO:0000269|PubMed:21705476, ECO:0000269|PubMed:23019336}; KM=173 uM for 2-OH-pyrimidine (at 37 degrees Celsius and pH 8) {ECO:0000269|PubMed:11562361, ECO:0000269|PubMed:21705476, ECO:0000269|PubMed:23019336}; Note=kcat is 4 sec(-1) for phthalazine oxidation (PubMed:11562361). kcat is 130 min(-1) for benzaldehyde oxidation, 384 min(-1) for butyraldehyde oxidation and 1279 min(-1) for 2-OH-pyrimidine oxidation (PubMed:21705476). kcat is 41.1 min(-1) for phthalazine oxidation, 41.9 min(-1) for benzaldehyde oxidation, 14.7 min(-1) for N1-methylnicotinamide oxidation and 51.7 min(-1) for phenanthridine oxidation (PubMed:23019336). {ECO:0000269|PubMed:11562361, ECO:0000269|PubMed:21705476, ECO:0000269|PubMed:23019336}; | null | null | null | FUNCTION: Oxidase with broad substrate specificity, oxidizing aromatic azaheterocycles, such as N1-methylnicotinamide and phthalazine, as well as aldehydes, such as benzaldehyde, retinal and pyridoxal. Plays a key role in the metabolism of xenobiotics and drugs containing aromatic azaheterocyclic substituents. Is probably involved in the regulation of reactive oxygen species homeostasis. May be a prominent source of superoxide generation via the one-electron reduction of molecular oxygen. May also catalyze nitric oxide (NO) production via the reduction of nitrite to NO with NADH or aldehyde as electron donor. {ECO:0000269|PubMed:11562361, ECO:0000269|PubMed:18981221, ECO:0000269|PubMed:21705476, ECO:0000269|PubMed:23019336}. | Mus musculus (Mouse) |
G3X9J0 | SI1L3_MOUSE | MTTYRPLPNDGVDLAASCGARSTDILPGPHPGDYTPMGFWAQNGSMPQPLGESPAATTTRPSPTTPAMPKMGVRARVADWPPKRDALREQSNPSPSQDTDGVKTTKVAHSMRNLQNGQLPSSTPASSGSRAFHRLSRRRSKDVEFQDGWPRSPGRAFLPLRHRSSSEITLSECDVEEPGDPRGTRHPGVLPLFREYGSTSSIDVQGVPEQSFFDILNEFRSEQPEARGSQNLRELLQVDPGALSGGSCGTKGDPRNGQPTKDSLQSLQPLKEKEKSRKKPVRGLGSGDTVDSSIFRKLRSSKPEGEVGRPLGETEESRSPPEASRPWVCQKSFAHFDVQSMLFDLNEAAANRVSVAQRRNTTTGASAASAASAMVTLTASRAHSLGTLDPAFTSTEDLNCKENLEQDLGDDNSNDLLLSCPHFRNEIGGERERNVSFSRASVGSPGGSSEAHMAEPTLSTHRTNASISVLEVPKEQQRTQSRPRQYSIEHVDLGARYYQDYFVGKEHANYFGVDEKLGPVAVSIKREKLEDHKDHGPQYQYRIIFRTRELITLRGSILEDATPTATKHGTGRGLPLKDALEYVIPELNIHCLRLALNTPKVTEQLLKLDEQGLCRKHKVGILYCKAGQSSEEEMYNNEEAGPAFEEFLDLLGDKVCLKGFTKYAAQLDVKTDSTGTHSLYTTYQDYEIMFHVSTLLPYTPNNRQQLLRKRHIGNDIVTIIFQEPGALPFTPKNIRSHFQHVFIIVRVHNPCTENVCYSMAVTRSKDAPPFGPPIPNGTTFRKSDVFRDFLLAKVINAENAAHKSDKFHTMATRTRQEYLKDLAENCVSNTPIDSSGKFNLISLTSKKKEKTKARAGAEQHSAGAIAWRVAAQDYAQGSEIDCILGISNEFVVLLDLRTKEVVFNCYCGDVIGWTPDSSTIKIFYGRGDHIFLQAAEGSVEDIRDIVQRLKVMTNGWETVDMTLRRNGLGQLGFHVKYDGTVAEVEDYGFAWQAGLRQGSRLVEICKVAVVTLSHDQMIDLLRTSVTVKVVIIPPFEDGTPRRGWPETYDMNASEPKTESETTTPGGRPPYRSNAPWQWSGPASHNSLPATKWTTPATPGHAQSLSRLPKQTPVVPFRESQPLHSKRPVSFPETPFAASPAGADRVPPYRQPSGSFSTPGSATYARYKPSPERYAAAPHPLLSFDPHFMHDGMSSGDSSSGGLTSQESTMERPKPEPLWHVPAQARLSAMTGSIGSKHPSRQDAAGKDSPNRHSKGEPQYSSHSSSNTLSSNASSSHSDDRWFDPLDPLEPEQDPFSKGGSSDSGIDTTLYTSSPSCMSLAKAPRPTKPHKPPGNIGLCGGGRESAGRPHPVDRRREVSPAPVVAGQNKGYRPKLYSSGSCTPPGLVGGSRDPPRQPSDMGSRAGYPTQVYKTASAETPRPSQLSQCSPFQLSTSVPKSFFSKQPAHNKHSTGWKRTDEPPPRPLPFTDSKKQVDTNAKNVFGQPRLRASLRDLRSPRKNYKSTIEDDLKKLIVMDNLGPEQERDTGQSPQKSLQRTLSDESLCSGRREPSFASPASLEPGLPSDVLFTSTCTFPSSTLPARRQHQHAHPPSGAPSTTPATGNGFPEKKSAISASELSLADGRDRPLRRLDPGMMPLPDTAAGLEWSSLVNAAKAYEVQRAVSLFSLNDPALSPEIPPAHSPVHSHLSLERGPQTPRATPTMSEESPLDLTGKVYQLEVMLKQLHTDLQKEKQDKVVLQSEVASLRQNNQRLQEESQAASEQLRKFAELFSREKKEL | null | null | cytoskeleton organization [GO:0007010]; epithelial cell morphogenesis [GO:0003382]; establishment of epithelial cell polarity [GO:0090162]; eye development [GO:0001654]; hematopoietic progenitor cell differentiation [GO:0002244]; regulation of small GTPase mediated signal transduction [GO:0051056] | apical part of cell [GO:0045177]; apical plasma membrane [GO:0016324]; cytoplasm [GO:0005737]; Golgi apparatus [GO:0005794]; nucleoplasm [GO:0005654]; plasma membrane [GO:0005886]; stress fiber [GO:0001725]; tricellular tight junction [GO:0061689] | GTPase activator activity [GO:0005096] | PF21022;PF02145;PF11881; | 2.30.42.10;6.10.140.210;3.40.50.11210; | null | null | SUBCELLULAR LOCATION: Apical cell membrane {ECO:0000250|UniProtKB:O60292}. Note=Detected in tricellular junctions. Colocalizes with apical F-actin. {ECO:0000250|UniProtKB:O60292}. | null | null | null | null | null | FUNCTION: Plays a critical role in epithelial cell morphogenesis, polarity, adhesion and cytoskeletal organization in the lens (PubMed:26231217). {ECO:0000269|PubMed:26231217}. | Mus musculus (Mouse) |
G3X9K3 | BIG1_MOUSE | MYEGKKTKNMFLTRALEKILADKEVKKAHHSQLRKACEVALEEIKVETEKQSPPHGEAKAGSGTLPPVKSKTNFIEADKYFLPFELACQSKCPRIVSTSLDCLQKLIAYGHLTGRAPDSTTPGKKLIDRIIETICGCFQGPQTDEGVQLQIIKALLTAVTSQHIEIHEGTVLQAVRTCYNIYLASKNLINQTTAKATLTQMLNVIFARMENQALQEAKQMERERHRQQQHLLQSPVSHHEPESPHLRYLPPQTVDHINQEHEGDLEPQTHDVDKSLQDDTEPENGSDISSAENEQTEADQATAAETLSKNDILYDGDYEEKPLDIVQSIVEEMVNIIVGDMGEGMAISASTEGNTGTVEDGSDSENIQANGIPGTPISVAYTPSLPDDRLSVSSNDTQESGNSSGPSPGAKFSHILQKDAFLVFRSLCKLSMKPLSDGPPDPKSHELRSKILSLQLLLSILQNAGPVFRTNEMFINAIKQYLCVALSKNGVSSVPEVFELSLSIFLTLLSNFKTHLKMQIEVFFKEIFLYILETSTSSFDHKWMVIQTLTRICADAQSVVDIYVNYDCDLNAANIFERLVNDLSKIAQGRGSQELGMSNVQELSLRKKGLECLVSILKCMVEWSKDQYVNPNSQTTLGQEKPSEQEISEVKHPETINRYGSLNSLESTSSSGIGSYSTQMSGTDNPEQFEVLKQQKEIIEQGIDLFNKKPKRGIQYLQEQGMLGTTPEDIAQFLHQEERLDSTQVGEFLGDNDKFNKEVMYAYVDQHDFSGKDFVSALRLFLEGFRLPGEAQKIDRLMEKFAARYLECNQGQTLFASADTAYVLAYSIIMLTTDLHSPQVKNKMTKEQYIKMNRGINDSKDLPEEYLSAIYNEIAGKKISMKETKELTIPTKSTKQNVASEKQRRLLYNLEMEQMAKTAKALMEAVSHVQAPFTSATHLEHVRPMFKLAWTPFLAAFSVGLQDCDDTEVASLCLEGIRCAIRIACIFSIQLERDAYVQALARFTLLTVSSGITEMKQKNIDTIKTLITVAHTDGNYLGNSWHEILKCISQLELAQLIGTGVKPRYISGTVRGREGSLTGTKDQAPDEFVGLGLVGGNVDWKQIASIQESIGETSSQSVVVAVDRIFTGSTRLDGNAIVDFVRWLCAVSMDELLSTTHPRMFSLQKIVEISYYNMGRIRLQWSRIWEVIGDHFNKVGCNPNEDVAIFAVDSLRQLSMKFLEKGELANFRFQKDFLRPFEHIMKRNRSPTIRDMVVRCIAQMVNSQAANIRSGWKNIFSVFHLAASDQDESIVELAFQTTGHIVTLVFEKHFPATIDSFQDAVKCLSEFACNAAFPDTSMEAIRLIRHCAKYVSDRPQAFKEYTSDDMSVAPEDRVWVRGWFPILFELSCIINRCKLDVRTRGLTVMFEIMKTYGHTYEKHWWQDLFRIVFRIFDNMKLPEQQTEKAEWMTTTCNHALYAICDVFTQYLEVLSDVLLDDIFAQLYWCVQQDNEQLARSGTNCLENVVILNGEKFTLEIWDKTCNCTLDIFKTTIPHALLTWRPTSGEAEPPSPSAVSEKPLDAISQKSVDIHDSIQPRSSDNRQQAPLVSVSTVSEEVSKVKSTAKFPEQKLFAALLIKCVVQLELIQTIDNIVFFPATSKKEDAENLAAAQRDAVDFDVRVDTQDQGMYRFLTSQQLFKLLDCLLESHRFAKAFNSNNEQRTALWKAGFKGKSKPNLLKQETSSLACGLRILFRMYMDESRVSAWEEVQQRLLNVCREALSYFLTLTSESHREAWTNLLLLFLTKVLKISDSRFKAHASFYYPLLCEIMQFDLIPELRAVLRRFFLRIGIVFQISQPPEQELGINRQ | null | null | endomembrane system organization [GO:0010256]; Golgi organization [GO:0007030]; negative regulation of actin filament polymerization [GO:0030837]; negative regulation of GTPase activity [GO:0034260]; neuron projection development [GO:0031175]; positive regulation of phosphatidylinositol 3-kinase/protein kinase B signal transduction [GO:0051897]; positive regulation of wound healing [GO:0090303]; protein glycosylation [GO:0006486]; protein transport [GO:0015031]; regulation of ARF protein signal transduction [GO:0032012]; regulation of establishment of cell polarity [GO:2000114] | cytosol [GO:0005829]; Golgi membrane [GO:0000139]; nuclear matrix [GO:0016363]; nucleolus [GO:0005730]; nucleoplasm [GO:0005654]; perinuclear region of cytoplasm [GO:0048471]; small nuclear ribonucleoprotein complex [GO:0030532]; trans-Golgi network [GO:0005802] | guanyl-nucleotide exchange factor activity [GO:0005085]; myosin binding [GO:0017022]; protein kinase A regulatory subunit binding [GO:0034237] | PF20252;PF16213;PF01369;PF09324;PF12783; | 1.10.220.20;1.10.1000.11;1.25.10.10; | null | PTM: Phosphorylated. In vitro phosphorylated by PKA reducing its GEF activity and dephosphorylated by phosphatase PP1 (By similarity). {ECO:0000250}. | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Cytoplasm, perinuclear region {ECO:0000250}. Golgi apparatus {ECO:0000250}. Golgi apparatus, trans-Golgi network {ECO:0000250}. Nucleus {ECO:0000250}. Nucleus, nucleolus {ECO:0000250}. Nucleus matrix {ECO:0000250}. Membrane {ECO:0000250}. Note=Translocates from cytoplasm to membranes and nucleus upon cAMP treatment. {ECO:0000250}. | null | null | null | null | null | FUNCTION: Promotes guanine-nucleotide exchange on ARF1 and ARF3. Promotes the activation of ARF1/ARF3 through replacement of GDP with GTP. Involved in vesicular trafficking. Required for the maintenance of Golgi structure; the function may be independent of its GEF activity. Required for the maturaion of integrin beta-1 in the Golgi. Involved in the establishment and persistence of cell polarity during directed cell movement in wound healing. Proposed to act as A kinase-anchoring protein (AKAP) and may mediate crosstalk between Arf and PKA pathways. Inhibits GAP activity of MYO9B probably through competitive RhoA binding. The function in the nucleus remains to be determined (By similarity). {ECO:0000250|UniProtKB:Q9Y6D6}. | Mus musculus (Mouse) |
G3X9X1 | KBTB2_MOUSE | MSTQEERQINTEYAVSLLEQLKLFYEQQLFTDIVLIVEGTEFPCHKMVLATCSSYFRAMFMSGLSESKQTHVHLRNVDAAALQMIIAYAYTGNLAVNDSTVEQLYETACFLQVEDVLQRCREYLIKKINAENCVRLLSFADLFSCEELKQSAKRMVEHKFTAVYRQEAFMQLSHDLLIDILSSDNLNVEKEETVREAAMLWLEYNTESRSQYLSSVLSQIRIDALSEVTQRAWFQGLPPNDKSVVVQGLYKSMPKFFKPRLGMTKEEMMIFIEASSENPCSLYSSVCYSPQAEKVYKLCSPPADLHKVGTVVTPDNDIYIAGGQVPLKNTKTNHSKTSKLQTAFRTVNCFYWFDAQQNTWFPKTPMLFVRVKPSLVCCEGYIYAIGGDSVGGELNRRTVERYDTEKDEWTMVSPLPCAWQWSAAVVVHDCIYVMTLNLMYCYFPRSDSWVEMAMRQTSRSFASAAAFGDKIFYIGGLHIATNSGIRLPSGTVDGSSVTVEIYDVNKNEWKMAANIPAKRYSDPCVRAVVISNSLCVFMRETHLNERAKYVTYQYDLELDRWSLRQHISERVLWDLGRDFRCTVGKLYPSCLEESPWKPPTYLFSPDGTEEFELDGEMVALPPV | null | null | gene expression [GO:0010467]; glucose metabolic process [GO:0006006]; lipid metabolic process [GO:0006629]; phosphatidylinositol 3-kinase/protein kinase B signal transduction [GO:0043491]; protein ubiquitination [GO:0016567]; response to insulin [GO:0032868] | null | null | PF07707;PF00651;PF01344; | 1.25.40.420;2.120.10.80; | null | null | null | null | null | PATHWAY: Protein modification; protein ubiquitination. {ECO:0000269|PubMed:27708159}. | null | null | FUNCTION: Substrate-specific adapter of a BCR (BTB-CUL3-RBX1) E3 ubiquitin ligase complex that acts as a regulator of the insulin signaling pathway, modulating insulin sensitivity by limiting PIK3R1/p85alpha abundance in adipocytes. Targets PIK3R1, the regulatory subunit of phosphatidylinositol 3-kinase (PI3K), for 'Lys-48'-linked polyubiquitination and proteasome-mediated degradation. {ECO:0000269|PubMed:27708159, ECO:0000269|PubMed:32381739}. | Mus musculus (Mouse) |
G3XA57 | RFIP2_MOUSE | MMLSEQAQKWFPTHVQVTVLQAKDLKPKGKSGTNDTYTIIQLGKEKYSTSVAEKTLEPVWKEEASFELPGLLMQGSPEKYILFLIVMHRSLVGLDKFLGQVAINLNDIFEDKQRRKTEWFRLESKQGKRIKNRGEIKVNIQFMRNNMTASMFDLSMKDKTRSPFAKLKDKMKGRKSDGVFSDTSSAIVPSTHMPDANPEFSSGEMQMKSKPKKPFLLGPQRLSSAHSMSDLTGSHLSSEKLKSSTVGPTHLLSRQIDSFGVVPESGSLKSPHRRTLSFDTSKLNQPGSIVDEGEHSFGRQSDPFTNVTASLPQKFATLPRKKNPFEESSEPWDSSMNLFSKPIEVRKESKREKREKVSLFERVTGKRDSRRPDKLNNGGSDSPCDLKSPSAFSENRQDYFEYESTNPFTAKFRASTIMPSSSFHVNPTSSEDLRKIPDNNPFDATAGYRSLTYEEVLQELVKHKELLRRKDTHIRELEDYIDNLLVRVMEETPSILRVPYEPSRKAGKFTNS | null | null | establishment of cell polarity [GO:0030010]; insulin secretion involved in cellular response to glucose stimulus [GO:0035773]; phagocytosis [GO:0006909]; positive regulation of protein localization to plasma membrane [GO:1903078]; regulated exocytosis [GO:0045055]; TRAM-dependent toll-like receptor 4 signaling pathway [GO:0035669] | endosome [GO:0005768]; nucleoplasm [GO:0005654]; phagocytic cup [GO:0001891]; recycling endosome membrane [GO:0055038] | protein homodimerization activity [GO:0042803]; protein kinase binding [GO:0019901]; small GTPase binding [GO:0031267] | PF00168;PF09457; | 1.20.5.2440;2.60.40.150; | null | PTM: Phosphorylation at Ser-227 by MARK2 regulates epithelial cell polarity. | SUBCELLULAR LOCATION: Cell membrane; Peripheral membrane protein. Recycling endosome membrane {ECO:0000250}; Peripheral membrane protein {ECO:0000250}. Note=Translocates with RAB11A from the vesicles of the endocytic recycling compartment (ERC) to the plasma membrane. {ECO:0000250}. | null | null | null | null | null | FUNCTION: A Rab11 effector binding preferentially phosphatidylinositol 3,4,5-trisphosphate (PtdInsP3) and phosphatidic acid (PA) and acting in the regulation of the transport of vesicles from the endosomal recycling compartment (ERC) to the plasma membrane. Involved in insulin granule exocytosis. Also involved in receptor-mediated endocytosis and membrane trafficking of recycling endosomes, probably originating from clathrin-coated vesicles. Required in a complex with MYO5B and RAB11 for the transport of NPC1L1 to the plasma membrane. Also acts as a regulator of cell polarity. Plays an essential role in phagocytosis through a mechanism involving TICAM2, RAC1 and CDC42 Rho GTPases for controlling actin-dynamics. {ECO:0000250|UniProtKB:Q7L804, ECO:0000269|PubMed:19335615}. | Mus musculus (Mouse) |
G3XA59 | LRC32_MOUSE | MSHQILLLLAMLTLGLAISQRREQVPCRTVNKEALCHGLGLLQVPSVLSLDIQALYLSGNQLQSILVSPLGFYTALRHLDLSDNQISFLQAGVFQALPYLEHLNLAHNRLATGMALNSGGLGRLPLLVSLDLSGNSLHGNLVERLLGETPRLRTLSLAENSLTRLARHTFWGMPAVEQLDLHSNVLMDIEDGAFEALPHLTHLNLSRNSLTCISDFSLQQLQVLDLSCNSIEAFQTAPEPQAQFQLAWLDLRENKLLHFPDLAVFPRLIYLNVSNNLIQLPAGLPRGSEDLHAPSEGWSASPLSNPSRNASTHPLSQLLNLDLSYNEIELVPASFLEHLTSLRFLNLSRNCLRSFEARQVDSLPCLVLLDLSHNVLEALELGTKVLGSLQTLLLQDNALQELPPYTFASLASLQRLNLQGNQVSPCGGPAEPGPPGCVDFSGIPTLHVLNMAGNSMGMLRAGSFLHTPLTELDLSTNPGLDVATGALVGLEASLEVLELQGNGLTVLRVDLPCFLRLKRLNLAENQLSHLPAWTRAVSLEVLDLRNNSFSLLPGNAMGGLETSLRRLYLQGNPLSCCGNGWLAAQLHQGRVDVDATQDLICRFGSQEELSLSLVRPEDCEKGGLKNVNLILLLSFTLVSAIVLTTLATICFLRRQKLSQQYKA | null | null | negative regulation of activated T cell proliferation [GO:0046007]; negative regulation of cytokine production [GO:0001818]; positive regulation of gene expression [GO:0010628]; regulation of transforming growth factor beta3 activation [GO:1901398]; secondary palate development [GO:0062009]; transforming growth factor beta receptor signaling pathway [GO:0007179] | cell surface [GO:0009986]; external side of plasma membrane [GO:0009897]; extracellular matrix [GO:0031012]; extracellular space [GO:0005615]; nucleoplasm [GO:0005654] | transforming growth factor beta binding [GO:0050431] | PF13855; | 3.80.10.10; | LRRC32/LRRC33 family | null | SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:Q14392}; Single-pass type I membrane protein {ECO:0000255}. Cell surface {ECO:0000250|UniProtKB:Q14392}. | null | null | null | null | null | FUNCTION: Key regulator of transforming growth factor beta (TGFB1, TGFB2 and TGFB3) that controls TGF-beta activation by maintaining it in a latent state during storage in extracellular space (PubMed:25127859). Associates specifically via disulfide bonds with the Latency-associated peptide (LAP), which is the regulatory chain of TGF-beta, and regulates integrin-dependent activation of TGF-beta (PubMed:25127859, PubMed:28912269). Able to outcompete LTBP1 for binding to LAP regulatory chain of TGF-beta (By similarity). Controls activation of TGF-beta-1 (TGFB1) on the surface of activated regulatory T-cells (Tregs) (PubMed:25127859). Required for epithelial fusion during palate development by regulating activation of TGF-beta-3 (TGFB3) (PubMed:28912269). {ECO:0000250|UniProtKB:Q14392, ECO:0000269|PubMed:25127859, ECO:0000269|PubMed:28912269}. | Mus musculus (Mouse) |
G3XAP7 | LP9A_THEAU | HGFVQNIVIDGKNYGGYLVNQYPYMSNPPEVIAWSTTATDLGFVDGTGYQTPDIICHRGAKPGALTAPVSPGGTVELQWTPWPDSHHGPVINYLAPCNGDCSTVDKTQLEFFKIAESGLINDDNPPGIWASDNLIAANNSWTVTIPTTIAPGNYVLRHEIIALHSAQNQDGAQNYPQCINLQVTGGGSDNPAGTLGTALYHDTDPGILINIYQKLSSYIIPGPPLYTG | 3.2.1.4 | COFACTOR: Name=Cu(2+); Xref=ChEBI:CHEBI:29036; Evidence={ECO:0000269|PubMed:21876164, ECO:0000269|PubMed:29971843, ECO:0000269|PubMed:35204695, ECO:0000269|PubMed:36071795, ECO:0000269|Ref.4}; Note=Binds 1 copper ion per subunit. {ECO:0000269|PubMed:21876164, ECO:0000269|PubMed:29971843, ECO:0000269|PubMed:35204695, ECO:0000269|PubMed:36071795, ECO:0000269|Ref.4}; | cellulose catabolic process [GO:0030245] | extracellular region [GO:0005576] | cellulase activity [GO:0008810]; cellulose binding [GO:0030248]; metal ion binding [GO:0046872] | PF03443; | 2.70.50.70; | Polysaccharide monooxygenase AA9 family | PTM: The catalytically essential N-terminal histidine His-22 is post-translationally modified by methylation to prevent protonation of the histidine side chain, and protect the critical active site of the enzyme from oxidative damage. {ECO:0000269|PubMed:21876164, ECO:0000269|PubMed:29971843}. | SUBCELLULAR LOCATION: Secreted {ECO:0000305|PubMed:21876164}. | CATALYTIC ACTIVITY: Reaction=Endohydrolysis of (1->4)-beta-D-glucosidic linkages in cellulose, lichenin and cereal beta-D-glucans.; EC=3.2.1.4; Evidence={ECO:0000269|PubMed:21876164, ECO:0000269|Ref.4}; | null | null | null | null | FUNCTION: Lytic polysaccharide monooxygenase that depolymerizes crystalline and amorphous polysaccharides via the oxidation of scissile alpha- or beta-(1-4)-glycosidic bonds, yielding C1 and C4 oxidation product (PubMed:21876164, PubMed:29971843, Ref.4). Catalysis by LPMOs requires the reduction of the active-site copper from Cu(II) to Cu(I) by a reducing agent and H(2)O(2) or O(2) as a cosubstrate (PubMed:21876164, PubMed:29971843, Ref.4). Is able to cleave cellulose and xylan to produce C1- and C4-oxidized products (Ref.4). {ECO:0000269|PubMed:21876164, ECO:0000269|PubMed:29971843, ECO:0000269|Ref.4}. | Thermoascus aurantiacus |
