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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A1B8Z0 | BHCD_PARDP | MLVVAEKEIAGLMTPEAAFEAIEAVFASMARRKAYNFPVVREAIGHEDALYGFKGGFDASALVLGLKAGGYWPNNQKHNLINHQSTVFLFDPDTGRVSAAVGGNLLTALRTAAASAVSIKYLAPKGAKVLGMIGAGHQSAFQMRAAANVHRFEKVIGWNPHPEMLSRLADTAAELGLPFEAVELDRLGAEADVIVSITSSFSPLLMNEHVKGPTHIAAMGTDTKGKQELDPALVARARIFTDEVAQSVSIGECQHAIAAGLIREDQVGELGAVVAGDDPGRGDAEVTIFDGTGVGLQDLAVAQAVVELAKHKGVAQEVEI | 1.4.1.- | null | glycolate catabolic process [GO:0046296]; glyoxylate catabolic process [GO:0009436]; thyroid hormone metabolic process [GO:0042403] | cytoplasm [GO:0005737] | NADH binding [GO:0070404]; oxidoreductase activity, acting on the CH-NH2 group of donors, NAD or NADP as acceptor [GO:0016639]; thyroid hormone binding [GO:0070324] | PF02423; | 3.40.50.720;3.30.1780.10; | Ornithine cyclodeaminase/mu-crystallin family, BhcD subfamily | null | null | CATALYTIC ACTIVITY: Reaction=L-aspartate + NAD(+) = H(+) + iminosuccinate + NADH; Xref=Rhea:RHEA:42440, ChEBI:CHEBI:15378, ChEBI:CHEBI:29991, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945, ChEBI:CHEBI:77875; Evidence={ECO:0000269|PubMed:31723261}; PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:42442; Evidence={ECO:0000269|PubMed:31723261}; | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=0.09 mM for iminosuccinate {ECO:0000269|PubMed:31723261}; KM=0.02 mM for NADH {ECO:0000269|PubMed:31723261}; KM=0.33 mM for NADPH {ECO:0000269|PubMed:31723261}; Note=kcat is 201 sec(-1). {ECO:0000269|PubMed:31723261}; | null | null | null | FUNCTION: Imine reductase that catalyzes the NADH-dependent reduction of iminosuccinate to L-aspartate. Is essential for the growth of P.denitrificans in the presence of glycolate and glyoxylate since it functions in glyoxylate assimilation via the beta-hydroxyaspartate cycle (BHAC). Thereby BhcD regenerates the amino group donor for the first step of the BHAC. {ECO:0000269|PubMed:31723261}. | Paracoccus denitrificans (strain Pd 1222) |
A1B8Z1 | BHCC_PARDP | MNAKTDFSGYEVGYDIPALPGMDESEIQTPCLILDLDALERNIRKMGDYAKAHGMRHRSHGKMHKSVDVQKLQESLGGSVGVCCQKVSEAEAFARGGIKDVLVTNEVREPAKIDRLARLPKTGATVTVCVDDVQNIADLSAAAQKHGTELGIFVEIDCGAGRCGVTTKEAVVEIAKAAAAAPNLTFKGIQAYQGAMQHMDSFEDRKAKLDAAIAQVKEAVDALEAEGLAPEFVSGGGTGSYYFESNSGIYNELQCGSYAFMDADYGRIHDAEGKRIDQGEWENALFILTSVMSHAKPHLAVVDAGLKAQSVDSGLPFVYGRDDVKYIKCSDEHGVVEDKDGVLKVNDKLRLVPGHCDPTCNVHDWYVGVRNGKVETVWPVSARGKGY | 4.1.3.41 | COFACTOR: Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326; Evidence={ECO:0000269|PubMed:31723261}; Note=Binds 1 pyridoxal phosphate per subunit. {ECO:0000269|PubMed:31723261}; COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000269|PubMed:31723261}; | D-serine catabolic process [GO:0036088]; glycolate catabolic process [GO:0046296]; glyoxylate catabolic process [GO:0009436] | null | D-serine ammonia-lyase activity [GO:0008721]; magnesium ion binding [GO:0000287]; oxo-acid-lyase activity [GO:0016833]; pyridoxal phosphate binding [GO:0030170] | PF01168;PF14031; | 3.20.20.10;2.40.37.20; | DSD1 family | null | null | CATALYTIC ACTIVITY: Reaction=(3S)-3-hydroxy-D-aspartate = glycine + glyoxylate; Xref=Rhea:RHEA:27934, ChEBI:CHEBI:36655, ChEBI:CHEBI:57305, ChEBI:CHEBI:60894; EC=4.1.3.41; Evidence={ECO:0000269|PubMed:31723261}; PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:27936; Evidence={ECO:0000269|PubMed:31723261}; CATALYTIC ACTIVITY: Reaction=(3R)-3-hydroxy-D-aspartate = glycine + glyoxylate; Xref=Rhea:RHEA:27938, ChEBI:CHEBI:36655, ChEBI:CHEBI:57305, ChEBI:CHEBI:60898; EC=4.1.3.41; Evidence={ECO:0000250|UniProtKB:Q8GRC8}; | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=0.23 mM for glyoxylate {ECO:0000269|PubMed:31723261}; KM=4.31 mM for glycine {ECO:0000269|PubMed:31723261}; KM=0.28 mM for (3S)-3-hydroxy-D-aspartate {ECO:0000269|PubMed:31723261}; KM=9.24 mM for D-threonine {ECO:0000269|PubMed:31723261}; Note=kcat is 91 sec(-1) for the condensation of glyoxylate and glycine. kcat is 33 sec(-1) for the cleavage of (3S)-3-hydroxy-D-aspartate. kcat is 76 sec(-1) for the cleavage of D-threonine into acetaldehyde and glycine (PubMed:31723261). {ECO:0000269|PubMed:31723261}; | null | null | null | FUNCTION: Catalyzes the condensation of glyoxylate and glycine into (2R,3S)-beta-hydroxyaspartate ((3S)-3-hydroxy-D-aspartate). Is essential for the growth of P.denitrificans in the presence of glycolate and glyoxylate since it functions in glyoxylate assimilation via the beta-hydroxyaspartate cycle (BHAC). Is also able to catalyze the reverse reaction in vitro, i.e. the cleavage of (3S)-3-hydroxy-D-aspartate, and that of D-threonine to a lesser extent. {ECO:0000269|PubMed:31723261}. | Paracoccus denitrificans (strain Pd 1222) |
A1B8Z2 | BHCB_PARDP | MYIPTYEDMLAAHERIKPHIRRTPIRTSDYLNELTGAQLFFKCENFQEPGAFKVRGATNAVFGLDDAQAAKGVATHSSGNHASCLSYAAMLRGIPCNVVMPRTAPQAKKDTVRRYGGVITECEPSTSSREETFAKVQAETGGDFVHPYNDPRVIAGQGTCAKELVEQVDGLDAVVAPIGGGGMISGTCLTLSTLAPETRVIAAEPEQADDAYRSFKAGYIIADDAPKTVADGLLVPLKDLTWHFVKNHVSEIYTASDAEIVDAMKLIWKHLRIVMEPSSAVPLATILKNPEAFAGKRVGVIVTGGNVDLDKLPWN | 4.2.1.- | COFACTOR: Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326; Evidence={ECO:0000305|PubMed:31723261}; | D-serine biosynthetic process [GO:0070179]; glycolate catabolic process [GO:0046296]; glyoxylate catabolic process [GO:0009436] | cytoplasm [GO:0005737] | ATP binding [GO:0005524]; D-serine ammonia-lyase activity [GO:0008721]; hydro-lyase activity [GO:0016836]; L-serine ammonia-lyase activity [GO:0003941]; magnesium ion binding [GO:0000287]; pyridoxal phosphate binding [GO:0030170]; serine racemase activity [GO:0030378]; threonine racemase activity [GO:0018114] | PF00291; | 3.40.50.1100; | null | null | null | CATALYTIC ACTIVITY: Reaction=(3S)-3-hydroxy-D-aspartate = H2O + iminosuccinate; Xref=Rhea:RHEA:62112, ChEBI:CHEBI:15377, ChEBI:CHEBI:60894, ChEBI:CHEBI:77875; Evidence={ECO:0000269|PubMed:31723261}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:62113; Evidence={ECO:0000269|PubMed:31723261}; | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=0.2 mM for (3S)-3-hydroxy-D-aspartate {ECO:0000269|PubMed:31723261}; Note=kcat is 35 sec(-1). {ECO:0000269|PubMed:31723261}; | null | null | null | FUNCTION: Catalyzes the dehydration of (2R,3S)-beta-hydroxyaspartate ((3S)-3-hydroxy-D-aspartate) into iminosuccinate. Is essential for the growth of P.denitrificans in the presence of glycolate and glyoxylate since it functions in glyoxylate assimilation via the beta-hydroxyaspartate cycle (BHAC). {ECO:0000269|PubMed:31723261}. | Paracoccus denitrificans (strain Pd 1222) |
A1B8Z3 | BHCA_PARDP | MTSQNPIFIPGPTNIPEEMRKAVDMPTIDHRSPVFGRMLHPALEGVKKVLKTTQAQVFLFPSTGTGGWETAITNTLSPGDKVLAARNGMFSHRWIDMCQRHGLDVTFVETPWGEGVPADRFEEILTADKGHEIRVVLATHNETATGVKSDIAAVRRALDAAKHPALLFVDGVSSIGSMDFRMDEWGVDIAVTGSQKGFMLPPGLAIVGFSPKAMEAVETARLPRTFFDIRDMATGYARNGYPYTPPVGLINGLNASCERILAEGLENVFARHHRIASGVRAAVDAWGLKLCAVRPELYSDSVSAIRVPEGFDANLIVSHALETYDMAFGTGLGQVAGKVFRIGHLGSLTDAMALSGIATAEMVMADLGLPIQLGSGVAAAQEHYRQTTAAAQKKAA | 2.6.1.35 | COFACTOR: Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326; Evidence={ECO:0000305|PubMed:31723261}; | glycine biosynthetic process, by transamination of glyoxylate [GO:0019265]; glycolate catabolic process [GO:0046296]; glyoxylate catabolic process [GO:0009436] | peroxisome [GO:0005777] | alanine-glyoxylate transaminase activity [GO:0008453]; glycine-oxaloacetate transaminase activity [GO:0047303]; serine-pyruvate transaminase activity [GO:0004760] | PF00266; | 3.90.1150.10;3.40.640.10; | Class-V pyridoxal-phosphate-dependent aminotransferase family | null | null | CATALYTIC ACTIVITY: Reaction=glycine + oxaloacetate = glyoxylate + L-aspartate; Xref=Rhea:RHEA:17141, ChEBI:CHEBI:16452, ChEBI:CHEBI:29991, ChEBI:CHEBI:36655, ChEBI:CHEBI:57305; EC=2.6.1.35; Evidence={ECO:0000269|PubMed:31723261}; PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:17143; Evidence={ECO:0000269|PubMed:31723261}; | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=0.43 mM for glyoxylate {ECO:0000269|PubMed:31723261}; KM=2.51 mM for L-aspartate {ECO:0000269|PubMed:31723261}; KM=9.52 mM for glycine {ECO:0000269|PubMed:31723261}; KM=2.9 mM for oxaloacetate {ECO:0000269|PubMed:31723261}; KM=2.1 mM for L-serine {ECO:0000269|PubMed:31723261}; KM=20.62 mM for L-glutamate {ECO:0000269|PubMed:31723261}; Note=kcat is 58 sec(-1) for the transamination of glyoxylate using L-aspartate. kcat is 0.76 sec(-1) for the transamination of glycine using oxaloacetate. kcat is 8.8 sec(-1) for the transamination of glyoxylate using L-serine. kcat is 5.0 sec(-1) for the transamination of glyoxylate using L-glutamate. {ECO:0000269|PubMed:31723261}; | null | null | null | FUNCTION: Catalyzes the transamination of glyoxylate into glycine using L-aspartate as the preferred amino group donor. Is essential for the growth of P.denitrificans in the presence of glycolate and glyoxylate since it functions in glyoxylate assimilation via the beta-hydroxyaspartate cycle (BHAC). Can catalyze the reverse reaction in vitro, and also use L-serine and L-glutamate as amino group donor, but with much less efficiency than L-aspartate. {ECO:0000269|PubMed:31723261}. | Paracoccus denitrificans (strain Pd 1222) |
A1C3L3 | FAP1_STRPA | MGKYKRAGETSRKTRVKMHKSGKNWVRTLISQIGLMHFLGGSISEKKINVDVYEQKNISASTILKGAVALGALTGATVVSGNVFADETVLAKETTLTTTDANEVKLSSENFDSEKAEEKISLSQSESASESVSESISESVSESVSTSESVSESVSESVSESISESVSESISESISESVSESTSTSIVLSESGAASGNKATSKGTEEKQDSVRENLDKMISEAEVLNDMAARKLITLDAEQQLELMKSLVATQSQLEATKNLIGDPNATVADLQIAYTTLGNNTQALGNELIKLNPNGQIYAVLNNTEASRAATLRSTTTGTKTTFTISDFSNGGTQYYWAGGNANNLKNPISSISAVYDSATGKISWTVEYDPTTILKSPALKTLKTYTGIYIDTSSDSKLSTPTNVLIDGAATNPVTNFYGNGSKGIEYVSKGTTKGVTKHTITFDTAFSGRANDLADLKIKMLAATTLSDPHFYEDGSKGNYGRYNGQTAPYVIANDSGTAIGGYQVSGVNADSIPSDTTSQSESTSKSESTSKSISESVIESISESVIGSVSESVSESVSESVSESITESVSESVSESISESVSESVSESISESVSESVSESISESVSESVSESISESVSESVSESISESISESVSESVSESISESVSESVSESISESVSESVSESISESVSESVSESISESVSESVSESISESVSESVSESISESVSESVSESISESVSESVSESISESVSESVSESISESVSESVSESISESVSESVSESISESVSESVSESVSESVSESVSESISESVSESVSESVSESVSESVSESVSESISESVSESVSESISESVSESVSESISESVSESVSESISESVSESVSESISESVSESVSESISESVSESVSESISESVSESVSESISESVSESVSESISESVSESVSESISESVSESVSESVSESVSESVSESVSESVSESISESVSESVSESISESVSESVSESISESVSESVSESISESVSESVSESISESVSESVSESVSESVSESVSESVSESVSESISESVSESVSESVSESISESVSESVSESISESVSESVSESISESVSESVSESVSESVSESVSESISESVSESVSESISESVSESVSESISESVSESVSESISESVSESVSESISESVSESVSESISESVSESVSESVSESVSESVSESISESVSESVSESISESVSESVSESVSESISESVSESVSESISESVSESVSESISESVSESVSESISESVSESVSESVSESVSESVSESVSESVSESVSESVSESISESVSESVSESVSESISESVSESVSESISESVSESVSESISESVSESVSESISESVSESVSESISESVSESVSESISESVSESVSESVSESVSESVSESISESVSESVSESISESVSESVSESISESVSESVSESISESVSESVSESVSESISESVSESVSESISESVSESVSESISESVSESVSESVSESVSESVSESVSESVSESVSESISESVSESVSESISESVSESVSESISESVSESVSESISESVSESVSESISESVSESVSESISESVSESVSESISESVSESVSESVSESVSESVSESISESVSESVSESISESVSESVSESVSESVSESVSESVSESVSESVSESISESVSESVSESVSESVSESVSESISESVSESVSESISESVSESVSESISESVSESVSESISESVSESVSESISESVSESVSESISESVSESVSESISESVSESVSESVSESVSESVSESVSESVSESISESVSESVSESISESVSESVSESISESVSESVSESVSESVSESVSESISESVSESVSESISESVSESVSESISESVSESVSESISESVSESVSESVSESISESVSESVSESISESVSESVSESISESVSESVSESISESVSESVSESISESVSESVSESISESVSESVSESVSESVSESVSESISESVSESISESVSESVSESISESVSESVSESISESVSESVSESISESVSESVSESISESVSESVSESISESVSESVSESISESVSESVSESISESVSESVSESVSESISESVSESVSESISESVSESVSESISESVSESVSESVSESVSESVSESVSESVSESVSESISESVSESVSESISESVSESVSESISESVSESVSESISESVSESVSESISESVSESVSESISESVSESVSESISESVSESVSESVSESVSESVSESISESVSESVSESVSESISESVSESVSESISESVSESVSESVSESVSESVSESVSESVSESVSESISESVSESVSESVSESVSESVSESISESVSESVSESISESVSESVSESISESVSESVSESISESVSESVSESISESVSESVSESISESVSESVSESISESVSESVSESISESVSESVSESVSESISESVSESVSESISESVSESVSESISESVSESVSESISESVSESVSESVSESVSESVSESVSESVSESISESVSESVSESISESVSESVSESVSESVSESVSESISESVSESISESVSESVSESISESVSESVSESISERTLPNTGENVSSSLGLVGLSGLLFGALLGRKKRKSEDAE | null | null | cell adhesion [GO:0007155] | cytoplasm [GO:0005737]; extracellular region [GO:0005576]; pilus [GO:0009289] | null | PF04286;PF00746;PF19258; | 2.60.40.2010;1.20.5.420; | Serine-rich repeat protein (SRRP) family | PTM: Glycosylated; occurs within the cytoplasm (PubMed:16997950, PubMed:20164186, PubMed:9632253). It is probable that most of the Ser residues in SSR1 and SSR2 are O-GlcNAcylated. Sequential glycosylation by sugar transferases are able to generate complex sugar polymorphisms (By similarity). {ECO:0000250|UniProtKB:A0A0H2URK1, ECO:0000269|PubMed:16997950, ECO:0000269|PubMed:20164186, ECO:0000269|PubMed:9632253}. | SUBCELLULAR LOCATION: Cytoplasm. Secreted. Secreted, cell wall; Peptidoglycan-anchor. Fimbrium. Note=Primarily but not exclusively exported by the accessory SecA2/SecY2 protein translocation apparatus. | null | null | null | null | null | FUNCTION: The major structural element of fimbriae. Required for adherence to saliva-coated hydroxyapatite beads (SHA), an in vitro tooth model. A Fap1-dependent increase in adherence is seen as the pH is reduced from pH 8 to pH 5. {ECO:0000269|PubMed:10594831, ECO:0000269|PubMed:9632253}. | Streptococcus parasanguinis |
A1C3L9 | GTFA_STRPA | MTIYNINLGIGWASSGVEYAQAYRAQILRSLGMPAKFIFTNMFQSENLEHFTKNIGFEDNEIIWLYGYFTDVKISGTTYKKDDLEATFSQCPTKKEASSDRKLIRYYFENQELYINASLYGENQEYVQRVEYVVKGKLIRKDYYSYTKVFSEFYSPGENGVQLCNRSFYNEDGSIAYEEILSNEKSTFVFSNKICYGLEELLEFMLEDLSLTKSDLILLDRATGIGQVVFENIGAAKLAVVIHAEHFNEKNTDEHNILWNNYYEYQFTNADKVNAFITSTERQKILLEEQFTQYTSLHPKIVAIPVGSLDQLKFPEQSRKSFSMMTGSRLAIEKHIDWLIEGVALAQKRLPELTFDIYGEGGERRKLTELLTKLHAGEFIELKGHKQLDEIYQNYELYLTASTSEGFGLTLMEAVGSGLPIIGFDVPYGNQTFVCSGENGLLIERPKGDDRSRIVQAFADSIYEYFTKFKMADAQQYSYNIAENYKHEKLVERWKDFIEEMLND | 2.4.1.- | null | glycolipid biosynthetic process [GO:0009247]; protein O-linked glycosylation via serine [GO:0018242]; sulfolipid biosynthetic process [GO:0046506] | cytoplasm [GO:0005737]; plasma membrane [GO:0005886]; protein N-acetylglucosaminyltransferase complex [GO:0017122] | glycosyltransferase activity [GO:0016757]; nucleotide binding [GO:0000166]; UDP-sulfoquinovose:DAG sulfoquinovosyltransferase activity [GO:0046510] | PF00534; | 3.40.50.2000; | Glycosyltransferase group 1 family, Glycosyltransferase 4 subfamily | null | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_01472, ECO:0000269|PubMed:21862581}. Cell membrane {ECO:0000255|HAMAP-Rule:MF_01472, ECO:0000269|PubMed:21862581}; Peripheral membrane protein {ECO:0000255|HAMAP-Rule:MF_01472, ECO:0000305|PubMed:21862581}. Note=Cell membrane association requires GtfB (Gtf2), protein is more active and protected from trypsin (PubMed:21862581). {ECO:0000255|HAMAP-Rule:MF_01472, ECO:0000269|PubMed:21862581}. | CATALYTIC ACTIVITY: Reaction=L-seryl-[protein] + UDP-N-acetyl-alpha-D-glucosamine = 3-O-[N-acetyl-alpha-D-glucosaminyl]-L-seryl-[protein] + H(+) + UDP; Xref=Rhea:RHEA:59872, Rhea:RHEA-COMP:9863, Rhea:RHEA-COMP:15471, ChEBI:CHEBI:15378, ChEBI:CHEBI:29999, ChEBI:CHEBI:57705, ChEBI:CHEBI:58223, ChEBI:CHEBI:143279; Evidence={ECO:0000255|HAMAP-Rule:MF_01472}; | null | PATHWAY: Protein modification; protein glycosylation. {ECO:0000255|HAMAP-Rule:MF_01472}. | null | null | FUNCTION: Required for polymorphic O-glycosylation of serine-rich repeat protein Fap1. Catalyzes the first step in glycosylation by transferring N-acetylglucosamine from UDP-GlcNAc to serine residues in Fap1. Part of the accessory SecA2/SecY2 system specifically required to export Fap1, a serine-rich fimbrial adhesin encoded upstream in the same operon. The GtfA-GtfB (Gtf1-Gtf2 in this bacteria) complex adds GlcNAc from UDP-GlcNAc to Fap1, attaching the first sugar residue. Cannot use not UDP-Glc as substrate. This subunit has very low glycosyltransferase activity; the GtfB stabilizing protein enhances membrane association, protease resistance and glycosyltransferase activity. {ECO:0000269|PubMed:16997950, ECO:0000269|PubMed:18083807, ECO:0000269|PubMed:20971868}. | Streptococcus parasanguinis |
A1C3M0 | GTFB_STRPA | MIRLFEWLTQESLDLHYSLEESGIHGTSIVLNDDGFLPEGIISPYTFFCEVEMDGSPLYFNQLEVPYLWQITGTNIEGEIWNRSSKRGVIHYHEPKYLRFVQSVDWLYPDGSIYMTDHYNKYGWAFARTYFFSDQQVSHKKYYTKSGQEVLSENILTGDILLNWKGKVYHFTKKVDFFLFYFKKSGLDLSSIWYNSLGMPFLISYYLGGEGRDILFWQENLADQLPGNMQIIFSGRTSRTKKVIVQDRSVYKKLLHLVEEKNKEMISFLNIIYPKLRENYSRKEILIVTNSDQIEGIETLTDNLSAYTFHIGALTSMSDKLQNIGQKENVLLYPNMSPKTMLDLLEQCDIYLDINHGNEVLSIVRLAFERSLLILAYDNTVHSPIFHHESGIFNHSKPQTLSDWLLNLDDYSQTVSCWRSDLFPMTYRDYKQVLVSNVD | null | null | protein glycosylation [GO:0006486]; regulation of protein stability [GO:0031647] | plasma membrane [GO:0005886]; protein N-acetylglucosaminyltransferase complex [GO:0017122] | null | null | null | GtfB family | null | SUBCELLULAR LOCATION: Cell membrane {ECO:0000305|PubMed:21862581}; Peripheral membrane protein {ECO:0000305|PubMed:21862581}. | null | null | PATHWAY: Protein modification; protein glycosylation. {ECO:0000255|HAMAP-Rule:MF_01473, ECO:0000269|PubMed:18083807, ECO:0000269|PubMed:20971868, ECO:0000269|PubMed:21862581}. | null | null | FUNCTION: Required for the polymorphic O-glycosylation of the serine-rich repeat protein Fap1. A stabilizing protein that is part of the accessory SecA2/SecY2 system specifically required to export Fap1, a serine-rich fimbrial adhesin encoded upstream in the same operon. The GtfA-GtfB (Gtf1-Gtf2 in this bacteria) complex adds GlcNAc from UDP-GlcNAc to Fap1, attaching the first sugar residue. Cannot use not UDP-Glc as substrate. Stabilizes the glycosylation activity of GtfA, causing it to partially localize to the cellular membrane where it is more protease resistant. {ECO:0000269|PubMed:18083807, ECO:0000269|PubMed:20971868, ECO:0000269|PubMed:21862581}. | Streptococcus parasanguinis |
A1C8C3 | OBLA_ASPCL | MACKYSTLIDSSLYDREGLCPGIDLRRHVAGELEEVGAFRAQEDWRRLVGPLPKPYAGLLGPDFSFITGAVPECHPDRMEIVAYALEFGFMHDDVIDTDVNHASLDEVGHTLDQSRTGKIEDKGSDGKRQMVTQIIREMMAIDPERAMTVAKSWASGVRHSSRRKEDTNFKALEQYIPYRALDVGYMLWHGLVTFGCAITIPNEEEEEAKRLIIPALVQASLLNDLFSFEKEKNDANVQNAVLIVMNEHGCSEEEARDILKKRIRLECANYLRNVKETNARADVSDELKRYINVMQYTLSGNAAWSTNCPRYNGPTKFNELQLLRSEHGLAKYPSRWSQENRTSGLVEGDCHESKPNELKRKRNGVSVDDEMRTNGTNGAKKPAHVSQPSTDSIVLEDMVQLARTCDLPDLSDTVILQPYRYLTSLPSKGFRDQAIDSINKWLKVPPKSVKMIKDVVKMLHSASLMLDDLEDNSPLRRGKPSTHSIYGMAQTVNSATYQYITATDITAQLQNSETFHIFVEELQQLHVGQSYDLYWTHNTLCPTIAEYLKMVDMKTGGLFRMLTRMMIAESPVVDKVPNSDMNLFSCLIGRFFQIRDDYQNLASADYAKAKGFAEDLDEGKYSFTLIHCIQTLESKPELAGEMMQLRAFLMKRRHEGKLSQEAKQEVLVTMKKTESLQYTLSVLRELHSELEKEVENLEAKFGEENFTLRVMLELLKV | 2.5.1.29; 2.5.1.81; 4.2.3.145 | COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250|UniProtKB:Q12051, ECO:0000250|UniProtKB:Q40577}; Note=Binds 4 Mg(2+) ions per subunit. {ECO:0000250|UniProtKB:Q12051, ECO:0000250|UniProtKB:Q40577}; | alcohol biosynthetic process [GO:0046165]; ketone biosynthetic process [GO:0042181]; mycotoxin biosynthetic process [GO:0043386]; terpenoid biosynthetic process [GO:0016114] | null | farnesyltranstransferase activity [GO:0004311]; geranylfarnesyl diphosphate synthase activity [GO:0044687]; lyase activity [GO:0016829]; metal ion binding [GO:0046872] | PF00348;PF19086; | 1.10.600.10; | Terpene synthase family; FPP/GGPP synthase family | null | null | CATALYTIC ACTIVITY: Reaction=(2E,6E)-farnesyl diphosphate + isopentenyl diphosphate = (2E,6E,10E)-geranylgeranyl diphosphate + diphosphate; Xref=Rhea:RHEA:17653, ChEBI:CHEBI:33019, ChEBI:CHEBI:58756, ChEBI:CHEBI:128769, ChEBI:CHEBI:175763; EC=2.5.1.29; Evidence={ECO:0000269|PubMed:23324037, ECO:0000269|PubMed:28362483}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:17654; Evidence={ECO:0000269|PubMed:23324037, ECO:0000269|PubMed:28362483}; CATALYTIC ACTIVITY: Reaction=(2E,6E,10E)-geranylgeranyl diphosphate + isopentenyl diphosphate = (2E,6E,10E,14E)-geranylfarnesyl diphosphate + diphosphate; Xref=Rhea:RHEA:25694, ChEBI:CHEBI:33019, ChEBI:CHEBI:57907, ChEBI:CHEBI:58756, ChEBI:CHEBI:128769; EC=2.5.1.81; Evidence={ECO:0000269|PubMed:23324037, ECO:0000269|PubMed:28362483}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:25695; Evidence={ECO:0000269|PubMed:23324037, ECO:0000269|PubMed:28362483}; CATALYTIC ACTIVITY: Reaction=(2E,6E,10E,14E)-geranylfarnesyl diphosphate + H2O = diphosphate + ophiobolin F; Xref=Rhea:RHEA:41552, ChEBI:CHEBI:15377, ChEBI:CHEBI:33019, ChEBI:CHEBI:57907, ChEBI:CHEBI:78293; EC=4.2.3.145; Evidence={ECO:0000269|PubMed:23324037, ECO:0000269|PubMed:28362483}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:41553; Evidence={ECO:0000269|PubMed:23324037, ECO:0000269|PubMed:28362483}; | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=0.024 uM for geranylgeranyl diphosphate (GGDP) {ECO:0000269|PubMed:28362483}; | PATHWAY: Secondary metabolite biosynthesis; terpenoid biosynthesis. {ECO:0000269|PubMed:23324037}. | null | null | FUNCTION: Bifunctional sesterterpene synthase; part of the gene cluster that mediates the biosynthesis of the sesterterpenes ophiobolins, fungal phytotoxins with potential anti-cancer activities (PubMed:23324037, PubMed:27116000, PubMed:28362483). The first step of the pathway is performed by the sesterterpene synthase oblA that possesses both prenyl transferase and terpene cyclase activity, converting isopentenyl diphosphate and dimethylallyl diphosphate into geranylfarnesyl diphosphate (GFPP) and further converting GFPP into ophiobolin F, respectively (PubMed:23324037). Other sesterterpenoids (C(25) terpenoids) are found as minor products of oblA (PubMed:23324037). It is expected that ophiobolin F is then oxidized to ophiobolin A via ophiobolin C and ophiobolin B intermediates by the combined action of the cytochrome P450 monooxygenase oblB and the FAD-dependent oxidoreductase oblC (Probable). Although oblB catalyzes multistep oxygenations at C5 and C21/C7 in a relatively efficient manner, it is unable to convert ophiobolin F to ophiobolin C and produces instead several unexpected derivatives (PubMed:27116000). {ECO:0000269|PubMed:23324037, ECO:0000269|PubMed:27116000, ECO:0000269|PubMed:28362483, ECO:0000305|PubMed:27116000}. | Aspergillus clavatus (strain ATCC 1007 / CBS 513.65 / DSM 816 / NCTC 3887 / NRRL 1 / QM 1276 / 107) |
A1C9U5 | SKP1_ASPCL | MSTTVTLTSSDGVDLTVDRDVAERSVLIKNMLEDLGESGEAIPIPNVNEVVLKKVIEWCTHHKNDPPSTGDDDDSRRKTTDIDEWDQKFMQVDQEMLFEIILAANYLDIKALLDVGCKTVANMIKGKSPEEIRKTFNIQNDFTPEEEDQIRRENEWAEE | null | null | exit from mitosis [GO:0010458]; G1/S transition of mitotic cell cycle [GO:0000082]; G2/M transition of mitotic cell cycle [GO:0000086]; kinetochore assembly [GO:0051382]; mitotic nuclear membrane biogenesis [GO:0101026]; negative regulation of cytoplasmic translation [GO:2000766]; negative regulation of mitotic metaphase/anaphase transition [GO:0045841]; positive regulation of glucose transmembrane transport [GO:0010828]; protein neddylation [GO:0045116]; protein ubiquitination [GO:0016567]; regulation of DNA recombination [GO:0000018]; regulation of exit from mitosis [GO:0007096]; regulation of protein-containing complex assembly [GO:0043254]; resolution of meiotic recombination intermediates [GO:0000712]; SCF-dependent proteasomal ubiquitin-dependent protein catabolic process [GO:0031146]; septin ring assembly [GO:0000921]; silent mating-type cassette heterochromatin formation [GO:0030466]; vacuolar acidification [GO:0007035]; vacuolar proton-transporting V-type ATPase complex assembly [GO:0070072] | CBF3 complex [GO:0031518]; kinetochore [GO:0000776]; nuclear SCF ubiquitin ligase complex [GO:0043224]; RAVE complex [GO:0043291]; single-stranded DNA-dependent ATP-dependent DNA helicase complex [GO:0017117] | cullin family protein binding [GO:0097602]; DNA replication origin binding [GO:0003688]; ubiquitin protein ligase activity [GO:0061630] | PF01466;PF03931; | null | SKP1 family | null | null | null | null | PATHWAY: Protein modification; protein ubiquitination. | null | null | FUNCTION: Essential component of the SCF (SKP1-CUL1-F-box protein) E3 ubiquitin ligase complexes, which mediate the ubiquitination and subsequent proteasomal degradation of target proteins. Controls sulfur metabolite repression, probably by mediating the inactivation or degradation of the metR transcription factor (By similarity). {ECO:0000250}. | Aspergillus clavatus (strain ATCC 1007 / CBS 513.65 / DSM 816 / NCTC 3887 / NRRL 1 / QM 1276 / 107) |
A1CAZ7 | UBA4_ASPCL | MENLEQTCASLRAQIAATEAQLAGLKRDLEVAEQAAAEIKAQDVKSTGIREEGSEKKNPWPLLSEEYKRYGRQMIVPQLGLQGQLKLRSARVLIVGAGGLGCPAALYLAGAGVGTLGLVDGDTVEHSNLHRQVLHRSKNVGKFKVDSAIEYLRELNPHPTYVPYRAHLTPQEAPEIFKDYDIVLDCTDNPATRYLISDTAVLLGKPLVSASALRTEGQLIVLNNPPRPVGDKSGGPCYRCVFPKPPPATSVVSCADGGIIGPVVGTMGVLQAIEAIKVITSSPADETSASPPSLLIFSAYSTPPFRSIKIRSRRANCAVCSAEASVTVETLKTGSTDYVFFCGVAGPETLLRPEERITPLEFKKKHPGQVSHEQELGGSKEPTIIDVREQVQFDICSLDNSINIPISTILSSAASPTTSTPESLPSWLPHDIVSSSSTDPIYVVCRLGNDSQIAVRKMKELGLDQGGKRFICDIQGGLRAWREQIDPDWPEY | 2.7.7.80; 2.8.1.11 | COFACTOR: Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000255|HAMAP-Rule:MF_03049}; Note=Binds 1 zinc ion per subunit. {ECO:0000255|HAMAP-Rule:MF_03049}; | cell budding [GO:0007114]; cellular response to oxidative stress [GO:0034599]; invasive growth in response to glucose limitation [GO:0001403]; Mo-molybdopterin cofactor biosynthetic process [GO:0006777]; protein urmylation [GO:0032447]; regulation of pseudohyphal growth [GO:2000220]; tRNA wobble position uridine thiolation [GO:0002143] | cytosol [GO:0005829] | AMPylase activity [GO:0070733]; ATP binding [GO:0005524]; identical protein binding [GO:0042802]; metal ion binding [GO:0046872]; molybdopterin-synthase adenylyltransferase activity [GO:0061605]; molybdopterin-synthase sulfurtransferase activity [GO:0061604]; sulfotransferase activity [GO:0008146]; thiosulfate sulfurtransferase activity [GO:0004792]; URM1 activating enzyme activity [GO:0042292] | PF00581;PF00899; | 3.40.50.720;3.40.250.10; | HesA/MoeB/ThiF family, UBA4 subfamily | null | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_03049}. | CATALYTIC ACTIVITY: Reaction=[molybdopterin-synthase sulfur-carrier protein]-C-terminal Gly-Gly + ATP + H(+) = [molybdopterin-synthase sulfur-carrier protein]-C-terminal Gly-Gly-AMP + diphosphate; Xref=Rhea:RHEA:43616, Rhea:RHEA-COMP:12159, Rhea:RHEA-COMP:12202, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:33019, ChEBI:CHEBI:90618, ChEBI:CHEBI:90778; EC=2.7.7.80; Evidence={ECO:0000255|HAMAP-Rule:MF_03049}; CATALYTIC ACTIVITY: Reaction=[molybdopterin-synthase sulfur-carrier protein]-C-terminal Gly-Gly-AMP + AH2 + S-sulfanyl-L-cysteinyl-[cysteine desulfurase] = [molybdopterin-synthase sulfur-carrier protein]-C-terminal Gly-NH-CH2-C(O)SH + A + AMP + H(+) + L-cysteinyl-[cysteine desulfurase]; Xref=Rhea:RHEA:48612, Rhea:RHEA-COMP:12157, Rhea:RHEA-COMP:12158, Rhea:RHEA-COMP:12159, Rhea:RHEA-COMP:12160, ChEBI:CHEBI:13193, ChEBI:CHEBI:15378, ChEBI:CHEBI:17499, ChEBI:CHEBI:29950, ChEBI:CHEBI:61963, ChEBI:CHEBI:90618, ChEBI:CHEBI:90619, ChEBI:CHEBI:456215; EC=2.8.1.11; Evidence={ECO:0000255|HAMAP-Rule:MF_03049}; | null | PATHWAY: tRNA modification; 5-methoxycarbonylmethyl-2-thiouridine-tRNA biosynthesis. {ECO:0000255|HAMAP-Rule:MF_03049}.; PATHWAY: Cofactor biosynthesis; molybdopterin biosynthesis. {ECO:0000255|HAMAP-Rule:MF_03049}. | null | null | FUNCTION: Plays a central role in 2-thiolation of mcm(5)S(2)U at tRNA wobble positions of cytosolic tRNA(Lys), tRNA(Glu) and tRNA(Gln). Also essential during biosynthesis of the molybdenum cofactor. Acts by mediating the C-terminal thiocarboxylation of sulfur carriers urm1 and mocs2a. Its N-terminus first activates urm1 and mocs2a as acyl-adenylates (-COAMP), then the persulfide sulfur on the catalytic cysteine is transferred to urm1 and mocs2a to form thiocarboxylation (-COSH) of their C-terminus. The reaction probably involves hydrogen sulfide that is generated from the persulfide intermediate and that acts as a nucleophile towards urm1 and mocs2a. Subsequently, a transient disulfide bond is formed. Does not use thiosulfate as sulfur donor; nfs1 probably acting as a sulfur donor for thiocarboxylation reactions (By similarity). {ECO:0000250}. | Aspergillus clavatus (strain ATCC 1007 / CBS 513.65 / DSM 816 / NCTC 3887 / NRRL 1 / QM 1276 / 107) |
A1CLY8 | CCSA_ASPCL | MGSFQNSSEPIAIIGTGCRFPGGCDSPSKLWELLRAPRDLLKEIPESRFSVDSFYHPDNAHHGTSNVRHSYFLEEDLRQFDVQFFGIKPIEANAVDPQQRLLLETVYEGLESAGLSIQRLQGSDTAVYVGVMSADFTDLVGRDTETFPTYFATGTARSILSNRLSYFFDWHGPSLTIDTACSSSLIAMHHAVQTLRSGDSSLAIVAGSNLILGPEQYIAESKLQMLSPTGRSRMWDAAADGYARGEGVAAIVLKRLSQAIADGDHIECVIRETGVNQDGKTPGITMPSATAQAALIRSTYAKAGLDLSNRSDRPQYFEAHGTGTPAGDPIEARAIQTAFFGPDLNFTADSRKDTLFVGSIKTVVGHTEGTAGLAAVIKASLALQSGTIPPNRLLEQLNPAIKPFYNSLKILAAAEDWPQLSRGGVRRVSVNSFGFGGANSHAILESYEPSLHSHKGTRDISFSPFTFSAASETALVASLRAYRDLLSTRSDVRLTDLAWTLNSRRSTLASRVAIAASDKDDLVLKLDDRAENYDGSDTFMDAGHRKPNANELRILGVFTGQGAQWARMGAELIEQCPGASKVVDALEQSLRSLPPQDRPTWSLREQLLAPPSSSMVSTASISQPLCTAIQIMLVDMLREAGIQFSAVVGHSSGEIGAAYAAGCLSAKDAIRVAYYRGVHLKSALQKGSMLAVGTTFEDAQDLCNLPTFEDRLCVAASNSPSSVTISGDSDAIEEIKVVFDEEKKFTRLLKVDRAYHSHHMQDCVEPYVRSLRQCSVTFRPPNRNQCVWISSVFVQDIHQLSEDGSDRYWGSNLARPVMFAEALQLLLSLEGSFDLAVEVGPHPALKGPASQTIQDALGYSIPYTGVLSRGNSDVEAFAAALGSIWTAFGDGAVDFSRLQKFTSGSAAQPQLLKGLPTYQWDHNRVFWHESRVSKAFRTRKDVPNELLGRQVLDGAPNQLRWRNILRPREIAWLEGHQVQGQMVFPCAGYVSACAEASMRLAVGQNVESIELEEFVVGQAIVFNDSNSEVETLATLTEVVHRQQTISANFAFYSCPTGGESLELVRNASCRLRITVGDSAVDLLQPQAEADFALLEVESDRFYNALGQLGFGYTGPFRSLTALKRKLGIARGLIENAPPSFNHSQPLLIHPATLDAAIQSIMLAYCYPGDSMLRAIHLPTGIEKLTLNPVNCLKFAGQSVQVPFDSSASTGSGRSLQGDVSIYSLDGSRAVQLEGLQTQPLSSPTEASDLNIFTELVWGVDRPDCEEILRTTVVEDFDAELLFSLERVAYFYLRSLGEAVPERERNGLEWHHKRLFAYVDHVLSRVARGVNRFARPEWAADSKNDILKILQKYPDNIDLRLMRAVGENLPAVVRGQLTMLEPMIQDNMLNDFYVIAHGMPRYTKYLAAMASQISHRYPHMNVLEIGAGTGGATKSFLKELGEGFSTYTFTDISSGFFEKASQVFASYSAKMNFKVLDIEKDIESQGFAPESFDLIIASLVLHATRDLAQTVRNVRRLLKPGGYLLLLEITENEQMRFGLIFGGLPGWWLGYEDGRPFSPCVDIEEWSRVLEQNGFSGIETAIPHHDTLPAPLSVIVSQAVNEKVQFLHNPLDSIRGSTVIPRLTIIGGGGRRSAQLIDAVSSLVQPQCGQLRVVDSLQKICSEVLPVGGSVLSLTDFDEPVFKSMDADKLRGFQEIFKQSKNVLWVTQGSRSGDPYARMVVGFGRTIVLEMLHLRLQFLDVSPSSSPDASAIAEAMLRLEVSGSWEDEGAEDGAVLHSVEPELSISDGRCWVPRFKPNKEQNERYNSVRRSIETEQSFSDTCVELVYRDNSLSLLEVTHSSSEPLAEPSTKYLELDVNYSVSKAVEVVPGCYLFLILGRDTDTGDRFIALSPKQSSRVRIPRALVLPQHTSHGTINENSLDAFFHEIVARSILRDVPYGSAAIALQPNSLLADALREAAQDKGVTLHLWSTQASDLESEWTYIHRKASKTEVQNAIPRNVTCFFDMGGDESIATKILACLPDHTQAKKEASITAHEAHLIPTVLPDIRSLLMDIGRAMRTRGKSSSPDLRIVDLTDIVKGQADSETSIINWLESSSRVPVAVEPIEARVQFRSDRTYWLVGLTGGLGLSLCEWMAQQGARYIVLSSRSPKVDGRWLAKMNRMGVTVEVVANDISNRDSVQRVYNKIRTELPPISGVAQGAMVLHDTMFLDLDMERMNKVLRPKVDGSTYLEEIFHDTELEFFVFFSSMAAVTGNPGQSAYAAANMFMASLANQRRQRGLNASAVHIGAIFGNGYVTRELTLVQQEFLRKVGNLWLSEHDFRRLFAEAVYAGRHHRGRSPELSTGLKILESDESESITWFNNPVFQHCIKQSGRVDLISETSTSAAPVKVRLAEASSSADIYDIISDAFVTKLKTSLQVEGDRPIVDLTADTLGIDSLVAVDIRSWFIKELQVEIPVLKILSGATVGEMVTQAQELLPKELTPNLDPNAEAKPSKPKNTVQPKQQTKKTIQLQNVAKAPQPALSQQVSSGVQNMIKTNPPKEAEAKQPRPEVKQAAPKDSQYPTALETPSKLQDPSRNIVVAKDLAAEEKHLTDQEPVPSNMSSSSWSEIDESEGKVETSSSSSSTSASQIITKTKPVEVKKSVPMAFGQSRFWFLRHYLEDPSSFNITVSIQLDGPLKIDHFARAVQVVGQRHEALRTRFVTDEAQGTTKQEVLALSNLTLEERTISTDEEAEGVYQELKGYAFDLEKGENIRIILLKRSNRSFTLIIAYHHINMDGVSLEVLLRDLQMAYDSKFLSPRILQYADFSEQQRRDYQSGKWAEDLAFWKKEFQTMPGPLPLLSMARTSTRSPLTAYKTHSAEFHIDPATLDTIQSTCQRMKVTPFHFHLAVFYTMLIRLVDVENLCIGISSANRSQQDTLQSVGLYLNLLPLNFTPQLDQTFTNVLHIVREKSVQAFAHSKVPFDVIVNELGAARSATHSPLFQVLVNYRAGVSERRSFCNCDSKVLTFEQGQTPYDLSLDVIDNPGGDCHVIMAGQSVLYGAEHVAVLRGVYQNLLVAFSRNPALRLNVPPLYDTDEVKHAIKLGHGPAYNYQWPATIPERIDEIVERYPTHVALIDGDGRKMSYTEMARRVNTLAVVLLRQDIGQGSKVGVFMEPGSSWICSLLAILRLDAIYIPLDSRMGLDRLSTIVRDCKPDLLLVDNTTLSNVALLGLSCPTLNVDVVSPGSDQQHVPNTAQPSSTAVIMYTSGSTGVPKGIVMQHHTFRNNIETSTEKWDFREGRETTLQQSSYSFDMSLSQTFLTLSNGGTLRIVPKKLRGDPKAIASLITAEGITFTETTPSEYISWLRYGDVDDLRKSKWRIAVSGGETITTNLTGLLRQLEKSDLRLIDCYGPTEITFCSHGREVQYDGEGDILSPAFRTWPNYSVYIVDSHMKPVPIGIPGEILIGGAGVVAGYVHSELDARGFARNNFMNTMFLENAWTRLHRTGDFGRLDQEGNLILGGRIAGDTQVKLRGIRIDLQEIESAILSSGDGKIVDAAVTVRESADSGSEYLMAFVTTLDAGDLSLERIRQELPLPQHMRPANIITLDQLPMTASNKVDRLALKSLPLPPGSHVADTGTDESPSMAKMRDVWATVIPQEVLAHFELGPASNFFQVGGDSMLLVRLQTEINKVFGTSISLFQLFDASSLTGMVSLIDHSESTSQRSEVDWETETTISPSLLQVPATKRFFAHPAVVVLTGATGFLGRAIVNRLLKDCSVQKIHCVAVRRDPSSLPDDFKSPKVVLHRGDLTLPQLGLTDRAATEIFAEADAVIHNGADVSFMKTYQSLKQANLEATKELVRLSAPHRLSFHYISSASVTRLAGQESFDQSSVSAFPPSAEDGYVASKWASERYLEKVSDQCGLPIWIHRPSSIVGEGAPDTDMMASLLGYSRTLRAIPQTDGWTGWLDFVSADRVAMQIADEVYEDYSWPGTVKYLYEAGDREIPLSDLRGVLERETGESFESIPLEEWVLRAEGQGLHPLLGEYLRRVSGIPLVLPRLVQQGSFF | 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 | null | null | PATHWAY: Mycotoxin biosynthesis. {ECO:0000269|PubMed:21983160}. | null | null | FUNCTION: Hybrid PKS-NRPS synthetase; part of the gene cluster that mediates the biosynthesis of the mycotoxins cytochalasins E and K (PubMed:21983160). The hybrid PKS-NRPS synthetase ccsA and the enoyl reductase ccsC are responsible for fusion of phenylalanine with an octaketide backbone and subsequent release of the stable tetramic acid precursor (PubMed:21983160, PubMed:27551732). The polyketide synthase module (PKS) of the PKS-NRPS ccsA is responsible for the synthesis of the octaketide backbone (PubMed:21983160). The downstream nonribosomal peptide synthetase (NRPS) amidates the carboxyl end of the octaketide with a phenylalanine (PubMed:21983160). A reductase-like domain (R) at the C-terminus catalyzes the reductive release of the polyketide-amino acid intermediate (PubMed:21983160). Because ccsA lacks a designated enoylreductase (ER) domain, the required activity is provided the enoyl reductase ccsC (PubMed:21983160, PubMed:27551732). Upon formation of the 11-membered carbocycle-fused perhydroisoindolone intermediate, a number of oxidative steps are required to afford the final cytochalasin E and K, including two hydroxylations at C17 and C18, one alcohol oxidation at C17, one epoxidation at C6 and C7 and two Baeyer-Villiger oxidations (PubMed:21983160). The oxidative modification at C17, C18 and the C6-C7 epoxidation are likely to be catalyzed by the two cytochrome P450 oxygenases ccsD and ccsG (PubMed:21983160). CcsD may be responsible for the epoxidation of the C6-C7 double bond (PubMed:21983160). CcsG may be responsible for the successive oxidative modifications at C17 and C18 (PubMed:21983160). The double Baeyer-Villiger oxidations of ketocytochalasin to precytochalasin and cytochalasin Z(16) are among the final steps leading to cytochalasin E and K and are catalyzed by ccsB (PubMed:21983160, PubMed:24838010). The first oxygen insertion step follows that of the classic BVMO mechanism, generating the ester precytochalasin (PubMed:24838010). Release of precytochalasin into an aqueous environment can generate the shunt product iso-precytochalasin through spontaneous isomerization (PubMed:24838010). Alternatively, precytochalasin can undergo further oxidation by ccsB to yield the in-line carbonate-containing cytochalasin Z(16) (PubMed:24838010). Cytochalasin Z(16) is a precursor to cytochalasin E and cytochalasin K, whereas iso-precytochalasin is a precursor to cytochalasin Z(17) and rosellichalasin (PubMed:21983160, PubMed:24838010). The hydrolyase ccsE may catalyze hydrolysis of epoxide bond in cytochalasin E to afford cytochalasin K (PubMed:21983160). The function of ccsF has not been assigned but it may play a role in post-PKS-NRPS biosynthetic step, resistance or transport of cytochalasins and related PKS-NRPS products (PubMed:21983160). {ECO:0000269|PubMed:21983160, ECO:0000269|PubMed:24838010, ECO:0000269|PubMed:27551732}. | Aspergillus clavatus (strain ATCC 1007 / CBS 513.65 / DSM 816 / NCTC 3887 / NRRL 1 / QM 1276 / 107) |
A1CP85 | ARO1_ASPCL | MIEPTKISILGQESIVADFGLWRNYVAKDLISGCPSTTYVLITDTNIGSIYTPSFQKSFEEAAAAVTPSPRLLTYYAPPGEVSKSRQTKADIEDWMLSQSPPCGRDTVIIALGGGVIGDLTGFVAATYMRGVRFVQVPTTLLAMVDSSIGGKTAIDTPLGKNLIGAIWQPARIYIDLEFLETLPVREFINGMAEVIKTAAISSEEEFTALEDNAETILAAVRREVKPGQRRFDGIEQILKARILASARHKAFVVSEDEREGGLRNLLNWGHSIGHAIEAILTPQILHGECVAIGMVKEAELARHLGVLKGVAVARIVKCIAAYGLPTSLKDARIRKLTAGKHCSVDQLLFNMALDKKNDGPKKKVVLLSAIGRTYEPRASVVANEDIGVVLAPSIEVFPGVSPKSTVICAPPGSKSISNRALVLAALGSGTCRIKNLLHSDDTEVMLNALERIGAATFSWEEEGEVLVVNGKGGALQAHPSELYLGNAGTASRFLTTVATLATPSNVDFSILTGNNRMKQRPIGDLVEALIANGAQVEYMESKGSLPLKIAASGGFTGGQINLAAKVSSQYVSSLLMCAPYAKEPVTLKLVGGKPISQPYIDMTTAMMRSFGIDVQKSTTEEHTYHIPQGRYTNPAEYVVESDASSATYPLAIAAVTGTTCTVPNIGSKSLQGDARFAVDVLRPMGCTVEQTDTSTTVTGPADGVLRPLPNVDMEPMTDAFLGASVLAAIARGEGSNHTTRIYGIANQRVKECNRIKAMHDELAKFGVVCREHEDGLEIDGIDRANLRQPAGGVFCYDDHRVAFSFSVLSLVAPKPTLILEKECVGKTWPGWWDTLRLKFAVKLEGRELKEAESPVLTSAEKASASVFIIGMRGAGKTTSGHWVASTLNRPFIDLDDELERIEGMTIPDIIKERGWQGFRDAELSLLQRTMKERPTGHVFACGGGVVEVPEARKLLINWHKSKGNVLLIMRDIKQVMDFLNIDKTRPAYVEDMMGVWLRRKPWFQECSNIQYYSQHASSGLTRASEDFARFVKIVTGQVDSLGAIKKKQHSFFVSLTLPDLRPAGDILEQACVGSDAVELRVDLLKDPSSSNGIPSVDYVAEQMSFLRSHTTLPLIFTIRTKSQGGFFPDEAHEEAMQLYQLAFRSGCEFVDLEIAFPDELLRTVSEMKGYSKIIASHHDPKGELSWANMSWMKYYNRALEYGDVIKLVGVATKLDDNTALRKFKSWAEEAHDVPLIAINMGDNGQLSRILNGFMTPVSHPALPFKAAPGQLSATEICKGLSLMGQIKKKRFALFGTPISESRSPALHNSLFAELGLPHEYTRLETANAEDVKEFIRAPDFGGASVTIPLKLDIMPLLDEIAPEAEIIGAVNTIVPVSDGEGKPQRLVGHNTDWQGMVQCLRNAGAYGSNGDASALVVGGGGTCRAGIYALHQMGYSPIYIVGRNLGKLQAMASTFPSSYNIRILEGNETLEHVPHVAIGTIPGDQPIDPGMREILCHMFARAEEADADAVRSIEGSPRVLLEMAYKPPVTALMQLATDAGWTTIPGLEVLVGQGFYQGGITQFQHWTGIRPLYEHARDAVLGTKAD | 1.1.1.25; 2.5.1.19; 2.7.1.71; 4.2.1.10; 4.2.3.4 | COFACTOR: Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Note=Binds 2 Zn(2+) ions per subunit.; | amino acid biosynthetic process [GO:0008652]; aromatic amino acid family biosynthetic process [GO:0009073]; chorismate biosynthetic process [GO:0009423]; phosphorylation [GO:0016310] | cytoplasm [GO:0005737] | 3-dehydroquinate dehydratase activity [GO:0003855]; 3-dehydroquinate synthase activity [GO:0003856]; 3-phosphoshikimate 1-carboxyvinyltransferase activity [GO:0003866]; ATP binding [GO:0005524]; metal ion binding [GO:0046872]; shikimate 3-dehydrogenase (NADP+) activity [GO:0004764]; shikimate kinase activity [GO:0004765] | PF01761;PF01487;PF00275;PF08501;PF01202; | 3.40.50.1970;3.20.20.70;1.20.1090.10;3.65.10.10;3.40.50.10860;3.40.50.720;3.40.50.300; | Sugar phosphate cyclases superfamily, Dehydroquinate synthase family; EPSP synthase family; Shikimate kinase family; Type-I 3-dehydroquinase family; Shikimate dehydrogenase family | null | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_03143}. | CATALYTIC ACTIVITY: Reaction=7-phospho-2-dehydro-3-deoxy-D-arabino-heptonate = 3-dehydroquinate + phosphate; Xref=Rhea:RHEA:21968, ChEBI:CHEBI:32364, ChEBI:CHEBI:43474, ChEBI:CHEBI:58394; EC=4.2.3.4; Evidence={ECO:0000255|HAMAP-Rule:MF_03143}; CATALYTIC ACTIVITY: Reaction=3-dehydroquinate = 3-dehydroshikimate + H2O; Xref=Rhea:RHEA:21096, ChEBI:CHEBI:15377, ChEBI:CHEBI:16630, ChEBI:CHEBI:32364; EC=4.2.1.10; Evidence={ECO:0000255|HAMAP-Rule:MF_03143}; CATALYTIC ACTIVITY: Reaction=NADP(+) + shikimate = 3-dehydroshikimate + H(+) + NADPH; Xref=Rhea:RHEA:17737, ChEBI:CHEBI:15378, ChEBI:CHEBI:16630, ChEBI:CHEBI:36208, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349; EC=1.1.1.25; Evidence={ECO:0000255|HAMAP-Rule:MF_03143}; CATALYTIC ACTIVITY: Reaction=ATP + shikimate = 3-phosphoshikimate + ADP + H(+); Xref=Rhea:RHEA:13121, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:36208, ChEBI:CHEBI:145989, ChEBI:CHEBI:456216; EC=2.7.1.71; Evidence={ECO:0000255|HAMAP-Rule:MF_03143}; CATALYTIC ACTIVITY: Reaction=3-phosphoshikimate + phosphoenolpyruvate = 5-O-(1-carboxyvinyl)-3-phosphoshikimate + phosphate; Xref=Rhea:RHEA:21256, ChEBI:CHEBI:43474, ChEBI:CHEBI:57701, ChEBI:CHEBI:58702, ChEBI:CHEBI:145989; EC=2.5.1.19; Evidence={ECO:0000255|HAMAP-Rule:MF_03143}; | null | PATHWAY: Metabolic intermediate biosynthesis; chorismate biosynthesis; chorismate from D-erythrose 4-phosphate and phosphoenolpyruvate: step 2/7. {ECO:0000255|HAMAP-Rule:MF_03143}.; PATHWAY: Metabolic intermediate biosynthesis; chorismate biosynthesis; chorismate from D-erythrose 4-phosphate and phosphoenolpyruvate: step 3/7. {ECO:0000255|HAMAP-Rule:MF_03143}.; PATHWAY: Metabolic intermediate biosynthesis; chorismate biosynthesis; chorismate from D-erythrose 4-phosphate and phosphoenolpyruvate: step 4/7. {ECO:0000255|HAMAP-Rule:MF_03143}.; PATHWAY: Metabolic intermediate biosynthesis; chorismate biosynthesis; chorismate from D-erythrose 4-phosphate and phosphoenolpyruvate: step 5/7. {ECO:0000255|HAMAP-Rule:MF_03143}.; PATHWAY: Metabolic intermediate biosynthesis; chorismate biosynthesis; chorismate from D-erythrose 4-phosphate and phosphoenolpyruvate: step 6/7. {ECO:0000255|HAMAP-Rule:MF_03143}. | null | null | FUNCTION: The AROM polypeptide catalyzes 5 consecutive enzymatic reactions in prechorismate polyaromatic amino acid biosynthesis. {ECO:0000255|HAMAP-Rule:MF_03143}. | Aspergillus clavatus (strain ATCC 1007 / CBS 513.65 / DSM 816 / NCTC 3887 / NRRL 1 / QM 1276 / 107) |
