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
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A2VEI2 | MICU1_DROME | MSVLRFLVTRQALAALTRPRTLNIIQNPAQIAYASTLCNQNSNHNAKDLTKSSANLSLMQTRGHKRFGHQEEKTPSVTKYFHMFILSLFLISVMDWGKVKRMLTPKVDADAGQRPSSAADVNGEDKSSESESEDSEDEEAGSDLHLHEGKKIREKVGFRERKIIEYENRIRQFSTPDKVFRYFATIQVPVADDRHEVYMTPTDFLTSMTPGMKQPDGLGLDQYRRYDPKSVGEQLNLHLEKNSIFYKLGSYGLITFSDYIFLLTVLSISRRHFEIAFRMFDLNGDGDVDCEEFEMVATLVRQQTSMGTRHRDHANTGNTFKGVNSALITYFFGPNMDEKLTIEKFLDFQEQLQREILSLEFERKEPNDEGNITEADFAELLLAYAGYPLKKKQKKLKRVKRRFRDHGKGISKQDYLDFFHFLNNINDVDTALTFYHIAGASIDQQTLQHVAKTVAMVNLSDHVVDVVFTIFDENNDNQLSNKEFISVMKNRVQRGLEKPKDTGFLKMMRSVFKCAKETKPVLLDI | null | null | anesthesia-resistant memory [GO:0007615]; calcium import into the mitochondrion [GO:0036444]; medium-term memory [GO:0072375]; mitochondrial calcium ion homeostasis [GO:0051560]; positive regulation of mitochondrial calcium ion concentration [GO:0051561] | mitochondrial intermembrane space [GO:0005758]; uniplex complex [GO:1990246] | calcium ion binding [GO:0005509] | PF13202;PF13833; | 1.10.238.10; | MICU1 family, MICU1 subfamily | null | SUBCELLULAR LOCATION: Mitochondrion inner membrane {ECO:0000250|UniProtKB:Q9BPX6}; Single-pass membrane protein {ECO:0000255}. Mitochondrion intermembrane space {ECO:0000250|UniProtKB:Q9BPX6}. Note=The topology is subject to debate. {ECO:0000250|UniProtKB:Q9BPX6}. | null | null | null | null | null | FUNCTION: Key regulator of mitochondrial calcium uniporter (MCU) that senses calcium level via its EF-hand domains (Probable). During development, required in alpha/beta or gamma mushroom body neurons to support olfactory intermediate-term memory in the adult (PubMed:27568554). {ECO:0000269|PubMed:27568554, ECO:0000305|PubMed:27568554}. | Drosophila melanogaster (Fruit fly) |
A2VEY9 | APP_DROME | MNLLCCCCCSNMAPNQRVTRKWELFAGRNKFYCDGLLMSAPHTGVFYLTCILITGTSALFFAFDCPFLADSINPAIPIVGAVLYFFTMSSLLRTTFTDPGVIPRASNDEAAYIEKQIEVPNSLNSPTYRPPPRTKEVLVKGQTVKLKYCFTCKIFRPPRASHCSLCDNCVDRFDHHCPWVGNCVGKRNYRFFYLFLVSLAFLAVFIFSCSVTHLVLLMKKEHEVFNVIKAAPFTVIVVFICFFSIWSVIGLAGFHTYLTTSDQTTNEDLKGSFSSKGGPRTQNPYSRGNICLNCCHILCGPMTPSLIDRRGIATDEFIQQMQHQSSPRHALSDVLSASHMVTTSQPMMGGLGGGGIGGAGGGISIGGAELKPRFYDESNPSSSTLEGNGGAINGHGNGHGNGFDHPPPSYDLVQNGNSNSLAQLVDNEIPLVQMDIPAYTHQTATQARQYRHRHHKQRQICNGGTVSYENQLANASSEDELDDPDVVVVGSPEVVAAVAAIASNKAREMRNRSGSYSNLFDADFEAALVNSSLADNHVRGEGASSSGKPSAGAALLAAAISGKTENMYSNVLPVDNDTDPADSTLHVYSNIIDERKQQEQANNVLSSTLLCDDLDLDDPVSASCHVKRKSLGDGAEQVKSAERLRMLHDNTMIDTALDLDSLDGSSMGNNSQSCLVKSGKPNATSVTTNVAIV | 2.3.1.225 | null | establishment of body hair or bristle planar orientation [GO:0048104]; establishment of imaginal disc-derived wing hair orientation [GO:0001737]; pattern specification process [GO:0007389]; protein palmitoylation [GO:0018345]; protein targeting to membrane [GO:0006612] | apical cortex [GO:0045179]; apical plasma membrane [GO:0016324]; endoplasmic reticulum [GO:0005783]; endoplasmic reticulum membrane [GO:0005789]; Golgi apparatus [GO:0005794] | protein-cysteine S-palmitoyltransferase activity [GO:0019706] | PF01529; | null | DHHC palmitoyltransferase family, ERF2/ZDHHC9 subfamily | null | SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000269|PubMed:18719403}; Multi-pass membrane protein {ECO:0000255}. Apical cell membrane {ECO:0000269|PubMed:18804377}; Multi-pass membrane protein {ECO:0000255}. | CATALYTIC ACTIVITY: Reaction=hexadecanoyl-CoA + L-cysteinyl-[protein] = CoA + S-hexadecanoyl-L-cysteinyl-[protein]; Xref=Rhea:RHEA:36683, Rhea:RHEA-COMP:10131, Rhea:RHEA-COMP:11032, ChEBI:CHEBI:29950, ChEBI:CHEBI:57287, ChEBI:CHEBI:57379, ChEBI:CHEBI:74151; EC=2.3.1.225; Evidence={ECO:0000255|RuleBase:RU079119, ECO:0000269|PubMed:27692068}; | null | null | null | null | FUNCTION: Palmitoylates Dlish which is required for the apical cell cortex localization, total cellular level and full activity of dachs. {ECO:0000269|PubMed:18804377, ECO:0000269|PubMed:27692068}. | Drosophila melanogaster (Fruit fly) |
A2WV32 | CESA4_ORYSI | MMESGVPPCAACGDDAHAACRACSYALCKACLDEDAAEGRTTCARCGGEYGAPDPAHGQGAVVEEEVEESHEPVASGVRERVTMASQLSDHQDEGVHARTMSTHARTISSVSGVGSELNDESGKPIWKNRVESWKEKKKEKKASAKKAAAKAQAPPVEEQIMDEKDLTDAYEPLSRIIPISKNKLTPYRAVIIMRLVVLGLFFHYRITNPVYSAFGLWMTSVICEIWFGFSWILDQFPKWCPINRETYVDRLIARYGDGEDSGLAPVDFFVSTVDPLKEPPLITANTVLSILAVDYPVEKISCYVSDDGSAMLTFESLAETAEFARRWVPFCKKYSIEPRAPEFYFSQKIDYLKDKIHPSFVKERRAMKRDYEEYKVRINALVAKAQKTPEEGWIMQDGTPWPGNNPRDHPGMIQVFLGETGARDFDGNELPRLVYVSREKRPGYQHHKKAGAMNALVRVSAVLTNAPYILNLDCDHYVNNSKAVREAMCFMMDPSVGRDVCYVQFPQRFDGIDRSDRYANRNVVFFDVNMKGLDGLQGPVYVGTGCCFYRQALYGYGPPSLPALPKSSVCSWCCCCCPKKKAEKSEKEMHRDSRREDLESAIFNLREIDNYDEYERSMLISQMSFEKSFGLSSVFIESTLMENGGVPESANPSTLIKEAIHVISCGYEEKTEWGKEIGWIYGSVTEDILTGFKMHCRGWRSIYCMPIRPAFKGSAPINLSDRLHQVLRWALGSVEIFLSRHCPLWYGYGGGRLKWLQRLSYINTIVYPFTSLPLIAYCCLPAICLLTGKFIIPTLSNAATIWFLGLFISIIVTSVLELRWSGIGIEDWWRNEQFWVIGGVSAHLFAVFQGILKMIAGLDTNFTVTAKATDDTEFGELYVFKWTTVLIPPTSILVLNLVGVVAGFSDALNSGYESWGPLFGKVFFAMWVIMHLYPFLKGLMGRQNRTPTIVVLWSVLLASVFSLLWVKIDPFIGSSETTTTNSCANFDC | 2.4.1.12 | COFACTOR: Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000250|UniProtKB:Q941L0}; COFACTOR: Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000250|UniProtKB:Q9SWW6}; Note=Binds 2 Zn(2+) ions per subunit. {ECO:0000250|UniProtKB:Q9SWW6}; | cell wall organization [GO:0071555]; cellulose biosynthetic process [GO:0030244]; defense response to bacterium [GO:0042742]; defense response to fungus [GO:0050832]; plant-type primary cell wall biogenesis [GO:0009833]; plant-type secondary cell wall biogenesis [GO:0009834]; response to osmotic stress [GO:0006970]; response to water deprivation [GO:0009414] | plasma membrane [GO:0005886]; trans-Golgi network [GO:0005802] | cellulose synthase (UDP-forming) activity [GO:0016760]; metal ion binding [GO:0046872] | PF03552; | null | Glycosyltransferase 2 family, Plant cellulose synthase subfamily | null | SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}. | CATALYTIC ACTIVITY: Reaction=[(1->4)-beta-D-glucosyl](n) + UDP-alpha-D-glucose = [(1->4)-beta-D-glucosyl](n+1) + H(+) + UDP; Xref=Rhea:RHEA:19929, Rhea:RHEA-COMP:10033, Rhea:RHEA-COMP:10034, ChEBI:CHEBI:15378, ChEBI:CHEBI:18246, ChEBI:CHEBI:58223, ChEBI:CHEBI:58885; EC=2.4.1.12; Evidence={ECO:0000305}; | null | PATHWAY: Glycan metabolism; plant cellulose biosynthesis. | null | null | FUNCTION: Catalytic subunit of cellulose synthase terminal complexes ('rosettes'), required for beta-1,4-glucan microfibril crystallization, a major mechanism of the cell wall formation (By similarity). Involved in the secondary cell wall formation. {ECO:0000250|UniProtKB:Q9SWW6, ECO:0000269|PubMed:12970476, ECO:0000269|PubMed:18037139}. | Oryza sativa subsp. indica (Rice) |
A2X0M1 | MPK13_ORYSI | MEFFTEYGEASQYQIQEVVGKGSYGVVAAAVDTHTGERVAIKKINDVFEHVSDAIRILREIKVLRLLRHPDIVVIKHIMLPPTRREFRDIYVVFELMESDLHQVIEANHDLSPEHHRFFLYQLLCALKYIHSANVFHRDLKPKNILANSDCKLKICDFGLARVAFNDSPSTIFWTDYVATRWYRAPELCGSFFSKYTPAIDIWSIGCIFAEILTGRPLFPGRNVVHQLDLITDLLGTPSSETLSRIRNENARGYLTGMQRKHPIPFSHKFHNADPLALRLLERLLAFDPKDRPTAEEALADPYFRGISKLSREPSRLPVSKFEFEFERRKLTKDDVREMIYREILEYHPQMLQEYIRGGEQISFLYPSGVDRFKRQFAHLEENYSRGERSTPLRRQHASLPRERVCSSVDSNNQDSDNEERRAISSIARTMISPPRSQEKGKNRASAYPNGIINLNSNPKIYLKSASISASTCIIRGNKGPKENGISEDMEEVVYELSDNVTRMLS | 2.7.11.24 | null | phosphorylation [GO:0016310] | cytoplasm [GO:0005737]; nucleus [GO:0005634] | ATP binding [GO:0005524]; MAP kinase activity [GO:0004707]; protein serine kinase activity [GO:0106310] | PF00069; | 1.10.510.10; | Protein kinase superfamily, CMGC Ser/Thr protein kinase family, MAP kinase subfamily | PTM: Dually phosphorylated on Thr-175 and Tyr-177, which activates the enzyme. {ECO:0000250}. | null | CATALYTIC ACTIVITY: Reaction=ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-[protein]; Xref=Rhea:RHEA:17989, Rhea:RHEA-COMP:9863, Rhea:RHEA-COMP:11604, ChEBI:CHEBI:15378, ChEBI:CHEBI:29999, ChEBI:CHEBI:30616, ChEBI:CHEBI:83421, ChEBI:CHEBI:456216; EC=2.7.11.24; 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 | null | Oryza sativa subsp. indica (Rice) |