G3XCV0 | FLEQ_PSEAE | MWRETKLLLIDDNLDRSRDLAVILNFLGEDQLTCNSEDWREVAAGLSNSREALCVLLGSVESKGGAVELLKQLASWDEYLPILLIGEPAPADWPEELRRRVLASLEMPPSYNKLLDSLHRAQVYREMYDQARERGRSREPNLFRSLVGTSRAIQQVRQMMQQVADTDASVLILGESGTGKEVVARNLHYHSKRREGPFVPVNCGAIPAELLESELFGHEKGAFTGAITSRAGRFELANGGTLFLDEIGDMPLPMQVKLLRVLQERTFERVGSNKTQNVDVRIIAATHKNLEKMIEDGTFREDLYYRLNVFPIEMAPLRERVEDIALLLNELISRMEHEKRGSIRFNSAAIMSLCRHDWPGNVRELANLVERLAIMHPYGVIGVGELPKKFRHVDDEDEQLASSLREELEERAAINAGLPGMDAPAMLPAEGLDLKDYLANLEQGLIQQALDDAGGVVARAAERLRIRRTTLVEKMRKYGMSRRDDDLSDD | null | null | DNA-templated transcription [GO:0006351]; negative regulation of extracellular matrix assembly [GO:1901202]; positive regulation of cell-substrate adhesion [GO:0010811]; positive regulation of cilium-dependent cell motility [GO:2000155]; regulation of bacterial-type flagellum-dependent cell motility [GO:1902021]; regulation of DNA-templated transcription [GO:0006355] | protein-DNA complex [GO:0032993] | ATP binding [GO:0005524]; ATP hydrolysis activity [GO:0016887]; cis-regulatory region sequence-specific DNA binding [GO:0000987]; cyclic-di-GMP binding [GO:0035438]; DNA-binding transcription activator activity [GO:0001216]; DNA-binding transcription repressor activity [GO:0001217]; transcription cis-regulatory region binding [GO:0000976] | PF06490;PF02954;PF00158; | 1.10.8.60;3.40.50.2300;1.10.10.60;3.40.50.300; | null | null | null | null | null | null | null | null | FUNCTION: AAA+ ATPase enhancer-binding protein that acts as a transcription regulator and plays a role in the modulation of mucin adhesion and flagellar gene expression (PubMed:11673434, PubMed:26362077, PubMed:9287015). In addition to flagella genes, regulates also expression of biofilm-related genes (PubMed:22581773). Functions as a transcriptional repressor in the absence of c-di-GMP and as an activator when c-di-GMP is present (PubMed:22581773). {ECO:0000269|PubMed:11673434, ECO:0000269|PubMed:22581773, ECO:0000269|PubMed:26362077, ECO:0000269|PubMed:9287015}. | Pseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C / PRS 101 / PAO1) |
G3XCX3 | PILU_PSEAE | MEFEKLLRLMVEKGGSDLFITAGVPPSMKVNGRVMPVTKTPLSPEQTRETVLGVMNEQQRRDFAENHECNFAISARGIGRFRVSAFYQRNLVGMVLRRIETNIPTLEELKLPEILKKLALTKRGLVIFVGATGTGKSTSLAAMIGYRNKNSTGHIISIEDPIEYIHQHQGCIVTQREVGLDTDSFEVALKNTLRQAPDVIMIGEVRSRETMDHAVAFAETGHLCLATLHANNANQALERIIHFFPADRHGQVWMDLSLNLKAIVAQQLVPTPDGKGRRAVIEVLLNTPLAADLIRKGEVHELKPLMKRSTEQGMQTFDQALYQLYTQGEITYEDALAHADSANDLRLMIKLGSESDADHLSSLTQGLSLEITDDDPAGRRFR | null | null | type IV pilus-dependent motility [GO:0043107] | cytoplasm [GO:0005737] | ATP binding [GO:0005524]; endodeoxyribonuclease activity, producing 5'-phosphomonoesters [GO:0016888] | PF00437; | 3.30.450.90;3.40.50.300; | GSP E family | null | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:15659660}. Note=Localizes only to the piliated pole. {ECO:0000269|PubMed:15659660}. | null | null | null | null | null | FUNCTION: ATPase component of the type IV pilus (T4P) that plays a role in surface and host cell adhesion, colonization, biofilm maturation, virulence, and twitching, a form of surface-associated motility facilitated by cycles of extension, adhesion, and retraction of T4P fibers (PubMed:10377148, PubMed:15659660, PubMed:18174131, PubMed:7854122). Functions as a PilT-dependent retraction ATPase, providing a functional coupling between PilT and PilU and an optimal mechanism for pilus retraction (PubMed:31525185, PubMed:31626631). {ECO:0000269|PubMed:10377148, ECO:0000269|PubMed:15659660, ECO:0000269|PubMed:18174131, ECO:0000269|PubMed:31525185, ECO:0000269|PubMed:31626631, ECO:0000269|PubMed:7854122}. | Pseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C / PRS 101 / PAO1) |
G3XCY4 | AMRZ_PSEAE | MRPLKQATPTYSSRTADKFVVRLPEGMREQIAEVARSHHRSMNSEIIARLEQSLLQEGALQDNLGVRLDSPELSLHERELLQRFRQLTHRQQNALVALIAHDAELAQA | null | null | bacterial-type flagellum assembly [GO:0044780]; negative regulation of bacterial-type flagellum-dependent cell motility [GO:1902201]; negative regulation of DNA-templated transcription [GO:0045892]; negative regulation of single-species biofilm formation on inanimate substrate [GO:1900232]; positive regulation of cell motility [GO:2000147]; positive regulation of single-species biofilm formation on inanimate substrate [GO:1900233]; regulation of polysaccharide biosynthetic process [GO:0032885]; type IV pilus-dependent motility [GO:0043107] | protein-DNA complex [GO:0032993] | DNA binding [GO:0003677]; DNA-binding transcription repressor activity [GO:0001217]; sequence-specific DNA binding [GO:0043565]; transcription cis-regulatory region binding [GO:0000976] | PF03869; | 1.10.1220.10; | null | null | null | null | null | null | null | null | FUNCTION: Functions both as a transcriptional activator and a repressor of multiple genes encoding virulence factors as well as genes involved in environmental adaptation (PubMed:16352829, PubMed:22511872, PubMed:26549743). Plays a role in alginate production via the activation of AlgD which is the first gene in the alginate biosynthetic operon (PubMed:10476040, PubMed:16352829). Regulates also the transcription of genes responsible for type IV pili localization and twitching motility (PubMed:16352829). Mediates transition of P.aeruginosa biofilm infections from colonizing to chronic biofilms through repression of the psl operon (PubMed:23354748). Represses also its own transcription by binding to two sites on amrZ promoter, amrZ1 and amrZ2 (PubMed:15968052). {ECO:0000269|PubMed:10476040, ECO:0000269|PubMed:15968052, ECO:0000269|PubMed:16352829, ECO:0000269|PubMed:22511872, ECO:0000269|PubMed:23354748, ECO:0000269|PubMed:26549743}. | Pseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C / PRS 101 / PAO1) |
G3XCY6 | GLTR_PSEAE | MSANGRSILLVDDDQEIRELLETYLSRAGFQVRSVSRGADFRQALCEEEASLAILDVMLPDEDGFSLCRWIRSHQRLACMPIIMLTASSDEADRVIGLELGADDYLGKPFSPRELLARIKALLRRAQFTQVRGGDVLAFEDWRLDTVSHRLFHEDGEEFFLSGADFALLKLFLDHPQQILDRDTIANATRGREVLPLERIVDMAVSRLRQRLRDTGKAPRLIQTVRGSGYLLAAQVRPHLQP | null | null | positive regulation of glucose transmembrane transport [GO:0010828]; regulation of DNA-templated transcription [GO:0006355] | cytosol [GO:0005829]; protein-DNA complex [GO:0032993] | phosphorelay response regulator activity [GO:0000156]; transcription cis-regulatory region binding [GO:0000976] | PF00072;PF00486; | 3.40.50.2300;6.10.250.690;1.10.10.10; | null | PTM: Phosphorylated by GtrS. {ECO:0000269|PubMed:24920832}. | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305}. | null | null | null | null | null | FUNCTION: Member of the two-component regulatory system GtrS/GltR involved in the regulation of glucose metabolism and transport, as well as regulation of the exotoxin A gene expression (PubMed:24920832). GltR controls the transcription of genes involved in glucose metabolism (glk and edd/gap-1) and transport (oprB) as well as the expression of toxA that encodes exotoxin A, the primary virulence factor (PubMed:24920832, PubMed:8830708). Acts as a repressor that is released from its target operators upon phosphorylation (PubMed:24920832). {ECO:0000269|PubMed:24920832, ECO:0000269|PubMed:8830708}.; FUNCTION: Contributes to modulation of the type III secretion system (T3SS) in response to host cells via the regulation of the OprB transport system. {ECO:0000269|PubMed:22262100}. | Pseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C / PRS 101 / PAO1) |
G3XD01 | WBPD_PSEAE | MSYYQHPSAIVDDGAQIGSDSRVWHFVHICAGARIGAGVSLGQNVFVGNKVVIGDRCKIQNNVSVYDNVTLEEGVFCGPSMVFTNVYNPRSLIERKDQYRNTLVKKGATLGANCTIVCGVTIGEYAFVGAGAVINKNVPSYALMVGVPARQIGWMSEFGEQLQLNEQGEAVCSHSGARYVLNGKILSKVDV | 2.3.1.201 | null | cell wall organization [GO:0071555]; O antigen biosynthetic process [GO:0009243]; polysaccharide biosynthetic process [GO:0000271]; protein trimerization [GO:0070206]; UDP-glucuronate biosynthetic process [GO:0006065] | null | acetyltransferase activity [GO:0016407]; acyltransferase activity [GO:0016746] | PF00132; | 2.20.70.110;2.160.10.10; | Transferase hexapeptide repeat family | null | null | CATALYTIC ACTIVITY: Reaction=acetyl-CoA + UDP-2-acetamido-3-amino-2,3-dideoxy-alpha-D-glucuronate = CoA + H(+) + UDP-2,3-diacetamido-2,3-dideoxy-alpha-D-glucuronate; Xref=Rhea:RHEA:33587, ChEBI:CHEBI:15378, ChEBI:CHEBI:57287, ChEBI:CHEBI:57288, ChEBI:CHEBI:58745, ChEBI:CHEBI:62245; EC=2.3.1.201; Evidence={ECO:0000269|PubMed:19282284, ECO:0000269|PubMed:19348502}; | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=107 uM for UDP-D-GlcNAc3NA {ECO:0000269|PubMed:19348502}; Note=kcat is 2900 min(-1).; | PATHWAY: Bacterial outer membrane biogenesis; LPS O-antigen biosynthesis. {ECO:0000269|PubMed:16102001, ECO:0000269|PubMed:19282284, ECO:0000269|PubMed:19348502, ECO:0000269|PubMed:8939432}. | null | null | FUNCTION: Plays a role in the biosynthesis of B-band O antigen for serotype O5. Catalyzes the transfer of an acetyl group to the C-3 amino position of UDP-2-acetamido-3-amino-2,3-dideoxy-alpha-D-glucuronate (UDP-D-GlcNAc3NA). {ECO:0000269|PubMed:16102001, ECO:0000269|PubMed:19282284, ECO:0000269|PubMed:19348502}. | Pseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C / PRS 101 / PAO1) |
G3XD23 | WBPB_PSEAE | MKNFALIGAAGYIAPRHMRAIKDTGNCLVSAYDINDSVGIIDSISPQSEFFTEFEFFLDHASNLKRDSATALDYVSICSPNYLHYPHIAAGLRLGCDVICEKPLVPTPEMLDQLAVIERETDKRLYNILQLRHHQAIIALKDKVAREKSPHKYEVDLTYITSRGNWYLKSWKGDPRKSFGVATNIGVHFYDMLHFIFGKLQRNVVHFTSEYKAAGYLEYEQARVRWFLSVDANDLPESVKGKKPTYRSITVNGEEMEFSEGFTDLHTTSYEEILAGRGYGIDDARHCVETVNTIRSAVIVPASDNEGHPFVAALAR | 1.1.1.335 | null | cell wall organization [GO:0071555]; lipopolysaccharide biosynthetic process [GO:0009103]; O antigen biosynthetic process [GO:0009243]; polysaccharide biosynthetic process [GO:0000271]; protein tetramerization [GO:0051262]; UDP-glucuronate biosynthetic process [GO:0006065] | null | NAD+ binding [GO:0070403]; NADH binding [GO:0070404]; NADH dehydrogenase activity [GO:0003954]; phosphoglycerate dehydrogenase activity [GO:0004617] | PF01408;PF02894; | 3.40.50.720; | Gfo/Idh/MocA family | null | null | CATALYTIC ACTIVITY: Reaction=NAD(+) + UDP-N-2-acetamido-2-deoxy-alpha-D-glucuronate = H(+) + NADH + UDP-2-acetamido-2-deoxy-alpha-D-ribo-hex-3-uluronate; Xref=Rhea:RHEA:33579, ChEBI:CHEBI:15378, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945, ChEBI:CHEBI:62250, ChEBI:CHEBI:65040; EC=1.1.1.335; Evidence={ECO:0000269|PubMed:19282284, ECO:0000269|PubMed:19348502}; CATALYTIC ACTIVITY: Reaction=2-hydroxyglutarate + NAD(+) = 2-oxoglutarate + H(+) + NADH; Xref=Rhea:RHEA:13449, ChEBI:CHEBI:11596, ChEBI:CHEBI:15378, ChEBI:CHEBI:16810, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945; | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=0.25 mM for UDP-GlcNAcA {ECO:0000269|PubMed:19348502, ECO:0000269|PubMed:20690587}; KM=1.35 mM for 2-oxoglutarate {ECO:0000269|PubMed:19348502, ECO:0000269|PubMed:20690587}; Vmax=28 umol/min/ug enzyme {ECO:0000269|PubMed:19348502, ECO:0000269|PubMed:20690587}; | PATHWAY: Bacterial outer membrane biogenesis; LPS O-antigen biosynthesis. {ECO:0000269|PubMed:18621892, ECO:0000269|PubMed:19282284, ECO:0000269|PubMed:19348502, ECO:0000269|PubMed:8939432}. | BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 8.0 for the coupled WbpB/WbpE reaction. {ECO:0000269|PubMed:19348502}; | BIOPHYSICOCHEMICAL PROPERTIES: Temperature dependence: Optimum temperature is 30 degrees Celsius for the coupled WbpB/WbpE reaction. {ECO:0000269|PubMed:19348502}; | FUNCTION: Plays a role in the biosynthesis of B-band O antigen for serotype O5. Catalyzes the NAD-dependent oxidation of UDP-N-acetylglucosaminuronic acid (UDP-D-GlcNAcA) to UDP-2-acetamido-2-deoxy-3-oxo-D-glucuronic acid (UDP-3-oxo-D-GlcNAcA). Cannot use UDP-GlcNAc or UDP-GalNAc as the nucleotide sugar substrate, and can use only poorly UDP-D-glucuronic acid (UDP-GlcA). Undergoes an NAD(+) recycling mechanism using 2-oxoglutarate as an oxidant. {ECO:0000269|PubMed:18621892, ECO:0000269|PubMed:19282284, ECO:0000269|PubMed:19348502, ECO:0000269|PubMed:20690587}. | Pseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C / PRS 101 / PAO1) |
G3XD24 | PCTA_PSEAE | MIKSLKFSHKILLAASLVVFAAFALFTLYNDYLQRNAIREDLESYLREMGDVTSSNIQNWLGGRLLLVEQTAQTLARDHSPETVSALLEQPALTSTFSFTYLGQQDGVFTMRPDSPMPAGYDPRSRPWYKDAVAAGGLTLTEPYVDAATQELIITAATPVKAAGNTLGVVGGDLSLKTLVQIINSLDFSGMGYAFLVSGDGKILVHPDKEQVMKTLSEVYPQNTPKIATGFSEAELHGHTRILAFTPIKGLPSVTWYLALSIDKDKAYAMLSKFRVSAIAAALISIVAILVLLGLLIRLLMQPLHLMGRAMQDIAQGEGDLTKRLAVTSRDEFGVLGDAFNQFVERIHRSIREVAGTAHKLHDVSQLVVNASNSSMANSDEQSNRTNSVAAAINELGAAAQEIARNAADASHHASDANHQAEDGKQVVEQTIRAMNELSEKISASCANIEALNSRTVNIGQILEVIKGISEQTNLLALNAAIEAARAGEAGRGFAVVADEVRNLAHRAQESAQQIQKMIEELQVGAREAVATMTESQRYSLESVEIANRAGESLSSVTRRIGEIDGMNQSVATATEEQTAVVDSLNMDITEINTLNQEGVENLQATLRACGELETQAGRLRQLVDSFKI | null | null | chemotaxis [GO:0006935]; response to amino acid [GO:0043200]; signal transduction [GO:0007165] | plasma membrane [GO:0005886] | amino acid binding [GO:0016597]; transmembrane signaling receptor activity [GO:0004888] | PF02743;PF00672;PF00015; | 1.10.287.950;3.30.450.20; | Methyl-accepting chemotaxis (MCP) protein family | null | SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000255}. | null | null | null | null | null | FUNCTION: Chemotactic-signal transducers respond to changes in the concentration of attractants and repellents in the environment, transduce a signal from the outside to the inside of the cell, and facilitate sensory adaptation through the variation of the level of methylation. Major receptor that responds to all naturally occurring L-amino acids, except L-Gln and L-Asp. Also involved in repellent responses to trichloroethylene (TCE), chloroform and methylthiocyanate (PubMed:16233808, PubMed:23650915, PubMed:8522505, PubMed:9353923). Also mediates chemotaxis to histamine, but does not bind histamine (PubMed:30425146). In addition, binds the quorum-sensing signal autoinducer 2 (AI-2), thus inducing chemotaxis toward AI-2 and biofilm formation (PubMed:33097715). {ECO:0000269|PubMed:16233808, ECO:0000269|PubMed:23650915, ECO:0000269|PubMed:30425146, ECO:0000269|PubMed:33097715, ECO:0000269|PubMed:8522505, ECO:0000269|PubMed:9353923}. | Pseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C / PRS 101 / PAO1) |