A1CQG2 | RSP5_ASPCL | MGSNLPSQPNLRLTIIAADGLYKRDVFRFPDPFAVATVGGEQTQTTSVIKKTLNPYWNEMFDLRVNEESILAIQIFDQKKFKKKDQGFLGVINVRIGDVIDLEMGGDEMLTRDLKKSNDNLVVHGKLIINLSTNLSTPNTNQANGLHRSHIQPSTSSGLVPQVGASAAHPAASPAPIDPAASNPSLHPQRVPSTNRPPSTVAPGAAAGATPTNTQGSRTNLSSFEDSQGRLPAGWERREDNLGRTYYVDHNTRTTTWTRPSSNYNEQTQRTQREANMQLERRAHQSRMLPEDRTGANSPNLPETSQQAPTPPAGGSANAVSMMATGATTAGTGELPPGWEQRTTPEGRPYFVDHNTRTTTWVDPRRQQYIRMYGQNANGTNTTIQQQPVSQLGPLPSGWEMRLTNTARVYFVDHNTKTTTWDDPRLPSSLDQGVPQYKRDFRRKLIYFRSQPALRIMSGQCHVKVRRNNIFEDSYAEIMRQSASDLKKRLMIKFDGEDGLDYGGLSREFFFLLSHEMFNPFYCLFEYSAHDNYTLQINPHSGVNPEHLNYFKFIGRVVGLAIFHRRFLDSFFIGAFYKMMLRKKVSLQDMEGVDEDLHRNLTWTLDNDIEGVLELTFAVDDEKFGERRTIDLKPGGRDIPVTNENKGEYVELVTEWKIVKRVEEQFNAFMSGFNELIPADLVNVFDERELELLIGGIADIDVDDWKKHTDYRGYQESDDVIQNFWKVVRTWDAEQKSRLLQFTTGTSRIPVNGFKDLQGSDGPRRFTIEKSGDPVALPKSHTCFNRLDLPPYKTYETLEHKMSIAVEETLGFGQE | 2.3.2.26 | null | chromatin organization [GO:0006325]; mitochondria-associated ubiquitin-dependent protein catabolic process [GO:0072671]; mitochondrion organization [GO:0007005]; nonfunctional rRNA decay [GO:0070651]; poly(A)+ mRNA export from nucleus [GO:0016973]; positive regulation of fatty acid biosynthetic process [GO:0045723]; positive regulation of proteasomal ubiquitin-dependent protein catabolic process [GO:0032436]; positive regulation of receptor-mediated endocytosis [GO:0048260]; positive regulation of transcription by RNA polymerase II [GO:0045944]; protein K63-linked ubiquitination [GO:0070534]; protein transport to vacuole involved in ubiquitin-dependent protein catabolic process via the multivesicular body sorting pathway [GO:0043328]; protein ubiquitination [GO:0016567]; regulation of actin cytoskeleton organization [GO:0032956]; regulation of dolichol biosynthetic process [GO:0010794]; regulation of ergosterol biosynthetic process [GO:0032443]; regulation of mRNA export from nucleus [GO:0010793]; regulation of multivesicular body size [GO:0010796]; regulation of nitrogen utilization [GO:0006808]; regulation of phosphate metabolic process [GO:0019220]; regulation of protein localization [GO:0032880]; regulation of ribosomal large subunit export from nucleus [GO:2000203]; regulation of rRNA processing [GO:2000232]; regulation of tRNA export from nucleus [GO:2000238]; regulation of tRNA processing [GO:2000235]; regulation of ubiquinone biosynthetic process [GO:0010795]; ribophagy [GO:0034517]; ubiquitin-dependent endocytosis [GO:0070086] | cellular bud tip [GO:0005934]; cytosolic ribosome [GO:0022626]; endosome membrane [GO:0010008]; Golgi apparatus [GO:0005794]; nucleus [GO:0005634]; RSP5-BUL ubiquitin ligase complex [GO:1990306]; ubiquitin ligase complex [GO:0000151] | phosphatidylinositol binding [GO:0035091]; ubiquitin binding [GO:0043130]; ubiquitin protein ligase activity [GO:0061630]; ubiquitin-protein transferase activity [GO:0004842] | PF00168;PF00632;PF00397; | 2.20.70.10;2.60.40.150;3.30.2160.10;3.30.2410.10;3.90.1750.10; | RSP5/NEDD4 family | null | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:P39940}. | 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=2.3.2.26; | null | PATHWAY: Protein modification; protein ubiquitination. | null | null | FUNCTION: E3 ubiquitin-protein ligase which accepts ubiquitin from an E2 ubiquitin-conjugating enzyme in the form of a thioester and then directly transfers the ubiquitin to targeted substrates. Probably involved in the regulatory network controlling carbon source utilization. {ECO:0000250|UniProtKB:Q5BDP1}. | Aspergillus clavatus (strain ATCC 1007 / CBS 513.65 / DSM 816 / NCTC 3887 / NRRL 1 / QM 1276 / 107) |
A1CX69 | ATG1_NEOFI | MSIGRYTRLDEIGRGSFATVYQGVHTKTRTYVAIKSVNLSKLNKKLKDNLSSEIHILKGLYHPHIVALIDCHETTSHIHLVMEYCALGDLSLFIKRRDTLGDHRYTRDMIAKYPNPPGGALNEVVVRHFLKQLASALKFLRDRNLIHRDIKPQNLLLCPSPSSYRSGVTQVVPFKGSEDSFNPATGLESLPLLKIADFGFARSLPATSLAETLCGSPLYMAPEILRYEKYDAKADLWSVGTVLYEMVVGKPPFRATNHVELLRKIEKGEDRIKFPEENPASDEIKALIRALLKRNPVERLNFPDFFENGVITSPIPGLVADDQPSIPRDPPADPETAESTPRPDSRSGAIVPGGTEREREVSYLPKGDTGLTQRPPSQNQRFGTPPTTTHMRRIGSGDRPPSTPKELTPPMTYPQRPSAVSHATAPGRQELVDRNAAFTAMERQRGRNTFSEGSPQTDRQADKLREERERAAQDVAFERDYVVVEKRAVEVNAFADELAHSPRIQGGISRGAQTGALSRRSTVHGPTPLNPSPPQATVGKAMQVLSGRSRADSMHNRQSSYERRYGQSPTSATSAISKALNMASGRLFGMGFSPPLAITKGGRSPPLAYNPFPAYPAHGSLMIGDGAKNNVALDEDTKTVQILEECATRSDVVYGFAEVKYKQLVPLAPSVQTDPSSKGNLAGERENPDSADGGLTVDAIVTLSEEALVLYVKALSLLAKSMDIAGAWWARKNRGDGFGDSAMSRADGASTLAGTRINNVVQWVRNRFNEVLEKGEFVRLKLIEAQKRLPPDHPSHPDNHSVGSSLGSGASVDVVVSPGVSAEKLMYDRALEMSRTAAINELTGEDLSGCEIAYVTAIRMLEAVLENGEVPRFGQGKDDTSKDSDKIVLDAVQAEERQVVIKLVSSIRSRLAALRKKLAILAKRAPTPSANVPSKMAPLNPVSVGATPPK | 2.7.11.1 | null | autophagosome assembly [GO:0000045]; axon extension [GO:0048675]; negative regulation of collateral sprouting [GO:0048671]; phosphorylation [GO:0016310]; piecemeal microautophagy of the nucleus [GO:0034727]; positive regulation of autophagy [GO:0010508]; protein transport [GO:0015031]; response to starvation [GO:0042594]; reticulophagy [GO:0061709] | Atg1/ULK1 kinase complex [GO:1990316]; autophagosome membrane [GO:0000421]; cytosol [GO:0005829]; phagophore [GO:0061908]; phagophore assembly site membrane [GO:0034045]; vacuole-isolation membrane contact site [GO:0120095] | ATP binding [GO:0005524]; protein serine kinase activity [GO:0106310]; protein serine/threonine kinase activity [GO:0004674] | PF12063;PF21127;PF00069; | 1.10.510.10; | Protein kinase superfamily, Ser/Thr protein kinase family, APG1/unc-51/ULK1 subfamily | null | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:P53104}. Preautophagosomal structure membrane {ECO:0000250|UniProtKB:P53104}; Peripheral membrane protein {ECO:0000250|UniProtKB:P53104}. | 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:0000250|UniProtKB:P53104}; 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:0000250|UniProtKB:P53104}; | null | null | null | null | FUNCTION: Serine/threonine protein kinase involved in the cytoplasm to vacuole transport (Cvt) and found to be essential in autophagy, where it is required for the formation of autophagosomes. Involved in the clearance of protein aggregates which cannot be efficiently cleared by the proteasome. Required for selective autophagic degradation of the nucleus (nucleophagy) as well as for mitophagy which contributes to regulate mitochondrial quantity and quality by eliminating the mitochondria to a basal level to fulfill cellular energy requirements and preventing excess ROS production. Also involved in endoplasmic reticulum-specific autophagic process, in selective removal of ER-associated degradation (ERAD) substrates. Plays a key role in ATG9 and ATG23 cycling through the pre-autophagosomal structure and is necessary to promote ATG18 binding to ATG9 through phosphorylation of ATG9. Catalyzes phosphorylation of ATG4, decreasing the interaction between ATG4 and ATG8 and impairing deconjugation of PE-conjugated forms of ATG8. {ECO:0000250|UniProtKB:P53104}. | Neosartorya fischeri (strain ATCC 1020 / DSM 3700 / CBS 544.65 / FGSC A1164 / JCM 1740 / NRRL 181 / WB 181) (Aspergillus fischerianus) |
A1CZG3 | SKP1_NEOFI | MTTVTLTSSDGVDITVDRDVAERSILIKNMLEDLGESDEAIPIPNVNEVVLKKVIEWCTHHKNDPPSTGDDDDSRRKTTDIDEWDQKFMQVDQEMLFEIILAANYLDIKALLDVGCKTVANMIKGKSPEEIRKTFNIQNDFTPEEEDQIRRENEWAEE | null | null | exit from mitosis [GO:0010458]; G1/S transition of mitotic cell cycle [GO:0000082]; G2/M transition of mitotic cell cycle [GO:0000086]; kinetochore assembly [GO:0051382]; mitotic nuclear membrane biogenesis [GO:0101026]; negative regulation of cytoplasmic translation [GO:2000766]; negative regulation of mitotic metaphase/anaphase transition [GO:0045841]; positive regulation of glucose transmembrane transport [GO:0010828]; protein neddylation [GO:0045116]; protein ubiquitination [GO:0016567]; regulation of DNA recombination [GO:0000018]; regulation of exit from mitosis [GO:0007096]; regulation of protein-containing complex assembly [GO:0043254]; resolution of meiotic recombination intermediates [GO:0000712]; SCF-dependent proteasomal ubiquitin-dependent protein catabolic process [GO:0031146]; septin ring assembly [GO:0000921]; silent mating-type cassette heterochromatin formation [GO:0030466]; vacuolar acidification [GO:0007035]; vacuolar proton-transporting V-type ATPase complex assembly [GO:0070072] | CBF3 complex [GO:0031518]; kinetochore [GO:0000776]; nuclear SCF ubiquitin ligase complex [GO:0043224]; RAVE complex [GO:0043291]; single-stranded DNA-dependent ATP-dependent DNA helicase complex [GO:0017117] | cullin family protein binding [GO:0097602]; DNA replication origin binding [GO:0003688]; ubiquitin protein ligase activity [GO:0061630] | PF01466;PF03931; | null | SKP1 family | null | null | null | null | PATHWAY: Protein modification; protein ubiquitination. | null | null | FUNCTION: Essential component of the SCF (SKP1-CUL1-F-box protein) E3 ubiquitin ligase complexes, which mediate the ubiquitination and subsequent proteasomal degradation of target proteins. Controls sulfur metabolite repression, probably by mediating the inactivation or degradation of the metR transcription factor (By similarity). {ECO:0000250}. | Neosartorya fischeri (strain ATCC 1020 / DSM 3700 / CBS 544.65 / FGSC A1164 / JCM 1740 / NRRL 181 / WB 181) (Aspergillus fischerianus) |
A1D244 | ARO1_NEOFI | MTGPTKISILGQESIVADFGLWRNYVAKDLISGCPSTTYVLITDTNIGSIYTPGFQKSFEEAAASVSPSPRLLIYNAPPGEVSKSRQTKADIEDWMLSQSPPCGRDTVVIALGGGVIGDLTGFVAATYMRGVRFVQVPTTLLAMVDSSIGGKTAIDTPLGKNLIGAIWQPSRIYIDLEFLETLPVREFINGMAEVIKTAAISSEEEFTALEDNAETILSAVRREVKPGQRRFEGIEEILKARILASARHKAFVVSADEREGGLRNLLNWGHSIGHAIEAILTPQILHGECVAIGMVKEAELARHLGILKGVAVARIVKCIAAYGLPTSLKDSRIRKLTAGKHCSVDQILFNMALDKKNDGPKKKIVLLSAIGRTYEPRASVVPNEDIGVVLAPSIEVYPGVSPASEVVCAPPGSKSISNRALVLAALGSGTVRIKNLLHSDDTEVMLNALERLGAATFSWEEEGEVLVVNGKGGALQAHPSPLYLGNAGTASRFLTTVATLATASSVDSSVLTGNNRMKQRPIGDLVDALTANGAQIEYVENKGSLPLKIAASGGFTGGQINLAAKVSSQYVSSLLMCAPYAKEPVTLKLVGGKPISQPYIDMTTAMMRSFGIDVKKSTTEEHTYHIPQGRYINPAEYVVESDASSATYPLAIAAVTGTTCTIPNIGSKSLQGDARFAVDVLRPMGCTVEQTDTSTTVTGPADGVLRPLPNVDMEPMTDAFLGASVLAAIARGKDSNHTTRIYGIANQRVKECNRIKAMHDELAKFGVVCREHDDGLEIDGIDRSTLRQPAGGVFCYDDHRVAFSFSVLSLVAPKPTLILEKECVGKTWPGWWDTLRQKFAVKLEGKELKEAESPVLTRAEKASASVFIIGMRGAGKTTSGNWVASTLKRPFIDLDDELERIEGMTIPDIIKQRGWQGFRDAELSLLQRTMKERPTGHVFACGGGVVEIPEARKLLIDWHKTKGNVLLIMRDIKQVMAFLNIDKTRPAYVEDMLGVWLRRKPWFQECSNIQYYSQHASAGLPRASEDFARFIKFVTGLEDSLSTIKKKQHSFFVSLTLPDVRGADQILEQACVGSDAVELRVDLLEDPDSANGIPTVDFVADQISYLRSRITLPVIFTIRTKGQGGRFPDDAHAEAMQLYRLAVRSGCEFVDLEIAFPDEMLRAVTEMKGYSKIITSHHDPKGELSWANMSWMKYYNRALEYGDVIKLVGVARNLDDNTALRKFKNWAEEAHDVPLIAINMGGNGQLSRILNGFMTPVSHPALPFRAAPGQLSATDIRKGLSLMGEIKKKRFALFGSPISESRSPALHNTLFAEMGLPHEYTRLETANVEDVKDFIRAPDFGGASVTIPLKLDIMPLLDEITAEAEIIGAVNTVVPVSDGEGKPQRLVGHNTDWQGMVQCLRNAGAYGADGNASGLVVGGGGTSRAAIYALHHMGFSPIYIVGRNPAKLESMVATFPTGYNIRIVEGNEKLEHVPHVAIGTIPADRPIDPGMREILCHMFERAQEADADAARTIEGSPRVLLEMAYKPRVTALMQLAVDAGWTTVPGLEALIGQGVHQFQHWTGIRPLYERARAIVLG | 1.1.1.25; 2.5.1.19; 2.7.1.71; 4.2.1.10; 4.2.3.4 | COFACTOR: Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Note=Binds 2 Zn(2+) ions per subunit.; | amino acid biosynthetic process [GO:0008652]; aromatic amino acid family biosynthetic process [GO:0009073]; chorismate biosynthetic process [GO:0009423]; phosphorylation [GO:0016310] | cytoplasm [GO:0005737] | 3-dehydroquinate dehydratase activity [GO:0003855]; 3-dehydroquinate synthase activity [GO:0003856]; 3-phosphoshikimate 1-carboxyvinyltransferase activity [GO:0003866]; ATP binding [GO:0005524]; metal ion binding [GO:0046872]; shikimate 3-dehydrogenase (NADP+) activity [GO:0004764]; shikimate kinase activity [GO:0004765] | PF01761;PF01487;PF00275;PF18317;PF08501;PF01202; | 3.40.50.1970;3.20.20.70;1.20.1090.10;3.65.10.10;3.40.50.10860;3.40.50.720;3.40.50.300; | Sugar phosphate cyclases superfamily, Dehydroquinate synthase family; EPSP synthase family; Shikimate kinase family; Type-I 3-dehydroquinase family; Shikimate dehydrogenase family | null | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_03143}. | CATALYTIC ACTIVITY: Reaction=7-phospho-2-dehydro-3-deoxy-D-arabino-heptonate = 3-dehydroquinate + phosphate; Xref=Rhea:RHEA:21968, ChEBI:CHEBI:32364, ChEBI:CHEBI:43474, ChEBI:CHEBI:58394; EC=4.2.3.4; Evidence={ECO:0000255|HAMAP-Rule:MF_03143}; CATALYTIC ACTIVITY: Reaction=3-dehydroquinate = 3-dehydroshikimate + H2O; Xref=Rhea:RHEA:21096, ChEBI:CHEBI:15377, ChEBI:CHEBI:16630, ChEBI:CHEBI:32364; EC=4.2.1.10; Evidence={ECO:0000255|HAMAP-Rule:MF_03143}; CATALYTIC ACTIVITY: Reaction=NADP(+) + shikimate = 3-dehydroshikimate + H(+) + NADPH; Xref=Rhea:RHEA:17737, ChEBI:CHEBI:15378, ChEBI:CHEBI:16630, ChEBI:CHEBI:36208, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349; EC=1.1.1.25; Evidence={ECO:0000255|HAMAP-Rule:MF_03143}; CATALYTIC ACTIVITY: Reaction=ATP + shikimate = 3-phosphoshikimate + ADP + H(+); Xref=Rhea:RHEA:13121, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:36208, ChEBI:CHEBI:145989, ChEBI:CHEBI:456216; EC=2.7.1.71; Evidence={ECO:0000255|HAMAP-Rule:MF_03143}; CATALYTIC ACTIVITY: Reaction=3-phosphoshikimate + phosphoenolpyruvate = 5-O-(1-carboxyvinyl)-3-phosphoshikimate + phosphate; Xref=Rhea:RHEA:21256, ChEBI:CHEBI:43474, ChEBI:CHEBI:57701, ChEBI:CHEBI:58702, ChEBI:CHEBI:145989; EC=2.5.1.19; Evidence={ECO:0000255|HAMAP-Rule:MF_03143}; | null | PATHWAY: Metabolic intermediate biosynthesis; chorismate biosynthesis; chorismate from D-erythrose 4-phosphate and phosphoenolpyruvate: step 2/7. {ECO:0000255|HAMAP-Rule:MF_03143}.; PATHWAY: Metabolic intermediate biosynthesis; chorismate biosynthesis; chorismate from D-erythrose 4-phosphate and phosphoenolpyruvate: step 3/7. {ECO:0000255|HAMAP-Rule:MF_03143}.; PATHWAY: Metabolic intermediate biosynthesis; chorismate biosynthesis; chorismate from D-erythrose 4-phosphate and phosphoenolpyruvate: step 4/7. {ECO:0000255|HAMAP-Rule:MF_03143}.; PATHWAY: Metabolic intermediate biosynthesis; chorismate biosynthesis; chorismate from D-erythrose 4-phosphate and phosphoenolpyruvate: step 5/7. {ECO:0000255|HAMAP-Rule:MF_03143}.; PATHWAY: Metabolic intermediate biosynthesis; chorismate biosynthesis; chorismate from D-erythrose 4-phosphate and phosphoenolpyruvate: step 6/7. {ECO:0000255|HAMAP-Rule:MF_03143}. | null | null | FUNCTION: The AROM polypeptide catalyzes 5 consecutive enzymatic reactions in prechorismate polyaromatic amino acid biosynthesis. {ECO:0000255|HAMAP-Rule:MF_03143}. | Neosartorya fischeri (strain ATCC 1020 / DSM 3700 / CBS 544.65 / FGSC A1164 / JCM 1740 / NRRL 181 / WB 181) (Aspergillus fischerianus) |
A1D3C5 | RSP5_NEOFI | MGSNLPAQPNLRLTIIAADGLYKRDVFRFPDPFAVATVGGEQTHTTSVIKKTLNPYWNEMFDLRVNEDSILAIQIFDQKKFKKKDQGFLGVINVRIGDVIDLQMGGDEMLTRDLKKSNDNLVVHGKLIINLSTNLSTPNTNQANGLHRSHVQSSTSSGLVPQVAPSSSHPAASGAAPVDPSASNPSLNPQRVPSTTRPSSTAAPASAAGAAASNTHGSRTNLSSFEDSQGRLPAGWERREDNLGRTYYVDHNTRTTTWTRPSSNYNEHAQRSQREANMQLERRAHQSRMLPEDRTGANSPNLPESSQQAHTPPAGGSANAVSMMATGATTAGTGELPPGWEQRTTPEGRPYFVDHNTRTTTWVDPRRQQYIRMYGQNANGTNTTIQQQPVSQLGPLPSGWEMRLTNTARVYFVDHNTKTTTWDDPRLPSSLDQGVPQYKRDFRRKLIYFRSQPALRIMSGQCHVKVRRNNIFEDSYAEIMRQSASDLKKRLMIKFDGEDGLDYGGLSREFFFLLSHEMFNPFYCLFEYSAHDNYTLQINPHSGVNPEHLNYFKFIGRVVGLAIFHRRFLDSFFIGAFYKMMLRKKVSLQDMEGVDEDLHRNLTWTLDNDIEGVLELTFSVDDEKFGERRTIDLKPGGRDIPVTNENKAEYVELVTEWKIVKRVEEQFNAFMSGFNELIPADLVNVFDERELELLIGGIADIDVDDWKKHTDYRGYQESDEVIQNFWKVVRSWDAEQKSRLLQFTTGTSRIPVNGFKDLQGSDGPRRFTIEKSGDPAALPKSHTCFNRLDLPPYKSYETLEHKMSIAVEETLGFGQE | 2.3.2.26 | null | chromatin organization [GO:0006325]; mitochondria-associated ubiquitin-dependent protein catabolic process [GO:0072671]; mitochondrion organization [GO:0007005]; nonfunctional rRNA decay [GO:0070651]; poly(A)+ mRNA export from nucleus [GO:0016973]; positive regulation of fatty acid biosynthetic process [GO:0045723]; positive regulation of proteasomal ubiquitin-dependent protein catabolic process [GO:0032436]; positive regulation of receptor-mediated endocytosis [GO:0048260]; positive regulation of transcription by RNA polymerase II [GO:0045944]; protein K63-linked ubiquitination [GO:0070534]; protein transport to vacuole involved in ubiquitin-dependent protein catabolic process via the multivesicular body sorting pathway [GO:0043328]; protein ubiquitination [GO:0016567]; regulation of actin cytoskeleton organization [GO:0032956]; regulation of dolichol biosynthetic process [GO:0010794]; regulation of ergosterol biosynthetic process [GO:0032443]; regulation of mRNA export from nucleus [GO:0010793]; regulation of multivesicular body size [GO:0010796]; regulation of nitrogen utilization [GO:0006808]; regulation of phosphate metabolic process [GO:0019220]; regulation of protein localization [GO:0032880]; regulation of ribosomal large subunit export from nucleus [GO:2000203]; regulation of rRNA processing [GO:2000232]; regulation of tRNA export from nucleus [GO:2000238]; regulation of tRNA processing [GO:2000235]; regulation of ubiquinone biosynthetic process [GO:0010795]; ribophagy [GO:0034517]; ubiquitin-dependent endocytosis [GO:0070086] | cellular bud tip [GO:0005934]; cytosolic ribosome [GO:0022626]; endosome membrane [GO:0010008]; Golgi apparatus [GO:0005794]; nucleus [GO:0005634]; RSP5-BUL ubiquitin ligase complex [GO:1990306]; ubiquitin ligase complex [GO:0000151] | phosphatidylinositol binding [GO:0035091]; ubiquitin binding [GO:0043130]; ubiquitin protein ligase activity [GO:0061630]; ubiquitin-protein transferase activity [GO:0004842] | PF00168;PF00632;PF00397; | 2.20.70.10;2.60.40.150;3.30.2160.10;3.30.2410.10;3.90.1750.10; | RSP5/NEDD4 family | null | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:P39940}. | 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=2.3.2.26; | null | PATHWAY: Protein modification; protein ubiquitination. | null | null | FUNCTION: E3 ubiquitin-protein ligase which accepts ubiquitin from an E2 ubiquitin-conjugating enzyme in the form of a thioester and then directly transfers the ubiquitin to targeted substrates. Probably involved in the regulatory network controlling carbon source utilization. {ECO:0000250|UniProtKB:Q5BDP1}. | Neosartorya fischeri (strain ATCC 1020 / DSM 3700 / CBS 544.65 / FGSC A1164 / JCM 1740 / NRRL 181 / WB 181) (Aspergillus fischerianus) |
A1DED8 | UBA4_NEOFI | MENLEQTCASLRAQIAATEAQLAGLKRELEIAEQAAADVKAQDTTITITADEGRINGTRTWPLLSEEYKRYGRQMIVPQVGLQGQLKLRSARVLIVGAGGLGCPAALYLAGAGVGTLGLVDGDTVENSNLHRQVLHRSKNVGKFKVDSAIEYLREAHLTPQEAPSIFKDYDIILDCTDNPATRYLISDTAVLLGKPLVSASALRTEGQLMVLNYPPRPVGDKSGGPCYRCVFPKPPPANSVVSCADGGILGPVVGTMGVLQALEAIKVITSPAVNPSASPPSLLIFSAYSTPPFRTIRLRARRANCAVCSADASVTLETLKIGSTDYVFFCGVAGLEATLSPEERISPLELRKRHPKEVPQDGGSISKEPTIIDVREKVQFDICNLEHSVNIPISTILSSASNAANADANAQPSLPSWLPRELASADSTNPIYVVCRHGNDSQIAVRRLKELGLDRGGQRYVGDIQGGLRAWREQIDPDWPEY | 2.7.7.80; 2.8.1.11 | COFACTOR: Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000255|HAMAP-Rule:MF_03049}; Note=Binds 1 zinc ion per subunit. {ECO:0000255|HAMAP-Rule:MF_03049}; | cell budding [GO:0007114]; cellular response to oxidative stress [GO:0034599]; invasive growth in response to glucose limitation [GO:0001403]; Mo-molybdopterin cofactor biosynthetic process [GO:0006777]; protein urmylation [GO:0032447]; regulation of pseudohyphal growth [GO:2000220]; tRNA wobble position uridine thiolation [GO:0002143] | cytosol [GO:0005829] | AMPylase activity [GO:0070733]; ATP binding [GO:0005524]; identical protein binding [GO:0042802]; metal ion binding [GO:0046872]; molybdopterin-synthase adenylyltransferase activity [GO:0061605]; molybdopterin-synthase sulfurtransferase activity [GO:0061604]; sulfotransferase activity [GO:0008146]; thiosulfate sulfurtransferase activity [GO:0004792]; URM1 activating enzyme activity [GO:0042292] | PF00581;PF00899; | 3.40.50.720;3.40.250.10; | HesA/MoeB/ThiF family, UBA4 subfamily | null | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_03049}. | CATALYTIC ACTIVITY: Reaction=[molybdopterin-synthase sulfur-carrier protein]-C-terminal Gly-Gly + ATP + H(+) = [molybdopterin-synthase sulfur-carrier protein]-C-terminal Gly-Gly-AMP + diphosphate; Xref=Rhea:RHEA:43616, Rhea:RHEA-COMP:12159, Rhea:RHEA-COMP:12202, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:33019, ChEBI:CHEBI:90618, ChEBI:CHEBI:90778; EC=2.7.7.80; Evidence={ECO:0000255|HAMAP-Rule:MF_03049}; CATALYTIC ACTIVITY: Reaction=[molybdopterin-synthase sulfur-carrier protein]-C-terminal Gly-Gly-AMP + AH2 + S-sulfanyl-L-cysteinyl-[cysteine desulfurase] = [molybdopterin-synthase sulfur-carrier protein]-C-terminal Gly-NH-CH2-C(O)SH + A + AMP + H(+) + L-cysteinyl-[cysteine desulfurase]; Xref=Rhea:RHEA:48612, Rhea:RHEA-COMP:12157, Rhea:RHEA-COMP:12158, Rhea:RHEA-COMP:12159, Rhea:RHEA-COMP:12160, ChEBI:CHEBI:13193, ChEBI:CHEBI:15378, ChEBI:CHEBI:17499, ChEBI:CHEBI:29950, ChEBI:CHEBI:61963, ChEBI:CHEBI:90618, ChEBI:CHEBI:90619, ChEBI:CHEBI:456215; EC=2.8.1.11; Evidence={ECO:0000255|HAMAP-Rule:MF_03049}; | null | PATHWAY: tRNA modification; 5-methoxycarbonylmethyl-2-thiouridine-tRNA biosynthesis. {ECO:0000255|HAMAP-Rule:MF_03049}. | null | null | FUNCTION: Plays a central role in 2-thiolation of mcm(5)S(2)U at tRNA wobble positions of cytosolic tRNA(Lys), tRNA(Glu) and tRNA(Gln). Also essential during biosynthesis of the molybdenum cofactor. Acts by mediating the C-terminal thiocarboxylation of sulfur carriers urm1 and mocs2a. Its N-terminus first activates urm1 and mocs2a as acyl-adenylates (-COAMP), then the persulfide sulfur on the catalytic cysteine is transferred to urm1 and mocs2a to form thiocarboxylation (-COSH) of their C-terminus. The reaction probably involves hydrogen sulfide that is generated from the persulfide intermediate and that acts as a nucleophile towards urm1 and mocs2a. Subsequently, a transient disulfide bond is formed. Does not use thiosulfate as sulfur donor; nfs1 probably acting as a sulfur donor for thiocarboxylation reactions (By similarity). {ECO:0000250}. | Neosartorya fischeri (strain ATCC 1020 / DSM 3700 / CBS 544.65 / FGSC A1164 / JCM 1740 / NRRL 181 / WB 181) (Aspergillus fischerianus) |
A1E280 | TRP6H_STRAO | MDNRIKTVVILGGGTAGWMTAAYLGKALQNTVKIVVLEAPTIPRIGVGEATVPNLQRAFFDYLGIPEEEWMRECNASYKMAVKFINWRTPGEGSPDPRTLDDGHTDTFHHPFGLLPSADQIPLSHYWAAKRLQGETDENFDEACFADTAIMNAKKAPRFLDMRRATNYAWHFDASKVAAFLRNFAVTKQAVEHVEDEMTEVLTDERGFITALRTKSGRILQGDLFVDCSGFRGLLINKAMEEPFIDMSDHLLCNSAVATAVPHDDEKNGVEPYTSSIAMEAGWTWKIPMLGRFGSGHVYSDHFATQDEATLAFSKLWGLDPDNTEFNHVRFRVGRNRRAWVRNCVSVGLASCFVEPLESSGIYFIYAAIHMLAKHFPDKTFDKVLVDRFNREIEEMFDDTRDFLQAHYYFSPRVDTPFWRANKELKLADSIKDKVETYRAGLPVNLPVTDEGTYYGNFEAEFRNFWTNGSYYCIFAGLGLMPRNPLPALAYKPQSIAEAELLFADVKRKGDTLVESLPSTYDLLRQLHGAS | 1.14.19.59 | null | null | null | monooxygenase activity [GO:0004497]; nucleotide binding [GO:0000166] | PF04820; | 3.50.50.60; | Flavin-dependent halogenase family, Bacterial tryptophan halogenase subfamily | null | null | CATALYTIC ACTIVITY: Reaction=chloride + FADH2 + L-tryptophan + O2 = 6-chloro-L-tryptophan + FAD + 2 H2O; Xref=Rhea:RHEA:55900, ChEBI:CHEBI:15377, ChEBI:CHEBI:15379, ChEBI:CHEBI:17996, ChEBI:CHEBI:57692, ChEBI:CHEBI:57912, ChEBI:CHEBI:58307, ChEBI:CHEBI:139335; EC=1.14.19.59; Evidence={ECO:0000269|PubMed:33465708, ECO:0000305|PubMed:24692213}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:55901; Evidence={ECO:0000305|PubMed:24692213}; CATALYTIC ACTIVITY: Reaction=chloride + D-tryptophan + FADH2 + O2 = 6-chloro-D-tryptophan + FAD + 2 H2O; Xref=Rhea:RHEA:56528, ChEBI:CHEBI:15377, ChEBI:CHEBI:15379, ChEBI:CHEBI:17996, ChEBI:CHEBI:57692, ChEBI:CHEBI:57719, ChEBI:CHEBI:58307, ChEBI:CHEBI:140509; EC=1.14.19.59; Evidence={ECO:0000269|PubMed:33465708}; | null | null | null | null | FUNCTION: Involved in the biosynthesis of thienodolin, a plant growth-regulating compound (PubMed:24692213). Catalyzes the chlorination of tryptophan (Trp) at C6 position to yield 6-chloro-tryptophan (PubMed:24692213, PubMed:33465708). It is also able to use bromide ions to generate monobrominated Trp (PubMed:33465708, PubMed:36259362). In vitro, accepts a wide range of amides and peptides carrying either L- or D-Trp at the N-terminus (PubMed:36259362). {ECO:0000269|PubMed:24692213, ECO:0000269|PubMed:33465708, ECO:0000269|PubMed:36259362}. | Streptomyces albogriseolus |
A1E959 | ODAM_HUMAN | MKIIILLGFLGATLSAPLIPQRLMSASNSNELLLNLNNGQLLPLQLQGPLNSWIPPFSGILQQQQQAQIPGLSQFSLSALDQFAGLLPNQIPLTGEASFAQGAQAGQVDPLQLQTPPQTQPGPSHVMPYVFSFKMPQEQGQMFQYYPVYMVLPWEQPQQTVPRSPQQTRQQQYEEQIPFYAQFGYIPQLAEPAISGGQQQLAFDPQLGTAPEIAVMSTGEEIPYLQKEAINFRHDSAGVFMPSTSPKPSTTNVFTSAVDQTITPELPEEKDKTDSLREP | null | null | biomineral tissue development [GO:0031214]; inflammatory response [GO:0006954]; odontogenesis of dentin-containing tooth [GO:0042475]; positive regulation of epithelial cell proliferation involved in wound healing [GO:0060054]; positive regulation of gene expression [GO:0010628]; positive regulation of GTPase activity [GO:0043547]; positive regulation of protein phosphorylation [GO:0001934]; regulation of actin cytoskeleton organization [GO:0032956] | cell periphery [GO:0071944]; cytoplasm [GO:0005737]; cytosol [GO:0005829]; extracellular region [GO:0005576]; extracellular space [GO:0005615]; mitotic spindle [GO:0072686]; nucleoplasm [GO:0005654]; nucleus [GO:0005634]; supramolecular fiber [GO:0099512] | null | PF15424; | null | ODAM family | PTM: O-glycosylated. {ECO:0000250}. | SUBCELLULAR LOCATION: Secreted {ECO:0000250|UniProtKB:Q3HS83}. Cytoplasm {ECO:0000269|PubMed:25911094}. Nucleus {ECO:0000269|PubMed:25911094}. | null | null | null | null | null | FUNCTION: Tooth-associated epithelia protein that probably plays a role in odontogenesis, the complex process that results in the initiation and generation of the tooth. May be incorporated in the enamel matrix at the end of mineralization process. Involved in the induction of RHOA activity via interaction with ARHGEF and expression of downstream factors such as ROCK. Plays a role in attachment of the junctional epithelium to the tooth surface. {ECO:0000269|PubMed:25911094}. | Homo sapiens (Human) |
A1E960 | ODAM_MOUSE | MKIIILLGLIGASSSAPLISQRLLSASNSHELLLNLNNGQLLPLQFQGAFNSWIPPFPGFLQQQQAQVSGRPQFTLSTLESFAGLFPNQIPLSRQVGLAQGGQAGQPDLSQQQTPPQTQQSASPMSYVVPVKVPQDQTQMFQYYPVYMLLPWEQPQTVTSSPQHTGQQLFEEQIPFYNQFGFAPPQAEPGVPGGQQHLAFDSFVGTAPETPGMPVEGSLLYPQKEPISFKHDNAGVFMPTTSPKPSTDNFFTSGIDPTIAPEQKVKTDSLREP | null | null | biomineral tissue development [GO:0031214]; inflammatory response [GO:0006954]; odontogenesis of dentin-containing tooth [GO:0042475]; positive regulation of epithelial cell proliferation involved in wound healing [GO:0060054]; positive regulation of gene expression [GO:0010628]; positive regulation of protein phosphorylation [GO:0001934]; regulation of actin cytoskeleton organization [GO:0032956]; response to wounding [GO:0009611] | cell periphery [GO:0071944]; cytoplasm [GO:0005737]; cytosol [GO:0005829]; extracellular region [GO:0005576]; extracellular space [GO:0005615]; mitotic spindle [GO:0072686]; nucleoplasm [GO:0005654]; nucleus [GO:0005634]; supramolecular fiber [GO:0099512] | null | PF15424; | null | ODAM family | PTM: O-glycosylated. {ECO:0000250}. | SUBCELLULAR LOCATION: Secreted {ECO:0000250|UniProtKB:Q3HS83}. Cytoplasm {ECO:0000250|UniProtKB:A1E959}. Nucleus {ECO:0000250|UniProtKB:A1E959}. | null | null | null | null | null | FUNCTION: Tooth-associated epithelia protein that probably plays a role in odontogenesis, the complex process that results in the initiation and generation of the tooth. May be incorporated in the enamel matrix at the end of mineralization process. Involved in the induction of RHOA activity via interaction with ARHGEF and expression of downstream factors such as ROCK. Plays a role in attachment of the junctional epithelium to the tooth surface. {ECO:0000250|UniProtKB:A1E959}. | Mus musculus (Mouse) |
A1EC31 | TDIF_ZINEL | MDIDLLWSFGGWFFILFPETINYCMAKLRSTSQISHFTNPRSCSSLFFVALLIITILITMLQSSTSMEVTSLPTHQPTSSNSHDESSTSSTATTTTDLHPKRTHHQSHPKPTRSFEAGAHEVPSGPNPISNR | null | null | cell-cell signaling involved in cell fate commitment [GO:0045168]; phloem or xylem histogenesis [GO:0010087]; procambium histogenesis [GO:0010067]; xylem development [GO:0010089] | apoplast [GO:0048046]; plasma membrane [GO:0005886] | receptor serine/threonine kinase binding [GO:0033612] | null | null | CLV3/ESR signal peptide family | PTM: [TDIFp]: The TDIFp peptide contains two hydroxprolines, but hydroxylation had no direct effect on TDIFp activity. {ECO:0000269|PubMed:16902140}.; PTM: [TDIFp]: The O-glycosylation (arabinosylation) of the hydroxyproline Pro-126 enhances binding affinity of the TDIFp peptide for its receptor. {ECO:0000250|UniProtKB:O49519}. | SUBCELLULAR LOCATION: [TDIFp]: Secreted, extracellular space {ECO:0000269|PubMed:16902140}.; SUBCELLULAR LOCATION: [CLAVATA3/ESR (CLE)-related protein TDIF]: Cell membrane {ECO:0000305}; Single-pass membrane protein {ECO:0000305}. | null | null | null | null | null | FUNCTION: [TDIFp]: Extracellular signal peptide that regulates cell fate. Represses tracheary element differentiation but promotes the formation of procambial cells adjacent to phloem cells in the veins. {ECO:0000269|PubMed:16902140, ECO:0000269|PubMed:18812507}. | Zinnia elegans (Garden zinnia) (Zinnia violacea) |
A1IHE6 | ACMA_GORST | MSTTTLDAAVIGTGVAGLYELHMLREQGLEVRAYDKASGVGGTWYWNRYPGARFDSEAYIYQYLFDEDLYKGWSWSQRFPGQEEIERWLNYVADSLDLRRDISLETEITSAVFDEDRNRWTLTTADGDTIDAQFLITCCGMLSAPMKDLFPGQSDFGGQLVHTARWPKEGIDFAGKRVGVIGNGATGIQVIQSIAADVDELKVFIRTPQYALPMKNPSYGPDEVAWYKSRFGELKDTLPHTFTGFEYDFTDAWEDLTPEQRRARLEDDYENGSLKLWLASFAEIFSDEQVSEEVSEFVREKMRARLVDPELCDLLIPSDYGFGTHRVPLETNYLEVYHRDNVTAVLVRDNPITRIRENGIELADGTVHELDVIIMATGFDAGTGALTRIDIRGRDGRTLADDWSRDIRTTMGLMVHGYPNMLTTAVPLAPSAALCNMTTCLQQQTEWISEAIRHLRATGKTVIEPTAEGEEAWVAHHDELADANLISKTNSWYVGSNVPGKPRRVLSYVGGVGAYRDATLEAAAAGYKGFALS | 1.14.13.226 | COFACTOR: Name=FAD; Xref=ChEBI:CHEBI:57692; Evidence={ECO:0000269|PubMed:30392152, ECO:0000305|PubMed:17071761}; Note=Binds 1 FAD per subunit. {ECO:0000250|UniProtKB:H3JQW0}; | null | null | flavin adenine dinucleotide binding [GO:0050660]; N,N-dimethylaniline monooxygenase activity [GO:0004499]; NADP binding [GO:0050661] | PF00743; | 3.50.50.60; | FAD-binding monooxygenase family | null | null | CATALYTIC ACTIVITY: Reaction=acetone + H(+) + NADPH + O2 = H2O + methyl acetate + NADP(+); Xref=Rhea:RHEA:49988, ChEBI:CHEBI:15347, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349, ChEBI:CHEBI:77700; EC=1.14.13.226; Evidence={ECO:0000269|PubMed:17071761, ECO:0000269|PubMed:30392152}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:49989; Evidence={ECO:0000269|PubMed:17071761}; | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=6.7 uM for NADPH {ECO:0000269|PubMed:30392152}; KM=170 uM for acetone {ECO:0000269|PubMed:30392152}; KM=0.34 uM for butanone {ECO:0000269|PubMed:30392152}; KM=0.37 uM for 2-pentanone {ECO:0000269|PubMed:30392152}; KM=1.5 uM for 2-heptanone {ECO:0000269|PubMed:30392152}; KM=4.4 uM for 3-methylbutanone {ECO:0000269|PubMed:30392152}; KM=1500 uM for 2,4-dimethyl-3-pentanone {ECO:0000269|PubMed:30392152}; KM=1.5 uM for cyclobutanone {ECO:0000269|PubMed:30392152}; KM=120 uM for cyclopentanone {ECO:0000269|PubMed:30392152}; KM=2400 uM for cyclohexanone {ECO:0000269|PubMed:30392152}; KM=6.7 uM for bicyclo[3.2.0]hept-2-en-6-one {ECO:0000269|PubMed:30392152}; KM=8.9 uM for phenylacetone {ECO:0000269|PubMed:30392152}; Note=kcat is 2.0 sec(-1) with NADPH as substrate. kcat is 1.4 sec(-1) with acetone as substrate. kcat is 2.1 sec(-1) with butanone as substrate. kcat is 1.9 sec(-1) with 2-pentanone as substrate. kcat is 3.9 sec(-1) with 2-heptanone as substrate. kcat is 2.2 sec(-1) with 3-methylbutanone as substrate. kcat is 1.5 sec(-1) with 2,4-dimethyl-3-pentanone as substrate. kcat is 2.0 sec(-1) with cyclobutanone as substrate. kcat is 4.3 sec(-1) with cyclopentanone as substrate. kcat is 3.6 sec(-1) with cyclohexanone as substrate. kcat is 1.5 sec(-1) with bicyclo[3.2.0]hept-2-en-6-one as substrate. kcat is 1.0 sec(-1) with phenylacetone as substrate. {ECO:0000269|PubMed:30392152}; | null | BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 8.0-8.5 (PubMed:17071761). Optimum pH is 7.0-8.0 (PubMed:30392152). {ECO:0000269|PubMed:17071761, ECO:0000269|PubMed:30392152}; | BIOPHYSICOCHEMICAL PROPERTIES: Temperature dependence: Optimum temperature is 35 degrees Celsius. {ECO:0000269|PubMed:17071761}; | FUNCTION: Plays an important role in the metabolism of acetone derived from propane oxidation (PubMed:17071761). Catalyzes the oxidation of acetone to methyl acetate (PubMed:17071761, PubMed:30392152). Exhibits high catalytic efficiency towards various linear and cyclic ketones, such as butanone, 2-pentanone, 2-heptanone, 2-octanone, 2-nonanone, 2-decanone, cyclobutanone, cyclopentanone and cyclohexanone (PubMed:17071761, PubMed:30392152). Elicits the highest catalytic efficiency towards butanone and cyclobutanone (PubMed:30392152). Is highly specific for NADPH and cannot use NADH (PubMed:17071761, PubMed:30392152). {ECO:0000269|PubMed:17071761, ECO:0000269|PubMed:30392152}. | Gordonia sp. (strain TY-5) |
A1IVT7 | HOG1_BOTFB | MAEFVRAQIFGTTFEITSRYSDLQPVGMGAFGLVCSAKDNLTGSNVAVKKIMKPFSTPVLSKRTYRELKLLKHLKHENVISLSDIFISPLEDIYFVTELLGTDLHRLLTSRPLEKQFIQYFLYQILRGLKYVHSAGVVHRDLKPSNILVNENCDLKICDFGLARIQDPQMTGYVSTRYYRAPEIMLTWQKYDVEVDVWSAGCIFAEMLEGKPLFPGKDHVNQFSIITELLGTPPDDVIHTIASENTLRFVQSLPKRERQPLASKFTQADPLAIDLLEKMLVFDPRARIKAAEGLAHEYLSPYHDPTDEPAAEERFDWSFNDADLPVDTWKIMMYSEILDYHNVINDAQNLTESQ | 2.7.11.24 | COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250}; | cellular response to oxidative stress [GO:0034599]; osmosensory signaling pathway [GO:0007231]; phosphorylation [GO:0016310]; stress-activated MAPK cascade [GO:0051403] | 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. HOG1 sub-subfamily | PTM: Dually phosphorylated on Thr-171 and Tyr-173, which activates the enzyme (By similarity). Phosphorylated under osmotic stress, specific fungicides, and oxidative stress mediated by H(2)O(2) and menadione. {ECO:0000250, ECO:0000269|PubMed:17189492}. | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Nucleus {ECO:0000250}. | 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; 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; | null | null | null | null | FUNCTION: Mitogen-activated protein kinase involved in a signal transduction pathway that is activated by changes in the osmolarity of the extracellular environment. Controls osmotic regulation of transcription of target genes (By similarity). Involved in vegetative and pathogenic development like conidia formation, sclerotial development, and in penetration into unwounded plant tissue. {ECO:0000250, ECO:0000269|PubMed:17189492}. | Botryotinia fuckeliana (strain B05.10) (Noble rot fungus) (Botrytis cinerea) |
A1JIG4 | FADB_YERE8 | MLYQSETLQLHWLENGIAELVFDAPGSVNKLDTQTVANLGEALVVLEKQSELKGLLLRSAKAAFIVGADITEFLSLFNEPPEKLHQWLVFANDIFNRLEDLPVPTIAAINGYALGGGCECILATDFRVASPEARIGLPETKLGIMPGFGGSVRLPRLLGADSALEIIAAGKDIIAKDALKVGLVDAVVAPEKLVDAALSILNQAIDGKLDWQAARRPKLEPLKLNPTEAAMCFTIAKGMVMQVAGKHYPAPLTAVKTIEAAAKFGRAEALILETNSFVPLAGSNEARALVGIFLNDQYVKGQAKKLSKGVSAPKQAAVLGAGIMGGGIAYQSALKGVPVIMKDINDKSLTLGMNEAAKLLNKQLERGKIDGLKMANILATIQPTLDYAGIERAQVIVEAVVENPKVKAAVLAEVETLIGEETVLASNTSTIPIDQLAKSLKRPENFCGMHFFNPVHRMPLVEIIRGTKTSDKTIAAVVAYATQMGKTPIVVNDCPGFFVNRVLFPYLAGFGMLVRDGADFRQIDKVMEKQFGWPMGPAYLLDVVGIDTAHHAQAVMAVGFPERMNKDYRDAVDVMFDNQRFGQKNGQGFYRYTQDTKGKPRKENDEQVDALLAQVSQPLQKFSDDDIIARTMIPMINEVVRCLEEGIIASPAEGDMALVYGLGFPPFHGGVFRYLDTIGSANYVEMAQRYTHLGALYQVPPGLRAKAEHNESYYPVAAALLDVSISQPA | 1.1.1.35; 4.2.1.17; 5.1.2.3; 5.3.3.8 | null | fatty acid beta-oxidation [GO:0006635] | fatty acid beta-oxidation multienzyme complex [GO:0036125] | 3-hydroxyacyl-CoA dehydrogenase activity [GO:0003857]; 3-hydroxybutyryl-CoA epimerase activity [GO:0008692]; delta(3)-delta(2)-enoyl-CoA isomerase activity [GO:0004165]; enoyl-CoA hydratase activity [GO:0004300]; NAD+ binding [GO:0070403] | PF00725;PF02737;PF00378; | 1.10.1040.50;3.40.50.720; | Enoyl-CoA hydratase/isomerase family; 3-hydroxyacyl-CoA dehydrogenase family | null | null | CATALYTIC ACTIVITY: Reaction=a (3S)-3-hydroxyacyl-CoA + NAD(+) = a 3-oxoacyl-CoA + H(+) + NADH; Xref=Rhea:RHEA:22432, ChEBI:CHEBI:15378, ChEBI:CHEBI:57318, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945, ChEBI:CHEBI:90726; EC=1.1.1.35; Evidence={ECO:0000255|HAMAP-Rule:MF_01621}; CATALYTIC ACTIVITY: Reaction=a (3S)-3-hydroxyacyl-CoA = a (2E)-enoyl-CoA + H2O; Xref=Rhea:RHEA:16105, ChEBI:CHEBI:15377, ChEBI:CHEBI:57318, ChEBI:CHEBI:58856; EC=4.2.1.17; Evidence={ECO:0000255|HAMAP-Rule:MF_01621}; CATALYTIC ACTIVITY: Reaction=a 4-saturated-(3S)-3-hydroxyacyl-CoA = a (3E)-enoyl-CoA + H2O; Xref=Rhea:RHEA:20724, ChEBI:CHEBI:15377, ChEBI:CHEBI:58521, ChEBI:CHEBI:137480; EC=4.2.1.17; Evidence={ECO:0000255|HAMAP-Rule:MF_01621}; CATALYTIC ACTIVITY: Reaction=(3S)-3-hydroxybutanoyl-CoA = (3R)-3-hydroxybutanoyl-CoA; Xref=Rhea:RHEA:21760, ChEBI:CHEBI:57315, ChEBI:CHEBI:57316; EC=5.1.2.3; Evidence={ECO:0000255|HAMAP-Rule:MF_01621}; CATALYTIC ACTIVITY: Reaction=a (3Z)-enoyl-CoA = a 4-saturated (2E)-enoyl-CoA; Xref=Rhea:RHEA:45900, ChEBI:CHEBI:85097, ChEBI:CHEBI:85489; EC=5.3.3.8; Evidence={ECO:0000255|HAMAP-Rule:MF_01621}; CATALYTIC ACTIVITY: Reaction=a (3E)-enoyl-CoA = a 4-saturated (2E)-enoyl-CoA; Xref=Rhea:RHEA:45228, ChEBI:CHEBI:58521, ChEBI:CHEBI:85097; EC=5.3.3.8; Evidence={ECO:0000255|HAMAP-Rule:MF_01621}; | null | PATHWAY: Lipid metabolism; fatty acid beta-oxidation. {ECO:0000255|HAMAP-Rule:MF_01621}. | null | null | FUNCTION: Involved in the aerobic and anaerobic degradation of long-chain fatty acids via beta-oxidation cycle. Catalyzes the formation of 3-oxoacyl-CoA from enoyl-CoA via L-3-hydroxyacyl-CoA. It can also use D-3-hydroxyacyl-CoA and cis-3-enoyl-CoA as substrate. {ECO:0000255|HAMAP-Rule:MF_01621}. | Yersinia enterocolitica serotype O:8 / biotype 1B (strain NCTC 13174 / 8081) |
A1KI36 | KGD_MYCBP | MANISSPFGQNEWLVEAMYRKFRDDPSSVDPSWHEFLVDYSPEPTSQPAAEPTRVTSPLVAERAAAAAPQAPPKPADTAAAGNGVVAALAAKTAVPPPAEGDEVAVLRGAAAAVVKNMSASLEVPTATSVRAVPAKLLIDNRIVINNQLKRTRGGKISFTHLLGYALVQAVKKFPNMNRHYTEVDGKPTAVTPAHTNLGLAIDLQGKDGKRSLVVAGIKRCETMRFAQFVTAYEDIVRRARDGKLTTEDFAGVTISLTNPGTIGTVHSVPRLMPGQGAIIGVGAMEYPAEFQGASEERIAELGIGKLITLTSTYDHRIIQGAESGDFLRTIHELLLSDGFWDEVFRELSIPYLPVRWSTDNPDSIVDKNARVMNLIAAYRNRGHLMADTDPLRLDKARFRSHPDLEVLTHGLTLWDLDRVFKVDGFAGAQYKKLRDVLGLLRDAYCRHIGVEYAHILDPEQKEWLEQRVETKHVKPTVAQQKYILSKLNAAEAFETFLQTKYVGQKRFSLEGAESVIPMMDAAIDQCAEHGLDEVVIGMPHRGRLNVLANIVGKPYSQIFTEFEGNLNPSQAHGSGDVKYHLGATGLYLQMFGDNDIQVSLTANPSHLEAVDPVLEGLVRAKQDLLDHGSIDSDGQRAFSVVPLMLHGDAAFAGQGVVAETLNLANLPGYRVGGTIHIIVNNQIGFTTAPEYSRSSEYCTDVAKMIGAPIFHVNGDDPEACVWVARLAVDFRQRFKKDVVIDMLCYRRRGHNEGDDPSMTNPYMYDVVDTKRGARKSYTEALIGRGDISMKEAEDALRDYQGQLERVFNEVRELEKHGVQPSESVESDQMIPAGLATAVDKSLLARIGDAFLALPNGFTAHPRVQPVLEKRREMAYEGKIDWAFGELLALGSLVAEGKLVRLSGQDSRRGTFSQRHSVLIDRHTGEEFTPLQLLATNSDGSPTGGKFLVYDSPLSEYAAVGFEYGYTVGNPDAVVLWEAQFGDFVNGAQSIIDEFISSGEAKWGQLSNVVLLLPHGHEGQGPDHTSARIERFLQLWAEGSMTIAMPSTPSNYFHLLRRHALDGIQRPLIVFTPKSMLRHKAAVSEIKDFTEIKFRSVLEEPTYEDGIGDRNKVSRILLTSGKLYYELAARKAKDNRNDLAIVRLEQLAPLPRRRLRETLDRYENVKEFFWVQEEPANQGAWPRFGLELPELLPDKLAGIKRISRRAMSAPSSGSSKVHAVEQQEILDEAFG | 1.2.4.2; 2.2.1.5; 2.3.1.61; 4.1.1.71 | COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250}; COFACTOR: Name=thiamine diphosphate; Xref=ChEBI:CHEBI:58937; Evidence={ECO:0000250}; | tricarboxylic acid cycle [GO:0006099] | cytosol [GO:0005829]; oxoglutarate dehydrogenase complex [GO:0045252] | 2-hydroxy-3-oxoadipate synthase activity [GO:0050439]; 2-oxoglutarate decarboxylase activity [GO:0008683]; dihydrolipoyllysine-residue succinyltransferase activity [GO:0004149]; magnesium ion binding [GO:0000287]; oxoglutarate dehydrogenase (succinyl-transferring) activity [GO:0004591]; thiamine pyrophosphate binding [GO:0030976] | PF00198;PF16078;PF00676;PF16870;PF02779; | 3.40.50.12470;3.40.50.970;3.30.559.10;3.40.50.11610;1.10.287.1150; | 2-oxoacid dehydrogenase family, Kgd subfamily | null | null | CATALYTIC ACTIVITY: Reaction=2-oxoglutarate + glyoxylate + H(+) = 2-hydroxy-3-oxoadipate + CO2; Xref=Rhea:RHEA:14341, ChEBI:CHEBI:15378, ChEBI:CHEBI:16526, ChEBI:CHEBI:16810, ChEBI:CHEBI:36655, ChEBI:CHEBI:57712; EC=2.2.1.5; CATALYTIC ACTIVITY: Reaction=2-oxoglutarate + H(+) = CO2 + succinate semialdehyde; Xref=Rhea:RHEA:10524, ChEBI:CHEBI:15378, ChEBI:CHEBI:16526, ChEBI:CHEBI:16810, ChEBI:CHEBI:57706; EC=4.1.1.71; CATALYTIC ACTIVITY: Reaction=2-oxoglutarate + H(+) + N(6)-[(R)-lipoyl]-L-lysyl-[dihydrolipoyllysine-residue succinyltransferase] = CO2 + N(6)-[(R)-S(8)-succinyldihydrolipoyl]-L-lysyl-[dihydrolipoyllysine-residue succinyltransferase]; Xref=Rhea:RHEA:12188, Rhea:RHEA-COMP:10483, Rhea:RHEA-COMP:10484, ChEBI:CHEBI:15378, ChEBI:CHEBI:16526, ChEBI:CHEBI:16810, ChEBI:CHEBI:83099, ChEBI:CHEBI:83120; EC=1.2.4.2; CATALYTIC ACTIVITY: Reaction=N(6)-[(R)-dihydrolipoyl]-L-lysyl-[2-oxoglutarate dehydrogenase complex component E2] + succinyl-CoA = CoA + N(6)-[(R)-S(8)-succinyldihydrolipoyl]-L-lysyl-[2-oxoglutarate dehydrogenase complex component E2]; Xref=Rhea:RHEA:15213, Rhea:RHEA-COMP:10581, Rhea:RHEA-COMP:10582, ChEBI:CHEBI:57287, ChEBI:CHEBI:57292, ChEBI:CHEBI:83100, ChEBI:CHEBI:83120; EC=2.3.1.61; | null | PATHWAY: Carbohydrate metabolism; tricarboxylic acid cycle; succinate from 2-oxoglutarate (transferase route): step 1/2.; PATHWAY: Carbohydrate metabolism; tricarboxylic acid cycle; succinyl-CoA from 2-oxoglutarate (dehydrogenase route): step 1/1. | null | null | FUNCTION: Shows three enzymatic activities that share a first common step, the attack of thiamine-PP on 2-oxoglutarate (alpha-ketoglutarate, KG), leading to the formation of an enamine-thiamine-PP intermediate upon decarboxylation. Thus, displays KGD activity, catalyzing the decarboxylation from five-carbon 2-oxoglutarate to four-carbon succinate semialdehyde (SSA). Also catalyzes C-C bond formation between the activated aldehyde formed after decarboxylation of alpha-ketoglutarate and the carbonyl of glyoxylate (GLX), to yield 2-hydroxy-3-oxoadipate (HOA), which spontaneously decarboxylates to form 5-hydroxylevulinate (HLA). And is also a component of the 2-oxoglutarate dehydrogenase (ODH) complex, that catalyzes the overall conversion of 2-oxoglutarate to succinyl-CoA and CO(2). The KG decarboxylase and KG dehydrogenase reactions provide two alternative, tightly regulated, pathways connecting the oxidative and reductive branches of the TCA cycle (By similarity). {ECO:0000250}. | Mycobacterium bovis (strain BCG / Pasteur 1173P2) |