A2XDA1 | PDS_ORYSI | MDTGCLSSMNITGTSQARSFAGQLPTHRCFASSSIQALKSSQHVSFGVKSLVLRNKGKRFRRRLGALQVVCQDFPRPPLENTINFLEAGQLSSFFRNSEQPTKPLQVVIAGAGLAGLSTAKYLADAGHKPILLEARDVLGGKIAAWKDEDGDWYETGLHIFFGAYPNIQNLFGELGINDRLQWKEHSMIFAMPNKPGEFSRFDFPETLPAPLNGIWAILRNNEMLTWPEKVKFALGLLPAMVGGQAYVEAQDGFTVSEWMKKQGVPDRVNDEVFIAMSKALNFINPDELSMQCILIALNRFLQEKHGSKMAFLDGNPPERLCMPIVDHVRSLGGEVRLNSRIQKIELNPDGTVKHFALTDGTQITGDAYVFATPVDILKLLVPQEWKEISYFKKLEKLVGVPVINVHIWFDRKLKNTYDHLLFSRSSLLSVYADMSVTCKEYYDPNRSMLELVFAPAEEWVGRSDTEIIEATMQELAKLFPDEIAADQSKAKILKYHVVKTPRSVYKTIPDCEPCRPLQRSPIEGFYLAGDYTKQKYLASMEGAVLSGKLCAQSVVEDYKMLSRRSLKSLQSEVPVAS | 1.3.5.5 | COFACTOR: Name=FAD; Xref=ChEBI:CHEBI:57692; Evidence={ECO:0000269|PubMed:26147209, ECO:0000269|PubMed:28669634, ECO:0000269|PubMed:29176862}; | carotene biosynthetic process [GO:0016120]; carotenoid biosynthetic process [GO:0016117]; protein homotetramerization [GO:0051289] | chloroplast [GO:0009507]; chloroplast thylakoid [GO:0009534]; chromoplast [GO:0009509]; plastid membrane [GO:0042170] | FAD binding [GO:0071949]; phytoene dehydrogenase activity [GO:0016166] | PF01593; | 3.50.50.60; | Carotenoid/retinoid oxidoreductase family | null | SUBCELLULAR LOCATION: Plastid, chloroplast {ECO:0000250|UniProtKB:Q40406}. Plastid, chromoplast {ECO:0000250|UniProtKB:Q40406}. Membrane {ECO:0000269|PubMed:26147209}; Peripheral membrane protein {ECO:0000269|PubMed:26147209}. | CATALYTIC ACTIVITY: Reaction=15-cis-phytoene + 2 a plastoquinone = 9,9',15-tri-cis-zeta-carotene + 2 a plastoquinol; Xref=Rhea:RHEA:30287, Rhea:RHEA-COMP:9561, Rhea:RHEA-COMP:9562, ChEBI:CHEBI:17757, ChEBI:CHEBI:27787, ChEBI:CHEBI:48717, ChEBI:CHEBI:62192; EC=1.3.5.5; Evidence={ECO:0000269|PubMed:26147209, ECO:0000269|PubMed:29176862}; | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=1.3 mM for decylplastoquinone (DPQ) {ECO:0000269|PubMed:29176862}; KM=53.9 mM for phytoene {ECO:0000269|PubMed:29176862}; KM=66.8 mM for phytofluene {ECO:0000269|PubMed:29176862}; Vmax=28 nmol/min/mg enzyme with decylplastoquinone (DPQ) as substrate {ECO:0000269|PubMed:29176862}; Vmax=46.3 nmol/min/mg enzyme with phytoene as substrate {ECO:0000269|PubMed:29176862}; Vmax=48.4 nmol/min/mg enzyme with phytofluene as substrate {ECO:0000269|PubMed:29176862}; | PATHWAY: Carotenoid biosynthesis; lycopene biosynthesis. | BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 6.0. {ECO:0000269|PubMed:29176862}; | BIOPHYSICOCHEMICAL PROPERTIES: Temperature dependence: Optimum temperature is 37 degrees Celsius. {ECO:0000269|PubMed:29176862}; | FUNCTION: Converts phytoene into zeta-carotene via the intermediary of phytofluene by the symmetrical introduction of two double bonds at the C-11 and C-11' positions of phytoene with a concomitant isomerization of two neighboring double bonds at the C9 and C9' positions from trans to cis. Active with decylplastoquinone (DPQ) as substrate (PubMed:26147209, PubMed:29176862). Also active with other benzoquinones, which are strongly preferred over naphthoquinones as substrates (PubMed:26147209). {ECO:0000269|PubMed:26147209, ECO:0000269|PubMed:29176862}. | Oryza sativa subsp. indica (Rice) |
A2XE45 | NSHB2_ORYSI | MALVEGNNGVSGGAVSFSEEQEALVLKSWAIMKKDSANIGLRFFLKIFEVAPSASQMFSFLRNSDVPLEKNPKLKTHAMSVFVMLRKAGKVTVRDTTLKRLGATHFKYGVGDAHFEVTRFALLETIKEAVPVDMWSPAMKSAWSEAYNQLVAAIKQEMKPAE | 1.7.2.- | COFACTOR: Name=heme b; Xref=ChEBI:CHEBI:60344; Evidence={ECO:0000250|UniProtKB:P68168}; Note=Binds 1 heme group per subunit. {ECO:0000250|UniProtKB:P68168}; | cellular response to calcium ion starvation [GO:0072732]; cellular response to potassium ion starvation [GO:0051365]; response to abscisic acid [GO:0009737]; response to cold [GO:0009409]; response to nitrate [GO:0010167]; response to nitric oxide [GO:0071731]; response to nitrite [GO:0080033]; response to osmotic stress [GO:0006970]; response to salt [GO:1902074]; response to water deprivation [GO:0009414] | cytoplasm [GO:0005737]; nucleus [GO:0005634] | heme binding [GO:0020037]; metal ion binding [GO:0046872]; oxidoreductase activity [GO:0016491]; oxygen binding [GO:0019825]; oxygen carrier activity [GO:0005344] | PF00042; | 1.10.490.10; | Plant globin family | null | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:29044557}. Nucleus {ECO:0000269|PubMed:29044557}. | CATALYTIC ACTIVITY: Reaction=Fe(III)-heme b-[protein] + H2O + nitric oxide = Fe(II)-heme b-[protein] + 2 H(+) + nitrite; Xref=Rhea:RHEA:77711, Rhea:RHEA-COMP:18975, Rhea:RHEA-COMP:18976, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:16301, ChEBI:CHEBI:16480, ChEBI:CHEBI:55376, ChEBI:CHEBI:60344; Evidence={ECO:0000250|UniProtKB:O04986}; PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:77713; Evidence={ECO:0000250|UniProtKB:O04986}; | null | null | null | null | FUNCTION: Phytoglobin that reduces nitrite to nitric oxide under anoxic conditions (e.g. during flooding or in waterlogged soil) (By similarity). May not function as an oxygen storage or transport protein (By similarity). Has an unusually high affinity for O(2) through an hexacoordinate heme iron because of a very low dissociation constant (By similarity). Promotes tolerance to low potassium K(+) conditions (PubMed:29044557). {ECO:0000250|UniProtKB:O04986, ECO:0000250|UniProtKB:Q42831, ECO:0000269|PubMed:29044557}. | Oryza sativa subsp. indica (Rice) |
A2XE98 | NSHB1_ORYSI | MALVEDNNAVAVSFSEEQEALVLKSWAILKKDSANIALRFFLKIFEVAPSASQMFSFLRNSDVPLEKNPKLKTHAMSVFVMTCEAAAQLRKAGKVTVRDTTLKRLGATHLKYGVGDAHFEVVKFALLDTIKEEVPADMWSPAMKSAWSEAYDHLVAAIKQEMKPAE | 1.7.2.- | COFACTOR: Name=heme b; Xref=ChEBI:CHEBI:60344; Evidence={ECO:0000250|UniProtKB:P68168}; Note=Binds 1 heme group per subunit. {ECO:0000250|UniProtKB:P68168}; | cellular response to calcium ion starvation [GO:0072732]; cellular response to potassium ion starvation [GO:0051365]; response to abscisic acid [GO:0009737]; response to cold [GO:0009409]; response to osmotic stress [GO:0006970]; response to salt [GO:1902074]; response to water deprivation [GO:0009414] | cytoplasm [GO:0005737]; nucleus [GO:0005634] | heme binding [GO:0020037]; metal ion binding [GO:0046872]; oxidoreductase activity [GO:0016491]; oxygen binding [GO:0019825]; oxygen carrier activity [GO:0005344] | PF00042; | 1.10.490.10; | Plant globin family | null | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:29044557}. Nucleus {ECO:0000269|PubMed:29044557}. | CATALYTIC ACTIVITY: Reaction=Fe(III)-heme b-[protein] + H2O + nitric oxide = Fe(II)-heme b-[protein] + 2 H(+) + nitrite; Xref=Rhea:RHEA:77711, Rhea:RHEA-COMP:18975, Rhea:RHEA-COMP:18976, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:16301, ChEBI:CHEBI:16480, ChEBI:CHEBI:55376, ChEBI:CHEBI:60344; Evidence={ECO:0000250|UniProtKB:O04986}; PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:77713; Evidence={ECO:0000250|UniProtKB:O04986}; | null | null | null | null | FUNCTION: Phytoglobin that reduces nitrite to nitric oxide under anoxic conditions (e.g. during flooding or in waterlogged soil) (By similarity). May not function as an oxygen storage or transport protein (By similarity). Has an unusually high affinity for O(2) through an hexacoordinate heme iron because of a very low dissociation constant (By similarity). {ECO:0000250|UniProtKB:O04986, ECO:0000250|UniProtKB:Q42831}. | Oryza sativa subsp. indica (Rice) |