G3XD94 | UGND_PSEAE | MIDVNTVVEKFKSRQALIGIVGLGYVGLPLMLRYNAIGFDVLGIDIDDVKVDKLNAGQCYIEHIPQAKIAKARASGFEATTDFSRVSECDALILCVPTPLNKYREPDMSFVINTTDALKPYLRVGQVVSLESTTYPGTTEEELLPRVQEGGLVVGRDIYLVYSPEREDPGNPNFETRTIPKVIGGHTPQCLEVGIALYEQAIDRVVPVSSTKAAEMTKLLENIHRAVNIGLVNEMKIVADRMGIDIFEVVDAAATKPFGFTPYYPGPGLGGHCIPIDPFYLTWKAREYGLHTRFIELSGEVNQAMPEYVLGKLMDGLNEAGRALKGSRVLVLGIAYKKNVDDMRESPSVEIMELIEAKGGMVAYSDPHVPVFPKMREHHFELSSEPLTAENLARFDAVVLATDHDKFDYELIKAEAKLVVDSRGKYRSPAAHIIKA | 1.1.1.136 | COFACTOR: Name=K(+); Xref=ChEBI:CHEBI:29103; Evidence={ECO:0000269|PubMed:15226302}; Name=NH4(+); Xref=ChEBI:CHEBI:28938; Evidence={ECO:0000269|PubMed:15226302}; Note=A monovalent cation. NH4(+) and K(+) are the most effective. {ECO:0000269|PubMed:15226302}; | cell wall organization [GO:0071555]; O antigen biosynthetic process [GO:0009243]; polysaccharide biosynthetic process [GO:0000271] | membrane [GO:0016020] | NAD binding [GO:0051287]; NADH dehydrogenase activity [GO:0003954]; oxidoreductase activity, acting on the CH-CH group of donors, NAD or NADP as acceptor [GO:0016628]; UDP-N-acetylglucosamine 6-dehydrogenase activity [GO:0047004] | PF00984;PF03720;PF03721; | 3.40.50.720; | UDP-glucose/GDP-mannose dehydrogenase family | null | SUBCELLULAR LOCATION: Membrane {ECO:0000255}; Single-pass membrane protein {ECO:0000255}. | CATALYTIC ACTIVITY: Reaction=H2O + 2 NAD(+) + UDP-N-acetyl-alpha-D-glucosamine = 3 H(+) + 2 NADH + UDP-N-2-acetamido-2-deoxy-alpha-D-glucuronate; Xref=Rhea:RHEA:13325, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:57540, ChEBI:CHEBI:57705, ChEBI:CHEBI:57945, ChEBI:CHEBI:65040; EC=1.1.1.136; Evidence={ECO:0000269|PubMed:15226302}; | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=0.094 mM for UDP-D-GlcNAc {ECO:0000269|PubMed:15226302}; KM=0.22 mM for NAD(+) {ECO:0000269|PubMed:15226302}; Vmax=2.9 nmol/min/ug enzyme {ECO:0000269|PubMed:15226302}; | PATHWAY: Bacterial outer membrane biogenesis; LPS O-antigen biosynthesis. {ECO:0000269|PubMed:10930727, ECO:0000269|PubMed:15226302, ECO:0000269|PubMed:18621892, ECO:0000269|PubMed:8939432}. | BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 8.0-9.0. {ECO:0000269|PubMed:15226302}; | BIOPHYSICOCHEMICAL PROPERTIES: Temperature dependence: Optimum temperature is 33-37 degrees Celsius. Active from temperatures ranging from 0 degrees Celsius to 65 degrees Celsius. {ECO:0000269|PubMed:15226302}; | FUNCTION: Plays a role in the biosynthesis of B-band O antigen for serotype O5. Catalyzes the C-6 dehydrogenation of UDP-D-GlcNAc to UDP-N-acetylglucosaminuronic acid (UDP-D-GlcNAcA). {ECO:0000269|PubMed:10930727, ECO:0000269|PubMed:15226302, ECO:0000269|PubMed:18621892}. | Pseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C / PRS 101 / PAO1) |
G3XD97 | PTXS_PSEAE | MNGSVLPSRGRVTINQVAEAAGVSKASVSRYIGGDRQLLADATARRIERAIDQLDYRPNQMARGLKRGRTRLIGMLVADILNPYSVAVMHGVETACREHGYSLVVCNTDRDDEQERHHLAALQSYNVEGLIVNTLGHHPGELRALHRELPMVLVDRQLAELDTDLVGLDNADAVEQALDHLQHRGFRDILLVTEPLDGTSSRIERVQAFNASIGRRPALKGQVLQTDDFFRDGLRAFLSASGPGPKALFTCNGVATLCATRQLRDLGCRLFDEVGLLALDELDWYPLVGSGITALAQPTDEIGRTAFERLLARLEGDREPARRVTFPAQLIVRGSTHPRG | null | null | negative regulation of DNA-templated transcription [GO:0045892]; regulation of DNA-templated transcription [GO:0006355] | protein-DNA complex [GO:0032993] | DNA-binding transcription factor activity [GO:0003700]; DNA-binding transcription repressor activity [GO:0001217]; transcription cis-regulatory region binding [GO:0000976] | PF00356;PF00532; | 3.40.50.2300;1.10.260.40; | null | null | null | null | null | null | null | null | FUNCTION: Negatively regulates glucose metabolism by binding directly to the promoter region of the kgu and gad operons (PubMed:22844393, PubMed:24019239). It also negatively regulates its own synthesis (PubMed:10438759, PubMed:10894751, PubMed:22844393). {ECO:0000269|PubMed:10438759, ECO:0000269|PubMed:10894751, ECO:0000269|PubMed:22844393, ECO:0000269|PubMed:24019239}.; FUNCTION: In addition, in pathogenic strains, PtxS modulates PtxR activity in response to 2-ketogluconate (PubMed:22844393, PubMed:24019239, PubMed:9645431). In the presence of PtxR, which also binds to the kgu and gad promoter regions, PtxS and PtxR form a tight complex, creating a DNA-loop that prevents RNA polymerase promoter access and expression of the glucose metabolism genes (PubMed:10931350, PubMed:22844393, PubMed:24019239). Binding of the 2-ketogluconate effector to PtxS causes PtxS/PtxR complex dissociation and leads to the dissolution of the repression DNA-loop, facilitating the entry of the RNA polymerase and enabling the transcription of the genes (PubMed:22844393, PubMed:24019239). Also plays an important role in the regulation of the expression of the virulence factor exotoxin A (toxA) (PubMed:22844393, PubMed:9645431). PtxS does not bind directly to the toxA promoter but negatively regulates the production of exotoxin A by binding to PtxR and interfering with its positive regulator activity (PubMed:22844393, PubMed:9645431). In the presence of 2-ketogluconate, PtxS is released and PtxR can recruit RNA polymerase (PubMed:22844393). {ECO:0000269|PubMed:10931350, ECO:0000269|PubMed:22844393, ECO:0000269|PubMed:24019239, ECO:0000269|PubMed:9645431}. | Pseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C / PRS 101 / PAO1) |
G3XDA8 | PSTS_PSEAE | MKLKRLMAALTFVAAGVGAASAVAAIDPALPEYQKASGVSGNLSSVGSDTLANLMTMWAEEYKRLYPNVNIQIQAAGSSTAPPALTEGTANLGPMSRKMKDVELQAFEQKYGYKPTAVPVAVDALAIFVHKDNPIKGLTMQQVDAIFSATRLCGSKQDVKTWGDLGLTGDWAKKPVQLFGRNSVSGTYGYFKEEALCKGDFRPNVNEQPGSASVVQSVSQSLNGIGYSGIGYKTASVKTVALAKKEGAAFVEDNEQNALNGTYPLSRFLYVYVNKAPNKPLDPLEAQFLKLVLSKTGQQVVVKDGYIPLPAKVAEKAIKELGL | null | null | cell adhesion [GO:0007155]; phosphate ion transport [GO:0006817]; single-species biofilm formation [GO:0044010] | extracellular region [GO:0005576]; periplasmic space [GO:0042597] | phosphate ion binding [GO:0042301] | PF12849; | 3.40.190.10; | PstS family | null | SUBCELLULAR LOCATION: Periplasm {ECO:0000269|PubMed:6436026, ECO:0000269|Ref.5}. Secreted {ECO:0000269|PubMed:18282104}. Note=In some strains (e.g. non-MDR PAO1 and virulent clinical strain MDR25) forms long appendages distinct from flagella or pili on the cell surface: cell surface expression depends on type II secretion effector hxcR (PubMed:18282104). {ECO:0000269|PubMed:18282104}. | null | null | null | null | null | FUNCTION: Binds 1 inorganic phosphate per subunit with a KD of 0.34 uM (PubMed:6436026). Required for phosphate transport (Ref.5). In strain PAO1 implicated in host cell adhesion; in some virulent strains (e.g. MDR25 which expresses very high levels of this protein) antibody fragments against this protein decrease host cell adhesion and increase transepithelial resistance of human epithelial cell monolayers. Its ability to bind phosphate may allow it to acquire phosphate from its host (PubMed:18282104). {ECO:0000269|PubMed:18282104, ECO:0000269|PubMed:6436026}. | Pseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C / PRS 101 / PAO1) |
G3XP38 | OTASE_ASPNA | MVRRIASATPMVQSPMSPLGTTYCVRPNSVSMNLQRRPLVIASTDEAKVTIIYAGLLIPGDGEPLRNAALVISDKIIAFVGSEADIPKKYLRSTQSTHRVPVLMPGLWDCHMHFGGDDDYYNDYTSGLATHPASSGARLARGCWEALQNGYTSYRDLAGYGCEVAKAINDGTIVGPNVYSSGAALSQTAGHGDIFALPAGEVLGSYGVMNPRPGYWGAGPLCIADGVEEVRRAVRLQIRRGAKVIKVMASGGVMSRDDNPNFAQFSPEELKVIVEEAARQNRIVSAHVHGKAGIMAAIKAGCKSLEHVSYADEEVWELMKEKGILYVATRSVIEIFLASNGEGLVKESWAKLQALADSHLKAYQGAIKAGVTIALGTDTAPGGPTALELQFAVERGGMTPLEAIKAATANAPLSVGPQAPLTGQLREGYEADVIALEENPLEDIKVFQEPKAVTHVWKGGKLFKGPGIGPWGEDARNPFL | 3.4.17.- | COFACTOR: Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000269|PubMed:24947135}; | proteolysis [GO:0006508] | extracellular region [GO:0005576] | carboxypeptidase activity [GO:0004180]; hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds [GO:0016810]; metal ion binding [GO:0046872]; metallopeptidase activity [GO:0008237] | PF01979; | 3.20.20.140; | Metallo-dependent hydrolases superfamily, Ochratoxinase amidase 2 family | null | SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:24947135}. | CATALYTIC ACTIVITY: Reaction=H2O + ochratoxin A = L-phenylalanine + ochratoxin alpha; Xref=Rhea:RHEA:72751, ChEBI:CHEBI:15377, ChEBI:CHEBI:58095, ChEBI:CHEBI:166829, ChEBI:CHEBI:192527; Evidence={ECO:0000269|PubMed:24947135}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:72752; Evidence={ECO:0000269|PubMed:24947135}; | null | null | BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 6. {ECO:0000269|PubMed:24947135}; | BIOPHYSICOCHEMICAL PROPERTIES: Temperature dependence: Optimum temperature is 66 degrees Celsius. {ECO:0000269|PubMed:24947135}; | FUNCTION: Carboxypeptidase that catalyzes the release of a C-terminal amino acid with specific catalytic activity for aromatic amino acids such as phenylalanine (PubMed:24947135, PubMed:33647354). Is able to degrade ochratoxin A, one of the five major mycotoxins most harmful to humans and animals that is produced by Aspergillus and Penicillium species and occurs in a wide range of agricultural products (PubMed:24947135). {ECO:0000269|PubMed:24947135, ECO:0000269|PubMed:33647354}. | Aspergillus niger (strain ATCC 1015 / CBS 113.46 / FGSC A1144 / LSHB Ac4 / NCTC 3858a / NRRL 328 / USDA 3528.7) |
G3Y419 | YANA_ASPNA | MSASRSSTKFSTPAEGSDNGKEFTTPATSTEGHEVPDRPGDALADVAIIGMACRTPGDVRSPDSLWQYLLKKGDASGSLPDWRWEPYRQRHPRNAALLAQTTAKGYFLDDIDHFDAAFFSISPREAEQMDPQQRLALEVAWEALENAGISPPQLAGSNTSVYMGVNSDDYAKLLLEDLPNVDAHMGVGTAYCGIPSRISYILDLMGPSVALDAACASSLVAVHHARQAIRAGETDLAIAGGVNALLGPGLTRVLDEAGAISTDGKCRSFDETASGYGRGEGAGVVILKRLDKALADGDHVLAVLKGSAVASDGKTLGIMAPNARAQLLVAQKALAEAKVSADSINYVEAHATSTSLGDPTETNALAEVYGAGSGRSPSDPCYIGSIKPNIGHLEAGAGVMGLIKAVLVLRHGQVPPQANLKTLNSKIAWNENLLCPPRELVTLPCPGPIHPLRAAVASYGYSGTVSHAVLEAFAGHSEFAERLSQIPTGDDPSPVLLLISAPQARRVSAAAGALKQWLSENEASISLKTVSSTLAQRRAHHRYRHAIVADSVPDAIAALDDVSKEAPNRWVIKDKIDSKAAKGPVWIFSGHGAQWADMGRELFESSPAFEEVVRNLEPIIQDEVGFSAIETLQKGCPDRSDVVQVMTFLMHLGIAAVLEIESGPPSAVVGHSLGEAAAAVVSGALTWREGALVVCRRARLYRELMGQGAMALVRVSAEEARTRIGRQTGVWVAIETSPSACVLSGEVDAIKQLSDRWREEGIEVRMVASDVPFHTPMLERLAKPLYESLRGELHPRVPNRALFSTSQPDPRSEVLRDAQYWVTNMIQPVRLQSAIAAIAQDGFRALVEVSSHPIVTHSVVETMGECTEDPVLVTPTMVRRQPALKSILAATGRLHCFGCAIKFIELDPNAPWNSSVPSTVWHHQPFYRAVSQTSASSQLETTHDPAANNLLGKRIALWGTEEVLYQTRLEEENRPFPGHHPLHGSEIVPAAVLLRTFLQALTPRCVEQVSLQVPVVVSPARKVQIRHNTRNITITSCLEESSSQEDGSWLVNTTAAVGAANVVPSQSRMDLSELRKRLPQKLADSFSIDYLASVGVSAMGFPWQVTHHVASDDEMLARVDANPDNMGGMNDFLTSLMDAATSISSTLWHRQPLLRMPTSVRRVVAVHEIPIPRVVYIHCTKVASTSECTADVTLTGEDGTVLMEIQGMSFAGLEGESFSRKSTAGLVHQIQWPPAALVEDPSEFSHIAFVTPDITDPRLEQYQSQLDALAITSSVHQAASDLPLTSHTSLAVVYLPQTMTDVFDTATRSCNDLVSIIQTITAAASSTTRVFVLTAGTELGHSALLGLSRIIQAEHPDIWGSLIEVEDTFSLPLMAMRYVRDADVIRIKDGVPRIARLRPLPSASSSLTPLTFSPASTYLITGGLGALGLSVAHWMVTQGARRLLLLSRRALPPRSTWSSTHMNNPTIQSILALERLGATVHCLPIDISLPMAASGLRSTLETLNLPSVAGVIHAAGIVSDQLVEQVTPDVLESVLAPKIKGALNLHDVFPPASLDFFVLFSSCGQLLGFPGQASYASGNAFLDGLARSRRAQGDNAISLLWTTWRGMGMGQSANGAMEAELYARGITDITPDEAFRAWSAVASTGGGGTDHAVIVRARVLEGGEPLPHPILTDIATRKAEVVNAGEHPAGSQEVKLSGRELEQHLRDVINGCVSKTLSVKEDEIDDAVALAEMGMDSVMTVNFRMTLQQTLKVPVGPTLIWKCPTVQHLVKHFTKELDA | 2.3.1.165 | null | fatty acid biosynthetic process [GO:0006633]; heterocycle biosynthetic process [GO:0018130]; methylation [GO:0032259]; organic cyclic compound biosynthetic process [GO:1901362]; secondary metabolite biosynthetic process [GO:0044550]; terpenoid biosynthetic process [GO:0016114] | null | 3-oxoacyl-[acyl-carrier-protein] synthase activity [GO:0004315]; 6-methylsalicylic acid synthase activity [GO:0050641]; fatty acid synthase activity [GO:0004312]; methyltransferase activity [GO:0008168]; phosphopantetheine binding [GO:0031177] | PF00698;PF00109;PF02801;PF08659;PF21089;PF00550; | 3.40.47.10;1.10.1200.10;3.30.70.250;3.40.366.10;3.40.50.720;3.10.129.110; | null | null | null | CATALYTIC ACTIVITY: Reaction=acetyl-CoA + 3 H(+) + 3 malonyl-CoA + NADPH = 6-methylsalicylate + 3 CO2 + 4 CoA + H2O + NADP(+); Xref=Rhea:RHEA:12240, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:16526, ChEBI:CHEBI:36658, ChEBI:CHEBI:57287, ChEBI:CHEBI:57288, ChEBI:CHEBI:57384, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349; EC=2.3.1.165; Evidence={ECO:0000269|PubMed:24684908}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:12241; Evidence={ECO:0000269|PubMed:24684908}; | null | PATHWAY: Secondary metabolite biosynthesis; terpenoid biosynthesis. {ECO:0000269|PubMed:24684908}. | null | null | FUNCTION: Non-reducing polyketide synthase; part of the gene cluster that mediates the biosynthesis of yanuthone D, a fungal isoprenoid epoxycyclohexenone that acts as an antibiotic against fungi and bacteria (PubMed:24684908). The first step of the pathway is the synthesis of 6-methylsalicylic acid (6-MSA) by the polyketide synthase yanA (PubMed:24684908). 6-MSA is then converted to m-cresol by the decarboxylase yanB (PubMed:24684908). The cytochrome P450 monooxygenase yanC then catalyzes the oxidation of m-cresol to toluquinol (PubMed:24684908). Epoxidation of toluquinol is then performed by the short chain dehydrogenase yanD, with the help of yanE, and a further prenylation by yanG leads to 7-deacetoxyyanuthone A (PubMed:24684908). The next step is the hydroxylation of C-22 of 7-deacetoxyyanuthone A by the cytochrome P450 monooxygenase yanH to yield 22-deacetylyanuthone A (PubMed:24684908). O-Mevalon transferase yanI then attaches mevalon to the hydroxyl group of 22-deacetylyanuthone A to produce yanuthone E (PubMed:24684908). Finally, the FAD-dependent monooxygenase yanF oxidizes the hydroxyl group at C15 of yanuthone E to form yanuthone D (PubMed:24684908). Furthermore, several branching points in the pathway lead to the production of yanuthones F and G from 7-deacetoxyyanuthone A; yanuthones H and I from 22-deacetylyanuthone A; and yanuthone J from yanuthone E (PubMed:24684908). {ECO:0000269|PubMed:24684908}. | Aspergillus niger (strain ATCC 1015 / CBS 113.46 / FGSC A1144 / LSHB Ac4 / NCTC 3858a / NRRL 328 / USDA 3528.7) |
G4FEF4 | AGAL_THEMA | MEIFGKTFREGRFVLKEKNFTVEFAVEKIHLGWKISGRVKGSPGRLEVLRTKAPEKVLVNNWQSWGPCRVVDAFSFKPPEIDPNWRYTASVVPDVLERNLQSDYFVAEEGKVYGFLSSKIAHPFFAVEDGELVAYLEYFDVEFDDFVPLEPLVVLEDPNTPLLLEKYAELVGMENNARVPKHTPTGWCSWYHYFLDLTWEETLKNLKLAKNFPFEVFQIDDAYEKDIGDWLVTRGDFPSVEEMAKVIAENGFIPGIWTAPFSVSETSDVFNEHPDWVVKENGEPKMAYRNWNKKIYALDLSKDEVLNWLFDLFSSLRKMGYRYFKIDFLFAGAVPGERKKNITPIQAFRKGIETIRKAVGEDSFILGCGSPLLPAVGCVDGMRIGPDTAPFWGEHIEDNGAPAARWALRNAITRYFMHDRFWLNDPDCLILREEKTDLTQKEKELYSYTCGVLDNMIIESDDLSLVRDHGKKVLKETLELLGGRPRVQNIMSEDLRYEIVSSGTLSGNVKIVVDLNSREYHLEKEGKSSLKKRVVKREDGRNFYFYEEGERE | 3.2.1.22 | null | carbohydrate metabolic process [GO:0005975]; glycoside catabolic process [GO:0016139] | null | alpha-galactosidase activity [GO:0004557]; carbohydrate binding [GO:0030246]; protein homodimerization activity [GO:0042803] | PF02065; | 2.60.40.2760;3.20.20.70; | Glycosyl hydrolase 36 family | null | null | CATALYTIC ACTIVITY: Reaction=Hydrolysis of terminal, non-reducing alpha-D-galactose residues in alpha-D-galactosides, including galactose oligosaccharides, galactomannans and galactolipids.; EC=3.2.1.22; Evidence={ECO:0000269|PubMed:17323919, ECO:0000269|PubMed:24237145, ECO:0000269|PubMed:25486100, ECO:0000269|PubMed:26005928, ECO:0000269|PubMed:27783466, ECO:0000269|PubMed:9741105}; | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=0.075 mM for p-nitrophenol-alpha-galactoside (at pH 5.0 and 75 degrees Celsius) {ECO:0000269|PubMed:9741105}; KM=2.1 mM for raffinose (at pH 5.0 and 75 degrees Celsius) {ECO:0000269|PubMed:9741105}; KM=0.11 mM for p-nitrophenyl-alpha-D-galactopyranoside (at pH 5.0 and 37 degrees Celsius) {ECO:0000269|PubMed:24237145}; KM=1.17 mM for melibiose (at pH 5.0 and 37 degrees Celsius) {ECO:0000269|PubMed:25486100}; KM=10.04 mM for raffinose (at pH 5.0 and 37 degrees Celsius) {ECO:0000269|PubMed:25486100}; KM=2.84 mM for stachyose (at pH 5.0 and 37 degrees Celsius) {ECO:0000269|PubMed:25486100}; Vmax=166 umol/min/mg enzyme for 4-nitrophenol-alpha-galactoside (at pH 5.0 and 75 degrees Celsius) {ECO:0000269|PubMed:9741105}; Vmax=103 umol/min/mg enzyme for raffinose (at pH 5.0 and 75 degrees Celsius) {ECO:0000269|PubMed:9741105}; Note=kcat is 176 s(1) for p-nitrophenol-alpha-galactoside (at pH 5.0 and 75 degrees Celsius). kcat is 109 s(1) for raffinose (at pH 5.0 and 75 degrees Celsius) (PubMed:9741105). kcat is 8 s(1) for p-nitrophenyl-alpha-D-galactopyranoside (at pH 5.0 and 37 degrees Celsius) (PubMed:24237145). kcat is 2.33 s(1) for melibiose (at pH 5.0 and 37 degrees Celsius). kcat is 5.0 s(1) for raffinose (at pH 5.0 and 37 degrees Celsius). kcat is 0.53 s(1) for stachyose (at pH 5.0 and 37 degrees Celsius) (PubMed:25486100). {ECO:0000269|PubMed:24237145, ECO:0000269|PubMed:25486100, ECO:0000269|PubMed:9741105}; | null | BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 5.0-5.5 when using synthetic substrate p-nitrophenyl-alpha-D-galactopyranoside. {ECO:0000269|PubMed:9741105}; | BIOPHYSICOCHEMICAL PROPERTIES: Temperature dependence: Optimum temperature is 90-95 degrees Celsius when using synthetic substrate p-nitrophenyl-alpha-D-galactopyranoside. The half-life of thermoinactivation is 6.5 h at 85 degrees Celsius. {ECO:0000269|PubMed:9741105}; | FUNCTION: Hydrolyzes the short-chain alpha-galactosaccharides raffinose, melibiose and stachyose. {ECO:0000269|PubMed:25486100, ECO:0000269|PubMed:9741105}. | Thermotoga maritima (strain ATCC 43589 / DSM 3109 / JCM 10099 / NBRC 100826 / MSB8) |