A1KJ57 | LYSX_MYCBP | MGLHLTVPGLRRDGRGVQSNSHDTSSKTTADISRCPQHTDAGLQRAATPGISRLLGISSRSVTLTKPRSATRGNSRYHWVPAAAGWTVGVIATLSLLASVSPLIRWIIKVPREFINDYLFNFPDTNFAWSFVLALLAAALTARKRIAWLVLLANMVLAAVVNAAEIAAGGNTAAESFGENLGFAVHVVAIVVLVLGYREFWAKVRRGALFRAAAVWLAGAVVGIVASWGLVELFPGSLAPDERLGYAANRVVGFALADPDLFTGRPHVFLNAIFGLFGAFALIGAAIVLFLSQRADNALTGEDESAIRGLLDLYGKDDSLGYFATRRDKSVVFASSGRACITYRVEVGVCLASGDPVGDHRAWPQAVDAWLRLCQTYGWAPGVMGASSQGAQTYREAGLTALELGDEAILRPADFKLSGPEMRGVRQAVTRARRAGLTVRIRRHRDIAEDEMAQTITRADSWRDTETERGFSMALGRLGDPADSDCLLVEAIDPHNQVLAMLSLVPWGTTGVSLDLMRRSPQSPNGTIELMVSELALHAESLGITRISLNFAVFRAAFEQGAQLGAGPVARLWRGLLVFFSRWWQLETLYRSNMKYQPEWVPRYACYEDARVIPRVGVASVIAEGFLVLPFSRRNRVHTGHHPAVPERLAATGLLHHDGSAPDVSGLRQVGLTNGDGVERRLPEQVRVRFDKLEKLRSSGIDAFPVGRPPSHTVAQALAADHQASVSVSGRIMRIRNYGGVLFAQLRDWSGEMQVLLDNSRLDQGCAAEFNAATDLGDLVEMTGHMGASKTGTPSLIVSGWRLIGKCLRPLPNKWKGLLDPEARVRTRYLDLAVNAESRALITARSSVLRAVRETLFAKGFVEVETPILQQLHGGATARPFVTHINTYSMDLFLRIAPELYLKRLCVGGVERVFELGRAFRNEGVDFSHNPEFTLLEAYQAHAGYLEWIDGCRELIQNAAQAANGAPIAMRPRTDKGSDGTRHHLEPVDISGIWPVRTVHDAISEALGERIDADTGLTTLRKLCDAAGVPYRTQWDAGAVVLELYEHLVECRTEQPTFYIDFPTSVSPLTRPHRSKRGVAERWDLVAWGIELGTAYSELTDPVEQRRRLQEQSLLAAGGDPEAMELDEDFLQAMEYAMPPTGGLGMGIDRVVMLITGRSIRETLPFPLAKPH | 2.3.2.3; 6.1.1.6 | COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250}; Note=Binds 3 Mg(2+) ions per subunit. {ECO:0000250}; | diadenosine tetraphosphate biosynthetic process [GO:0015966]; lipid metabolic process [GO:0006629]; lysyl-tRNA aminoacylation [GO:0006430]; positive regulation of macrophage activation [GO:0043032]; response to antibiotic [GO:0046677] | aminoacyl-tRNA synthetase multienzyme complex [GO:0017101]; cytosol [GO:0005829]; extracellular space [GO:0005615]; plasma membrane [GO:0005886] | ATP adenylyltransferase activity [GO:0003877]; ATP binding [GO:0005524]; DNA binding [GO:0003677]; lysine-tRNA ligase activity [GO:0004824]; magnesium ion binding [GO:0000287]; phosphatidylglycerol lysyltransferase activity [GO:0050071]; tRNA binding [GO:0000049] | PF09924;PF00152;PF16995;PF01336; | 2.40.50.140; | LPG synthetase family; Class-II aminoacyl-tRNA synthetase family | null | SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}. | CATALYTIC ACTIVITY: Reaction=ATP + L-lysine + tRNA(Lys) = AMP + diphosphate + L-lysyl-tRNA(Lys); Xref=Rhea:RHEA:20792, Rhea:RHEA-COMP:9696, Rhea:RHEA-COMP:9697, ChEBI:CHEBI:30616, ChEBI:CHEBI:32551, ChEBI:CHEBI:33019, ChEBI:CHEBI:78442, ChEBI:CHEBI:78529, ChEBI:CHEBI:456215; EC=6.1.1.6; CATALYTIC ACTIVITY: Reaction=1,2-diacyl-sn-glycero-3-phospho-(1'-sn-glycerol) + L-lysyl-tRNA(Lys) = 1,2-diacyl-sn-glycero-3-phospho-1'-(3'-O-L-lysyl)-sn-glycerol + tRNA(Lys); Xref=Rhea:RHEA:10668, Rhea:RHEA-COMP:9696, Rhea:RHEA-COMP:9697, ChEBI:CHEBI:64716, ChEBI:CHEBI:75792, ChEBI:CHEBI:78442, ChEBI:CHEBI:78529; EC=2.3.2.3; | null | null | null | null | FUNCTION: Catalyzes the production of L-lysyl-tRNA(Lys)transfer and the transfer of a lysyl group from L-lysyl-tRNA(Lys) to membrane-bound phosphatidylglycerol (PG), which produces lysylphosphatidylglycerol (LPG), one of the components of the bacterial membrane with a positive net charge. LPG synthesis contributes to the resistance to cationic antimicrobial peptides (CAMPs) and likely protects M.tuberculosis against the CAMPs produced by competiting microorganisms (bacteriocins). In fact, the modification of anionic phosphatidylglycerol with positively charged L-lysine results in repulsion of the peptides (By similarity). {ECO:0000250}. | Mycobacterium bovis (strain BCG / Pasteur 1173P2) |
A1KPA8 | CH601_MYCBP | MSKLIEYDETARRAMEVGMDKLADTVRVTLGPRGRHVVLAKAFGGPTVTNDGVTVAREIELEDPFEDLGAQLVKSVATKTNDVAGDGTTTATILAQALIKGGLRLVAAGVNPIALGVGIGKAADAVSEALLASATPVSGKTGIAQVATVSSRDEQIGDLVGEAMSKVGHDGVVSVEESSTLGTELEFTEGIGFDKGFLSAYFVTDFDNQQAVLEDALILLHQDKISSLPDLLPLLEKVAGTGKPLLIVAEDVEGEALATLVVNAIRKTLKAVAVKGPYFGDRRKAFLEDLAVVTGGQVVNPDAGMVLREVGLEVLGSARRVVVSKDDTVIVDGGGTAEAVANRAKHLRAEIDKSDSDWDREKLGERLAKLAGGVAVIKVGAATETALKERKESVEDAVAAAKAAVEEGIVPGGGASLIHQARKALTELRASLTGDEVLGVDVFSEALAAPLFWIAANAGLDGSVVVNKVSELPAGHGLNVNTLSYGDLAADGVIDPVKVTRSAVLNASSVARMVLTTETVVVDKPAKAEDHDHHHGHAH | 5.6.1.7 | null | chaperone cofactor-dependent protein refolding [GO:0051085]; mitochondrial unfolded protein response [GO:0034514]; positive regulation of interferon-alpha production [GO:0032727]; positive regulation of interleukin-6 production [GO:0032755]; positive regulation of T cell activation [GO:0050870]; positive regulation of type II interferon production [GO:0032729]; protein import into mitochondrial intermembrane space [GO:0045041]; protein refolding [GO:0042026]; response to heat [GO:0009408] | GroEL-GroES complex [GO:1990220] | ATP binding [GO:0005524]; ATP-dependent protein folding chaperone [GO:0140662]; isomerase activity [GO:0016853]; metal ion binding [GO:0046872]; protein-folding chaperone binding [GO:0051087]; unfolded protein binding [GO:0051082] | PF00118; | 3.50.7.10;1.10.560.10;3.30.260.10; | Chaperonin (HSP60) family | null | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00600}. Note=Although thought of as a cytoplasmic chaperone this protein has been found to interact in vitro with a host extracellular protein. {ECO:0000269|PubMed:21203928}. | CATALYTIC ACTIVITY: Reaction=ATP + H2O + a folded polypeptide = ADP + phosphate + an unfolded polypeptide.; EC=5.6.1.7; Evidence={ECO:0000255|HAMAP-Rule:MF_00600}; | null | null | null | null | FUNCTION: Together with its co-chaperonin GroES, plays an essential role in assisting protein folding. The GroEL-GroES system forms a nano-cage that allows encapsulation of the non-native substrate proteins and provides a physical environment optimized to promote and accelerate protein folding. {ECO:0000255|HAMAP-Rule:MF_00600}.; FUNCTION: Involved in copper homeostasis (PubMed:32812602). Binds copper and may help maintaining copper homeostasis when copper is present in excess, notably in the macrophage phagosome, by acting as a metal storage protein (PubMed:32812602). Increases copper tolerance during biofilm formation (PubMed:32812602). In vitro binds to human CD209 (DC-SIGN) and may help mediate adherence to host cells (PubMed:21203928). {ECO:0000269|PubMed:21203928, ECO:0000269|PubMed:32812602}. | Mycobacterium bovis (strain BCG / Pasteur 1173P2) |
A1KXC4 | FCMR_MOUSE | MDFWLWLLYFLPVSGALRVLPEVQLNVEWGGSIIIECPLPQLHVRMYLCRQMAKPGICSTVVSNTFVKKEYERRVTLTPCLDKKLFLVEMTQLTENDDGIYACGVGMKTDKGKTQKITLNVHNEYPEPFWEDEWTSERPRWLHRFLQHQMPWLHGSEHPSSSGVIAKVTTPAPKTEAPPVHQPSSITSVTQHPRVYRAFSVSATKSPALLPATTASKTSTQQAIRPLEASYSHHTRLHEQRTRHHGPHYGREDRGLHIPIPEFHILIPTFLGFLLLVLLGLVVKRAIQRRRASSRRAGRLAMRRRGRGASRPFPTQRRDASQRPRSQNNVYSACPRRARGPDSLGPAEAPLLNAPASASPASPQVLEAPWPHTPSLKMSCEYVSLGYQPAVNLEDPDSDDYINIPDPSHLPSYAPGPRSSCP | null | null | Fc receptor-mediated immune complex endocytosis [GO:0160006]; humoral immune response mediated by circulating immunoglobulin [GO:0002455]; immunoglobulin transcytosis in epithelial cells [GO:0002414]; negative regulation of extrinsic apoptotic signaling pathway [GO:2001237]; negative regulation of lymphocyte apoptotic process [GO:0070229]; regulation of B cell receptor signaling pathway [GO:0050855] | cell surface [GO:0009986]; early endosome membrane [GO:0031901]; external side of plasma membrane [GO:0009897]; lysosomal membrane [GO:0005765]; plasma membrane [GO:0005886]; trans-Golgi network membrane [GO:0032588] | high-affinity IgM receptor activity [GO:0002172]; IgM binding [GO:0001791]; polymeric immunoglobulin binding [GO:0001790] | PF07686; | 2.60.40.10; | null | PTM: Phosphorylated on both Tyr and Ser residues. {ECO:0000250|UniProtKB:O60667}.; PTM: O-glycosylated. Sialylated. O-linked glycans regulate trafficking to the plasma membrane. {ECO:0000250|UniProtKB:O60667}. | SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:22988094, ECO:0000269|PubMed:25732732, ECO:0000269|PubMed:28135254}; Single-pass membrane protein {ECO:0000255}. Early endosome membrane {ECO:0000250|UniProtKB:O60667}; Single-pass membrane protein {ECO:0000255}. Golgi apparatus, trans-Golgi network membrane {ECO:0000269|PubMed:28135254}; Single-pass membrane protein {ECO:0000255}. Lysosome membrane {ECO:0000250|UniProtKB:O60667}; Single-pass membrane protein {ECO:0000255}. Note=Continuously recycles between cytoplasmic pool and the plasma membrane to bind as much IgM as possible (By similarity). In immature B cells, colocalizes with IgM in the trans-Golgi network and plasma membrane (PubMed:28135254). {ECO:0000250|UniProtKB:O60667, ECO:0000269|PubMed:28135254}. | null | null | null | null | null | FUNCTION: High-affinity Fc receptor for immunoglobulin M (IgM), both secreted and membrane-bound IgM (By similarity). Primarily regulates IgM transport and homeostasis. In lymphoid cells, enables exocytosis of membrane-bound IgM on the plasma membrane as well as endocytosis of IgM-antigen complexes toward lysosomes for degradation. In mucosal epithelium, mediates retrotranscytosis of antigen-IgM complexes across mucosal M cells toward antigen-presenting cells in mucosal lymphoid tissues (PubMed:28135254, PubMed:34788614). Triggers costimulatory signaling and mediates most of IgM effector functions involved in B cell development and primary immune response to infection. Likely limits tonic IgM BCR signaling to self-antigens for proper negative selection of autoreactive B cells in the bone marrow and for the maintenance of regulatory B cell pool in peripheral lymphoid organs. Mediates antibody responses to T cell-dependent and T cell-independent antigens and promotes induction of an efficient neutralizing IgG response. Engages in cross-talk with antigen-receptor signaling via the non-canonical NF-kappa-B, MAP kinases and calcium signaling pathways (By similarity) (PubMed:22988094, PubMed:23267023, PubMed:25732732, PubMed:28135254, PubMed:29461978). {ECO:0000250|UniProtKB:O60667, ECO:0000269|PubMed:22988094, ECO:0000269|PubMed:23267023, ECO:0000269|PubMed:25732732, ECO:0000269|PubMed:28135254, ECO:0000269|PubMed:29461978, ECO:0000269|PubMed:34788614}. | Mus musculus (Mouse) |
A1KXE4 | F168B_HUMAN | MNPVYSPGSSGVPYANAKGIGYPAGFPMGYAAAAPAYSPNMYPGANPTFQTGYTPGTPYKVSCSPTSGAVPPYSSSPNPYQTAVYPVRSAYPQQSPYAQQGTYYTQPLYAAPPHVIHHTTVVQPNGMPATVYPAPIPPPRGNGVTMGMVAGTTMAMSAGTLLTAHSPTPVAPHPVTVPTYRAPGTPTYSYVPPQW | null | null | null | axon [GO:0030424]; extracellular exosome [GO:0070062]; perinuclear region of cytoplasm [GO:0048471]; plasma membrane [GO:0005886] | null | PF14944; | null | FAM168 family | PTM: N-glycosylated. {ECO:0000250|UniProtKB:D4AEP3}. | SUBCELLULAR LOCATION: Cytoplasm, perinuclear region {ECO:0000250|UniProtKB:D4AEP3}. Cell membrane {ECO:0000250|UniProtKB:Q80XQ8}; Multi-pass membrane protein {ECO:0000250|UniProtKB:Q80XQ8}. Cell projection, axon {ECO:0000250|UniProtKB:Q80XQ8}. Note=Expressed in neuronal cell bodies and axonal fibers. {ECO:0000250|UniProtKB:Q80XQ8}. | null | null | null | null | null | FUNCTION: Inhibitor of neuronal axonal outgrowth. Acts as a negative regulator of CDC42 and STAT3 and a positive regulator of STMN2. Positive regulator of CDC27. {ECO:0000250|UniProtKB:D4AEP3}. | Homo sapiens (Human) |
A1KZ92 | PXDNL_HUMAN | MEPRLFCWTTLFLLAGWCLPGLPCPSRCLCFKSTVRCMHLMLDHIPQVPQQTTVLDLRFNRIREIPGSAFKKLKNLNTLLLNNNHIRKISRNAFEGLENLLYLYLYKNEIHALDKQTFKGLISLEHLYIHFNQLEMLQPETFGDLLRLERLFLHNNKLSKIPAGSFSNLDSLKRLRLDSNALVCDCDLMWLGELLQGFAQHGHTQAAATCEYPRRLHGRAVASVTVEEFNCQSPRITFEPQDVEVPSGNTVYFTCRAEGNPKPEIIWIHNNHSLDLEDDTRLNVFDDGTLMIRNTRESDQGVYQCMARNSAGEAKTQSAMLRYSSLPAKPSFVIQPQDTEVLIGTSTTLECMATGHPHPLITWTRDNGLELDGSRHVATSSGLYLQNITQRDHGRFTCHANNSHGTVQAAANIIVQAPPQFTVTPKDQVVLEEHAVEWLCEADGNPPPVIVWTKTGGQLPVEGQHTVLSSGTLRIDRAAQHDQGQYECQAVSSLGVKKVSVQLTVKPKALAVFTQLPQDTSVEVGKNINISCHAQGEPQPIITWNKEGVQITESGKFHVDDEGTLTIYDAGFPDQGRYECVARNSFGLAVTNMFLTVTAIQGRQAGDDFVESSILDAVQRVDSAINSTRRHLFSQKPHTSSDLLAQFHYPRDPLIVEMARAGEIFEHTLQLIRERVKQGLTVDLEGKEFRYNDLVSPRSLSLIANLSGCTARRPLPNCSNRCFHAKYRAHDGTCNNLQQPTWGAALTAFARLLQPAYRDGIRAPRGLGLPVGSRQPLPPPRLVATVWARAAAVTPDHSYTRMLMHWGWFLEHDLDHTVPALSTARFSDGRPCSSVCTNDPPCFPMNTRHADPRGTHAPCMLFARSSPACASGRPSATVDSVYAREQINQQTAYIDGSNVYGSSERESQALRDPSVPRGLLKTGFPWPPSGKPLLPFSTGPPTECARQEQESPCFLAGDHRANEHLALAAMHTLWFREHNRMATELSALNPHWEGNTVYQEARKIVGAELQHITYSHWLPKVLGDPGTRMLRGYRGYNPNVNAGIINSFATAAFRFGHTLINPILYRLNATLGEISEGHLPFHKALFSPSRIIKEGGIDPVLRGLFGVAAKWRAPSYLLSPELTQRLFSAAYSAAVDSAATIIQRGRDHGIPPYVDFRVFCNLTSVKNFEDLQNEIKDSEIRQKLRKLYGSPGDIDLWPALMVEDLIPGTRVGPTLMCLFVTQFQRLRDGDRFWYENPGVFTPAQLTQLKQASLSRVLCDNGDSIQQVQADVFVKAEYPQDYLNCSEIPKVDLRVWQDCCADCRSRGQFRAVTQESQKKRSAQYSYPVDKDMELSHLRSRQQDKIYVGEDARNVTVLAKTKFSQDFSTFAAEIQETITALREQINKLEARLRQAGCTDVRGVPRKAEERWMKEDCTHCICESGQVTCVVEICPPAPCPSPELVKGTCCPVCRDRGMPSDSPEKR | 1.-.-.- | COFACTOR: Name=heme b; Xref=ChEBI:CHEBI:60344; Evidence={ECO:0000255|PROSITE-ProRule:PRU00298}; | hydrogen peroxide catabolic process [GO:0042744]; response to oxidative stress [GO:0006979] | endoplasmic reticulum [GO:0005783]; extracellular space [GO:0005615]; plasma membrane [GO:0005886] | endonuclease activity [GO:0004519]; heme binding [GO:0020037]; lactoperoxidase activity [GO:0140825]; metal ion binding [GO:0046872]; peroxidase activity [GO:0004601] | PF03098;PF07679;PF13927;PF13855;PF00093; | 6.20.200.20;1.10.640.10;2.60.40.10;3.80.10.10; | Peroxidase family, XPO subfamily | PTM: Phosphorylation by SRC on tyrosine residues is required for targeting to polysomes. {ECO:0000269|PubMed:22543864}. | SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:24253521}. Endoplasmic reticulum {ECO:0000269|PubMed:24253521}. Cell membrane {ECO:0000269|PubMed:24253521}.; SUBCELLULAR LOCATION: [Isoform PMR1]: Cytoplasm. Note=Associates with polysomes. | null | null | null | null | null | FUNCTION: Probable oxidoreductase (Probable). Lacks peroxidase activity (PubMed:24253521). Inhibits the peroxidase activity of PXDN through its interaction (PubMed:24253521). {ECO:0000269|PubMed:24253521, ECO:0000305|PubMed:24253521}.; FUNCTION: [Isoform PMR1]: Endonuclease selectively degrading some target mRNAs while they are engaged by translating ribosomes, among which albumin and beta-globin mRNAs. {ECO:0000269|PubMed:22543864}. | Homo sapiens (Human) |
A1L0T0 | HACL2_HUMAN | METPAAAAPAGSLFPSFLLLACGTLVAALLGAAHRLGLFYQLLHKVDKASVRHGGENVAAVLRAHGVRFIFTLVGGHISPLLVACEKLGIRVVDTRHEVTAVFAADAMARLSGTVGVAAVTAGPGLTNTVTAVKNAQMAQSPILLLGGAASTLLQNRGALQAVDQLSLFRPLCKFCVSVRRVRDIVPTLRAAMAAAQSGTPGPVFVELPVDVLYPYFMVQKEMVPAKPPKGLVGRVVSWYLENYLANLFAGAWEPQPEGPLPLDIPQASPQQVQRCVEILSRAKRPLMVLGSQALLTPTSADKLRAAVETLGVPCFLGGMARGLLGRNHPLHIRENRSAALKKADVIVLAGTVCDFRLSYGRVLSHSSKIIIVNRNREEMLLNSDIFWKPQEAVQGDVGSFVLKLVEGLQGQTWAPDWVEELREADRQKEQTFREKAAMPVAQHLNPVQVLQLVEETLPDNSILVVDGGDFVGTAAHLVQPRGPLRWLDPGAFGTLGVGAGFALGAKLCRPDAEVWCLFGDGAFGYSLIEFDTFVRHKIPVMALVGNDAGWTQISREQVPSLGSNVACGLAYTDYHKAAMGLGARGLLLSRENEDQVVKVLHDAQQQCRDGHPVVVNILIGRTDFRDGSIAV | 4.1.2.- | COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250|UniProtKB:Q8CHM7}; Note=Binds 1 Mg(2+) ion per subunit. {ECO:0000250|UniProtKB:Q8CHM7}; COFACTOR: Name=thiamine diphosphate; Xref=ChEBI:CHEBI:58937; Evidence={ECO:0000269|PubMed:28289220}; Note=Binds 1 thiamine pyrophosphate per subunit. {ECO:0000250|UniProtKB:Q8CHM7}; | fatty acid alpha-oxidation [GO:0001561]; isoleucine biosynthetic process [GO:0009097]; valine biosynthetic process [GO:0009099] | acetolactate synthase complex [GO:0005948]; endoplasmic reticulum membrane [GO:0005789]; membrane [GO:0016020] | acetolactate synthase activity [GO:0003984]; flavin adenine dinucleotide binding [GO:0050660]; lyase activity [GO:0016829]; magnesium ion binding [GO:0000287]; thiamine pyrophosphate binding [GO:0030976] | PF02775;PF00205;PF02776; | 3.40.50.970;3.40.50.1220; | TPP enzyme family | null | SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000269|PubMed:28289220}; Single-pass membrane protein {ECO:0000255}. | CATALYTIC ACTIVITY: Reaction=2-hydroxyoctadecanoyl-CoA = formyl-CoA + heptadecanal; Xref=Rhea:RHEA:55196, ChEBI:CHEBI:57376, ChEBI:CHEBI:74116, ChEBI:CHEBI:138631; Evidence={ECO:0000269|PubMed:28289220}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:55197; Evidence={ECO:0000305|PubMed:28289220}; CATALYTIC ACTIVITY: Reaction=(2R)-hydroxyhexadecanoyl-CoA = formyl-CoA + pentadecanal; Xref=Rhea:RHEA:55212, ChEBI:CHEBI:17302, ChEBI:CHEBI:57376, ChEBI:CHEBI:138654; Evidence={ECO:0000269|PubMed:28289220}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:55213; Evidence={ECO:0000305|PubMed:28289220}; | null | null | null | null | FUNCTION: Endoplasmic reticulum 2-OH acyl-CoA lyase involved in the cleavage (C1 removal) reaction in the fatty acid alpha-oxydation in a thiamine pyrophosphate (TPP)-dependent manner. Involved in the phytosphingosine degradation pathway. {ECO:0000269|PubMed:28289220}. | Homo sapiens (Human) |
A1L167 | U2QL1_HUMAN | MKELQDIARLSDRFISVELVDESLFDWNVKLHQVDKDSVLWQDMKETNTEFILLNLTFPDNFPFSPPFMRVLSPRLENGYVLDGGAICMELLTPRGWSSAYTVEAVMRQFAASLVKGQGRICRKAGKSKKSFSRKEAEATFKSLVKTHEKYGWVTPPVSDG | 2.3.2.23 | null | protein polyubiquitination [GO:0000209] | nucleoplasm [GO:0005654]; nucleus [GO:0005634]; plasma membrane [GO:0005886] | ATP binding [GO:0005524]; ubiquitin conjugating enzyme activity [GO:0061631] | PF00179; | 3.10.110.10; | Ubiquitin-conjugating enzyme family | null | SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:24000165}. | CATALYTIC ACTIVITY: Reaction=S-ubiquitinyl-[E1 ubiquitin-activating enzyme]-L-cysteine + [E2 ubiquitin-conjugating enzyme]-L-cysteine = [E1 ubiquitin-activating enzyme]-L-cysteine + S-ubiquitinyl-[E2 ubiquitin-conjugating enzyme]-L-cysteine.; EC=2.3.2.23; Evidence={ECO:0000255|PROSITE-ProRule:PRU00388}; | null | PATHWAY: Protein modification; protein ubiquitination. {ECO:0000255|PROSITE-ProRule:PRU00388}. | null | null | FUNCTION: Probable E2 ubiquitin-protein ligase that catalyzes the covalent attachment of ubiquitin to target proteins. May facilitate the monoubiquitination and degradation of MTOR and CCNE1 through interaction with FBXW7. {ECO:0000269|PubMed:24000165}. | Homo sapiens (Human) |
A1L190 | SYCE3_HUMAN | MDDADPEERNYDNMLKMLSDLNKDLEKLLEEMEKISVQATWMAYDMVVMRTNPTLAESMRRLEDAFVNCKEEMEKNWQELLHETKQRL | null | null | apoptotic process [GO:0006915]; cell division [GO:0051301]; ectopic germ cell programmed cell death [GO:0035234]; positive regulation of apoptotic process [GO:0043065]; positive regulation of developmental process [GO:0051094]; positive regulation of reproductive process [GO:2000243]; reciprocal meiotic recombination [GO:0007131]; spermatogenesis [GO:0007283]; synaptonemal complex assembly [GO:0007130] | central element [GO:0000801]; chromosome [GO:0005694]; nucleus [GO:0005634] | null | PF15191; | null | null | null | SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:B5KM66}. Chromosome {ECO:0000250|UniProtKB:B5KM66}. Note=Colocalizes with SYCE1 in the central elements. {ECO:0000250|UniProtKB:B5KM66}. | null | null | null | null | null | FUNCTION: Major component of the transverse central element of synaptonemal complexes (SCS), formed between homologous chromosomes during meiotic prophase. Required for chromosome loading of the central element-specific SCS proteins, and for initiating synapsis between homologous chromosomes. Chromosome loading appears to require SYCP1. Required for fertility. {ECO:0000250|UniProtKB:B5KM66}. | Homo sapiens (Human) |
A1L1K7 | ACBG2_RAT | MTQEKKAEDPDRGMDTTSAAPRLWSTHCDGEVLLRLSKHGPGHETPMTIPELFQESVERFGAYPALASKNGKKWDTLTFSQYYDVCRKAARSLIKLGLQRFHGVGILGFNSVEWVVAALGAILAGGLCVGIYATNSAEACQYVIKQANVNVLIVENDQQLQKILSIPPDKMETVKAIVQYRLPLMENSTNLYSWQDFMELGNAIPNIQLDRVILSQKANQCAVIIYTSGTTGSPKGVMLSHDNITWTAGAMAREIELIHVSGKQDTIVSYLPLSHIAAQLMDIWIPIKVGVLTFFAQPDALRGTLVYTLQEVKPTYFLGVPRVWEKMQDTIKENVAKSSNLRKKAFAWAKMLGLKVNTKKMLGKRDIPMNYRMAKALVFTKVRTSLGLDNCHTFFSGASPLSQDVSEFFLSLDIPIGEIYGMTECSGPHTVSCKSIYRVLSCGKVLNGCKNMLYKQNKDGVGEVCMWGRHVFMGYLGKEDATLEVLDEDGWLHSGDIGRLDSHDFLYITGRIKEVLITAGGENIWPIPIETLVKEKIPIISHAMLVGDKAKFLSMLLTLKCETDQMSGEPLDKLNLEAISFCQMLGSQAVTVSDILKIRDPVVYTAIQYGIDIVNQQAVSDSHRIRKWIILEKDFSIQGGELGPTSKLKRDLITQKYKAQIDNMYSS | 6.2.1.15; 6.2.1.3 | null | cell differentiation [GO:0030154]; fatty acid metabolic process [GO:0006631]; long-chain fatty acid biosynthetic process [GO:0042759]; spermatogenesis [GO:0007283] | cytoplasm [GO:0005737]; cytosol [GO:0005829]; endoplasmic reticulum [GO:0005783]; membrane [GO:0016020]; mitochondrion [GO:0005739] | arachidonate-CoA ligase activity [GO:0047676]; ATP binding [GO:0005524]; fatty acyl-CoA hydrolase activity [GO:0047617]; long-chain fatty acid-CoA ligase activity [GO:0004467] | PF00501; | 3.40.50.12780; | ATP-dependent AMP-binding enzyme family, Bubblegum subfamily | null | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Membrane {ECO:0000250}; Peripheral membrane protein {ECO:0000250}. | CATALYTIC ACTIVITY: Reaction=a long-chain fatty acid + ATP + CoA = a long-chain fatty acyl-CoA + AMP + diphosphate; Xref=Rhea:RHEA:15421, ChEBI:CHEBI:30616, ChEBI:CHEBI:33019, ChEBI:CHEBI:57287, ChEBI:CHEBI:57560, ChEBI:CHEBI:83139, ChEBI:CHEBI:456215; EC=6.2.1.3; Evidence={ECO:0000250|UniProtKB:Q5FVE4}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:15422; Evidence={ECO:0000250|UniProtKB:Q5FVE4}; CATALYTIC ACTIVITY: Reaction=(5Z,8Z,11Z,14Z)-eicosatetraenoate + ATP + CoA = (5Z,8Z,11Z,14Z)-eicosatetraenoyl-CoA + AMP + diphosphate; Xref=Rhea:RHEA:19713, ChEBI:CHEBI:30616, ChEBI:CHEBI:32395, ChEBI:CHEBI:33019, ChEBI:CHEBI:57287, ChEBI:CHEBI:57368, ChEBI:CHEBI:456215; EC=6.2.1.15; Evidence={ECO:0000250|UniProtKB:Q5FVE4}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:19714; Evidence={ECO:0000250|UniProtKB:Q5FVE4}; CATALYTIC ACTIVITY: Reaction=ATP + CoA + hexadecanoate = AMP + diphosphate + hexadecanoyl-CoA; Xref=Rhea:RHEA:30751, ChEBI:CHEBI:7896, ChEBI:CHEBI:30616, ChEBI:CHEBI:33019, ChEBI:CHEBI:57287, ChEBI:CHEBI:57379, ChEBI:CHEBI:456215; Evidence={ECO:0000250|UniProtKB:Q5FVE4}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:30752; Evidence={ECO:0000250|UniProtKB:Q5FVE4}; CATALYTIC ACTIVITY: Reaction=(9Z)-octadecenoate + ATP + CoA = (9Z)-octadecenoyl-CoA + AMP + diphosphate; Xref=Rhea:RHEA:33607, ChEBI:CHEBI:30616, ChEBI:CHEBI:30823, ChEBI:CHEBI:33019, ChEBI:CHEBI:57287, ChEBI:CHEBI:57387, ChEBI:CHEBI:456215; Evidence={ECO:0000250|UniProtKB:Q5FVE4}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:33608; Evidence={ECO:0000250|UniProtKB:Q5FVE4}; CATALYTIC ACTIVITY: Reaction=(9Z,12Z)-octadecadienoate + ATP + CoA = (9Z,12Z)-octadecadienoyl-CoA + AMP + diphosphate; Xref=Rhea:RHEA:33651, ChEBI:CHEBI:30245, ChEBI:CHEBI:30616, ChEBI:CHEBI:33019, ChEBI:CHEBI:57287, ChEBI:CHEBI:57383, ChEBI:CHEBI:456215; Evidence={ECO:0000250|UniProtKB:Q5FVE4}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:33652; Evidence={ECO:0000250|UniProtKB:Q5FVE4}; CATALYTIC ACTIVITY: Reaction=ATP + CoA + tetracosanoate = AMP + diphosphate + tetracosanoyl-CoA; Xref=Rhea:RHEA:33639, ChEBI:CHEBI:30616, ChEBI:CHEBI:31014, ChEBI:CHEBI:33019, ChEBI:CHEBI:57287, ChEBI:CHEBI:65052, ChEBI:CHEBI:456215; Evidence={ECO:0000250|UniProtKB:Q5FVE4}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:33640; Evidence={ECO:0000250|UniProtKB:Q5FVE4}; | null | null | null | null | FUNCTION: Catalyzes the conversion of fatty acids such as long chain and very long-chain fatty acids to their active form acyl-CoAs for both synthesis of cellular lipids, and degradation via beta-oxidation. Can activate diverse saturated, monosaturated and polyunsaturated fatty acids. Has increased ability to activate oleic and linoleic acid. May play a role in spermatogenesis. {ECO:0000250|UniProtKB:Q5FVE4}. | Rattus norvegicus (Rat) |
A1L1K8 | HABP4_RAT | MKGALGSPVAAAGAAMQETFGCVVANRFHQLLDDESDPFDILREAEHRRQQQLQRKRRDEAAAASGAGHRGGRSPAVASGHRPGAAGRRESQKERKSLAVSSAQQPDSPGGPQPPGQKRTPRRGEQQGWNDNRGTDVVLDRAERRSYREYRPYDTERQAESTAEKFTDEKPVDRFDRDRPLRGRGGPRGGLRNRGRGGPGNRAFDSFDQRGKRDFERYGSSDKANRMEDSMGGCGVRTWGSGKDTSDTEPPAPMEETSMMEECQGVLDEESASKVPELEVEEENQVQEMTLDEWKNLQEQTRPKPEFNIRKPESTVPSKAVVIHKSRYRDDIVKDDYEDESHVFRKAANDITSQLEINFGNLPRPGRGARGSTRGGRGRIRRTENYGPRAEVVTQDVAPNPDDPEDFPALA | null | null | cellular response to mechanical stimulus [GO:0071260]; mRNA processing [GO:0006397]; negative regulation of DNA binding [GO:0043392]; PML body organization [GO:0030578]; positive regulation of RNA splicing [GO:0033120]; positive regulation of translational initiation [GO:0045948]; ribosome hibernation [GO:0141014]; RNA splicing [GO:0008380] | Cajal body [GO:0015030]; cytoplasm [GO:0005737]; cytoplasmic stress granule [GO:0010494]; cytosol [GO:0005829]; Gemini of coiled bodies [GO:0097504]; nuclear membrane [GO:0031965]; nuclear speck [GO:0016607]; nucleolus [GO:0005730]; nucleus [GO:0005634]; sarcomere [GO:0030017]; sarcoplasm [GO:0016528]; synapse [GO:0045202] | ribosome binding [GO:0043022]; RNA binding [GO:0003723]; SUMO binding [GO:0032183]; translation elongation factor binding [GO:0061770] | PF04774;PF16174; | null | SERBP1-HABP4 family | PTM: Phosphorylated by phorbol 12-myristate 13-acetate (PMA)-activated PKC isoforms at Thr-352 and Thr-373. {ECO:0000250|UniProtKB:Q5JVS0}.; PTM: Methylated. Methylation is decreased by phorbol 12-myristate 13-acetate (PMA)-activated PKC, in vitro. {ECO:0000250|UniProtKB:Q5JVS0}. | SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:15862299}. Cytoplasm {ECO:0000269|PubMed:15862299}. Cytoplasm, Stress granule {ECO:0000250|UniProtKB:Q5JVS0}. Cytoplasm, sarcoplasm {ECO:0000269|PubMed:15862299}. Nucleus, nuclear body {ECO:0000250|UniProtKB:Q5JVS0}. Nucleus, nucleolus {ECO:0000250|UniProtKB:Q5JVS0}. Nucleus speckle {ECO:0000250|UniProtKB:Q5JVS0}. Nucleus, Cajal body {ECO:0000250|UniProtKB:Q5JVS0}. Nucleus, gem {ECO:0000250|UniProtKB:Q5JVS0}. Note=Transported into the nuclear compartment in activated leukocytes. Inhibition of methylation alters its distribution between the nuclear and cytoplasmic compartments. Methylation may be required for its localization in subnuclear structures, such as nucleoli, nuclear speckles, Cajal bodies and Gemini of coiled bodies (gems). Colocalizes with FMR1, FXR1 and FXR2 in cytoplasmic stress granules (By similarity). In myocardial cells, localization at the sarcoplasm is reduced in response to mechanical stress (PubMed:15862299). {ECO:0000250|UniProtKB:Q5JVS0, ECO:0000269|PubMed:15862299}. | null | null | null | null | null | FUNCTION: Ribosome-binding protein that promotes ribosome hibernation, a process during which ribosomes are stabilized in an inactive state and preserved from proteasomal degradation (By similarity). Acts via its association with EEF2/eEF2 factor at the A-site of the ribosome, promoting ribosome stabilization in an inactive state compatible with storage (By similarity). Plays a key role in ribosome hibernation in the mature oocyte by promoting ribosome stabilization (By similarity). Ribosomes, which are produced in large quantities during oogenesis, are stored and translationally repressed in the oocyte and early embryo (By similarity). Also binds RNA, regulating transcription and pre-mRNA splicing. Binds (via C-terminus) to poly(U) RNA. Seems to play a role in PML-nuclear bodies formation (By similarity). Negatively regulates DNA-binding activity of the transcription factor MEF2C in myocardial cells in response to mechanical stress (PubMed:15862299). {ECO:0000250|UniProtKB:Q5JVS0, ECO:0000250|UniProtKB:Q5XJA5, ECO:0000269|PubMed:15862299}. | Rattus norvegicus (Rat) |
A1L1N5 | HN1BA_DANRE | MFANMVSKLTSLQQELLSALLDSGVTKDVLLQALEDLDPSPSAFGVKLDSLQMSPSGSKLSDTDSKPVFHTLTNGHSKGKLSGDEGSEDGDDYDTPPILKELQSQNTEEAAEQRAEIERMLAEDPWRAARMIKGYMQQHNIPQREVVDVTGLNQSHLSQHLNKGTPMKTQKRAALYTWYVRKQREILRQFNQATQGSGATMLDKGNQDQVLLFFSEFSQSGQGMVQPGDDAAIEPACKKLRRNRFKWGPASQQILYQAYERQKNPSKEEREALVEECNRAECLQRGVSPSKAHGLGSNLVTEVRVYNWFANRRKEEAFRQKLAMDAYSGPAHSLNSLLSHSSPHHPQTSSSPPSKMQGVRYSQQGPGEVTSSTTINHHSSNAMSTSQSVLQQVSPGALDPSHSLLSPDAKMISVSGGGLPPVSTLTNIHASHHVHQQTPNLIMPLSGVMAIAQSLNTSQAQTVPVINSVAGSLAALQPVQFSQQLNSQHQQLMQQSSGHMSQQSFMASVSHSHMYPHKQEPPQYSHSSRFPPAMVVTDANSLSTLSSMSSSKQCPLQAW | null | null | anterior/posterior pattern specification [GO:0009952]; anterior/posterior pattern specification involved in pronephros development [GO:0034672]; digestive tract morphogenesis [GO:0048546]; embryonic digestive tract development [GO:0048566]; endocrine pancreas development [GO:0031018]; endoderm formation [GO:0001706]; glucose homeostasis [GO:0042593]; hepaticobiliary system development [GO:0061008]; hindbrain development [GO:0030902]; hindbrain morphogenesis [GO:0021575]; insulin secretion [GO:0030073]; intrahepatic bile duct development [GO:0035622]; liver development [GO:0001889]; liver morphogenesis [GO:0072576]; otic placode formation [GO:0043049]; otic vesicle formation [GO:0030916]; otolith development [GO:0048840]; otolith morphogenesis [GO:0032474]; pancreas development [GO:0031016]; pancreas regeneration [GO:1990798]; positive regulation of DNA-templated transcription [GO:0045893]; regulation of transcription by RNA polymerase II [GO:0006357]; rhombomere 5 development [GO:0021571]; rhombomere 5 morphogenesis [GO:0021664]; rhombomere 6 development [GO:0021572]; rhombomere 6 morphogenesis [GO:0021667]; semicircular canal morphogenesis [GO:0048752]; tube formation [GO:0035148]; type B pancreatic cell development [GO:0003323] | nucleus [GO:0005634] | DNA binding [GO:0003677]; DNA-binding transcription factor activity [GO:0003700]; DNA-binding transcription factor activity, RNA polymerase II-specific [GO:0000981]; protein dimerization activity [GO:0046983]; RNA polymerase II cis-regulatory region sequence-specific DNA binding [GO:0000978] | PF04814;PF04812; | 1.10.10.60;1.10.260.40; | HNF1 homeobox family | null | SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00108}. | null | null | null | null | null | FUNCTION: Transcription factor that binds to the inverted palindrome 5'-GTTAATNATTAAC-3' (By similarity). Required for induction of rhombomere r5/r6 gene expression in the hindbrain. {ECO:0000250|UniProtKB:P35680, ECO:0000269|PubMed:18945197}. | Danio rerio (Zebrafish) (Brachydanio rerio) |
A1L1V4 | LOL2B_DANRE | MLALWSISFVLLCSWRLSYAQYEHLGFAIAYQEPEQDLYTPPELPADTPRIQLRLAGEKRKHNEGRVEVFYEGEWGTVCDDDFTIHAAQVICRELGYFEAISWSPSSKYGKGEGRIWFDNVHCKGKEKSLAQCESNGIGVSDCKHSEDVGVVCSDKRIPGFKFVNTLTNNINSLNIQVEDVRIRPILASYRKRIPVTEGYVEVKDGGKWKQICDDEWTQMNSRVICGMFGFPGQKRYNTRVYKMFARRRKPSYWDYTINCTGKEAHLSSCTLGHTLSNSTCEEGTPVVVSCIPGRAFAPTPMTGYKKAFRQEQPLVRLRGGAVVGEGRVEVLKNGEWGTICDDNWNLLAATVVCRELGFGSAKEALSGGQLGQGMGPVHMNEVQCSGFEKSVTECSFNMEKDSEGCSHEEDAGVKCNVPAMGFQQRLRLSGGRNPFEGRVEVLVERNGSLVWGTVCGEGWTTMEAMVVCRQLGLGFASNAFQETWYWPGAVNADAVVMSGVRCAGTEMSLSHCLHHGEYLSCPKGGGRFAAGVSCSETAPDLVLNPQVVEQTTYLEDRPMFMLQCAYEENCLASTSSATPANSPRRLLRFSSQIHNNGQSDFRPKISRENWVWHDCHRHYHSMEVFTHYDLLSTNGTKVAEGHKASFCLEDSECDEGIEKRYECANFGEQGITVGCWDTYRHDIDCQWVDITDVKPGDYIFQIVINPNYEVAESDYTNNIVKCRCRYDGHRIWMYNCHIGGSFSAETEDTFPGLINNQVTHR | 1.4.3.13 | COFACTOR: Name=Cu cation; Xref=ChEBI:CHEBI:23378; Evidence={ECO:0000250|UniProtKB:Q9Y4K0}; COFACTOR: Name=lysine tyrosylquinone residue; Xref=ChEBI:CHEBI:20489; Evidence={ECO:0000250|UniProtKB:Q9Y4K0}; Note=Contains 1 lysine tyrosylquinone. {ECO:0000250|UniProtKB:P33072, ECO:0000250|UniProtKB:Q9Y4K0}; | collagen fibril organization [GO:0030199]; endothelial cell migration [GO:0043542]; endothelial cell proliferation [GO:0001935]; epithelial to mesenchymal transition [GO:0001837]; heterochromatin organization [GO:0070828]; negative regulation of DNA-templated transcription [GO:0045892]; negative regulation of stem cell population maintenance [GO:1902455]; negative regulation of transcription by RNA polymerase II [GO:0000122]; peptidyl-lysine oxidation [GO:0018057]; positive regulation of chondrocyte differentiation [GO:0032332]; positive regulation of epithelial to mesenchymal transition [GO:0010718]; response to hypoxia [GO:0001666]; sprouting angiogenesis [GO:0002040] | basement membrane [GO:0005604]; chromatin [GO:0000785]; collagen-containing extracellular matrix [GO:0062023]; endoplasmic reticulum [GO:0005783]; extracellular space [GO:0005615]; membrane [GO:0016020]; nucleus [GO:0005634] | calcium ion binding [GO:0005509]; copper ion binding [GO:0005507]; protein-lysine 6-oxidase activity [GO:0004720] | PF01186;PF00530; | 3.10.250.10; | Lysyl oxidase family | PTM: The lysine tyrosylquinone cross-link (LTQ) is generated by condensation of the epsilon-amino group of a lysine with a topaquinone produced by oxidation of tyrosine. {ECO:0000250|UniProtKB:Q9Y4K0}. | SUBCELLULAR LOCATION: Secreted, extracellular space, extracellular matrix, basement membrane {ECO:0000250|UniProtKB:Q9Y4K0}. Nucleus {ECO:0000250|UniProtKB:Q9Y4K0}. Chromosome {ECO:0000250|UniProtKB:Q9Y4K0}. Endoplasmic reticulum {ECO:0000250|UniProtKB:Q9Y4K0}. Note=Associated with chromatin. It is unclear how LOXL2 is nuclear as it contains a signal sequence and has been shown to be secreted. However, a number of reports confirm its intracellular location and its key role in transcription regulation. {ECO:0000250|UniProtKB:Q9Y4K0}. | CATALYTIC ACTIVITY: Reaction=H2O + L-lysyl-[protein] + O2 = (S)-2-amino-6-oxohexanoyl-[protein] + H2O2 + NH4(+); Xref=Rhea:RHEA:24544, Rhea:RHEA-COMP:9752, Rhea:RHEA-COMP:12448, ChEBI:CHEBI:15377, ChEBI:CHEBI:15379, ChEBI:CHEBI:16240, ChEBI:CHEBI:28938, ChEBI:CHEBI:29969, ChEBI:CHEBI:131803; EC=1.4.3.13; Evidence={ECO:0000250|UniProtKB:Q9Y4K0}; | null | null | null | null | FUNCTION: Mediates the post-translational oxidative deamination of lysine residues on target proteins leading to the formation of deaminated lysine (allysine) (By similarity). Acts as a transcription corepressor and specifically mediates deamination of trimethylated 'Lys-4' of histone H3 (H3K4me3), a specific tag for epigenetic transcriptional activation (By similarity). Shows no activity against histone H3 when it is trimethylated on 'Lys-9' (H3K9me3) or 'Lys-27' (H3K27me3) or when 'Lys-4' is monomethylated (H3K4me1) or dimethylated (H3K4me2) (By similarity). Also mediates deamination of methylated TAF10, a member of the transcription factor IID (TFIID) complex, which induces release of TAF10 from promoters, leading to inhibition of TFIID-dependent transcription (By similarity). LOXL2-mediated deamination of TAF10 results in transcriptional repression of genes required for embryonic stem cell pluripotency (By similarity). Involved in epithelial to mesenchymal transition (EMT) and participates in repression of E-cadherin, probably by mediating deamination of histone H3 (By similarity). When secreted into the extracellular matrix, promotes cross-linking of extracellular matrix proteins by mediating oxidative deamination of peptidyl lysine residues in precursors to fibrous collagen and elastin (By similarity). Acts as a regulator of sprouting angiogenesis, probably via collagen IV scaffolding (PubMed:21835952). Acts as a regulator of chondrocyte differentiation, probably by regulating expression of factors that control chondrocyte differentiation (By similarity). Required with loxl2a for correct expression of Sox2 and for neural differentiation (PubMed:25959397). {ECO:0000250|UniProtKB:P58022, ECO:0000250|UniProtKB:Q9Y4K0, ECO:0000269|PubMed:25959397}. | Danio rerio (Zebrafish) (Brachydanio rerio) |
A1L259 | URAD_DANRE | MDINVVNALAYEDFVKLFGNVVEKCPLISAAIWSYRPFKDLADIEARISEFIHSLPDSGKEGILRCHPDLAGRDLQSGTLTPESQEEQSQAGMTTLDSAEIVHMYRLNSEYKERFGFPFVICARLNNKADIVRQLSERLKNRRTAELECAIEEVKKICSLRLHSIVLSDIQTKL | 4.1.1.97 | null | allantoin metabolic process [GO:0000255]; purine nucleobase metabolic process [GO:0006144]; urate catabolic process [GO:0019628] | peroxisome [GO:0005777] | 2-oxo-4-hydroxy-4-carboxy-5-ureidoimidazoline decarboxylase activity [GO:0051997] | PF09349; | 1.10.3330.10; | OHCU decarboxylase family | null | SUBCELLULAR LOCATION: Peroxisome {ECO:0000305}. | CATALYTIC ACTIVITY: Reaction=5-hydroxy-2-oxo-4-ureido-2,5-dihydro-1H-imidazole-5-carboxylate + H(+) = (S)-allantoin + CO2; Xref=Rhea:RHEA:26301, ChEBI:CHEBI:15378, ChEBI:CHEBI:15678, ChEBI:CHEBI:16526, ChEBI:CHEBI:58639; EC=4.1.1.97; | null | PATHWAY: Purine metabolism; urate degradation; (S)-allantoin from urate: step 3/3. | null | null | FUNCTION: Catalyzes the stereoselective decarboxylation of 2-oxo-4-hydroxy-4-carboxy-5-ureidoimidazoline (OHCU) to (S)-allantoin. {ECO:0000269|PubMed:17428786}. | Danio rerio (Zebrafish) (Brachydanio rerio) |
A1L2G3 | BAP1_DANRE | MNKGWLELESDPGLFTLLVEDFGVKGVQVEEIYDLQSKCQSPVYGFIFLFKWIEERRSRRKVSTLVDETSVIDDDIVNDMFFAHQLIPNSCATHALLSVLLNCSGVELGMTLSRMKAFTKGFNPESKGYAIGNAPELAKAHNSHARPEPRHLPEKQNGISAVRTMEAFHFVSYVPIKDRLFELDGLKAYPIDHGPWGEDEEWTDKARRVIMERIGLATAGEPYHDIRFNLMAVVPDRRIKYESKLDILKRNRQIILEGLQQIREKKVIRMTQQESGQDRKQQDSSSSEDTPPVVKKEEVQETPIPSGAEQATPTEAQEGAASLPSPAGKVRSMAKPALPAGGAPPPAPLPAPSTNTIVQRLPAFLDNHNYAKSPMQEEEDLAAGVGRSRPPQPPYSDDEDDYDDEEEECSTAGVTNSRVRRKLGLRTRTMSRTAVGGVAAMEGQLALSVLAEKLKKEVQRKDALATTGSTPLNVRTEGRTGGISITSACQPSPTPSNESTDTASEIGSAFNSPLRSPARSQATTRPSSPVASHVGRVLFGEEEGLPRLDARHNRAVRDLGVLVSSTQLQLQEDGVIFALPPTEALEGLKKVGGVDKKKKEEASGPGGEEEVKEGPSVEMKAEDVKESVDVKPEKENLPTTDVENSTKPPGEKYTPKELLALLKYVEADIANYEVYLKEEVEKRKKYKIDDQRRTHNYDEFICTFISMLAQEGMLASLVEQNISVRRRQGVSIGRLHKQRKPDRRKRSRPYKAKRQ | 3.4.19.12 | null | chromatin organization [GO:0006325]; cranial skeletal system development [GO:1904888]; negative regulation of DNA-templated transcription [GO:0045892]; Notch signaling pathway [GO:0007219]; protein deubiquitination [GO:0016579]; protein K48-linked deubiquitination [GO:0071108]; regulation of cell cycle [GO:0051726]; regulation of cell growth [GO:0001558]; ubiquitin-dependent protein catabolic process [GO:0006511] | cytoplasm [GO:0005737]; nucleus [GO:0005634]; PR-DUB complex [GO:0035517] | chromatin binding [GO:0003682]; cysteine-type deubiquitinase activity [GO:0004843] | PF01088;PF18031; | 1.20.58.860;3.40.532.10; | Peptidase C12 family, BAP1 subfamily | null | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q92560}. Nucleus {ECO:0000250|UniProtKB:Q92560}. Note=Mainly nuclear. Binds to chromatin. {ECO:0000250|UniProtKB:Q92560}. | CATALYTIC ACTIVITY: Reaction=Thiol-dependent hydrolysis of ester, thioester, amide, peptide and isopeptide bonds formed by the C-terminal Gly of ubiquitin (a 76-residue protein attached to proteins as an intracellular targeting signal).; EC=3.4.19.12; Evidence={ECO:0000250|UniProtKB:Q92560}; | null | null | null | null | FUNCTION: Deubiquitinating enzyme that plays a key role in chromatin by mediating deubiquitination of histone H2A. Catalytic component of the PR-DUB complex, a complex that specifically mediates deubiquitination of histone H2A monoubiquitinated at 'Lys-119' (H2AK119ub1) (By similarity). {ECO:0000250|UniProtKB:Q92560}. | Danio rerio (Zebrafish) (Brachydanio rerio) |
A1L314 | MPEG1_MOUSE | MNSFMALVLIWMIIACAEADKPLGETGTTGFQICKNALKLPVLEVLPGGGWDNLRNVDMGRVMDLTYTNCKTTEDGQYIIPDEVYTIPQKESNLEMNSEVLESWMNYQSTTSLSINTELALFSRVNGKFSTEFQRMKTLQVKDQAVTTRVQVRNRIYTVKTTPTSELSLGFTKALMDICDQLEKNQTKMATYLAELLILNYGTHVITSVDAGAALVQEDHVRSSFLLDNQNSQNTVTASAGIAFLNIVNFKVETDYISQTSLTKDYLSNRTNSRVQSFGGVPFYPGITLETWQKGITNHLVAIDRAGLPLHFFIKPDKLPGLPGPLVKKLSKTVETAVRHYYTFNTHPGCTNVDSPNFNFQANMDDDSCDAKVTNFTFGGVYQECTELSGDVLCQNLEQKNLLTGDFSCPPGYSPVHLLSQTHEEGYSRLECKKKCTLKIFCKTVCEDVFRVAKAEFRAYWCVAAGQVPDNSGLLFGGVFTDKTINPMTNAQSCPAGYIPLNLFESLKVCVSLDYELGFKFSVPFGGFFSCIMGNPLVNSDTAKDVRAPSLKKCPGGFSQHLAVISDGCQVSYCVKAGIFTGGSLLPVRLPPYTKPPLMSQVATNTVIVTNSETARSWIKDPQTNQWKLGEPLELRRAMTVIHGDSNGMSGGEAAGITLGVTIALGIVITLAIYGTRKYKKKEYQEIEEQESLVGSLATDATVLNGEEDPSPA | null | null | adaptive immune response [GO:0002250]; antibacterial innate immune response [GO:0140367]; antigen processing and presentation of exogenous peptide antigen [GO:0002478]; antigen processing and presentation of exogenous peptide antigen via MHC class I [GO:0042590]; defense response to bacterium [GO:0042742]; defense response to Gram-negative bacterium [GO:0050829]; defense response to Gram-positive bacterium [GO:0050830]; dendritic cell antigen processing and presentation [GO:0002468] | cytoplasmic vesicle [GO:0031410]; endolysosome [GO:0036019]; phagocytic vesicle [GO:0045335]; phagocytic vesicle membrane [GO:0030670]; phagolysosome membrane [GO:0061474] | pore-forming activity [GO:0140911]; wide pore channel activity [GO:0022829] | PF01823; | null | MPEG1 family | PTM: Proteolytically processed in two steps to generate the Macrophage-expressed gene 1 protein, processed form: cleaved by trypsin in proximity of the helical transmembrane domain releases the ectodomain into the lysosomal lumen to orient the pore-forming domain toward the endogenous membranes, and processed by the asparagine endopeptidase (LGMN) (PubMed:37347855). Proteolytic processing in antigen-containing vesicles is pH-dependent (PubMed:37347855). {ECO:0000269|PubMed:37347855}.; PTM: Monoubiquitinated in response to bacterial infection; ubiquitination is required for vesicular localization and antibacterial activity and can be blocked by bacterial cell cycle inhibiting factor (cif) (PubMed:26418746). {ECO:0000269|PubMed:26418746}. | SUBCELLULAR LOCATION: Cytoplasmic vesicle membrane {ECO:0000269|PubMed:26402460, ECO:0000269|PubMed:26418746, ECO:0000269|PubMed:35471730}; Multi-pass membrane protein {ECO:0000269|PubMed:32064340, ECO:0000269|PubMed:36245269}. Note=Bacterial infection induces translocation of the cytoplasmic vesicles to bacterium-containing phagocytic vesicles and fusing of the vesicles. {ECO:0000269|PubMed:26402460}.; SUBCELLULAR LOCATION: [Macrophage-expressed gene 1 protein, processed form]: Cytoplasmic vesicle, phagosome membrane {ECO:0000269|PubMed:37347855}; Multi-pass membrane protein {ECO:0000269|PubMed:32064340, ECO:0000269|PubMed:36245269}. Note=Proteolytically processed in lysosomes, leading to its maturation and forms pores in the membrane of antigen-containing phagosomes. {ECO:0000269|PubMed:37347855}. | null | null | null | null | null | FUNCTION: Pore-forming protein involved in both innate and adaptive immunity (PubMed:26402460, PubMed:30249808, PubMed:32064340, PubMed:36028507, PubMed:36245269, PubMed:37347855). Plays a central role in antigen cross-presentation in dendritic cells by forming a pore in antigen-containing compartments, thereby promoting delivery of antigens for cross-presentation (PubMed:35471730, PubMed:37347855). Also involved in innate immune response following bacterial infection; shows antibacterial activity against a wide spectrum of Gram-positive, Gram-negative and acid-fast bacteria (PubMed:23257510, PubMed:23753625, PubMed:26402460). Reduces the viability of the intracytosolic pathogen L.monocytogenes by inhibiting acidification of the phagocytic vacuole of host cells which restricts bacterial translocation from the vacuole to the cytosol (PubMed:26831467). Required for the antibacterial activity of reactive oxygen species and nitric oxide (PubMed:26402460). {ECO:0000269|PubMed:23257510, ECO:0000269|PubMed:23753625, ECO:0000269|PubMed:26402460, ECO:0000269|PubMed:26831467, ECO:0000269|PubMed:30249808, ECO:0000269|PubMed:32064340, ECO:0000269|PubMed:35471730, ECO:0000269|PubMed:36028507, ECO:0000269|PubMed:36245269, ECO:0000269|PubMed:37347855}.; FUNCTION: [Macrophage-expressed gene 1 protein, processed form]: Pore-forming protein that plays a central role in antigen cross-presentation in dendritic cells by mediating delivery of antigens for cross-presentation (PubMed:37347855). Dendritic cells bridge innate and adaptive immunity by capturing exogenous antigens on MHC class-I molecules and presenting them to naive CD8(+) T-cells (PubMed:37347855). Acts by forming a pore in antigen-containing compartments, promoting the release of antigens into the cytosol, enabling generation of MHCI:peptide complexes and T-cell priming (PubMed:37347855). {ECO:0000269|PubMed:37347855}. | Mus musculus (Mouse) |