A2XE99 | NSHB3_ORYSI | MAANGSNVVSRGAVRFTEEQEALVLKSWAIMKNDSAHIGHRFFLKIFEVAPSARQLFSFLRNSDVPLEKNPKLKIHAMAVFVMTCEAAAQLRKTGRVTVRDTTIKRLGSTHFKNGVSDAHFEVAKFALLETIKEAVPASMWSPAMKGAWGEAYDHLVAAIKQGMKPAAA | 1.7.2.- | COFACTOR: Name=heme b; Xref=ChEBI:CHEBI:60344; Evidence={ECO:0000250|UniProtKB:P68168}; Note=Binds 1 heme group per subunit. {ECO:0000250|UniProtKB:P68168}; | cellular response to calcium ion starvation [GO:0072732]; response to abscisic acid [GO:0009737]; response to cold [GO:0009409]; response to salt [GO:1902074]; response to water deprivation [GO:0009414] | cytoplasm [GO:0005737]; nucleus [GO:0005634] | heme binding [GO:0020037]; metal ion binding [GO:0046872]; oxidoreductase activity [GO:0016491]; oxygen binding [GO:0019825]; oxygen carrier activity [GO:0005344] | PF00042; | 1.10.490.10; | Plant globin family | null | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:A2XE98}. Nucleus {ECO:0000250|UniProtKB:A2XE98}. | CATALYTIC ACTIVITY: Reaction=Fe(III)-heme b-[protein] + H2O + nitric oxide = Fe(II)-heme b-[protein] + 2 H(+) + nitrite; Xref=Rhea:RHEA:77711, Rhea:RHEA-COMP:18975, Rhea:RHEA-COMP:18976, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:16301, ChEBI:CHEBI:16480, ChEBI:CHEBI:55376, ChEBI:CHEBI:60344; Evidence={ECO:0000250|UniProtKB:O04986}; PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:77713; Evidence={ECO:0000250|UniProtKB:O04986}; | null | null | null | null | FUNCTION: Phytoglobin that reduces nitrite to nitric oxide under anoxic conditions (e.g. during flooding or in waterlogged soil) (By similarity). May not function as an oxygen storage or transport protein (By similarity). Has an unusually high affinity for O(2) through an hexacoordinate heme iron because of a very low dissociation constant (By similarity). {ECO:0000250|UniProtKB:O04986, ECO:0000250|UniProtKB:Q42831}. | Oryza sativa subsp. indica (Rice) |
A2XEA0 | NSHB4_ORYSI | MAFASASNGAVRFTEEQEALVLKSWAIMKDDSANIGHRFFLKIFEVAPSARHLFSFLRNSDVPLEKNPNLKKHAMAVFVMTCEAAAQLRKTGRVTVRDTTIKRLGSTHFKNGVSDTHFEVARFALLETIKDGIPASMWSPEMKNAWGEAYEHLVAAIKEGMKPVALL | 1.7.2.- | COFACTOR: Name=heme b; Xref=ChEBI:CHEBI:60344; Evidence={ECO:0000250|UniProtKB:P68168}; Note=Binds 1 heme group per subunit. {ECO:0000250|UniProtKB:P68168}; | cellular response to calcium ion starvation [GO:0072732]; response to abscisic acid [GO:0009737]; response to cold [GO:0009409]; response to salt [GO:1902074]; response to water deprivation [GO:0009414] | cytoplasm [GO:0005737]; nucleus [GO:0005634] | heme binding [GO:0020037]; metal ion binding [GO:0046872]; oxidoreductase activity [GO:0016491]; oxygen binding [GO:0019825]; oxygen carrier activity [GO:0005344] | PF00042; | 1.10.490.10; | Plant globin family | null | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:A2XE98}. Nucleus {ECO:0000250|UniProtKB:A2XE98}. | CATALYTIC ACTIVITY: Reaction=Fe(III)-heme b-[protein] + H2O + nitric oxide = Fe(II)-heme b-[protein] + 2 H(+) + nitrite; Xref=Rhea:RHEA:77711, Rhea:RHEA-COMP:18975, Rhea:RHEA-COMP:18976, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:16301, ChEBI:CHEBI:16480, ChEBI:CHEBI:55376, ChEBI:CHEBI:60344; Evidence={ECO:0000250|UniProtKB:O04986}; PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:77713; Evidence={ECO:0000250|UniProtKB:O04986}; | null | null | null | null | FUNCTION: Phytoglobin that reduces nitrite to nitric oxide under anoxic conditions (e.g. during flooding or in waterlogged soil) (By similarity). May not function as an oxygen storage or transport protein (By similarity). Has an unusually high affinity for O(2) through an hexacoordinate heme iron because of a very low dissociation constant (By similarity). {ECO:0000250|UniProtKB:O04986, ECO:0000250|UniProtKB:Q42831}. | Oryza sativa subsp. indica (Rice) |
A2XFC1 | TOP6A_ORYSI | MSEKKRRGGAGAGAASGSASKKPRVSTAASYAESLRSKLRPDASILATLRSLASACSKSKPAGSSSSSSSASKALAAEDDPAASYIVVADQDSASVTSRINRLVLAAARSILSGRGFSFAVPSRAASNQVYLPDLDRIVLVRRESARPFANVATARKATITARVLSLVHAVLRRGIHVTKRDLFYTDVKLFGDQAQSDAVLDDVSCMLGCTRSSLHVVASEKGVVVGRLTFADDGDRIDCTRMGVGGKAIPPNIDRVSGIESDALFILLVEKDAAFMRLAEDRFYNRFPCIILTAKGQPDVATRLFLRRLKVELKLPVLALVDSDPYGLKILSVYMCGSKNMSYDSANLTTPDIKWLGVRPSDLDKYRVPEQCRLPMTDHDIKVGKELLEEDFVKQNEGWVKELETMLRTRQKAEIQALSSFGFQYLTEVYLPLKLQQQDWI | 5.6.2.2 | COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000255|HAMAP-Rule:MF_03164}; | DNA topological change [GO:0006265]; meiotic DNA double-strand break formation [GO:0042138]; meiotic DNA double-strand break processing [GO:0000706]; reciprocal meiotic recombination [GO:0007131] | DNA topoisomerase type II (double strand cut, ATP-hydrolyzing) complex [GO:0009330]; nuclear chromosome [GO:0000228] | ATP binding [GO:0005524]; DNA binding [GO:0003677]; DNA topoisomerase type II (double strand cut, ATP-hydrolyzing) activity [GO:0003918]; magnesium ion binding [GO:0000287] | PF21180;PF20768;PF04406; | 3.40.1360.10;1.10.10.10; | TOP6A family | null | SUBCELLULAR LOCATION: Nucleus {ECO:0000255|HAMAP-Rule:MF_03164, ECO:0000269|PubMed:17116242}. | CATALYTIC ACTIVITY: Reaction=ATP-dependent breakage, passage and rejoining of double-stranded DNA.; EC=5.6.2.2; Evidence={ECO:0000255|HAMAP-Rule:MF_03164}; | null | null | null | null | FUNCTION: Component of the DNA topoisomerase VI involved in chromatin organization and progression of endoreduplication cycles. Relaxes both positive and negative superturns and exhibits a strong decatenase activity (By similarity). May be involved in cell proliferation and stress tolerance. {ECO:0000255|HAMAP-Rule:MF_03164}. | Oryza sativa subsp. indica (Rice) |
A2XFC8 | MPK5_ORYSI | MDGAPVAEFRPTMTHGGRYLLYDIFGNKFEVTNKYQPPIMPIGRGAYGIVCSVMNFETREMVAIKKIANAFNNDMDAKRTLREIKLLRHLDHENIIGIRDVIPPPIPQAFNDVYIATELMDTDLHHIIRSNQELSEEHCQYFLYQILRGLKYIHSANVIHRDLKPSNLLLNANCDLKICDFGLARPSSESDMMTEYVVTRWYRAPELLLNSTDYSAAIDVWSVGCIFMELINRQPLFPGRDHMHQMRLITEVIGTPTDDELGFIRNEDARKYMRHLPQYPRRTFASMFPRVQPAALDLIERMLTFNPLQRITVEEALDHPYLERLHDIADEPICLEPFSFDFEQKALNEDQMKQLIFNEAIEMNPNIRY | 2.7.11.24 | null | defense response [GO:0006952]; phosphorylation [GO:0016310] | cytoplasm [GO:0005737]; nucleus [GO:0005634] | ATP binding [GO:0005524]; MAP kinase activity [GO:0004707]; protein serine kinase activity [GO:0106310] | PF00069; | 1.10.510.10; | Protein kinase superfamily, CMGC Ser/Thr protein kinase family, MAP kinase subfamily | PTM: Dually phosphorylated on Thr-194 and Tyr-196, which activates the enzyme. {ECO:0000250}. | null | CATALYTIC ACTIVITY: Reaction=ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-[protein]; Xref=Rhea:RHEA:17989, Rhea:RHEA-COMP:9863, Rhea:RHEA-COMP:11604, ChEBI:CHEBI:15378, ChEBI:CHEBI:29999, ChEBI:CHEBI:30616, ChEBI:CHEBI:83421, ChEBI:CHEBI:456216; EC=2.7.11.24; 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: Involved in disease resistance and abiotic stress tolerance signaling pathways. {ECO:0000250}. | Oryza sativa subsp. indica (Rice) |