G4MQX3 | MIP11_PYRO7 | MAEQLILKGTLEGHNGWVTSLATSMENPNMLLSSSRDKTLIIWNLTRDETSYGYPKRSLKGHSHIVSDCVISSDGAYALSASWDKTLRLWELATGTTTRRFVGHTNDVLSVSFSADNRQIVSGSRDRSIKLWNTLGDCKYTITEKGHSEWVSCVRFSPNPQNPVIVSSGWDKLVKVWELSSCKLQTDHIGHTGYINTVTISPDGSLCASGGKDGTTMLWDLNESKHLYSLNANDEIHALVFSPNRYWLCAATASSIIIFDLEKKSKVDELKPEFAAVGKKSREPECISLAWSADGQTLFAGYTDNIIRAWGVMSRA | null | null | G protein-coupled receptor signaling pathway [GO:0007186]; GCN2-mediated signaling [GO:0140469]; mRNA destabilization [GO:0061157]; negative regulation of cell wall integrity MAPK cascade [GO:1903138]; negative regulation of glucose mediated signaling pathway [GO:1902660]; negative regulation of p38MAPK cascade [GO:1903753]; negative regulation of translational frameshifting [GO:2001125]; positive regulation of autophagy [GO:0010508]; positive regulation of conjugation with cellular fusion [GO:0031139]; positive regulation of protein phosphorylation [GO:0001934]; regulation of cytoplasmic translation [GO:2000765]; rescue of stalled ribosome [GO:0072344]; ribosome-associated ubiquitin-dependent protein catabolic process [GO:1990116] | cytosolic small ribosomal subunit [GO:0022627]; nucleus [GO:0005634] | G-protein alpha-subunit binding [GO:0001965]; GDP-dissociation inhibitor activity [GO:0005092]; protein kinase C binding [GO:0005080]; ribosome binding [GO:0043022]; translation regulator activity [GO:0045182] | PF00400; | 2.130.10.10; | WD repeat G protein beta family, Ribosomal protein RACK1 subfamily | null | null | null | null | null | null | null | FUNCTION: Involved in regulating the cell wall integrity and MPS1 activation via its interaction with the MAPKKK MCK1. {ECO:0000269|PubMed:28244240}. | Pyricularia oryzae (strain 70-15 / ATCC MYA-4617 / FGSC 8958) (Rice blast fungus) (Magnaporthe oryzae) |
G4MVZ2 | ACE1_PYRO7 | MRDEMWNTATEPIAIIGSGCKFPGGSTTPSKLWELLKDPKDIVSEIRPDRFDVDKYFHPDHKHHGTSNVRHSYFLEENFKHFDAKFFGIRPQEAMAMDPQQRFLLETVYESLEAAGITISDLKGSQAGVFVGNMGVDYSELLSQDIDAFPTYFAPGTARSILSNRISYFFDLHGPSVTVDTACSSSLVAVHQAVQSLRLGETPVAIVCGANLLLGPAQYIAESKLQMLSPNGRSRMWDASADGYARGEGFASIVLKPLSVALANGDHIECIIRETGCNQDGRTKGITMPSPLAQCKLIQETYKRAGLDLSKSSDRPQYFEAHGTGTPAGDPVEAEAISTAFFGPESGFRRTSHDPKLYVGSVKTVIGHTEGTAGLAGLIKASLAMKAKSIPPNLHLERVNPAVQPFYGNLEIPTRLMDWPEPAPGQPLRASVNSFGFGGANAHVILESYTPAAEVAMVTPTAAAGPVFSPFVFSASSDKALASMLSAYSDYLSLNPTVDLRSVAYTLSQHRSVFDKRAAISAPDLDTLKTKLKARSEEASPSGKTAAVQSLERRPRYLGVFTGQGAQWARMGVDVINASPAARAIFEDLEQSLKTLPEEDRPSWSMLEELLAPPETSRVYQANISQTVCTAVQVMMVQLLRAAGIEFSCVVGHSSGEMAAAYTAGYLSARDAVRAAYFRGVHSQLAKGSNGQPGGMIAVGTNFEDAEELCELDDFKGRLCVAASNSAELVTLSGDLDAVQEVKKILDAEEKFNKQLQVDKGYHSHHMLPCSEPYVASLQKCGIQAQVPGDATACRWISSVYVDDMTNLDCRVQDRYWIENLAKPVMFSQALSHALGGDDKFDSVIEVGPHPALKGPASQTIQACLGERLPYFGCLSRGTDSNEAFAEFLGGVWSTFGSSAVDLAAYERFATGGCDQRLVKGLPSYTWDHDVEHYFQSRLSKVVLHRSTPPNELLGTRLPDDTAGEVRWRNSLHPGELPWLLQHSAQGQTVFPGTGYIATTLEAVKQLFDSSGVQTVEIRDMVIGNALVIEANTGVETLFSLTFINTQTDRITAHFSFCSQQGGSTKLVENASGDLVVLLGEPSEDALPRSFHPGTQMKDIDEERFYEAIDKLGYGYEGPFRALSQLQRRMGAATGLVAIPEKTKHFDQMVLHPAALDAMVQTVLLAYCYPGDTRLQGISLPTGIDCIRFNYGMLSEAARPGCQLPFLSCTAFEGDDVLGGVGGDVGGDVDVFSEDKRFALIQLQGLHTKPLSPPSAATDLQIFSEMEWKTASPEGADMEVRGEKRAYVADLYSSMERVAYFYMRHVDREIGKDRSGLAPHQVRFLEWVDHMCGRVEAGTLPHISRKWDHDTRQDILKIIAKYPDSIDLELMHAVGENLCSVFRGEMNALEPMVKKNMLNRFYSDALGMSPYTEDLARMVGHITHRYPHMNILEVGAGTGGATKVMLRRLQDAFASYTYTDISSGFFADARQVFKAHESKMLFKTLDIEKDIVDQGYEENSFDLVIANLVVHATADLDATMGRLRRLVKPGGHLVLLEITTNDPLRFGFIFGPLPGWWLGGEDGRVHSPCVDVEWWDRVMKRNGFSGADIVTPHHTLGPLSVIMTQAVDHRVQLLRQPTSADFGDFTIDPERLTIVGGVKPLAEGLEQLLKPRYQSVAWIPTLEEVSSHSLPVMGSVLSLVELDEPLFKDMTAQTLEGFKFVFQQSRSVYWITCGASGANPYSNMAAGVARTVALEMRHLRLGFLDFEDAKDATVQRLADRFLEFEILGTLEQQGKLDHLTWYQEPELRFDGKNLLVPRMKLSKDRNGRYNSRRRQLTKNVNPREVPVSLVPTTSGKDFVLKESLSSSSTKHGAQDTVSLRVHYASQRSLRLESSDYLFLVLGTNLSSGEAMFALADSNRSIVHVDRQWTTSYLGNLDHGRHALADLYTQIMASTVVAGLSAGDSLVVLDAETPLSQALSARCAAKGVRLTLLSTTTATSHSEADGTNKTNVRIHPLESRRSIESKLPSNATCFLDLSTNNGSEAAAVINSYIPAQCRVETRDTLTATACQVTRSTSTGGLGPAVGDVLPACWANVEAAGRDLSFFSAAVVTPTELTAAAGNGKTSAPRVGDDALLLITDWTAEAEVGVLVQPADSMVRFRQDKTYWLVGLTGGLALSLCRWMVNRGARYVVMTSRNPKIDKEWLQGVESCGATVKIFSNDVTDRAAVNSAYRTISATLPPIAGVVQGAMVLRDTMFAETTMETIESILGPKVRGSIYLDEIFYSTPLDFFVFLSSVTATSGNPGQSIYAGANMFMNSLAAQRRKRGVAGSSVEIGCIMGNGSVTTILSYEHQKYLFSVGNTWLAEQDFLTMFGEAVLASPPDAPDSVTSVTGLRLQFNDDKPDITWFSNPIFQHLVLQSGNAMQTSLSVARQGTPVKSLLQEAKSSEEVLDILKDAFTAKLVSSLQADPDSNLLEVDLETLGMDSLVAVDLRSWFLAELSVDVPVLKILNGSTARLLLEFVQGLIPASMTPKLDGSDGADAAAQEAPPVAPPVTKPKPDVSVKVPPPHQPVASLKPSGPASPTSPSSATASPGRSRSVASPVTADTPVSPTTSASMASLNDSRKLIRTVPVSFGQSRFWFLGSYNPDPLAFNITSLMRISGPLRTNDFGKAVDKVLNHHEALRTSFVSENDAPVQKIWSSPAFALEQRKIADDESEVVKAYTEVQNTRYNLEAGQTMRIMLLTKSPTKHVLVLGYHHINMDGVSFEVLFSDIEKAYNRTPLDRSVMQFPDFTIREAGEYKSGAWRSELQYWQSKFTSLPEPTPLLSVSKRRTRPVNLSYTTHSVSRRINAEQSQAIHTVGRKFKATPFHFYLSVFKTLIARFSGADDFCIGIADANRKEDKVMGAVGLYLNLLPLRVRSALGQTFGETLADMKKVSQEAFANSKVPFDVLLNELSVPRSSSQTPLFQTFVNYRRGVSEERSFCGCTGAGELISGGQIGYDISLDIVENPGGDALVTLSVQKDLYNVDMANLLLDSYFRLVDSFAKNPATSLNRPAIYDPVAVDKALTLGCGPTLEDSSWPETLIHRIENMSVKYATKFALRNGQNGGLTYSQMIARINDIAAKLIDAKVGTGIVGVMQASTMDFICSILAVWKAGAIYTPLDPRLNSTDRLKAVVDECQPACILVDATTKPLFDSLATNAVQIDVSMVQSSKTLEASPKVAIHAKAPSAAAVFYTSGSTGVPKGITLSHASLTYNIMAATRQFGFKEGVDIMLQQSSFSFDMALAQMLTSLSNGGTLVVVPSHLRGDALGLSQLIVAENVSIVQASPTEYKSLIGVNAQHLKTSKWRVALSGGENMTQSLLEVFRSLGKPDLVLFNGYGPTEATINANTRIVPYHEPNSNPDLPLLTWPNYSISIVDLELNPVPVGVFGEVCIGGAGVGLGYFKNDELTAKAFVADKTAPAEFVAKGWKTKFRTGDLGRLSPDGGLIIEGRIDGDTQVKLRGMRIDLKNIESAILQAGAGKIIDAAVSVRRGGADESEPQYLVGHVVLDADQTPEDSQQDFLAQLIPRLRLPRHMKPSLLVPIRALPQTASHKLDRRALQQLPISDAGQIAKQSQQGAELGSDQARMWKLWKQVIPRDVVSQYSITPQSDFFHVGGTSLLLVNLQSLIAREHGRAPPLHAMFESSTVAAMTDLVLSDDASGSTALIDWEQETSIPTLPPHIIPGGAGNKVSVPPRVVLLTGATGFLGRQLMAFLLRQPSVKRIHCLAVRGGAPPSSAAPFSDPRVSIHAGDLNAPHLGLGEAVAELLFAQADVIIHNGADVSFLKTYATLRATNVGSTRELARLAAPRRIPFHFVSSASITQLTGLDEFGEASMAAWAPPADPRGMSGGYAAAKWASEVLLEKAARAWGLPVVIHRPSSITGEGTNSLDLMGNMFKYIEQLEAVPESDSWKGNFDFVSVENVAADIVQAVVAANVVAAGGVKFIYEAGDIVYPLSMVKDMSEGGAKLPVKTMPLAKWVEKAAEKGLDSMLAEYLIKAASTGTSLAFPRLLKDGN | 2.3.1.-; 6.3.2.- | null | amide biosynthetic process [GO:0043604]; fatty acid biosynthetic process [GO:0006633]; heterocycle biosynthetic process [GO:0018130]; methylation [GO:0032259]; organic cyclic compound biosynthetic process [GO:1901362]; organonitrogen compound biosynthetic process [GO:1901566]; toxin biosynthetic process [GO:0009403] | cytoplasm [GO:0005737] | 3-oxoacyl-[acyl-carrier-protein] synthase activity [GO:0004315]; fatty acid synthase activity [GO:0004312]; isomerase activity [GO:0016853]; ligase activity [GO:0016874]; methyltransferase activity [GO:0008168]; oxidoreductase activity [GO:0016491]; phosphopantetheine binding [GO:0031177] | PF00698;PF00501;PF00668;PF16197;PF00109;PF02801;PF08659;PF08242;PF07993;PF21089;PF00550;PF14765; | 3.30.300.30;3.40.47.10;1.10.1200.10;3.30.559.10;3.40.366.10;3.40.50.12780;3.40.50.720;3.30.559.30;3.10.129.110;3.40.50.150; | NRP synthetase family | null | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:15319478}. Note=Localizes in the cytoplasm of the appressorium. {ECO:0000269|PubMed:15319478}. | null | null | PATHWAY: Secondary metabolite biosynthesis. {ECO:0000269|PubMed:29142718}. | null | null | FUNCTION: Hybrid PKS-NRPS synthetase; part of the gene cluster that mediates the biosynthesis of a tyrosine-derived cytochalasan acting as a fungal signal recognized by resistant rice plants and leads to avirulence in Pi33 resistant rice cultivars (PubMed:12838393, PubMed:15319478, PubMed:17142568, PubMed:18433432, PubMed:29142718). The first step in the pathway is catalyzed by the hybrid PKS-NRPS ACE1, assisted by the enoyl reductase RAP1, that are responsible for fusion of the tyrosine precursor and the polyketide backbone (PubMed:29142718). The polyketide synthase module (PKS) of ACE1 is responsible for the synthesis of the polyketide backbone and the downstream nonribosomal peptide synthetase (NRPS) amidates the carboxyl end of the polyketide with the tyrosine precursor (PubMed:29142718). Because ACE1 lacks a designated enoylreductase (ER) domain, the required activity is provided the enoyl reductase RAP1 (PubMed:29142718). Reduction by the hydrolyase ORFZ, followed by dehydration and intra-molecular Diels-Alder cyclization by the Diels-Alderase ORF3 then yield the required isoindolone-fused macrocycle (Probable). A number of oxidative steps catalyzed by the tailoring enzymes identified within the cluster, including cytochrome P450 monooxygenases CYP1 to CYP4, the FAD-linked oxidoreductase OXR2 and the short-chain dehydrogenase/reductase OXR1, are further required to afford the final cytochalasans that confer avirulence and which have still to be identified (Probable). The monooxygenase CYP1 has been shown to be a site-selective C-18 hydroxylase whereas the function of CYP3 is the site-selective epoxidation of the C-6/C-7 olefin that is present in some intermediate compounds (PubMed:31644300). Finally, SYN2 and RAP2 are not required for avirulence in Pi33 resistant rice cultivars (PubMed:18433432). {ECO:0000269|PubMed:12838393, ECO:0000269|PubMed:15319478, ECO:0000269|PubMed:17142568, ECO:0000269|PubMed:18433432, ECO:0000269|PubMed:29142718, ECO:0000269|PubMed:31644300, ECO:0000305|PubMed:18433432, ECO:0000305|PubMed:29142718}. | Pyricularia oryzae (strain 70-15 / ATCC MYA-4617 / FGSC 8958) (Rice blast fungus) (Magnaporthe oryzae) |
G4MY67 | FNTB_PYRO7 | MRHHTKNLRRRAIFLRTTPRGNMDSSSSVATSTSSSSNHRLVRSSEGSPSAGGDDIEEVIMTPGIATGRVQPAVSVAIPDLFTQLPPVKDDLATSTSKTQDETVAICLPYLAGSDANADVEHNAHGVPHIDRKKHVRFLRNMLRQLPAPFIAADASRPWFLYWSLNAMAILGENVKEDYAESLADTARSMQNESGGFSGGHGQTSHLATTYAVVLALAVVGDEEGLSLIDRRALWKWLCDLKEADGGFRMSLGGEEDVRGAYCAAVIISLLNLPLDLCKDSEAYIRDPTANLFTGLGDYVRKCQTFEGGISGQPDAEAHGAYAFCALGCLSLLGTPSETIPKYLNIERLISWLSSRQYAPEGGFSGRTNKLVDGCYSHWVGGCWPLIEACLNGPVKVSSLDVEPQPLFSREGLMRYILCCCQEQGKRGGLRDKPGKPSDAYHSCYVLSGLSSAQNRWQLVVGDDDMPAWMVSPFPNEEEIFDEKDRVGTVHPVYVIPEDKVAKVQTFFASRDGF | 2.5.1.58 | COFACTOR: Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000250|UniProtKB:P49356}; Note=Binds 1 zinc ion per subunit. {ECO:0000250|UniProtKB:P49356}; | establishment of protein localization to plasma membrane [GO:0061951] | cytoplasm [GO:0005737]; protein farnesyltransferase complex [GO:0005965] | metal ion binding [GO:0046872]; protein farnesyltransferase activity [GO:0004660] | PF00432; | 1.50.10.20; | Protein prenyltransferase subunit beta family | null | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:31250536}. | CATALYTIC ACTIVITY: Reaction=(2E,6E)-farnesyl diphosphate + L-cysteinyl-[protein] = diphosphate + S-(2E,6E)-farnesyl-L-cysteinyl-[protein]; Xref=Rhea:RHEA:13345, Rhea:RHEA-COMP:10131, Rhea:RHEA-COMP:11535, ChEBI:CHEBI:29950, ChEBI:CHEBI:33019, ChEBI:CHEBI:86019, ChEBI:CHEBI:175763; EC=2.5.1.58; Evidence={ECO:0000250|UniProtKB:P22007}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:13346; Evidence={ECO:0000250|UniProtKB:P22007}; | null | null | null | null | FUNCTION: Catalyzes the transfer of a farnesyl moiety from farnesyl diphosphate to a cysteine at the fourth position from the C-terminus of several proteins having the C-terminal sequence Cys-aliphatic-aliphatic-X. The beta subunit is responsible for peptide-binding. {ECO:0000269|PubMed:31250536}. | Pyricularia oryzae (strain 70-15 / ATCC MYA-4617 / FGSC 8958) (Rice blast fungus) (Magnaporthe oryzae) |
G4N0Z0 | PMK1_PYRO7 | MSRANPPSNSSGSRKISFNVSEQYDIQDVVGEGAYGVVCSAIHKPSGQKVAIKKITPFDHSMFCLRTLREMKLLRYFNHENIISILDIQKPRSYETFNEVYLIQELMETDMHRVIRTQDLSDDHCQYFIYQTLRALKAMHSANVLHRDLKPSNLLLNANCDLKVCDFGLARSAASQEDNSGFMTEYVATRWYRAPEIMLTFKEYTKAIDVWSVGCILAEMLSGKPLFPGKDYHHQLTLILDVLGTPTMEDYYGIKSRRAREYIRSLPFKKKVPFRTLFPKTSDLALDLLEKLLAFNPVKRITVEEALKHPYLEPYHDPDDEPTAPPIPEEFFDFDKHKDNLSKEQLKQFIYQEIMR | 2.7.11.24 | COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000255|RuleBase:RU361165}; | cell-to-cell migration by invasive hypha [GO:0140649]; hyphal growth [GO:0030448]; MAPK cascade [GO:0000165]; pheromone-dependent signal transduction involved in conjugation with cellular fusion [GO:0000750]; phosphorylation [GO:0016310]; positive regulation of appressorium formation [GO:0075018]; septin ring assembly [GO:0000921] | cytoplasm [GO:0005737]; nucleus [GO:0005634] | ATP binding [GO:0005524]; MAP kinase activity [GO:0004707]; protein serine kinase activity [GO:0106310] | PF00069; | 1.10.510.10; | Protein kinase superfamily, CMGC Ser/Thr protein kinase family, MAP kinase subfamily | PTM: Phosphorylated by MST7. {ECO:0000269|PubMed:15749760}. | null | CATALYTIC ACTIVITY: Reaction=ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-[protein]; Xref=Rhea:RHEA:17989, Rhea:RHEA-COMP:9863, Rhea:RHEA-COMP:11604, ChEBI:CHEBI:15378, ChEBI:CHEBI:29999, ChEBI:CHEBI:30616, ChEBI:CHEBI:83421, ChEBI:CHEBI:456216; EC=2.7.11.24; Evidence={ECO:0000269|PubMed:8946911}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:17990; Evidence={ECO:0000269|PubMed:8946911}; CATALYTIC ACTIVITY: Reaction=ATP + L-threonyl-[protein] = ADP + H(+) + O-phospho-L-threonyl-[protein]; Xref=Rhea:RHEA:46608, Rhea:RHEA-COMP:11060, Rhea:RHEA-COMP:11605, ChEBI:CHEBI:15378, ChEBI:CHEBI:30013, ChEBI:CHEBI:30616, ChEBI:CHEBI:61977, ChEBI:CHEBI:456216; EC=2.7.11.24; Evidence={ECO:0000269|PubMed:8946911}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:46609; Evidence={ECO:0000269|PubMed:8946911}; | null | null | null | null | FUNCTION: Mitogen-activated protein kinase; part of the MST11-MST7-PMK1 MAP kinase (MAPK) cascade that is essential for appressorium formation, penetration and invasive growth (PubMed:11952120, PubMed:15749760, PubMed:21283781, PubMed:23085322, PubMed:23454094, PubMed:27059015, PubMed:8946911). Central regulator of appressorium development that acts downstream of the cAMP signal (PubMed:23591122, PubMed:8946911). The MST11-MST7-PMK1 MAP kinase cascade transduces signals from the cell surface sensors MDB2 and SHO1 that recognize various surface signals such as surface hydrophobicity, cutin monomers, and rice leaf waxes (PubMed:21283781). Regulates expression of secreted fungal effector proteins implicated of host immune defenses, preventing reactive oxygen species generation and excessive callose deposition at plasmodesmata (PubMed:29567712). Furthermore, controls the hyphal constriction required for fungal growth from one rice cell to the neighboring cell, enabling host tissue colonization and blast disease (PubMed:29567712). Targets downstream of the PMK1-MAPK pathway include transcription factor MST12 and pathogenicity-related genes GAS1 and GAS2, both of which are expressed during appressorium formation, even if regulation of MST12 is not associated with expression of GAS1 or GAS2 (PubMed:11952120, PubMed:12215509, PubMed:23454094). {ECO:0000269|PubMed:11952120, ECO:0000269|PubMed:12215509, ECO:0000269|PubMed:15749760, ECO:0000269|PubMed:21283781, ECO:0000269|PubMed:23085322, ECO:0000269|PubMed:23454094, ECO:0000269|PubMed:23591122, ECO:0000269|PubMed:27059015, ECO:0000269|PubMed:29567712, ECO:0000269|PubMed:8946911}. | Pyricularia oryzae (strain 70-15 / ATCC MYA-4617 / FGSC 8958) (Rice blast fungus) (Magnaporthe oryzae) |