A1L390 | PKHG3_HUMAN | MPVSTSLHQDGSQERPVSLTSTTSSSGSSCDSRSAMEEPSSSEAPAKNGAGSLRSRHLPNSNNNSSSWLNVKGPLSPFNSRAAAGPAHHKLSYLGRVVREIVETERMYVQDLRSIVEDYLLKIIDTPGLLKPEQVSALFGNIENIYALNSQLLRDLDSCNSDPVAVASCFVERSQEFDIYTQYCNNYPNSVAALTECMRDKQQAKFFRDRQELLQHSLPLGSYLLKPVQRILKYHLLLQEIAKHFDEEEDGFEVVEDAIDTMTCVAWYINDMKRRHEHAVRLQEIQSLLINWKGPDLTTYGELVLEGTFRVHRVRNERTFFLFDKTLLITKKRGDHFVYKGNIPCSSLMLIESTRDSLCFTVTHYKHSKQQYSIQAKTVEEKRNWTHHIKRLILENHHATIPQKAKEAILEMDSYYPNRYRCSPERLKKAWSSQDEVSTNVRQGRRQSEPTKHLLRQLNEKARAAGMKGKGRRESESSRSSRRPSGRSPTSTEKRMSFESISSLPEVEPDPEAGSEQEVFSAVEGPSAEETPSDTESPEVLETQLDAHQGLLGMDPPGDMVDFVAAESTEDLKALSSEEEEEMGGAAQEPESLLPPSVLDQASVIAERFVSSFSRRSSVAQEDSKSSGFGSPRLVSRSSSVLSLEGSEKGLARHGSATDSLSCQLSPEVDISVGVATEDSPSVNGMEPPSPGCPVEPDRSSCKKKESALSTRDRLLLDKIKSYYENAEHHDAGFSVRRRESLSYIPKGLVRNSISRFNSLPRPDPEPVPPVGSKRQVGSRPTSWALFELPGPSQAVKGDPPPISDAEFRPSSEIVKIWEGMESSGGSPGKGPGQGQANGFDLHEPLFILEEHELGAITEESATASPESSSPTEGRSPAHLARELKELVKELSSSTQGELVAPLHPRIVQLSHVMDSHVSERVKNKVYQLARQYSLRIKSNKPVMARPPLQWEKVAPERDGKSPTVPCLQEEAGEPLGGKGKRKPVLSLFDYEQLMAQEHSPPKPSSAGEMSPQRFFFNPSAVSQRTTSPGGRPSARSPLSPTETFSWPDVRELCSKYASRDEARRAGGGRPRGPPVNRSHSVPENMVEPPLSGRVGRCRSLSTKRGRGGGEAAQSPGPLPQSKPDGGETLYVTADLTLEDNRRVIVMEKGPLPSPTAGLEESSGQGPSSPVALLGQVQDFQQSAECQPKEEGSRDPADPSQQGRVRNLREKFQALNSVG | null | null | regulation of cell migration [GO:0030334]; regulation of establishment of cell polarity [GO:2000114]; regulation of small GTPase mediated signal transduction [GO:0051056] | cytoskeleton [GO:0005856]; cytosol [GO:0005829] | actin binding [GO:0003779]; guanyl-nucleotide exchange factor activity [GO:0005085]; small GTPase binding [GO:0031267] | PF00169;PF00621; | 1.20.900.10;2.30.29.30; | null | null | SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton {ECO:0000269|PubMed:27555588}. Note=Colocalizes with actin at the leading edge of polarized cells. {ECO:0000269|PubMed:27555588}. | null | null | null | null | null | FUNCTION: Plays a role in controlling cell polarity and cell motility by selectively binding newly polymerized actin and activating RAC1 and CDC42 to enhance local actin polymerization. {ECO:0000269|PubMed:27555588}. | Homo sapiens (Human) |
A1L3C1 | GAR5A_MOUSE | MKGGRDLKAARGGADRPLAPAYAPCRPGRLQRHLLSGEFDQLRDFPIFESNFVQVTRFGEVANKVTMGVAASSPALELPDLLLLAGPDKENGHLQLLGLFPLQFVQLFVHDESRQQLKVKFRTGRAFYLQLRSPPETRDCEFGRWVRLLYRLRFHSPTCAVPFTHEDTAPEEEEEEEEEEEEEEVKEGQLQPPEFQATEARLDPQVSELWGL | null | null | defense response to virus [GO:0051607]; innate immune response [GO:0045087]; positive regulation of type I interferon production [GO:0032481] | Golgi apparatus [GO:0005794]; nucleus [GO:0005634] | null | PF12480; | null | GARIN family | null | SUBCELLULAR LOCATION: Golgi apparatus {ECO:0000269|PubMed:28930687}. | null | null | null | null | null | FUNCTION: RAB2B effector protein which promotes cytosolic DNA-induced innate immune responses. Regulates IFN responses against DNA viruses by regulating the CGAS-STING signaling axis. {ECO:0000269|PubMed:28930687}. | Mus musculus (Mouse) |
A1L3G9 | NMP1B_XENLA | MAGEVEGRGCGFSLGVLVTLLVLPLPSLCTLSTEKELHVIKLYEGRMVRYNESRNFCYQRTYEPKWSDVWTKIQIRINSTKMIRVTQVDNEEKLKEMETFNMFDFFSSFLKEKLNDTFIYVNLYSNKTCVKVHLTDTDTYYSVALSRGFDPRLFFVFLCGLLLFFYGDTLSRSQLFFYSTGITVGMLASMLILVFMLSKLMPKKSPFFALLLGGWSVSIYVIQLVFRNLQAICSEYWQYLIVYLGIVGFVSFAFCYIYGPLENERSINILNWTLQLIGLLLMYVSVQIQHIAVTIVVIAFCTKQIEYPVQWIYILYRKIKLKRAKPGPPRLLTEEEYRKQADVETRKALEELRECCSSPDFAAWKTISRIQSPKRFADFVEGSSHLTPNEVSVHEHEYGLGGSFLEDELFGEDSDVEEEMEIEPPLYPIPRSVF | null | null | erythrocyte enucleation [GO:0043131]; erythrocyte maturation [GO:0043249]; eye development [GO:0001654] | nuclear envelope [GO:0005635]; nuclear inner membrane [GO:0005637] | protein self-association [GO:0043621] | PF10225; | null | NEMP family | PTM: Phosphorylated. {ECO:0000269|PubMed:25946333}. | SUBCELLULAR LOCATION: Nucleus inner membrane {ECO:0000269|PubMed:19167377, ECO:0000269|PubMed:25946333}; Multi-pass membrane protein {ECO:0000255}; Nucleoplasmic side {ECO:0000269|PubMed:19167377}. Nucleus envelope {ECO:0000269|PubMed:19167377}. Note=Localization in the nuclear membrane is essential for its function. Colocalizes with lamins and banf1-a/b at the nuclear envelope. {ECO:0000269|PubMed:19167377, ECO:0000269|PubMed:25946333}. | null | null | null | null | null | FUNCTION: In concert with ran, required for proper eye development (PubMed:25946333). May be involved in the expression of early eye marker genes (PubMed:19167377). Contributes to nuclear envelope stiffness in germ cells (By similarity). Required for fertility (By similarity). Essential for normal erythropoiesis (By similarity). Required for efficient nuclear envelope opening and enucleation during the late stages of erythroblast maturation (By similarity). {ECO:0000250|UniProtKB:O14524, ECO:0000250|UniProtKB:Q6ZQE4, ECO:0000269|PubMed:19167377, ECO:0000269|PubMed:25946333}. | Xenopus laevis (African clawed frog) |
A1L3P4 | SL9A6_MOUSE | MAGARRGWRLAPVRRGVCGPRARPLMRPLWLLFAVSFFGWTGALDGSGGTTRAMDEEIVSEKQAEESHRQDSANLLIFILLLTLTILTIWLFKHRRARFLHETGLAMIYGLLVGLVLRYGIHVPSDVNNVTLSCEVQSSPTTLLVNVSGKFYEYTLKGEISSHELNNVQDNEMLRKVTFDPEVFFNILLPPIIFYAGYSLKRRHFFRNLGSILAYAFLGTAISCFVIGSIMYGCVTLMKVTGQLAGDFYFTDCLLFGAIVSATDPVTVLAIFHELQVDVELYALLFGESVLNDAVAIVLSSSIVAYQPAGDNSHTFDVTAMFKSIGIFLGIFSGSFAMGAATGVVTALVTKFTKLREFQLLETGLFFLMSWSTFLLAEAWGFTGVVAVLFCGITQAHYTYNNLSTESQHRTKQLFELLNFLAENFIFSYMGLTLFTFQNHVFNPTFVVGAFIAIFLGRAANIYPLSLLLNLGRRSKIGSNFQHMMMFAGLRGAMAFALAIRDTATYARQMMFSTTLLIVFFTVWVFGGGTTAMLSCLHIRVGVDSDQEHLGVPDNERRTTKAESAWLFRMWYNFDHNYLKPLLTHSGPPLTTTLPACCGPIARCLTSPQAYENQEQLKDDDSDLILNDGDISLTYGDSTVNTESATASAPRRFMGNSSEDALDRELTFGDHELVIRGTRLVLPMDDSEPALNSLDDTRHSPA | null | null | axon extension [GO:0048675]; brain-derived neurotrophic factor receptor signaling pathway [GO:0031547]; dendrite extension [GO:0097484]; dendritic spine development [GO:0060996]; establishment of cell polarity [GO:0030010]; glial cell activation [GO:0061900]; neuron projection morphogenesis [GO:0048812]; potassium ion transmembrane transport [GO:0071805]; proton transmembrane transport [GO:1902600]; regulation of intracellular pH [GO:0051453]; regulation of neurotrophin TRK receptor signaling pathway [GO:0051386]; regulation of postsynaptic membrane neurotransmitter receptor levels [GO:0099072]; sodium ion import across plasma membrane [GO:0098719]; synapse organization [GO:0050808] | axon terminus [GO:0043679]; axonal spine [GO:0044308]; cytoplasmic vesicle [GO:0031410]; dendrite [GO:0030425]; early endosome [GO:0005769]; early endosome membrane [GO:0031901]; endosome [GO:0005768]; glutamatergic synapse [GO:0098978]; late endosome [GO:0005770]; late endosome membrane [GO:0031902]; mitochondrion [GO:0005739]; plasma membrane [GO:0005886]; recycling endosome [GO:0055037]; recycling endosome membrane [GO:0055038]; Schaffer collateral - CA1 synapse [GO:0098685]; synapse [GO:0045202] | 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: Ubiquitinated (in vitro). {ECO:0000250|UniProtKB:Q92581}.; PTM: Glycosylated. {ECO:0000250|UniProtKB:Q92581}. | SUBCELLULAR LOCATION: Endosome membrane {ECO:0000250|UniProtKB:Q92581}; Multi-pass membrane protein {ECO:0000255}. Recycling endosome membrane {ECO:0000269|PubMed:23303939, ECO:0000269|PubMed:24035762}; Multi-pass membrane protein {ECO:0000255}. Early endosome membrane {ECO:0000269|PubMed:23303939, ECO:0000269|PubMed:24035762}; Multi-pass membrane protein {ECO:0000255}. Late endosome membrane {ECO:0000269|PubMed:24035762}; Multi-pass membrane protein {ECO:0000255}. Cell membrane {ECO:0000269|PubMed:17005858}; Multi-pass membrane protein {ECO:0000255}. Note=Present predominantly in the recycling compartments including early and recycling endosomes, but undergoes plasma membrane localization during vesicular recycling, which is enhanced upon certain stimuli, such as hypoxia. {ECO:0000250|UniProtKB:Q92581}. | CATALYTIC ACTIVITY: Reaction=H(+)(out) + Na(+)(in) = H(+)(in) + Na(+)(out); Xref=Rhea:RHEA:29419, ChEBI:CHEBI:15378, ChEBI:CHEBI:29101; Evidence={ECO:0000305|PubMed:21413028}; CATALYTIC ACTIVITY: Reaction=H(+)(out) + K(+)(in) = H(+)(in) + K(+)(out); Xref=Rhea:RHEA:29467, ChEBI:CHEBI:15378, ChEBI:CHEBI:29103; Evidence={ECO:0000269|PubMed:17005858}; | null | null | null | null | FUNCTION: Endosomal Na(+), K(+)/H(+) antiporter. Mediates the electroneutral exchange of endosomal luminal H(+) for a cytosolic Na(+) or K(+). By facilitating proton efflux, SLC9A6 counteracts the acidity generated by vacuolar (V)-ATPase, thereby limiting luminal acidification. Responsible for alkalizing and maintaining the endosomal pH, and consequently in, e.g., endosome maturation and trafficking of recycling endosomal cargo (PubMed:17005858, PubMed:21413028, PubMed:24035762, PubMed:34526390). Plays a critical role during neurodevelopment by regulating synaptic development and plasticity (PubMed:21413028, PubMed:34526390). Implicated in the maintenance of cell polarity in a manner that is dependent on its ability to modulate intravesicular pH (By similarity). Regulates intracelular pH in some specialized cells, osteoclasts and stereocilia where this transporter localizes to the plasma membrane (PubMed:17005858, PubMed:21413028). {ECO:0000250|UniProtKB:Q92581, ECO:0000269|PubMed:17005858, ECO:0000269|PubMed:21413028, ECO:0000269|PubMed:24035762, ECO:0000269|PubMed:34526390}. | Mus musculus (Mouse) |
A1L3X0 | ELOV7_HUMAN | MAFSDLTSRTVHLYDNWIKDADPRVEDWLLMSSPLPQTILLGFYVYFVTSLGPKLMENRKPFELKKAMITYNFFIVLFSVYMCYEFVMSGWGIGYSFRCDIVDYSRSPTALRMARTCWLYYFSKFIELLDTIFFVLRKKNSQVTFLHVFHHTIMPWTWWFGVKFAAGGLGTFHALLNTAVHVVMYSYYGLSALGPAYQKYLWWKKYLTSLQLVQFVIVAIHISQFFFMEDCKYQFPVFACIIMSYSFMFLLLFLHFWYRAYTKGQRLPKTVKNGTCKNKDN | 2.3.1.199 | null | fatty acid elongation, monounsaturated fatty acid [GO:0034625]; fatty acid elongation, polyunsaturated fatty acid [GO:0034626]; fatty acid elongation, saturated fatty acid [GO:0019367]; long-chain fatty-acyl-CoA biosynthetic process [GO:0035338]; sphingolipid biosynthetic process [GO:0030148]; unsaturated fatty acid biosynthetic process [GO:0006636]; very long-chain fatty acid biosynthetic process [GO:0042761] | endoplasmic reticulum [GO:0005783]; endoplasmic reticulum membrane [GO:0005789] | fatty acid elongase activity [GO:0009922] | PF01151; | null | ELO family, ELOVL7 subfamily | null | SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000255|HAMAP-Rule:MF_03207, ECO:0000269|PubMed:20937905}; Multi-pass membrane protein {ECO:0000255|HAMAP-Rule:MF_03207}. | CATALYTIC ACTIVITY: Reaction=a very-long-chain acyl-CoA + H(+) + malonyl-CoA = a very-long-chain 3-oxoacyl-CoA + CO2 + CoA; Xref=Rhea:RHEA:32727, ChEBI:CHEBI:15378, ChEBI:CHEBI:16526, ChEBI:CHEBI:57287, ChEBI:CHEBI:57384, ChEBI:CHEBI:90725, ChEBI:CHEBI:90736; EC=2.3.1.199; Evidence={ECO:0000255|HAMAP-Rule:MF_03207, ECO:0000269|PubMed:20937905, ECO:0000269|PubMed:21959040, ECO:0000269|PubMed:34117479}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:32728; Evidence={ECO:0000305|PubMed:20937905}; CATALYTIC ACTIVITY: Reaction=eicosanoyl-CoA + H(+) + malonyl-CoA = 3-oxodocosanoyl-CoA + CO2 + CoA; Xref=Rhea:RHEA:35327, ChEBI:CHEBI:15378, ChEBI:CHEBI:16526, ChEBI:CHEBI:57287, ChEBI:CHEBI:57380, ChEBI:CHEBI:57384, ChEBI:CHEBI:71451; Evidence={ECO:0000269|PubMed:20937905, ECO:0000269|PubMed:21959040}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:35328; Evidence={ECO:0000305|PubMed:20937905}; CATALYTIC ACTIVITY: Reaction=(5Z,8Z,11Z,14Z)-eicosatetraenoyl-CoA + H(+) + malonyl-CoA = (7Z,10Z,13Z,16Z)-3-oxodocosatetraenoyl-CoA + CO2 + CoA; Xref=Rhea:RHEA:36475, ChEBI:CHEBI:15378, ChEBI:CHEBI:16526, ChEBI:CHEBI:57287, ChEBI:CHEBI:57368, ChEBI:CHEBI:57384, ChEBI:CHEBI:73852; Evidence={ECO:0000269|PubMed:20937905, ECO:0000269|PubMed:21959040}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:36476; Evidence={ECO:0000305|PubMed:20937905}; CATALYTIC ACTIVITY: Reaction=(6Z,9Z,12Z)-octadecatrienoyl-CoA + H(+) + malonyl-CoA = (8Z,11Z,14Z)-3-oxoeicosatrienoyl-CoA + CO2 + CoA; Xref=Rhea:RHEA:35379, ChEBI:CHEBI:15378, ChEBI:CHEBI:16526, ChEBI:CHEBI:57287, ChEBI:CHEBI:57363, ChEBI:CHEBI:57384, ChEBI:CHEBI:71481; Evidence={ECO:0000269|PubMed:20937905, ECO:0000269|PubMed:21959040}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:35380; Evidence={ECO:0000305|PubMed:20937905}; CATALYTIC ACTIVITY: Reaction=(9Z,12Z)-octadecadienoyl-CoA + H(+) + malonyl-CoA = (11Z,14Z)-3-oxoicosa-11,14-dienoyl-CoA + CO2 + CoA; Xref=Rhea:RHEA:36503, ChEBI:CHEBI:15378, ChEBI:CHEBI:16526, ChEBI:CHEBI:57287, ChEBI:CHEBI:57383, ChEBI:CHEBI:57384, ChEBI:CHEBI:74012; Evidence={ECO:0000269|PubMed:20937905, ECO:0000269|PubMed:21959040}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:36504; Evidence={ECO:0000305|PubMed:20937905}; CATALYTIC ACTIVITY: Reaction=(9Z)-octadecenoyl-CoA + H(+) + malonyl-CoA = (11Z)-3-oxoicosenoyl-CoA + CO2 + CoA; Xref=Rhea:RHEA:36511, ChEBI:CHEBI:15378, ChEBI:CHEBI:16526, ChEBI:CHEBI:57287, ChEBI:CHEBI:57384, ChEBI:CHEBI:57387, ChEBI:CHEBI:74011; Evidence={ECO:0000269|PubMed:20937905, ECO:0000269|PubMed:21959040}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:36512; Evidence={ECO:0000305|PubMed:20937905}; CATALYTIC ACTIVITY: Reaction=H(+) + malonyl-CoA + octadecanoyl-CoA = 3-oxoeicosanoyl-CoA + CO2 + CoA; Xref=Rhea:RHEA:35319, ChEBI:CHEBI:15378, ChEBI:CHEBI:16526, ChEBI:CHEBI:57287, ChEBI:CHEBI:57384, ChEBI:CHEBI:57394, ChEBI:CHEBI:65115; Evidence={ECO:0000269|PubMed:20937905, ECO:0000269|PubMed:21959040, ECO:0000269|PubMed:34117479}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:35320; Evidence={ECO:0000305|PubMed:20937905}; CATALYTIC ACTIVITY: Reaction=H(+) + hexadecanoyl-CoA + malonyl-CoA = 3-oxooctadecanoyl-CoA + CO2 + CoA; Xref=Rhea:RHEA:35315, ChEBI:CHEBI:15378, ChEBI:CHEBI:16526, ChEBI:CHEBI:57287, ChEBI:CHEBI:57379, ChEBI:CHEBI:57384, ChEBI:CHEBI:71407; Evidence={ECO:0000269|PubMed:20937905, ECO:0000269|PubMed:21959040}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:35316; Evidence={ECO:0000305|PubMed:20937905}; CATALYTIC ACTIVITY: Reaction=(9Z,12Z,15Z)-octadecatrienoyl-CoA + H(+) + malonyl-CoA = (11Z,14Z,17Z)-3-oxoeicosatrienoyl-CoA + CO2 + CoA; Xref=Rhea:RHEA:36523, ChEBI:CHEBI:15378, ChEBI:CHEBI:16526, ChEBI:CHEBI:57287, ChEBI:CHEBI:57384, ChEBI:CHEBI:74034, ChEBI:CHEBI:74054; Evidence={ECO:0000269|PubMed:20937905, ECO:0000269|PubMed:21959040}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:36524; Evidence={ECO:0000305|PubMed:20937905}; | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=2.6 uM for (9Z,12Z,15Z)-octadecatrienoyl-CoA/C18:3(n-3)-CoA {ECO:0000269|PubMed:21959040}; KM=11.7 uM for malonyl-CoA {ECO:0000269|PubMed:21959040}; Vmax=0.33 pmol/min/ug enzyme with (9Z,12Z,15Z)-octadecatrienoyl-CoA/C18:3(n-3)-CoA as substrate {ECO:0000269|PubMed:21959040}; Vmax=0.31 pmol/min/ug enzyme with malonyl-CoA as substrate {ECO:0000269|PubMed:21959040}; | PATHWAY: Lipid metabolism; fatty acid biosynthesis. {ECO:0000255|HAMAP-Rule:MF_03207, ECO:0000269|PubMed:20937905, ECO:0000269|PubMed:21959040}. | null | null | FUNCTION: Catalyzes the first and rate-limiting reaction of the four reactions that constitute the long-chain fatty acids elongation cycle. This endoplasmic reticulum-bound enzymatic process allows the addition of 2 carbons to the chain of long- and very long-chain fatty acids (VLCFAs) per cycle. Condensing enzyme with higher activity toward C18 acyl-CoAs, especially C18:3(n-3) acyl-CoAs and C18:3(n-6)-CoAs. Also active toward C20:4-, C18:0-, C18:1-, C18:2- and C16:0-CoAs, and weakly toward C20:0-CoA. Little or no activity toward C22:0-, C24:0-, or C26:0-CoAs. May participate in the production of saturated and polyunsaturated VLCFAs of different chain lengths that are involved in multiple biological processes as precursors of membrane lipids and lipid mediators. {ECO:0000255|HAMAP-Rule:MF_03207, ECO:0000269|PubMed:19826053, ECO:0000269|PubMed:20937905, ECO:0000269|PubMed:21959040, ECO:0000269|PubMed:34117479}. | Homo sapiens (Human) |
A1L4H1 | SRCRL_HUMAN | MRVLACLLAALVGIQAVERLRLADGPHGCAGRLEVWHGGRWGTVCDDGWDLRDAAVACRQLGCGGALAAPGGAFFGEGAGPVWLSELACRGNEGQLGLCHHRGWKAHICSHEEDAGVVCAGQRVANSRDDSTSPLDGAPWPGLLLELSPSTEEPLVTHAPRPAGNPQNASRKKSPRPKQAKSTRAPLLTTGAPRQERLRLVSGPHRCAGRLEVWHGGRWGTVCDDGWDLRDAAVACRELGCGGALAAPGGARFGPGAGPVWMDDVGCGGGEQALRDCPRSPWGRSNCDHSEDAGLVCTGPAPRLRLADGPHGCAGRLEVWHGGRWGSVCDDAWDLRDAAVACRELGCGGALAAPGGAFFGEGSGPIILDDLRCRGNETALRFCPARPWGQHDCHHREDAGAVCDGMPLGYVPPTAPTDSNNSTPREAASRPPSTMTSQAPGTAGVSPPPASPTVLWEPGPEAGSPQLRLVAGPSKCSGRLEVWHDQRWGTVCDDSWDMRDSAVVCRELGCGGPQQPDPAAGRFGWGAGPIWLDDVGCVGTEASLSDCPAAPWGKHNCAHNEDVGVTCTGPPGLDSISDPFSWSWIPGLGRDRDAWLPGELATKPSASVTASVLEKTTTKAPGKMPKSTKKWVTKNAKRPTTQPPVMPTTKHSRAQSPPDLTSQTTAALTTEASRRPTSEFTRRPTTEAPQRWTSHTTATLTPQAPRERTTKTMAMLTTQGPQEMTSESTIKSIPQASLEPSAEIPEGSPESPKDPAPSPSVSTTGESGLFRVRLADGPNRCAGRLEVWHAGRWGTVCDDNWDLRDATVACWELGCGKVRPRVGKTHYGPGTGPIWLDDMGCKGSEASLSDCPSGAWGKHNCDHEEDVGLTCTGYTDYDDYPPWTWDPTSREDLAKGTTTAGVPGHTLPWRTTRRPGSSSPAIRRLPDTGSKDGYKLPWTWDTPSGRGLAEGTPTAGKLGPTLGAGTTRSPGSPPTLRVHGDTGSPRKPWPERRPPRPAATRTAPPTPSPGPSASPGPPGPALTSDSSRELTPHSALTSEATSDAPDTSPPTPDPASRTNPDLILTSPDFALSTPDSSVVPALTPEPSPTPLPTLPKELTSDPSTPSEVTSLSPTSEQVPESDTTPDLDTTPYSSTVSEYSRSPDPSPSPHPTTTPDPTMAPDPITTLNPTVTPHFPTTPHPTTTPHPTTITHSTMIPDPTTTPQPFTTITHSTMIPDPTTTPQPFTTMQPTTTPHSTTPHPTTTPHPTTITHSTMIPDPTTTPQPFTTMQPTTMPHPTTTPHPTTTPHPTTTPHPTTTPHPTMTPDPTTTPYPTTTPDPTTTPHPTTPDPSSTPVITTVSLPTSLGTELSSPTLAPTVKPSLHPQLTFTAPAPHTSTSQIPTLEPSPALESSPSRSSTATSMDPLSTEDFKPPRSQSPNLTPPPTHTPHSASDLTVSPDPLLSPTAHPLDHPPLDPLTLGPTPGQSPGPHGPCVAPTPPVRVMACEPPALVELVAAVRDVGGQLQRLTQVVEQERQERQALLLGLTQLVEAARGLGQLGEAVKRLAEMAWTTSMPAPTTTTPEEEERPLRGDV | null | null | defense response [GO:0006952]; defense response to Gram-negative bacterium [GO:0050829]; defense response to Gram-positive bacterium [GO:0050830]; detection of bacterial lipoprotein [GO:0042494]; innate immune response [GO:0045087]; negative regulation of interleukin-8 production [GO:0032717]; zymogen activation [GO:0031638] | collagen-containing extracellular matrix [GO:0062023]; cytoplasm [GO:0005737]; extracellular matrix [GO:0031012]; extracellular space [GO:0005615]; plasma membrane [GO:0005886] | extracellular matrix binding [GO:0050840]; fibronectin binding [GO:0001968]; laminin binding [GO:0043236]; scavenger receptor activity [GO:0005044]; serine-type endopeptidase activity [GO:0004252] | PF00530; | 3.10.250.10; | null | null | SUBCELLULAR LOCATION: Secreted {ECO:0000250}. Cytoplasm {ECO:0000250}. | null | null | null | null | null | FUNCTION: Binds to extracellular matrix proteins. Binds to pathogen-associated molecular patterns (PAMPs) present on the cell walls of Gram-positive and Gram-negative bacteria and fungi, behaving as a pattern recognition receptor (PRR). Induces bacterial and fungal aggregation and subsequent inhibition of PAMP-induced cytokine release. Does not possess intrinsic bactericidal activity. May play a role in the innate defense and homeostasis of certain epithelial surfaces (By similarity). {ECO:0000250}. | Homo sapiens (Human) |
A1L4K1 | FSD2_HUMAN | MEEESGEELGLDRSTPKDFHFYHMDLYDSEDRLHLFPEENTRMRKVVQAEMANESRGAGDGKAQRDLQEEVDELVHLYGLEDDHELGDEFVDENIPRTGVSEYPPYMMKRRDPAREQRDWRLSGEAAEAEDLGFGGWGSAGQCQDLREAYRYTHGRASEEYECYVIPEEEDEEEAADVFCVTCKTPIRAFQKVFDEHKEHEVIPLNEALESAKDEIHKNMYKLEKQIIEMENFANHLEEVFITVEENFGKQEQNFESHYNEILETLAQKYEEKIQALGEKKKEKLEALYGQLVSCGENLDTCKELMETIEEMCHEEKVDFIKDAVAMADRLGKFLKTKTDVEISAQPEFEDQTLDFSDVEQLMGSINTIPAPSAPVINPQVPNSATGSSVRVCWSLYSDDTVESYQLSYRPVQDSSPGTDQAEFTVTVKETYCSVTNLVPNTQYEFWVTAHNRAGPSPSSERAVYMTAPSPPIIKTKEIRSCEEAVLICWESGNLNPVDSYTVELTQAESPEASGVTESVVGIPTCESVVQLQPGRSYIIYVRALNMGGPSVRSEPATVHTIGSYFRLNKDTCHPWLTISEDGLTAVRSERRTPARELSPSDTHFTRCVAVMGNLIPVRGHHYWEVEVDEHLDYRVGVAFADVRKQEDLGANCLSWCMRHTFASSRHKYEFLHNRTTPDIRITVPPKKIGILLDYEHSKLSFFNVDLSQHLYTFSCQLHEFVHPCFSLEKPGCLKVHNGISMPKHVTFY | null | null | null | nucleus [GO:0005634]; perinuclear region of cytoplasm [GO:0048471]; sarcoplasmic reticulum [GO:0016529] | null | PF00041;PF00622; | 2.60.120.920;3.30.160.60;2.60.40.10; | null | null | SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:H0UZ81}. Sarcoplasmic reticulum {ECO:0000250|UniProtKB:H0UZ81}. Cytoplasm, perinuclear region {ECO:0000250|UniProtKB:H0UZ81}. Note=In skeletal muscles and striated muscles flanks Z-disks. Partially colocalizes with RYR2 in the sarcoplasmic reticulum. {ECO:0000250|UniProtKB:H0UZ81}. | null | null | null | null | null | null | Homo sapiens (Human) |
A1S1I8 | FADB_SHEAM | MIYQSPTIQVELTADKIARLCFNAPGSVNKFDRETLASLNAALDVLKDSDAKAAVLTSGKDTFIVGADITEFLALFAEEDAKLMEWIAQANVVFNKLEDLPFPTVSAIKGFALGGGCEAILATDFRVADTSAKIGLPETKLGLIPGFGGTVRLPRLIGADNALEWITTGKDQRPEDALKVGAIDAVVAPENLEAAAIQMLNDALAGKLDWQARRARKQAPLTLPKLEAMMSFTTAKGMVYAVAGKHYPAPMAAVSVVEQAAGMSRAEALVVEHNAFIKLAKTDVATALIGIFLNDQLVKGKAKKASKLAKDIKHAAVLGAGIMGGGIAYQSASKGTPIVMKDINQAALDLGVNEAAKLLSAQVARGRSTPDKMAKVLNNITPALDYAPLKDVNVVVEAVVENPKVKAMVLADVENVVADDAIIASNTSTISIDLLAKSLKNPARFCGMHFFNPVHKMPLVEVIRGKDTSEETVASVVAYASKMGKTPIVVNDCPGFFVNRVLFPYFAGFNGLLADGGDFAAIDKVMEKQFGWPMGPAYLLDVVGLDTGHHAQAVMADGFPDRMGKSDKDAIDVMYEAGRLGQKNGKGFYQYSIDKRGKPKKDVDPASYTMLAEAFGAQKAFEADEIIARTMIPMIIETVRCLEEGIVASPAEADMGLVYGLGFPPFRGGVFRYLDTMGVANFVALADKYAHLGGLYQVTDAMRELASNNGSYYPKA | 1.1.1.35; 4.2.1.17; 5.1.2.3; 5.3.3.8 | null | fatty acid beta-oxidation [GO:0006635] | fatty acid beta-oxidation multienzyme complex [GO:0036125] | 3-hydroxyacyl-CoA dehydrogenase activity [GO:0003857]; 3-hydroxybutyryl-CoA epimerase activity [GO:0008692]; delta(3)-delta(2)-enoyl-CoA isomerase activity [GO:0004165]; enoyl-CoA hydratase activity [GO:0004300]; NAD+ binding [GO:0070403] | PF00725;PF02737;PF00378; | 1.10.1040.50;3.40.50.720; | Enoyl-CoA hydratase/isomerase family; 3-hydroxyacyl-CoA dehydrogenase family | null | null | CATALYTIC ACTIVITY: Reaction=a (3S)-3-hydroxyacyl-CoA + NAD(+) = a 3-oxoacyl-CoA + H(+) + NADH; Xref=Rhea:RHEA:22432, ChEBI:CHEBI:15378, ChEBI:CHEBI:57318, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945, ChEBI:CHEBI:90726; EC=1.1.1.35; Evidence={ECO:0000255|HAMAP-Rule:MF_01621}; CATALYTIC ACTIVITY: Reaction=a (3S)-3-hydroxyacyl-CoA = a (2E)-enoyl-CoA + H2O; Xref=Rhea:RHEA:16105, ChEBI:CHEBI:15377, ChEBI:CHEBI:57318, ChEBI:CHEBI:58856; EC=4.2.1.17; Evidence={ECO:0000255|HAMAP-Rule:MF_01621}; CATALYTIC ACTIVITY: Reaction=a 4-saturated-(3S)-3-hydroxyacyl-CoA = a (3E)-enoyl-CoA + H2O; Xref=Rhea:RHEA:20724, ChEBI:CHEBI:15377, ChEBI:CHEBI:58521, ChEBI:CHEBI:137480; EC=4.2.1.17; Evidence={ECO:0000255|HAMAP-Rule:MF_01621}; CATALYTIC ACTIVITY: Reaction=(3S)-3-hydroxybutanoyl-CoA = (3R)-3-hydroxybutanoyl-CoA; Xref=Rhea:RHEA:21760, ChEBI:CHEBI:57315, ChEBI:CHEBI:57316; EC=5.1.2.3; Evidence={ECO:0000255|HAMAP-Rule:MF_01621}; CATALYTIC ACTIVITY: Reaction=a (3Z)-enoyl-CoA = a 4-saturated (2E)-enoyl-CoA; Xref=Rhea:RHEA:45900, ChEBI:CHEBI:85097, ChEBI:CHEBI:85489; EC=5.3.3.8; Evidence={ECO:0000255|HAMAP-Rule:MF_01621}; CATALYTIC ACTIVITY: Reaction=a (3E)-enoyl-CoA = a 4-saturated (2E)-enoyl-CoA; Xref=Rhea:RHEA:45228, ChEBI:CHEBI:58521, ChEBI:CHEBI:85097; EC=5.3.3.8; Evidence={ECO:0000255|HAMAP-Rule:MF_01621}; | null | PATHWAY: Lipid metabolism; fatty acid beta-oxidation. {ECO:0000255|HAMAP-Rule:MF_01621}. | null | null | FUNCTION: Involved in the aerobic and anaerobic degradation of long-chain fatty acids via beta-oxidation cycle. Catalyzes the formation of 3-oxoacyl-CoA from enoyl-CoA via L-3-hydroxyacyl-CoA. It can also use D-3-hydroxyacyl-CoA and cis-3-enoyl-CoA as substrate. {ECO:0000255|HAMAP-Rule:MF_01621}. | Shewanella amazonensis (strain ATCC BAA-1098 / SB2B) |
A1TDK2 | KGD_MYCVP | MNSPSPFGQNEWLVEEMYRKFREDPSSVDPSWHEFLVDYSPEPTNDAPAGNGKPAAAPTAPPEPASAPAPKPASTNGGAPPAKADTSTTRAPEKKPEEKTSPAPKAKTAAPAGVSDDDETQVLRGAAAAVVKNMSASLDVPTATSVRAIPAKAMIDNRIVINNHLKRTRGGKISFTHLLGYAIVQAVKKFPNMNRHFAEIDGKPVAVTPAHTNLGLAIDLPGKDGKRSLVVAAIKNCETMHFGQFIAAYEDIVRRARDGKLTAEDFAGVTISLTNPGTIGTVHSVPRLMKGQGAIVGAGAMEYPAEFQGASEERIAELGVGKLMTLTSTYDHRIIQGAESGDFLRTIHTLLLDDEFYDEIFRELGIPHEPVRWRIDNPDSIEDKNARVIELIAAYRNRGHLMADIDPLRLDKTRFRSHPDLDVNTHGLTLWDLDREFKVNGFAGKTHKKLRDILGLLRDAYCRHIGVEYTHILEPEQQQWLQERIEVKHEKPTVAEQKYILSKLNAAEAFETFLQTKYVGQKRFSLEGAETVIPMMDAAIDQCAEHGLDEVVIGMPHRGRLNVLANIVGKPYSQIFTEFEGNLNPSQAHGSGDVKYHLGANGTYIQMFGDNDIDVSLVANPSHLEAVDPVLEGLVRAKQDILDKGNGPDGFTVVPMMLHGDAAFAGQGVVAETLNLALLRGYRTGGTIHIIVNNQIGFTTSPYDSRSSEYCTDVAKMIGAPIFHVNGDDPEACVWVAKLAVDFRQKFKKDVVIDMLCYRRRGHNEGDDPSMTQPTMYDVIDTKRGVRKSYTEALIGRGDISMKEAEDALRDYQGQLERVFNEVRELEKHAIAPSSSVESDQMVPAGMSTAVDKSLLARIGDAHLGYPDDFNVHPRVKPVLEKRREMAYEGKVDWAFAELLALGTFLAEGKTIRFTGQDTRRGTFTQRHSVIIDRQTGREFTPLDLLTVDSDGNPTGGKFMAYDSALSEFAAVGFEYGYSVGNPNALVLWEAQFGDFVNGAQSIIDEFISSGEAKWGQLSDVVLLLPHGHEGQGPDHTSGRIERFLLLWAEGSMTIAMPSTPANYFHLLRRHGLDGIHRPLIVFTPKSMLRNKAAVSDLKDFTEMKFRSVLEEPTYTEGTGDRSKAKRILLTSGKLYYELAARKSKEGRDDVAILRLEQLAPLPKRRLAATLDEYPNAEQYFWVQEEPANQGAWPTLGLTLPEVLPEKLAGIKRISRRAMSAPSSGSSKVHAVEQQEIIDEAFG | 1.2.4.2; 2.2.1.5; 2.3.1.61; 4.1.1.71 | COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250}; COFACTOR: Name=thiamine diphosphate; Xref=ChEBI:CHEBI:58937; Evidence={ECO:0000250}; | tricarboxylic acid cycle [GO:0006099] | cytosol [GO:0005829]; oxoglutarate dehydrogenase complex [GO:0045252] | 2-hydroxy-3-oxoadipate synthase activity [GO:0050439]; 2-oxoglutarate decarboxylase activity [GO:0008683]; dihydrolipoyllysine-residue succinyltransferase activity [GO:0004149]; magnesium ion binding [GO:0000287]; oxoglutarate dehydrogenase (succinyl-transferring) activity [GO:0004591]; thiamine pyrophosphate binding [GO:0030976] | PF00198;PF16078;PF00676;PF16870;PF02779; | 3.40.50.12470;3.40.50.970;3.30.559.10;3.40.50.11610;1.10.287.1150; | 2-oxoacid dehydrogenase family, Kgd subfamily | null | null | CATALYTIC ACTIVITY: Reaction=2-oxoglutarate + glyoxylate + H(+) = 2-hydroxy-3-oxoadipate + CO2; Xref=Rhea:RHEA:14341, ChEBI:CHEBI:15378, ChEBI:CHEBI:16526, ChEBI:CHEBI:16810, ChEBI:CHEBI:36655, ChEBI:CHEBI:57712; EC=2.2.1.5; CATALYTIC ACTIVITY: Reaction=2-oxoglutarate + H(+) = CO2 + succinate semialdehyde; Xref=Rhea:RHEA:10524, ChEBI:CHEBI:15378, ChEBI:CHEBI:16526, ChEBI:CHEBI:16810, ChEBI:CHEBI:57706; EC=4.1.1.71; CATALYTIC ACTIVITY: Reaction=2-oxoglutarate + H(+) + N(6)-[(R)-lipoyl]-L-lysyl-[dihydrolipoyllysine-residue succinyltransferase] = CO2 + N(6)-[(R)-S(8)-succinyldihydrolipoyl]-L-lysyl-[dihydrolipoyllysine-residue succinyltransferase]; Xref=Rhea:RHEA:12188, Rhea:RHEA-COMP:10483, Rhea:RHEA-COMP:10484, ChEBI:CHEBI:15378, ChEBI:CHEBI:16526, ChEBI:CHEBI:16810, ChEBI:CHEBI:83099, ChEBI:CHEBI:83120; EC=1.2.4.2; CATALYTIC ACTIVITY: Reaction=N(6)-[(R)-dihydrolipoyl]-L-lysyl-[2-oxoglutarate dehydrogenase complex component E2] + succinyl-CoA = CoA + N(6)-[(R)-S(8)-succinyldihydrolipoyl]-L-lysyl-[2-oxoglutarate dehydrogenase complex component E2]; Xref=Rhea:RHEA:15213, Rhea:RHEA-COMP:10581, Rhea:RHEA-COMP:10582, ChEBI:CHEBI:57287, ChEBI:CHEBI:57292, ChEBI:CHEBI:83100, ChEBI:CHEBI:83120; EC=2.3.1.61; | null | PATHWAY: Carbohydrate metabolism; tricarboxylic acid cycle; succinate from 2-oxoglutarate (transferase route): step 1/2.; PATHWAY: Carbohydrate metabolism; tricarboxylic acid cycle; succinyl-CoA from 2-oxoglutarate (dehydrogenase route): step 1/1. | null | null | FUNCTION: Shows three enzymatic activities that share a first common step, the attack of thiamine-PP on 2-oxoglutarate (alpha-ketoglutarate, KG), leading to the formation of an enamine-thiamine-PP intermediate upon decarboxylation. Thus, displays KGD activity, catalyzing the decarboxylation from five-carbon 2-oxoglutarate to four-carbon succinate semialdehyde (SSA). Also catalyzes C-C bond formation between the activated aldehyde formed after decarboxylation of alpha-ketoglutarate and the carbonyl of glyoxylate (GLX), to yield 2-hydroxy-3-oxoadipate (HOA), which spontaneously decarboxylates to form 5-hydroxylevulinate (HLA). And is also a component of the 2-oxoglutarate dehydrogenase (ODH) complex, that catalyzes the overall conversion of 2-oxoglutarate to succinyl-CoA and CO(2). The KG decarboxylase and KG dehydrogenase reactions provide two alternative, tightly regulated, pathways connecting the oxidative and reductive branches of the TCA cycle (By similarity). {ECO:0000250}. | Mycolicibacterium vanbaalenii (strain DSM 7251 / JCM 13017 / BCRC 16820 / KCTC 9966 / NRRL B-24157 / PYR-1) (Mycobacterium vanbaalenii) |
A1TFU9 | HPXO_MYCVP | MKVVIVGAGMGGMSAAIALRQIGIDTVVYERVTENKPVGAAISVWSNGVKCLNYLGLQEETAELGGKVETMSYVDGHTGDTMCRFSMHPLIEQVGQRPYPIARAELQLMLMKAYGIDDINFGMKMVGVENDTAGSAAKATFADGTTVSADVIIGADGAGSITREYVLGGPVSRRYAGYVNYNGLVSTDDAIGPATEWTTYVGDGKRVSVMPVSDDRFYFFFDVVEPQGSPYEEGRVREVLRAHFAGWTPGVQTLIDTLDPLATNRVEILDLDPFHTWVKGRVAVLGDAAHNTTPDIGQGGCSAMEDAIALQWAFKDHPDDVHAALAAYQSARTERAADLVLRARKRCDVTHAKDPQVTSRWYDELRNEDGTNIIRGIVGNIVGGPLTPVTAATEG | 1.14.13.113 | COFACTOR: Name=FAD; Xref=ChEBI:CHEBI:57692; Evidence={ECO:0000269|PubMed:23760935}; | purine nucleobase metabolic process [GO:0006144]; urate catabolic process [GO:0019628] | null | FAD binding [GO:0071949]; FAD-dependent urate hydroxylase activity [GO:0102099]; NADH binding [GO:0070404]; NADPH binding [GO:0070402]; 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]; urate oxidase activity [GO:0004846] | PF01494; | 3.50.50.60; | FAD-dependent urate hydroxylase family | null | null | CATALYTIC ACTIVITY: Reaction=H(+) + NADH + O2 + urate = 5-hydroxyisourate + H2O + NAD(+); Xref=Rhea:RHEA:27329, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, ChEBI:CHEBI:17775, ChEBI:CHEBI:18072, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945; EC=1.14.13.113; Evidence={ECO:0000269|PubMed:23760935}; | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=413 uM for urate {ECO:0000269|PubMed:23760935}; Note=kcat is 56.0 sec(-1) for the NADH-dependent oxidation of urate. Exhibits a Michaelian behavior only toward urate and a cooperative behavior toward NADH and NADPH. {ECO:0000269|PubMed:23760935}; | PATHWAY: Purine metabolism; urate degradation. {ECO:0000305|PubMed:23760935}. | null | null | FUNCTION: Catalyzes the hydroxylation of urate to 5-hydroxyisourate (HIU). Is likely to be involved in the urate degradation pathway to allantoin. Prefers NADH over NADPH as the electron donor. {ECO:0000269|PubMed:23760935}. | Mycolicibacterium vanbaalenii (strain DSM 7251 / JCM 13017 / BCRC 16820 / KCTC 9966 / NRRL B-24157 / PYR-1) (Mycobacterium vanbaalenii) |
A1UK81 | KGD_MYCSK | MSSSPSPFGQNEWLVEEMYRKFREDPSSVDPSWHEFLVDYNPEPTTDSSASENGQQTRTAAPKAPPEPAPAPAPKTPDSKTPDSKSQAPKQDSKPQESKPQAKAKPAESKSSTKPADAKSEKSGKSGTNGAAKPAAQPADDSDQNQVLRGAAAAVAKNMSASLDVPTATSVRAIPAKLMIDNRVVINNHLKRTRGGKISFTHLIGYAIVAAVKKFPNMNRHFAEVDGKPNAVTPAHTNLGLAIDLQGKDGNRQLVVAAIKKADTMRFGQFIAAYEDIVRRARDGKLTAEDFSGVTISLTNPGTIGTVHSVPRLMRGQGAIIGVGAMEYPAEFQGASEERIADLGIGKLITLTSTYDHRIIQGAESGDFLRTVHQLLLSDDFFDEIFRELGIPYEPVRWRTDNPDSIEDKNARVIELIAAYRNRGHLMADIDPLRLDSNRFRSHPDLDVLTHGLTLWDLDREFKVNGFAGAERKKLRDVLAVLRDAYCRHIGVEYTHILEPEQQQWLQERIEGKHEKPTVAQQKYILSRLNAAEAFETFLQTKYVGQKRFSLEGAETVIPAMDAVIDQCAEHALDEVVIGMPHRGRLNVLANIVGKPYSQIFSEFEGNLNPSQAHGSGDVKYHLGSSGTYLQMFGDNDITVSLTANPSHLEAVDPVMEGLVRAKQDLLDKGDTEDGYTVVPLMLHGDAAFAGQGVVAETLNLALLRGYRTGGTIHLIVNNQIGFTTSPAAAKSSEYCTDVAKMIGAPIFHVNGDDPEAAVWVSRLAVDFRQKFKKDVVIDLLCYRRRGHNEGDDPSMTQPSMYDVIDTKRGVRKSYTEALIGRGDISMKEAEDALRDYQGQLEQVFNEVRELEKHEIEPSESVEADQQIPAKLATAVDKSLLARIGDAHLAVPEGFTVHPRVKPVLEKRREMAYEGKVDWAFAELLALGTMISEGKLVRLSGQDTRRGTFTQRHSVVIDRKTGKEFTPLQLLATDSDGNPTGGKFLVYDSPLSEFAAVGFEYGYSVGNPDAMVLWEAQFGDFINGAQSIIDEFISSGEAKWGQLSDVVLLLPHGHEGQGPDHTSGRIERFLQLWAEGSMTIALPSTPANYFHLLRRHSLDGIQRPLIVFTPKSMLRNKAAVSDIRDFTEQKFRSVLEEPTYTDGDGDRNKVTRILLTSGKIYYELVARKNKESRDDVAIVRIEQLAPLPKRRLAETLDKYPNVEEKFWVQEEPANQGAWPTFGLTLPEMLPDHFTGIKRISRRAMSAPSSGSSKVHAVEQQEILDEAFAP | 1.2.4.2; 2.2.1.5; 2.3.1.61; 4.1.1.71 | COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250}; COFACTOR: Name=thiamine diphosphate; Xref=ChEBI:CHEBI:58937; Evidence={ECO:0000250}; | tricarboxylic acid cycle [GO:0006099] | cytosol [GO:0005829]; oxoglutarate dehydrogenase complex [GO:0045252] | 2-hydroxy-3-oxoadipate synthase activity [GO:0050439]; 2-oxoglutarate decarboxylase activity [GO:0008683]; dihydrolipoyllysine-residue succinyltransferase activity [GO:0004149]; magnesium ion binding [GO:0000287]; oxoglutarate dehydrogenase (succinyl-transferring) activity [GO:0004591]; thiamine pyrophosphate binding [GO:0030976] | PF00198;PF16078;PF00676;PF16870;PF02779; | 3.40.50.12470;3.40.50.970;3.30.559.10;3.40.50.11610;1.10.287.1150; | 2-oxoacid dehydrogenase family, Kgd subfamily | null | null | CATALYTIC ACTIVITY: Reaction=2-oxoglutarate + glyoxylate + H(+) = 2-hydroxy-3-oxoadipate + CO2; Xref=Rhea:RHEA:14341, ChEBI:CHEBI:15378, ChEBI:CHEBI:16526, ChEBI:CHEBI:16810, ChEBI:CHEBI:36655, ChEBI:CHEBI:57712; EC=2.2.1.5; CATALYTIC ACTIVITY: Reaction=2-oxoglutarate + H(+) = CO2 + succinate semialdehyde; Xref=Rhea:RHEA:10524, ChEBI:CHEBI:15378, ChEBI:CHEBI:16526, ChEBI:CHEBI:16810, ChEBI:CHEBI:57706; EC=4.1.1.71; CATALYTIC ACTIVITY: Reaction=2-oxoglutarate + H(+) + N(6)-[(R)-lipoyl]-L-lysyl-[dihydrolipoyllysine-residue succinyltransferase] = CO2 + N(6)-[(R)-S(8)-succinyldihydrolipoyl]-L-lysyl-[dihydrolipoyllysine-residue succinyltransferase]; Xref=Rhea:RHEA:12188, Rhea:RHEA-COMP:10483, Rhea:RHEA-COMP:10484, ChEBI:CHEBI:15378, ChEBI:CHEBI:16526, ChEBI:CHEBI:16810, ChEBI:CHEBI:83099, ChEBI:CHEBI:83120; EC=1.2.4.2; CATALYTIC ACTIVITY: Reaction=N(6)-[(R)-dihydrolipoyl]-L-lysyl-[2-oxoglutarate dehydrogenase complex component E2] + succinyl-CoA = CoA + N(6)-[(R)-S(8)-succinyldihydrolipoyl]-L-lysyl-[2-oxoglutarate dehydrogenase complex component E2]; Xref=Rhea:RHEA:15213, Rhea:RHEA-COMP:10581, Rhea:RHEA-COMP:10582, ChEBI:CHEBI:57287, ChEBI:CHEBI:57292, ChEBI:CHEBI:83100, ChEBI:CHEBI:83120; EC=2.3.1.61; | null | PATHWAY: Carbohydrate metabolism; tricarboxylic acid cycle; succinate from 2-oxoglutarate (transferase route): step 1/2.; PATHWAY: Carbohydrate metabolism; tricarboxylic acid cycle; succinyl-CoA from 2-oxoglutarate (dehydrogenase route): step 1/1. | null | null | FUNCTION: Shows three enzymatic activities that share a first common step, the attack of thiamine-PP on 2-oxoglutarate (alpha-ketoglutarate, KG), leading to the formation of an enamine-thiamine-PP intermediate upon decarboxylation. Thus, displays KGD activity, catalyzing the decarboxylation from five-carbon 2-oxoglutarate to four-carbon succinate semialdehyde (SSA). Also catalyzes C-C bond formation between the activated aldehyde formed after decarboxylation of alpha-ketoglutarate and the carbonyl of glyoxylate (GLX), to yield 2-hydroxy-3-oxoadipate (HOA), which spontaneously decarboxylates to form 5-hydroxylevulinate (HLA). And is also a component of the 2-oxoglutarate dehydrogenase (ODH) complex, that catalyzes the overall conversion of 2-oxoglutarate to succinyl-CoA and CO(2). The KG decarboxylase and KG dehydrogenase reactions provide two alternative, tightly regulated, pathways connecting the oxidative and reductive branches of the TCA cycle (By similarity). {ECO:0000250}. | Mycobacterium sp. (strain KMS) |
A1X148 | CAV2_ECHTE | MGLESEKADVQLFMDDDAYSRHSGVDFVEAEKFSASGPDRDPHRLNSHLQLGFQDVIAEPETTHSFDKVWICSHALFEISKYVLYKFLTFFLAIPLAFAAGILFAILSCLHIWIIMPFVKTCLMVLPSVQTIWKSVTDVVIAPLCTSVGRSFSSVSLQLSQD | null | null | caveola assembly [GO:0070836]; endoplasmic reticulum organization [GO:0007029]; insulin receptor signaling pathway [GO:0008286]; mitochondrion organization [GO:0007005]; negative regulation of endothelial cell proliferation [GO:0001937]; positive regulation of dopamine receptor signaling pathway [GO:0060161]; positive regulation of MAPK cascade [GO:0043410]; regulation of cytosolic calcium ion concentration [GO:0051480]; skeletal muscle fiber development [GO:0048741]; vesicle docking [GO:0048278]; vesicle fusion [GO:0006906] | caveola [GO:0005901]; cytoplasmic vesicle [GO:0031410]; focal adhesion [GO:0005925]; Golgi membrane [GO:0000139]; nucleus [GO:0005634]; perinuclear region of cytoplasm [GO:0048471]; plasma membrane raft [GO:0044853]; sarcolemma [GO:0042383] | D1 dopamine receptor binding [GO:0031748]; molecular adaptor activity [GO:0060090]; protein kinase binding [GO:0019901] | PF01146; | null | Caveolin family | PTM: Phosphorylated on serine and tyrosine residues. CAV1 promotes phosphorylation on Ser-23 which then targets the complex to the plasma membrane, lipid rafts and caveolae. Phosphorylation on Ser-36 appears to modulate mitosis in endothelial cells. Phosphorylation on Tyr-19 is required for insulin-induced phosphorylation of MAPK1 and DNA binding of STAT3. Tyrosine phosphorylation is induced by both EGF and insulin (By similarity). {ECO:0000250}. | SUBCELLULAR LOCATION: Nucleus {ECO:0000250}. Golgi apparatus membrane; Peripheral membrane protein. Cell membrane; Peripheral membrane protein. Membrane, caveola; Peripheral membrane protein. Note=Potential hairpin-like structure in the membrane. Membrane protein of caveolae. Tyr-19-phosphorylated form is enriched at sites of cell-cell contact and is translocated to the nucleus in complex with MAPK1 in response to insulin. CAV1-mediated Ser-23-phosphorylated form locates to the plasma membrane. Ser-36-phosphorylated form resides in intracellular compartments (By similarity). {ECO:0000250}. | null | null | null | null | null | FUNCTION: May act as a scaffolding protein within caveolar membranes. Interacts directly with G-protein alpha subunits and can functionally regulate their activity. Acts as an accessory protein in conjunction with CAV1 in targeting to lipid rafts and driving caveolae formation. The Ser-36 phosphorylated form has a role in modulating mitosis in endothelial cells. Positive regulator of cellular mitogenesis of the MAPK signaling pathway. Required for the insulin-stimulated nuclear translocation and activation of MAPK1 and STAT3, and the subsequent regulation of cell cycle progression (By similarity). {ECO:0000250}. | Echinops telfairi (Lesser hedgehog tenrec) |