A2XID3 | AOC_ORYSI | MAAAAPSRVSVRAAAPGQTGGFAKIRPQVVVAAAARSAGVSGRRARSVRASLFSPKPATPKDARPAKVQEMFVYEINERDRESPAYLRLSAKQTENALGDLVPFTNKLYSGSLDKRLGISAGICILIQHVPERNGDRYEAIYSFYFGDYGHISVQGPYLTYEESYLAVTGGSGVFEGAYGQVKLNQIVFPFKIFYTFYLKGIPDLPRELLCTPVPPSPTVEPTPAAKATEPHACLNNFTN | 5.3.99.6 | null | auxin-activated signaling pathway [GO:0009734]; circadian rhythm [GO:0007623]; defense response to fungus [GO:0050832]; developmental vegetative growth [GO:0080186]; flower development [GO:0009908]; induced systemic resistance, jasmonic acid mediated signaling pathway [GO:0009864]; jasmonic acid biosynthetic process [GO:0009695]; photoperiodism, flowering [GO:0048573]; positive regulation of defense response to insect [GO:1900367]; response to abscisic acid [GO:0009737]; response to absence of light [GO:0009646]; response to blue light [GO:0009637]; response to ethylene [GO:0009723]; response to far red light [GO:0010218]; response to hydrogen peroxide [GO:0042542]; response to insect [GO:0009625]; response to metal ion [GO:0010038]; response to red light [GO:0010114]; response to salicylic acid [GO:0009751]; response to salt stress [GO:0009651]; response to vitamin B2 [GO:0033274]; response to wounding [GO:0009611]; unsaturated fatty acid biosynthetic process [GO:0006636] | chloroplast [GO:0009507] | allene-oxide cyclase activity [GO:0046423] | PF06351; | 2.40.480.10; | Allene oxide cyclase family | null | SUBCELLULAR LOCATION: Plastid, chloroplast {ECO:0000250|UniProtKB:Q9LS01}. | CATALYTIC ACTIVITY: Reaction=(9Z,13S,15Z)-12,13-epoxyoctadeca-9,11,15-trienoate = (9S,13S,15Z)-12-oxophyto-10-15-dienoate; Xref=Rhea:RHEA:22592, ChEBI:CHEBI:36438, ChEBI:CHEBI:57411; EC=5.3.99.6; Evidence={ECO:0000250|UniProtKB:Q75KD7}; | null | PATHWAY: Lipid metabolism; polyunsaturated fatty acid biosynthesis. {ECO:0000305}. | null | null | FUNCTION: Involved in the production of 12-oxo-phytodienoic acid (OPDA), a precursor of jasmonic acid (JA). Required for the production of JA in response to wounding. Necessary for flower and coleoptile development regulation by light, including blue (BL), red (RL) and far red (FR) lights. Involved in the auxin-mediated signaling pathway leading to growth stimulation. Essential for photodestruction of phyA upon activation by RL and FR. Implicated in responses to salt stress (NaCl). {ECO:0000250|UniProtKB:Q75KD7}.; FUNCTION: Confers resistance to incompatible strains of the blast fungus Magnaporthe grisea, jasmonic acid (JA) thus playing a significant role in the resistance to fungal infection. Implicated in riboflavin-induced resistance to the sheath blight Rhizoctonia solani. Required for Pseudomonas fluorescens-mediated JA-dependent induced systemic resistance (ISR). Confers some resistance, independently of the JA pathway but probably via OPDA accumulation, to brown planthopper (BPH, Nilaparvata lugens), a destructive, monophagous, piercing-sucking insect, mainly by reducing its feeding activity and survival rate. Triggers resistance to the chewing insect striped stem borer (SSB) Chilo suppressalis, to the root hemiparasite witchweed Striga hermonthica, and to the root feeder insect rice water weevil Lissorhoptrus oryzophilus, in a JA-dependent manner, by attenuating both the growth mass and growth rate of caterpillars. {ECO:0000250|UniProtKB:Q75KD7}. | Oryza sativa subsp. indica (Rice) |
A2XKG2 | RH10_ORYSI | MAKKKDVEVEELDEEVVAAAAAPAADGGEEQEAEPPARRPSTFAELGVVPELVAACDAMGWKEPTRIQAEAIPHALEGRDLIGLGQTGSGKTGAFALPIIQALLKQDKPQALFACVLSPTRELAFQIGQQFEALGSAIGLSCTVLVGGVDRVQQAVSLAKRPHIVVGTPGRLLDHLTDTKGFSLNKLKYLVLDEADKLLNVEFQKALDDILNVIPKERRTFLFSATMTNKVSKLQRACLRNPVKVEVASKYSTVDTLRQEFYFVPADYKDCFLVHVLNELPGSMIMIFVRTCESTRLLALTLRNLRFKAISISGQMSQDKRLGALNRFKTKDCNILICTDVASRGLDIQGVDVVINYDIPMNSKDYVHRVGRTARAGNTGYAVSLVNQYEAMWFKMIEKLLGYEIPDRKVDNAEIMILRERISDSKRIALTTMKEGGGHKKKRRKNEDDEEEEERNAPVSRKSKSFNKSRRR | 3.6.4.13 | null | rRNA processing [GO:0006364] | nucleolus [GO:0005730] | ATP binding [GO:0005524]; ATP hydrolysis activity [GO:0016887]; RNA binding [GO:0003723]; RNA helicase activity [GO:0003724] | PF00270;PF00271; | 3.40.50.300; | DEAD box helicase family, DDX47/RRP3 subfamily | null | SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:26848586}. Nucleus, nucleolus {ECO:0000269|PubMed:26848586}. Note=Localization is not affected by temperature. {ECO:0000269|PubMed:26848586}. | CATALYTIC ACTIVITY: Reaction=ATP + H2O = ADP + H(+) + phosphate; Xref=Rhea:RHEA:13065, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:456216; EC=3.6.4.13; Evidence={ECO:0000269|PubMed:26848586}; | null | null | null | null | FUNCTION: Has ATP-dependent RNA helicase activity in vitro. Acts as a thermosensitive RNA chaperone required for normal processing of pre-rRNA intermediates. Required for normal cell division at high temperatures. Required for a primary metabolism adaptation to high temperatures to support thermotolerant growth by regulating gene expression. Partially rescues the yeast rRNA helicase RRP3 mutant which has repressed cell proliferation at 38 degrees Celsius. {ECO:0000269|PubMed:26848586}. | Oryza sativa subsp. indica (Rice) |
A2XW02 | STRK1_ORYSI | MFTGCGLFACVRRCDGGDVRKRGEAGAMSSRVAADPAGVEEEGSCKNVAAASARQLAWADVESVTGGFSSRVIGHGGFSTVYLASLSSSRLGAVKVHCSSERLHRAFRQELEVLLSLRHPHIVRLLGYCDERDEGVLVFEYAPNGDLHERLHCSEVAGGVASVLPWARRVAIAFQVAMALEYLHESRHPAVIHGDIKASNVLLDANMNAKLCDFGFAHVGFSATVGCRPSARAVMGSPGYVDPHLIRSGVATKKSDVYSFGVLLLELVTGKEAVCRDTGRRLTAAVGPMLSEGKVADVVDRRLGGEHDGAEAAVMAELAMQCIGDSPGLRPSMADVVRALQEKTSALASAVGSRLDRKMMF | 2.7.12.1 | null | peptidyl-tyrosine phosphorylation [GO:0018108]; regulation of hydrogen peroxide metabolic process [GO:0010310]; regulation of response to oxidative stress [GO:1902882]; regulation of response to salt stress [GO:1901000]; response to cold [GO:0009409]; response to oxidative stress [GO:0006979]; response to salt [GO:1902074]; response to salt stress [GO:0009651]; response to water deprivation [GO:0009414] | plasma membrane [GO:0005886] | ATP binding [GO:0005524]; protein self-association [GO:0043621]; protein serine kinase activity [GO:0106310]; protein serine/threonine kinase activity [GO:0004674]; protein serine/threonine/tyrosine kinase activity [GO:0004712]; protein tyrosine kinase activity [GO:0004713] | PF00069; | 1.10.510.10; | Protein kinase superfamily, Ser/Thr protein kinase family | PTM: Palmitoylated. {ECO:0000250|UniProtKB:Q7XR88}.; PTM: Autophosphorylated. {ECO:0000250|UniProtKB:Q7XR88}. | SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:Q7XR88}; Lipid-anchor {ECO:0000250|UniProtKB:Q7XR88}. | 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=2.7.12.1; Evidence={ECO:0000250|UniProtKB:Q7XR88}; 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=2.7.12.1; Evidence={ECO:0000250|UniProtKB:Q7XR88}; 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=2.7.12.1; Evidence={ECO:0000250|UniProtKB:Q7XR88}; | null | null | null | null | FUNCTION: Acts probably as a dual specificity protein kinase (Probable). Regulates hydrogen peroxide (H(2)O(2)) homeostasis and improves salt tolerance by phosphorylating tyrosine residues of CATC thus activating its catalase activity. Promotes growth at the seedling stage and prevents grain yield loss under salt stress conditions (By similarity). {ECO:0000250|UniProtKB:Q7XR88, ECO:0000305}. | Oryza sativa subsp. indica (Rice) |