G4N137 | TAS1_PYRO7 | MYNRCCRKVWIQGRVAYRPAYIRQSPPQQTLYRGIDLLPFTTIVMDHQSGFQNPSPSGGLMFSASAKRFISRIVGFVGRGAEVQQKAVGLCPLKTERRRAAAGGLLLPTGLRMGRSIIMSVRPLPFLTGPAPSPDTAAGFKPSPPTGNLVSVSPLSKAQMALWFDYLQHPTSTHYFLTLKVELDKQPLSLDKIIQVIRGLGKQHAMLRTTFHVDTDTDDMSKSYMAVHDDSWDQEIHVLMNDAQLYEALRKPFQLSSESPVRWVVQMKLQPGSARSTYTVYAAGHHIGVDGASMSVLSNQLLEAVASEVEDQPDHSGPHYGDYIQRQARYLRSSAGAAAGRFWLSQLRHTQPFRWRMEPPEEINTPNYRQLDTWNFFPTAEIQEWGNLYKTSWFRVATSIVGLVTAAMAEPQAHHDHALMVAFGARPRGFENNVSHMANTMPVKFPLSSLLRDDATFSDAVKAMGRNVSTAKKHENFPFMSLMEQANRHMDPTLLDFKVAITYSPKLANKSCELFPVEGIWDLFFCFLEQEDGVALGVISNPRVFGAEALGQLQSLFNEVFALSKARPSFKLSDLAFLQNRTPARFISGPALDDVESISKSRVYRLIKARAASQPDLVALMSAEKGVQMTYRELAAQSSQVAHFLQKQRLCKGDAVLVHLERGFAQIVWILGVMEAGACYVALDKTWPAARKEAILRTANGKLLVTDDEQMDFEKQDTTVVFLAPSAAEIASMPQSTCECEVADDDLAYVVFTSGSTGQPKGVMVEHSNLSHYVSATRSLVKTGPHSRMLQLASFAFDAIVLEYAVTLAHGGTLCFANHPEVLVGEYLADVIDSNQVNFFHCTPSVLSTLPAGRRLPSLRIVSVGGEASPPGLLDHWRKRVELLHAYGPTECTVICTLESLTQDESTQTAIDATVIGKALPNLDIRICEEGKLEPLAPNQVGEICVVGPQVSRGYMGQEELTASKFHNITLADGHPSRLYRTGDKGFIDDDGKLHIQGRIGNREIKVRGYRLDLYEVEKNVMAFDPEVTQVSIQQVGESLVALVVPASIDCDRIRSKLLKDMPRYAVPTRFIRVASLPLNTNGKIDHTQASSLAAELVMHDTVLPTVDATPTPTAAVRAVGVTEENLRLKTKENGMERQEMLRRHLTAEVTALWAKLLGSSRQFDPEVGFFDAGGHSLLLTQLHKLIKERFGTGSRPSLLDIFSMSSIRKQVDCLMGIVDQDAMLGSEPTGGSSSRSQSRRSAETSSSSTSAPSSVPVDAERNLYAIVGISCRFPGANTAEQLWNVLMEQRDAITTFCPAENLGFALEENSVFVPRYGMIDALKDFEPSAYSMSDAEAQTIDPQKRVFLDVAADALADAGTSASPGNPLDPVGVFVGAATNTFLSSRDNPGSKPPGDEEPQSFANHYQQLLDCPIGTFASFKLNLTGPVVTLNTACSSALAALHLACASLSHGDCNAAVVGGVSMAYPQEGGYVTARPGGDSSAVFSPSGVCHPLDSRADGCVPADGAAALVIKRLADARADGCRVYAVIEGVAVSADGSDDKAGLGVPSSSGQSRTVEAALRRAGPQALSRLRYVEMHGSGTPWGDALEVQGLKMAFDRLSKTGAAEQSGTGRAQPEADRIYLGSNKGNCGNTEAASGLLSLIKASMALNLGVVPPLPNLAEPNPKCEFEETKFEPLGKQLALAPGDRVMNKRQRIVRSPNWISDATWFVISTVDNLLPKLTPAAVA | 6.3.2.50 | COFACTOR: Name=pantetheine 4'-phosphate; Xref=ChEBI:CHEBI:47942; Evidence={ECO:0000255|PROSITE-ProRule:PRU00258}; | amino acid activation for nonribosomal peptide biosynthetic process [GO:0043041]; fatty acid biosynthetic process [GO:0006633]; secondary metabolite biosynthetic process [GO:0044550] | cytosol [GO:0005829] | 3-oxoacyl-[acyl-carrier-protein] synthase activity [GO:0004315]; ligase activity [GO:0016874]; phosphopantetheine binding [GO:0031177] | PF00501;PF00668;PF00109;PF02801;PF00550; | 3.30.300.30;3.40.47.10;1.10.1200.10;3.30.559.10;3.40.50.12780;3.30.559.30; | NRP synthetase family | null | null | CATALYTIC ACTIVITY: Reaction=acetoacetyl-CoA + ATP + L-isoleucine = AMP + CoA + diphosphate + 2 H(+) + tenuazonic acid; Xref=Rhea:RHEA:52800, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:33019, ChEBI:CHEBI:57286, ChEBI:CHEBI:57287, ChEBI:CHEBI:58045, ChEBI:CHEBI:136842, ChEBI:CHEBI:456215; EC=6.3.2.50; Evidence={ECO:0000269|PubMed:26503170}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:52801; Evidence={ECO:0000269|PubMed:28820236, ECO:0000269|PubMed:32565425}; | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=44.3 mM for isoleucine {ECO:0000269|PubMed:26503170}; KM=1.2 mM for acetoacetyl-CoA {ECO:0000269|PubMed:26503170}; KM=8.1 mM for ATP {ECO:0000269|PubMed:26503170}; KM=0.34 mM for N-acetoacetyl-L-Ile-SNAC (for the KS domain) {ECO:0000269|PubMed:32565425}; | null | null | null | FUNCTION: Hybrid PKS-NRPS synthetase that mediates the biosynthesis of the toxin tenuazonic acid (TeA), an inhibitor of protein biosynthesis on ribosomes by suppressing the release of new protein (PubMed:26503170, PubMed:28820236, PubMed:32565425, PubMed:32765467). TAS1 alone is sufficient for TeA synthesis via the condensation of isoleucine (Ile) with acetoacetyl-CoA by the N-terminal NRPS module and subsequent cyclization conducted by the C-terminal KS domain (PubMed:26503170, PubMed:32565425). {ECO:0000269|PubMed:26503170, ECO:0000269|PubMed:28820236, ECO:0000269|PubMed:32565425, ECO:0000269|PubMed:32765467}. | Pyricularia oryzae (strain 70-15 / ATCC MYA-4617 / FGSC 8958) (Rice blast fungus) (Magnaporthe oryzae) |
G4N2X9 | OXEAS_PYRO7 | MDGAVRLDWTGLDLTGHEIHDGVPIASRVQVMVSFPLFKDQHIIMSSKESPSRKSSTIGQSTRNGSCQADTQKGQLPPVGEKPKPVKENPMKKLKEMSQRPLPTQHGDGTYPTEKKLTGIGEDLKHIRGYDVKTLLAMVKSKLKGEKLKDDKTMLMERVMQLVARLPTESKKRAELTDSLINELWESLDHPPLNYLGPEHSYRTPDGSYNHPFNPQLGAAGSRYARSVIPTVTPPGALPDPGLIFDSIMGRTPNSYRKHPNNVSSILWYWATIIIHDIFWTDPRDINTNKSSSYLDLAPLYGNSQEMQDSIRTFKDGRMKPDCYADKRLAGMPPGVSVLLIMFNRFHNHVAENLALINEGGRFNKPSDLLEGEAREAAWKKYDNDLFQVARLVTSGLYINITLVDYVRNIVNLNRVDTTWTLDPRQDAGAHVGTADGAERGTGNAVSAEFNLCYRWHSCISEKDSKFVEAQFQNIFGKPASEVRPDEMWKGFAKMEQNTPADPGQRTFGGFKRGPDGKFDDDDLVRCISEAVEDVAGAFGARNVPQAMKVVETMGIIQGRKWNVAGLNEFRKHFHLKPYSTFEDINSDPGVAEALRRLYDHPDNVELYPGLVAEEDKQPMVPGVGIAPTYTISRVVLSDAVCLVRGDRFYTTDFTPRNLTNWGYKEVDYDLSVNHGCVFYKLFIRAFPNHFKQNSVYAHYPMVVPSENKRILEALGRADLFDFEAPKYIPPRVNITSYGGAEYILETQEKYKVTWHEGLGFLMGEGGLKFMLSGDDPLHAQQRKCMAAQLYKDGWTEAVKAFYAGMMEELLVSKSYFLGNNKHRHVDIIRDVGNMVHVHFASQVFGLPLKTAKNPTGVFTEQEMYGILAAIFTTIFFDLDPSKSFPLRTKTREVCQKLAKLVEANVKLINKIPWSRGMFVGKPAKDEPLSIYGKTMIKGLKAHGLSDYDIAWSHVVPTSGAMVPNQAQVFAQAVDYYLSPAGMHYIPEIHMVALQPSTPETDALLLGYAMEGIRLAGTFGSYREAAVDDVVKEDNGRQVPVKAGDRVFVSFVDAARDPKHFPDPEVVNPRRPAKKYIHYGVGPHACLGRDASQIAITEMFRCLFRRRNVRRVPGPQGELKKVPRPGGFYVYMREDWGGLFPFPVTMRVMWDDE | 1.-.-.-; 1.13.11.-; 1.13.11.62 | COFACTOR: Name=heme b; Xref=ChEBI:CHEBI:60344; Evidence={ECO:0000255|PROSITE-ProRule:PRU00298}; COFACTOR: Name=heme; Xref=ChEBI:CHEBI:30413; Evidence={ECO:0000250|UniProtKB:P04798}; | fatty acid metabolic process [GO:0006631]; response to oxidative stress [GO:0006979] | null | dioxygenase activity [GO:0051213]; heme binding [GO:0020037]; iron ion binding [GO:0005506]; monooxygenase activity [GO:0004497]; oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen [GO:0016705]; peroxidase activity [GO:0004601] | PF03098;PF00067; | 1.10.630.10;1.10.640.10; | Peroxidase family; Cytochrome P450 family | null | null | CATALYTIC ACTIVITY: Reaction=(9Z)-octadecenoate + O2 = (8R)-hydroperoxy-(9Z)-octadecenoate; Xref=Rhea:RHEA:75655, ChEBI:CHEBI:15379, ChEBI:CHEBI:30823, ChEBI:CHEBI:194403; Evidence={ECO:0000269|PubMed:25121983}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:75656; Evidence={ECO:0000269|PubMed:25121983}; CATALYTIC ACTIVITY: Reaction=(9Z)-octadecenoate + O2 = 10-hydroperoxy-(8E)-octadecenoate; Xref=Rhea:RHEA:75635, ChEBI:CHEBI:15379, ChEBI:CHEBI:30823, ChEBI:CHEBI:77755; Evidence={ECO:0000269|PubMed:25121983}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:75636; Evidence={ECO:0000269|PubMed:25121983}; CATALYTIC ACTIVITY: Reaction=(9Z,12Z)-octadecadienoate + O2 = (8E,10R,12Z)-10-hydroperoxyoctadeca-8,12-dienoate; Xref=Rhea:RHEA:31695, ChEBI:CHEBI:15379, ChEBI:CHEBI:30245, ChEBI:CHEBI:63324; EC=1.13.11.62; Evidence={ECO:0000269|PubMed:25121983}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:31696; Evidence={ECO:0000269|PubMed:25121983}; CATALYTIC ACTIVITY: Reaction=(9Z,12Z,15Z)-octadecatrienoate + O2 = (10R)-hydroperoxy-(8E,12Z,15Z)-octadecatrienoate; Xref=Rhea:RHEA:75643, ChEBI:CHEBI:15379, ChEBI:CHEBI:32387, ChEBI:CHEBI:194405; Evidence={ECO:0000269|PubMed:25121983}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:75644; Evidence={ECO:0000269|PubMed:25121983}; CATALYTIC ACTIVITY: Reaction=(9Z,12Z,15Z)-octadecatrienoate + O2 = (8R)-hydroperoxy-(9Z,12Z,15Z)-octadecatrienoate; Xref=Rhea:RHEA:75647, ChEBI:CHEBI:15379, ChEBI:CHEBI:32387, ChEBI:CHEBI:194406; Evidence={ECO:0000269|PubMed:25121983}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:75648; Evidence={ECO:0000269|PubMed:25121983}; CATALYTIC ACTIVITY: Reaction=(11Z,14Z)-eicosadienoate + O2 = 12-hydroperoxy-(10E,14Z)-eicosadienoate; Xref=Rhea:RHEA:75659, ChEBI:CHEBI:15379, ChEBI:CHEBI:77220, ChEBI:CHEBI:194414; Evidence={ECO:0000269|PubMed:25121983}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:75660; Evidence={ECO:0000269|PubMed:25121983}; CATALYTIC ACTIVITY: Reaction=(11Z,14Z,17Z)-eicosatrienoate + O2 = 12-hydroperoxy-(10E,14Z,17Z)-eicosatrienoate; Xref=Rhea:RHEA:75667, ChEBI:CHEBI:15379, ChEBI:CHEBI:77223, ChEBI:CHEBI:194415; Evidence={ECO:0000269|PubMed:25121983}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:75668; Evidence={ECO:0000269|PubMed:25121983}; CATALYTIC ACTIVITY: Reaction=(12R,13S)-epoxy-(9Z)-octadecenoate + O2 = (12R,13S)-epoxy-(10R)-hydroperoxy-(8E)-octadecenoate; Xref=Rhea:RHEA:75683, ChEBI:CHEBI:15379, ChEBI:CHEBI:194416, ChEBI:CHEBI:194417; Evidence={ECO:0000269|PubMed:25121983}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:75684; Evidence={ECO:0000269|PubMed:25121983}; CATALYTIC ACTIVITY: Reaction=(8E,10R,12Z)-10-hydroperoxyoctadeca-8,12-dienoate = (12S,13R)-epoxy-(10R)-hydroxy-(8E)-octadecenoate; Xref=Rhea:RHEA:75639, ChEBI:CHEBI:63324, ChEBI:CHEBI:194375; Evidence={ECO:0000269|PubMed:25121983}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:75640; Evidence={ECO:0000269|PubMed:25121983}; CATALYTIC ACTIVITY: Reaction=(10R)-hydroperoxy-(8E,12Z,15Z)-octadecatrienoate = 12,13-epoxy-(10R)-hydroxy-(8E,15Z)-octadecadienoate; Xref=Rhea:RHEA:75651, ChEBI:CHEBI:194405, ChEBI:CHEBI:194407; Evidence={ECO:0000269|PubMed:25121983}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:75652; Evidence={ECO:0000269|PubMed:25121983}; CATALYTIC ACTIVITY: Reaction=12-hydroperoxy-(10E,14Z)-eicosadienoate = 10,11-epoxy-12-hydroxy-(14Z)-eicosenoate; Xref=Rhea:RHEA:75663, ChEBI:CHEBI:194408, ChEBI:CHEBI:194414; Evidence={ECO:0000269|PubMed:25121983}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:75664; Evidence={ECO:0000269|PubMed:25121983}; CATALYTIC ACTIVITY: Reaction=12-hydroperoxy-(10E,14Z,17Z)-eicosatrienoate = 14,15-epoxy-12-hydroxy-(10E,17Z)-eicosadienoate; Xref=Rhea:RHEA:75671, ChEBI:CHEBI:194411, ChEBI:CHEBI:194415; Evidence={ECO:0000269|PubMed:25121983}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:75672; Evidence={ECO:0000269|PubMed:25121983}; CATALYTIC ACTIVITY: Reaction=(13R)-hydroperoxy-(9Z,11E)-octadecadienoate = (12R,13R)-epoxy-(11S)-hydroxy-(9Z)-octadecenoate; Xref=Rhea:RHEA:75675, ChEBI:CHEBI:133985, ChEBI:CHEBI:194412; Evidence={ECO:0000269|PubMed:25121983}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:75676; Evidence={ECO:0000269|PubMed:25121983}; CATALYTIC ACTIVITY: Reaction=(13S)-hydroperoxy-(9Z,11E)-octadecadienoate = (12R,13R)-epoxy-(11S)-hydroxy-(9Z)-octadecenoate; Xref=Rhea:RHEA:75679, ChEBI:CHEBI:57466, ChEBI:CHEBI:194412; Evidence={ECO:0000269|PubMed:25121983}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:75680; Evidence={ECO:0000269|PubMed:25121983}; CATALYTIC ACTIVITY: Reaction=12-hydroperoxy-(10E,14Z)-eicosadienoate = 14,15-epoxy-12-hydroxy-(10E)-eicosenoate; Xref=Rhea:RHEA:75703, ChEBI:CHEBI:194409, ChEBI:CHEBI:194414; Evidence={ECO:0000269|PubMed:25121983}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:75704; Evidence={ECO:0000269|PubMed:25121983}; CATALYTIC ACTIVITY: Reaction=12-hydroperoxy-(10E,14Z,17Z)-eicosatrienoate = 10,11-epoxy-12-hydroxy-(14Z,17Z)-eicosadienoate; Xref=Rhea:RHEA:75707, ChEBI:CHEBI:194410, ChEBI:CHEBI:194415; Evidence={ECO:0000269|PubMed:25121983}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:75708; Evidence={ECO:0000269|PubMed:25121983}; | null | null | null | null | FUNCTION: Bifunctional dioxygenase (DOX)-epoxy alcohol synthase (EAS) that converts linoleic acid (18:2n-6) sequentially to 10(R)-hydroperoxy-8(E),12(Z)-octadecadienoic acid (10R-HPODE) and 10R-HPODE further to 12 S(13R)-epoxy-10(R)-hydroxy-8(E)-octadecenoic acid as the end product (PubMed:25121983). Oxygenation at C-10 occurs by retention of the pro-R hydrogen of C-8 of 18:2n-6, suggesting antarafacial hydrogen abstraction and oxygenation. The epoxy alcohol is formed from 10R-HPODE, likely by heterolytic cleavage of the dioxygen bond and subsequent intramolecular epoxidation of the 12(Z) double bond (PubMed:25121983). The DOX domain is also able to oxygenate position C-8 of linoleic acid to produce 8(R)-hydroperoxy-8(E),12(Z)-octadecadienoic acid (8R-HPODE) (PubMed:25121983). Moreover, the DOX domain can oxygenate alpha-linolenic acid (18:3n-3) at C-8 or C-10 to produce respectively 8HOTrE and 10HOTrE, oleic acid (18:1n-9) at C-8 or C-10 to produce respectively 8-H(P)OME and 10-H(P)OME (with 8R stereoisomer to over 95%), eicosadienoic acid (20:2n-6) at C-10 or C-12 to produce respectively 10(11)-epoxy-12-hydroxy-14(Z)-eicosenoic acid and 14(15)-epoxy-12-hydroxy-10(E)-eicosenoic acid, as well as eicosatrienoic acid (20:3n-3) at C-10 or C-12 to produce respectively 10(11)-epoxy-12-hydroxy-14(Z),17(Z)-eicosadienoic acid and 14(15)-epoxy-12-hydroxy-14(Z),17(Z)-eicosadienoic acid (PubMed:25121983). On the other side, the enzyme EAS domain can also catalyze the conversion of 10HOTrE into 12(13)-epoxy-10(R)-hydroxy-8(E),15(Z)-octadecadienoic acid, 13-R-HPODE into the stereoisomers of 12(13)-epoxy-11-hydroxy-9(Z)-octadecenoic acids (erythro/threo, 1:4), as well as 13S-HPODE into the stereoisomers of 12(13)-epoxy-11-hydroxy-9(Z)-octadecenoic acids (erythro/threo, 1:4) (EAS activity) (PubMed:25121983). Gamma-linolenic acid (18:3n-6) is not a substrate (PubMed:25121983). {ECO:0000269|PubMed:25121983}. | Pyricularia oryzae (strain 70-15 / ATCC MYA-4617 / FGSC 8958) (Rice blast fungus) (Magnaporthe oryzae) |
G4N374 | MPS1_PYRO7 | MSDLQGRKIFKVFNQDFIVDERYTVTKELGQGAYGIVCAAVNNQTSEGVAIKKVTNVFSKKILAKRALREIKLLQHFRGHRNITCLYDMDIPRPDNFNETYLYEELMECDLAAIIRSGQPLTDAHFQSFIYQILCGLKYIHSANVLHRDLKPGNLLVNADCELKICDFGLARGFSVDPEENAGYMTEYVATRWYRAPEIMLSFQSYTKAIDVWSVGCILAELLGGRPFFKGRDYVDQLNQILHILGTPNEETLSRIGSPRAQEYVRNLPFMAKKPFPTLFPNANPDALDLLDRMLAFDPSSRISVEQALEHPYLHIWHDASDEPDCPTTFNFDFEVVEDVGEMRKMILDEVYRFRQLVRTAPGAGGHGAPHAPQVPIPAGAGQGQWKAEDPRPQEYVGQMNDLEAELAGGLDQRR | 2.7.11.24 | COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000255|RuleBase:RU361165}; | negative regulation of glucose mediated signaling pathway [GO:1902660]; negative regulation of mitotic cytokinesis [GO:1902413]; phosphorylation [GO:0016310]; positive regulation of calcium ion import across plasma membrane [GO:1905665]; positive regulation of calcium-mediated signaling [GO:0050850]; positive regulation of developmental process [GO:0051094] | cytoplasm [GO:0005737]; nucleus [GO:0005634] | ATP binding [GO:0005524]; MAP kinase activity [GO:0004707]; protein serine kinase activity [GO:0106310] | PF00069; | 1.10.510.10; | Protein kinase superfamily, Ser/Thr protein kinase family, MAP kinase subfamily | null | null | CATALYTIC ACTIVITY: Reaction=ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-[protein]; Xref=Rhea:RHEA:17989, Rhea:RHEA-COMP:9863, Rhea:RHEA-COMP:11604, ChEBI:CHEBI:15378, ChEBI:CHEBI:29999, ChEBI:CHEBI:30616, ChEBI:CHEBI:83421, ChEBI:CHEBI:456216; EC=2.7.11.24; Evidence={ECO:0000305|PubMed:9770551}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:17990; Evidence={ECO:0000305|PubMed:9770551}; CATALYTIC ACTIVITY: Reaction=ATP + L-threonyl-[protein] = ADP + H(+) + O-phospho-L-threonyl-[protein]; Xref=Rhea:RHEA:46608, Rhea:RHEA-COMP:11060, Rhea:RHEA-COMP:11605, ChEBI:CHEBI:15378, ChEBI:CHEBI:30013, ChEBI:CHEBI:30616, ChEBI:CHEBI:61977, ChEBI:CHEBI:456216; EC=2.7.11.24; Evidence={ECO:0000305|PubMed:9770551}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:46609; Evidence={ECO:0000305|PubMed:9770551}; | null | null | null | null | FUNCTION: Mitogen-activated protein kinase; part of the MCK1-MKK2-MPS1 MAP kinase (MAPK) signal transduction cascade that is essential for cell wall integrity and plant infection, but not for plant defense responses (PubMed:18344407, PubMed:22321443, PubMed:28424497, PubMed:28799700, PubMed:9770551). Beside its role in pathogenesis, the MPS1 cascade is active in conidiation and cellular stress responses (PubMed:9770551). Targets downstream of the MPS1-MAPK pathway include transcription factors MIG1 and SWI6, as well as GSK1 and MPG1 (PubMed:18344407, PubMed:22321443, PubMed:28424497). {ECO:0000269|PubMed:18344407, ECO:0000269|PubMed:22321443, ECO:0000269|PubMed:28424497, ECO:0000269|PubMed:28799700, ECO:0000269|PubMed:9770551}. | Pyricularia oryzae (strain 70-15 / ATCC MYA-4617 / FGSC 8958) (Rice blast fungus) (Magnaporthe oryzae) |
G4N4J5 | LIDS_PYRO7 | MASSSSSGSSTRSSSPSDPPSSFFQKLGAFLGLFSKPQPPRPDYPHAPGNSAREEQTDITEDIQKLGFKDVETLLLYLNSSVKGVNDDKQLLLERLIQLLSKLPPTSTNGKKVTDGLITGLWESLDHPPVSSLGEKYRFREADGSNNNIHNPTLGVAGSHYARSAKPMVYQNPNPPAPETIFDTLMARDPAKFRPHPNQISSVLFYFATIITHDIFQTSSRDPSINLTSSYLDLSPLYGRNLEEQLSVRAMKDGLLKPDTFCSKRVHGFPPGVGVLLIMFNRFHNYVVTSLAKINEGNRFKKPVGDDTAAWEKYDNDLFQTGRLITCGLYVNIVLVDYVRTILNLNRVDSSWILDPRTEEGKSLLSKPTPEAVGNQVSVEFNLIYRWHCGMSQRDDKWTTDMLTEALGGKDPATATLPEFFGALGRFESSFPNEPEKRTLAGLKRQEDGSFEDEGLIKIMQESIEEVAGAFGPNHVPACMRAIEILGMNQARSWNVATLNEFREFIGLKRYDTFEDINPDPKVANLLAEFYGSPDAVELYPGINAEAPKPVIVPGSGLCPPSTTGRAILSDAVTLVRGDRFFTVDYTPRNLTNFGYQEAATDKSVDNGNVIYKLFFRAFPNHYAQNSIYAHFPFVIPSENKKIMESLGLADKYSWQPPQRKPATQMIRSHAAAVKILNNQKDFKVVWGESIGFLTKFPTGENPGLGFALAGDAPANQQSRDQLMKCIFSPKAWEDEVRQFCEATTWDLLRRYSAKVQDKGPHLKVHTHEIDVIRDVISLANARFFAAVYSLPLKTENGDDGVYSDHEMYRSLMLIFSAIFWDNDVSKSFKLRRDARAATQKLGALVEKHIVEMGSLFHSFKHSHSAVSDKTNGLANGGANGHANGNANGHTNGNGIHQNGGAAPSMLRSYGDLMLRRMIEAYGEGKSVKEAVYGQIMPSIAAGTANQTQIMAQCLDYYMSDDGAEHLPEMKRLASLETPEAFNTLMKYLFEGARIRNTTAVPRLVATDQTVEDNIPCLPDPKDSTFLRPIPNPQQAETTRTVKLSRGSMVLVDLTVAAHDATAFPDPEKVRLDRDLDSYTFFGLGPHRCAGDKVVRITMTAVFKVLLQLDGLRRAEGGRGVFKSLPASQWNGQAGRVAGEKPQWSGLRTYVNADESAFSQTPMNMKIRWDD | 1.13.11.60; 5.4.4.6 | COFACTOR: Name=heme b; Xref=ChEBI:CHEBI:60344; Evidence={ECO:0000255|PROSITE-ProRule:PRU00298}; COFACTOR: Name=Ca(2+); Xref=ChEBI:CHEBI:29108; Evidence={ECO:0000255|PROSITE-ProRule:PRU00298}; COFACTOR: Name=heme; Xref=ChEBI:CHEBI:30413; Evidence={ECO:0000250|UniProtKB:P04798}; | fatty acid metabolic process [GO:0006631]; response to oxidative stress [GO:0006979] | null | dioxygenase activity [GO:0051213]; heme binding [GO:0020037]; iron ion binding [GO:0005506]; isomerase activity [GO:0016853]; monooxygenase activity [GO:0004497]; oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen [GO:0016705]; peroxidase activity [GO:0004601] | PF03098; | 1.10.630.10;1.10.640.10; | Peroxidase family; Cytochrome P450 family | null | null | CATALYTIC ACTIVITY: Reaction=(9Z,12Z)-octadecadienoate + O2 = (8R,9Z,12Z)-8-hydroperoxyoctadeca-9,12-dienoate; Xref=Rhea:RHEA:25395, ChEBI:CHEBI:15379, ChEBI:CHEBI:30245, ChEBI:CHEBI:58659; EC=1.13.11.60; Evidence={ECO:0000269|PubMed:20023302, ECO:0000269|PubMed:25121983}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:25396; Evidence={ECO:0000269|PubMed:20023302, ECO:0000269|PubMed:25121983}; CATALYTIC ACTIVITY: Reaction=(8R,9Z,12Z)-8-hydroperoxyoctadeca-9,12-dienoate = (7S,8S,9Z,12Z)-7,8-dihydroxyoctadeca-9,12-dienoate; Xref=Rhea:RHEA:25399, ChEBI:CHEBI:57468, ChEBI:CHEBI:58659; EC=5.4.4.6; Evidence={ECO:0000269|PubMed:20023302, ECO:0000269|PubMed:25121983}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:25400; Evidence={ECO:0000269|PubMed:20023302, ECO:0000269|PubMed:25121983}; | null | null | null | null | FUNCTION: 7,8-linoleate diol synthase is a bifunctional enzyme that converts linoleic acid (18:2n-6) into 8-hydroperoxy-8(E),12(Z)-octadecadienoic acid (8-HPODE) and then catalyzes the isomerization of the resulting hydroperoxide to 7,8-dihydroxy-9(Z),12(Z)-octadecadienoic acid (7,8-DiHODE). {ECO:0000269|PubMed:20023302, ECO:0000269|PubMed:25121983}. | Pyricularia oryzae (strain 70-15 / ATCC MYA-4617 / FGSC 8958) (Rice blast fungus) (Magnaporthe oryzae) |