A1X149 | CAV1_ECHTE | MSGGKYVDSEGHLYTLPIREQGNIYKPNNKAMAEDMNEKQVYDAHTKEIDLVNRDPKHLNDDVVKIDFEDVIAEPEGTHSFDGIWKASFTTFTVTKYWFYRLLSGIFGIPMALIWGVYFAILSFLHIWAVVPCIKSFLIEIQCISRVYSIYVHTFCDPLFEAIGKIFSNIRISTQKEI | null | null | apoptotic signaling pathway [GO:0097190]; canonical Wnt signaling pathway [GO:0060070]; caveola assembly [GO:0070836]; caveolin-mediated endocytosis [GO:0072584]; cell differentiation [GO:0030154]; cellular response to exogenous dsRNA [GO:0071360]; cellular response to hyperoxia [GO:0071455]; cellular response to misfolded protein [GO:0071218]; negative regulation of anoikis [GO:2000811]; negative regulation of endothelial cell proliferation [GO:0001937]; negative regulation of peptidyl-serine phosphorylation [GO:0033137]; negative regulation of peptidyl-tyrosine autophosphorylation [GO:1900085]; negative regulation of pinocytosis [GO:0048550]; negative regulation of potassium ion transmembrane transport [GO:1901380]; negative regulation of protein ubiquitination [GO:0031397]; positive regulation of canonical NF-kappaB signal transduction [GO:0043123]; positive regulation of cell adhesion molecule production [GO:0060355]; positive regulation of cell migration [GO:0030335]; positive regulation of cholesterol efflux [GO:0010875]; positive regulation of ERAD pathway [GO:1904294]; positive regulation of extrinsic apoptotic signaling pathway [GO:2001238]; positive regulation of intrinsic apoptotic signaling pathway [GO:2001244]; positive regulation of peptidyl-serine phosphorylation [GO:0033138]; positive regulation of protein ubiquitination [GO:0031398]; positive regulation of toll-like receptor 3 signaling pathway [GO:0034141]; receptor internalization [GO:0031623]; receptor-mediated endocytosis of virus by host cell [GO:0019065]; regulation of blood coagulation [GO:0030193]; regulation of cytosolic calcium ion concentration [GO:0051480]; regulation of entry of bacterium into host cell [GO:2000535]; regulation of membrane repolarization during action potential [GO:0098903]; regulation of ruffle assembly [GO:1900027]; response to bacterium [GO:0009617]; response to estrogen [GO:0043627]; response to progesterone [GO:0032570]; T cell costimulation [GO:0031295] | caveola [GO:0005901]; endoplasmic reticulum [GO:0005783]; endosome [GO:0005768]; focal adhesion [GO:0005925]; Golgi membrane [GO:0000139]; membrane raft [GO:0045121]; perinuclear region of cytoplasm [GO:0048471]; protein-containing complex [GO:0032991]; sarcolemma [GO:0042383] | ATPase binding [GO:0051117]; identical protein binding [GO:0042802]; inward rectifier potassium channel inhibitor activity [GO:0070320]; molecular adaptor activity [GO:0060090]; nitric-oxide synthase binding [GO:0050998]; oxysterol binding [GO:0008142]; protein kinase binding [GO:0019901]; protein-containing complex binding [GO:0044877]; signaling receptor binding [GO:0005102]; small GTPase binding [GO:0031267]; transmembrane transporter binding [GO:0044325] | PF01146; | null | Caveolin family | PTM: Phosphorylated at Tyr-14 by ABL1 in response to oxidative stress. {ECO:0000250|UniProtKB:Q03135}.; PTM: Ubiquitinated. Undergo monoubiquitination and multi- and/or polyubiquitination. Monoubiquitination of N-terminal lysines promotes integration in a ternary complex with UBXN6 and VCP which promotes oligomeric CAV1 targeting to lysosomes for degradation. Ubiquitinated by ZNRF1; leading to degradation and modulation of the TLR4-mediated immune response. {ECO:0000250|UniProtKB:Q03135}. | SUBCELLULAR LOCATION: Golgi apparatus membrane {ECO:0000250}; Peripheral membrane protein {ECO:0000250}. Cell membrane {ECO:0000250}; Peripheral membrane protein {ECO:0000250}. Membrane, caveola {ECO:0000250|UniProtKB:P49817}; Peripheral membrane protein {ECO:0000250}. Membrane raft {ECO:0000250|UniProtKB:Q03135}. Note=Colocalized with DPP4 in membrane rafts. Potential hairpin-like structure in the membrane. Membrane protein of caveolae (By similarity). {ECO:0000250}. | null | null | null | null | null | FUNCTION: May act as a scaffolding protein within caveolar membranes. Forms a stable heterooligomeric complex with CAV2 that targets to lipid rafts and drives caveolae formation. Mediates the recruitment of CAVIN proteins (CAVIN1/2/3/4) to the caveolae (By similarity). Interacts directly with G-protein alpha subunits and can functionally regulate their activity (By similarity). Involved in the costimulatory signal essential for T-cell receptor (TCR)-mediated T-cell activation. Its binding to DPP4 induces T-cell proliferation and NF-kappa-B activation in a T-cell receptor/CD3-dependent manner (By similarity). Recruits CTNNB1 to caveolar membranes and may regulate CTNNB1-mediated signaling through the Wnt pathway (By similarity). Negatively regulates TGFB1-mediated activation of SMAD2/3 by mediating the internalization of TGFBR1 from membrane rafts leading to its subsequent degradation (By similarity). Binds 20(S)-hydroxycholesterol (20(S)-OHC) (By similarity). {ECO:0000250|UniProtKB:P49817, ECO:0000250|UniProtKB:Q03135}. | Echinops telfairi (Lesser hedgehog tenrec) |
A1X150 | MET_ECHTE | MKAPAALAPGILVLLLTLVQKGGGECREALAKSEMNVNMRYRLPNFTADTPIQNVVVHEGHVFLGAINSIYVLRERDLQQVSEYKTGPVWEHPDCLPCQACGLAGGQWRENVNMALLVETYYDDQLISCGSVHRGTCQRHVLPRDNPADIQAEVHCMHSPRADEDEASQCPDCVVSALGTKVLLAEKQRFVNFFVGNTLNGSSLPGHALHSISVRRIKETQDGFKFLTDKSYIDVLPEFQASYPIKYIHAFESNRFIYFLTVQRETLDSPSFHTRIIRFCSADSGLRSYMEMPLECILTEKRRKRALRSEVFNVLQAAYVGKPGAQLAKQIGASAHDDILYGVFSQSRPDSAEPTDRSALCAFPVKYVDEFFHRIVNKNNVRCLQHFYGPNHLHCFNRTLLRNSSGCEVRSDEYRTEFTTALQRIDLSAGHFSQVLLTSISTFIKGDLTIANLGTSEGRFMQVVVSRSGSWTPHVDFRLDSHAVSPEVIVEHPVNQNGYTLVVTGKKITKIPLDGLGCEHFQSCSQCLSAPPFVQCGWCHDKCARAEDCPNGTWTQEICLPTIYEVFPASAPLEGGTTLTVCGWDFGFRRNNKSDFKRTRVLIGNESCPLTLSESTPNMLKCTVGPAMSEHSNLSIIISNVRGTAPQYRTFSYVDPEITSISPSYGPKAGGTLVTLTGKYLNSGNSRHISIGGKTCTLKSVSDSVLECYTPAQSISADFPVKLKIDLANREAYSFSYQENPLVVEIHPTKSFVSGGSTITVVGKNLNSVSVPRMIINVHEVEMNFTVACQQRSNSELICCTTPSLQQLDLQLPLKATAFFMLDGIHSRDFDLIYVPNPVFKLFEKPVMISMGNENVLEIKGNDIDPEAVKGEVLKVGNKSCENIHSYPESVLCTVPNDLLKLNSELNIEWKQAVSSTVLGKVIVQPDQNFTGLIVGVVSISVILLSSLGLFLWLKKRKQIKDLGSELVCYDARVHTPHLDRLVSARSVSPTTEMVSNESVDYRATFPEDQFPNSSQNGSCRQVQYPLPDLSPILTSGDSDISSPLLQNTVHIDLSALNPELVQAVQHVVIGPSSLIVHFNEVIGRGHFGCVYHGTLLDNDDRKIHCAVKSLNRITDIGEVSQFLTEGIIMKDFSHPNVLSLLGICLRSEGSPLVVLPYMKHGDLRNFIRNETHSPTVKDLIGFGLQVAKGMKYLASKKFVHRDLAARNCMLDGKFTVKVADFGLARDMYDKEYYSVHNKTGAKLPVKWMALESLQTQKFTTKSDVWSFGVLLWELMTRGAPPYPDVNTFDITVYLLQGRRLLQPEYCPDPLYEVMLKCWHPKAEMRPSFTELVSRISAIFSTFIGEHYVHVNATYVNVKCVAPYPSLLSSHDTVDGEVDT | 2.7.10.1 | null | phosphorylation [GO:0016310]; positive chemotaxis [GO:0050918]; positive regulation of endothelial cell chemotaxis [GO:2001028]; semaphorin-plexin signaling pathway [GO:0071526]; semaphorin-plexin signaling pathway involved in axon guidance [GO:1902287]; transmembrane receptor protein tyrosine kinase signaling pathway [GO:0007169] | membrane [GO:0016020]; semaphorin receptor complex [GO:0002116] | ATP binding [GO:0005524]; semaphorin receptor activity [GO:0017154]; transmembrane receptor protein tyrosine kinase activity [GO:0004714] | PF07714;PF01437;PF01403;PF01833; | 2.60.40.10;1.10.510.10;2.130.10.10; | Protein kinase superfamily, Tyr protein kinase family | PTM: Autophosphorylated in response to ligand binding on Tyr-1233 and Tyr-1234 in the kinase domain leading to further phosphorylation of Tyr-1348 and Tyr-1355 in the C-terminal multifunctional docking site. Dephosphorylated by PTPRJ at Tyr-1348 and Tyr-1364. Dephosphorylated by PTPN1 and PTPN2 (By similarity). {ECO:0000250|UniProtKB:P08581}.; PTM: Ubiquitinated. Ubiquitination by CBL regulates the receptor stability and activity through proteasomal degradation (By similarity). {ECO:0000250|UniProtKB:P08581}.; PTM: O-mannosylation of IPT/TIG domains by TMEM260 is required for protein maturation. O-mannosylated residues are composed of single mannose glycans that are not elongated or modified. {ECO:0000250|UniProtKB:P08581}. | SUBCELLULAR LOCATION: Membrane {ECO:0000250}; Single-pass type I membrane protein {ECO:0000250}. | 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 kinase that transduces signals from the extracellular matrix into the cytoplasm by binding to hepatocyte growth factor/HGF ligand. Regulates many physiological processes including proliferation, scattering, morphogenesis and survival. Ligand binding at the cell surface induces autophosphorylation of MET on its intracellular domain that provides docking sites for downstream signaling molecules. Following activation by ligand, interacts with the PI3-kinase subunit PIK3R1, PLCG1, SRC, GRB2, STAT3 or the adapter GAB1. Recruitment of these downstream effectors by MET leads to the activation of several signaling cascades including the RAS-ERK, PI3 kinase-AKT, or PLCgamma-PKC. The RAS-ERK activation is associated with the morphogenetic effects while PI3K/AKT coordinates prosurvival effects. During embryonic development, MET signaling plays a role in gastrulation, development and migration of muscles and neuronal precursors, angiogenesis and kidney formation. In adults, participates in wound healing as well as organ regeneration and tissue remodeling. Promotes also differentiation and proliferation of hematopoietic cells (By similarity). {ECO:0000250}. | Echinops telfairi (Lesser hedgehog tenrec) |
A1X283 | SPD2B_HUMAN | MPPRRSIVEVKVLDVQKRRVPNKHYVYIIRVTWSSGSTEAIYRRYSKFFDLQMQMLDKFPMEGGQKDPKQRIIPFLPGKILFRRSHIRDVAVKRLIPIDEYCKALIQLPPYISQCDEVLQFFETRPEDLNPPKEEHIGKKKSGGDQTSVDPMVLEQYVVVANYQKQESSEISLSVGQVVDIIEKNESGWWFVSTAEEQGWVPATCLEGQDGVQDEFSLQPEEEEKYTVIYPYTARDQDEMNLERGAVVEVIQKNLEGWWKIRYQGKEGWAPASYLKKNSGEPLPPKPGPGSPSHPGALDLDGVSRQQNAVGREKELLSSQRDGRFEGRPVPDGDAKQRSPKMRQRPPPRRDMTIPRGLNLPKPPIPPQVEEEYYTIAEFQTTIPDGISFQAGLKVEVIEKNLSGWWYIQIEDKEGWAPATFIDKYKKTSNASRPNFLAPLPHEVTQLRLGEAAALENNTGSEATGPSRPLPDAPHGVMDSGLPWSKDWKGSKDVLRKASSDMSASAGYEEISDPDMEEKPSLPPRKESIIKSEGELLERERERQRTEQLRGPTPKPPGVILPMMPAKHIPPARDSRRPEPKPDKSRLFQLKNDMGLECGHKVLAKEVKKPNLRPISKSKTDLPEEKPDATPQNPFLKSRPQVRPKPAPSPKTEPPQGEDQVDICNLRSKLRPAKSQDKSLLDGEGPQAVGGQDVAFSRSFLPGEGPGRAQDRTGKQDGLSPKEISCRAPPRPAKTTDPVSKSVPVPLQEAPQQRPVVPPRRPPPPKKTSSSSRPLPEVRGPQCEGHESRAAPTPGRALLVPPKAKPFLSNSLGGQDDTRGKGSLGPWGTGKIGENREKAAAASVPNADGLKDSLYVAVADFEGDKDTSSFQEGTVFEVREKNSSGWWFCQVLSGAPSWEGWIPSNYLRKKP | null | null | adipose tissue development [GO:0060612]; bone development [GO:0060348]; cell differentiation [GO:0030154]; extracellular matrix disassembly [GO:0022617]; eye development [GO:0001654]; heart development [GO:0007507]; podosome assembly [GO:0071800]; protein localization to membrane [GO:0072657]; skeletal system development [GO:0001501]; superoxide anion generation [GO:0042554]; superoxide metabolic process [GO:0006801] | anchoring junction [GO:0070161]; cell projection [GO:0042995]; cytoplasm [GO:0005737]; podosome [GO:0002102] | phosphatidylinositol-3,5-bisphosphate binding [GO:0080025]; phosphatidylinositol-3-phosphate binding [GO:0032266]; phosphatidylinositol-5-phosphate binding [GO:0010314]; SH2 domain binding [GO:0042169]; superoxide-generating NADPH oxidase activator activity [GO:0016176] | PF00787;PF00018;PF07653; | 3.30.1520.10;2.30.30.40; | SH3PXD2 family | PTM: Phosphorylated in SRC-transformed cells. {ECO:0000250}. | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Cell projection, podosome {ECO:0000250}. Note=Cytoplasmic in normal cells and localizes to podosomes in SRC-transformed cells. {ECO:0000250}. | null | null | null | null | null | FUNCTION: Adapter protein involved in invadopodia and podosome formation and extracellular matrix degradation. Binds matrix metalloproteinases (ADAMs), NADPH oxidases (NOXs) and phosphoinositides. Acts as an organizer protein that allows NOX1- or NOX3-dependent reactive oxygen species (ROS) generation and ROS localization. Plays a role in mitotic clonal expansion during the immediate early stage of adipocyte differentiation (By similarity). {ECO:0000250, ECO:0000269|PubMed:12615925, ECO:0000269|PubMed:19755710, ECO:0000269|PubMed:20609497}. | Homo sapiens (Human) |
A1XBS5 | CBAR1_HUMAN | MMRRTLENRNAQTKQLQTAVSNVEKHFGELCQIFAAYVRKTARLRDKADLLVNEINAYAATETPHLKLGLMNFADEFAKLQDYRQAEVERLEAKVVEPLKTYGTIVKMKRDDLKATLTARNREAKQLTQLERTRQRNPSDRHVISQAETELQRAAMDASRTSRHLEETINNFERQKMKDIKTIFSEFITIEMLFHGKALEVYTAAYQNIQNIDEDEDLEVFRNSLYAPDYSSRLDIVRANSKSPLQRSLSAKCVSGTGQVSTCRLRKDQQAEDDEDDELDVTEEENFLK | null | null | cilium assembly [GO:0060271]; inner mitochondrial membrane organization [GO:0007007]; limb morphogenesis [GO:0035108]; membrane organization [GO:0061024]; membrane tubulation [GO:0097749]; positive regulation of smoothened signaling pathway [GO:0045880] | centriole [GO:0005814]; ciliary basal body [GO:0036064]; ciliary base [GO:0097546]; ciliary transition zone [GO:0035869]; cytoplasm [GO:0005737]; mitochondrial crista [GO:0030061]; mitochondrial inner membrane [GO:0005743]; mitochondrion [GO:0005739]; nucleus [GO:0005634] | phospholipid binding [GO:0005543] | PF06730; | 1.20.1270.60; | CIBAR family | null | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:27528616, ECO:0000269|PubMed:30404948}. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome, centriole {ECO:0000269|PubMed:27528616}. Cytoplasm, cytoskeleton, cilium basal body {ECO:0000269|PubMed:27528616, ECO:0000269|PubMed:30395363}. Cell projection, cilium {ECO:0000250|UniProtKB:Q8BP22}. Nucleus {ECO:0000269|PubMed:30404948}. Mitochondrion inner membrane {ECO:0000269|PubMed:30404948}; Peripheral membrane protein {ECO:0000269|PubMed:30404948}; Matrix side {ECO:0000269|PubMed:30404948}. Note=Weak punctate vesicular distribution throughout the cytoplasm (PubMed:27528616). Localizes at the distal end of mother centrioles (PubMed:27528616). Extensive colocalization with CBY1 at mother centrioles (PubMed:27528616). {ECO:0000269|PubMed:27528616}.; SUBCELLULAR LOCATION: [Isoform 3]: Nucleus {ECO:0000269|PubMed:17646714}. | null | null | null | null | null | FUNCTION: Acts as a positive regulator of ciliary hedgehog signaling (By similarity). Probable regulator of ciliogenesis involved in limb morphogenesis (PubMed:27528616, PubMed:30395363). In cooperation with CBY1 it is involved in the recruitment and fusion of endosomal vesicles at distal appendages during early stages of ciliogenesis (PubMed:27528616, PubMed:30395363). Plays an important role in the mitochondrial function and is essential for maintaining mitochondrial morphology and inner membrane ultrastructure (PubMed:30404948). In vitro, can generate membrane curvature through preferential interaction with negatively charged phospholipids such as phosphatidylinositol 4,5-bisphosphate and cardiolipin and hence orchestrate cristae shape (PubMed:30404948). {ECO:0000250|UniProtKB:Q8BP22, ECO:0000269|PubMed:27528616, ECO:0000269|PubMed:30395363, ECO:0000269|PubMed:30404948}. | Homo sapiens (Human) |
A1XGB4 | PIMP1_CAPAN | MTPPPTSTVPPYVSLIVRILTLICLLISFIVIATNNQTVSTVAGDVKIKFKDFYAYRYLIATVIIGMAYTLLQIAFSISLLTTGNRIGGEGFLLFDFYGDKFISYFLVTGAAASFGMTQDLKQLEGSDNYSKFLNTSNAAASLCLIGFFFAVASSIFSSYNLPKRI | null | null | defense response to bacterium [GO:0042742]; defense response to oomycetes [GO:0002229]; response to abscisic acid [GO:0009737]; response to bacterium [GO:0009617]; response to cold [GO:0009409]; response to ethylene [GO:0009723]; response to jasmonic acid [GO:0009753]; response to salt stress [GO:0009651]; response to wounding [GO:0009611] | plasma membrane [GO:0005886] | null | PF04535; | null | Casparian strip membrane proteins (CASP) family | null | SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:18506481}; Multi-pass membrane protein {ECO:0000269|PubMed:18506481}. | null | null | null | null | null | FUNCTION: Required for defense response to Xanthomonas campestris pv. vesicatoria (Xcv). In heterologous systems, confers resistance to bacterial pathogens such as Pseudomonas syringae pv. tomato but susceptibility to pathogenic oomycetes such as Hylaloperonospora parasitica when expressed in Arabidopsis thaliana. May be involved in the regulation of responses to bitoic and abiotic stresses. {ECO:0000269|PubMed:18506481, ECO:0000269|PubMed:18936963}. | Capsicum annuum (Capsicum pepper) |
A1XLE2 | TFP_LEPSV | MALTLQGEWIKIEQKGGPAPGPRSSHCMAVVGDKLYMFGGELKPQFHLDKHLYVFDFKTNTWSIAEPKGEAPSLSCLGVRMVAVGTKIYIFGGRDENRNYSDFYSYDTVKKEWKFLTKLDEERVPEARSFPAIAADDNHVYIFGGVSKGGVQSTPFRFKSTIVYNIAEGTWSQLPNPGPDFEPRGGAGLAVIDKKLWVVCGFANSTSGGINDYNSNKVQYYDLVSGKWIEVKTSGVKPSGRSVFAYAVIGKQIVIYGGEIFRDENGHLGPGTMSNEGYALDTETLVWEKLVDGGEPMTPLGWTANCTGTVYGKTGLLMHGGKQPFNNRTDDFYFYSF | 4.8.1.7; 4.8.1.8 | COFACTOR: Name=Fe(2+); Xref=ChEBI:CHEBI:29033; Evidence={ECO:0000269|PubMed:17139450}; | glucosinolate metabolic process [GO:0019760]; nitrile biosynthetic process [GO:0080028]; thiocyanate metabolic process [GO:0018969] | cytosol [GO:0005829]; nucleus [GO:0005634] | enzyme regulator activity [GO:0030234]; lyase activity [GO:0016829]; metal ion binding [GO:0046872] | PF01344;PF13418;PF13964; | 2.120.10.80; | null | null | null | CATALYTIC ACTIVITY: Reaction=(Z)-phenyl-N-(sulfonatooxy)methanimidothioate = benzyl thiocyanate + sulfate; Xref=Rhea:RHEA:69312, ChEBI:CHEBI:16017, ChEBI:CHEBI:16189, ChEBI:CHEBI:183061; EC=4.8.1.7; Evidence={ECO:0000269|PubMed:17139450}; CATALYTIC ACTIVITY: Reaction=(Z)-phenyl-N-(sulfonatooxy)methanimidothioate = phenylacetonitrile + sulfate + sulfur; Xref=Rhea:RHEA:69308, ChEBI:CHEBI:16189, ChEBI:CHEBI:25979, ChEBI:CHEBI:26833, ChEBI:CHEBI:183061; Evidence={ECO:0000269|PubMed:17139450}; CATALYTIC ACTIVITY: Reaction=(Z)-N-(sulfonatooxy)prop-2-enimidothioate = 2-(thiiran-2-yl)acetonitrile + sulfate; Xref=Rhea:RHEA:69252, ChEBI:CHEBI:16189, ChEBI:CHEBI:183062, ChEBI:CHEBI:183064; EC=4.8.1.8; Evidence={ECO:0000269|PubMed:17139450}; CATALYTIC ACTIVITY: Reaction=(Z)-4-methylsulfanylbutyl-N-(sulfonatooxy)methanimidothioate = 5-(methylsulfanyl)pentanenitrile + H(+) + sulfate + sulfur; Xref=Rhea:RHEA:69328, ChEBI:CHEBI:15378, ChEBI:CHEBI:16189, ChEBI:CHEBI:26833, ChEBI:CHEBI:183222, ChEBI:CHEBI:183223; Evidence={ECO:0000269|PubMed:17139450}; | null | null | BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 9.5. {ECO:0000269|PubMed:17139450}; | null | FUNCTION: Specifier protein that contributes to constitutive and herbivore-induced simple nitrile formation (By similarity). Catalyzes thiocyanate and simple nitrile formation from benzylglucosinolate in the presence of myrosinase (PubMed:17139450, PubMed:23999604). Converts also aliphatic glucosinolates to both epithionitriles and simple nitriles (PubMed:17139450). {ECO:0000250|UniProtKB:Q93XW5, ECO:0000269|PubMed:17139450, ECO:0000269|PubMed:23999604}. | Lepidium sativum (Garden cress) |
A1XRN2 | PLIA_ATRNM | MRLILLSGLLLLGTFLANGDEKDSDVQMLNSMIEAVMILQRDFANLRHALMTVHNARSFGRGSERLYVTNKEVSKFEGLEEICSQAGGHIPSPQLENQNKAFEDVLERHNKAAYLVVGDSANFTNWAAGQPNEADGTCVKADTHGSWHSASCDDNLLVVCEFYFIL | null | null | null | extracellular region [GO:0005576] | carbohydrate binding [GO:0030246]; phospholipase A2 inhibitor activity [GO:0019834] | PF00059; | 3.10.100.10; | Alpha-type phospholipase A2 inhibitor family | PTM: N-glycosylated. {ECO:0000269|PubMed:17071122}. | SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:17071122}. Note=Secreted in plasma. {ECO:0000269|PubMed:17071122}. | null | null | null | null | null | FUNCTION: This phospholipase A2 inhibitor neutralizes the activity of basic PLA2 myotoxins of its own and related venoms. The inhibitory profile shows specificity towards group II PLA2, either belonging to the catalytically-active (D49) or -inactive (K49) subtypes. | Atropoides nummifer (Jumping pit viper) (Porthidium nummifer) |
A1XSY8 | EGR2_PIG | MMTAKAVDKIPVTLSGFVHQLSDNIYPVEDLAATSVTIFPNAELGSPFDQMNGVAGDGMINIDMTGEKRSLDLPYPSSFAPVSAPRNQTFTYMGKFSIDPQYPGASCYPEGIINIVSAGILQGVTSPASTTASSNVTSASPNPLATGPLGVCTMSQTQPDLDHLYSPPPPPPYSGCAGDLYQDPSAFLSAATTSTSSSLAYPPPPSYPSPKPATDPGLFPMIPDYPGFFPSQCQRDLHGTAGPDRKPFPCPLDSLRVPPPLTPLSTIRNFTLGGPSAGTTGPGASGGSEGPRLPGSSAAAAAAAYNPHHLPLRPILRPRKYPNRPSKTPVHERPYPCPAEGCDRRFSRSDELTRHIRIHTGHKPFQCRICMRNFSRSDHLTTHIRTHTGEKPFACDYCGRKFARSDERKRHTKIHLRQKERKSSAPSSSVPAASTASCTGGAQPGGPLCSSNSSTIGGGSLGPCSSRTRTP | 2.3.2.- | null | facial nerve structural organization [GO:0021612]; positive regulation of DNA-templated transcription [GO:0045893]; positive regulation of myelination [GO:0031643]; positive regulation of Schwann cell differentiation [GO:0014040]; positive regulation of transcription by RNA polymerase II [GO:0045944]; protein export from nucleus [GO:0006611]; protein sumoylation [GO:0016925]; regulation of transcription by RNA polymerase II [GO:0006357]; rhombomere 3 structural organization [GO:0021659]; rhombomere 5 structural organization [GO:0021665]; Schwann cell differentiation [GO:0014037]; skeletal muscle cell differentiation [GO:0035914] | cytoplasm [GO:0005737]; nucleus [GO:0005634] | chromatin binding [GO:0003682]; DNA-binding transcription factor activity [GO:0003700]; DNA-binding transcription factor activity, RNA polymerase II-specific [GO:0000981]; metal ion binding [GO:0046872]; RNA polymerase II cis-regulatory region sequence-specific DNA binding [GO:0000978]; sequence-specific DNA binding [GO:0043565]; transcription cis-regulatory region binding [GO:0000976]; transferase activity [GO:0016740] | PF11928;PF00096; | 3.30.160.60; | EGR C2H2-type zinc-finger protein family | PTM: Ubiquitinated by WWP2 leading to proteasomal degradation. {ECO:0000250|UniProtKB:P08152}.; PTM: Acetylated at Lys-246. May be deacetylated by HDAC6, HDAC10 or SIRT1. {ECO:0000250|UniProtKB:P08152}. | SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:P08152}. | null | null | PATHWAY: Protein modification; protein sumoylation. | null | null | FUNCTION: Sequence-specific DNA-binding transcription factor (By similarity). Plays a role in hindbrain segmentation by regulating the expression of a subset of homeobox containing genes and in Schwann cell myelination by regulating the expression of genes involved in the formation and maintenance of myelin (By similarity). Binds to two EGR2-consensus sites EGR2A (5'-CTGTAGGAG-3') and EGR2B (5'-ATGTAGGTG-3') in the HOXB3 enhancer and promotes HOXB3 transcriptional activation (By similarity). Binds to specific DNA sites located in the promoter region of HOXA4, HOXB2 and ERBB2 (By similarity). Regulates hindbrain segmentation by controlling the expression of Hox genes, such as HOXA4, HOXB3 and HOXB2, and thereby specifying odd and even rhombomeres (By similarity). Promotes the expression of HOXB3 in the rhombomere r5 in the hindbrain (By similarity). Regulates myelination in the peripheral nervous system after birth, possibly by regulating the expression of myelin proteins, such as MPZ, and by promoting the differentiation of Schwann cells (By similarity). Involved in the development of the jaw openener musculature, probably by playing a role in its innervation through trigeminal motor neurons (By similarity). May play a role in adipogenesis, possibly by regulating the expression of CEBPB (By similarity). {ECO:0000250|UniProtKB:P08152}.; FUNCTION: E3 SUMO-protein ligase helping SUMO1 conjugation to its coregulators NAB1 and NAB2, whose sumoylation down-regulates EGR2 transcriptional activity. {ECO:0000250|UniProtKB:P11161}. | Sus scrofa (Pig) |
A1XWY7 | CFAT_PETHY | MGNTDFHVTVKKKEVVAAVLPMHHEHWLPMSNLDLLLPPLDFGVFFCYKRSKINNDTKDDDETIKKALAETLVSFYALAGEVVFNSLGEPELLCNNRGVDFFHAYADIELNNLDLYHPDVSVHEKLIPIKKHGVLSVQVTGLKCGGIVVGCTFDHRVADAYSANMFLVAWAAIARKDNNINTVIPSFRRSLLNPRRPPQFDDSFIDSTYVFLSSPPKQPNDVLTSRVYYINSQEINLLQSQATRNGSKRSKLECFSAFLWKTIAEGGIDDSKRCKLGIVVDGRQRLRHDSSTTMKNYFGNVLSVPYTEASVGQLKQTPLGKVADLVHTCLDNVANEHHFPSLIDWVELHRPRQAIVKVYCKDECNDEAAIVVSSGLRFPLSQVNFGWGCPDFGSYIFPWGGQTGYVMPMPSPNKNGDWIVYMHLQKKHLDLVETRAPHIFHPLTACYLDLTATY | 2.3.1.-; 2.3.1.224 | null | circadian rhythm [GO:0007623]; green leaf volatile biosynthetic process [GO:0010597]; phenylpropanoid biosynthetic process [GO:0009699]; response to ethylene [GO:0009723] | null | 2-phenylethanol acetyltransferase activity [GO:0102387]; acetyl-coenzyme A:acetyl alcohol acetyltransferase activity [GO:0102720]; alcohol O-acyltransferase activity [GO:0034318] | PF02458; | 3.30.559.10; | Plant acyltransferase family | null | null | CATALYTIC ACTIVITY: Reaction=(E)-coniferol + acetyl-CoA = (E)-coniferyl acetate + CoA; Xref=Rhea:RHEA:64616, ChEBI:CHEBI:17745, ChEBI:CHEBI:47905, ChEBI:CHEBI:57287, ChEBI:CHEBI:57288; Evidence={ECO:0000269|PubMed:17241449}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:64617; Evidence={ECO:0000269|PubMed:17241449}; CATALYTIC ACTIVITY: Reaction=(E)-cinnamyl alcohol + acetyl-CoA = (E)-cinnamyl acetate + CoA; Xref=Rhea:RHEA:36151, ChEBI:CHEBI:33227, ChEBI:CHEBI:57287, ChEBI:CHEBI:57288, ChEBI:CHEBI:156069; EC=2.3.1.224; Evidence={ECO:0000269|PubMed:17241449}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:36152; Evidence={ECO:0000269|PubMed:17241449}; CATALYTIC ACTIVITY: Reaction=(2E)-geraniol + acetyl-CoA = (2E)-geranyl acetate + CoA; Xref=Rhea:RHEA:64624, ChEBI:CHEBI:5331, ChEBI:CHEBI:17447, ChEBI:CHEBI:57287, ChEBI:CHEBI:57288; Evidence={ECO:0000269|PubMed:17241449}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:64625; Evidence={ECO:0000269|PubMed:17241449}; CATALYTIC ACTIVITY: Reaction=acetyl-CoA + octan-1-ol = CoA + octyl acetate; Xref=Rhea:RHEA:64628, ChEBI:CHEBI:16188, ChEBI:CHEBI:57287, ChEBI:CHEBI:57288, ChEBI:CHEBI:87495; Evidence={ECO:0000269|PubMed:17241449}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:64629; Evidence={ECO:0000269|PubMed:17241449}; CATALYTIC ACTIVITY: Reaction=(E)-sinapyl alcohol + acetyl-CoA = (E)-sinapoyl actetate + CoA; Xref=Rhea:RHEA:64620, ChEBI:CHEBI:57287, ChEBI:CHEBI:57288, ChEBI:CHEBI:64557, ChEBI:CHEBI:156067; Evidence={ECO:0000269|PubMed:17241449}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:64621; Evidence={ECO:0000269|PubMed:17241449}; | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=56.5 uM for coniferyl alcohol (in the presence of acetyl CoA and at pH 6) {ECO:0000269|PubMed:17241449}; KM=30.6 uM for acetyl CoA (in the presence of coniferyl alcohol and at pH 6) {ECO:0000269|PubMed:17241449}; KM=27.5 uM for coniferyl alcohol (in the presence of acetyl CoA and at pH 7.5) {ECO:0000269|PubMed:17241449}; KM=44.1 uM for acetyl CoA (in the presence of coniferyl alcohol and at pH 7.5) {ECO:0000269|PubMed:17241449}; KM=4500 uM for benzyl alcohol (in the presence of acetyl CoA and at pH 7.5) {ECO:0000269|PubMed:17241449}; KM=22.6 uM for acetyl CoA (in the presence of benzyl alcohol and at pH 7.5) {ECO:0000269|PubMed:17241449}; KM=3600 uM for 2-phenyl ethanol (in the presence of acetyl CoA and at pH 7.5) {ECO:0000269|PubMed:17241449}; KM=45.1 uM for acetyl CoA (in the presence of 2-phenyl ethanol and at pH 7.5) {ECO:0000269|PubMed:17241449}; Vmax=40.1 nmol/sec/mg enzyme with coniferyl alcohol as substrate (in the presence of acetyl CoA and at pH 6) {ECO:0000269|PubMed:17241449}; Vmax=45.3 nmol/sec/mg enzyme with acetyl CoA as substrate (in the presence of coniferyl alcohol and at pH 6) {ECO:0000269|PubMed:17241449}; Vmax=15.9 nmol/sec/mg enzyme with coniferyl alcohol as substrate (in the presence of acetyl CoA and at pH 7.5) {ECO:0000269|PubMed:17241449}; Vmax=29.5 nmol/sec/mg enzyme with acetyl CoA as substrate (in the presence of coniferyl alcohol and at pH 7.5) {ECO:0000269|PubMed:17241449}; Vmax=16 nmol/sec/mg enzyme with benzyl alcohol as substrate (in the presence of acetyl CoA and at pH 7.5) {ECO:0000269|PubMed:17241449}; Vmax=22.1 nmol/sec/mg enzyme with acetyl CoA as substrate (in the presence of benzyl alcohol and at pH 7.5) {ECO:0000269|PubMed:17241449}; Vmax=17.8 nmol/sec/mg enzyme with 2-phenyl ethanol as substrate (in the presence of acetyl CoA and at pH 7.5) {ECO:0000269|PubMed:17241449}; Vmax=18.3 nmol/sec/mg enzyme with acetyl CoA as substrate (in the presence of 2-phenyl ethanol and at pH 7.5) {ECO:0000269|PubMed:17241449}; Note=kcat is 2.05 sec(-1) with coniferyl alcohol as substrate (in the presence of acetyl CoA and at pH 6) (PubMed:17241449). kcat is 2.32 sec(-1) with acetyl CoA as substrate (in the presence of coniferyl alcohol and at pH 6) (PubMed:17241449). kcat is 0.81 sec(-1) with coniferyl alcohol as substrate (in the presence of acetyl CoA and at pH 7.5) (PubMed:17241449). kcat is 1.51 sec(-1) with acetyl CoA as substrate (in the presence of coniferyl alcohol and at pH 7.5) (PubMed:17241449). kcat is 0.82 sec(-1) with benzyl alcohol as substrate (in the presence of acetyl CoA and at pH 7.5) (PubMed:17241449). kcat is 1.13 sec(-1) with acetyl CoA as substrate (in the presence of benzyl alcohol and at pH 7.5) (PubMed:17241449). kcat is 0.91 sec(-1) with 2-phenyl ethanol as substrate (in the presence of acetyl CoA and at pH 7.5) (PubMed:17241449). kcat is 0.93 sec(-1) with acetyl CoA as substrate (in the presence of 2-phenyl ethanol and at pH 7.5) (PubMed:17241449). {ECO:0000269|PubMed:17241449}; | PATHWAY: Aromatic compound metabolism; phenylpropanoid biosynthesis. {ECO:0000269|PubMed:17241449}. | BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 6. Larger substrate spectrum at pH 7.5, with a lower activity, thought. {ECO:0000269|PubMed:17241449}; | null | FUNCTION: Acyltransferase involved in the biosynthesis of the floral volatile isoeugenol, and which promotes the formation of phenylacetaldehyde, phenylethyl alcohol, phenyl-ethyl acetate, phenylethyl benzoate and benzyl acetate (PubMed:17241449). Catalyzes the acetylation of coniferyl alcohol to produce coniferyl acetate (PubMed:17241449). Also active toward 1-octanol, cinnamyl alcohol, geraniol and sinapyl alcohol (PubMed:17241449). {ECO:0000269|PubMed:17241449}. | Petunia hybrida (Petunia) |
A1Y2K1 | FYN_PIG | MGCVQCKDKEATKLTEERDGSLNQSSGFRYGTDPTPQHYPSFGVTSIPNYNNFHAAGGQGLTVFGGVSSSSHTGTLRTRGGTGVTLFVALYDYEARTEDDLSFHKGEKFQILNSSEGDWWEARSLTTGETGYIPSNYVAPVDSIQAEEWYFGKLGRKDAERQLLSFGNPRGTFLIRESETTKGAYSLSIRDWDDMKGDHVKHYKIRKLDNGGYYITTRAQFETLQQLVQHYSERAAGLCCRLVVPCHKGMPRLTDLSVKTKDVWEIPRESLQLIKRLGNGQFGEVWMGTWNGNTKVAIKTLKPGTMSPESFLEEAQIMKKLKHDKLVQLYAVVSEEPIYIVTEYMNKGSLLDFLKDGEGRALKLPNLVDMAAQVAAGMAYIERMNYIHRDLRSANILVGNGLICKIADFGLARLIEDNEYTARQGAKFPIKWTAPEAALYGRFTIKSDVWSFGILLTELVTKGRVPYPGMNNREVLEQVERGYRMPCPQDCPISLHELMIHCWKKDPEERPTFEYLQGFLEDYFTATEPQYQPGENL | 2.7.10.2 | COFACTOR: Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000250|UniProtKB:P06241}; | adaptive immune response [GO:0002250]; cell differentiation [GO:0030154]; innate immune response [GO:0045087]; peptidyl-tyrosine phosphorylation [GO:0018108]; T cell receptor signaling pathway [GO:0050852]; transmembrane receptor protein tyrosine kinase signaling pathway [GO:0007169] | cytoplasm [GO:0005737]; extrinsic component of cytoplasmic side of plasma membrane [GO:0031234]; nucleus [GO:0005634]; perikaryon [GO:0043204] | ATP binding [GO:0005524]; metal ion binding [GO:0046872]; non-membrane spanning protein tyrosine kinase activity [GO:0004715]; protein tyrosine kinase activity [GO:0004713]; signaling receptor binding [GO:0005102] | PF07714;PF00017;PF00018; | 3.30.505.10;2.30.30.40;1.10.510.10; | Protein kinase superfamily, Tyr protein kinase family, SRC subfamily | PTM: Autophosphorylated at Tyr-420 (By similarity). Phosphorylation on the C-terminal tail at Tyr-531 by CSK maintains the enzyme in an inactive state. PTPRC/CD45 dephosphorylates Tyr-531 leading to activation. Ultraviolet B (UVB) strongly increase phosphorylation at Thr-12 and kinase activity, and promotes translocation from the cytoplasm to the nucleus. Dephosphorylation at Tyr-420 by PTPN2 negatively regulates T-cell receptor signaling (By similarity). Phosphorylated at tyrosine residues, which can be enhanced by NTN1 (By similarity). {ECO:0000250|UniProtKB:P06241, ECO:0000250|UniProtKB:P39688}.; PTM: Palmitoylated. Palmitoylation at Cys-3 and Cys-6, probably by ZDHHC21, regulates subcellular location. {ECO:0000250|UniProtKB:P39688}. | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:P06241}. Nucleus {ECO:0000250|UniProtKB:P06241}. Cell membrane {ECO:0000250|UniProtKB:P06241}. Perikaryon {ECO:0000250|UniProtKB:Q62844}. Note=Present and active in lipid rafts (By similarity). Palmitoylation is crucial for proper trafficking (By similarity). {ECO:0000250|UniProtKB:P06241}. | 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=2.7.10.2; Evidence={ECO:0000250|UniProtKB:P06241, ECO:0000255|PROSITE-ProRule:PRU10028}; | null | null | null | null | FUNCTION: Non-receptor tyrosine-protein kinase that plays a role in many biological processes including regulation of cell growth and survival, cell adhesion, integrin-mediated signaling, cytoskeletal remodeling, cell motility, immune response and axon guidance. Inactive FYN is phosphorylated on its C-terminal tail within the catalytic domain. Following activation by PKA, the protein subsequently associates with PTK2/FAK1, allowing PTK2/FAK1 phosphorylation, activation and targeting to focal adhesions. Involved in the regulation of cell adhesion and motility through phosphorylation of CTNNB1 (beta-catenin) and CTNND1 (delta-catenin). Regulates cytoskeletal remodeling by phosphorylating several proteins including the actin regulator WAS and the microtubule-associated proteins MAP2 and MAPT. Promotes cell survival by phosphorylating AGAP2/PIKE-A and preventing its apoptotic cleavage. Participates in signal transduction pathways that regulate the integrity of the glomerular slit diaphragm (an essential part of the glomerular filter of the kidney) by phosphorylating several slit diaphragm components including NPHS1, KIRREL1 and TRPC6. Plays a role in neural processes by phosphorylating DPYSL2, a multifunctional adapter protein within the central nervous system, ARHGAP32, a regulator for Rho family GTPases implicated in various neural functions, and SNCA, a small pre-synaptic protein. Participates in the downstream signaling pathways that lead to T-cell differentiation and proliferation following T-cell receptor (TCR) stimulation. Phosphorylates PTK2B/PYK2 in response to T-cell receptor activation. Also participates in negative feedback regulation of TCR signaling through phosphorylation of PAG1, thereby promoting interaction between PAG1 and CSK and recruitment of CSK to lipid rafts. CSK maintains LCK and FYN in an inactive form. Promotes CD28-induced phosphorylation of VAV1. In mast cells, phosphorylates CLNK after activation of immunoglobulin epsilon receptor signaling (By similarity). {ECO:0000250|UniProtKB:P06241, ECO:0000250|UniProtKB:P39688}. | Sus scrofa (Pig) |
A1Y9I9 | TOMT_MOUSE | MSPAIALAFLPLVVTLLVRYRHHFRLLVRTVLLRGFRDCLSGLRIEERAFSYVLTHALPGDPGHILTTLDHWSSCCEYLSHMGPVKGQILMRLVEEKAPACVLELGTYCGYSTLLIARALPPGSRLLTVERDSRTAAVAEKVIRLAGFDEQMVELIAGSSEEVIPRLRAQHQLNRADLVLLAHRPRYYLRDLQLLEAHALLPHGATVLADHVLFPGAPRFLQYTKSCGRYRCRLHHTSLPDFPAIKDGIAQLTYTGPG | 2.1.1.6 | null | auditory receptor cell development [GO:0060117]; catecholamine catabolic process [GO:0042424]; developmental process [GO:0032502]; dopamine metabolic process [GO:0042417]; methylation [GO:0032259]; positive regulation of protein import [GO:1904591]; sensory perception of sound [GO:0007605] | apical part of cell [GO:0045177]; cytoplasm [GO:0005737]; endoplasmic reticulum [GO:0005783] | catechol O-methyltransferase activity [GO:0016206]; L-dopa O-methyltransferase activity [GO:0102084]; orcinol O-methyltransferase activity [GO:0102938] | PF01596; | 3.40.50.150; | Class I-like SAM-binding methyltransferase superfamily, Cation-dependent O-methyltransferase family | null | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:18953341, ECO:0000269|PubMed:28504928}. Endoplasmic reticulum {ECO:0000269|PubMed:28504928}. Note=Localized to the cell body of the cochlear hair cells, but is not present in the stereocilia. Present but not restricted to the apical cistern, Hensen's body and the subsurface cistern. {ECO:0000269|PubMed:28504928}. | CATALYTIC ACTIVITY: Reaction=a catechol + S-adenosyl-L-methionine = a guaiacol + H(+) + S-adenosyl-L-homocysteine; Xref=Rhea:RHEA:17877, ChEBI:CHEBI:15378, ChEBI:CHEBI:33566, ChEBI:CHEBI:57856, ChEBI:CHEBI:59789, ChEBI:CHEBI:134251; EC=2.1.1.6; Evidence={ECO:0000269|PubMed:18794526}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:17878; Evidence={ECO:0000305|PubMed:18794526}; | null | null | null | null | FUNCTION: Catalyzes the O-methylation, and thereby the inactivation, of catecholamine neurotransmitters and catechol hormones (PubMed:18794526). Required for auditory function (PubMed:18794526, PubMed:28504928). Component of the cochlear hair cell's mechanotransduction (MET) machinery. Involved in the assembly of the asymmetric tip-link MET complex. Required for transportation of TMC1 and TMC2 proteins into the mechanically sensitive stereocilia of the hair cells. The function in MET is independent of the enzymatic activity (PubMed:28504928). {ECO:0000269|PubMed:18794526, ECO:0000269|PubMed:28504928}. | Mus musculus (Mouse) |
A1YB07 | AMOL2_DANRE | MRTAEESSGTVLHRLIQEQLRYGNPTDPTLLAIQQQALRGGSSGGGAGSPRSSLESLTQEESLSPQLSARQEPQGQEHQGDFQHSESPVCHLYQLHTEELPTYEEAKAHSQYLAYQRGQIGLHQGSLESPGGVGGAEQDDSMWDAKREHARSLSERLLQLSLERNCAHDNIPMSSSHSYPQLSNNHSDTVVNEQSVHQPDQRGPPPEYPFMVRSPGYMLSHSQEHGHYYNEPPPAFHSQHYRLFPTQPQAPRHNGLPTLTPAGQDVNVGGYSIPANNFQMEQLIKENERLKREVDSYSEKAARLQKLEQEIQRISEAYETLMKGSAKREALEKTMRNKLESEIKRLHDFNRDLRDRLETANKQRAAIEVEDKSRHAFAKLVEQNEDHLRERERLEKETQHLRASGEEWKRRREALEQALITAQTRNRQLEEELRRKRAYVEKVERMQSALAQLQAACEKREALELRLRTRLEQELKSLRAQQWQAQTQHASPGSYLDLNVSSLQQQLREREEQVLALEADITRWEQKYLEESTMRQFAMDAAATAAAQRDTTIINHSPRNSPNSSFNEDLPSPNHRHQEMENRIRALYAQLLEKDAIIKVMQQRSRREQGRPELQGLRPARSVPSINTVATASTTRAKGKSLSDDQTAVASLPPLPHLLAKIQCRDSSTQCDSEEPSCKAEPADVAVSAPEPSTASSSESTSLKTTQISSAVENDMVEILI | null | null | actin cytoskeleton organization [GO:0030036]; angiogenesis [GO:0001525]; cell migration [GO:0016477]; convergent extension [GO:0060026]; cortical actin cytoskeleton organization [GO:0030866]; dorsal aorta development [GO:0035907]; dorsal aorta morphogenesis [GO:0035912]; embryonic pattern specification [GO:0009880]; endothelial cell proliferation [GO:0001935]; establishment of cell polarity involved in ameboidal cell migration [GO:0003365]; establishment of localization in cell [GO:0051649]; filopodium assembly [GO:0046847]; hippo signaling [GO:0035329]; regulation of cell migration [GO:0030334]; regulation of cell shape [GO:0008360]; Wnt signaling pathway [GO:0016055] | bicellular tight junction [GO:0005923]; cell cortex [GO:0005938]; cell junction [GO:0030054]; cell-cell junction [GO:0005911]; cytoplasmic vesicle [GO:0031410]; plasma membrane [GO:0005886]; polymeric cytoskeletal fiber [GO:0099513]; recycling endosome [GO:0055037] | null | PF12240; | null | Angiomotin family | PTM: Phosphorylation at Tyr-103 is necessary for efficient binding to SRC and synergistically functioning with SRC to activate the downstream MAPK pathway. {ECO:0000269|PubMed:21937427}. | SUBCELLULAR LOCATION: Recycling endosome {ECO:0000269|PubMed:22362771}. | null | null | null | null | null | FUNCTION: Regulates the translocation of phosphorylated SRC to peripheral cell-matrix adhesion sites. Required for proper architecture of actin filaments and for cell movements during embryogenesis. Inhibits the Wnt/beta-catenin signaling pathway, probably by recruiting CTNNB1 to recycling endosomes and hence preventing its translocation to the nucleus. Participates in angiogenesis. May play a role in the polarity, proliferation and migration of endothelial cells. Selectively promotes FGF-induced MAPK activation through SRC. {ECO:0000269|PubMed:17293535, ECO:0000269|PubMed:21937427, ECO:0000269|PubMed:22362771}. | Danio rerio (Zebrafish) (Brachydanio rerio) |
A1YER0 | SIX1_GORGO | MSMLPSFGFTQEQVACVCEVLQQGGNLERLGRFLWSLPACDHLHKNESVLKAKAVVAFHRGNFRELYKILESHQFSPHNHPKLQQLWLKAHYVEAEKLRGRPLGAVGKYRVRRKFPLPRTIWDGEETSYCFKEKSRGVLREWYAHNPYPSPREKRELAEATGLTTTQVSNWFKNRRQRDRAAEAKERENTENNNSSSNKQNQLSPLEGGKPLMSSSEEEFSPPQSPDQNSVLLLQGNMGHARSSNYSLPGLTASQPSHGLQTHQHQLQDSLLGPLTSSLVDLGS | null | null | aorta morphogenesis [GO:0035909]; apoptotic process [GO:0006915]; branching involved in ureteric bud morphogenesis [GO:0001658]; cochlea morphogenesis [GO:0090103]; embryonic cranial skeleton morphogenesis [GO:0048701]; embryonic skeletal system morphogenesis [GO:0048704]; endothelin receptor signaling pathway [GO:0086100]; epithelial cell differentiation [GO:0030855]; facial nerve morphogenesis [GO:0021610]; fungiform papilla morphogenesis [GO:0061197]; gene expression [GO:0010467]; generation of neurons [GO:0048699]; inner ear development [GO:0048839]; inner ear morphogenesis [GO:0042472]; kidney development [GO:0001822]; mesenchymal cell proliferation involved in ureter development [GO:0072198]; mesonephric tubule formation [GO:0072172]; metanephric mesenchyme development [GO:0072075]; middle ear morphogenesis [GO:0042474]; myoblast migration [GO:0051451]; myoblast proliferation [GO:0051450]; myotome development [GO:0061055]; negative regulation of neuron apoptotic process [GO:0043524]; negative regulation of transcription by RNA polymerase II [GO:0000122]; neural crest cell differentiation [GO:0014033]; neuron fate specification [GO:0048665]; Notch signaling pathway [GO:0007219]; olfactory placode formation [GO:0030910]; organ induction [GO:0001759]; otic vesicle development [GO:0071599]; outflow tract morphogenesis [GO:0003151]; pattern specification process [GO:0007389]; pharyngeal system development [GO:0060037]; positive regulation of branching involved in ureteric bud morphogenesis [GO:0090190]; positive regulation of brown fat cell differentiation [GO:0090336]; positive regulation of DNA-templated transcription [GO:0045893]; positive regulation of mesenchymal cell proliferation involved in ureter development [GO:2000729]; positive regulation of myoblast proliferation [GO:2000288]; positive regulation of secondary heart field cardioblast proliferation [GO:0072513]; positive regulation of transcription by RNA polymerase II [GO:0045944]; positive regulation of ureteric bud formation [GO:0072107]; protein localization to nucleus [GO:0034504]; regulation of branch elongation involved in ureteric bud branching [GO:0072095]; regulation of DNA-templated transcription [GO:0006355]; regulation of epithelial cell proliferation [GO:0050678]; regulation of neuron differentiation [GO:0045664]; regulation of protein localization [GO:0032880]; regulation of skeletal muscle cell differentiation [GO:2001014]; regulation of skeletal muscle cell proliferation [GO:0014857]; regulation of skeletal muscle satellite cell proliferation [GO:0014842]; regulation of synaptic assembly at neuromuscular junction [GO:0008582]; regulation of transcription by RNA polymerase II [GO:0006357]; sensory perception of sound [GO:0007605]; skeletal muscle fiber development [GO:0048741]; skeletal muscle tissue development [GO:0007519]; thymus development [GO:0048538]; thyroid gland development [GO:0030878]; trigeminal ganglion development [GO:0061551]; ureter smooth muscle cell differentiation [GO:0072193]; ureteric bud development [GO:0001657] | cytoplasm [GO:0005737]; nucleolus [GO:0005730]; nucleoplasm [GO:0005654]; 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 [GO:0003700]; DNA-binding transcription factor activity, RNA polymerase II-specific [GO:0000981]; RNA polymerase II cis-regulatory region sequence-specific DNA binding [GO:0000978]; sequence-specific DNA binding [GO:0043565] | PF05920;PF16878; | 1.10.10.60; | SIX/Sine oculis homeobox family | PTM: Phosphorylated during interphase; becomes hyperphosphorylated during mitosis. Hyperphosphorylation impairs binding to promoter elements (By similarity). {ECO:0000250}.; PTM: Ubiquitinated by the anaphase promoting complex (APC), leading to its proteasomal degradation. {ECO:0000250}. | SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00108}. Cytoplasm {ECO:0000250}. | null | null | null | null | null | FUNCTION: Transcription factor that is involved in the regulation of cell proliferation, apoptosis and embryonic development (By similarity). Plays an important role in the development of several organs, including kidney, muscle and inner ear (By similarity). Depending on context, functions as a transcriptional repressor or activator (By similarity). Lacks an activation domain, and requires interaction with EYA family members for transcription activation (By similarity). Mediates nuclear translocation of EYA1 and EYA2 (By similarity). Binds the 5'-TCA[AG][AG]TTNC-3' motif present in the MEF3 element in the MYOG promoter and CIDEA enhancer (By similarity). Regulates the expression of numerous genes, including MYC, CCNA1, CCND1 and EZR (By similarity). Acts as an activator of the IGFBP5 promoter, probably coactivated by EYA2 (By similarity). Repression of precursor cell proliferation in myoblasts is switched to activation through recruitment of EYA3 to the SIX1-DACH1 complex (By similarity). During myogenesis, seems to act together with EYA2 and DACH2 (By similarity). Regulates the expression of CCNA1 (By similarity). Promotes brown adipocyte differentiation (By similarity). {ECO:0000250|UniProtKB:Q15475, ECO:0000250|UniProtKB:Q62231}. | Gorilla gorilla gorilla (Western lowland gorilla) |