A2Y5T7 | SNAT1_ORYSI | MASAASASASAVVTPSSFRCVPTASCGLGARGKAPAPRRLLHDHAQGKKRAAATWSLKAGLWDSLRSGFLKSNNSTETVEPPSAPIEEEEPLPEELVLLERTLADGSTEQIIFSSAGDVNVYDLQALCDKVGWPRRPLTKIAASLRNSYLVATLHSVTTPSKAEGEERKQLIGMARATSDHAFNATIWDVLVDPSYQGQGLGKALMEKVIRTLLQRDISNITLFADNKVVDFYKNLGFEADPQGIKGMFWYPRF | 2.3.1.-; 2.3.1.87 | null | circadian rhythm [GO:0007623]; defense response to fungus [GO:0050832]; melatonin biosynthetic process [GO:0030187]; mucilage biosynthetic process involved in seed coat development [GO:0048354]; negative regulation of seed germination [GO:0010187]; photosynthetic state transition [GO:0062055]; protein quality control for misfolded or incompletely synthesized proteins [GO:0006515]; regulation of anthocyanin metabolic process [GO:0031537]; regulation of photoperiodism, flowering [GO:2000028]; regulation of starch metabolic process [GO:2000904]; regulation of stomatal closure [GO:0090333]; response to cold [GO:0009409]; response to high light intensity [GO:0009644]; response to hydrogen sulfide [GO:1904880]; response to mannitol [GO:0010555]; response to osmotic stress [GO:0006970]; seed oilbody biogenesis [GO:0010344]; serotonin metabolic process [GO:0042428]; thylakoid membrane organization [GO:0010027]; transport of virus in multicellular host [GO:0046739] | chloroplast [GO:0009507]; nucleus [GO:0005634] | aralkylamine N-acetyltransferase activity [GO:0004059]; lysine N-acetyltransferase activity, acting on acetyl phosphate as donor [GO:0004468] | PF00583; | 3.40.630.30; | null | null | SUBCELLULAR LOCATION: Plastid, chloroplast {ECO:0000250|UniProtKB:Q5KQI6}. Nucleus {ECO:0000250|UniProtKB:Q7X9V3}. | CATALYTIC ACTIVITY: Reaction=a 2-arylethylamine + acetyl-CoA = an N-acetyl-2-arylethylamine + CoA + H(+); Xref=Rhea:RHEA:20497, ChEBI:CHEBI:15378, ChEBI:CHEBI:55469, ChEBI:CHEBI:57287, ChEBI:CHEBI:57288, ChEBI:CHEBI:77827; EC=2.3.1.87; Evidence={ECO:0000250|UniProtKB:Q5KQI6}; | null | PATHWAY: Aromatic compound metabolism; melatonin biosynthesis; melatonin from serotonin: step 1/2. {ECO:0000305}. | null | null | FUNCTION: Catalyzes the N-acetylation of serotonin into N-acetylserotonin, the penultimate step in the synthesis of melatonin. Catalyzes in vitro the N-acetylation of tryptamine to produce N-acetyltryptamine, 5-methoxytryptamine to produce melatonin and tyramine to produce N-acetyltyramine (By similarity). Acetyltransferase required for geminivirus infection and systemic spread (By similarity). {ECO:0000250|UniProtKB:Q5KQI6, ECO:0000250|UniProtKB:Q7X9V3}. | Oryza sativa subsp. indica (Rice) |
A2Z1C8 | CESA9_ORYSI | MEASAGLVAGSHNRNELVLIRGHEEPKPLRALSGQVCEICGDEVGRTVDGDLFVACNECGFPVCRPCYEYERREGTQNCPQCKTRYKRLKGSPRVPGDEDEEDIDDLEHEFNIDDEKQKQLQQDQDGMQNSHITEAMLHGKMSYGRGPDDGDGNSTPLPPIITGARSVPVSGEFPISNSHGHGEFSSSLHKRIHPYPVSEPGSAKWDEKKEVSWKERMDDWKSKQGIVAGGAPDPDDYDADVPLNDEARQPLSRKVSIASSKVNPYRMVIILRLVVLGFFLRYRILHPVPDAIPLWLTSIICEIWFAVSWILDQFPKWYPIDRETYLDRLSLRYEREGEPSLLSAVDLFVSTVDPLKEPPLVTANTVLSILAVDYPVDKVSCYVSDDGASMLTFESLSETAEFARKWVPFCKKFSIEPRAPEFYFSQKVDYLKDKVHPNFVQERRAMKREYEEFKVRINALVAKAQKVPAEGWIMKDGTPWPGNNTRDHPGMIQVFLGHSGGHDTEGNELPRLVYVSREKRPGFQHHKKAGAMNALIRVSAVLTNAPFMLNLDCDHYINNSKAIREAMCFLMDPQVGRKVCYVQFPQRFDGIDVHDRYANRNTVFFDINMKGLDGIQGPVYVGTGCVFRRQALYGYNPPKGPKRPKMVTCDCCPCFGRKKRKHGKDGLPEAVAADGGMDSDKEMLMSQMNFEKRFGQSAAFVTSTLMEEGGVPPSSSPAALLKEAIHVISCGYEDKTDWGLELGWIYGSITEDILTGFKMHCRGWRSVYCMPKRAAFKGSAPINLSDRLNQVLRWALGSVEIFFSRHSPLLYGYKNGNLKWLERFSYINTTIYPFTSLPLLAYCTLPAVCLLTGKFIMPPISTFASLFFIALFISIFATGILEMRWSGVSIEEWWRNEQFWVIGGVSAHLFAVVQGLLKVLAGIDTNFTVTSKATGDEDDEFAELYAFKWTTLLIPPTTLLILNIIGVVAGVSDAINNGSEAWGPLFGKLFFAFWVIVHLYPFLKGLMGRQNRTPTIVVIWSVLLASIFSLLWVRIDPFTIKARGPDVRQCGINC | 2.4.1.12 | COFACTOR: Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000250|UniProtKB:Q941L0}; COFACTOR: Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000250|UniProtKB:Q9SWW6}; Note=Binds 2 Zn(2+) ions per subunit. {ECO:0000250|UniProtKB:Q9SWW6}; | cell wall organization [GO:0071555]; cellulose biosynthetic process [GO:0030244]; plant-type primary cell wall biogenesis [GO:0009833]; plant-type secondary cell wall biogenesis [GO:0009834] | plasma membrane [GO:0005886]; trans-Golgi network [GO:0005802] | cellulose synthase (UDP-forming) activity [GO:0016760]; metal ion binding [GO:0046872] | PF03552;PF14569; | 3.30.40.10; | Glycosyltransferase 2 family, Plant cellulose synthase subfamily | null | SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}. | CATALYTIC ACTIVITY: Reaction=[(1->4)-beta-D-glucosyl](n) + UDP-alpha-D-glucose = [(1->4)-beta-D-glucosyl](n+1) + H(+) + UDP; Xref=Rhea:RHEA:19929, Rhea:RHEA-COMP:10033, Rhea:RHEA-COMP:10034, ChEBI:CHEBI:15378, ChEBI:CHEBI:18246, ChEBI:CHEBI:58223, ChEBI:CHEBI:58885; EC=2.4.1.12; Evidence={ECO:0000305}; | null | PATHWAY: Glycan metabolism; plant cellulose biosynthesis. | null | null | FUNCTION: Catalytic subunit of cellulose synthase terminal complexes ('rosettes'), required for beta-1,4-glucan microfibril crystallization, a major mechanism of the cell wall formation (By similarity). Involved in the secondary cell wall formation. {ECO:0000250|UniProtKB:Q9SWW6, ECO:0000269|PubMed:12970476}. | Oryza sativa subsp. indica (Rice) |
A3BF39 | HMA2_ORYSJ | MAAEGGRCQKSYFDVLGICCPSEVPLVEKLLQPLEGVQKVTVIVPSRTVIVVHDVDAISQSQIVKALNQARLEASVRAYGNGSEKITNKWPSPYVLLCGLLLVVSLFEHFWHPLKWFALVAAAAGLPPIVLRSIAAIRRLTLDVNILMLIAVAGAIALKDYSEAGFIVFLFTTAEWLETRASHKATAGMSALMSMAPQKAILAETGEVVAARDVKVNTVIAVKAGEVIPIDGVVVDGRSEVDESTLTGESFPVSKQPDSQVWAGTLNIDGYIAVRTTAMADNSAVAKMARLVEEAQNSRSSTQRLIDTCAKYYTPAVVVMAGSVAAIPAIAKAHNLKHWFQLALVLLVSACPCALVLSTPIATFCALLRAARTGLLIKGGDVLESLASIKVAAFDKTGTITRGEFSVEEFQPVGERVSLQQLLYWVSSVESRSSHPMASVLVDYAQSKSVEPKSENVSEFQIYPGEGIYGEIDGAGIYIGNKRILSRASCETVPDMKDMKGVTIGYVACNNELIGVFTLSDACRTGSAEAIKELRSLGIKSVMLTGDSSAAATYAQNQLGNILAEVHAELLPEDKVRIVGELKEKDGPTLMVGDGMNDAPALAKADVGVSMGVSGSAVAMETSHVALMSNDIRRIPKAVRLARRTHRTIIVNIIFSVITKLAIVGLAFAGHPLIWAAVLADVGTCLLVIMYSMLLLREKDSRKAKKCAASHHGSPKKCCSSSHHGSHAKKNHGVSHHCSDGPCKSMVSCKESSVAKNACHDHHHEHNHHEEPAHKHSSNQHGCHDHSHGHSNCKEPSNQLITNKHACHDGHNHCADTSNLHDTKKHDCHGHEHSTCKEELNALPPTNDHACHGHEHSHCEEPVALHSTGEHACHEHEHEHIHCDEPIGSHCADKHACHDHEQVHEHHCCDEQQTPHTADLHPCHDHDHDNLEVEEVKDCHAEPPHHHNHCCHEPHDQVKNDTHPVQEHSISIEESSDHHEHHHNEEHKAEDCGHHPKPKDCAPPPTDCISRNCCSNTSKGKDICSSLHRDHHTSQASRCCRSYVKCSRPSRSCCSHSIVKLPEIVVE | 7.2.2.12; 7.2.2.21 | null | transmembrane transport [GO:0055085] | membrane [GO:0016020]; plasma membrane [GO:0005886] | ATP binding [GO:0005524]; ATP hydrolysis activity [GO:0016887]; metal ion binding [GO:0046872]; P-type cadmium transporter activity [GO:0008551]; P-type zinc transporter activity [GO:0016463]; transmembrane transporter activity [GO:0022857] | PF00122;PF00702; | 3.30.70.100;3.40.1110.10;2.70.150.10;3.40.50.1000; | Cation transport ATPase (P-type) (TC 3.A.3) family, Type IB subfamily | null | SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:22123790, ECO:0000269|PubMed:22548273, ECO:0000269|PubMed:23575418}; Multi-pass membrane protein {ECO:0000255}. | CATALYTIC ACTIVITY: Reaction=ATP + H2O + Zn(2+)(in) = ADP + H(+) + phosphate + Zn(2+)(out); Xref=Rhea:RHEA:20621, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:29105, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:456216; EC=7.2.2.12; Evidence={ECO:0000269|PubMed:22123790}; CATALYTIC ACTIVITY: Reaction=ATP + Cd(2+)(in) + H2O = ADP + Cd(2+)(out) + H(+) + phosphate; Xref=Rhea:RHEA:12132, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:48775, ChEBI:CHEBI:456216; EC=7.2.2.21; Evidence={ECO:0000269|PubMed:22123790}; | null | null | null | null | FUNCTION: Zinc/cadmium transporter that plays an essential role in promoting translocation of zinc and cadmium from roots to shoots (PubMed:21388416, PubMed:22123790, PubMed:22548273, PubMed:23575418). May control cadmium loading into xylem (PubMed:21388416). In roots, transports zinc and cadmium from the apoplast to the symplast to facilitate translocation via the phloem. In nodes, functions to load zinc and cadmium to the phloem for the preferential distribution to the upper nodes and panicles (PubMed:23575418). {ECO:0000269|PubMed:21388416, ECO:0000269|PubMed:22123790, ECO:0000269|PubMed:22548273, ECO:0000269|PubMed:23575418}. | Oryza sativa subsp. japonica (Rice) |