G4N4W3 | MSB2_PYRO7 | MHNFSKLAVAFVAAASFASAEPETKAKVERPIIYFPRHIKRQFANTTTPASEASSSTSRPPPIPVPETSSFSSSASSSSAQELTASRQPTSIDEFFSTLSDALTTDSTPFSQRPATSGAGRSSATGDVTPIIVPSSASPPSTAVKPGSVSALTTSQNSTSAATSESVTSPGSTSGPAGTPESSSASDFTSAVATSRASTATSNTGLIPETTILPTTATSNTGLIPETTILPTTASLSTAESAVTPSITSSASSSGILIAPTGVVTPTSSSSTEDPVFDGIGTLISSIVSSVSTVLQPNGTAPVTTTPNTSVDVATTPVDIASTTASDTLSPTTAVVSTTGPVTSVQTLPPVSTPTANGTVTSPPVDSQTTVLPTTTPGLSSDTIVTSPGVTANSTQVPTTVPTTIPTTQPPVTEPTITPTVLPPSPNNTVPSNTTTQLPPTQAPTLTQLPTTTTSPALTTPATTPSVAPTSATSSANSNDDWLPTTIIVQAPLPSTTGSSTNAPSSAPTVLPSDLPKIINPSDDITEPLGPDMMEIQVAFKFALNYRFITNENPNAGAQIFEYLPKSLKYMEGLTEEQKKRLQVLRVVPLNTEQQLGYVTSVAIATWPKAFFPQLRLDVKTPFSQFYQNTSNGMLAHNLTMLVNPAIDILPGATLDGKPAGAGSGTGGNGSNGPNDVFNNDNNSTNQSATQRGTVAGIAFGAVSLAAAYGAAMFIVARRYKKKRQAHRRSSSVATPSEMRQSGSPALMGGALLSRDFTHYGGVMGPAGGRESHGSNGSGRSAGNSARTAGISAPVAQENSLGWN | null | null | cellular bud site selection [GO:0000282]; fungal-type cell wall organization [GO:0031505]; hyperosmotic response [GO:0006972]; osmosensory signaling pathway via Sho1 osmosensor [GO:0007232]; signal transduction involved in filamentous growth [GO:0001402] | cell surface [GO:0009986]; extracellular region [GO:0005576]; plasma membrane [GO:0005886]; site of polarized growth [GO:0030427]; vacuolar membrane [GO:0005774] | osmosensor activity [GO:0005034] | null | null | HKR1/MSB2 family | null | SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:21283781}; Single-pass membrane protein {ECO:0000255}. Vacuole membrane {ECO:0000269|PubMed:21283781}; Single-pass membrane protein {ECO:0000255}. Note=During conidium germination and appressorium formation, localizes at the cell membrane and in vacuoles (PubMed:21283781). In mature appressoria, mainly localized to vacuole-like structures (PubMed:21283781). {ECO:0000269|PubMed:21283781}. | null | null | null | null | null | FUNCTION: MSB2 and SHO1 have overlapping functions in recognizing various surface signals for MAPK PMK1 activation and appressorium formation (PubMed:21283781). While MSB2 is critical for sensing surface hydrophobicity and cutin monomers, SHO1 may play a more important role in recognizing rice leaf waxes (PubMed:21283781). {ECO:0000269|PubMed:21283781}. | Pyricularia oryzae (strain 70-15 / ATCC MYA-4617 / FGSC 8958) (Rice blast fungus) (Magnaporthe oryzae) |
G4N6Z6 | MKK2_PYRO7 | MHDQEAANGGETATNPISSLDVPTPPATTIPTLSSPAPLLRPAIPGARSAGARTPRLGLAIPPSPNVKPVGGAPGRPPLPTLHLATPMGSSVTPHEQPPGRPSIVTQQGQSASGGSESSAAHSRSGSFGPLDGRTSNPTSAGSQYSALSFASHFGIGSTRPQGTPDPASAVGSIYSERSDGGAGMDKDGNLKGLENFDKLTIDKARTADVEDLDVEGWKIASMEKRIVELGGLGEGAGGAVTRCKLTGGKTVFALKVITANPDPDVKKQIMRELDFNIQCASEHICRYYGAFEDPSTATISIAMEFCEGGSLDSIYKEVKRLGGRTGEKVLGKIAEGVLRGLTYLNSKKIIHRDIKPSNILLCRNGDVKLCDFGVSGDFGTKGEANTFIGTSYYMAPERITGQSYTITSDVWSTGVTLLEVAQHRFPFPADGTEMAPRAGLIDLLTYIVRQPIPKLKDEPSAQISWSENFKYFIECCLEKDPQRRASPWRMLEHPWMVDMKSKRVNMTRYLAQVWGWDDKGEAKPAE | 2.7.11.24 | null | MAPK cascade [GO:0000165]; phosphorylation [GO:0016310]; positive regulation of appressorium formation [GO:0075018]; positive regulation of calcium-mediated signaling [GO:0050850] | cytoplasm [GO:0005737]; division septum [GO:0000935] | ATP binding [GO:0005524]; MAP kinase activity [GO:0004707]; MAP kinase kinase activity [GO:0004708] | PF00069; | 1.10.510.10; | Protein kinase superfamily, STE Ser/Thr protein kinase family, MAP kinase kinase subfamily | null | null | CATALYTIC ACTIVITY: Reaction=ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-[protein]; Xref=Rhea:RHEA:17989, Rhea:RHEA-COMP:9863, Rhea:RHEA-COMP:11604, ChEBI:CHEBI:15378, ChEBI:CHEBI:29999, ChEBI:CHEBI:30616, ChEBI:CHEBI:83421, ChEBI:CHEBI:456216; EC=2.7.11.24; Evidence={ECO:0000305|PubMed:28244240}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:17990; Evidence={ECO:0000305|PubMed:28244240}; CATALYTIC ACTIVITY: Reaction=ATP + L-threonyl-[protein] = ADP + H(+) + O-phospho-L-threonyl-[protein]; Xref=Rhea:RHEA:46608, Rhea:RHEA-COMP:11060, Rhea:RHEA-COMP:11605, ChEBI:CHEBI:15378, ChEBI:CHEBI:30013, ChEBI:CHEBI:30616, ChEBI:CHEBI:61977, ChEBI:CHEBI:456216; EC=2.7.11.24; Evidence={ECO:0000305|PubMed:28244240}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:46609; Evidence={ECO:0000305|PubMed:28244240}; | null | null | null | null | FUNCTION: Mitogen-activated protein kinase kinase; part of the MCK1-MKK2-MPS1 MAP kinase (MAPK) signal transduction cascade that is essential for appressorium formation, penetration and invasive growth (PubMed:28244240). Beside its role in pathogenesis, the MPS1 cascade is active in conidiation and cellular stress responses (By similarity). Targets downstream of the the MPS1-MAPK pathway include transcription factors MIG1 and SWI6, as well as GSK1 and MPG1 (PubMed:28244240). {ECO:0000250|UniProtKB:G4N0Z0, ECO:0000269|PubMed:28244240}. | Pyricularia oryzae (strain 70-15 / ATCC MYA-4617 / FGSC 8958) (Rice blast fungus) (Magnaporthe oryzae) |
G4N7S6 | HAT1_PYRO7 | MAESDLWSVDANSALELSLVEPTEDGLTTVTRFHPRFTYPLFGEEEQIFGYQDLKINLQYHAPDMRPNVKITHSKKFKSIGETQPTDLDALLQGYLPPVAFAKKREFEDAIRLMPADWTPPGEILSEFDGVDGAKFEIRRSNLADDASRQIIDRVQLLILLFIEGGSYIGTDTTDSLDRWDIFFLYNIKPSTTDGTSRYQFAGYSTVYKFFPLQRFPLEPKEAHENLELPSGEFPFSNLRSRTRISQFLILPPFQKSGNGSRLYRTIYDYCLRDPNVIEVTVEDPNEAFDDMRDVADLDFLRQKSEFTDLRINTDIHIPKQGAAPRGVVDEVKSEEARCLYRIAPRQFSRVLEMHLMSRLAETVRPTLVDDKVVAKPTKIETHEYDLWKLFVKQRLYRHNKEVLSQLDRHDRIERLNETLGSVELEYARILALAERRTQATSSNLKRKLDDDENTEGSSSKKARVEDA | 2.3.1.48 | null | autophagy [GO:0006914]; DNA repair [GO:0006281]; subtelomeric heterochromatin formation [GO:0031509] | chromosome, telomeric region [GO:0000781]; nucleus [GO:0005634]; phagophore assembly site [GO:0000407] | histone H4 acetyltransferase activity [GO:0010485] | PF10394; | 3.40.630.30;3.90.360.10; | HAT1 family | PTM: Phosphorylated at Ser-8 by GSK1 in the nucleus which impairs its translocation to the cytoplasm through interfering the interaction between HAT1 and SSB1. Dephosphorylation under nutrient starvation conditions promotes the interaction between HAT1 and SSB1 and results in the translocation of HAT1 from the nucleus to the cytoplasm in order to acetylate ATG3 and ATG9. {ECO:0000269|PubMed:30776962}. | SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:30776962}. Cytoplasm {ECO:0000269|PubMed:30776962}. Preautophagosomal structure {ECO:0000269|PubMed:30776962}. Note=Is only present in the nucleus under nutrient-rich condition, and translocates from the nucleus to the cytoplasm with the assistance of SSB1 during germination or upon starvation. {ECO:0000269|PubMed:30776962}. | CATALYTIC ACTIVITY: Reaction=acetyl-CoA + L-lysyl-[protein] = CoA + H(+) + N(6)-acetyl-L-lysyl-[protein]; Xref=Rhea:RHEA:45948, Rhea:RHEA-COMP:9752, Rhea:RHEA-COMP:10731, ChEBI:CHEBI:15378, ChEBI:CHEBI:29969, ChEBI:CHEBI:57287, ChEBI:CHEBI:57288, ChEBI:CHEBI:61930; EC=2.3.1.48; Evidence={ECO:0000269|PubMed:30776962}; | null | null | null | null | FUNCTION: Catalytic component of the histone acetylase B (HAT-B) complex. Has intrinsic substrate specificity that modifies lysine in recognition sequence GXGKXG (By similarity). Involved in DNA double-strand break repair (PubMed:30776962). Required for appressorium turgor pressure, autophagy and conidial nuclear degradation (PubMed:30776962). During the germination process and upon starvation conditions, translocates from the nucleus to the cytoplasm where it acetylates ATG3 at 'lys-262' and 'Lys-267', thus influencing autophagy through controlling ATG3-ATG8 interaction (PubMed:30776962). Also acetylates ATG9 at 'Lys-621' to regulate ATG9 binding to vesicles, which is also important for autophagy and pathogenicity (PubMed:30776962). {ECO:0000250|UniProtKB:Q12341, ECO:0000269|PubMed:30776962}. | Pyricularia oryzae (strain 70-15 / ATCC MYA-4617 / FGSC 8958) (Rice blast fungus) (Magnaporthe oryzae) |
G4NAP4 | MNLOX_PYRO7 | MRVLVWIAGLAPLAVAVPSSSYRVAVAARADNTSASVAPSQNVSGAAPPELVVYTLPCEDGNSTARTAEIRLKQATLLYGPSLLGNASYFPGGPLGDAISLRDQTVWEGAAVVQSLRAFTDAAKVAANIKQNGGLNSLDDFKVLYQDGWKGSVPQGIARGQSENYTSDLLFSMERLSVNPYILKRLHPTEDALPFQVDRATVKQLTKTSLKALHAAGRLFVADHSYQRNYTRLANRYSAACTALFYLDPRSNQFLPLAIKTNVGADLTYTPLDTDNNNWLLAKIMFNNNDLFHGQIFHVAYPHAIAEIVHLAALRTMSARHPVLALMERLMYQAYAVRPLGERVLFNKGGLFEQNFAYPQDMVYKFVGDSYPTTGRWRAGYLDTDVRARGLVDADYGPELPHFPFYEDGSRLVEVIRRFVRSFVDATYHESDEMVAKDAELQAWVAEANGPAGVEDFEPGPLDTRERLVEVLTHMAWLTGCAHHVLNQGEPVTASGVLPMHPTALYAPVPTSKANTTADLLGYLPSAQKSVDQVTLLARFNRPDVVPTNQTLRYMFAAPQLLLGNGEAYRRANQRFVRAMGRISDEVKARRFDDRGLSQGMPFIWQALDPGNIPFYLSV | 1.13.11.-; 1.13.11.45; 1.13.11.58 | COFACTOR: Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000269|PubMed:26783260}; Note=Three His residues, the carboxyl oxygen of the C-terminal Ile or Val residue, and a fifth residue, usually Asn, ligate the metal, which binds water to form a catalytic base Mn(2+)OH(2) for hydrogen abstraction. {ECO:0000250|UniProtKB:Q8X151}; | arachidonic acid metabolic process [GO:0019369]; hepoxilin biosynthetic process [GO:0051122]; linoleic acid metabolic process [GO:0043651]; lipid oxidation [GO:0034440]; lipoxygenase pathway [GO:0019372] | extracellular region [GO:0005576] | linoleate 11-lipoxygenase activity [GO:0050584]; linoleate 9S-lipoxygenase activity [GO:1990136]; metal ion binding [GO:0046872] | PF00305; | 3.10.450.60; | Lipoxygenase family, Manganese lipoxygenase subfamily | null | SUBCELLULAR LOCATION: Secreted {ECO:0000250|UniProtKB:Q8X151}. | CATALYTIC ACTIVITY: Reaction=(9Z,12Z)-octadecadienoate + O2 = (9S)-hydroperoxy-(10E,12Z)-octadecadienoate; Xref=Rhea:RHEA:30291, ChEBI:CHEBI:15379, ChEBI:CHEBI:30245, ChEBI:CHEBI:60955; EC=1.13.11.58; Evidence={ECO:0000269|PubMed:26264916}; CATALYTIC ACTIVITY: Reaction=(9Z,12Z)-octadecadienoate + O2 = (11S)-hydroperoxy-(9Z,12Z)-octadecadienoate; Xref=Rhea:RHEA:18993, ChEBI:CHEBI:15379, ChEBI:CHEBI:30245, ChEBI:CHEBI:57467; EC=1.13.11.45; Evidence={ECO:0000269|PubMed:26264916}; CATALYTIC ACTIVITY: Reaction=(9Z,12Z)-octadecadienoate + O2 = (13R)-hydroperoxy-(9Z,11E)-octadecadienoate; Xref=Rhea:RHEA:51240, ChEBI:CHEBI:15379, ChEBI:CHEBI:30245, ChEBI:CHEBI:133985; Evidence={ECO:0000269|PubMed:26264916}; CATALYTIC ACTIVITY: Reaction=(9Z,12Z,15Z)-octadecatrienoate + O2 = (9S)-hydroperoxy-(10E,12Z,15Z)-octadecatrienoate; Xref=Rhea:RHEA:51248, ChEBI:CHEBI:15379, ChEBI:CHEBI:32387, ChEBI:CHEBI:60962; Evidence={ECO:0000269|PubMed:26264916}; CATALYTIC ACTIVITY: Reaction=(9Z,12Z,15Z)-octadecatrienoate + O2 = (11R)-hydroperoxy-(9Z,12Z,15Z)-octadecatrienoate; Xref=Rhea:RHEA:51252, ChEBI:CHEBI:15379, ChEBI:CHEBI:32387, ChEBI:CHEBI:133989; Evidence={ECO:0000269|PubMed:26264916, ECO:0000269|PubMed:26783260}; CATALYTIC ACTIVITY: Reaction=(9Z,12Z,15Z)-octadecatrienoate + O2 = (13R)-hydroperoxy-(9Z,11E,15Z)-octadecatrienoate; Xref=Rhea:RHEA:51244, ChEBI:CHEBI:15379, ChEBI:CHEBI:32387, ChEBI:CHEBI:133987; Evidence={ECO:0000269|PubMed:26264916}; CATALYTIC ACTIVITY: Reaction=(9S)-hydroperoxy-(10E,12Z,15Z)-octadecatrienoate + O2 = (9S,16S)-dihydroperoxy-(10E,12Z,14E)-octadecatrienoate; Xref=Rhea:RHEA:51256, ChEBI:CHEBI:15379, ChEBI:CHEBI:60962, ChEBI:CHEBI:133991; Evidence={ECO:0000269|PubMed:26264916, ECO:0000269|PubMed:26783260}; | null | null | null | null | FUNCTION: Lipoxygenase that metabolizes linoleic and alpha-linolenic acids to 9S-, 11- and 13R-hydroperoxy fatty acids. At the end of lipoxygenation, the intermediate product 11S-HPODE from linoleic acid is then transformed into 9S-HPODE and 13R-HPODE as the final products. The intermediate product 11R-HPOTrE from alpha-linolenic acid is transformed into 9S-HPOTrE and 13R-HPOTrE as the final products. 9S-HPOTrE is further oxidized by the enzyme to 9S,16S-DiHPOTrE as the end product. {ECO:0000269|PubMed:26264916}. | Pyricularia oryzae (strain 70-15 / ATCC MYA-4617 / FGSC 8958) (Rice blast fungus) (Magnaporthe oryzae) |
G4NEB8 | MST7_PYRO7 | MADPFAPRTMKRRNVKGLALTPAAPKPPPTAENAPIHRDSDQHAQLEIGIEFNLDLRPEDLEVIKDLGSGNGGTVSKVRHIPTNTVMARKVIHVEAKREMRKRIVRELQIMHSCNSEYIVTFYGAFLNENNDVIMCMEYADVGSLDRVSRVFGPIRVDVLGKIAEATLGGLTYLYAKHHIMHRDIKPSNILVNSRGSIKLCDFGVSGELINSIADTFVGTSTYMAPERIQGEKYTVKSDVWSFGLSIMELAIGKFPFAASEQLSDAESAPAGILDLLQQIVHEPAPKLPKSDAFPQILEDMIQKCLYKNPDDRPTPEELFERDPFVQAAKRTPVDLREWAFGLMERDNRKSHLAPQLSPATADLLRSSDSPTATYHGDDRPLETPTSAYRVDPRRGPAEGSAGLADQVDRLYIRD | 2.7.11.24 | null | MAPK cascade [GO:0000165]; phosphorylation [GO:0016310]; positive regulation of appressorium formation [GO:0075018] | null | ATP binding [GO:0005524]; MAP kinase activity [GO:0004707]; MAP kinase kinase activity [GO:0004708] | PF00069; | 1.10.510.10; | Protein kinase superfamily, STE Ser/Thr protein kinase family, MAP kinase kinase subfamily | null | null | CATALYTIC ACTIVITY: Reaction=ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-[protein]; Xref=Rhea:RHEA:17989, Rhea:RHEA-COMP:9863, Rhea:RHEA-COMP:11604, ChEBI:CHEBI:15378, ChEBI:CHEBI:29999, ChEBI:CHEBI:30616, ChEBI:CHEBI:83421, ChEBI:CHEBI:456216; EC=2.7.11.24; Evidence={ECO:0000269|PubMed:15749760}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:17990; Evidence={ECO:0000269|PubMed:15749760}; CATALYTIC ACTIVITY: Reaction=ATP + L-threonyl-[protein] = ADP + H(+) + O-phospho-L-threonyl-[protein]; Xref=Rhea:RHEA:46608, Rhea:RHEA-COMP:11060, Rhea:RHEA-COMP:11605, ChEBI:CHEBI:15378, ChEBI:CHEBI:30013, ChEBI:CHEBI:30616, ChEBI:CHEBI:61977, ChEBI:CHEBI:456216; EC=2.7.11.24; Evidence={ECO:0000269|PubMed:15749760}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:46609; Evidence={ECO:0000269|PubMed:15749760}; | null | null | null | null | FUNCTION: Mitogen-activated protein kinase kinase; part of the MST11-MST7-PMK1 MAP kinase (MAPK) cascade that is essential for appressorium formation, penetration and invasive growth (PubMed:15749760, PubMed:21283781, PubMed:23454094, PubMed:27059015). The MST11-MST7-PMK1 MAP kinase cascade transduces signals from the cell surface sensors MDB2 and SHO1 that recognize various surface signals such as surface hydrophobicity, cutin monomers, and rice leaf waxes (PubMed:21283781). MST7 acts as the upstream MAPKK that directly phosphorylates MAP kinase PMK1 (PubMed:15749760). {ECO:0000269|PubMed:15749760, ECO:0000269|PubMed:21283781, ECO:0000269|PubMed:23454094, ECO:0000269|PubMed:27059015}. | Pyricularia oryzae (strain 70-15 / ATCC MYA-4617 / FGSC 8958) (Rice blast fungus) (Magnaporthe oryzae) |