A1YES6 | APEX1_GORGO | MPKRGKKGAVAEDGDELKTEPEAKKSKTAAKKNDKEAAGEGPALYEDPPDQKTSPSGKPATLKICSWNVDGLRAWIKKKGLDWVKEEAPDILCLQETKCSENKLPAELQELPGLSYQYWSAPXXKEGYSGVGLLSRQCPLKVSYGIGEEEHDQEGRVIVAEFDSFVLVTAYVPNAGRGLVRLEYRQRWDEAFRRFLKGLASRKPLVLCGDLNVAHEEIDLRNPKGNKKNAGFTPQERQGFGELLQAVPLADSFRHLYPNTPYAYTFWTYMMNARSKNVGWRLDYFLLSHSLLPALCDSKIRSKALGSDHCPITLYLAL | 3.1.11.2; 3.1.21.- | COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250|UniProtKB:P27695}; Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000250|UniProtKB:P27695}; Note=Probably binds two magnesium or manganese ions per subunit. {ECO:0000250|UniProtKB:P27695}; | base-excision repair [GO:0006284]; DNA recombination [GO:0006310]; DNA repair [GO:0006281]; positive regulation of gene expression via CpG island demethylation [GO:0044029]; regulation of apoptotic process [GO:0042981]; regulation of mRNA stability [GO:0043488] | cytoplasm [GO:0005737]; endoplasmic reticulum [GO:0005783]; mitochondrion [GO:0005739]; nuclear speck [GO:0016607]; nucleolus [GO:0005730]; nucleoplasm [GO:0005654]; nucleus [GO:0005634] | 3'-5' exonuclease activity [GO:0008408]; chromatin DNA binding [GO:0031490]; class II DNA-(apurinic or apyrimidinic site) endonuclease activity [GO:0052720]; damaged DNA binding [GO:0003684]; DNA-(abasic site) binding [GO:0140431]; DNA-(apurinic or apyrimidinic site) endonuclease activity [GO:0003906]; double-stranded DNA 3'-5' DNA exonuclease activity [GO:0008311]; metal ion binding [GO:0046872]; oxidoreductase activity [GO:0016491]; phosphoric diester hydrolase activity [GO:0008081]; RNA binding [GO:0003723]; site-specific endodeoxyribonuclease activity, specific for altered base [GO:0016890] | PF03372; | 3.60.10.10; | DNA repair enzymes AP/ExoA family | PTM: Phosphorylated. Phosphorylation by kinase PKC or casein kinase CK2 results in enhanced redox activity that stimulates binding of the FOS/JUN AP-1 complex to its cognate binding site. AP-endodeoxyribonuclease activity is not affected by CK2-mediated phosphorylation. Phosphorylation of Thr-233 by CDK5 in response to MPP(+)/MPTP (1-methyl-4-phenylpyridinium) reduces AP-endodeoxyribonuclease activity resulting in accumulation of DNA damage and contributing to neuronal death (By similarity). {ECO:0000250|UniProtKB:P27695}.; PTM: Acetylated on Lys-6 and Lys-7. Acetylation is increased by the transcriptional coactivator EP300 acetyltransferase, genotoxic agents like H(2)O(2) and methyl methanesulfonate (MMS). Acetylation increases its binding affinity to the negative calcium response element (nCaRE) DNA promoter. The acetylated form induces a stronger binding of YBX1 to the Y-box sequence in the MDR1 promoter than the unacetylated form. Deacetylated on lysines. Lys-6 and Lys-7 are deacetylated by SIRT1 (By similarity). {ECO:0000250|UniProtKB:P27695}.; PTM: Cleaved at Lys-31 by granzyme A to create the mitochondrial form; leading in reduction of binding to DNA, AP endodeoxyribonuclease activity, redox activation of transcription factors and to enhanced cell death. Cleaved by granzyme K; leading to intracellular ROS accumulation and enhanced cell death after oxidative stress (By similarity). {ECO:0000250|UniProtKB:P27695}.; PTM: Cys-69 and Cys-93 are nitrosylated in response to nitric oxide (NO) and lead to the exposure of the nuclear export signal (NES). {ECO:0000250|UniProtKB:P27695}.; PTM: Ubiquitinated by MDM2; leading to translocation to the cytoplasm and proteasomal degradation. {ECO:0000250|UniProtKB:P27695}. | SUBCELLULAR LOCATION: Nucleus. Nucleus, nucleolus {ECO:0000250}. Nucleus speckle {ECO:0000255|PROSITE-ProRule:PRU00764}. Endoplasmic reticulum {ECO:0000250}. Cytoplasm {ECO:0000255|PROSITE-ProRule:PRU00764}. Note=Detected in the cytoplasm of B-cells stimulated to switch. Colocalized with SIRT1 in the nucleus. Colocalized with YBX1 in nuclear speckles after genotoxic stress. Together with OGG1 is recruited to nuclear speckles in UVA-irradiated cells. Colocalized with nucleolin and NPM1 in the nucleolus. Its nucleolar localization is cell cycle dependent and requires active rRNA transcription (By similarity). Colocalized with calreticulin in the endoplasmic reticulum. Translocation from the nucleus to the cytoplasm is stimulated in presence of nitric oxide (NO) and function in a CRM1-dependent manner, possibly as a consequence of demasking a nuclear export signal (amino acid position 64-80). S-nitrosylation at Cys-93 and Cys-310 regulates its nuclear-cytosolic shuttling. Ubiquitinated form is localized predominantly in the cytoplasm (By similarity). {ECO:0000250}.; SUBCELLULAR LOCATION: [DNA repair nuclease/redox regulator APEX1, mitochondrial]: Mitochondrion. Note=Translocation from the cytoplasm to the mitochondria is mediated by ROS signaling and cleavage mediated by granzyme A. Tom20-dependent translocated mitochondrial APEX1 level is significantly increased after genotoxic stress. The cleaved APEX2 is only detected in mitochondria (By similarity). {ECO:0000250}. | CATALYTIC ACTIVITY: Reaction=Exonucleolytic cleavage in the 3'- to 5'-direction to yield nucleoside 5'-phosphates.; EC=3.1.11.2; Evidence={ECO:0000250|UniProtKB:P27695}; | null | null | null | null | FUNCTION: Multifunctional protein that plays a central role in the cellular response to oxidative stress. The two major activities of APEX1 are DNA repair and redox regulation of transcriptional factors. Functions as an apurinic/apyrimidinic (AP) endodeoxyribonuclease in the DNA base excision repair (BER) pathway of DNA lesions induced by oxidative and alkylating agents. Initiates repair of AP sites in DNA by catalyzing hydrolytic incision of the phosphodiester backbone immediately adjacent to the damage, generating a single-strand break with 5'-deoxyribose phosphate and 3'-hydroxyl ends. Also incises at AP sites in the DNA strand of DNA/RNA hybrids, single-stranded DNA regions of R-loop structures, and single-stranded RNA molecules. Has 3'-5' exoribonuclease activity on mismatched deoxyribonucleotides at the 3' termini of nicked or gapped DNA molecules during short-patch BER. Possesses DNA 3' phosphodiesterase activity capable of removing lesions (such as phosphoglycolate) blocking the 3' side of DNA strand breaks. May also play a role in the epigenetic regulation of gene expression by participating in DNA demethylation. Acts as a loading factor for POLB onto non-incised AP sites in DNA and stimulates the 5'-terminal deoxyribose 5'-phosphate (dRp) excision activity of POLB. Plays a role in the protection from granzyme-mediated cellular repair leading to cell death. Also involved in the DNA cleavage step of class switch recombination (CSR). On the other hand, APEX1 also exerts reversible nuclear redox activity to regulate DNA binding affinity and transcriptional activity of transcriptional factors by controlling the redox status of their DNA-binding domain, such as the FOS/JUN AP-1 complex after exposure to IR. Involved in calcium-dependent down-regulation of parathyroid hormone (PTH) expression by binding to negative calcium response elements (nCaREs). Together with HNRNPL or the dimer XRCC5/XRCC6, associates with nCaRE, acting as an activator of transcriptional repression. Stimulates the YBX1-mediated MDR1 promoter activity, when acetylated at Lys-6 and Lys-7, leading to drug resistance. Acts also as an endoribonuclease involved in the control of single-stranded RNA metabolism. Plays a role in regulating MYC mRNA turnover by preferentially cleaving in between UA and CA dinucleotides of the MYC coding region determinant (CRD). In association with NMD1, plays a role in the rRNA quality control process during cell cycle progression. Associates, together with YBX1, on the MDR1 promoter. Together with NPM1, associates with rRNA. Binds DNA and RNA (By similarity). {ECO:0000250|UniProtKB:P27695}. | Gorilla gorilla gorilla (Western lowland gorilla) |
A1YF08 | PDX1_GORGO | MNGEEQYYAATQLYKDPCAFQRGPAPEFSASPPACLYMGRQPPPPPPPHPFPGALGALEQGSPPDISPYEVPPLADDPAVAHLHHHLPAQLALPHPPAGPFPEGAEPGVLEEPNRVQLPFPWMKSTKAHAWKGQWAGGAYAAEPEENKRTRTAYTRAQLLELEKEFLFNKYISRPRRVELAVMLNLTERHIKIWFQNRRMKWKKEEDKKRGGGTAVGGGGVAEPEQDCAVTSGEELLALPPPPPPGGAVPPAAPVAAREGRLPPGLSASPQPSSVAPRRPQEPR | null | null | digestive tract development [GO:0048565]; exocrine pancreas development [GO:0031017]; glucose homeostasis [GO:0042593]; glucose metabolic process [GO:0006006]; insulin secretion [GO:0030073]; intrinsic apoptotic signaling pathway in response to endoplasmic reticulum stress [GO:0070059]; liver development [GO:0001889]; morphogenesis of embryonic epithelium [GO:0016331]; negative regulation of endoplasmic reticulum stress-induced intrinsic apoptotic signaling pathway [GO:1902236]; negative regulation of epithelial cell proliferation [GO:0050680]; negative regulation of transcription by RNA polymerase II [GO:0000122]; negative regulation of type B pancreatic cell apoptotic process [GO:2000675]; positive regulation of insulin secretion [GO:0032024]; positive regulation of insulin secretion involved in cellular response to glucose stimulus [GO:0035774]; positive regulation of transcription by RNA polymerase II [GO:0045944]; positive regulation of type B pancreatic cell proliferation [GO:1904692]; regulation of transcription by RNA polymerase II [GO:0006357]; type B pancreatic cell apoptotic process [GO:0097050]; type B pancreatic cell differentiation [GO:0003309]; type B pancreatic cell proliferation [GO:0044342] | cytosol [GO:0005829]; nuclear speck [GO:0016607]; nucleus [GO:0005634] | chromatin binding [GO:0003682]; 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; | Antp homeobox family, IPF1/XlHbox-8 subfamily | PTM: Phosphorylated by the SAPK2 pathway at high intracellular glucose concentration. Phosphorylated by HIPK2 on Ser-269 upon glucose accumulation. This phosphorylation mediates subnuclear localization shifting. Phosphorylation by PASK may lead to translocation into the cytosol (By similarity). {ECO:0000250}. | SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00108}. Cytoplasm, cytosol {ECO:0000250}. | null | null | null | null | null | FUNCTION: Activates insulin and somatostatin gene transcription. Key regulator of islet peptide hormone expression but also responsible for the development of the pancreas, most probably by determining maturation and differentiation of common pancreatic precursor cells in the developing gut. Binds the DNA sequence 5'-CC[CT]TAATGGG-3' (By similarity). {ECO:0000250}. | Gorilla gorilla gorilla (Western lowland gorilla) |
A1YFA7 | PQBP1_GORGO | MPLPVALQTRLAKRGILKHLEPEPEEEIIAEDYDDDPVDYEATRLEGLPPSWYKVFDPSCGLPYYWNADTDLVSWLSPHDPNSVVTKSAKKLRSSNADAEEKLDRSHDKSDRGHDKSDRSHEKLDRGHDKSDRGHDKSDRDRERGYDKVDRERERDRERDRDRGYDKADREEGKERRHHRREELAPYPKSKKAVSRKDEELDPMDPSSYSDAPRGTWSTGLPKRNEAKTGADTTAAGPLFQQRPYPSPGAVLRANAEASRTKQQD | null | null | activation of innate immune response [GO:0002218]; alternative mRNA splicing, via spliceosome [GO:0000380]; cellular response to exogenous dsRNA [GO:0071360]; defense response to virus [GO:0051607]; innate immune response [GO:0045087]; neuron projection development [GO:0031175]; positive regulation of defense response to virus by host [GO:0002230]; positive regulation of type I interferon production [GO:0032481]; regulation of dendrite morphogenesis [GO:0048814]; regulation of RNA splicing [GO:0043484] | cytoplasm [GO:0005737]; cytoplasmic stress granule [GO:0010494]; cytosol [GO:0005829]; neuronal ribonucleoprotein granule [GO:0071598]; nuclear body [GO:0016604]; nuclear speck [GO:0016607]; plasma membrane [GO:0005886] | double-stranded DNA binding [GO:0003690]; lipid binding [GO:0008289]; ribonucleoprotein complex binding [GO:0043021] | null | 2.20.70.10;3.40.30.10; | null | null | SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:O60828}. Nucleus speckle {ECO:0000250|UniProtKB:Q91VJ5}. Cytoplasmic granule {ECO:0000250|UniProtKB:O60828}. Note=Colocalizes with SRSF2 in nuclear speckles (By similarity). Colocalized with POU3F2. Colocalized with ATXN1 in nuclear inclusion bodies. Localizes to cytoplasmic stress granules (By similarity). {ECO:0000250|UniProtKB:O60828, ECO:0000250|UniProtKB:Q91VJ5}. | null | null | null | null | null | FUNCTION: Intrinsically disordered protein that acts as a scaffold, and which is involved in different processes, such as pre-mRNA splicing, transcription regulation, innate immunity and neuron development. Interacts with splicing-related factors via the intrinsically disordered region and regulates alternative splicing of target pre-mRNA species. May suppress the ability of POU3F2 to transactivate the DRD1 gene in a POU3F2 dependent manner. Can activate transcription directly or via association with the transcription machinery. May be involved in ATXN1 mutant-induced cell death. The interaction with ATXN1 mutant reduces levels of phosphorylated RNA polymerase II large subunit. Involved in the assembly of cytoplasmic stress granule, possibly by participating in the transport of neuronal RNA granules. Also acts as an innate immune sensor of infection by retroviruses, by detecting the presence of reverse-transcribed DNA in the cytosol. Directly binds retroviral reverse-transcribed DNA in the cytosol and interacts with CGAS, leading to activate the cGAS-STING signaling pathway, triggering type-I interferon production. {ECO:0000250|UniProtKB:O60828}. | Gorilla gorilla gorilla (Western lowland gorilla) |
A1YFZ3 | APEX1_PANPA | MPKRGKKGAVAEDGDELRTEPEAKKSKTAAKKNDKEAAGEGPALYEDPPDQKTSPSGKPATLKICSWNVDGLRAWIKKKGLDWVKEEAPDILCLQETKCSENKLPAELQELPGLSHQYWSAPSDKEGYSGVGLLSRQCPLKVSYGIGEEEHDQEGRVIVAEFDSFVLVTAYVPNAGRGLVRLEYRQRWDEAFRKFLKGLASRKPLVLCGDLNVAHEEIDLRNPKGNKKNAGFTPQERQGFGELLQAVPLADSFRHLYPNTPYAYTFWTYMMNARSKNVGWRLDYFLLSHSLLPALCDSKIRSKALGSDHCPITLYLAL | 3.1.11.2; 3.1.21.- | COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250|UniProtKB:P27695}; Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000250|UniProtKB:P27695}; Note=Probably binds two magnesium or manganese ions per subunit. {ECO:0000250|UniProtKB:P27695}; | base-excision repair [GO:0006284]; DNA recombination [GO:0006310]; DNA repair [GO:0006281]; positive regulation of gene expression via CpG island demethylation [GO:0044029]; regulation of apoptotic process [GO:0042981]; regulation of mRNA stability [GO:0043488] | cytoplasm [GO:0005737]; endoplasmic reticulum [GO:0005783]; mitochondrion [GO:0005739]; nuclear speck [GO:0016607]; nucleolus [GO:0005730]; nucleoplasm [GO:0005654]; nucleus [GO:0005634] | 3'-5' exonuclease activity [GO:0008408]; chromatin DNA binding [GO:0031490]; class II DNA-(apurinic or apyrimidinic site) endonuclease activity [GO:0052720]; damaged DNA binding [GO:0003684]; DNA-(abasic site) binding [GO:0140431]; DNA-(apurinic or apyrimidinic site) endonuclease activity [GO:0003906]; double-stranded DNA 3'-5' DNA exonuclease activity [GO:0008311]; metal ion binding [GO:0046872]; oxidoreductase activity [GO:0016491]; phosphoric diester hydrolase activity [GO:0008081]; RNA binding [GO:0003723]; site-specific endodeoxyribonuclease activity, specific for altered base [GO:0016890] | PF03372; | 3.60.10.10; | DNA repair enzymes AP/ExoA family | PTM: Phosphorylated. Phosphorylation by kinase PKC or casein kinase CK2 results in enhanced redox activity that stimulates binding of the FOS/JUN AP-1 complex to its cognate binding site. AP-endodeoxyribonuclease activity is not affected by CK2-mediated phosphorylation. Phosphorylation of Thr-233 by CDK5 in response to MPP(+)/MPTP (1-methyl-4-phenylpyridinium) reduces AP-endodeoxyribonuclease activity resulting in accumulation of DNA damage and contributing to neuronal death (By similarity). {ECO:0000250|UniProtKB:P27695}.; PTM: Acetylated on Lys-6 and Lys-7. Acetylation is increased by the transcriptional coactivator EP300 acetyltransferase, genotoxic agents like H(2)O(2) and methyl methanesulfonate (MMS). Acetylation increases its binding affinity to the negative calcium response element (nCaRE) DNA promoter. The acetylated form induces a stronger binding of YBX1 to the Y-box sequence in the MDR1 promoter than the unacetylated form. Deacetylated on lysines. Lys-6 and Lys-7 are deacetylated by SIRT1 (By similarity). {ECO:0000250|UniProtKB:P27695}.; PTM: Cleaved at Lys-31 by granzyme A to create the mitochondrial form; leading in reduction of binding to DNA, AP endodeoxyribonuclease activity, redox activation of transcription factors and to enhanced cell death. Cleaved by granzyme K; leading to intracellular ROS accumulation and enhanced cell death after oxidative stress (By similarity). {ECO:0000250|UniProtKB:P27695}.; PTM: Cys-69 and Cys-93 are nitrosylated in response to nitric oxide (NO) and lead to the exposure of the nuclear export signal (NES). {ECO:0000250|UniProtKB:P27695}.; PTM: Ubiquitinated by MDM2; leading to translocation to the cytoplasm and proteasomal degradation. {ECO:0000250|UniProtKB:P27695}. | SUBCELLULAR LOCATION: Nucleus. Nucleus, nucleolus {ECO:0000250}. Nucleus speckle {ECO:0000255|PROSITE-ProRule:PRU00764}. Endoplasmic reticulum {ECO:0000250}. Cytoplasm {ECO:0000255|PROSITE-ProRule:PRU00764}. Note=Detected in the cytoplasm of B-cells stimulated to switch. Colocalized with SIRT1 in the nucleus. Colocalized with YBX1 in nuclear speckles after genotoxic stress. Together with OGG1 is recruited to nuclear speckles in UVA-irradiated cells. Colocalized with nucleolin and NPM1 in the nucleolus. Its nucleolar localization is cell cycle dependent and requires active rRNA transcription (By similarity). Colocalized with calreticulin in the endoplasmic reticulum. Translocation from the nucleus to the cytoplasm is stimulated in presence of nitric oxide (NO) and function in a CRM1-dependent manner, possibly as a consequence of demasking a nuclear export signal (amino acid position 64-80). S-nitrosylation at Cys-93 and Cys-310 regulates its nuclear-cytosolic shuttling. Ubiquitinated form is localized predominantly in the cytoplasm (By similarity). {ECO:0000250}.; SUBCELLULAR LOCATION: [DNA repair nuclease/redox regulator APEX1, mitochondrial]: Mitochondrion. Note=Translocation from the cytoplasm to the mitochondria is mediated by ROS signaling and cleavage mediated by granzyme A. Tom20-dependent translocated mitochondrial APEX1 level is significantly increased after genotoxic stress. The cleaved APEX2 is only detected in mitochondria (By similarity). {ECO:0000250}. | CATALYTIC ACTIVITY: Reaction=Exonucleolytic cleavage in the 3'- to 5'-direction to yield nucleoside 5'-phosphates.; EC=3.1.11.2; Evidence={ECO:0000250|UniProtKB:P27695}; | null | null | null | null | FUNCTION: Multifunctional protein that plays a central role in the cellular response to oxidative stress. The two major activities of APEX1 are DNA repair and redox regulation of transcriptional factors. Functions as an apurinic/apyrimidinic (AP) endodeoxyribonuclease in the DNA base excision repair (BER) pathway of DNA lesions induced by oxidative and alkylating agents. Initiates repair of AP sites in DNA by catalyzing hydrolytic incision of the phosphodiester backbone immediately adjacent to the damage, generating a single-strand break with 5'-deoxyribose phosphate and 3'-hydroxyl ends. Also incises at AP sites in the DNA strand of DNA/RNA hybrids, single-stranded DNA regions of R-loop structures, and single-stranded RNA molecules. Has 3'-5' exoribonuclease activity on mismatched deoxyribonucleotides at the 3' termini of nicked or gapped DNA molecules during short-patch BER. Possesses DNA 3' phosphodiesterase activity capable of removing lesions (such as phosphoglycolate) blocking the 3' side of DNA strand breaks. May also play a role in the epigenetic regulation of gene expression by participating in DNA demethylation. Acts as a loading factor for POLB onto non-incised AP sites in DNA and stimulates the 5'-terminal deoxyribose 5'-phosphate (dRp) excision activity of POLB. Plays a role in the protection from granzyme-mediated cellular repair leading to cell death. Also involved in the DNA cleavage step of class switch recombination (CSR). On the other hand, APEX1 also exerts reversible nuclear redox activity to regulate DNA binding affinity and transcriptional activity of transcriptional factors by controlling the redox status of their DNA-binding domain, such as the FOS/JUN AP-1 complex after exposure to IR. Involved in calcium-dependent down-regulation of parathyroid hormone (PTH) expression by binding to negative calcium response elements (nCaREs). Together with HNRNPL or the dimer XRCC5/XRCC6, associates with nCaRE, acting as an activator of transcriptional repression. Stimulates the YBX1-mediated MDR1 promoter activity, when acetylated at Lys-6 and Lys-7, leading to drug resistance. Acts also as an endoribonuclease involved in the control of single-stranded RNA metabolism. Plays a role in regulating MYC mRNA turnover by preferentially cleaving in between UA and CA dinucleotides of the MYC coding region determinant (CRD). In association with NMD1, plays a role in the rRNA quality control process during cell cycle progression. Associates, together with YBX1, on the MDR1 promoter. Together with NPM1, associates with rRNA. Binds DNA and RNA (By similarity). {ECO:0000250|UniProtKB:P27695}. | Pan paniscus (Pygmy chimpanzee) (Bonobo) |
A1YG22 | MYC_PANPA | MPLNVSFTNRNYDLDYDSVQPYFYCDEEENFYQQQQQSELQPPAPSEDIWKKFELLPTPPLSPSRRSGLCSPSYVAVTPFSLRGDNDGGGGSFSTADQLEMVTELLGGDMVNQSFICDPDDETFIKNIIIQDCMWSGFSAAAKLVSEKLASYQAARKDSGSPNPARGHSVCSTSSLYLQDLSAAASECIDPSVVFPYPLNDGSSPKSCPSQDSSAFSPSSDSLLSSTESSPQGSPEPLVLHEETPPTTSSDSEEEQEDEEEIDVVSVEKRQAPGKRSESGSPSAGGHSKPPHSPLVLKRCHVSTHQHNYAAPPSTRKDYPAAKRVKLDSVRVLRQISNNRKCTSPRSSDTEENDKRRTHNVLERQRRNELKRSFFALRDQIPELENNEKAPKVVILKKATAYILSVQAEEQKLISEEDLLRKRREQLKHKLEQLRNSCA | null | null | chromatin remodeling [GO:0006338]; chromosome organization [GO:0051276]; DNA damage response [GO:0006974]; G1/S transition of mitotic cell cycle [GO:0000082]; intracellular iron ion homeostasis [GO:0006879]; MAPK cascade [GO:0000165]; negative regulation of apoptotic process [GO:0043066]; negative regulation of cell division [GO:0051782]; negative regulation of monocyte differentiation [GO:0045656]; negative regulation of stress-activated MAPK cascade [GO:0032873]; positive regulation of cysteine-type endopeptidase activity involved in apoptotic process [GO:0043280]; positive regulation of DNA-templated transcription [GO:0045893]; positive regulation of epithelial cell proliferation [GO:0050679]; positive regulation of fibroblast proliferation [GO:0048146]; positive regulation of transcription by RNA polymerase II [GO:0045944]; regulation of DNA-templated transcription [GO:0006355]; regulation of somatic stem cell population maintenance [GO:1904672]; regulation of telomere maintenance [GO:0032204]; response to gamma radiation [GO:0010332]; response to xenobiotic stimulus [GO:0009410] | cytoplasm [GO:0005737]; nucleolus [GO:0005730]; nucleoplasm [GO:0005654]; nucleus [GO:0005634] | DNA binding [GO:0003677]; DNA-binding transcription factor activity, RNA polymerase II-specific [GO:0000981]; E-box binding [GO:0070888]; protein dimerization activity [GO:0046983]; protein-containing complex binding [GO:0044877] | PF00010;PF02344;PF01056; | 4.10.280.10; | null | PTM: Phosphorylated by PRKDC (By similarity). Phosphorylation at Ser-329 by PIM2 leads to the stabilization of MYC (By similarity). Phosphorylation at Ser-62 by CDK2 prevents Ras-induced senescence. Phosphorylated at Ser-62 by DYRK2; this primes the protein for subsequent phosphorylation by GSK3B at Thr-58. Phosphorylation at Thr-58 and Ser-62 by GSK3 is required for ubiquitination and degradation by the proteasome. Dephosphorylation at Ser-62 by protein phosphatase 2A (PPP2CA) promotes its degradation; interaction with PPP2CA is enhanced by AMBRA1 (By similarity). {ECO:0000250|UniProtKB:P01106, ECO:0000250|UniProtKB:P01108}.; PTM: Ubiquitinated by the SCF(FBXW7) complex when phosphorylated at Thr-58 and Ser-62, leading to its degradation by the proteasome. Ubiquitination is counteracted by USP28 in the nucleoplasm and USP36 in the nucleolus, both interacting with of FBXW7, leading to its deubiquitination and preventing degradation. Also polyubiquitinated by the DCX(TRPC4AP) complex. Ubiquitinated by TRIM6 in a phosphorylation-independent manner. {ECO:0000250|UniProtKB:P01106, ECO:0000250|UniProtKB:P01108}. | SUBCELLULAR LOCATION: Nucleus, nucleoplasm {ECO:0000250|UniProtKB:P01106}. Nucleus, nucleolus {ECO:0000250|UniProtKB:P01106}. Nucleus {ECO:0000250|UniProtKB:P01106}. Cytoplasm {ECO:0000250|UniProtKB:P01106}. | null | null | null | null | null | FUNCTION: Transcription factor that binds DNA in a non-specific manner, yet also specifically recognizes the core sequence 5'-CAC[GA]TG-3'. Activates the transcription of growth-related genes. Binds to the VEGFA promoter, promoting VEGFA production and subsequent sprouting angiogenesis. Regulator of somatic reprogramming, controls self-renewal of embryonic stem cells. Functions with TAF6L to activate target gene expression through RNA polymerase II pause release (By similarity). Positively regulates transcription of HNRNPA1, HNRNPA2 and PTBP1 which in turn regulate splicing of pyruvate kinase PKM by binding repressively to sequences flanking PKM exon 9, inhibiting exon 9 inclusion and resulting in exon 10 inclusion and production of the PKM M2 isoform (By similarity). {ECO:0000250|UniProtKB:P01106, ECO:0000250|UniProtKB:P01108}. | Pan paniscus (Pygmy chimpanzee) (Bonobo) |
A1YG32 | S38A2_PANPA | MKKAEMGRFNISPDEDSSSYSSNSDFNYSYPTKQAALKSHYADVDPENQNFLLESNLGKKKYETEFHPGTTSFGMSVFNLSNAIVGSGILGLSYAMANTGIALFIILLTFVSIFSLYSVHLLLKTANEGGSLLYEQLGYKAFGLVGKLAASGSITMQNIGAMSSYLFIVKYELPLVIQALTNIEDKTGLWYLNGNYLVLLVSLVVILPLSLFRNLGYLGYTSGLSLLCMVFFLIVVICKKFQVPCPVEAALIINETINTTLTQPTALVPALSHNVTENDSCRPHYFIFNSQTVYAVPILIFSFVCHPAVLPIYEELKDRSRRRMMNVSKISFFAMFLMYLLAALFGYLTFYEHVESELLHTYSSILGTDILLLIVRLAVLMAVTLTVPVVIFPIRSSVTHLLCASKDFSWWRHSLITVSILAFTNLLVIFVPTIRDIFGFIGASAASMLIFILPSAFYIKLVKKEPMKSVQKIGALFFLLSGVLVMTGSMALIVLDWVHNAPGGGH | null | null | alanine transport [GO:0032328]; amino acid import [GO:0043090]; amino acid transport [GO:0006865]; L-glutamine import across plasma membrane [GO:1903803]; L-proline import across plasma membrane [GO:1904271]; L-serine import across plasma membrane [GO:1903812]; neutral amino acid transport [GO:0015804]; proline transport [GO:0015824]; regulation of glutamate secretion, neurotransmission [GO:1903294] | plasma membrane [GO:0005886] | acidic amino acid transmembrane transporter activity [GO:0015172]; alanine:sodium symporter activity [GO:0015655]; amino acid transmembrane transporter activity [GO:0015171]; amino acid:sodium symporter activity [GO:0005283]; L-glutamine transmembrane transporter activity [GO:0015186]; neutral L-amino acid transmembrane transporter activity [GO:0015175]; neutral L-amino acid:sodium symporter activity [GO:0005295]; proline:sodium symporter activity [GO:0005298] | PF01490; | null | Amino acid/polyamine transporter 2 family | PTM: Polyubiquitination by NEDD4L regulates the degradation and the activity of SLC38A2. {ECO:0000250|UniProtKB:Q8CFE6}. | SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:Q9JHE5}; Multi-pass membrane protein {ECO:0000250|UniProtKB:Q9JHE5}. Note=Insulin promotes recruitment to the plasma membrane from a pool localized in the trans-Golgi network or endosomes. Enriched in the somatodendritic compartment of neurons, it is also detected at the axonal shaft but excluded from the nerve terminal. {ECO:0000250|UniProtKB:Q9JHE5}. | CATALYTIC ACTIVITY: Reaction=L-alanine(in) + Na(+)(in) = L-alanine(out) + Na(+)(out); Xref=Rhea:RHEA:29283, ChEBI:CHEBI:29101, ChEBI:CHEBI:57972; Evidence={ECO:0000250|UniProtKB:Q9JHE5}; PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:29285; Evidence={ECO:0000250|UniProtKB:Q9JHE5}; CATALYTIC ACTIVITY: Reaction=glycine(in) + Na(+)(in) = glycine(out) + Na(+)(out); Xref=Rhea:RHEA:68228, ChEBI:CHEBI:29101, ChEBI:CHEBI:57305; Evidence={ECO:0000250|UniProtKB:Q9JHE5}; PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:68230; Evidence={ECO:0000250|UniProtKB:Q9JHE5}; CATALYTIC ACTIVITY: Reaction=L-serine(in) + Na(+)(in) = L-serine(out) + Na(+)(out); Xref=Rhea:RHEA:29575, ChEBI:CHEBI:29101, ChEBI:CHEBI:33384; Evidence={ECO:0000250|UniProtKB:Q9JHE5}; PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:29577; Evidence={ECO:0000250|UniProtKB:Q9JHE5}; CATALYTIC ACTIVITY: Reaction=L-proline(in) + Na(+)(in) = L-proline(out) + Na(+)(out); Xref=Rhea:RHEA:28967, ChEBI:CHEBI:29101, ChEBI:CHEBI:60039; Evidence={ECO:0000250|UniProtKB:Q9JHE5}; PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:28969; Evidence={ECO:0000250|UniProtKB:Q9JHE5}; CATALYTIC ACTIVITY: Reaction=L-methionine(in) + Na(+)(in) = L-methionine(out) + Na(+)(out); Xref=Rhea:RHEA:68240, ChEBI:CHEBI:29101, ChEBI:CHEBI:57844; Evidence={ECO:0000250|UniProtKB:Q9JHE5}; PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:68242; Evidence={ECO:0000250|UniProtKB:Q9JHE5}; CATALYTIC ACTIVITY: Reaction=L-histidine(in) + Na(+)(in) = L-histidine(out) + Na(+)(out); Xref=Rhea:RHEA:71583, ChEBI:CHEBI:29101, ChEBI:CHEBI:57595; Evidence={ECO:0000250|UniProtKB:Q9JHE5}; PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:71585; Evidence={ECO:0000250|UniProtKB:Q9JHE5}; CATALYTIC ACTIVITY: Reaction=L-asparagine(in) + Na(+)(in) = L-asparagine(out) + Na(+)(out); Xref=Rhea:RHEA:71383, ChEBI:CHEBI:29101, ChEBI:CHEBI:58048; Evidence={ECO:0000250|UniProtKB:Q9JHE5}; PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:71385; Evidence={ECO:0000250|UniProtKB:Q9JHE5}; CATALYTIC ACTIVITY: Reaction=L-glutamine(in) + Na(+)(in) = L-glutamine(out) + Na(+)(out); Xref=Rhea:RHEA:68236, ChEBI:CHEBI:29101, ChEBI:CHEBI:58359; Evidence={ECO:0000250|UniProtKB:Q9JHE5}; PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:68238; Evidence={ECO:0000250|UniProtKB:Q9JHE5}; CATALYTIC ACTIVITY: Reaction=L-threonine(in) + Na(+)(in) = L-threonine(out) + Na(+)(out); Xref=Rhea:RHEA:69999, ChEBI:CHEBI:29101, ChEBI:CHEBI:57926; Evidence={ECO:0000250|UniProtKB:Q9JHE5}; PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:70001; Evidence={ECO:0000250|UniProtKB:Q9JHE5}; CATALYTIC ACTIVITY: Reaction=L-leucine(in) + Na(+)(in) = L-leucine(out) + Na(+)(out); Xref=Rhea:RHEA:29263, ChEBI:CHEBI:29101, ChEBI:CHEBI:57427; Evidence={ECO:0000250|UniProtKB:Q9JHE5}; PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:29265; Evidence={ECO:0000250|UniProtKB:Q9JHE5}; CATALYTIC ACTIVITY: Reaction=L-phenylalanine(in) + Na(+)(in) = L-phenylalanine(out) + Na(+)(out); Xref=Rhea:RHEA:68244, ChEBI:CHEBI:29101, ChEBI:CHEBI:58095; Evidence={ECO:0000250|UniProtKB:Q9JHE5}; PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:68246; Evidence={ECO:0000250|UniProtKB:Q9JHE5}; | null | null | null | null | FUNCTION: Symporter that cotransports neutral amino acids and sodium ions from the extracellular to the intracellular side of the cell membrane. The transport is pH-sensitive, Li(+)-intolerant, electrogenic, driven by the Na(+) electrochemical gradient and cotransports of neutral amino acids and sodium ions with a stoichiometry of 1:1. May function in the transport of amino acids at the blood-brain barrier (By similarity). May function in the transport of amino acids in the supply of maternal nutrients to the fetus through the placenta (By similarity). Maintains a key metabolic glutamine/glutamate balance underpinning retrograde signaling by dendritic release of the neurotransmitter glutamate (By similarity). Transports L-proline in differentiating osteoblasts for the efficient synthesis of proline-enriched proteins and provides proline essential for osteoblast differentiation and bone formation during bone development (By similarity). {ECO:0000250|UniProtKB:Q8CFE6, ECO:0000250|UniProtKB:Q9JHE5}. | Pan paniscus (Pygmy chimpanzee) (Bonobo) |
A1YKT1 | TCP18_ARATH | MNNNIFSTTTTINDDYMLFPYNDHYSSQPLLPFSPSSSINDILIHSTSNTSNNHLDHHHQFQQPSPFSHFEFAPDCALLTSFHPENNGHDDNQTIPNDNHHPSLHFPLNNTIVEQPTEPSETINLIEDSQRISTSQDPKMKKAKKPSRTDRHSKIKTAKGTRDRRMRLSLDVAKELFGLQDMLGFDKASKTVEWLLTQAKPEIIKIATTLSHHGCFSSGDESHIRPVLGSMDTSSDLCELASMWTVDDRGSNTNTTETRGNKVDGRSMRGKRKRPEPRTPILKKLSKEERAKARERAKGRTMEKMMMKMKGRSQLVKVVEEDAHDHGEIIKNNNRSQVNRSSFEMTHCEDKIEELCKNDRFAVCNEFIMNKKDHISNESYDLVNYKPNSSFPVINHHRSQGAANSIEQHQFTDLHYSFGAKPRDLMHNYQNMY | null | null | regulation of DNA-templated transcription [GO:0006355]; regulation of secondary shoot formation [GO:2000032]; secondary shoot formation [GO:0010223] | nucleus [GO:0005634] | DNA-binding transcription factor activity [GO:0003700]; transcription cis-regulatory region binding [GO:0000976] | PF03634; | null | null | null | SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00701, ECO:0000269|PubMed:17307924}. | null | null | null | null | null | FUNCTION: Transcription factor that prevents axillary bud outgrowth and delays early axillary bud development. Indirectly required for the auxin-induced control of apical dominance. {ECO:0000269|PubMed:17307924, ECO:0000269|PubMed:17452340}. | Arabidopsis thaliana (Mouse-ear cress) |
A1YKW7 | RTXA_KINKI | MNLATTKAKLKSGAQAGVQALNKAGHAAKTGTVAAGKATVAGAKSLYLTIPKDYDIEKGGSLNELIKAADELGIARLQEDANNIESAKKSIDTVEKLLSFTQTGVAVSAKKLDELLQKYSSSQLAKSLGSSANIDSKLTKTNHILSTLSSFLGTALAGMDLDSLVKQGDASATDLAKASLDLINELVNNISNSVQSIEAFSEQLGRLGAAISQTKGLSGLGNKLQNLPNFGKANLALEMISGLLSGISAGFTLADKNASTEKKVAAGFELSNQVIGNVTKAISSYVLAQRAAAGLSTTGAVASLITASIMLAISPLAFMNAADKFKNASLIDEFAKQFKKFGYDGDSLLAEYQRGAGTIEASLTAINTALGAVSAGVSAAAVGSVVGSPVALLVAGVTGLISGILEASKQAMFESVANRLQSKILAWEKENGGKNYFENGYDARHAHYLERNLKLLSELNKELQAERVIAITQQRWDANIGELAGITKLGDRISSGKAYADAFEDGKKLDGASNVTVDTRTGVVDISNANGKKTQALHFTSPLLTAGTETRERVQNGKYSYINQLKFNRVKSWTVKDGEANSRLDFSKVIQHVAFNDEDGRLSGKTEEIALNVNAGSGNDDIFAGQGKMNVDGGTGHDRVFYSKDGGLGQVNVDGTKATEAGSYTVNRSINNGSFYHEVIKRQTTQVGKRTETLEYRDFELKRPEHGYQTTDTLKSVEEIVGSQFSDTFKGSKFADIFHGGDGNDTLEGNDGDDRLFGGNGDDHLYGGNGDDLLDGGKGNDVINGGDGNDVYISRKGDGNDTLYDSHGSDKLAFADADLSELTIERTAQGIMIKRNDGSGSINMAEWYKTLSQQNYHGNATDDKIEQIIGKNGDYITSEQIDKLLKDKQTGTITSAQLQQLAQENKSKSIDSGNLASTLNKLIESMASFGSRGATASNYLQPAHKSPQNVLAPSAV | null | null | killing of cells of another organism [GO:0031640] | extracellular region [GO:0005576]; host cell membrane [GO:0033644]; host cell plasma membrane [GO:0020002]; membrane [GO:0016020] | calcium ion binding [GO:0005509]; cholesterol binding [GO:0015485]; monoatomic cation channel activity [GO:0005261]; pore-forming activity [GO:0140911]; toxin activity [GO:0090729] | PF00353;PF02382;PF08339; | 2.150.10.10; | RTX prokaryotic toxin (TC 1.C.11) family | PTM: Myristoylated by RtxC; the toxin only becomes active when modified (PubMed:30405113, PubMed:32461253). Mainly myristoylated; a very minor fraction is acylated with hydroxymyristoyl, lauroyl and palmitoleyl chains fatty acyl groups (PubMed:30405113). Fatty acylation is involved in binding to host membranes and promotes the irreversible insertion of RtxA into the host cell membrane (PubMed:30405113). {ECO:0000269|PubMed:30405113, ECO:0000269|PubMed:32461253}. | SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:21443941}. Host cell membrane {ECO:0000269|PubMed:25858109, ECO:0000269|PubMed:30405113, ECO:0000269|PubMed:33260488}; Multi-pass membrane protein {ECO:0000305}. | null | null | null | null | null | FUNCTION: Bacterial cytolysin that attacks host cell membranes and causes cell rupture by forming a pore (PubMed:25858109, PubMed:30405113). Binds and permeabilizes target cells by forming cation-selective pores (PubMed:25858109). Constitutes the key virulence cytotoxin of K.kingae (PubMed:21248099, PubMed:24664507). Binds cholesterol and oligosaccharides on the surface of host cells (PubMed:30405113). Does not bind beta-2 integrin (ITGB2) on the host cell surface (PubMed:33260488). {ECO:0000269|PubMed:21248099, ECO:0000269|PubMed:24664507, ECO:0000269|PubMed:25858109, ECO:0000269|PubMed:30405113, ECO:0000269|PubMed:33260488}. | Kingella kingae |
A1YYW7 | ALPH_SPHSX | MLKHVAAALLLATAMPVVAQSPAPAAAPAPAARSIAATPPKLIVAISVDQFSADLFSEYRQYYTGGLKRLTSEGAVFPRGYQSHAATETCPGHSTILTGSRPSRTGIIANNWFDLDAKREDKNLYCAEDESQPGSSSDKYEASPLHLKVPTLGGRMKAANPATRVVSVAGKDRAAIMMGGATADQVWWLGGPQGYVSYKGVAPTPLVTQVNQAFAQRLAQPNPGFELPAQCVSKDFPVQAGNRTVGTGRFARDAGDYKGFRISPEQDAMTLAFAAAAIENMQLGKQAQTDIISIGLSATDYVGHTFGTEGTESCIQVDRLDTELGAFFDKLDKDGIDYVVVLTADHGGHDLPERHRMNAMPMEQRVDMALTPKALNATIAEKAGLPGKKVIWSDGPSGDIYYDKGLTAAQRARVETEALKYLRAHPQVQTVFTKAEIAATPSPSGPPESWSLIQEARASFYPSRSGDLLLLLKPRVMSIPEQAVMGSVATHGSPWDTDRRVPILFWRKGMQHFEQPLGVETVDILPSLAALIKLPVPKDQIDGRCLDLVAGKDDSCAGQ | 3.1.3.1 | COFACTOR: Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000269|PubMed:21829507}; Note=Binds 2 Zn(2+) ions. {ECO:0000269|PubMed:21829507}; | dephosphorylation [GO:0016311]; nucleoside triphosphate metabolic process [GO:0009141] | extracellular region [GO:0005576]; vacuole [GO:0005773] | alkaline phosphatase activity [GO:0004035]; metal ion binding [GO:0046872]; nucleoside triphosphate diphosphatase activity [GO:0047429]; ribonucleoside triphosphate phosphatase activity [GO:0017111]; zinc ion binding [GO:0008270] | PF01663; | 3.30.1360.150;3.40.720.10; | null | null | SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:18641147}. | CATALYTIC ACTIVITY: Reaction=a phosphate monoester + H2O = an alcohol + phosphate; Xref=Rhea:RHEA:15017, ChEBI:CHEBI:15377, ChEBI:CHEBI:30879, ChEBI:CHEBI:43474, ChEBI:CHEBI:67140; EC=3.1.3.1; Evidence={ECO:0000269|PubMed:18641147, ECO:0000269|PubMed:21829507}; | null | null | BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 9.0. {ECO:0000269|PubMed:18641147}; | null | FUNCTION: Alkaline phosphatase with broad substrate specificity. Precipitates uranium from alkaline solutions. {ECO:0000269|PubMed:18641147, ECO:0000269|PubMed:21829507}. | Sphingomonas sp |
A1Z0M0 | HEPC_LARCR | MKTFSVAVAVAVVLAFICLQESSAVPANEEQELEQQIYFADPEMPVESCKMPYYMRENRQGSPARCRFCCRCCPRMRGCGICCRF | null | null | defense response to fungus [GO:0050832]; defense response to Gram-negative bacterium [GO:0050829]; defense response to Gram-positive bacterium [GO:0050830]; intracellular iron ion homeostasis [GO:0006879]; negative regulation of iron ion transmembrane transport [GO:0034760] | extracellular region [GO:0005576]; extracellular space [GO:0005615] | hormone activity [GO:0005179] | PF06446; | null | Hepcidin family | null | SUBCELLULAR LOCATION: Secreted {ECO:0000250|UniProtKB:Q9EQ21}. | null | null | null | null | null | FUNCTION: Seems to act as a signaling molecule involved in the maintenance of iron homeostasis. Seems to be required in conjunction with HFE to regulate both intestinal iron absorption and iron storage in macrophages (By similarity). {ECO:0000250|UniProtKB:Q9EQ21}.; FUNCTION: Has very strong antibacterial activity against the marine Gram-negative bacteria V.alginolyticus (MIC=24 uM), V.fluvialis, V.harveyis (MIC=12 uM) and V.parahaemolyticus (MIC=6 uM). Has antibacterial activity against the Gram-negative bacteria A.hydrophila (MIC=6 uM), E.coli (MIC=24 uM), and E.coli BL21(DE3)plysS (MIC=6 uM), and the Gram-positive bacteria B.cereus (MIC=24 uM), B.subtilis (MIC=6 uM), C.glutamicum (MIC=3 uM), M.luteus (MIC=3 uM), M.lysodeikticus, S.aureus (MIC=6 uM) and S.epidermis (MIC=12 uM). Possesses antifungal activity against A.niger (MIC=24 uM), F.graminearum (MIC24 uM) and F.solani (MIC=24 uM), but lacks antifungal activity against the yeasts P.pastoris GS115 and C.albicans. {ECO:0000269|PubMed:19150638, ECO:0000269|PubMed:19344770}. | Larimichthys crocea (Large yellow croaker) (Pseudosciaena crocea) |