A3BLS0 | GH38_ORYSI | MAVMTDVSTTGTALRTPAAGAVKEGDVEKLRFIDEMTTNVDAVQERVLGEILGRNAGTEYLTKCGLDGATDRAAFRAKVPVVSYDDLQPYIQRIANGDRSPILSTHPVSEFLTSSGTSAGERKLMPTIMDELDRRQLLYSLLMPVMNLYVPGLDKGKGLYFLFVKSETKTPGGLTARPVLTSYYKSDHFKNRPYDPYHNYTSPTAAILCADAFQSMYAQMVCGLCQRNDVLRLGAVFASGLLRAIRFLQLNWEQLADDIESGELTPRVTDPSVREAVAAILLPDPELAKLIRAECSKGDWAGIITRVWPNTKYLDVIVTGAMAQYIPTLEFYSGGLPMACTMYASSECYFGLNLRPMCDPSEVSYTIMPNMGYFEFLPVDETGAASGDATQLVDLARVEVGREYELVITTYAGLNRYRVGDVLRVTGFHNAAPQFRFVRRKNVLLSIESDKTDEAELQRAVERASALLRPHGASVVEYTSQACTKRIPGHYVIYWELLTKGAGATVVDADTLGRCCLEMEEALNTVYRQSRVADGSIGPLEIRVVRPGTFEELMDYAISRGASINQYKVPRCVTFPPIVELLDSRVVSSHFSPALPHWTPARRSE | 6.3.2.- | null | auxin biosynthetic process [GO:0009851]; defense response [GO:0006952]; intracellular auxin homeostasis [GO:0140964]; pollen development [GO:0009555]; regulation of defense response to bacterium [GO:1900424] | cytoplasm [GO:0005737] | AMP binding [GO:0016208]; indole-3-acetic acid amido synthetase activity [GO:0010279] | PF03321; | null | IAA-amido conjugating enzyme family | null | null | null | null | null | null | null | FUNCTION: Catalyzes the synthesis of indole-3-acetic acid (IAA)-amino acid conjugates, providing a mechanism for the plant to cope with the presence of excessive free auxin (PubMed:18192436). Produces more IAA-Asp levels than IAA-Ala levels in vitro (PubMed:18192436). May participate in the activation of disease resistance by preventing the accumulation of free IAA, which reduces the expression of a group of auxin-responsive genes encoding expansins that control cell wall loosening and expansion (PubMed:18192436). Contributes to late events in stamen and carpel differentiation, and influences floret fertility (PubMed:22016342). {ECO:0000269|PubMed:18192436, ECO:0000269|PubMed:22016342}. | Oryza sativa subsp. indica (Rice) |
A3BMZ5 | BGL26_ORYSJ | MRKFIAALRLALAAAAHLLLTLPPAQCYWLNPEIYDAGGLSRRAFPEGFVFGTAASAYQVEGMAKQGGRGPSIWDAFIEKPGTIPNNATADVTVDEYHRYKEDVNIMKNMGFDAYRFSISWSRIFPNGTGMVNQEGVDYYNRLIDYMVKKGIKPYANLYHYDLPLALHEQYLGWLSPNIVEAFADYADFCFQTFGDRVKDWFTFNEPRCVAALGYDNGFHAPGRCSGCDAGGNSTTEPYLAAHHLILSHAAAVKRYREKYQLYQKGRIGILLDFVWYEPFSDSNADRAAAQRARDFHLGWFLDPIIHGRYPYSMLEIVKDRMPTFSDEESRMVKDSIDYVGINHYTSFYMKDPGPWNLTPTSYQDDWHVGFAYERNGVPIGAQANSYWLYIVPWGINKAVTYVKETYGNPTMILSENGMDQPGNVSITQGVHDTVRIRYYRNYITELKKAIDDGAKVIGYFAWSLLDNFEWRLGYTSRFGIVYVDYKTLKRYPKDSAFWFKNMLSSKKRN | 3.2.1.21 | null | carbohydrate metabolic process [GO:0005975] | null | beta-D-fucosidase activity [GO:0033907]; beta-galactosidase activity [GO:0004565]; beta-glucosidase activity [GO:0008422]; beta-L-arabinosidase activity [GO:0047701]; beta-mannosidase activity [GO:0004567]; cellobiose glucosidase activity [GO:0080079]; glucan exo-1,3-beta-glucosidase activity [GO:0004338]; scopolin beta-glucosidase activity [GO:0102483] | PF00232; | 3.20.20.80; | Glycosyl hydrolase 1 family | null | null | CATALYTIC ACTIVITY: Reaction=Hydrolysis of terminal, non-reducing beta-D-glucosyl residues with release of beta-D-glucose.; EC=3.2.1.21; Evidence={ECO:0000269|PubMed:19766588}; | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=0.27 mM for p-nitrophenyl beta-D-glucoside (at pH 5.0) {ECO:0000269|PubMed:19766588}; KM=0.52 mM for p-nitrophenyl beta-D-mannoside (at pH 5.0) {ECO:0000269|PubMed:19766588}; KM=19.6 mM for cellobiose (at pH 5.0) {ECO:0000269|PubMed:19766588}; KM=0.52 mM for cellotriose (at pH 5.0) {ECO:0000269|PubMed:19766588}; KM=0.09 mM for cellotetraose (at pH 5.0) {ECO:0000269|PubMed:19766588}; KM=0.06 mM for cellopentaose (at pH 5.0) {ECO:0000269|PubMed:19766588}; KM=0.05 mM for cellohexaose (at pH 5.0) {ECO:0000269|PubMed:19766588}; KM=0.86 mM for laminaribiose (at pH 5.0) {ECO:0000269|PubMed:19766588}; KM=8.7 mM for laminaritriose (at pH 5.0) {ECO:0000269|PubMed:19766588}; | null | null | null | FUNCTION: Hydrolyzes p-nitrophenyl beta-D-glucoside, p-nitrophenyl beta-D-mannoside, p-nitrophenyl beta-D-galactoside, p-nitrophenyl beta-D-xyloside, p-nitrophenyl beta-D-fucoside, p-nitrophenyl beta-L-arabinoside, cello-oligosaccharides, laminari-oligosaccharides and sophorose. {ECO:0000269|PubMed:19766588}. | Oryza sativa subsp. japonica (Rice) |
A3BV95 | BCL1_ORYSJ | MADFSPHHSLLLKATAAGAAIATTNDPNISSFFLYNHSHGSQAPQPANAAAAAIVEDASLESSVSAVLDTSPSVDRKRKAAEDSAHSKDSCKDGKSRRGKKASKEVEEKSTTEDEPPKGYIHVRARRGQATDSHSLAERVRRERISERMRMLQALVPGCDKVTGKALILDEIINYVQSLQNQVEFLSMRIASMSPVLYGFGMDSDGLHDQKIGGMFQEALAMPNPVLNQSSPAPSQAIMDTTSTTSYSLQSQHGAISFSQDNGSYLMQAVGEPRQQEMLNQLVFNNMCSFQ | null | null | gibberellic acid mediated signaling pathway [GO:0009740]; positive regulation of gibberellin biosynthetic process [GO:0010372]; regulation of unidimensional cell growth [GO:0051510] | nucleus [GO:0005634] | DNA-binding transcription factor activity [GO:0003700]; protein dimerization activity [GO:0046983] | PF00010; | 4.10.280.10; | BHLH protein family | null | SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00768, ECO:0000255|PROSITE-ProRule:PRU00981, ECO:0000269|PubMed:34360554}. | null | null | null | null | null | FUNCTION: Together with BCL2, positive regulator of cell elongation at least partially through increased gibberellic acid (GA) biosynthesis. {ECO:0000269|PubMed:34360554}. | Oryza sativa subsp. japonica (Rice) |
A3DD66 | ENG1_ACET2 | MPPGAKVPQAEIYKTSNLQGAVPTNSWESSILWNQYSLPIYAHPLTFKFKAEGIEVGKPALGGSGIAYFGAHKNDFTVGHSSVYTFPDARADKISDFAVDAVMASGSGSIKATLMKGSPYAYFVFTGGNPRIDFSGTPTVFYGDSGSQCLGVTINGVNYGLFAPSGSKWQGIGTGTITCILPAGKNYFSIAVLPDNTVSTLTYYKDYAYCFVTDTKVEWSYNETESTLTTTFTAEVSVKEGTNKGTILALYPHQWRNNPHILPLPYTYSTLRGIMKTIQGTSFKTVYRYHGILPNLPDKGTYDREALNRYINELALQADAPVAVDTYWFGKHLGKLSCALPIAEQLGNISAKDRFISFMKSSLEDWFTAKEGETAKLFYYDSNWGTLIGYPSSYGSDEELNDHHFHYGYFLHAAAQIALRDPQWASRDNWGAMVELLIKDIANWDRNDTRFPFLRNFDPYEGHSWASGHAGFADGNNQESSSEAINAWQAIILWGEATGNKTIRDLGIYLYTTEVEAVCNYWFDLYKDIFSPSYGHNYASMVWGGKYCHEIWWNGTNSEKHGINFLPITAASLYLGKDPNYIKQNYEEMLRECGTSQPPNWKDIQYMYYALYDPAAAKNMWNESIVPEDGESKAHTYHWICNLDSLGLPDFSVTADTPLYSVFNKNNIRTYVVYNASSSAKKVTFSDGKVMTVGPHSMAVSTGSESEVLAGDLNGDGKINSTDISLMKRYLLKQIVDLPVEDDIKAADINKDGKVNSTDMSILKRVILRNYPL | 3.2.1.39 | COFACTOR: Name=Ca(2+); Xref=ChEBI:CHEBI:29108; Evidence={ECO:0000269|PubMed:29870811, ECO:0007744|PDB:6FOP}; COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000269|PubMed:29870811, ECO:0007744|PDB:6FOP}; | cell wall organization [GO:0071555]; polysaccharide catabolic process [GO:0000272] | cell surface [GO:0009986]; extracellular region [GO:0005576] | calcium ion binding [GO:0005509]; glucan endo-1,3-beta-D-glucosidase activity [GO:0042973]; glucan endo-1,3-beta-glucanase activity, C-3 substituted reducing group [GO:0052861]; magnesium ion binding [GO:0000287]; nickel cation binding [GO:0016151] | PF00404;PF17652; | 1.10.1330.10; | Glycosyl hydrolase 81 family | null | SUBCELLULAR LOCATION: Secreted {ECO:0000250|UniProtKB:Q47N06}. | CATALYTIC ACTIVITY: Reaction=Hydrolysis of (1->3)-beta-D-glucosidic linkages in (1->3)-beta-D-glucans.; EC=3.2.1.39; Evidence={ECO:0000269|PubMed:29870811}; | null | null | BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 7. {ECO:0000269|PubMed:29870811}; | BIOPHYSICOCHEMICAL PROPERTIES: Temperature dependence: Optimum temperature is 75 degrees Celsius. {ECO:0000269|PubMed:29870811}; | FUNCTION: Cleaves internal linkages in 1,3-beta-glucan (PubMed:29870811). May contribute to plant biomass degradation (By similarity). {ECO:0000250|UniProtKB:Q47N06, ECO:0000269|PubMed:29870811}. | Acetivibrio thermocellus (strain ATCC 27405 / DSM 1237 / JCM 9322 / NBRC 103400 / NCIMB 10682 / NRRL B-4536 / VPI 7372) (Clostridium thermocellum) |