G4NH08 | GSK1_PYRO7 | MSQNRPAAFNTLRMGEVIREKVQDGITGETRDLQYTQCKIVGNGSFGVVFQTKLSPSNEDAAIKRVLQDKRFKNRELQIMRIVRHPNIVQLKAFYYSNGERKDEVYLNLVQEFVPETVYRASRFFNKMKTTMPILEVKLYIYQLFRALAYIHSQGICHRDIKPQNLLLDPTTGILKLCDFGSAKILVENEPNVSYICSRYYRAPELIFGATNYTTKIDVWSTGCVMAELMLGQPLFPGESGIDQLVEIIKVLGTPTREQIRTMNPNYMEHKFPQIKPHPFNRVLRKADNNAIDLIARLLEYTPTERLGAIDAMVHPFFDDLRNPSTKLPDSRHQTGQVRDLPPLFDFNRHELSIAPQLNHQLVPPHVRPTLAAQGLDIDHFTPMRKEDMLARLD | 2.7.11.1 | null | extrinsic apoptotic signaling pathway in absence of ligand [GO:0097192]; negative regulation of canonical Wnt signaling pathway [GO:0090090]; phosphorylation [GO:0016310]; positive regulation of chromosome segregation [GO:0051984]; positive regulation of developmental process [GO:0051094]; positive regulation of protein localization to kinetochore [GO:1905342]; regulation of neuron projection development [GO:0010975]; SREBP signaling pathway [GO:0032933] | cytosol [GO:0005829]; nucleus [GO:0005634] | ATP binding [GO:0005524]; protein serine kinase activity [GO:0106310]; protein serine/threonine kinase activity [GO:0004674]; protein serine/threonine/tyrosine kinase activity [GO:0004712]; protein tyrosine kinase activity [GO:0004713] | PF00069; | 1.10.510.10; | Protein kinase superfamily, CMGC Ser/Thr protein kinase family, GSK-3 subfamily | null | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:28424497}. Note=Mainly localizes to the cytoplasm at the conidial stage. {ECO:0000269|PubMed:28424497}. | CATALYTIC ACTIVITY: Reaction=ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-[protein]; Xref=Rhea:RHEA:17989, Rhea:RHEA-COMP:9863, Rhea:RHEA-COMP:11604, ChEBI:CHEBI:15378, ChEBI:CHEBI:29999, ChEBI:CHEBI:30616, ChEBI:CHEBI:83421, ChEBI:CHEBI:456216; EC=2.7.11.1; Evidence={ECO:0000269|PubMed:30776962}; | null | null | null | null | FUNCTION: Protein kinase that acts downstream of the MPS1 MAPK cascade as a highly conservative signal modulator that dictates growth, conidiation and pathogenicity (PubMed:28424497). Phosphorylates HAT1 at 'Ser-8' to block its translocation from the nucleus to the cytoplasm where HAT1 positively regulates appressorium development and pathogenicity (PubMed:30776962). {ECO:0000269|PubMed:28424497, ECO:0000269|PubMed:30776962}. | Pyricularia oryzae (strain 70-15 / ATCC MYA-4617 / FGSC 8958) (Rice blast fungus) (Magnaporthe oryzae) |
G4RK16 | PFP_THETK | MKIGVLTGGGDAPGLNIAVYTFVKLAERKHEVYAIYHGWRGLLNKEVKRVSSRDLLDFAFSGGTYIRTSRTNPFKDEERARLLESNVKELGLDVVVAIGGDDTLGAAGEAQRRGILDAVGIPKTIDNDVYGTDYTIGFDSAVNAAIEATESFKTTLISHERIGVVEVMGREAGWIALFTGLSTMADAVLIPERPASWDSVAKRVKEAYNERRWALVVVSEGIKEYGGPKDEYGHSRLGGVGNELAEYIERSTGIEARAVVLGHTIRGVPPTAFDRILAVRYATAAYEAVENGRYGVMVAYSNGDIAYVPIVDVVGKNRLVSGYWMRLYETYWPDLAG | 2.7.1.90 | COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000255|HAMAP-Rule:MF_01976}; | canonical glycolysis [GO:0061621]; fructose 1,6-bisphosphate metabolic process [GO:0030388]; fructose 6-phosphate metabolic process [GO:0006002] | 6-phosphofructokinase complex [GO:0005945] | 6-phosphofructokinase activity [GO:0003872]; AMP binding [GO:0016208]; ATP binding [GO:0005524]; diphosphate-fructose-6-phosphate 1-phosphotransferase activity [GO:0047334]; fructose-6-phosphate binding [GO:0070095]; identical protein binding [GO:0042802]; metal ion binding [GO:0046872]; monosaccharide binding [GO:0048029] | PF00365; | 3.40.50.450;3.40.50.460; | Phosphofructokinase type A (PFKA) family, Mixed-substrate PFK group III subfamily | null | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_01976}. | CATALYTIC ACTIVITY: Reaction=beta-D-fructose 6-phosphate + diphosphate = beta-D-fructose 1,6-bisphosphate + H(+) + phosphate; Xref=Rhea:RHEA:13613, ChEBI:CHEBI:15378, ChEBI:CHEBI:32966, ChEBI:CHEBI:33019, ChEBI:CHEBI:43474, ChEBI:CHEBI:57634; EC=2.7.1.90; Evidence={ECO:0000255|HAMAP-Rule:MF_01976, ECO:0000269|PubMed:9555897}; | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=0.023 mM for diphosphate {ECO:0000269|PubMed:9555897}; KM=0.053 mM for D-fructose 6-phosphate {ECO:0000269|PubMed:9555897}; KM=1.43 mM for phosphate {ECO:0000269|PubMed:9555897}; KM=0.033 mM for D-fructose 1,6-bisphosphate {ECO:0000269|PubMed:9555897}; | PATHWAY: Carbohydrate degradation; glycolysis; D-glyceraldehyde 3-phosphate and glycerone phosphate from D-glucose: step 3/4. {ECO:0000255|HAMAP-Rule:MF_01976}. | null | null | FUNCTION: Catalyzes the phosphorylation of D-fructose 6-phosphate, the first committing step of glycolysis. Uses inorganic phosphate (PPi) as phosphoryl donor instead of ATP like common ATP-dependent phosphofructokinases (ATP-PFKs), which renders the reaction reversible, and can thus function both in glycolysis and gluconeogenesis. Consistently, PPi-PFK can replace the enzymes of both the forward (ATP-PFK) and reverse (fructose-bisphosphatase (FBPase)) reactions. {ECO:0000255|HAMAP-Rule:MF_01976, ECO:0000269|PubMed:9555897}. | Thermoproteus tenax (strain ATCC 35583 / DSM 2078 / JCM 9277 / NBRC 100435 / Kra 1) |
G4RK44 | TPSP_THETK | MRLIVVSNRLPVTISPSGEIRESVGGLATAMKSFLGAVNGGRELGLEEVVWVGWSGVPSERESNDLRERLRGMGLEPVPLSSEEVEGFYEGFSNSTLWPLFHGFSEYATYEEKHWRAYRGVNEKYAKAVVALARPGDLVWIHDYHLMLAPAIVREAAEVGVGFFLHIPFPPAELLQLLPSEWRREILEGLLGSDLVGFHTYEYSANFSRSVVRFLGYKVEMGAIAVGHRRVRVGVFPIGIDFDRFYNSSQDPSVVEEMAKLREMLGRAKVVFSIDRLDYTKGVLRRVAAWERFLREHPEWRGRAVFVLVVVPSRTGVPMYEEMKRQIDREVGRINGELGELNWVPIVYLYRFIPSPTLMALYNIADVALITPLRDGMNLVAKEFVASKRDCRGVLILSELAGASKELAEALVINPNDVGGTAEAIAEALSMSEDEQCRRIRAMQERLRMRDVVRWGTDFIYSLISAKSAREEVEKALRYMEELSVDKLKSDFAKAKRRLLLLDYDGTLVPHYPYPHMAVPDGDLLELLSRLAALPETAVYVVSGRGRDFLDGWLGRLPVGLVAEHGFFLKHPGGEWKSLGKVDPSWRQYAKGIMEDFASNVPGSFVEVKEAGIAWHYRNADETIAEKAVVELIDALSNALAGSGLSILRGKKVVEVRPAGYTKGTAAKMLLDELSPDFVFVAGDDETDEGMFEVAPQSAYTVKVGPGPTLAKFRVGDYRGLRSLLEQLRPP | 2.4.1.15; 3.1.3.12 | COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250|UniProtKB:P31678, ECO:0000269|PubMed:23626675}; | cellular response to heat [GO:0034605]; trehalose biosynthetic process [GO:0005992]; trehalose metabolism in response to stress [GO:0070413] | alpha,alpha-trehalose-phosphate synthase complex (UDP-forming) [GO:0005946]; cytosol [GO:0005829] | alpha,alpha-trehalose-phosphate synthase (UDP-forming) activity [GO:0003825]; metal ion binding [GO:0046872]; trehalose-phosphatase activity [GO:0004805] | PF00982;PF02358; | 3.40.50.2000;3.40.50.1000; | Glycosyltransferase 20 family; Trehalose phosphatase family | null | null | CATALYTIC ACTIVITY: Reaction=D-glucose 6-phosphate + UDP-alpha-D-glucose = alpha,alpha-trehalose 6-phosphate + H(+) + UDP; Xref=Rhea:RHEA:18889, ChEBI:CHEBI:15378, ChEBI:CHEBI:58223, ChEBI:CHEBI:58429, ChEBI:CHEBI:58885, ChEBI:CHEBI:61548; EC=2.4.1.15; Evidence={ECO:0000269|PubMed:23626675}; CATALYTIC ACTIVITY: Reaction=alpha,alpha-trehalose 6-phosphate + H2O = alpha,alpha-trehalose + phosphate; Xref=Rhea:RHEA:23420, ChEBI:CHEBI:15377, ChEBI:CHEBI:16551, ChEBI:CHEBI:43474, ChEBI:CHEBI:58429; EC=3.1.3.12; Evidence={ECO:0000269|PubMed:23626675}; | null | PATHWAY: Glycan biosynthesis; trehalose biosynthesis. {ECO:0000269|PubMed:23626675}. | null | BIOPHYSICOCHEMICAL PROPERTIES: Temperature dependence: Active at 80 degrees Celsius. {ECO:0000269|PubMed:23626675}; | FUNCTION: Bifunctional enzyme which catalyzes the transfer of glucose from UDP-alpha-D-glucose to glucose-6-phosphate to form trehalose-6-phosphate (Tre6P) and removes the phosphate from Tre6P to produce free trehalose. {ECO:0000269|PubMed:23626675}. | Thermoproteus tenax (strain ATCC 35583 / DSM 2078 / JCM 9277 / NBRC 100435 / Kra 1) |
G4SLH0 | TTN1_CAEEL | MEGNEKKGGGLPPTQQRHLNIDTTVGGSISQPVSPSMSYSTDRETVMRSASGHATVAETHLIRSIGSQSQSYTEEHWSSEITSFVALAPPKFIQVIKAYRVHSTDTISLVVEVASDPPAIFEWFYNEKSVLQDRDRFQVGHGINISRLKVSRPEQGVYKCVTRNPAGVSTSYGYITVNADREHLSSSKEDMRLQRQHSVTYHQAPRFLTQVPNLFVTAGSNVIIDVEVDANPPARFSWFVNGKEYRDSIHGVEMFSPDVNRSVVRFSIPVAGEYKVVASNVHGSAMSCGHVDIQKVIELEESTLTTSTTAFDPMTTSMRALGNNGRNSRQAVNMFELNYTQRSSSVPRGVRHLESHIEVSNMTGEEKKTQQQTRTDAASIVESRFHPQPPKPPRAGTSRRFLPEPPKFVTTLPSVITVNAEEKLVLSVDVQAIPAAEFAWHVNGFEVKKSQSVVLLDEHNKSTLVLHPPVKQGKYKVTARNDVGSDSVTTQVTRIGEVKDGAGSEPPDIVESAVTVTCSHEEDVGSHSSLQTVRRIQEMQEEDEVDPIKPFIEATSPKVKESVEHPFANILNPKKREERLSPSGKGKHLLFAPRITAHPSESVFKILDGSPLKLRVMASSLPPATFLWMLNNFELRSNQNVTIRNDEENSSEIEFQKAPNGNVTVSAKNHLGEDRWTGKVILQYESPPPGQKITTIEKVTESWTLEEAVITQVVPTAADPGDRIVIIVRFDENKTSNCQFNWTINGVNIEKLEENLVAVESTEFESSLIVEKLEEQLCGEVVCVVKNQHGEVFSSSAHLRIRDDDSSFEIVPPNLPEECAPKIVEPLHSASFLDGQAMSLRCKITANPSAAVVWSKDDVNVEDWVLNKDVTTTVLDGGVCELLNPECFAEDAGLYKCTATNPHGTAETAAFINVEGAEYIKDHEEAEISESVLTDDVHIILPPKFIETLTAETDNFQQLGYVRMVATVRSVAPITVSWQKDGMDIYENEKYEVMQFADGAQILTIRAPTNLDSGVYTCTAESEHGVSNSSCQVELTISAESSPESFEKVEITPPEEVKETGIDDDIEVILKEEVSGTAQIEKREEEFKLLVKVADQVASTLVANVFLEAVHEAVKKIVETEDEEEDNQIEATQEPRFETSTDEYHVKENGTIKMAATISGHPTPFLEWYFGEEKLQVSQNVSMYYEAGTSAIILKNVQKRQGGNYFLRAHNCHGESILPMKLTVDPIEAVTHVLETSIPKVVVEQDAKEEEVRRAAEIISEQFAQLWVQDAQTEAVSAQAHQTPVVAEQASEEPTLPEVVAALQEQKPSVEKAPQPQFEVLETEDQDVVEQMQKQLPPVQKSMSVQEEKASSQRTPSPMNYEDKVKTIQSNLLRVNSHEAMEPIEATNLLLNTALQLKNEHVCDETTTVIVTQQPQKYDQLVTVVESNIEYHALRLSTSSSSPLKFIDLETIIQKPSTSCESIDRMFVEKSKRTANAQHRIVVLQGMSNTFHNAITWSLKKVKKLVGDAEAKAYADVEVVKQDETNEQVMTIIDNDTIVPQLLQVAAAANKLKLENVSVALIKEGDRAHQELVIEYESSIDEPMFEPVHNTSHLTFHQQQPTGPDQHVWSRRSKFEEDEAHVVAVFVEVDANCPDQSVEIVATVNAAYEGDNRQGIEDEPFTEVSQSLATESSAAPQAPKFLRKLVNCFGRIGEPVQLKCLIAGMPQPEIEWTVDGDPIVPNDEYSIVYEDGVCILRIESTLIEDEGEYCCTASNVAGTTFSKCYLKLSEADDDAVDLLRQLSEIKIIDPTLSTGYPMSMISDEENTSHQLLSNVLLTDKEVPITATYNEDLSRAESFRRFFESAETTVKVTELYQGESVEAQFQQPEKREQVSTSNTDVMFVNQKVDVMESTVSTVGNAVRQSVSSSTNSWDYMFNDPFPESQEINVIENELYEPRVPLLPQKLSYKGQEIFANTNTVERNSKAGAKAKGEVENLKKCVETLLLFDAEMDMKDIKESSPKKEIISKKDQQSLDDQIKVTQQILKDVERDLNKMERTSPGKSLSPNKRTFAPKDVEDIEAAIFSISDQLADRQSSEEALREALQEMILSNSSPMKELSRNNETSKPEVLKSEIQKIPEVETKISEVYPIVKLKQAISAIENSLLEDTEVTEIMKRKGSDKDKRKATRIKRVPSAHSARITPITSNLRDRLNQLHQLTVSEDSGSLKQNEEAKEIQELFVKIEKEINTIAELCKEKMTKKGADTVTHVLNSVLQHVASIINVILVAQDHQPIEVHAETTKTAEVSVWYSFDVHPESEDIIGIVDEEPTNRRPSSTPRGSTRSSNLTTSQDSQATTKMTVSSEDTIEAPIAPPRKGRSLSRDAERLLEIQPRAPPRRSRQSGDTLSPEPTPVLTLVKSDETPAPVRPPRSRSRHSGDELAETSPEAQPIRPPRSHSRHSGDELEEVQPVRPPRSKSKTADANCLQIESMDESQYSLSCIHIQKTNFAFTNSTHETSNASVVVDLRNMAQLECTVQSLDDLASIQMLCEESDYPSDTDRSLLLAGTVRYFNRASPSLHEVSPSLNMESVSMDLKPETEPEEIVQDVYVNVELHSVPSLSSLVEVNPNTLMQTLASEKSSLKAAEEDEKEGEEEGEEEVTADVSFIGRSVLSTETLDVVLEEKDMSQMNSTLPLDYERAFSSNTIRETDILSDESITVDSSYHKSPEPTVDFARSQVKSEEVTENFSLIHKPARRRVTGIVVNSLIYTIAANIAEDNTFDVDVVQEPQRYNISIKVIEDIVDFTSLTIMSDCEDDPPADVLVLKQDTSKLQALSYDDISVATTRTGITVSIVARSLNDGIYASLEEIAWGEVEMTVPDIMQMSTEEKSSLQFNVTVSESNLEEAKSLKSQVSFRSSQNSVSEMDNTISSTATISIPSYVVKLESTATITCELNNYLPKNCTIDWYCGKTKIIIDHEQFDRISHDLLEVLIIRSVEAINGNLYSLKINEDLFPVAYLIVENTNLTTSANILTRPETQFVMEGQPTVITVELDDPNVIVNWLKDRRPLHENERIRLETDGQGNHRVIIPNTCVGDQGTYLALTSSESVAITLVVEERIEEKEVMVIASGTESEEDDVQEYLVPPGSTATIACELEECELKRSIRWLRDGKDIRFEQGKTEHVQNGLKHYLVVHDATSLDSGLYKTERSEEQCEETIIPRGVVATIQCQTSEPQESIQWSKDGNIIPSDISRFEFRSLDNNQSHEMVISNISWSDAGVYSVLINGKSSFVSKIVVVESELITQSVEEEPEAEPEIDVSLHIVESEQIIELNVPQSPKLGASHETLVPIGQDDIEVIDKQEAAPVVESIEETSSIGSEEFEIIEKFTEEEVPKVAEPSEPTQADVPKIAAPLEQSQIQQEVPTVAAPSEPTQADVPKEAAPSEPSQADVPKVAAPLEQTQIQQEVPMVAAPLEPTQADVPKVAAPLEQSQIQQEVPTVAAPSEPTQADVPKEAAPSEPSQADVPKVAAPLEQTQIQQEVPMVAAPLEPIQEEVPKEAAPSEPTQEDVPKGAAPLEPTQEDVPKEAAPSGPTQEDVPKEEAPSEPTQEDVPKEAAPSEPTQENVPKEAAPSEPTKDVPKEAAPSEPIQEEVPKEATLSEPTQEQSEVSKRSEPVEPTQIQQAASEEETPLEETNETVVQTNEDVKEAEVPENAEAQKVVDSSDLQVAASEIAHLAIDEAVLETSNQPSQFDSLQEQKPSVVHENEHVRSVCVDLTFSRDSEQIVSDVIVAEVGYDEDECSTIADTITSLSSSPLYTAPVFTERLPSSACFANSKLTLEVMFSGVPQPTISWLIDDHELVSDGERISIKCENGVSAIRFFNVDRNAGGFLKCRATNCAGQVETSCEIVAADEISVISDSSITSSTRPHFVVPLPERVTHTVNDHITIKCKFSGQPLPAAMWEKDGVLLDLQKYQVTTEDGTSILKIESASLDDKAVYTCTIANEAGCESTSCTIDVVDDHLGLQQTGLHVMCERDQNDVELDILVQSPNHLGVTFNFPPVNRTLARQPPYFLLPLSDKVVIDEKCTLKCVVMGIPLVIVKWIVDGVVVTEDDNHEIHFEDGIALLRMKNIKKDKSVVQCEAINCKGKVTTSCVLTKCGVEESEAGDLQKPSFVLSLKDTCTTTDHATLKCIVVGTPLPDVSCSFNGVTDNSKIRSEDGIVLIQVNDVTEEGIVVECTISNETGSSTSNCVVKIIKQEEKNYQRPIIVFNQAGSVNNERELSVKVGVIASPEPTLFWKHNGKSIEEGGDYYLIFEDGIGILKVFNIQDGSHEFTCIAKNEYGQTTVEIPVEIGLKTENKLTLVKTLNDIAVVDDIVQLKIVAEGDLPIEFKWFEDGQILEDDSSHKITVDKCISTLQLKLEETGTRIITCEVSNSSSKVNASCNVERVHNTVSDFVMTNDNSTRFLAVGRKCTRERNNTILKAVVVARENIGDICEIDGEKIPDAYIEGNSLSIKVDTLSKKLSNVSFKVSASEGKVFETRKIEIAQEDTDEENFEINYSLRIDEQSGNTTYTFENSELYQGNQSRELDNTERNFTVNKEKDESKKPSEVQPAEIVEQKDVPVQETSAPTVEKLAPVESKETPEVQAAEIVEQKDVPVPETRAPTVEPTVEKHTPVDSKETSEVEPAEIVEQKDVPVPETSAPTVEPTVEKHTPVESKEKSEVQPAEIVEQKDVTCEEEIKELLTEVEVELFFSQAEVFSGLELDLLMECSEYVTTSIQKGSTAAPAQEPTVEKLAPVESKETSEVEPAEIVEQKDVPVPETSAPSVEPTVEKLAPVESKETSEVQQAEIVEQKDVPVPETSAPSVEPTVEKLAPAESKETSEVQPAEIVEQKDVTCEEEIKELLTEVEVELFFSQAEVFSGLELDLLMECSEYVTTSIQKGSTAAPAQEPTVEKLAPVESKETSEVQQAEIIEQKDVPVPETSAPTVEPTVEKLKPVESKETSEVQQVEIIEQKDVPVPETSAPTVEPTVEKLAPVESKETSEVQQAEIIEQKDVPVPETSAPTVEPTVEKLKPVESKETSEVQQVEIIEQKDVPVPETSAPTVEPTVEKLAPVESKETSEVQQAEIIEQKDVPVPETSAPTVEPTVEKLKPVESKETSEVQQVEIIEQKDVPVPETSAPTVEPTVEKHAPVESKETSEVQPAEIVEQKVVPVPETSAPTVEPTVEKLAPVESKETPEVQPAEILEQKDVTCEEEIKELLTEVEVELFFSKAEVFSGLELDLLMECSEYVTTSIQKGSTAAPAQEPTVEKLAPVESKETSEVEPAEIVEQKDVPVPETSAPTVEPTVEKLKSVESKETSEVQQAEIIEQKDVPVPETSAPTVEPTVEKLAPVDSKETSEVEPAEIVEQKDVTCEEEIKELLTEVEVELLFSQAEVFSGLELDLLMECSEYVTTSIQKGSTAAPAQEPTVEKLAPVESKETSEVEPAEIVEQKDVPVPETSAPTVEPTVEKLKSVESKETSEVQQAEIIEQKDVPVPETSAPTVEPTVEKHAPVESKETSEVQPAEIVEQKVVPVPETSAPTVEPTVEKLAPVESKETSEVEPAEIVEQKDVPVPETSAPTVEPTVEKLAPVESKETSEVEPAEIVEQKDVPVPETSAPTVEPTIEKLAPVESKETSEVEPAEIVEQKDVSVPETSAPTVEPTIEKLAPVESKETSEVEPAEIVEQKDVSVPETSAPTVEPTVEKLAPVESKETSEVEPAEIVEQKDVPVPETSAPTVEPTVEKLAPVESKETSEVQPAEIVEHKDVQVPETSSPTVEPTVEKLAPVESKETSEVEPAEIVEQKDVPVPETSAPTVEPTVEKLAPVESKETSEVEPAEIVEQKDVPVPETSAPTVEPTVEKLAPVESKETSEVQPAEIVEQKDVSVPETSAPTVEPTVEKLAPVESKETSEVQPAEIVEQKDVPVPETSAPTVEPTVEKLAPVESKETSEVQPAEIVEHKDVQVPETSSPTVEPTVEKLAPVESKETSEVEPAEIVEQKDVPVPETSAPTVEPTVEKLAPVESKETSEVQPAEIVEHKDVQVPETSAPTVEPTIEKLAPVESKETSEVEPAEIVEQKDVSVPETSAPTVEPTIEKLAPVESKETSEVQPAEIVEHKDVQVPETSSPTVEPTVEKLAPVESKETSEVQPAEIVEQKDVTCEEEIKELLTEVEVELFFSQAEVFSGLELDLLMECSEYVTTSIQKGSTAAPAHEPTVEKLAPVESKETSEVEPAEIVEQKDVPVPETSAPTVEPTVEKLAPVESKETSEVEPAEIVEQKDLPVPETSAPTVEPTVEKLAPVESKKTSEVEPAEIVEQKDVPVPETSAPTVEPTVEKLAPVESKETSEVEPAEIVEQKDVPVPETSAPTVEPTVEKLAPVESKETSEVEPAEIVEQKDVPVPETSAPTVEPTIEKLAPVESKETSEVEPAEIVEQKDVSVPETSAPTVEPTIEKLAPVESKETSEVEPAEIVEQKDVSVPETSAPTVEPTVEKLAPVESKETSEVEPAEIVEQKDVPVPETSAPTVEPTVEKLAPVESKETSEVQPAEIVEHKDVQVPETSSPTVEPTVEKLAPVESKETSEVEPAEIVEQKDVPVPETSAPTVEPTVEKLAPVESKETSEVEPAEIVEQKDVPVPETSAPTVEPTVEKLAPVESKETSEVQPAEIVEHKDVQVPETTATTFEPTKEKLAPVDSKETSEVQTAEIVEQKDVPVPETSATTVEPTKEKLAPGESKETSEVQQAAIVEQKDVAVPETSATTVEPTKEKLAPVESKETSEIQTAEIVEQKDVPVPETSTSYVEPTKEKLAPGESKETSEVQQAAIVEQKDVPVPETSATTVEPTKEKLAPVESKETSEIQQAAVVEQKDVPVPETSATTVEPTKEKLAPVESKETSEVQQAAIVEQKDVPVPEANAPTFEPTVEKLAPVESKETSEVQQAAIVEQKDVPVPEANAPTVEPTVEKLAPVESKETSVESKETQADAKLKKEKDDKHKQEADAKLQKENDDKLKQEADAKLKKENDDKLKQEADAKLKKENDDKLKQEADAKLKKENDDKLKQEAAAKLKKENDDKLKQEADAKLKKENDDKLKQEADAKLQKENDDKLKQEADAKLQKENDDKLKQEADAKLQKENDDKLKQEADAKLQKENDDKLKQEADAKLQKENDDKLKQEADAKLKKENDDKLKQEADAKLKKEKHDKLKQEADAKLQKENDDKLKQEADAKLQKENDDKLKQEADAKLQKEKDDKLKQEADAKLKKEKDDKLKQDADAKLQKEKDDKLKQEADAKLKKEKDDKLKHEADAKLQKEKDDKLKQEADAKLKKEKDDRLKKDADAKLQKEKDDKLKQEADAKLKKEKDDKLKHEADAKLQKEKDDKLKQEADAKLKKEKDDKLKQEADAKLQKEKDDKLKQEADAKLKKEKDDKLKQEADAKLQKEKDDKLKQEADAKLKKEKDDKLKQEADAKLQKEKDDKLKQEADAKLKKEKDDKLKQEADAKLKKEKDDKLKQDADAKLQKEKDDKLKQEADAKLKKEKDDKLKHEADAKLKKEKDDKLKQEADAKLKKEKDDKLKQDADAKLKKEKDDKLKHEADAKLQKEKDDNFKQEANAKLQKEKDDKLKQEKDDNFKQEANAKLQKEKDDKLKQEKDDKLKQEADAKLKKEKDDKLKQEADAKLKKEKDDKLKQEADAKLKKDKDDKLKQEADAKLKKEKDDKLKQEADAKLKKDKDDKLKQEADAKLKKDKDDKLKQEADAKLKKEKDDKLKQEKNDKLKQEADAKLKKEKDDKLKQEADAKLKKEKDDKLKQETDAKLKKDKDDKLKQEADAKLKKDKDDKLKQEADAKLKKDKDDKLKQEADGKLKKEKDNKLKQEADGKLKKEKDNKLKQEADAKLKKEKDDKLKQEADAKLKKEKDDKLKQEADAKLKKDKDDKLKQEADAKLKKEKDDKLKQEADAKLKKDKDDKLKQEANAKLQKEKDDKLKQEADAKLQKEKDDKLKQEADAKLKKEKDDKLKQEADAKLQKEKDDKLKQEADAKLKKEKDDKLKQEADAKLQKEKDDNFKQEANAKLQKEKDDKLKQEKDDKLKQEADAKLKKEKDDKLKQEADAKLKKDKDDKLKQEADAKLKKEKDDKLKQEADAKLKKEKDDKLKQEADAKLKKDKDDKLKQEADAKLKKDKDDKLKQEADAKLKKEKDDKLKQETDAKLKKDKDDKLKQEADAKLKKEKDDKLKQEADAKLKKEKDDKLKQEADAKLKKEKDDKLKQEADAKLKKDKDDKLKQEADAKLKKDKDDKLKQEADGKLKKEKDNKLKQEADGKLKKEKDNKLKQEADAKLKKEKDDKLKQEADAKLKKDKDDKLKQEADAKLKKEKDDKLKQEADAKLKKEKDDKLKQEADAKLKKDKDDKLKQEADAKLKKDKDDKLKQEADAKLKKEKDDKLKQEADAKLKKDKDDKLKQEADAKLKKDKDDKLKQEADAKLKKEKGDKLKLEDQTNQSRIFEETSIEVTSLLKCKQQAIIVSKSFALCERVVLNAEEPFTLEVFCNAVFVKQRTDKIGIGIIFERSGASKKDESRPDRLDDNCVLTDVTDGLSILSPPPKAKKHLKKKKKHHKKEKIAVKETEQDEKTVSHLKPEISGMERKRSNSGSSDIFVDVDIEAGEESIHTDALVDLNFYDYDQMELSIFEDYDSDDDSASIDCDVSLSNVAADDGIDVFPSDGDTQEVEQKVTLPKKHQSDEDVISKEEENLETSVSYGSIEETVSFTIGTGQSIIEHPKSHAVGQMNSEVIIKCKTSQPISDAKWFCNGMVLLPDEQVNMTVTGCEAVLRLVKFLPQNKGNYHVLIDGSIGSQPAILSGPVPPVILNKLTKPITHQAGKSFTYKFNFMGAPAPRLRVLSNGEPVSFDVKYEIYDNIASLYIPKMSKRDGGEYTVVLENKYGKDESDLHITMVDTPLKPRKAQLVALTDTSATFKWLPPHTGESDILHYIVMRRSTESRRWRNIGHVQEKTFTAIELVPNEFYAFRIVAVNGFGEGAPSEIIEVNTLDYDQEESFDFAGEEELKLDDVQVNNEVVTEITIEESEVTIEEHRKLKKKSKKSKKTTDEPELDSEIALEVSSDITSSLEITTESTIPDTAPESQETLNVEIAVTETTVQKITNPSDESAKKDVNEDTAVSSIVKKDDKDVNKKSLPESGLTTKKEIQGKPEKKIMKKKTEKADSSISETSETLTKDLTQTKQSEPEPAKRTTETSVQDEVKRKTETTSKSKQTTEEHPQPGGKSDSSISSTSDASEVKQVQQSESEAQKVTEKPETAKLESKSKMTEDTTKESDNKETVDEKPKKKVLKKKTEKSDSTISETSETSAVESAGPSESETQNVAAVDKEKKQKETDEKQKLEAEIAGKKSTEQKSKLEAEAKLKRAAEEDAAKKQKEKTEAASKKAAAEKLELEKQAQINKAAEADAVKKQNELDEQNKLEATKKLAAEKLKLEEQSAAKSKQAAEEQAKLDAQTKAKAAEKQTGLEKDEKSNKDSGSNETVEEKPKKKVLKKKTEKSDSSISQKSDTSKTVAESAGSSESETQKVADATSKQKETDKKQKLEAEITAKKSADEKSKLETESKLIKAAEDAAKKQKEKEDKLKLEADVASKKAAAEKLELEKQAQIKKAAEADAVKKQKELAEKQKLESEAATKKAAAEKLKLEEQAQINKAAEADAVKKQKELDEKNKLEANKKSAAEKLKLEEESAAKSKQTVEEQAKLDAQTKEKTAEKQTGLEKDDKSTKDSESKETVDEKPKKKVLKKKTEKSDSSISQKSVTSKTVVESGGPSESETQKVADAARKQKETDEKQKLEAEITAKKSADEKSKLEAESKLKKAAEVEAAKKQKEKDEQLKLDTEAASKKAAAEKLELEKQAQIKKAAEADAVKKEKELAEKQKLESEAATKKAAAEKLKLEEQKKKDAETASIEKQKEQEKLAQEQSKLEVDAKKSAEKQKLESETKSKKTEEAPKESVDEKPKKKVLKKKTEKSDSSISQKSDTAKTVAESAGQSDSETQKVSEADKAHKQKESDEKQKLESEIAAKKSAEQKSKLETEAKTKKVIEDESAKKQKEQEDKKKGDDSAKKQKDQKEKQKLESEATSKKPTSEKQKDEKTPQEKAKSENETVMTTEPQQLEVKSEPKKSDKTETVEKEVASSTEKSDDSKTKEPKEKKKIIKKKKDTTKPQEASKELSSDESRIDLESDISLSLDTVTESDDLSTASTIKLQKESDESGIDSRMGQTSEAEDSPFISQPVSATVTEMAGEAKFTVKFSRKPIYVKWMRDDREIRVAYGKASVETTDDSSVLVIKNIDGKDVGNIYAVFDSEYRSAMARLDLRVPCKITLESSSNAPEIVAGKNLDLSFKISGYPLPTNIELLHNNENLRTRSDVTDFDDSISIRMKRLKLEDSGEIKIIGKNDSSEDQLRIPINVIEVTSKPTSLQVTSTERETVTLTWSLPTELNGSNVNEYLVERKTVDGGRWRHACTVTDSRAVVDGLFSGTEYVFRVVAVNGAGQSAPSDTIEATTQAEEEIDETVPTSPVEKVKEPVSKKPENTKESEGHKKRDRKESEDHDENNLGKSGKDEFATSGESGTSNQNEESAQLNTSFTSTEQHGQTEKQVRKGTRKSLTRSLNIRESDIDADVVEVEYDEQGDDIPSDPTTSGTYAFDKIEEEPARTSGEMAMAEKDSDAMEVRGLNKKLSKKGGKEGTSTEKSSSKTKKQEKSALSVQEMNKSLKKKGEKGEAETAASDFIENADQTGMSIQDLNKSMKKKVESGEATGQINDASNNKDADELSIQDSQQSLKKKSENESVTGEQLDKSQEVEDDKMTIQSLKKSIKKKPESREVSGGKSEKSKEKESDEMSIQQLNKSVKKKPENEAVTQGKSGKSQEQESDKMSIQALNKSMKKKDGVDGVEGNINIGRSDGDQLSVNDIDAELSTSEQVENASQNLGATADSDGDSLSLQTLKKRISKKGIHGEAESKLGEKQSGSDSFTLQDLYEELKAKEDAVEAGAETSNADQSAEKTSLEVRDMKKKMKKKQVSGTAENLIGESNRDETSMEIRDLNTQHSNQTGEDESSTFNFGQKDQEQYSMVMKDVSKKLARQNAEEIQSGKLIPTTNEEKTGLALTGKNKNLKKGEENEKTKFEAKHLGSSSASDSLAESTLRSKKTKKGEVEKSELSIDMKNQDKTTLATTLLEDDLAKTTSAEESEAEHLVALQNKEKTSLAMRRKRVSFDSSTKSESIEDVIPDKNRDSDKMSITGIKKKMSQKSESAEAQKNESPEVKEISSFEEKTLKSKKKSKADRNQGTEANLGDKTIDKDYLSVTDKNQSLEKSEASGQAEKSIKAPNKSKVTTSFADESLTSELDRLMADEEMAEMMFAEEEKAADLLNVMNKNKGLNKSEQEESQEISLKSQSKVKDSDSLSSTDKKIGLKKSDKDQKLGTSKIFGSKDQESVGYEEKTSNFSKQRRGVSDLGSDAMTDQKNVQESQYAEISADDHMSKTGADGEISATRTIVDGSDAAQGSEYAEISKKRKFKRAEQIGEAETSLCDSRENTHDSLSISDVNPELRRSNVEISAFGQIDLTAEEVTSLTDINKDAQLTKKQDENDAKKSVSKNLKAGAKKDSDTLSITSKKDKFGKRQDSREASATVEQQGEEKVTKNLKGSRGKKEKLGDAGIDVNFENQEEFASTTGDIESIVSEKGHDTYSEKTVKSSKKKSPQTAGAEYGGSESLNASSALSTTDVDAQLKNQEKDGVAESSIGKSNQKDSYSEQELNVNKKKKQAVGAAMNQGSGSTKESDNLAVASVESNLAKDSANQEASLHGLVDNDATSLSQLDSEHRLKKRDDELSAHTKLGKHTQSENIALTETDDSLVKGDSEESAELNIKQQGETAEDKYVESRKKTTLKKKPEQKQVTDTLSAVDGRHDTTSLSVADSGISFDKSMENELAGSGDGTASASVSAKVRGADGNAKTNLISSFEKPGQESKTSKTLSGKQKKQEKSSFAEKNAGFDLSMGEGKNDESVESSLQKNRDADSLALQGTDLAFSKPSDSSANAHLDMPQRELTLRICQAETVDWSDDSEVEEGTRTSAPGEVKKKKKFIISAISQDGEFSDAESITFDENGVRVEKRRRKKRDPKEYMGAGELAMRIPAFAKKMQYIGCIEGDVVVFTIKVVSDDVPLIRMYRNDFPVANFDKMAFEGFTKGSEHSFNVTINDIRKLDGGKLVFEAKNDYGVDKCTILLDVRDSGSFIEDYSEIHRSAEIQNSVGDVQVKEGETAKLTGRVDGFPLPELIWIKNGKEIDMMVPSTKYQLDYHSDGEFEARIANCTFEDDDDYSLLVENLAGVDSCNFQVFVDCNEYPDDEHFNRRRRLQRGRRVMEASSDSELDDAKKRKKRRIKRVVERRNPNAPRLTQLIPPRFDKILSDHDAIEGENVVMMVETLGEPEPQVRFYRDGKLIDDGSGDRMEVRHEDEMRKHWLILKDICKDEEAEYACQAINVAGEAWCFSDVVVHMSEESRDDDKSVDEVDDSTVLEEKKDDGDDKSKPKTKKKIIKKKETPESEQVTAAEPEQQKISEVDVQSVAETEVGAKKKPDAEKPTDLSKAKKDSKSKKSDEPEASTEEKSTTEKPTNDKTSKKSAEKKTVKPKKEVTGKPLEAKKPVEDKKDASQPSSSKESSPPTDGKKKKQIPKALFIPDEISSRFGDPSTMHSETNITTTIRGREGSADAKTPLVEPLSASVSMKVESAKEKAEFSFKRRSETPDDKSRKKEGLPPAKKSEKKDEVTAEKQSTEALIESKKKEVDESKISEQQPSDKNKSEVVGVPEKAAGPETKKDVSEIEEVPKKKTIKKKTEKSDSSISQKSNVLKPADDDKSKSDDVTDKSKKTTEDQTKVATDSKLEKAADTTKQIETETVVDDKSKKKVLKKKTEKSDSFISQKSETPPVVEPTKPAESEAQKIAEVNKAKKQKEVDDNLKREAEVAAKKIADEKLKIEAEANIKKTAEVEAAKKQKEKDEQLKLETEVVSKKSAAEKLELEKQAQIKKAAEADAVKKQKELNEKNKLEAAKKSAADKLKLEEESAAKSKKVSEESVKFGEEKKTKAGEKTVQVESEPTSKKTIDTKDVGATEPADETPKKKIIKKKTEKSDSSISQKSATDSEKVSKQKEQDEPTKPAVSETQMVTEADKSKKQKETDEKLKLDAEIAAKTKQEADEKSKLDAQEKIKKVSEDDAARKEKELNDKLKLESEIATKKASADKLKLEEQAQAKKAAEVEAAKKQKEKDEQLKLDTEAASKKAAAEKLELEKQAQIKKAAGADAVKKQKELDEKNKLEANKKSAAGKLKIEEESAAKSKQTVEEQAKLDAQTKAKTAEKQTKLEKDEKSTKESESKETVDEKPKKKVLKKKTEKSDSSISQKSETSKTVVESAGPSESETQKVADAARKQKETDEKQKLEAEITAKKSADEKSKLEAESKLKKAAEVEAAKKQKEKDEQLKLDTEAASKKAAAEKLELEKQSHIKKAAEVDAVKKQKELEEKQRLESEAATKKADAEKLKLEEQKKKAAEIALIEIQKEQEKLAQEQSRLEDEAKKSAEKQKLESETKSKQTEEAPKESVDEKPKKKVLKKKTEKSDSSISQKSKSAKSTVDAAETLESDFNLVEKKTVQKVEQSPDESTSATIKRDPAQKTEEISKQDDGDEKKTTTDGKPPKPEDSEATPKKRVVKKKTQKSDSVASDASLADVSKLSDDVEEKPKKKVLKKKTEKSDSVISETSSVDTIKPESVEIPTEKAEQMILHNRFSTDSAVESEPKNAHKDDTEKTTDDMMTRRKSSAIFSDDEQSISSKTSSEGRRRRRRTGFASKFASDTLALRGDNVEIEAELLAEDDTVTWKVNGKDADLNSRCHEMSHTFFRTLIIDEVEPTDSGMEITATCGTESHTTILKVEELPVDFVKYLPRKTSGKEGQEVTISVTLNHPIDISKVVWLKDGKPLEINKDYSIDTVGCSVSLTLRRAKYEDSGKYKVVCDGVDCSTHLSIQGKPVLKNVSETKPVITVDKDDQFSLLVAYDSNPEASFSMTVDGKDLEFDGRSRIDVVDDGLKLTKRGVSKTDAGEYEVKLKNEFGEVAQKFDVKVNDTPSAPGDVSVVKAESDCLHIEWTAPTEDNGAEVTSYVIEKKESGRRKFHKVATVNGKKTSYVVDDLEIETPYIVRIAAVNKFGTGEFIETKPVQTGSPFQVPTVEFPPTIDNVTSTSCSLSWPKPIEDGGSPVYGYDVYKRENEGEWQKMNGEELVFTESFNVRALSSGKEYEFKIEACNEAGLRSNSNVVSKKLTVEGLVPEIILDMPMVKVLDNDKVEVTWKSDGEKEFVVQYKSDGSSIWASVDIGGPRSESAATSKCIIDGLREGIPYVFRVAARNQHGTGEFSEPTIPVVVLADDAPRVLKAIKPVKIPKKGELRLECHAAGHPAPEYIWYKDGKEIIPTDENTEIVNEGSMSALIIHELAGEDVGLYKVLVENIHGTAESEAEVGISDVRAHFNSSFSELTEIEEGHDIELTCEVSDEEAVVNWYKDGKKLVASDRVQFYAMARKRTLRIKGSTDADSGVYKCETTDGRSRTEGEVIVNEQEPHILVGPQDAIVKDFGETMVLFCETSKPVRKVKWFKNGVEIWPQMNKAIMENDGKRATLEIKNFDKHDIGAYTASVSEKETSAPAKLVFEVAPNLIIPTEIRDGVTVHAGNEFDFAVEFSGFPIPTIHLTNNGTPLKAIAVVTEYDDSVSVRMKDVTLDNSGTVRVIAESPLGQCIKEIPLKIIDKPSAPCDLQFKEVTEDSVFLSWQPPLETNGAPLTGYVIERKAVDNNRWRPCGQVKPTKLTFVAEDLFCNQVYGFRILAVNEVGESEPCDTVDVLTLESSEPVSESSELFVPKIAILRTPQVTVAVDETKVTLRWEECPETSLYKVERKKVGDSDWLEIANTDRNKFKDRSLTESGEYVYQVTATGIHAVSSPSEETNPVKILVPGSEMPASKTEKKTDAAKSESEQKSAEEIVAEKQVDQSQASESTTEAVEEKKTKKVVKKKVAENKGEETLQEVKEKLKKGKAVEKVQDESRRGSLQASSDNESVTTTSEKRSEAELEKNSEKSAEKKSTSADLEAADKAETEKSETGKETTEKKKKVVKKVAKKGLVKADKSKIELTAGKEGEISAQVAETGVSVEWKKDGKALDASYTVTSTGGVSTVKIPIVDVNTSGVFTCKVKSSEGDEEEVSIAVTVKLPEVPKVEAEQSIVEVKVGDVAKLSAKISEPASSVNWTKDDKPIKEDGNVKAQLSPDGTAQLTISKTDSAHSGIYKLNVENDAGKGKVEIALRIKGAAKGAPGIPTGPIVFDDVTESSAEFSWKAPENNGGCEITGYNVERKESKNKGWKQCGKTKELKFKADGLEEGTDYDVKVSAVNTMGTGSALEGKITTLKKKEETGKQKSEKSESDEKKSESDKVSELKQIGKPEYVSSTATSIALKWTSDNDEVTYTVQMKEANSKRPWAVVAKEISECSATIAQLKEGTSYLFRVIAQNKTGQTVTSEQSESIECKDTTESKKPAFTNAPTDLTAVKNGKTKITAEFTGHPAPEIHWFKNKKEIFSGKRQWIENIAGATSLTIGEMREDDEGEYKIVVKNTAGSVEHSCKLTMDQLPEINRVDRYASTLVFDKGETVKLRLSFSGRPQPEVIWIDNNGKVIEESRKMKIEKTVLNTVLTINSIDSQDQGEFALKIKNRCGEDKYAIGIQVTDRPAAPGKPAVEDQNVDSVRLRWAAPTNDGGSPVRNYTVEMCTEKGKTWTKAEVTKQAFITLFNLVPGESYRFRVRADNTFGQSEPSDESELVVVKNVSRVVEEPKKKEVKVKEQESVDYERVAKDSEPSEYKTIDIHRLPNDLQAKYIIHEELGKGAYGTVYRATEKATGKTWAAKMVQVRPGVKKENVIHEISMMNQLHHEKLLNLHEAFDMGNEMWLIEEFVSGGELFEKILEDDSLMSEEEVRDYMHQILLGVSHMHKNQIVHLDLKPENILLKAKNSNELKIIDFGLARKLDPKKSVKLLFGTPEFCAPEVVNYQPVGLSTDMWTVGVISYVLLSGLSPFLGDSDEDTLANVSASDWDFDDPSWDDVSDLAKDFICRLMIKDKRKRMSVQDALRHPWITGPLLSAFNDLSEYVKKMQPKLDKSGVPARQKRNFLSLKRWSDDLLPIGRLAKRGAIFRRLTMDGVFERNIAFDTDAAPSVKKQLEDIVANVGDLIATLSCDVDGVPSPKVQWYKDDKELTVPSMKYDSFYNEGLAELTVKNIVESDAGKYTCRATNDLGSIMTHAKLSVKADEKKKKKSKTSPAVIEKKKDRKTSKVVVIEEMIDMPPNFHHLLQDDEAKIGEPKILVVTNTTLPEPTVDWYHNGEHISINDSNYLRKHDKGRYELHILSVDSTDEGKWKAVGKNAFGECESEAKLTVVIPDGQYAPSFGKQLSDVKCSESDILKLEVNIQANPAPEINWFRNESEIEHSQHHRLQFDDGSGNYSLTIIDAYAEDSGEYKCVAKNKIGKAHTVCCVRIEELLSKRSKKIDGSKAPRFRMQLPTPREVPQGADLTLVCSVSGTPHPNIKWTKDDKPIDMSNKQVRHENGVCTLHIIGARDDDQGRYVCEAENIHGVAQSFSVVEIKEAVDKDHVRPKFLEPLVNCSTCEGNEMVLECCVTGKPIPTITWYKDGLKLIIENRMLQYTDRKGVSRLNIMNVVMNDDGEYTCEAVNSLGKDFTHCTVKVVDMGLSKTRLTPVRSRSRSRSRSPSVVGGEIQRPPVVTRPLADATVTEGNRELLEVEVDGFPTPTIEWYHDGKLVAESRTLRTYFDGRVAFLKIYEAHEEHNGQYVCKVSNKLGAVETRAIVVVEAPDAAEHVTQMPTFVKKLQDVVLKTAGETATFTCQSYANPAAQVVWLHNGKALQQTKSNYKTRLFDDNTATLVIENVTDELCGTYTAVANNQFGDVHTSAQLTISGSEAKKIAASLPYFIIELKPKINVVEGATLSIQADLNGSPIPEVVWLKDNSELVESDRIQMKCDGVNYQLLVRDVGLEDEGTYTITAENEKGKIRQNTEVSVTKSKEVKEKKEKKKVEKKDEGKKKPGRPGLPRPSGASKTEQVTMAFDAPSEGPADSYEVERRCPDQREWVSCGSTKSLELEIKGLTPNTEYIFRVAGKNKQGLGEWSEMTSTLKTASVGQAPQFTISPQSKIIANRDDEFEIAVEFSGTPTPSVKWYKENLQIVPDEKIDVATTSTSSILNLKSQEENGTFNCLIENELGQASASCQVTIFNKPASLQSTPDHSLERNLVPTLQKALNNESAQAGQQIMLTCRISSRSESTVAWFKDDERIESAGRYELSSDKKSNHKLVCHAVQSQDTGKYRCVVTNKYGYAESECNVAVEDVTKFIAPSFSATLSDSTAILGHNITLECKVEGSPAPEVSWTKDGERISTTRRIRQTQDENGNCKLSISKAESDDMGVYVCSATSVAGVDSTSSMVMIAKTTGTDSHLVIAQTADEKHEKPRFTRAPPSLIEVNESGQFTLIAKAVGEPKPTVTWLKDGREILRTNRIYHHFVTGDGESHLIAECVVSKTSGIFSCKAENPNGTVIAETQVIVQRMKPANQLANVAPKFTIPLTDMGIVNGHPTTLSCNVTGSPEPTLEWIYIDDSGHKINLTSSTTDWTECRFGKVAELKSERVLREQRGTYQCIATNSSGQATTQCYLLVGELSDEPAGPPRFVKCLQDTWTPLKESIEFSVELAGFPTPDLTWYHNEKKINEGKDVKITFPSDTTSVLSIKNVSLASLGMYFVEASNIHGVLRTAGRLNVSDERRKAEPPQFKHVLEPVLAVQPKVAFSEEHPRASSSAATARVKKGAAPMFLQGLEDMDLKAGASAAVAGKLGRKLRPHRSTTNDADKLAKALAQSLRLDEPRASIDSRPESAANAALDEVRAAINSRNKRVCRPKFMVKPKPRKVLEEYKSLRLKTAISGNPMPQVHWDKEGIILETGNKYSIYNDGDFYYLEVHHVSTFDKGFYNCTAANNEGIITCTSEIDVLPNKEDSAAQVAKRKSRKEAKAPNFIEVLPGRSQANLNESLCVECSVSAYPCASIIWTRNSVRLLPQADRYTMSYDGECASLKFISVTPGDEGTYACEAVNELGSAVTNMNLQVSGVDPNAAEGIPPLFRFEKIKSVRKVVDGSRVELAAELVQASEPLQIRWLRNKVTIVDSPSFSYSRSENMVFLTIADVFPEDGGEYTVEAKNQSGIARCTMQLDVRNNERSVADEAPRVFDFEPTTRSDPGVSVELRAKVIGHPDPVISWTKAGQKLNNEEKYMMRNEGDKFILRIANVTRADAGKYELTAINPSGQANAELELTVVQSTKTVGAKPKFNESPISVQTCEKNRAELRASFSGTPAPACRWFYNGNELIDGLDGYTITSSDTNSSLLINSVDKKHFGEYLCTIRNQNGEELANAMILSEVLSMFYSSLFLVVFVDIVAQCHVARLLHFLNEERFVGRNIFA | 2.7.11.1 | COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000269|PubMed:18390597}; | phosphorylation [GO:0016310] | A band [GO:0031672]; I band [GO:0031674]; nuclear membrane [GO:0031965] | actin filament binding [GO:0051015]; ATP binding [GO:0005524]; metal ion binding [GO:0046872]; myosin binding [GO:0017022]; protein serine kinase activity [GO:0106310]; protein serine/threonine kinase activity [GO:0004674] | PF00041;PF07679;PF00069; | 2.60.40.10;1.10.510.10; | Protein kinase superfamily, CAMK Ser/Thr protein kinase family | null | SUBCELLULAR LOCATION: Cytoplasm, myofibril, sarcomere, A band {ECO:0000269|PubMed:20346955}. Cytoplasm, myofibril, sarcomere, I band {ECO:0000269|PubMed:20346955}. Nucleus membrane {ECO:0000269|PubMed:16410549}; Peripheral membrane protein {ECO:0000269|PubMed:16410549}. Note=Localizes throughout the I-band except for dense bodies and in the outer edge of the A-band (PubMed:20346955). In embryo, co-localizes with lamin lmn-1 at the nuclear membrane. The localization to the nuclear envelope is lmn-1-dependent (PubMed:16410549). {ECO:0000269|PubMed:16410549, ECO:0000269|PubMed:20346955}. | CATALYTIC ACTIVITY: Reaction=ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-[protein]; Xref=Rhea:RHEA:17989, Rhea:RHEA-COMP:9863, Rhea:RHEA-COMP:11604, ChEBI:CHEBI:15378, ChEBI:CHEBI:29999, ChEBI:CHEBI:30616, ChEBI:CHEBI:83421, ChEBI:CHEBI:456216; EC=2.7.11.1; Evidence={ECO:0000269|PubMed:12381307, ECO:0000269|PubMed:18390597}; CATALYTIC ACTIVITY: Reaction=ATP + L-threonyl-[protein] = ADP + H(+) + O-phospho-L-threonyl-[protein]; Xref=Rhea:RHEA:46608, Rhea:RHEA-COMP:11060, Rhea:RHEA-COMP:11605, ChEBI:CHEBI:15378, ChEBI:CHEBI:30013, ChEBI:CHEBI:30616, ChEBI:CHEBI:61977, ChEBI:CHEBI:456216; EC=2.7.11.1; Evidence={ECO:0000269|PubMed:12381307, ECO:0000269|PubMed:18390597}; | null | null | null | null | FUNCTION: Serine/threonine-protein kinase (PubMed:18390597, PubMed:20346955). Key component in the assembly and functioning of muscles. By providing connections at the level of individual microfilaments, it contributes to the fine balance of forces between the two halves of the sarcomere. The size and extensibility of the cross-links are the main determinants of sarcomere extensibility properties of muscle. In non-muscle cells, seems to play a role in chromosome condensation and chromosome segregation during mitosis. Might link the lamina network to chromatin or nuclear actin, or both during interphase (By similarity). {ECO:0000250|UniProtKB:Q9I7U4, ECO:0000269|PubMed:18390597, ECO:0000269|PubMed:20346955}. | Caenorhabditis elegans |
G4STG9 | PFP_META2 | MNKPKKVAILTAGGLAPCLSSAIGSLIERYTEIDPSIEIICYRSGYKGLLLGDSYAVTPKIRENAALLHKFGGSPIGNSRVKLTNVKDCIKRGLVQEGQDPQKVAADQLVKDGVDVLHTIGGDDTNTAAADLAAFLAKNDYGLTVIGLPKTIDNDVFPIKQSLGAWTAAEQGAQYFQNVVAEYNANPRMLIVHEVMGRNCGWLTAATAMEYRKLLDRSEWLPEIGLDRAAYEVHGVFVPEMEIDLAAEAKRLREVMDKVDCVNIFVSEGAGVDAIVAEMQAKGQEVPRDAFGHIKLDAVNPGKWFGEQFAEMIGAEKTLIQKSGYFARASASNVDDIRLIKSCADLAVECAFRRESGVIGHDEDNGNVLRAIEFPRIKGGKPFDIDTPWFVQMLAGIGQSKGARVEVSH | 2.7.1.90 | COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000255|HAMAP-Rule:MF_01977, ECO:0000269|PubMed:20868748}; | fructose 6-phosphate metabolic process [GO:0006002] | cytoplasm [GO:0005737] | 6-phosphofructokinase activity [GO:0003872]; diphosphate-fructose-6-phosphate 1-phosphotransferase activity [GO:0047334]; metal ion binding [GO:0046872] | PF00365; | 3.40.50.450; | Phosphofructokinase type A (PFKA) family, PPi-dependent PFK group II subfamily, Clade 'P' sub-subfamily | null | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_01977}. | CATALYTIC ACTIVITY: Reaction=beta-D-fructose 6-phosphate + diphosphate = beta-D-fructose 1,6-bisphosphate + H(+) + phosphate; Xref=Rhea:RHEA:13613, ChEBI:CHEBI:15378, ChEBI:CHEBI:32966, ChEBI:CHEBI:33019, ChEBI:CHEBI:43474, ChEBI:CHEBI:57634; EC=2.7.1.90; Evidence={ECO:0000255|HAMAP-Rule:MF_01977, ECO:0000269|PubMed:20868748}; | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=3.4 mM for phosphate {ECO:0000269|PubMed:20868748}; KM=0.118 mM for diphosphate {ECO:0000269|PubMed:20868748}; KM=0.64 mM for fructose 6-phosphate {ECO:0000269|PubMed:20868748}; KM=0.095 mM for fructose 1,6-bisphosphate {ECO:0000269|PubMed:20868748}; KM=1.01 mM for sedoheptulose-7-phosphate {ECO:0000269|PubMed:20868748}; Vmax=577 umol/min/mg enzyme for the forward reaction {ECO:0000269|PubMed:20868748}; Vmax=805 umol/min/mg enzyme for the reverse reaction {ECO:0000269|PubMed:20868748}; | PATHWAY: Carbohydrate degradation; glycolysis; D-glyceraldehyde 3-phosphate and glycerone phosphate from D-glucose: step 3/4. {ECO:0000255|HAMAP-Rule:MF_01977}. | BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 7.5. {ECO:0000269|PubMed:20868748}; | BIOPHYSICOCHEMICAL PROPERTIES: Temperature dependence: Optimum temperature is 30 degrees Celsius. {ECO:0000269|PubMed:20868748}; | FUNCTION: Catalyzes the phosphorylation of D-fructose 6-phosphate, the first committing step of glycolysis. Uses inorganic phosphate (PPi) as phosphoryl donor instead of ATP like common ATP-dependent phosphofructokinases (ATP-PFKs), which renders the reaction reversible, and can thus function both in glycolysis and gluconeogenesis. Consistently, PPi-PFK can replace the enzymes of both the forward (ATP-PFK) and reverse (fructose-bisphosphatase (FBPase)) reactions. {ECO:0000255|HAMAP-Rule:MF_01977, ECO:0000269|PubMed:20868748}. | Methylotuvimicrobium alcaliphilum (strain DSM 19304 / NCIMB 14124 / VKM B-2133 / 20Z) (Methylomicrobium alcaliphilum) |
G4SW86 | ERG_META2 | MSEQESRDNAAVDAVRQKYGFGFSWLVLMIALPPLVYYLWICVTYYQGELVFTSDAAAWRRFWSHVAPPTWHAAGLYAAWFLGQAALQVWAPGPTVQGMKLPDGSRLDYRMNGIFSFLFTLAVVFGLVTMGWLDATVLYDQLGPLLTVVNIFTFVFAGFLYFWGLNGKQWERPTGRPFYDYFMGTALNPRIGSLDLKLFCEARPGMIFWLLMNLSMAAKQYELHGTVTVPMLLVVGFQSFYLIDYFIHEEAVLTTWDIKHEKFGWMLCWGDLVWLPFTYTLQAQYLVHHTHDLPVWGIIAIVALNLAGYAIFRGANIQKHHFRRDPNRIVWGKPAKYIKTKQGSLLLTSGWWGIARHMNYFGDLMIALSWCLPAAFGSPIPYFHIVYFTILLLHREKRDDAMCLAKYGEDWLQYRKKVPWRIVPKIY | 1.3.1.70 | null | ergosterol biosynthetic process [GO:0006696]; sterol biosynthetic process [GO:0016126] | plasma membrane [GO:0005886] | delta14-sterol reductase activity [GO:0050613]; NADP binding [GO:0050661] | PF01222; | 1.20.120.1630; | ERG4/ERG24 family | null | SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000305|PubMed:25307054}; Multi-pass membrane protein {ECO:0000269|PubMed:25307054}. | CATALYTIC ACTIVITY: Reaction=4,4-dimethyl-5alpha-cholesta-8,24-dien-3beta-ol + NADP(+) = 4,4-dimethyl-5alpha-cholesta-8,14,24-trien-3beta-ol + H(+) + NADPH; Xref=Rhea:RHEA:18561, ChEBI:CHEBI:15378, ChEBI:CHEBI:17813, ChEBI:CHEBI:18364, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349; EC=1.3.1.70; Evidence={ECO:0000269|PubMed:25307054}; | null | PATHWAY: Steroid biosynthesis; zymosterol biosynthesis; zymosterol from lanosterol. {ECO:0000305}. | null | null | FUNCTION: Reduces the C14=C15 double bond of 4,4-dimethyl-cholesta-8,14,24-trienol to produce 4,4-dimethyl-cholesta-8,24-dienol. Complements the deletion of the Delta(14)-sterol reductase gene ERG24 in yeast. {ECO:0000269|PubMed:25307054}. | Methylotuvimicrobium alcaliphilum (strain DSM 19304 / NCIMB 14124 / VKM B-2133 / 20Z) (Methylomicrobium alcaliphilum) |
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