A1Z198 | NL1B2_MOUSE | MEESQYKQEHNKKVAQDEGQEDKDTIFETIEAIEAKLMELKTNPESTFNYGIFPEVYMNQGEEILYPAWSLKEENLFQTFKSLRLFQKLCPRGSGNLVKKSWYPCVPEEGGHIINIQDLFGPNIGTQKEPQLVIIEGAAGIGKSTLARQVKRAWMEGELYRDHFQHVFFFSCRELAQCKKLSLAELITQGQDVPTAPINQILSHPEKLLFILDGIDEPAWVLADQNPELCLYWSQTQPVHTLLGSLLGKSILPEASFLLTTRTTALQKFIPSLPQSCQVEVLGFSDFEQEIYIYKYFAKQIFGIKALMMVESNPVLLTLCEVPWVCWLVCNCLKKQMEQGGDVSLTSQTTTAICLKYISLTIPVHHMRTQLRALCSLAAEGIWKRRTLFSESDLCKQGLDEDAVAIFLKTGVLQKQASSLSYSFAHLCLQEFFASMSCILEDSEERHGDMEMDRIVETLVERYGRQNLFEAPTVRFLFGLLSKEGLKEMEKLFSCSLPGKTKLKLLWHILGKSQPHQPPCLGLLHCLYENQDMKLLTHVMHDLQGTIVPDTDDITHTVLQTNVKHLVVRTDMELMVVTFCIQFCSHMRSLQLNMEGQQGYALTAPRMVLYRWTPITNASWKILFYNLKFNSNLEGLDLSGNPLSYSAVQYLCDAMIYPGCQLKTLWLVECGLTPTYCSLLASVLSACSSLRELDLQLNDLCDDGVRMLCEGLRNRACNLRILRLDLYSLSAQVITELRTLEENNLKLHISSIWMPQMMVPTENMDEEDILTSFKQQRQQSGANPMEILGTEEDFWGPIGPVATEVVYRERNLYRVQLPMAGSYHCPSTRLHFVVTRAVTIEIEFCAWSQFLDKTPLQQSHMVVGPLFDIKAEQGAVTAVYLPHFVSLKDTKASTFDFKVAHFQEHGMVLETPDRVKPGYTVLKNPSFSPMGVVLRIIPAARHFIPITSITLIYYRVNQEEVTLHLYLVPNDCTIQKAIDDEEMKFQFVRINKPPPVDNLFIGSRYIVSGSENLEITPKELELCYRSSKEFQLFSEIYVGNMGSEIKLQIKNKKHMKLIWEALLKPGDLRPALPRIAQALKDAPSLLHFMDQHREQLVARVTSVDPLLDKLHGLVLNEESYEAVRAENTNQDKMRKLFNLSRSWSRACKDLFYQALKETHPHLVMDLLEKSGGVSLGS | 3.4.-.- | null | inflammatory response [GO:0006954]; innate immune response [GO:0045087]; pattern recognition receptor signaling pathway [GO:0002221]; positive regulation of inflammatory response [GO:0050729]; positive regulation of interleukin-1 beta production [GO:0032731]; protein catabolic process [GO:0030163]; protein homooligomerization [GO:0051260]; proteolysis [GO:0006508]; pyroptosis [GO:0070269]; regulation of apoptotic process [GO:0042981] | canonical inflammasome complex [GO:0061702]; cytoplasm [GO:0005737]; NLRP1 inflammasome complex [GO:0072558] | ATP binding [GO:0005524]; cysteine-type endopeptidase activator activity [GO:0140608]; peptidase activity [GO:0008233]; protein self-association [GO:0043621] | PF00619;PF13553;PF13516;PF05729;PF17776;PF17779; | 1.10.533.10;3.40.50.300;3.80.10.10; | NLRP family | PTM: [NACHT, LRR and PYD domains-containing protein 1b allele 2]: Autocatalytically cleaved. Autocatalytic cleavage in FIIND region occurs constitutively, prior to activation signals, and is required for inflammasome activity (IL1B release), possibly by facilitating CASP1 binding. Both N- and C-terminal parts remain associated non-covalently. {ECO:0000305|PubMed:31383852}.; PTM: [NACHT, LRR and PYD domains-containing protein 1b, N-terminus]: Ubiquitinated by the N-end rule pathway in response to pathogens and other damage-associated signals, leading to its degradation by the proteasome and subsequent release of the cleaved C-terminal part of the protein (NACHT, LRR and PYD domains-containing protein 1b, C-terminus), which polymerizes and forms the Nlrp1b inflammasome. {ECO:0000250|UniProtKB:Q2LKW6}. | SUBCELLULAR LOCATION: Cytoplasm, cytosol {ECO:0000250|UniProtKB:Q2LKW6}.; SUBCELLULAR LOCATION: [NACHT, LRR and PYD domains-containing protein 1b, C-terminus]: Inflammasome {ECO:0000250|UniProtKB:Q2LKW6}. | null | null | null | null | null | FUNCTION: Acts as the sensor component of the Nlrp1b inflammasome, which mediates inflammasome activation in response to various pathogen-associated signals, leading to subsequent pyroptosis (By similarity). Inflammasomes are supramolecular complexes that assemble in the cytosol in response to pathogens and other damage-associated signals and play critical roles in innate immunity and inflammation (By similarity). Acts as a recognition receptor (PRR): recognizes specific pathogens and other damage-associated signals: in response to pathogen-associated signals, the N-terminal part of Nlrp1b is degraded by the proteasome, releasing the cleaved C-terminal part of the protein (NACHT, LRR and PYD domains-containing protein 1b, C-terminus), which polymerizes to initiate the formation of the inflammasome complex: the inflammasome directly recruits pro-caspase-1 (proCASP1) independently of PYCARD/ASC and promotes caspase-1 (CASP1) activation, which subsequently cleaves and activates inflammatory cytokines IL1B and IL18 and gasdermin-D (GSDMD), leading to pyroptosis (By similarity). In the absence of GSDMD expression, the Nlrp1b inflammasome is able to recruit and activate CASP8, leading to activation of gasdermin-E (GSDME) (By similarity). Activation of Nlrp1b inflammasome is also required for HMGB1 secretion; the active cytokines and HMGB1 stimulate inflammatory responses (By similarity). Contrary to Nlrp1b allele 1, allele 2 is not activated by Bacillus anthracis lethal toxin (PubMed:16429160, PubMed:21170303, PubMed:24492532). {ECO:0000250|UniProtKB:Q2LKW6, ECO:0000269|PubMed:16429160, ECO:0000269|PubMed:21170303, ECO:0000269|PubMed:24492532}.; FUNCTION: [NACHT, LRR and PYD domains-containing protein 1b allele 2]: Constitutes the precursor of the Nlrp1b inflammasome, which mediates autoproteolytic processing within the FIIND domain to generate the N-terminal and C-terminal parts, which are associated non-covalently in absence of pathogens and other damage-associated signals. {ECO:0000250|UniProtKB:Q2LKW6}.; FUNCTION: [NACHT, LRR and PYD domains-containing protein 1b, N-terminus]: Regulatory part that prevents formation of the Nlrp1b inflammasome: in absence of pathogens and other damage-associated signals, interacts with the C-terminal part of Nlrp1b (NACHT, LRR and PYD domains-containing protein 1b, C-terminus), preventing activation of the Nlrp1b inflammasome. In response to pathogen-associated signals, this part is ubiquitinated by the N-end rule pathway and degraded by the proteasome, releasing the cleaved C-terminal part of the protein, which polymerizes and forms the Nlrp1b inflammasome. {ECO:0000250|UniProtKB:Q2LKW6}.; FUNCTION: [NACHT, LRR and PYD domains-containing protein 1b, C-terminus]: Constitutes the active part of the Nlrp1b inflammasome. In absence of pathogens and other damage-associated signals, interacts with the N-terminal part of Nlrp1b (NACHT, LRR and PYD domains-containing protein 1b, N-terminus), preventing activation of the Nlrp1b inflammasome. In response to pathogen-associated signals, the N-terminal part of Nlrp1b is degraded by the proteasome, releasing this form, which polymerizes to form the Nlrp1b inflammasome complex: the Nlrp1b inflammasome complex then directly recruits pro-caspase-1 (proCASP1) and promotes caspase-1 (CASP1) activation, leading to gasdermin-D (GSDMD) cleavage and subsequent pyroptosis. {ECO:0000250|UniProtKB:Q2LKW6}. | Mus musculus (Mouse) |
A1Z1Q3 | MACD2_HUMAN | MYPSNKKKKVWREEKERLLKMTLEERRKEYLRDYIPLNSILSWKEEMKGKGQNDEENTQETSQVKKSLTEKVSLYRGDITLLEVDAIVNAANASLLGGGGVDGCIHRAAGPCLLAECRNLNGCDTGHAKITCGYDLPAKYVIHTVGPIARGHINGSHKEDLANCYKSSLKLVKENNIRSVAFPCISTGIYGFPNEPAAVIALNTIKEWLAKNHHEVDRIIFCVFLEVDFKIYKKKMNEFFSVDDNNEEEEDVEMKEDSDENGPEEKQSVEEMEEQSQDADGVNTVTVPGPASEEAVEDCKDEDFAKDENITKGGEVTDHSVRDQDHPDGQENDSTKNEIKIETESQSSYMETEELSSNQEDAVIVEQPEVIPLTEDQEEKEGEKAPGEDTPRMPGKSEGSSDLENTPGPDAGAQDEAKEQRNGTK | 3.2.2.-; 3.5.1.- | null | brain development [GO:0007420]; DNA damage response [GO:0006974]; peptidyl-glutamate ADP-deribosylation [GO:0140291]; protein de-ADP-ribosylation [GO:0051725]; purine nucleoside metabolic process [GO:0042278]; response to bacterium [GO:0009617] | nucleolus [GO:0005730]; nucleoplasm [GO:0005654]; nucleus [GO:0005634] | ADP-ribosylglutamate hydrolase activity [GO:0140293]; deacetylase activity [GO:0019213]; hydrolase activity, acting on glycosyl bonds [GO:0016798]; O-acetyl-ADP-ribose deacetylase activity [GO:0061463] | PF01661; | 3.40.220.10; | null | null | SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:23474712}. Note=Recruited to DNA lesions, probably via mono-APD-ribosylated proteins. {ECO:0000269|PubMed:23474712}. | CATALYTIC ACTIVITY: Reaction=2''-O-acetyl-ADP-D-ribose + H2O = acetate + ADP-D-ribose + H(+); Xref=Rhea:RHEA:57060, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30089, ChEBI:CHEBI:57967, ChEBI:CHEBI:83767; Evidence={ECO:0000305|PubMed:21257746}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:57061; Evidence={ECO:0000305|PubMed:21257746}; CATALYTIC ACTIVITY: Reaction=4-O-(ADP-D-ribosyl)-L-aspartyl-[protein] + H2O = ADP-D-ribose + H(+) + L-aspartyl-[protein]; Xref=Rhea:RHEA:54428, Rhea:RHEA-COMP:9867, Rhea:RHEA-COMP:13832, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:29961, ChEBI:CHEBI:57967, ChEBI:CHEBI:138102; Evidence={ECO:0000269|PubMed:23474714}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:54429; Evidence={ECO:0000269|PubMed:23474714}; CATALYTIC ACTIVITY: Reaction=5-O-(ADP-D-ribosyl)-L-glutamyl-[protein] + H2O = ADP-D-ribose + H(+) + L-glutamyl-[protein]; Xref=Rhea:RHEA:58248, Rhea:RHEA-COMP:10208, Rhea:RHEA-COMP:15089, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:29973, ChEBI:CHEBI:57967, ChEBI:CHEBI:142540; Evidence={ECO:0000269|PubMed:23474712, ECO:0000269|PubMed:23474714}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:58249; Evidence={ECO:0000269|PubMed:23474712, ECO:0000269|PubMed:23474714}; CATALYTIC ACTIVITY: Reaction=alpha-NAD(+) + H2O = ADP-D-ribose + H(+) + nicotinamide; Xref=Rhea:RHEA:68792, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:17154, ChEBI:CHEBI:57967, ChEBI:CHEBI:77017; Evidence={ECO:0000269|PubMed:31599159}; | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=107 uM for O-acetyl-ADP-ribose {ECO:0000269|PubMed:21257746}; | null | null | null | FUNCTION: Removes ADP-ribose from aspartate and glutamate residues in proteins bearing a single ADP-ribose moiety (PubMed:23474712, PubMed:23474714). Inactive towards proteins bearing poly-ADP-ribose (PubMed:23474712, PubMed:23474714). Deacetylates O-acetyl-ADP ribose, a signaling molecule generated by the deacetylation of acetylated lysine residues in histones and other proteins (PubMed:21257746). {ECO:0000269|PubMed:21257746, ECO:0000269|PubMed:23474712, ECO:0000269|PubMed:23474714}. | Homo sapiens (Human) |
A1Z651 | POL_XMRV6 | MGQTVTTPLSLTLQHWGDVQRIASNQSVDVKKRRWVTFCSAEWPTFNVGWPQDGTFNLGVISQVKSRVFCPGPHGHPDQVPYIVTWEALAYDPPPWVKPFVSPKPPPLPTAPVLPPGPSAQPPSRSALYPALTPSIKSKPPKPQVLPDSGGPLIDLLTEDPPPYGAQPSSSARENNEEEAATTSEVSPPSPMVSRLRGRRDPPAADSTTSQAFPLRMGGDGQLQYWPFSSSDLYNWKNNNPSFSEDPGKLTALIESVLITHQPTWDDCQQLLGTLLTGEEKQRVLLEARKAVRGNDGRPTQLPNEVNAAFPLERPDWDYTTTEGRNHLVLYRQLLLAGLQNAGRSPTNLAKVKGITQGPNESPSAFLERLKEAYRRYTPYDPEDPGQETNVSMSFIWQSAPDIGRKLERLEDLKSKTLGDLVREAEKIFNKRETPEEREERIRREIEEKEERRRAEDEQRERERDRRRHREMSKLLATVVIGQRQDRQGGERRRPQLDKDQCAYCKEKGHWAKDCPKKPRGPRGPRPQTSLLTLGDXGGQGQEPPPEPRITLKVGGQPVTFLVDTGAQHSVLTQNPGPLSDKSAWVQGATGGKRYRWTTDRKVHLATGKVTHSFLHVPDCPYPLLGRDLLTKLKAQIHFEGSGAQVVGPMGQPLQVLTLNIEDEYRLHETSKEPDVPLGSTWLSDFPQAWAETGGMGLAVRQAPLIIPLKATSTPVSIKQYPMSQEARLGIKPHIQRLLDQGILVPCQSPWNTPLLPVKKPGTNDYRPVQDLREVNKRVEDIHPTVPNPYNLLSGLPPSHQWYTVLDLKDAFFCLRLHPTSQPLFAFEWRDPEMGISGQLTWTRLPQGFKNSPTLFDEALHRDLADFRIQHPDLILLQYVDDLLLAATSEQDCQRGTRALLQTLGNLGYRASAKKAQICQKQVKYLGYLLKEGQRWLTEARKETVMGQPTPKTPRQLREFLGTAGFCRLWIPGFAEMAAPLYPLTKTGTLFNWGPDQQKAYQEIKQALLTAPALGLPDLTKPFELFVDEKQGYAKGVLTQKLGPWRRPVAYLSKKLDPVAAGWPPCLRMVAAIAVLTKDAGKLTMGQPLVILAPHAVEALVKQPPDRWLSNARMTHYQAMLLDTDRVQFGPVVALNPATLLPLPEKEAPHDCLEILAETHGTRPDLTDQPIPDADYTWYTDGSSFLQEGQRRAGAAVTTETEVIWARALPAGTSAQRAELIALTQALKMAEGKKLNVYTDSRYAFATAHVHGEIYRRRGLLTSEGREIKNKNEILALLKALFLPKRLSIIHCPGHQKGNSAEARGNRMADQAAREAAMKAVLETSTLLIEDSTPYTPPHFHYTETDLKRLRELGATYNQTKGYWVLQGKPVMPDQSVFELLDSLHRLTHLSPQKMKALLDREESPYYMLNRDRTIQYVTETCTACAQVNASKAKIGAGVRVRGHRPGTHWEVDFTEVKPGLYGYKYLLVFVDTFSGWVEAFPTKRETAKVVSKKLLEDIFPRFGMPQVLGSDNGPAFASQVSQSVADLLGIDWKLHCAYRPQSSGQVERMNRTIKETLTKLTLASGTRDWVLLLPLALYRARNTPGPHGLTPYEILYGAPPPLVNFHDPEMSKLTNSPSLQAHLQALQAVQQEVWKPLAAAYQDQLDQPVIPHPFRVGDAVWVRRHQTKNLEPRWKGPYTVLLTTPTALKVDGISAWIHAAHVKAATTPPAGTAWKVQRSQNPLKIRLTRGAP | 2.7.7.-; 2.7.7.49; 2.7.7.7; 3.1.-.-; 3.1.26.4; 3.4.23.- | COFACTOR: [Reverse transcriptase/ribonuclease H p80]: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250}; Note=Binds 2 magnesium ions for reverse transcriptase polymerase activity. {ECO:0000250}; COFACTOR: [Reverse transcriptase/ribonuclease H p80]: Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000305|PubMed:22252812}; Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000269|PubMed:22252812, ECO:0000269|PubMed:22724525}; Note=Binds 2 Mn(2+)/Mg(2+) ions for ribonuclease H (RNase H) activity (By similarity). Shows 4- to 6-fold increased rates of cleavage in the presence of Mn(2+) versus Mg2(2+) (PubMed:22252812). {ECO:0000250|UniProtKB:Q2F7J3, ECO:0000269|PubMed:22252812}; COFACTOR: [Integrase p46]: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250}; Note=Magnesium ions are required for integrase activity. Binds at least 1, maybe 2 magnesium ions. {ECO:0000250}; | DNA integration [GO:0015074]; DNA recombination [GO:0006310]; establishment of integrated proviral latency [GO:0075713]; proteolysis [GO:0006508]; symbiont entry into host cell [GO:0046718]; viral genome integration into host DNA [GO:0044826]; virion assembly [GO:0019068] | host cell plasma membrane [GO:0020002]; membrane [GO:0016020]; viral nucleocapsid [GO:0019013] | aspartic-type endopeptidase activity [GO:0004190]; DNA binding [GO:0003677]; DNA-directed DNA polymerase activity [GO:0003887]; identical protein binding [GO:0042802]; RNA binding [GO:0003723]; RNA-directed DNA polymerase activity [GO:0003964]; RNA-DNA hybrid ribonuclease activity [GO:0004523]; structural constituent of virion [GO:0039660]; zinc ion binding [GO:0008270] | PF01140;PF01141;PF02093;PF18697;PF00075;PF17919;PF00665;PF00077;PF00078;PF00098;PF16721; | 1.10.340.70;2.30.30.850;3.10.20.370;3.30.70.270;2.40.70.10;1.10.150.180;3.10.10.10;1.10.375.10;3.30.420.10;4.10.60.10; | null | PTM: [Gag-Pol polyprotein]: Specific enzymatic cleavages by the viral protease yield mature proteins. The protease is released by autocatalytic cleavage. The polyprotein is cleaved during and after budding, this process is termed maturation (By similarity). {ECO:0000250}.; PTM: [Capsid protein p30]: Sumoylated. Required for virus replication.; PTM: [RNA-binding phosphoprotein p12]: Phosphorylated on serine residues. {ECO:0000250}. | SUBCELLULAR LOCATION: [Gag-Pol polyprotein]: Host cell membrane {ECO:0000305}; Lipid-anchor {ECO:0000305}.; SUBCELLULAR LOCATION: [Matrix protein p15]: Virion {ECO:0000305}.; SUBCELLULAR LOCATION: [Capsid protein p30]: Virion {ECO:0000305}.; SUBCELLULAR LOCATION: [Nucleocapsid protein p10]: Virion {ECO:0000305}. | CATALYTIC ACTIVITY: [Reverse transcriptase/ribonuclease H p80]: Reaction=a 2'-deoxyribonucleoside 5'-triphosphate + DNA(n) = diphosphate + DNA(n+1); Xref=Rhea:RHEA:22508, Rhea:RHEA-COMP:17339, Rhea:RHEA-COMP:17340, ChEBI:CHEBI:33019, ChEBI:CHEBI:61560, ChEBI:CHEBI:173112; EC=2.7.7.49; Evidence={ECO:0000255|PROSITE-ProRule:PRU00405}; CATALYTIC ACTIVITY: [Reverse transcriptase/ribonuclease H p80]: Reaction=a 2'-deoxyribonucleoside 5'-triphosphate + DNA(n) = diphosphate + DNA(n+1); Xref=Rhea:RHEA:22508, Rhea:RHEA-COMP:17339, Rhea:RHEA-COMP:17340, ChEBI:CHEBI:33019, ChEBI:CHEBI:61560, ChEBI:CHEBI:173112; EC=2.7.7.7; Evidence={ECO:0000255|PROSITE-ProRule:PRU00405}; CATALYTIC ACTIVITY: [Protease p14]: Reaction=Endonucleolytic cleavage to 5'-phosphomonoester.; EC=3.1.26.4; Evidence={ECO:0000255|PROSITE-ProRule:PRU00408}; | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=10.4 nM for RNA/DNA duplex {ECO:0000269|PubMed:22724525}; | null | null | null | FUNCTION: [Gag-Pol polyprotein]: Plays a role in budding and is processed by the viral protease during virion maturation outside the cell. During budding, it recruits, in a PPXY-dependent or independent manner, Nedd4-like ubiquitin ligases that conjugate ubiquitin molecules to Gag, or to Gag binding host factors. Interaction with HECT ubiquitin ligases probably link the viral protein to the host ESCRT pathway and facilitate release. {ECO:0000250|UniProtKB:P03332}.; FUNCTION: [Matrix protein p15]: Targets Gag and gag-pol polyproteins to the plasma membrane via a multipartite membrane binding signal, that includes its myristoylated N-terminus. Also mediates nuclear localization of the pre-integration complex (By similarity). {ECO:0000250}.; FUNCTION: [Capsid protein p30]: Forms the spherical core of the virion that encapsulates the genomic RNA-nucleocapsid complex. {ECO:0000250}.; FUNCTION: [Nucleocapsid protein p10]: Involved in the packaging and encapsidation of two copies of the genome. Binds with high affinity to conserved UCUG elements within the packaging signal, located near the 5'-end of the genome. This binding is dependent on genome dimerization (By similarity). {ECO:0000250}.; FUNCTION: [Protease p14]: The aspartyl protease mediates proteolytic cleavages of Gag and Gag-Pol polyproteins during or shortly after the release of the virion from the plasma membrane. Cleavages take place as an ordered, step-wise cascade to yield mature proteins. This process is called maturation. Displays maximal activity during the budding process just prior to particle release from the cell. {ECO:0000255|PROSITE-ProRule:PRU00275}.; FUNCTION: [Reverse transcriptase/ribonuclease H p80]: Multifunctional enzyme that converts the viral dimeric RNA genome into dsDNA in the cytoplasm, shortly after virus entry into the cell. This enzyme displays a DNA polymerase activity that can copy either DNA or RNA templates, and a ribonuclease H (RNase H) activity that cleaves the RNA strand of RNA-DNA heteroduplexes in a partially processive 3' to 5' endonucleasic mode. Conversion of viral genomic RNA into dsDNA requires many steps. A tRNA binds to the primer-binding site (PBS) situated at the 5' end of the viral RNA. RT uses the 3' end of the tRNA primer to perform a short round of RNA-dependent minus-strand DNA synthesis. The reading proceeds through the U5 region and ends after the repeated (R) region which is present at both ends of viral RNA. The portion of the RNA-DNA heteroduplex is digested by the RNase H, resulting in a ssDNA product attached to the tRNA primer. This ssDNA/tRNA hybridizes with the identical R region situated at the 3' end of viral RNA. This template exchange, known as minus-strand DNA strong stop transfer, can be either intra- or intermolecular. RT uses the 3' end of this newly synthesized short ssDNA to perform the RNA-dependent minus-strand DNA synthesis of the whole template. RNase H digests the RNA template except for a polypurine tract (PPT) situated at the 5' end of the genome. It is not clear if both polymerase and RNase H activities are simultaneous. RNase H probably can proceed both in a polymerase-dependent (RNA cut into small fragments by the same RT performing DNA synthesis) and a polymerase-independent mode (cleavage of remaining RNA fragments by free RTs). Secondly, RT performs DNA-directed plus-strand DNA synthesis using the PPT that has not been removed by RNase H as primers. PPT and tRNA primers are then removed by RNase H. The 3' and 5' ssDNA PBS regions hybridize to form a circular dsDNA intermediate. Strand displacement synthesis by RT to the PBS and PPT ends produces a blunt ended, linear dsDNA copy of the viral genome that includes long terminal repeats (LTRs) at both ends (By similarity). {ECO:0000250}.; FUNCTION: [Integrase p46]: Catalyzes viral DNA integration into the host chromosome, by performing a series of DNA cutting and joining reactions. This enzyme activity takes place after virion entry into a cell and reverse transcription of the RNA genome in dsDNA. The first step in the integration process is 3' processing. This step requires a complex comprising the viral genome, matrix protein and integrase. This complex is called the pre-integration complex (PIC). The integrase protein removes 2 nucleotides from each 3' end of the viral DNA, leaving recessed CA OH's at the 3' ends. In the second step that requires cell division, the PIC enters cell nucleus. In the third step, termed strand transfer, the integrase protein joins the previously processed 3' ends to the 5' ends of strands of target cellular DNA at the site of integration. The last step is viral DNA integration into host chromosome (By similarity). {ECO:0000250}. | Xenotropic MuLV-related virus (isolate VP62) (XMRV) |
A1Z6E0 | GUS_DROME | MGQKISGGVKTVSRNDSQSTFKPIIPRELQADFVKPARIDILLDMPPASRDLQLKHSWNSEDRSLNIFVKEDDKLTFHRHPVAQSTDCIRGKVGLTKGLHIWEIYWPTRQRGTHAVVGVCTADAPLHSVGYQSLVGSTEQSWGWDLGRNKLYHDSKNCAGVTYPAILKNDEAFLVPDKFLVALDMDEGTLSFIVDQQYLGIAFRGLRGKKLYPIVSAVWGHCEITMRYIGGLDPEPLPLMDLCRRTIRQKIGRTNLEEHIQQLQLPLSMKTYLLYKNRR | null | null | cuticle pattern formation [GO:0035017]; dorsal appendage formation [GO:0046843]; germ cell development [GO:0007281]; intracellular signal transduction [GO:0035556]; oocyte anterior/posterior axis specification [GO:0007314]; pole cell migration [GO:0007280]; pole plasm assembly [GO:0007315]; positive regulation of protein catabolic process [GO:0045732]; proteasome-mediated ubiquitin-dependent protein catabolic process [GO:0043161]; protein localization [GO:0008104]; wing disc morphogenesis [GO:0007472] | cell cortex [GO:0005938]; Cul5-RING ubiquitin ligase complex [GO:0031466]; cytoplasm [GO:0005737]; elongin complex [GO:0070449]; nucleus [GO:0005634]; perinuclear region of cytoplasm [GO:0048471]; pole plasm [GO:0045495]; SCF ubiquitin ligase complex [GO:0019005] | null | PF07525;PF00622; | 2.60.120.920;1.10.750.20; | SPSB family | null | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:12479811, ECO:0000269|PubMed:20123973}. Nucleus {ECO:0000269|PubMed:12479811, ECO:0000269|PubMed:20123973}. Note=Component of the cytoplasmic ribonucleoprotein (RNP) bodies which concentrate at the perinuclear region of the nurse cell and in punctate aggregates throughout the cytoplasm. Some cortical enrichment of these aggregates is also observed. At stage 7, accumulates in the anterior cytoplasm of the oocyte, whereas during stage 10 accumulates at the posterior pole. This posterior distribution is not maintained in later developmental stages. {ECO:0000269|PubMed:12479811, ECO:0000269|PubMed:20123973}. | null | null | null | null | null | FUNCTION: Involved in the localization of vas to the posterior pole of the oocyte. Required maternally in the germ line for efficient primordial germ cell formation. {ECO:0000269|PubMed:12479811, ECO:0000269|PubMed:20123973}. | Drosophila melanogaster (Fruit fly) |
A1Z6H7 | PO210_DROME | MDSILCMILLILVRNHASEAARLNHPRVLLPIFEDKAINFTLEVDEPNCYKWSSSRQDLISVMPIYKGFSECAYQAVVTVRTHDRRRNTAIVFAEEVQTGETLRSDVIVDVIASLNVRTATRQLYLEEAPAMFELHAFDEQGNEFFTLEGIEFDWEILEPGSKRPTAMRYLTFTDSPYHTVPPTIEKFEADGKKGHMILLEGINTGTAKVTIAMPQAEYKHVRPVEVYISVLANIIIEPSEVTIMAGDSVSFRILQLKMDRLHVIDNNQYYLEVEDSSIAYLRGNSATGAALGRTQVFLRDRNMADSDEVQKGPSALLTVAYPNRLSISLLPHLNWVTVQGEHHAIALDLFAADGQKITMGTKYSINSEVDESFFAIVDRTRNGSRLFGQAKKEGITQVYGSYKDLSVQAELQIFEELQLAPTKVVLPYDPNSLKPLKLQFHASGGDNNYAWFSGNPQVIQIDTQGQATTEIRDVKSAYVNQEVLKDGGKLTAHTTVKVALSKNQKISRVAHIYFLPPERLQITRSNFETALKDFVHVHVGVYARINNSEVPYTSCDNLHFQLDFSQPILQLEGNEGAEAAHEACHVLRLRATAVGTTSLRVSYMYMDKVLYDIIDLYVFEPLVVLNPIENEVVLPVGSSRNIIYANGPQRSFTVAAEIIQSTAFDEKILKVSKLEFDTQNLITAFTVLCRELGETQFTYRVHNSLPTSSFALYQSEVTTKVHCVRPRFLKLYARHNLRDSCPLEKRTSLLFLKDPENKIEIEIEVHDSNNRRLMNISSLGLDWEFSAGEERYQKNIIPHRQISELEFNHGVTLPSRDLLVLTLSEVATNFRIKGTVSQYNDKLLAQHGIHAERPPFGIKNPQTGLIYTPLIENEIRLHAVNSTLLPKDYMSIFLASGYSERIPIAQGSGYLQLELSEAGIVQVEYNENTRILVLTPLRLGHVRLELTDRCLMNEPSHLSISVVGIGAIEVVSMDRLERTTRIEAIVRLFDTNDNLLLVDQSKLSAYDLSEVVADQSILSVRLGEQENVGPGEIRYTITGNQVGETKILFQSGKGIYKVASDPLNIQVFAPIRLFPRDSTLVVGSSIQVYFHGGPHPNTNMIISVEKEQVATISSTVVTAHKLGTTKIVGKCLLKNPVTGKDEVVSQDSVEVHVVALKGVQIRTPLVRIHSGAVMPATLWGLSDLSPMILGTLQNTKISWKVSQPQVVEIFNVFTTAGIEYQSGDLISVRVRALNPGKATITASVTLADGTILPPATVDLQVFKTLELVTPNAIKMDSILAAPRSILQLKSNMDNVVYKLDDRSNGIVSVTPDGLVHTKDSLGRDLIIATTADQSLPIGIEVKNVQYILVTLMPILKLRELEHKIPRGMNFVFKVSLHDNLGNELSHNIEDFNGLRYELGNKDDVDVQIDNNLTFALNLMRETNNVIGISLKDSTGVKHSMDFIKLSVVESDNLFPTKTIFSVGDIICFDSPLTLSSTWRSSNEQIVYINKHTGIAQVLSHRLKPGEKIEITNGDETKRGGFLKYDLEVRESDTILFVKSVDTFSGPEYRGQLVIRNHLQSEKYSNLIAQNVSKCARELGSVPVNFFTCRLAAKDALGRNLLKMYKVDALFEPSIGQYSCRLQLLTGFIELLSIVKTHDVYLELEAVVAKGVSDKMSLKLVPGIKVFPESVRVTDLKPHEIHISGLDKALLKVQVKPSDSKYFAVDFIEHGHGLSKYRLELFDDLPLDENFYILVVSPDTKQSIEVPIIGNTMLAPKCTDRRYGGPLVYRILENLGFVLTTTVIVIISIWVYMSCFQTQGVTQVNFEAFKKGKSRTELMQQSGRSSQDDTFGDSFNVRNFSPDRRRPPSNALSESYIYGHPRLNSSNRSENSTSFS | null | null | mRNA transport [GO:0051028]; nuclear pore organization [GO:0006999]; protein import into nucleus [GO:0006606] | cytoplasm [GO:0005737]; nuclear membrane [GO:0031965]; nuclear pore [GO:0005643]; nuclear pore inner ring [GO:0044611]; nuclear pore nuclear basket [GO:0044615]; nuclear pore transmembrane ring [GO:0070762] | null | null | null | NUP210 family | PTM: Glycosylated. {ECO:0000269|PubMed:3919018}. | SUBCELLULAR LOCATION: Nucleus membrane {ECO:0000269|PubMed:2517292, ECO:0000269|PubMed:3919018}; Single-pass type I membrane protein {ECO:0000255}. Nucleus, nuclear pore complex {ECO:0000269|PubMed:17682050, ECO:0000269|PubMed:7641726}. Cytoplasm {ECO:0000269|PubMed:2517292}. Note=During mitosis diffusively localized throughout the cytoplasm. {ECO:0000269|PubMed:2517292}. | null | null | null | null | null | FUNCTION: Component of the nuclear pore complex. {ECO:0000269|PubMed:17682050, ECO:0000269|PubMed:7641726}. | Drosophila melanogaster (Fruit fly) |
A1Z6J5 | TBCE_DROME | MVGIIDEVQLFYPLGTRIKIGDNYGTVRYVGEVSGHMGSWLGIEWDDGLRGKHNGIVDGKRYFQTQTPTGGSFIRPGKVGPCATLEDAARERYLNYDSSNVDESLIREAQASLQASLFEVVGMDKIARKQSKFEQLEEVSVDQTPVNAAGYLKELTHLTTLNVSHTLIWNWEIVASIAQQLPSLTNLNLSSNRLVLPTSSQITELEPSFRQLKRINLRSCGFSDWKDVMHTALLWPNILSLGLQENSLGQLAEVDRTKIFKQLHELDLHRTNIMDFDQVTKLGNLTTLRLLNIMENGIEEIKLPDCDSQEKLNIFVSLEQLNLLHNPIWNEADAFNELDKLPQLKRLSKTPHLKSNFDEMFSKAVASIASLQFINKAEVTAEQRRGAEYDIWKKYALDWMQATQGGTDSLREFCRRHRTYPLLVKKYGSPADFVPRSQAKQSNLINVSIRHQLTGETWEKKVPRMITVQTLQGLVMKRFRLSGDVPQLCYVDALHPDLVVPLDNNAKTLDFYSVQEHDTVLVQ | null | null | microtubule cytoskeleton organization [GO:0000226]; microtubule polymerization [GO:0046785]; nervous system development [GO:0007399]; neuromuscular synaptic transmission [GO:0007274]; post-chaperonin tubulin folding pathway [GO:0007023]; regulation of synaptic assembly at neuromuscular junction [GO:0008582]; signal transduction [GO:0007165]; tubulin complex assembly [GO:0007021] | cytoplasm [GO:0005737]; synapse [GO:0045202] | alpha-tubulin binding [GO:0043014] | PF01302; | 2.30.30.190;3.80.10.10; | TBCE family | null | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:19297412}. | null | null | null | null | null | FUNCTION: Tubulin-folding protein which is required for the development of the neuronal microtubule network. Essential for the development and function of neuromuscular synapses. Likely to promote microtubule formation by acting in the negative regulation of the microtubule-severing protein spas. {ECO:0000269|PubMed:19297412}. | Drosophila melanogaster (Fruit fly) |
A1Z6S7 | GDS1_DROME | MATAEIDDLIEKLKTTSVSPANTTNLLCEISATKDPKLFDKHELAECFLGLTKCDDTNVRKEAAKCIAEITKSEVQRKKFTKRNIIAAFLECLRQVPTSDGSMELPIQICRALGNICYLNDEARDLILELEGDAVLLRLLDITTIEDVANAAQFIKVRGGLLSNYLLGGEGLAKRAMELGVMKKLQGIIDIGASNVEQHEDLLLNTLPLLSILTENVSDLNFDSSLNIQLSRILAASTNPDLAEMCLELLHYQAESDEVKLILAKDGLCETIYNLLEKYKTLASTSEARALMKLACELIVLILTGDDSMHYLYTTPLLKNMVDWLDSTDIDLLTTGVLALGNFARTDSHCIYFVEQQTMNKLLEVLAKNNGVKDDVRLQHALLSALRNLVIPKPNKNAVIQAGLVQTILPMLEIHQPPVVFKLLGTLRMTVDGQEKLALELLKNKTLIEQLVHWSKSSDYAGVTGESLRLMAWLIKHAYLSKIAYALPRKGDAPAEQIADKIPLTQDYDRSSLSEFLANEGTVEAMVSMLTAQHLVMQNEALIALCILSVVYLSQPSEAAQAQLLQDELVKCEVGKKLAELISKSSDTMTKEIVENLQNCVNLLKSSEQLVAHLEQHNINELLKSIPILTEYCTL | null | null | muscle cell cellular homeostasis [GO:0046716]; regulation of mitochondrion organization [GO:0010821]; rhabdomere development [GO:0042052] | cytosol [GO:0005829]; endoplasmic reticulum [GO:0005783]; mitochondrial outer membrane [GO:0005741]; mitochondrion [GO:0005739]; plasma membrane [GO:0005886] | guanyl-nucleotide exchange factor activity [GO:0005085] | null | 1.25.10.10; | null | null | SUBCELLULAR LOCATION: Endoplasmic reticulum {ECO:0000269|PubMed:27716788}. Mitochondrion {ECO:0000269|PubMed:27716788}. Cytoplasm, cytosol {ECO:0000269|PubMed:27716788}. | null | null | null | null | null | FUNCTION: Probably acts as a GEF (guanine nucleotide exchange factor) for the Rho family of small GTP-binding proteins (G proteins) that stimulates the dissociation of GDP to enable subsequent binding of GTP (By similarity). May also chaperone the processing and/or trafficking of small GTPases independently of GEF activity (By similarity). By interacting with Miro, promotes mitochondrial fission in response to high calcium concentrations (PubMed:27716788). {ECO:0000250|UniProtKB:P52306, ECO:0000269|PubMed:27716788}. | Drosophila melanogaster (Fruit fly) |
A1Z6W3 | PRIC1_DROME | MSSLSTGGGAGGSSGGPGGADAAAAPAAGQATVTATGNMEPAMVPRTANLLACKQWWRVCFLYGDQQKYYRQLYSKAAAQRLADANQEPDNARDREYDTVDCDLIAGQLDAVEDADDGIDLGDHSSTPKGGATTAGRPLFPHSSSPRRSKKLLRSLRAHVRGEKLPKNDTTTANESSEVTQRNARVTVLDDPFLFGIDADHLGDLVVRGKRYSTLDATENMARFYAEQEATAQVLEIIEQEEESPEQEAPKPALPPKQKQQRPVPPLPPPPANRVTQDQGTQPAAPQVPLQPLTAGDLQFLNLSLRQRSLPRSMKPFKDAHDISFTFNELDTSAEPEVATGAAQQESNEPISRTPLTQISYLQKIPTLPRHFSPSGQGLATPPALGSGGMGLPSSSSASALYAAQAAAGILPTSPLPLQRHQQYLPPHHQQHPGAGMGPGPGSGAAAGPPLGPQYSPGCSANPKYSNAQLPPPPHHHHQLSPALSTPSPPSLLHHPAGGTSSASAHAPFLGGPHMDMQRQSHSDDDSGCALEEYTWVPPGLRPDQVRLYFSQIPDDKVPYVNSPGEQYRVRQLLHQLPPHDNEVRYCHSLTDEERKELRLFSTQRKRDALGRGNVRQLMSARPCDGCDDLISTGDIAVFATRLGPNASWHPACFACSVCRELLVDLIYFHRDGRMYCGRHHAETLKPRCSACDEIILADECTEAEGRAWHMNHFACHECDKQLGGQRYIMREGKPYCLHCFDAMFAEYCDYCGEAIGVDQGQMSHDGQHWHATDECFSCNTCRCSLLGRAFLPRRGAIYCSIACSKGEPPTPSDSSGTGMYTTPTPPTQRVRPHPQAPLPARIPSSHASSSPPMSPQQQQQHQATFNQAMYQMQSQQMEAAGGLVDQSKSYAASDSDAGVVKDLEHGGHMGGGDLTDFSGGRASSTSQNLSPLNSPGDFQPHFLPKPMELQRDGVYNFNEMSSNLDAAWSAKPTNSYHLQRQLLENPHTASMPELAGKLVAPPAHMQHLSQLHAVSSHQFQQHEYADILHPPPPPPGEIPELPTPNLSVASTALPPELMGSPTHSAGDRSLNTPMSTQSASHAPPHPVSILSGASSSSPMSGEPAKKKGVRFEGIPDTLPRSRSYSGNGAGTSGGGERERDRDKDKEGGGRHGHGHSSRRRRRRKSSSSSSHHRSGSGHRSHSTTRADTYAPAQPLSSSYQGPPSVLQAANLVHESPSRQQREREREREREESEESDVCSTCSSSSSSSEDYMMMYQLPQRRHYGGVRVSYVPNDALAYDRKRKPSELGGDKDKNCIIS | null | null | anterior/posterior axis specification [GO:0009948]; axonal transport [GO:0098930]; establishment of imaginal disc-derived wing hair orientation [GO:0001737]; establishment of ommatidial planar polarity [GO:0042067]; establishment of planar polarity [GO:0001736]; establishment of protein localization [GO:0045184]; establishment of tissue polarity [GO:0007164]; establishment or maintenance of cell polarity [GO:0007163]; establishment or maintenance of microtubule cytoskeleton polarity [GO:0030951]; maintenance of protein location [GO:0045185]; morphogenesis of a polarized epithelium [GO:0001738]; ommatidial rotation [GO:0016318]; positive regulation of axon extension [GO:0045773]; positive regulation of axon guidance [GO:1902669] | axon [GO:0030424]; cytoplasm [GO:0005737]; cytosol [GO:0005829]; plasma membrane [GO:0005886] | zinc ion binding [GO:0008270] | PF00412;PF06297; | 2.10.110.10; | Prickle / espinas / testin family | null | SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:12015986, ECO:0000269|PubMed:12642492, ECO:0000269|PubMed:12941693, ECO:0000269|PubMed:15937478}; Peripheral membrane protein {ECO:0000269|PubMed:12015986, ECO:0000269|PubMed:12642492, ECO:0000269|PubMed:12941693, ECO:0000269|PubMed:15937478}; Cytoplasmic side {ECO:0000269|PubMed:12015986, ECO:0000269|PubMed:12642492, ECO:0000269|PubMed:12941693, ECO:0000269|PubMed:15937478}. Note=Localized to the proximal wing cell boundary where fz and dsh localization is antagonized by binding the dsh DEP domain and preventing dsh cortical localization. Localization to the anterior photoreceptor cell membrane. {ECO:0000269|PubMed:12015986, ECO:0000269|PubMed:12642492, ECO:0000269|PubMed:12941693, ECO:0000269|PubMed:15937478}. | null | null | null | null | null | FUNCTION: Acts in a planar cell polarity (PCP) complex; polarization along the apical/basal axis of epithelial cells. Correct expression of the alternative isoforms is required for PCP signaling in imaginal disks. PCP signaling in the wing disk requires the receptor fz and the cytoplasmic proteins dsh and pk. These act in a feedback loop leading to activation of the jnk cascade and subsequent polarized arrangement of hairs and bristles. Dgo and pk compete with one another for dsh binding, thereby modulating fz dsh activity and ensuring tight control over fz PCP signaling. Vang, stan and pk function together to regulate the establishment of tissue polarity in the adult eye. {ECO:0000269|PubMed:12015986, ECO:0000269|PubMed:12642492, ECO:0000269|PubMed:15937478}. | Drosophila melanogaster (Fruit fly) |
A1Z7A6 | ASAP_DROME | MPPSLIAVSEFVEETRSDYSSPTTSTFASRMPDCRHTIGVLEERLEFDREGLTKLKKAVKAIHNSGNTHVDNEMFMVRALERLGGKVIEQDEPDIGAAFLKFSVVTKELSALMKTLMQNINNIVMFPVDSMLKSELRGVKGDMKRPFDKAAKDYEAKFIKIEKEKKAQAKEAGMVRTEIDAAVVAEEMEKERRLYQLQTCEYLLKYKDIKTKTGIELLQHLIEYYHALSNYFKDGLQTIEHFGTYIGDLSEKLHEIKQKQDEDRRSLLDLRTVLRSTPDFERVDNVPSSESRSGGAGYSLHQLQGDKHHGVTRQGHLLKKSEGKVRRVWQKRRCRVTSDGFLDIFHADESKPPTRVNLLTCQIKPVPDDKRGFDLISYNRPYHFQAEDEGDQKAWMAVLVNCKEKALTKAFQHANPQMSPSLVELQKTVIRYVQLLPGNDRCCDCGSRNDVTWISLNFGILVCIQCSGVHRDLGVHHSRIQSLTLDNLTTANLLIARAMGNSTLNDIMEAKLGRGKLQHESSMEERYDFIRAKYVAKRYVMRTCSDDNDLRCDLEQAVVNADMSQLLQVWAEGADLTCCLPSSDAGETALHLAVLREMGSTLHIVDFLIQNMPPKGLNKATNPAGLLDVTGKNTALHLCALHDRRECMKLLLRSGADYELKNSQNKTALDIAKEMGHNSCRELIECAIKREKSAFDHINTDWNLPNEDGSTDFSDDETVIDERKSRSRPPSFAGGDSPVLRSRSSTCDSIQSSSSPIANCPSRQFTLPSGLPSYTHSAGTSPKQHISVGQYLGSATNVGGNGPGNGGSSPSSASSQSVRAARNSLNMQSDLGGHVTGARKSTSTANMNSLKKRTAPAPPPGTLGSASSSSFYGTLPHPPRHSQNFDASDIRAINHKNQSLDVAYGTLPHLRSVESSPRGGGGYGYGVSQDPGGSGNGSNNSLMPAMTTFGHKRSPSGESLNRNIHLAGAKLVLPPTGELPTLKHVDKSALTRPKIPPPGPPSEREISNGQSNESISSMDEGPVAPPRKLVNQSANFPDYESWHTDMDSSGGGLDHSAESNVSSSDNDRLNSSPDNPSKTGGAGLGGKFHYNGQRRCRALYDCVADNDDELEFKEGEILIVLNERTDDENWMEGIIEGQPTRKGMFPVSFVHMLPD | null | null | compound eye morphogenesis [GO:0001745]; mitotic cleavage furrow ingression [GO:1990386]; positive regulation of protein localization [GO:1903829]; regulation of Golgi organization [GO:1903358]; regulation of GTPase activity [GO:0043087] | apical part of cell [GO:0045177]; cytoplasm [GO:0005737]; microvillus [GO:0005902]; nucleus [GO:0005634]; plasma membrane [GO:0005886] | GTPase activator activity [GO:0005096]; metal ion binding [GO:0046872]; phosphatidylinositol phosphate binding [GO:1901981] | PF12796;PF01412;PF16746;PF00169;PF14604; | 1.25.40.950;1.25.40.20;1.10.220.150;1.20.1270.60;2.30.29.30;2.30.30.40; | null | null | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:21976699, ECO:0000269|PubMed:27535433}. Nucleus {ECO:0000269|PubMed:27535433}. Cell membrane; Peripheral membrane protein {ECO:0000269|PubMed:21976699, ECO:0000269|PubMed:27535433}. Cell projection, microvillus {ECO:0000269|PubMed:27535433}. Note=Detected in large puncta at the plasma membrane (PubMed:21976699, PubMed:27535433). Excluded from the nucleus at interphase (PubMed:27535433). Enriched in the nucleus at prometaphase (PubMed:27535433). {ECO:0000269|PubMed:21976699, ECO:0000269|PubMed:27535433}. | null | null | null | null | null | FUNCTION: Probable GTPase-activating protein (GAP) for Arf family proteins (Probable). Involved in Golgi apparatus organization by targeting Arf1 to the Golgi, which may be important for membrane trafficking during epithelial morphogenesis (PubMed:27535433). Regulates the positioning of interommatidial precursor cells during compound eye morphogenesis together with Arf6 and Cindr (PubMed:21976699). Required for cleavage furrow ingression in early embryonic cells (PubMed:27535433). {ECO:0000269|PubMed:21976699, ECO:0000269|PubMed:27535433, ECO:0000305}. | Drosophila melanogaster (Fruit fly) |
A1Z7A8 | COIL_DROME | MQHSSMKVDLSNFFKDERRNSLVFIDAAWNNIKDLQDHIQNLFSLKDISLLTSDGCYLPPRESIKVLNSAEGLKAFRFASHDSDTFVSPAPVKSSKKRKNRSVEEQVHLTASTPLRPSKRSKNQNNSEWINIAENPSRVRKKELLDMAPGPSVQSKLLTNKGTPKAPETQTEVSNMSANIETENKESAPQIKNKSKNKKPTKSPEASDQVENEPAPKSISRCTLKEGKMSESKNQETSPDILSEKSGVVTKENETREEQQDKTHLESNKIPDKLSQLKAGDQIEKSPGIAASLLSISFRSPLLEMPFNVPRIFQFPTKKQQIEILEYKKLKPISPRFLLQKGAKSDDTAKQFPSNGKDSTLKPKSYEILHDEELPDVKDKKNVSEGIKRAVAPLCEDIIETSTTLPGAIGAVESAYLDNSTEAETTLPSEAEATNPLELTESFLQNNTSMEKTPKVEKILPDDGSASPIKNNVDSKDVKTVTVPIFEEQLVSDSDDDVMLVDDSNIDVSYGDSDIEPIPVVENRQSLDIIRDLLRTATPLNSLPSRGDTVIFKLLKIKGNANSGTTEFVAGRCTYVNRRTKIVTVETITYPPEIGRMLRQYYMSGLDESSEDVRTLSIHLKDMLEAKIIVATID | null | null | Cajal body organization [GO:0030576] | Cajal body [GO:0015030]; chromosome, centromeric region [GO:0000775]; cytoplasm [GO:0005737]; histone locus body [GO:0035363]; nuclear body [GO:0016604]; nucleoplasm [GO:0005654]; spindle [GO:0005819] | null | PF15862; | null | Coilin family | null | SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:19158395}. Nucleus, nucleoplasm {ECO:0000269|PubMed:19158395}. Nucleus, Cajal body {ECO:0000269|PubMed:19158395, ECO:0000269|PubMed:23885126}. Chromosome, centromere {ECO:0000269|PubMed:19158395}. Cytoplasm, cytoskeleton, spindle {ECO:0000269|PubMed:19158395}. Note=Detected in the CBs of cells from a number of different larval and adult tissues. In stage 8-9 oocytes detected only in the single CB of the germinal vesicle. Also detected in the histone locus bodies (HLBs) of late stage nurse cells, and low expression in the HLBs of large polytene or polyploid nuclei within the salivary glands, fat bodies and Malpighian tubule cells. In germline stem cells and cystocytes (where CBs are not evident), expressed throughout the nucleoplasm. During interphase localized to foci scattered throughout the nucleoplasm. During metaphase (in meiotic and mitotic cells) these foci localize to the centromere regions on the metaphase plate. At anaphase, no longer detected as foci and is instead detected throughout the spindle. When the nucleus reforms, it localizes to multiple nuclear foci and throughout the nucleoplasm. {ECO:0000269|PubMed:19158395}.; SUBCELLULAR LOCATION: [Isoform C]: Cytoplasm {ECO:0000269|PubMed:19158395}. Note=Very low expression and not detected at the protein level. Relatively higher levels of expression in the cytoplasm of follicle cells that have no expression of Isoform D in their CBs. {ECO:0000269|PubMed:19158395}. | null | null | null | null | null | FUNCTION: Component of nuclear coiled bodies, also known as Cajal bodies or CBs, which are involved in the modification and assembly of nucleoplasmic snRNPs (PubMed:19846657). Required for Cajal body formation (PubMed:19158395, PubMed:19846657). {ECO:0000269|PubMed:19158395, ECO:0000269|PubMed:19846657}. | Drosophila melanogaster (Fruit fly) |
A1Z7G7 | LPHN_DROME | MILSKYQTAYACEGKKLTIECDPGDVINLIRANYGRFSITICNDHGNVEWSVNCMFPKSLSVLNSRCAHKQSCGVLAATSMFGDPCPGTHKYLEAHYQCISAAQTSTTTNRPSPPPWVLSNGPPIFGNGSGLIHPPGVGAGAPPPPRLPTLPGVVGISGNPGLFNVPPQHTAVTHSTPSSSTTAVGGGRLKGGATSTTTTKHPAGRHDGLPPPPQLHHHHNHHGEDTASPTKPSSKLPAGGNATSPSNTRILTGVGGSGTDDGTLLTTKSSPNRPPGTAASGSVVPGNGSVVRTINNINLNAAGMSGGDDESKLFCGPTHARNLYWNMTRVGDVNVQPCPGGAAGIAKWRCVLMKRIPDSGYDEYDDDISSTTPAPSGGDCLHNSSSCEPPVSMAHKVNQRLRNFEPTWHPATPDLTQCRSLWLNNLEMRVNQRDSSLISIANDMSEVTSSKTLYGGDMLVTTKIIQTVSEKMMHDKETFPDQRQREAMIMELLHCVVKTGSNLLDESQLSSWLDLNPEDQMRVATSLLTGLEYNAFLLADTIIRERSVVQKVKNILLSVRVLETKTIQSSVVFPDSDQWPLSSDRIELPRAALIDNSEGGLVRIVFAAFDRLESILKPSYDHFDLKSSRSYVRNTAILSNDSDVNAGEIQQRLRILNSKVISASLGKGRHIQLSQPITLTLKHLKTENVTNPTCVFWNYIDHAWSANGCSLESTNRTHSVCSCNHLTNFAILMDVVDEHQHSLFTMFDGNMRIFIYISIGICVVFIVIALLTLKLFNGVFVKSARTSIYTSIYLCLLAIELLFLLGIEQTETSIFCGFITIFLHCAILSGTAWFCYEAFHSYSTLTSDELLLEVDQTPKVNCYYLLSYGLSLSVVAISLVIDPSTYTQNDYCVLMEANALFYATFVIPVLVFFVAAIGYTFLSWIIMCRKSRTGLKTKEHTRLASVRFDIRCSFVFLLLLSAVWCSAYFYLRGAKMDDDTADVYGYCFICFNTLLGLYIFVFHCIQNEKIRREYRKYVRQHAWLPKCLRCSKTSISSGIVTGNGPTAGTLCSVSTSKKPKLPLGVSEEAHDDPQQQQQTPVPITEDAIMGATSDCELNEAQQRRTLKSGLMTGTLQAPPQTLGGHVVLERGSTLRSTGHASPTSSAGSTHLIFAHKQQQQQQQQGPLGESYYHQPDYYSWKQPSTGTGGLKTPREYYNNAGAAASSPQQAHEVFYWTQKPNSGHNGKKKRGAGGVPASPSGSLHSRTAAASQVLFYPSYKKTKPGQPTGYPQYAEALDPPLATGNAAAYYQQQQQLRRQQLHQQQQQQQQQQLSSDEEQAEQHAHLLHLQRRAGSQQQLPAPPPHMAQYQQEFMQRQYRNKHSNCDLGMGDAYYNQGSVGGADGGPVYEEILSNRNSDVQHYEVGDFDVDEVYNNSVGTGVFNNMRAAVAAGGSRYGGGSLSGGSVSSRSQQQQLKKQQQQQSLAQQRSARRCTADDDDDEDEEEDEEATAAEQLHDSVCDEDEEEDESDLEDDAHGLPPQSDERMRRLMAMQDEDFKRRFQRQLRKHGAPLDYGALPPGAGPQPEHNGAVFGVSGGVGEGSLRGAFRQQQQQALNAKSPGGRLAVNELFGHGNSGPPLPPANQTPAQKRQQLQKLSPQSTTSSSSHTSHSNPNPHPHQLTHPHPHQHPPHHQQRHLSAMLDENNTVRCYLEPLAK | null | null | adenylate cyclase-activating G protein-coupled receptor signaling pathway [GO:0007189]; adult locomotory behavior [GO:0008344]; cell surface receptor signaling pathway [GO:0007166]; proprioception [GO:0019230] | plasma membrane [GO:0005886] | carbohydrate binding [GO:0030246]; G protein-coupled receptor activity [GO:0004930]; mechanoreceptor activity [GO:0140897]; transmembrane signaling receptor activity [GO:0004888] | PF00002;PF16489;PF02140;PF01825; | 1.25.40.610;2.60.120.740;2.60.220.50;4.10.1240.10;1.20.1070.10; | G-protein coupled receptor 2 family, LN-TM7 subfamily | PTM: Proteolytically cleaved into 2 subunits, an extracellular subunit and a seven-transmembrane subunit. {ECO:0000250|UniProtKB:O88923}. | SUBCELLULAR LOCATION: Cell membrane {ECO:0000255}; Multi-pass membrane protein {ECO:0000250|UniProtKB:O88923, ECO:0000255}. | null | null | null | null | null | null | Drosophila melanogaster (Fruit fly) |