A3DH67 | GUNS_ACET2 | MVKSRKISILLAVAMLVSIMIPTTAFAGPTKAPTKDGTSYKDLFLELYGKIKDPKNGYFSPDEGIPYHSIETLIVEAPDYGHVTTSEAFSYYVWLEAMYGNLTGNWSGVETAWKVMEDWIIPDSTEQPGMSSYNPNSPATYADEYEDPSYYPSELKFDTVRVGSDPVHNDLVSAYGPNMYLMHWLMDVDNWYGFGTGTRATFINTFQRGEQESTWETIPHPSIEEFKYGGPNGFLDLFTKDRSYAKQWRYTNAPDAEGRAIQAVYWANKWAKEQGKGSAVASVVSKAAKMGDFLRNDMFDKYFMKIGAQDKTPATGYDSAHYLMAWYTAWGGGIGASWAWKIGCSHAHFGYQNPFQGWVSATQSDFAPKSSNGKRDWTTSYKRQLEFYQWLQSAEGGIAGGATNSWNGRYEKYPAGTSTFYGMAYVPHPVYADPGSNQWFGFQAWSMQRVMEYYLETGDSSVKNLIKKWVDWVMSEIKLYDDGTFAIPSDLEWSGQPDTWTGTYTGNPNLHVRVTSYGTDLGVAGSLANALATYAAATERWEGKLDTKARDMAAELVNRAWYNFYCSEGKGVVTEEARADYKRFFEQEVYVPAGWSGTMPNGDKIQPGIKFIDIRTKYRQDPYYDIVYQAYLRGEAPVLNYHRFWHEVDLAVAMGVLATYFPDMTYKVPGTPSTKLYGDVNDDGKVNSTDAVALKRYVLRSGISINTDNADLNEDGRVNSTDLGILKRYILKEIDTLPYKN | 3.2.1.176 | null | cellulose catabolic process [GO:0030245] | extracellular region [GO:0005576] | cellulase activity [GO:0008810]; cellulose 1,4-beta-cellobiosidase activity (reducing end) [GO:0102252]; metal ion binding [GO:0046872] | PF00404;PF02011; | 1.50.10.10;1.10.1330.10;2.170.160.10;4.10.870.10; | Glycosyl hydrolase 48 (cellulase L) family | null | SUBCELLULAR LOCATION: Secreted. | CATALYTIC ACTIVITY: Reaction=Hydrolysis of (1->4)-beta-D-glucosidic linkages in cellulose and similar substrates, releasing cellobiose from the reducing ends of the chains.; EC=3.2.1.176; Evidence={ECO:0000269|PubMed:7883725}; | null | null | BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 5-6. {ECO:0000269|PubMed:7883725}; | BIOPHYSICOCHEMICAL PROPERTIES: Temperature dependence: Optimum temperature is 70 degrees Celsius. {ECO:0000269|PubMed:7883725}; | FUNCTION: This enzyme catalyzes the exohydrolysis of 1,4-beta-glucosidic linkages in cellulose with a preference for amorphous or crystalline cellulose over carboxymethyl cellulose. {ECO:0000269|PubMed:7883725}. | Acetivibrio thermocellus (strain ATCC 27405 / DSM 1237 / JCM 9322 / NBRC 103400 / NCIMB 10682 / NRRL B-4536 / VPI 7372) (Clostridium thermocellum) |
A3DIH0 | IABF_ACET2 | MKKARMTVDKDYKIAEIDKRIYGSFVEHLGRAVYDGLYQPGNSKSDEDGFRKDVIELVKELNVPIIRYPGGNFVSNYFWEDGVGPVEDRPRRLDLAWKSIEPNQVGINEFAKWCKKVNAEIMMAVNLGTRGISDACNLLEYCNHPGGSKYSDMRIKHGVKEPHNIKVWCLGNEMDGPWQVGHKTMDEYGRIAEETARAMKMIDPSIELVACGSSSKDMPTFPQWEATVLDYAYDYVDYISLHQYYGNKENDTADFLAKSDDLDDFIRSVIATCDYIKAKKRSKKDIYLSFDEWNVWYHSNNEDANIMQNEPWRIAPPLLEDIYTFEDALLVGLMLITLMKHADRIKIACLAQLINVIAPIVTERNGGAAWRQTIFYPFMHASKYGRGIVLQPVINSPLHDTSKHEDVTDIESVAIYNEEKEEVTIFAVNRNIHEDIVLVSDVRGMKDYRLLEHIVLEHQDLKIRNSVNGEEVYPKNSDKSSFDDGILTSMLRRASWNVIRIGK | 3.2.1.55 | null | arabinan catabolic process [GO:0031222]; L-arabinose metabolic process [GO:0046373] | cytoplasm [GO:0005737] | alpha-L-arabinofuranosidase activity [GO:0046556] | PF06964; | 3.20.20.80;2.60.40.1180; | Glycosyl hydrolase 51 family | null | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305|PubMed:16336192}. | CATALYTIC ACTIVITY: Reaction=Hydrolysis of terminal non-reducing alpha-L-arabinofuranoside residues in alpha-L-arabinosides.; EC=3.2.1.55; Evidence={ECO:0000269|PubMed:16336192}; | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=5.5 uM for wheat arabinoxylan (at 37 degrees Celsius and at pH 7) {ECO:0000269|PubMed:16336192}; KM=0.25 mM for p-nitrophenyl alpha-L-arabinofuranoside (pNP-Araf)(at 37 degrees Celsius and at pH 7) {ECO:0000269|PubMed:16336192}; KM=0.55 mM for alpha-(1->5)-linked arabinotriose (at 37 degrees Celsius and at pH 7) {ECO:0000269|PubMed:16336192}; KM=0.95 mM for alpha-(1->3)-linked arabinoside of xylobiose (at 37 degrees Celsius and at pH 7) {ECO:0000269|PubMed:16336192}; | PATHWAY: Glycan metabolism; L-arabinan degradation. | BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 6.0. {ECO:0000269|PubMed:16336192}; | BIOPHYSICOCHEMICAL PROPERTIES: Temperature dependence: Optimum temperature is 60 degrees Celsius. {ECO:0000269|PubMed:16336192}; | FUNCTION: Involved in the degradation of arabinan and is a key enzyme in the complete degradation of the plant cell wall. Catalyzes the cleavage of terminal alpha-(1->5)-arabinofuranosyl bonds in small oligosaccharides as alpha-(1->5)-linked arabinobiose/arabinotriose, but does not display significant activity against linear non-substituted arabinan. It is also highly efficient in the cleavage of alpha-(1->3)-linked arabinoside of xylobiose and of the alpha-(1->3)-linked arabinoside decorations of polymeric wheat arabinoxylan. It exhibits very low activity against sugar beet arabinan. {ECO:0000269|PubMed:16336192}. | Acetivibrio thermocellus (strain ATCC 27405 / DSM 1237 / JCM 9322 / NBRC 103400 / NCIMB 10682 / NRRL B-4536 / VPI 7372) (Clostridium thermocellum) |
A3DIJ8 | 3PASE_ACET2 | MGKEIEKKFIVSGDAYKSLAKGVLYRQGYIFFDKDKSVRVRVFNDKGYLTVKGTSTGISRLEYEYEIPVGEANEILEYLCEKPVIEKLRYKFQFEGFTWEVDEFLGENEGLVIAEIELPDENAVFKKPDWIGREVTGDPRYLNSNLVKNPYKNFKE | 3.6.1.25 | null | null | null | ATP binding [GO:0005524]; ATP hydrolysis activity [GO:0016887]; inorganic triphosphate phosphatase activity [GO:0050355] | PF01928; | 2.40.320.10; | null | null | null | CATALYTIC ACTIVITY: Reaction=H2O + triphosphate = diphosphate + phosphate; Xref=Rhea:RHEA:14157, ChEBI:CHEBI:15377, ChEBI:CHEBI:18036, ChEBI:CHEBI:33019, ChEBI:CHEBI:43474; EC=3.6.1.25; Evidence={ECO:0000269|PubMed:17303560}; CATALYTIC ACTIVITY: Reaction=ATP + H2O = ADP + H(+) + phosphate; Xref=Rhea:RHEA:13065, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:456216; Evidence={ECO:0000269|PubMed:17303560}; | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=26 uM for ATP {ECO:0000269|PubMed:17303560}; Note=kcat is 25 min(-1) for ATPase activity.; | null | BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is between 8 and 8.5 for ATPase activity and between 9 and 9.5 for PPPase activity. Hydrolysis of ATP declines sharply as the pH is increased to 9.5 or decreased to below 7.0. {ECO:0000269|PubMed:17303560}; | null | FUNCTION: Involved in the hydrolysis of the beta-gamma-phosphoanhydride linkage of triphosphate-containing substrates (inorganic or nucleoside-linked). Catalyzes vigorously the hydrolysis of inorganic triphosphate (PPPi), however it can also catalyze the hydrolysis of ATP to ADP and phosphate. It can use ribonucleotides such as GTP, CTP, or UTP and deoxynucleotides such as dATP, dGTP, dCTP, and dTTP. {ECO:0000269|PubMed:17303560}. | Acetivibrio thermocellus (strain ATCC 27405 / DSM 1237 / JCM 9322 / NBRC 103400 / NCIMB 10682 / NRRL B-4536 / VPI 7372) (Clostridium thermocellum) |