A1Z7K9 | PAN2_DROME | MDYVYCGTDPIGASEDILSVYDAGSAPGNGHFSPSFNGFNIGTTDPEYVELVPVLADGGEHFGVSSVAFDDYEELLWMGNQGGHVTSYYTNSMQKYTSFQVHATDIVRDISTLDSGVLALTQTSLRHQIRRGLPKFTFKSNNMKEMVSMLQLSPHRLVMAGLQDELIDFDLRTLKETRIEHVGAGGCTVLRKNSRYLFAGDQLGTVTLRDLNSLSVQHTIKTHTNILSDFSVQGNLLISCGYSGRQNNLAIDRFLMVYDLRMLRLIAPIQVMIDPQMLKFLPSLTSQLAVVSSYGQVQLVDTVELSEPRVSMYQINTNGSQCLSFDISSSSQAMAFGDQSGHINMIAAVQTPQPQFNLYSRSTEFADVVPQLPMVSITDTNFPLSSVMLPHLTTGTQWFSDWPEELLRYRYHRPKTIDPEVLSNMKMQGPIGYSPNPRTARRNQIPYVIEQGGVCSPNGNGTAAATKAENGVKIIPRRYRKVELKYTKLGTQDFDFDQHNQTCFAGLEATLPNSYCNAMLQILYFTDALRVKLLEHSCIKEFCLSCELGFLFNMLDKSTASSPCQASNFLRSFRTVPEASALGLILTDRSSNVNLISLIQNWNRFILHQMHYEIFDSSKNASTYSGSVQTSTNAENAGSSETSGSSDLYDSISDENSKEDDRERSKINAETDISKIFGTKQICINRCIKCQEEKIKESILLACNLSYPNHIKDSDQYFNFGTILKRSLSSEKSIQAFCERCKKFSPTNQSVKVTSLPQILSINCGLNNEKDITFLKRQLNRCSEKTTVDAAASLSTSKPCRYGANCSRSDCHFMHPDRKSPSHTSQPNAVNNSPNGRQKSWFPLTFTMGINDQGEVQVQTQSDASSGKSEQEEETEKPPTKGLDNNRMYALHAVVCQVDDGTQKNLVSLINVQRPYHTMKLAESADDPQSQWYIFNDFSISPVSPQESVWFTLDWKVPCILFYRHVEDDSESASTTSSTVTESEETIPSESSSGSPTNLSNPFLEEIVSPMLGNLSADATLQPLQSDEMPQSGDLVAMDAEFVTLNPEENEIRPDGKTATIKPCHMSVARISCIRGQGPAEGVPFMDDYISTQEKVVDYLTQFSGIKPGDLDANFSKKRLTALKYSYQKLKYLVDVGVIFVGHGLKNDFRVINIYVPSEQIIDTVHLFHMPHHRMVSLRFLAWHFLGTKIQSETHDSIEDARTTLQLYKHYLKLQEEKKFANALKNLYERGKQLQWKVPED | 3.1.13.4 | COFACTOR: Name=a divalent metal cation; Xref=ChEBI:CHEBI:60240; Evidence={ECO:0000255|HAMAP-Rule:MF_03182}; Note=Binds 2 metal cations per subunit in the catalytic exonuclease domain. {ECO:0000255|HAMAP-Rule:MF_03182}; | mRNA processing [GO:0006397]; nuclear-transcribed mRNA poly(A) tail shortening [GO:0000289]; positive regulation of cytoplasmic mRNA processing body assembly [GO:0010606] | nucleus [GO:0005634]; P-body [GO:0000932]; PAN complex [GO:0031251] | metal ion binding [GO:0046872]; mRNA regulatory element binding translation repressor activity [GO:0000900]; poly(A)-specific ribonuclease activity [GO:0004535] | PF20770;PF00929;PF13423; | 3.90.70.10;3.30.420.10;2.130.10.10; | Peptidase C19 family, PAN2 subfamily | null | SUBCELLULAR LOCATION: Cytoplasm, P-body {ECO:0000255|HAMAP-Rule:MF_03182}. Nucleus {ECO:0000255|HAMAP-Rule:MF_03182}. Note=Shuttles between nucleus and cytoplasm. {ECO:0000255|HAMAP-Rule:MF_03182}. | CATALYTIC ACTIVITY: Reaction=Exonucleolytic cleavage of poly(A) to 5'-AMP.; EC=3.1.13.4; Evidence={ECO:0000255|HAMAP-Rule:MF_03182, ECO:0000269|PubMed:24880343}; | null | null | null | null | FUNCTION: Catalytic subunit of the poly(A)-nuclease (PAN) deadenylation complex, one of two cytoplasmic mRNA deadenylases involved in general and miRNA-mediated mRNA turnover. PAN specifically shortens poly(A) tails of RNA and the activity is stimulated by poly(A)-binding protein (PABP). PAN deadenylation is followed by rapid degradation of the shortened mRNA tails by the CCR4-NOT complex. Deadenylated mRNAs are then degraded by two alternative mechanisms, namely exosome-mediated 3'-5' exonucleolytic degradation, or deadenylation-dependent mRNA decaping and subsequent 5'-3' exonucleolytic degradation by XRN1. {ECO:0000255|HAMAP-Rule:MF_03182}. | Drosophila melanogaster (Fruit fly) |
A1Z7R6 | S46_DROME | MNEEPHAHENLVAKAQRSGDADPEVASTASEKQRSSGASAIAVGTEFPGNPQASRPQSLGMYLLEPFILILLFAYNFSSTVLKNEVIYQSCTAGFGYPDSVCQLLGTKNITNETKRIEEQVQPYAAQVTLAMRLVECFIPAFCGLFAGSWADHYGRKPLLMCSFLGYGLQYLISAAIAYCAMYTQGLVSPWWYVLSIVPLSCLGSSVTYSVAAVCFIADVSGGKVRSYRMIAYELAIYVGLLLGSLGSGYAYEATDAYIVFSISAVCIFTALFLMALLLPESLPARNRTLSTPTTDTSVVSMLKSLWSTCSKPREHQNRFMLTTIMVVLLLTAFVSDGSNSVFYKFMRIKFHWTVKQFTEYETVGILVPAVAGSGGVLFIWSLRKCTNSAILWLALVSLLSHCSSSLMKGFALESWQIYVAIGLGVFKSLVNPMCRTMITNLLPADERGKIFALLGVLQALSPLISSTLYVAIYTRTLNTEPGIFNVFSAFLFGIGIILLGTVWHKKSRNLVYYEPVFK | null | null | innate immune response [GO:0045087]; peptidoglycan transport [GO:0015835]; positive regulation of antimicrobial humoral response [GO:0002760]; positive regulation of peptidoglycan recognition protein signaling pathway [GO:0061059]; transmembrane transport [GO:0055085] | membrane [GO:0016020]; phagocytic vesicle membrane [GO:0030670] | peptidoglycan transmembrane transporter activity [GO:0015647]; transmembrane transporter activity [GO:0022857] | PF07690; | 1.20.1250.20; | Major facilitator superfamily, SLC46 family | null | SUBCELLULAR LOCATION: Cytoplasmic vesicle, phagosome membrane {ECO:0000305|PubMed:28539433}; Multi-pass membrane protein {ECO:0000255}. | CATALYTIC ACTIVITY: Reaction=n H(+)(out) + N-acetyl-beta-D-glucosaminyl-(1->4)-1,6-anhydro-N-acetyl-beta-D-muramoyl-L-alanyl-gamma-D-glutamyl-meso-diaminoheptanedioate-D-alanine(out) = n H(+)(in) + N-acetyl-beta-D-glucosaminyl-(1->4)-1,6-anhydro-N-acetyl-beta-D-muramoyl-L-alanyl-gamma-D-glutamyl-meso-diaminoheptanedioate-D-alanine(in); Xref=Rhea:RHEA:76355, ChEBI:CHEBI:15378, ChEBI:CHEBI:195208; Evidence={ECO:0000305|PubMed:28539433}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:76356; Evidence={ECO:0000305|PubMed:28539433}; | null | null | null | null | FUNCTION: Putative proton-coupled transporter that delivers pathogen-associated molecular patterns to cytosolic pattern recognition receptors as part of the innate immune response to microbes. Likely transports anhydro-muropeptides that contain the amino acid diaminopimelic acid (DAP-type peptidoglycan muropeptides) such as tracheal toxin (TCT), common in Gram-negative bacteria. May transport TCT across the phagosome membrane for cytosolic recognition by PGRP-LE, triggering the activation of imd/Relish pathway and production of antimicrobial peptides (PubMed:28539433). The transport mechanism, its electrogenicity and stoichiometry remain to be elucidated (Probable). {ECO:0000269|PubMed:28539433, ECO:0000305}. | Drosophila melanogaster (Fruit fly) |
A1Z7T0 | PKN_DROME | MSDSYYQGEYIKHPVLYELSHKYGFTENLPESCMSIRLEEIKEAIRREIRKELKIKEGAEKLREVAKDRRSLSDVAVLVKKSKSKLAELKSELQELESQILLTSANTAVNSNGQESITACIDPNGGFLVSGAVGGLGGGNTALEGGAPATANDKVLASLEKQLQIEMKVKTGAENMIQSLGIGCDKKLLAEAHQMLADSKAKIEFLRLRIIKVKQNREQADRLKASRQMIDEHGQTIGGNNSSQPQSLETTLEERIEELRHRLRIEAAVVDGAKNVIRTLQTANRAPDKKALQEAHGRLSESSRKLDLLRYSLDLRRQELPADSPAAQQLKTELQIVQLSTSPAPVTYTSLQSGQAGILGGKPYQSVSSLGRCASVTGKLEVRLLGCQDLLEDVPGRSRRDKDNNSSPGDLRSFVKGVTSRSSSKSYSVKDETSIEIMAVIKLDNITVGQTSWKQCSQQAWDQRFSIDLDRSRELEIGVYWRDWRSLCAVKVLRLEEFIDDVRHGMALQLEPQGLLFAEVKFLNPMISQKPKLRRQRMIFNRQQAKNISRAKQMNINVATWGRLLKRNAPNHVHMGSAGSGSSLTGSSPMVVGGSRDSESPISRTPSSDALVEPEPYTPGEQAQNLEFDPDAGINEHVETPGEYPDPAASGLSGMRPLSMHMQGISVLPPESPPVATGAAGRPNTLSLQMPGASKGQVIQGGRTAAPTTAPPPPPVLKATSTTPILDQEVIPQLGKLYVGSSQQQYAQQSSPIIQEPATPTIYGNSAAAGAPQFPQPAQRQEKQPPQQQPIYANQYELNVAKAAAAASVYSPSSSTTSNSNQQQQQQRRNVARGLQYRESGGLETGRAGKQPPNAGMLSMDNFRLLSVLGRGHFGKVILSQLRSNNQYYAIKALKKGDIIARDEVESLLSEKRIFEVANAMRHPFLVNLYSCFQTEQHVCFVMEYAAGGDLMMHIHTDVFLEPRAVFYAACVVLGLQYLHENKIIYRDLKLDNLLLDTEGYVKIADFGLCKEGMGFGDRTGTFCGTPEFLAPEVLTETSYTRAVDWWGLGVLIFEMLVGESPFPGDDEEEVFDSIVNDEVRYPRFLSLEAIAVMRRLLRKNPERRLGSSERDAEDVKKQAFFRSIVWDDLLLRKVKPPFVPTINHLEDVSNFDEEFTSEKAQLTPPKEPRHLTEEEQLLFQDFSYTAEWC | 2.7.11.13 | null | actin cytoskeleton organization [GO:0030036]; cell adhesion [GO:0007155]; dorsal closure [GO:0007391]; intracellular signal transduction [GO:0035556]; mitotic cytokinesis, division site positioning [GO:1902408]; positive regulation of wound healing [GO:0090303]; protein autophosphorylation [GO:0046777]; wing disc morphogenesis [GO:0007472] | anchoring junction [GO:0070161]; apical cortex [GO:0045179]; cleavage furrow [GO:0032154]; cytoplasm [GO:0005737]; cytoskeleton [GO:0005856]; cytosol [GO:0005829]; lamellipodium [GO:0030027]; midbody [GO:0030496]; nucleus [GO:0005634] | ATP binding [GO:0005524]; diacylglycerol-dependent serine/threonine kinase activity [GO:0004697]; protein kinase activity [GO:0004672]; protein serine kinase activity [GO:0106310]; protein serine/threonine kinase activity [GO:0004674]; small GTPase binding [GO:0031267] | PF02185;PF00069;PF00433; | 1.10.287.160;1.10.510.10; | Protein kinase superfamily, Ser/Thr protein kinase family | PTM: Phosphorylated (By similarity). Autophosphorylated; autophosphorylation is stimulated by GTP-bound Rho/Rac GTPases. {ECO:0000250}. | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:17507675}. Nucleus {ECO:0000250}. Membrane {ECO:0000250}. Cell projection, lamellipodium {ECO:0000250}. Cytoplasm, cytoskeleton {ECO:0000250}. Cleavage furrow {ECO:0000250}. Midbody {ECO:0000250}. Cell junction {ECO:0000250}. | 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=2.7.11.13; 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=2.7.11.13; | null | null | null | null | FUNCTION: Pkc-related serine/threonine-protein kinase and Rho/Rac effector protein that participates in specific signal transduction responses in the cell. May play a role in the regulation of cell cycle progression, actin cytoskeleton assembly, cell migration, cell adhesion and transcription activation signaling processes (By similarity). Plays a role in regulating Rho-mediated dorsal closure during embryogenesis. {ECO:0000250, ECO:0000269|PubMed:10323867, ECO:0000269|PubMed:17507675}. | Drosophila melanogaster (Fruit fly) |
A1Z7Z9 | CP131_DROME | MDLCLKGSQINLATRQKTKPKYTSRSLTTLHNPCPHFRPRSANFLQQRSRSSPFLGRPQSADPKFGRRLSNYFVEKELRNGGKRQVSSNDLLKSLLEEPIKRSWLCRSTCNSSESDYSLHKRTPDSSEEGEQFLVNMPVGEKVKSYSSYSGNQGLSNGALLQRTAKPDLPGRVSFSKPNMHADLDSSDCDNDKQEVRPSISAPGPLTLPSFLSKVEQADPVGQKKSVHFGSTAAEGEVLAETYEYPKCPSENCTCSTRSSSTTSTNEASASDVKCACDAPSCRFMESSKQVEPTSPTPTLPKAPSSELDVIREYKQAVEGVQVVKNHLGTDTLNNIEILPNYLDKYASPTKEKQNNLSETKNMATNSSAVNNGSVVYRPVGNPRNFGAENNFLPAVQDDRRSFANGSSDGVINNYLKVASTPPFVGKKKENVKPASADPIARSSKSKVTKSTINPAPLGKMKKAISVGSLREERKLSEYNLDKVDSWMSMQDQKQYDGKHKPGLEDLDEAQDNDTASQLSLKSNEDSRDSTYDEIVSVIKEIEEDKKRDNFSEGIPSELNLNLDSRCETADTVTVSEGKVPESGDKYKDILAYLNNVESSCDKTLMETRRSIPDSNRSEVEFVVEPDVTDEVPKLSELLMLPNHQLARRVIALSLRANELANAIHMSKEHVFQLRGEKQKSLRAEKSTAAAKLRDQKKHYEEVVTRHQGFIEQLLKDKGSLCEKVAALTRRLESQNQAWEHRLETELARTKETTMAGEKIRRERWVRENTKKIKELTVKGLEAEINKMNCDHQREVTELKRTHQMQLLDALEEARTKHEQIETSIRESCAQDREAIIEKERTAIRERFERQLEEEQRTQAEQRQKLTEEFAAERDRLQSELRQRENEHQARRQEALREQEQELEQAKFEMQERMAKQEEKYQNRVNTIEQQYQADFELWKTEHENKTKLAQAEKENAIRQHYRAERDRQLDELVVRMEADALQHKEEHELKMNRLKEKYEKDLVLAESVEKSLREKYAETRGKLAEADAQVRNSQAEVKQLQLELSHSKKMCGDIIMERDRLRDNLNADIQSELGVLNERHKQEMDQLQKRVHQTIQRQEETIEILKGDNDALRQQCLKLNAVIRQQRKDYCVK | null | null | adult locomotory behavior [GO:0008344]; axoneme assembly [GO:0035082]; ciliary basal body-plasma membrane docking [GO:0097711]; ciliary transition zone assembly [GO:1905349]; cilium assembly [GO:0060271]; intraciliary transport [GO:0042073]; intraciliary transport involved in cilium assembly [GO:0035735]; non-motile cilium assembly [GO:1905515]; peripheral nervous system neuron development [GO:0048935]; protein localization to ciliary transition zone [GO:1904491]; regulation of centrosome duplication [GO:0010824]; sperm axoneme assembly [GO:0007288]; spermatogenesis [GO:0007283] | centriolar satellite [GO:0034451]; centriole [GO:0005814]; ciliary basal body [GO:0036064]; ciliary cap [GO:0061822]; ciliary transition zone [GO:0035869]; cytoplasm [GO:0005737]; pericentriolar material [GO:0000242] | null | null | null | CEP131 family | null | SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, microtubule organizing center, centrosome {ECO:0000269|PubMed:21750193}. Cytoplasm, cytoskeleton, cilium basal body {ECO:0000269|PubMed:21750193, ECO:0000269|PubMed:27646273}. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome, centriole {ECO:0000269|PubMed:27646273}. Note=Co-localizes with the pericentriolar material (PCM) protein cp190 at centrosomes in undifferentiated sensory neurons (PubMed:21750193, PubMed:27646273). Localizes to the ciliary base, including the basal body and transition zone in sensory neurons and germ cells (PubMed:21750193, PubMed:27646273). {ECO:0000269|PubMed:21750193, ECO:0000269|PubMed:27646273}. | null | null | null | null | null | FUNCTION: Cilium-specific protein with a role in cilium/flagellum formation (PubMed:21750193, PubMed:27646273). May be involved in transport of components into the growing cilium (PubMed:21750193). In germ cells and sensory neurons, plays a role with Cby in the building of the transition zone necessary for the formation of the ciliary cap and for the correct elongation of the axoneme (PubMed:27646273). {ECO:0000269|PubMed:21750193, ECO:0000269|PubMed:27646273}. | Drosophila melanogaster (Fruit fly) |
A1Z877 | NDG_DROME | MPTFGSKLLACLLLSSVILVSGQFEHYLDSLRASELYEFEDGSLGSIHLLPKGDSETIVLQLEQPIHFYGEQYEQLYINTNGILTFNSEFPEYLNQPFPLEYASIAAFYSNVDTSFSDEGTSISLFESKEQSILDRASSLVRYAFSSQSEFEARQVIVATWRNVGYFDSKTDRLNTFQVALIANEQSTFVQFIYPDGGLNWLQGETAGLGLPDIRAQAGFVAEDGRFYTLNGSGSENARFLSESTNLGVPGVWLFEVAPIENEQNVRSPDNAESLTESPALALSCQAHAHQCHEKAECHDKAEGYCCVCGSGFYGNGKSCLANDQPIRVTGTLTGELNKQPVSEEAKLQSYVVTSEGRTYTTINPLTPELGAQLRLVLPLLTTVPWLFAKSVGGVANGYQLTGGVYTHVSRLQFDSGENLHVNQTFEGLNYWDQLSVKIEIYGEVPAVAADAVLILPDYVEEYTFERPGELKSVQVLNINITEEQRVLGLQVEQRILYRSCLRDDEADPSATKVLQKISKVALDYVERDQALRIGAMSKVGVTPESNACNDGTADCVENSVCVPYEDTYRCDCYHGFAAQLDERGVEVCLDIDECATGSHVCDENAVCDNTEGGFNCYCTEGFEGNGYRCLSNSTADNIEYPPAVEGQAEPTSEPSPNPSPYPDQGQDQEREREDDQYPQPNPYPYPEEQIPQHPDECYRCSKDADCYQGRCTCHEGFDGDGYTCTNICGHGEVWENGRCEPLLLERHDVDPLCDALGECRCPYGYELSEDSQRCTYVQEFDGERNADLIPCDVDENCHINATCNWYGQELRHICTCQPGFRGDGYNCDPISDDSCAIRPDICDVHADCVYEEHLGKSECQCQAGYTGNGFNCQLAAECQSAEHCGENAFCDDGVCRCQADFERDVSDRCVPAGRCGSVFCGSNAICKWDSAEGVQYCDCLDGYQGDALTGCTSKPLSCHVLNNCGIHATCEPTEDPANYECQCIAGFKGDGYVCIEEQNCLNNPTLCDMNAQCRSTNSGLVCVCNQGFFGNGSLCQERQHQDSDFLIVSQGVMIARVPLNGRNVRPISVAQMAIGLDKDCVEGRVYWGDISTKKIVSTKYDGTDLRPFITTDIESPEGIAIDVISRRLYWADSAKDTIEVASLDDPSLRAVIINKQLVNPRGIAVDPYREKLFWSDWDRESPKIEMSNLDGTGRELLLGKDDVTLPNSLVVLENSGEVCYADAGTKKVECIEPQNRQIRTISNELSYPFGITFTHDQFYWTDWTTKKVEIVDSLGARQTPIQPPFFGSHKMYGMTVVEQHCPQYQSPCQISNGGCTDSRLCLVNRQAPSGKSCKCTSASTGCTVLAPGY | null | null | basement membrane assembly involved in embryonic body morphogenesis [GO:2001197]; basement membrane organization [GO:0071711]; cell-matrix adhesion [GO:0007160]; regulation of basement membrane organization [GO:0110011] | basement membrane [GO:0005604]; extracellular space [GO:0005615] | calcium ion binding [GO:0005509]; extracellular matrix structural constituent [GO:0005201] | PF12947;PF07645;PF07474;PF00058;PF06119; | 2.40.155.10;2.10.25.10;2.120.10.30; | null | null | SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:30260959}. Secreted, extracellular space, extracellular matrix, basement membrane {ECO:0000269|PubMed:30260959, ECO:0000269|PubMed:30567930}. Note=Secreted in the hemolymph (PubMed:30260959). Localization to the basal membranes depends on laminin (PubMed:30260959, PubMed:30567930). {ECO:0000269|PubMed:30260959, ECO:0000269|PubMed:30567930}. | null | null | null | null | null | FUNCTION: Cell adhesion glycoprotein which is widely distributed in basement membranes (PubMed:30260959, PubMed:30567930). Involved in cell-extracellular matrix (ECM) interactions probably by connecting the laminin and collagen IV networks (PubMed:30260959, PubMed:30567930). Required for permeability and mechanical stability of basement membranes, and ECM dependent neural plasticity (PubMed:30567930). Not involved in assembly of the embryonic basement membrane (PubMed:30567930). {ECO:0000269|PubMed:30260959, ECO:0000269|PubMed:30567930}. | Drosophila melanogaster (Fruit fly) |
A1Z8D0 | PWP1_DROME | MAEEGPPEPSIDFVPALCFVPRGVAKDRPDKIVLTQAELARIIGDTQQELDEESDDDAEEGENAEEDQNDMDVDDHADANSENRDPQDEFQFQEYDNEANANVTSLANIVDAGEQIPDEDEDSEAEDEVIKPSDNLILVGHVQDDAASMEVWVFNQEEEALYTHHDFLLPSFPLCIEWMNHDAGSEKAGNMCAIGCMDPIITVWDLDIQDAIEPTFKLGSKGSRKQNKEQYGHKDAVLDLSWNTNFEHILASGSVDQTVILWDMDEGQPHTTITAFGKQIQSLEFHPQEAQSILTGCADGYVRLFDCRDAEGVNSSSIEWKVDGEVEKVLWHPTQTDYFIVGTNDGTLHYADKRSPGQLLWSVKAHNEEISGVCFNNQKPNLLTSTSTEGTLKVWNFDGTEAKHVYEHEFNMGRLQCMRQCPEDPYTLAFGGEKPPRCAIFNIKNSIAVRRTFGIPDAE | null | null | cellular response to insulin stimulus [GO:0032869]; follicle cell of egg chamber development [GO:0030707]; germ cell development [GO:0007281]; male germ-line stem cell population maintenance [GO:0036098]; male gonad development [GO:0008584]; ovarian fusome organization [GO:0030723]; positive regulation of ribosome biogenesis [GO:0090070]; positive regulation of transcription by RNA polymerase III [GO:0045945]; positive regulation of transcription of nucleolar large rRNA by RNA polymerase I [GO:1901838]; regulation of gene expression [GO:0010468]; rRNA processing [GO:0006364] | chromosome [GO:0005694]; nucleolus [GO:0005730]; nucleoplasm [GO:0005654]; nucleus [GO:0005634] | chromatin DNA binding [GO:0031490] | PF00400; | 2.130.10.10; | WD repeat PWP1 family | PTM: Phosphorylated in response to nutrient-activated TORC1 signaling. {ECO:0000269|PubMed:29065309}. | SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:21752937}. Nucleus, nucleolus {ECO:0000269|PubMed:29065309}. Chromosome {ECO:0000269|PubMed:21752937}. Nucleus, nucleoplasm {ECO:0000269|PubMed:29065309}. Note=Co-localizes with active forms of RNA polymerase II (PubMed:21752937). Associates with open chromatin and chromosomal puffs of polytene chromosomes in larval salivary glands (PubMed:21752937). Nucleolar localization is controlled by mTORC1 signaling (PubMed:29065309). {ECO:0000269|PubMed:21752937, ECO:0000269|PubMed:29065309}. | null | null | null | null | null | FUNCTION: Chromatin-associated factor that regulates transcription (PubMed:21752937). Regulates Pol I-mediated rRNA biogenesis and, probably, Pol III-mediated transcription (PubMed:29065309). Regulates the localization to the nucleolus of Cdk7, a regulator of the Pol I-elongation factor TFIIH (PubMed:29065309). Acts as a regulator of cell proliferation and tissue growth as part of the TORC1 and Myc signaling pathway in response to nutrients (PubMed:29065309). Required in males for both germline stem cell (GSC) maintenance and early stages of germ cell differentiation of germ cell cysts (PubMed:21752937). Not required for female germline stem cell (GSC) maintenance, but necessary to regulate germ cell differentiation and egg chamber development (PubMed:21752937). In female somatic cells, required for follicle stem cell survival and maintenance (PubMed:21752937). {ECO:0000269|PubMed:21752937, ECO:0000269|PubMed:29065309}. | Drosophila melanogaster (Fruit fly) |
A1Z8N1 | TRE11_DROME | MSGRDNRGAGGGGGGHQPLSNAMGKLKEKLTRVGDELGYHRVESNLSTSNTATSLDTILPEDPFLFPQVSPQRHPQNTVRTQRLLEDEPPLSFRPLLEDDDINEPPTQQQQRTPLRASGSLELTPLPPPPTSLEIREHRDRQQRGAQGDELQRSKQSLKGSRVSFERRDTGNSNTNSNKAAESSDEDSFEEKRTGFQQQKATSVDHKGILKDLKHILANDNRRQFQAKKHVSLDVKGTRFLQDLLKESSSEEEFHKTRREFQGRKHQSLDPRVTFKLDKVLQGSSTDSDEEGEDAEHKRLIHRPKDITKPVIIDLKDLESESDEDFLTSRQHFQQQRSISTDSRKSRRLYEMDEMDNKRGENIRHAVPFVRQITEDGKPKLEVYRPTTNPIYIWTQVLAALSVSLGSLVVGFVSAYTSPALVSMTDRNITSFEVTQDAGSWVGGIMPLAGLAGGIAGGPLIEYLGRRNTILATAVPFIVSSLLIACAVNVAMVLCGRFLAGFCVGIASLSLPVYLGETVQPEVRGTLGLLPTAFGNIGILLCFVAGSFMNWSMLAFLGAALPVPFLILMFLIPETPRWFVGRGLEERARKALKWLRGKEADVEPELKGLMRSQADADRQASRNTMLELLKLNNLKPLSISLGLMFFQQFSGINAVIFYTVQIFKDAGSTIDGNLCTIIVGIVNFLATFIGIVLIDRAGRKILLYVSDIAMVLTLFVLGGFFYCKTYGPDVSHLGWLPLTCFVIYILGFSLGFGPIPWLMMGEILPAKIRGSAASVATAFNWFCTFVVTKTFQDLTVAMGAHGAFWLFGAICFVGLFFVIIYVPETQGKTLEDIERKMMGRVRRMSSVANIKPLSFNM | null | null | glucose transmembrane transport [GO:1904659]; transmembrane transport [GO:0055085]; trehalose transport [GO:0015771] | membrane [GO:0016020]; plasma membrane [GO:0005886] | glucose transmembrane transporter activity [GO:0005355]; transmembrane transporter activity [GO:0022857]; trehalose transmembrane transporter activity [GO:0015574] | PF00083; | 1.20.1250.20; | Major facilitator superfamily, Sugar transporter (TC 2.A.1.1) family, Trehalose transporter subfamily | null | SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:20035867}; Multi-pass membrane protein {ECO:0000255, ECO:0000269|PubMed:20035867}. | null | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=10.94 mM for trehalose {ECO:0000269|PubMed:20035867}; | null | null | null | FUNCTION: Low-capacity facilitative transporter for trehalose. Does not transport maltose, sucrose or lactose. Mediates the bidirectional transfer of trehalose. Responsible for the transport of trehalose synthesized in the fat body and the incorporation of trehalose into other tissues that require a carbon source, thereby regulating trehalose levels in the hemolymph. {ECO:0000269|PubMed:20035867}. | Drosophila melanogaster (Fruit fly) |
A1Z8P9 | TPR_DROME | MDLSGPQTLNNILQPDELKLVPEDVQKKLSEYINNFSDEYCKNRAAANRLAEAEQKKEELENKMEDYLVKFTSFELNVNELRTHLDQMSSERVNLMDTIAKGEQTISQLRKEKASVVEERDSMMKVIERQQAELERLKQDLHTYQQQLSSAIAAKCEAIARVDEIQSKEVALELKENRMESERDMLHKEILLISGDLNKSNAELQNIRREHTINTMQLQSCLKEKTESLKLMQEQYEQAVKTIGELTSKIEMQNDTAFKQNQATEEYVGKLKKELDAKEKLFEIFKSTESDHLIQREELLQGISEIKRLLEEAEEQCAQLTEQMETMKQKHSAELDEQNKKIQAMEQELASANDLLKQARESNLESAICQLAPSAAVASRLIRSDLSLTELYSMYAKSSEELEMRNCEIEQLKLQLKSIIAEISESAPILEKQNSDYQKMKETNSELLREHDELLQNKLCLERELERALSTLNHNQNENKKLKQTHTDLSRQVCMLLDELNCIRAGVKHVRIQPTRQLPTSESLISDNLVTFSSIEELVDRNTYLLNMSRELTELLEASEKNQDKMLLEQSKNHIRKLDARFAELEDLLTQKNNTVTTLLSKCDRYKKLYFAAQKKLGQNTVDLDDSNLEPNDSALDTSEQPAANFEESRKLEKRVRQLEQQLEGEVKKYASLKENYDYYTSEKRKNDALAQEQFDSMRKEVRELTSSNCKLMNTTEFQKEQIELLHKNIGTYKQQVTTLEERTKNYEKTIIKHEQTVHLLKDEMMAAHRKHAAADAEAQSLRQENRILRDTSSRLQIEKETYHREQQSQSLLLNSLEFIKTNLERSEMEGRQRLEQRLDDTVRELAAQRRHFQEEEEKFRESINEFKRQAETAIKLKDEEKQLADKWQAELTSVREELAEKVNKVNELSKKLQEVLTPTLNDNPITAANKRAREFELKLDQATVEIESLTKELAKTREHGEQFYKMSQSAESEIKRLHELHGELVAKQEEEIKKLRSSEAELKTRISDLEAEAMLSNVTEQSKTVNQSGQLKSAQDDLKSLLEKLTEANCTIRTLRSENTSLVESLNAAEVKYANGMIQHSADIQELTRYKAEFFKANDELNQLKSGRESLQAAYDELLRSNAEAQKLLDKEREESEKRVADLHALNSNLHDQIEALASKLAVLASQSQNPNSSLNESAMDGDQSLNASGLTAAEEGRNNEQLLKIIKFLRKEKDLFAAKLDILKAENARLISEHAIQQKKVDELNGYLNQERAKSQTDVVSANKHEEVLRKIETLNAITDSNRILREERNALTLRVAELTDRISSVEKELFPLQCSNKELTSKIEEINVENTSLRTEAIKWRQRANALVEKSNRNPEEFKRLQAEREHLAKLLTAEKELNKKQSDELTVLKQRMNTEIPMLNKQMQILDEARKKQVDEFTNLKQNNTRQTQDIMELKNRLLQKEEELLKANEELETKDKTIADKETKELQLRKLAKRYKDFYIGLQSQGGGTESAAELEKVRSELEEVNNQLRALKDEHEKITKECDEVKKRTEPETDTSAIRQEYKAKLDKLVVDLTVARTDLVNQETTFAGTKSSYDETIARLEKELQENIAANKDINQRLTRENESLHMRINQLTRQLGSQQSTKPSTSSVAEKGNISESSPRTANVKPMSGSATVQQSATVTPWRGGETPLASIRPISVQNSRTAAILPTSQQPPAGSSTSTSSSSSSSSTSTTSAAGGGSSAVAQTALVPPQQQVHTTGSAALESMASSSPTSSHTDYMPSTSSASVAVAAIPPMGASSAAESSQEAESIQHPQQNDSQLFVGGAQQQVVALVSPRVEGSSSSSSSTSVPTATAPSIQDGGSQSQQPSTSGSSSSSSTVVSSHSRHTPSSSNVTTTQAGCSSQGIKRPRDIEGDSSTGTEEGVAEKMSKITKRLRGPMHSGELSAGHIGDSGMDVDQMPTSSQRDQEDDIQVVDSDDEEDVLADADDGPIDGGEAEQEGYEDSYEQDNEMDDNEGGDDDNDIAVDAQDNNEVDIEVPEQHMQAQEESQSLDNQAIATASASTQENNQSQAITSGSGESSNPVTLPQAEASNWKQAAASTSTAAARRNESSVEIVSSPQVSNFCEQPARLESAEVDGTAEVAGGAPHESAGPSDTGAASASSPQKQSEAGESSGSDALKAADDGGDHADGTDNAREADEAFAEETMATGQGEDSQPLGNDNPNVGTSQSEVSHNQANLGEGNPTEDSEGADGVSSEGEKQAVGVEEEGREAEATSPSENTRFRTLRSAVPTRRGHRAMRGGSPNSQNRPQRIVWQRDTSPGNIQQNQMSANNNRFAQRTRNRRPIRRPPPNNFNNGGRFP | null | null | chromatin organization [GO:0006325]; chromatin remodeling [GO:0006338]; germ-line stem-cell niche homeostasis [GO:0060250]; male germ-line stem cell asymmetric division [GO:0048133]; mitotic spindle assembly checkpoint signaling [GO:0007094]; mitotic spindle elongation [GO:0000022]; mRNA export from nucleus [GO:0006406]; negative regulation of transcription by RNA polymerase II [GO:0000122]; positive regulation of cell division [GO:0051781]; positive regulation of intracellular protein transport [GO:0090316]; positive regulation of mitotic cell cycle spindle assembly checkpoint [GO:0090267]; positive regulation of mitotic nuclear division [GO:0045840]; positive regulation of transcription by RNA polymerase II [GO:0045944]; protein import into nucleus [GO:0006606]; regulation of DNA-templated transcription [GO:0006355]; regulation of metaphase plate congression [GO:0090235]; regulation of mitotic cell cycle [GO:0007346]; regulation of mitotic sister chromatid separation [GO:0010965]; regulation of mitotic spindle assembly [GO:1901673]; regulation of mitotic spindle organization [GO:0060236]; response to endoplasmic reticulum stress [GO:0034976]; response to heat [GO:0009408]; sex-chromosome dosage compensation [GO:0007549]; spindle assembly [GO:0051225] | chromosome, centromeric region [GO:0000775]; cytoplasm [GO:0005737]; euchromatin [GO:0000791]; metaphase plate [GO:0070090]; midbody [GO:0030496]; mitotic spindle [GO:0072686]; nuclear envelope [GO:0005635]; nuclear inclusion body [GO:0042405]; nuclear lamina [GO:0005652]; nuclear matrix [GO:0016363]; nuclear membrane [GO:0031965]; nuclear periphery [GO:0034399]; nuclear pore [GO:0005643]; nucleolus [GO:0005730]; nucleoplasm [GO:0005654]; nucleus [GO:0005634]; spindle [GO:0005819]; spindle matrix [GO:1990047]; spindle midzone [GO:0051233] | chromatin DNA binding [GO:0031490]; histone acetyltransferase binding [GO:0035035]; ribonucleoprotein complex binding [GO:0043021]; structural constituent of nuclear pore [GO:0017056] | PF07926; | null | TPR family | PTM: Mps1-mediated phosphorylation disrupts interaction with Mad1 during mitosis. {ECO:0000269|PubMed:31913420}. | SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:12027452, ECO:0000269|PubMed:15356261, ECO:0000269|PubMed:20174442, ECO:0000269|PubMed:22855526}. Nucleus matrix {ECO:0000269|PubMed:9152019}. Nucleus lamina {ECO:0000269|PubMed:15356261}. Nucleus envelope {ECO:0000269|PubMed:18562695, ECO:0000269|PubMed:9152019}. Nucleus membrane {ECO:0000269|PubMed:16543150, ECO:0000269|PubMed:22855526}; Peripheral membrane protein {ECO:0000305}; Nucleoplasmic side {ECO:0000269|PubMed:12027452}. Nucleus, nuclear pore complex {ECO:0000269|PubMed:12027452, ECO:0000269|PubMed:22855526, ECO:0000269|PubMed:31913420, ECO:0000269|PubMed:9152019}. Cytoplasm, cytoskeleton, spindle {ECO:0000269|PubMed:15356261, ECO:0000269|PubMed:18562695, ECO:0000269|PubMed:22855526}. Chromosome, centromere, kinetochore {ECO:0000269|PubMed:19273613}. Midbody {ECO:0000269|PubMed:15356261}. Note=In interphase, localized to the nucleoplasmic side of the nuclear pore complex (NPC) core structure, forming a fibrous structure called the nuclear basket (PubMed:15356261). Enriched at the nuclear lamina and at intranuclear spaces surrounding the chromosomes and the nucleolus (PubMed:15356261, PubMed:15962301). Colocalized with hnRNPs and snRNPs at a single heat shock puff during heat shock (PubMed:12027452). Reorganized during mitosis in a viscous and dynamic nuclear-derived spindle matrix that embeds the microtubule spindle apparatus from pole to pole in a microtubule-independent manner (PubMed:15356261). In prometaphase, localized at the spindle (PubMed:15356261). Localized to spindle midbody at telophase (PubMed:15356261). Recruited to the reforming nuclear envelope in early G1 (PubMed:15356261). Colocalized with Skeletor (Skel), Chro and east at the spindle matrix (PubMed:15356261, PubMed:15962301, PubMed:19273613, PubMed:22855526). Colocalized with Mad2 at the spindle matrix and kinetochore (PubMed:19273613). Associated with chromatin (PubMed:20174442). {ECO:0000269|PubMed:12027452, ECO:0000269|PubMed:15356261, ECO:0000269|PubMed:15962301, ECO:0000269|PubMed:19273613, ECO:0000269|PubMed:20174442, ECO:0000269|PubMed:22855526}. | null | null | null | null | null | FUNCTION: Component of the nuclear pore complex (NPC), a complex required for the trafficking across the nuclear envelope (PubMed:9152019). Functions as a scaffolding element in the nuclear phase of the NPC (PubMed:12027452, PubMed:15356261). Plays a role in chromosomal organization and gene expression regulation; stimulates transcription by promoting the formation of an open chromatin environment (PubMed:12027452, PubMed:20174442). Binds chromatin to nucleoporin-associated regions (NARs) that define transcriptionally active regions of the genome (PubMed:20174442). Associates with extended chromosomal regions that alternate between domains of high density binding with those of low occupancy (PubMed:20174442). Preferentially binds to NARs of the male X chromosome (PubMed:20174442). In males, together with Nup153, required for the localization of the male-specific lethal (MSL) histone acetyltransferase complex to the X chromosome and therefore for the transcription of dosage compensation genes (PubMed:16543150). In males, restrains dosage-compensated expression at the level of nascent transcription probably by interacting with the MSL complex and by modulating RNA Polymerase II phosphorylation status and activity (PubMed:34133927). During mitosis forms a gel-like spindle matrix complex together with Skeletor (Skel), Chro, east, and Asator embedding the microtubule spindle apparatus (PubMed:15356261, PubMed:15962301, PubMed:19273613, PubMed:22855526). During interphase localizes Mad1 to the nuclear pore complex and thereby might act as a scaffold to assemble the Mad1-C-Mad2 complex, an heterotetramer that catalyzes the structural conversion of open-Mad2 (O-Mad2) into closed-Mad2 (C-Mad2) which is essential for spindle-assembly checkpoint (SAC) (PubMed:31913420). During the metaphase-anaphase transition and before chromosome congression, is phosphorylated by Msp-1; this modification releases Mad1 from the nuclear pore complex and thereby promotes assembly of SAC ensuring a timely and effective recruitment of spindle checkpoint proteins like Mad1, Mad2 and Mps1 to unattached kinetochores (KT) (PubMed:22855526, PubMed:26714316, PubMed:31913420). In testes, has a role in stem cell asymmetric division and maintenance via regulation of mitotic spindle assembly checkpoint (SAC) complex (PubMed:26714316). {ECO:0000269|PubMed:12027452, ECO:0000269|PubMed:15356261, ECO:0000269|PubMed:15962301, ECO:0000269|PubMed:16543150, ECO:0000269|PubMed:19273613, ECO:0000269|PubMed:20174442, ECO:0000269|PubMed:22855526, ECO:0000269|PubMed:26714316, ECO:0000269|PubMed:31913420, ECO:0000269|PubMed:34133927, ECO:0000269|PubMed:9152019}. | Drosophila melanogaster (Fruit fly) |
A1Z8R8 | PARL_DROME | MLMSRALCRSWLPQVARRCHANVNVPILRINSGHPAARSCRQIHSNRKQSSNLKPTTGEPAAAEQNTPVPVNNVIKAVAFTGAFTVGCFAGATILEYENTRSLILEKARQARFGWWQSRSLADRDYWTQIKQDIRRHWDSLTPGDKMFAPILLCNLVAFAMWRVPALKSTMITYFTSNPAAKVVCWPMFLSTFSHYSAMHLFANMYVMHSFANAAAVSLGKEQFLAVYLSAGVFSSLMSVLYKAATSQAGMSLGASGAIMTLLAYVCTQYPDTQLSILFLPALTFSAGAGIKVLMGIDFAGVVMGWKFFDHAAHLGGAMFGIFWATYGAQIWAKRIGLLNYYHDLRRTKQK | 3.4.21.105 | null | mitochondrial fusion [GO:0008053]; protein processing [GO:0016485]; signal peptide processing [GO:0006465] | mitochondrial inner membrane [GO:0005743]; mitochondrion [GO:0005739] | endopeptidase activity [GO:0004175]; serine-type endopeptidase activity [GO:0004252] | PF01694; | 1.20.1540.10; | Peptidase S54 family | null | SUBCELLULAR LOCATION: Mitochondrion inner membrane {ECO:0000305|PubMed:16713954}; Multi-pass membrane protein {ECO:0000255}. | CATALYTIC ACTIVITY: Reaction=Cleaves type-1 transmembrane domains using a catalytic dyad composed of serine and histidine that are contributed by different transmembrane domains.; EC=3.4.21.105; Evidence={ECO:0000250|UniProtKB:P20350}; | null | null | null | null | FUNCTION: Mitochondrial intramembrane protease which plays a critical role in the regulation of mitochondrial function (PubMed:16713954, PubMed:21945938). Essential for mitochondrial development and fusion during spermatogenesis and the development of neurons and muscles (PubMed:16713954, PubMed:21945938). Essential for proteolytic processing of Pink1 and HtrA2 into their mature forms (PubMed:19048081). May also be involved, but not required, for the proteolytic processing of Opa1 (PubMed:19048081, PubMed:21945938). {ECO:0000269|PubMed:16713954, ECO:0000269|PubMed:19048081, ECO:0000269|PubMed:21945938}. | Drosophila melanogaster (Fruit fly) |
A1Z8X3 | RTTN_DROME | MSTKQSPALQLAEGQLTKLTSESEEIRMRALDQIETRFIRCLQLGEPIQFKPVLLLKQLIRWFGYTPPLVPDRVLAMIMELLRSEYAEAVIRKIPYERFKAELQKVRRVLHKQESKRVSELLDDMNLLLLEKYNIDRVTPSVSSLSSNDIPSQATESADSSSNQIYDNLKPEDYEPSWSHPCLDDVATMKSMIDLPRNSVELQLQLTELIIRMGDYPTEYFLQPPFVFLHLVQLQTMTDGSLIHVNRALIACLRLLQQRILLRRNTLSYADRFDPPSRPKQVKVVSALVILLENCMKLIRPLLFSCTNDNWHIMELIVEIVRTHDVLSSKIPLVSITLIADAVKSLLAYCNSVEGSCMTQLMDSLRIPRLQSLILNGVLHDMVALNINYDKRMDRRQAKALIQPIVLDSAYLSGMPERMKSLNTLISSLDSGPSPDEELIKLKRAYSVALNQLHPNTELTGSLLIQKYRQVCLVLVQLGSETLVKQLFGAVVKCIPFYAGNLKLRKDADELLYTLVDLPALKLRSLIYRLMIKSTVAHFHSFMNKTVYMTGCSNVDLIRQHILGVPLTPLLLRRMIIQSSEANTSERMQQWCLDYPIMIMKLNAILAPQDFSVVFPLLLPVLPLLISRSVTHKILHNVIWNVLEPDSSRLDPQLMLRGYVYFMFHPDGEVRSEATTTIAYVLQCQEQTNRYLPTASNVPVEHIANDLCIIQPPFCYRSIFIKCSDERFQGQRSLDALFRLLQAKDIKSNIRKSTMTQLNVLLRNWRACEEFSTKEDGYRLIMESLHNALKKGNDTDILLPTVSILMKLLFNDDEFRLEVANTFGVYTLLLRALFLFPHLEQLRQDVSICLFQMLFQNCITSTEDKLVLNANMEPLILPVTYEIEHKVIPTAVTEGLELQQNVEATHFGRDRAKAAQHWRLYMAYRVCQVPSSITLESVSALDIRESLKIKMADLALVRSSDLNEQLSCQFIAAENCSKHEDLQKTVSAIQLFLVVLRNSLSDTVAENLWKLIHKYIRLAPGNEADDKVYKSMLDLCVTCIRFSQPHAINGLSYALETDHHHSFQLLLHDSQISLDKLFLICQCMMQLLSNELSDDSMNWYGKFFMQLSAVAKTHFELRQLQHVRCILCMLRFVSERNLKFSNAQLMSYSQHFIQLSSNLRTSTQTGSEWQRDCLYIICQLQIHLIYQEPKASSKASIPNDVGASYKVLRYFLTLCGHGDSEVRALSWVSLANWITICGSQVAEILPRLDFLPGGLPACCLTTLTDAHEMMLIRELAGRVFILLMPLIGAESSLELLRKHDLLKTAYNSLKAIHDTPWMFKKIVGERHSCEVISCYVAICTKMVAMKPEWCAALCGHSLMSGLSDVMKKLKSQASCSIPLVELCASQICELYSMCYTNNFEFLKMTICRDSVFLQNYLTLINDVLSLECPEYMVIPLLKMFLIFCTDSNSNSFLIEQIKNKPSLFMDFFLFGLHVKLINSPFQRFTLSALSLVFTKAQLAAYDISMLSELEKFELAFSDPDIAKDGKQEFESKKKQSVSQCIYDESSDNSDDNKQRPNHAIQATNAAIIIFHRLDQLFDRYYLSKALNFLELPAVGQVQVCEALGELLKASTWAVKAAGESKLLGKVVHILDDFLNDEKIGNAAVYVKRVGPHKAQSIISNLLVLINMLSQWHSSPNSEIIQTSMAANIAKILIRIWPWLSHSYHLKKVTVQLIMFLTEHSFEMCKQISLLQSGHAQSLLHLMARVADFETTKKEIPNKEPSLNMVPALRVMVNCCCCTEGRLSLSKMNLLDMFDTILPANPCSTHLKVRPPVLIAWLGFWEVFSRYDVGGKACHLQSLINTIRRSPPLSHKRILCLRILRNMCFFNGNRPRLVELADFINLLRDILEQRVQKAPTSEKNGLNSFEEHRLAVLMLWKLFGFGAKYKGMLRGTKLFKLLIGLRVEMSVVFSEEENKYAGVPYANDLAKLLEKLMESMRQ | null | null | centriole assembly [GO:0098534]; centriole replication [GO:0007099]; centriole-centriole cohesion [GO:0010457]; centrosome cycle [GO:0007098]; ciliary basal body organization [GO:0032053] | centriole [GO:0005814]; centrosome [GO:0005813]; ciliary basal body [GO:0036064]; cytoplasm [GO:0005737]; ring centriole [GO:0061823] | null | PF14726; | null | Rotatin family | null | SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, microtubule organizing center, centrosome, centriole {ECO:0000269|PubMed:19948479, ECO:0000269|PubMed:32543652}. Note=Associated with the daughter centriole on mitotic entry (PubMed:32543652). Ana3 recruitment to the procentriole in interphase precedes the Rcd4 one (PubMed:32543652). Localizes to the basal bodies (PubMed:19948479). {ECO:0000269|PubMed:19948479, ECO:0000269|PubMed:32543652}. | null | null | null | null | null | FUNCTION: Participes in the structural integrity of both centrioles and basal bodies and in centriole cohesion (PubMed:19948479). Participates in the later stages of centriole assembly through the interaction with Rcd4 leading to the centriole to centrosome conversion (PubMed:32543652). {ECO:0000269|PubMed:19948479, ECO:0000269|PubMed:32543652}. | Drosophila melanogaster (Fruit fly) |
A1Z9E2 | LIN54_DROME | MDTSGGNLDSLDDTEPLPELSFEDFLEPTSEKSSQHMEIEALDSEEDNIGGEDLADPANDSLNTPQFKKNVVHILEDKRLNSSGLTVLKSHAIKMVTAGGTPPAKAQVTDVKILNKLKPIPSSTLKIGSTTIATKSTPGSITKTLGNLTQIRTKDGQVIFVQKSVPGTQSSTAVTGSPSGGIRRLVAPSGIQKAVLSKGVTMASTGLVKAAVPAKASTSVPGSAITLKGIQPLAGGTAKASTSSTTATTSPSLAQPNKIQVVRTADGKIIKINQAGPSLLVNAKQGTGTTVTPGGSAATSVKLSPSTGNVVLNKPVGQVVVRTETPVKTATGSVASASATPGKMLVQSGGKQILVSNKNIIKLSPNASATSSTTHTTGGQTPSTSSGLHAIQLPGKGGIQYVRVLNNNKSAAGTSATASIPKTVQTQKITVVRPPAATGVPATSTTTSAAAASPAAASKANLAMGNTNKIVMRSMGGSIVPLPSVQTLVSKRALGAISNASKPASAASSSATPSASQELPRKHRLTDLNVQLKQSASVSSEASDSSDAGPEAKKPRYVITMQQGSQKAASQPVQKLINRTANVQRVVSSSTSPSSNSTKKIYNYVQPTGSNGAKYMICNSGVPQSSTSAMRRGYTGYVENKTRRPPPISPQQHRFKQMGPQQQSKHQQLQAQAKQRIRQQQLPTEQSTPIKVEPKLPTLPPGVKANVPAKPLFEVLKPPATAAAAGAVDPLGGMTSRRKHCNCSKSQCLKLYCDCFANGEFCQDCTCKDCFNNLDYEVERERAIRSCLDRNPSAFKPKITAPNSGDMRLHNKGCNCKRSGCLKNYCECYEAKIPCSSICKCVGCRNMEDRPDVDMDSLDGLMGVEGQKKDKAKNKQLNENRANIYFTDDVIEATIMCMISRIVMHEKQNVAVEDMEREVMEEMGESLTQIIAFAKEKQETSQIDESKPSS | null | null | cell cycle [GO:0007049]; determination of adult lifespan [GO:0008340]; eggshell chorion gene amplification [GO:0007307]; flagellated sperm motility [GO:0030317]; negative regulation of transcription by RNA polymerase II [GO:0000122]; oogenesis [GO:0048477]; regulation of DNA-templated transcription [GO:0006355] | chromatin [GO:0000785]; Myb complex [GO:0031523]; nucleus [GO:0005634]; polytene chromosome [GO:0005700] | DNA binding [GO:0003677] | PF03638; | null | Lin-54 family | null | SUBCELLULAR LOCATION: Nucleus {ECO:0000305}. | null | null | null | null | null | FUNCTION: Component of the DREAM complex, a multiprotein complex that can both act as a transcription activator or repressor depending on the context. In follicle cells, the complex plays a central role in the site-specific DNA replication at the chorion loci. During development, the complex represses transcription of developmentally controlled E2F target genes. {ECO:0000269|PubMed:12490953, ECO:0000269|PubMed:15256498, ECO:0000269|PubMed:15479636, ECO:0000269|PubMed:18316477}. | Drosophila melanogaster (Fruit fly) |
A1Z9G2 | SYF1_DROME | MVTKTIKSLNLEINFEVEDVPYEEEILRNAYSVKHWLRYIDHKAKAPNNGVNMVYERALKELPGSYKIWHNYLRTRRKQVRGKIPTDPMYEEVNSAFERALVFMHKMPRIWMDYGAFMTSQCKITRTRHVFDRALRALPITQHGRIWPLYLQFVRRFEMPETALRVYRRYLKLFPEDTEEYVDYLQEADRLDEAAQQLAHIVDNEHFVSKHGKSNHQLWNELCDLISKNPHKVHSLNVDAIIRGGLRRYTDQLGHLWNSLADYYVRSGLFDRARDIYEEAIQTVTTVRDFTQVFDEYAQFEELSLNRRMEQVAANEAATEEDDIDVELRLSRFEYLMERRLLLLNSVLLRQNPHNVHEWHKRVTLYEDKPAEIISTYTEAVQTVQPKQAVGKLHTLWVEFAKFYEANGQVEDARVVFERGTEVEYVKVEDLAAVWCEWAEMELRQQQFEAALKLMQRATAMPKRKIAYYDDTETVQARLHRSLKVWSMYADLEESFGTFKTCKAVYERIIDLKICTPQIIINYGMFLEEHNYFEEAYRAYEKGISLFKWPNVYDIWNSYLTKFLERYGGTKLERARDLFEQCLDQCPPEHAKYFYLLYAKLEEEHGLARHAMSVYDRATSAVKEDEMFDMYNIFIKKAAEIYGLPRTREIYEKAIESLPEQNMRHMCVKFAELETKLGEVDRARAIYAHCSQVCDPRITADFWQTWKEFEVRHGNEDTMREMLRIKRSVQATYNTQVNMMAAQFLSTNNGAAADAGAGAGPDAMRLLEEKARQAAAESKQKPIEKAASNIMFVRGETQGGAKDKKDTVVNPDEIDIGDSDEDDEEEDDDEENEMTNENQASAAVTKTDEEGLVMKKLRFEQKAIPAKVFGSLKPSNQGDSDGE | null | null | cardioblast cell fate determination [GO:0007510]; generation of catalytic spliceosome for first transesterification step [GO:0000349]; Malpighian tubule morphogenesis [GO:0007443]; morphogenesis of an epithelium [GO:0002009]; mRNA splicing, via spliceosome [GO:0000398]; regulation of alternative mRNA splicing, via spliceosome [GO:0000381]; RNA splicing [GO:0008380] | catalytic step 2 spliceosome [GO:0071013]; nucleus [GO:0005634]; post-mRNA release spliceosomal complex [GO:0071014]; precatalytic spliceosome [GO:0071011]; Prp19 complex [GO:0000974]; U2-type catalytic step 2 spliceosome [GO:0071007] | null | PF13181; | 1.25.40.10; | Crooked-neck family | null | SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:24755291}. | null | null | null | null | null | FUNCTION: Subunit of the NTC(Nineteen)/Prp19 complex, which is part of the spliceosome (PubMed:24755291, PubMed:28087625). The complex participates in spliceosome assembly, its remodeling and is required for efficient spliceosome activation (PubMed:24755291, PubMed:28087625). Essential for efficient pre-mRNA splicing (PubMed:24755291, PubMed:28087625). In embryos, efficient pre-mRNA splicing of zygotic transcripts is essential during dynamic cellular processes that require rapid division and/or dramatic changes in gene expression such as blastoderm cellularization, tracheal branching morphogenesis, Malpighian morphogenesis and epidermal development (PubMed:10502111, PubMed:24755291, PubMed:28087625). Part of its role in promoting embryo tracheal development is also due to specifically splicing bnl transcripts which results in the activation of the BNL-FGF pathway (PubMed:28087625). {ECO:0000269|PubMed:10502111, ECO:0000269|PubMed:24755291, ECO:0000269|PubMed:28087625}. | Drosophila melanogaster (Fruit fly) |
A1Z9J4 | DJ1A_DROME | MLSVLRKSFPNGVTHAHRVIRCKSNQDKCAKNALIILAPGAEEMEFTISADVLRRGKILVTVAGLHDCEPVKCSRSVVIVPDTSLEEAVTRGDYDVVVLPGGLAGNKALMNSSAVGDVLRCQESKGGLIAAICAAPTALAKHGIGKGKSITSHPDMKPQLKELYCYIDDKTVVQDGNIITSRGPGTTFDFALKITEQLVGAEVAKEVAKAMLWTYKP | null | null | dopamine metabolic process [GO:0042417]; glycolate biosynthetic process [GO:0046295]; glyoxal metabolic process [GO:1903189]; mitochondrial ATP synthesis coupled electron transport [GO:0042775]; neuron cellular homeostasis [GO:0070050]; positive regulation of phosphatidylinositol 3-kinase/protein kinase B signal transduction [GO:0051897]; response to oxidative stress [GO:0006979] | cytoplasm [GO:0005737]; mitochondrion [GO:0005739]; nucleus [GO:0005634] | peroxiredoxin activity [GO:0051920]; protein deglycase activity [GO:0036524] | PF01965; | 3.40.50.880; | null | null | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:16203113}. Nucleus {ECO:0000269|PubMed:16203113}. Mitochondrion {ECO:0000269|PubMed:16203113}. | null | null | null | null | null | FUNCTION: Plays an important role in cell protection against oxidative stress and cell death acting as oxidative stress sensor (PubMed:16139213, PubMed:16139214, PubMed:20457924). Does not play a role in methylglyoxal detoxification (By similarity). {ECO:0000250|UniProtKB:Q99497, ECO:0000250|UniProtKB:Q9VA37, ECO:0000269|PubMed:16139213, ECO:0000269|PubMed:16139214, ECO:0000269|PubMed:20457924}. | Drosophila melanogaster (Fruit fly) |
Subsets and Splits