A3DP49 | DNLI_STAMF | MPFRELADTFERIEIITSRTQMTVLLVNLFKKTPPEIIDKVVYLLQGRLWPDWKGLPELGVGEKMLIKAIALATQSTESEVESLYKSLGDLGKAAEKLKAIYEEKLKKGAMSILAFVPVKRELTVSQVYETLSRVALATGEGSRDIKLKLLAGLLSDASPKEAKYIIRFVEGRLRLGIGDATIMDALAIVYGGGAHARPIVERAYNLRADLGHIAKILATQGLNALKGIKPQVGIPIRPMLAERLNNPVEILKKVGGIAFVEYKYDGERAQIHKLGDKIWIYSRRLENITHQYPDVVDYARKYIKANEAIVEGEIVAYDPDTGELRPFQELMHRKRKHDIHIAIKEVPVKVYLFDLLYVDGEDYTLKPLPERRAKLVEIIEQTETFQIAEYIRTNNPDELEKFFLKAIEDGAEGVMIKALHKNAIYQAGTRGWLWIKYKRDYKSEMIDTVDLVVIGAFYGRGRRGGKYGALLMASYNPDKDVFESVCKVGSGFKDEDIDKLPEMLKPYIIEHKHPRVVARMKPDVWVTPALVAEIIGAELTLSPLHTCCLDIIKPGVGISIRFPRFIRWRPDKGPEDATTSQELLEMYKRQLKKLSE | 6.5.1.7 | COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000269|PubMed:17118474}; Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000269|PubMed:17118474}; | base-excision repair, DNA ligation [GO:0006288]; cell cycle [GO:0007049]; cell division [GO:0051301]; DNA biosynthetic process [GO:0071897]; DNA recombination [GO:0006310]; double-strand break repair [GO:0006302]; lagging strand elongation [GO:0006273] | null | ATP binding [GO:0005524]; DNA binding [GO:0003677]; DNA ligase (ATP) activity [GO:0003910]; metal ion binding [GO:0046872] | PF04679;PF01068;PF04675; | 1.10.3260.10;3.30.470.30;2.40.50.140; | ATP-dependent DNA ligase family | null | null | CATALYTIC ACTIVITY: Reaction=ATP + (deoxyribonucleotide)n-3'-hydroxyl + 5'-phospho-(deoxyribonucleotide)m = (deoxyribonucleotide)n+m + AMP + diphosphate.; EC=6.5.1.7; Evidence={ECO:0000255|HAMAP-Rule:MF_00407, ECO:0000269|PubMed:17118474}; CATALYTIC ACTIVITY: Reaction=ADP + (deoxyribonucleotide)n-3'-hydroxyl + 5'-phospho-(deoxyribonucleotide)m = (deoxyribonucleotide)n+m + AMP + phosphate.; EC=6.5.1.7; Evidence={ECO:0000269|PubMed:17118474}; CATALYTIC ACTIVITY: Reaction=GTP + (deoxyribonucleotide)n-3'-hydroxyl + 5'-phospho-(deoxyribonucleotide)m = (deoxyribonucleotide)n+m + GMP + diphosphate.; EC=6.5.1.7; Evidence={ECO:0000250|UniProtKB:A2BJX6}; | null | null | BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 6.5. {ECO:0000269|PubMed:17118474}; | BIOPHYSICOCHEMICAL PROPERTIES: Temperature dependence: Optimum temperature is 75 degrees Celsius. Activity declines at temperatures from 75 to 80 degrees Celsius. {ECO:0000269|PubMed:17118474}; | FUNCTION: DNA ligase that seals nicks in double-stranded DNA during DNA replication, DNA recombination and DNA repair. Can use both ATP and ADP. {ECO:0000269|PubMed:17118474}. | Staphylothermus marinus (strain ATCC 43588 / DSM 3639 / JCM 9404 / F1) |
A3DRP1 | M2_I96A2 | MSLLTEVETPIRNEWGCRCNDSSDPLVVAASIIGIVHLILWIIDRLFFKCIYRIFKHGLKRGPSTEGVPESMREEYREEQQNAVDADEGHFVSIELE | null | null | protein complex oligomerization [GO:0051259]; suppression by virus of host autophagy [GO:0039521] | host cell plasma membrane [GO:0020002]; membrane [GO:0016020]; virion membrane [GO:0055036] | monoatomic ion channel activity [GO:0005216]; proton transmembrane transporter activity [GO:0015078] | PF00599; | 6.10.250.1640; | Influenza viruses matrix protein M2 family | null | SUBCELLULAR LOCATION: Virion membrane {ECO:0000255|HAMAP-Rule:MF_04069}. Host apical cell membrane {ECO:0000255|HAMAP-Rule:MF_04069}; Single-pass type III membrane protein {ECO:0000255|HAMAP-Rule:MF_04069}. Note=Abundantly expressed at the apical plasma membrane in infected polarized epithelial cells, in close proximity to budding and assembled virions. Minor component of virions (only 16-20 molecules/virion). {ECO:0000255|HAMAP-Rule:MF_04069}. | null | null | null | null | null | FUNCTION: Forms a proton-selective ion channel that is necessary for the efficient release of the viral genome during virus entry. After attaching to the cell surface, the virion enters the cell by endocytosis. Acidification of the endosome triggers M2 ion channel activity. The influx of protons into virion interior is believed to disrupt interactions between the viral ribonucleoprotein (RNP), matrix protein 1 (M1), and lipid bilayers, thereby freeing the viral genome from interaction with viral proteins and enabling RNA segments to migrate to the host cell nucleus, where influenza virus RNA transcription and replication occur. Also plays a role in viral proteins secretory pathway. Elevates the intravesicular pH of normally acidic compartments, such as trans-Golgi network, preventing newly formed hemagglutinin from premature switching to the fusion-active conformation. {ECO:0000255|HAMAP-Rule:MF_04069}. | Influenza A virus (strain A/USA:Memphis/10/1996 H1N1) |
A3EWL3 | REV1_ARATH | MKRSLGSNSSNNSGSGSNKKSKKNNNPSNQKTLGAAWGAASSRSSFRSSPFSDFGSYMEVKNRKLQNQFETEASAASRGVSGSEKLIFQGVSIFVDGFTIPSHQELKGYMMKYGGRFENYFSRRSVTHIICSNLPDSKVKNLRTFSRGLPVVKPTWIVDSISANRLLGWVPYQLDQLNDTQPKLSAFFAPRSHLTPQMASPVTSFQPDTGYSEAEEGSSIRADDSEEARDHIDDEIDGVYIENTTPELTEQTGTGDLKSSEMNAEGLGNYDIEEKEVSSELQSTTNLHSTSDNKSVHANGKNGGKSIATAAGSSTRRHSTLEDPNFVENYFKNSRLHFIGTWRNRYRKRFHGSSNGLKWADSGQNTAEMAKKSTIIHIDLDCFFVSVVIKNRLELHDKPVAVCHSDNPKGTAEISSANYPARAYGVKAGMFVRHAKDLCPQLVIVPYNFEAYEEVADQFYDILHRHCRKVQALSCDEAFLDVSDLSDVETEVLASTIRNEILETTGCSASAGIGGTMLMARLATRVAKPAGQLYISAEKVEEFLDQLPVGTLPGVGSVLKEKLVKQNIQTCGQLRLISKDSLQKDFGVKTGEMLWSYSRGLDLRSVTAVQESKSIGAEVNWGVRFRDQQDVFILVQHFLQCLCKEVSLRLQGCEMIGRTFTLKIKKRKKDAEEPTKYMGCGDCDNLSRSITVPAATDDIEVLQRISKKLFGSFCLDVKEVRGVGLQVSKLDSADPSNKGSRTLKSWLSSAPAVVQIEQDDNVFAAKVRENSDCNRPVTGGVSRLRESNSEESSIQSGDTNSSLPPMCYLDMEVLENLPPELLSELDGTYGGKLFELIEKKRGKRRINCNSPHVSLDGTAASIKELKSLSVKIHGLSTSGEKEYKEPYVPHPSIARTSNQHTIEMTDLLPSSLSQVDVSVLQELPEELRADVLGAFPSHRRQQSSSDVPKETCKKQDEEPIDLKGTENEIGLSFSSLWFGNPPLWTEKFKVSGNCTMEKLSAIYFKVAQSRPMLSLVLQHAISEMSSFPDAASASDLDKAIYDVCELLKQYINLKVGGDIEEIYLCFRLLKRLAARSQLFLQVYEILSPFIQASISEHYGGSLSIP | 2.7.7.- | COFACTOR: Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000269|PubMed:17827267}; Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000269|PubMed:17827267}; Note=Mn(2+) ions. Can also use Mg(2+) ions with a lower efficiency. {ECO:0000269|PubMed:17827267}; | DNA damage response [GO:0006974]; error-free translesion synthesis [GO:0070987]; error-prone translesion synthesis [GO:0042276]; response to UV-B [GO:0010224] | nucleus [GO:0005634] | damaged DNA binding [GO:0003684]; deoxycytidyl transferase activity [GO:0017125]; DNA-directed DNA polymerase activity [GO:0003887]; metal ion binding [GO:0046872] | PF00533;PF00817;PF11799; | 3.30.70.270;3.40.1170.60;6.10.250.1490;1.10.150.20;3.40.50.10190;3.30.1490.100; | DNA polymerase type-Y family | null | SUBCELLULAR LOCATION: Nucleus {ECO:0000250}. | null | null | null | null | null | FUNCTION: Deoxycytidyl transferase involved in DNA repair and translesion synthesis (TLS). Transfers a dCMP residue from dCTP to the 3'-end of a DNA primer in a template-dependent reaction. Mediates also the insertion of dTMP or dGMP when the opposite base is G, and, with a low efficiency, dGMP insertions opposite G, T, and C, dAMP insertions opposite G, A, and T, and dTMP insertion opposite A. May assist in the first step in the bypass of abasic lesions by the insertion of a nucleotide opposite the lesion. Required for normal induction of mutations by physical and chemical agents (e.g. UV and gamma ray), mostly via G to T transversions, and of spontaneous mutations in somatic cells. Confers resistance to ultraviolet-B (UV-B) and various DNA cross-linkers (e.g. mitomycin C MMC and cisplatin). Promotes stem growth. {ECO:0000269|PubMed:17827267, ECO:0000269|PubMed:18339443, ECO:0000269|PubMed:21030509, ECO:0000269|PubMed:21455019}. | Arabidopsis thaliana (Mouse-ear cress) |
A3EX94 | SPIKE_BCHK4 | MTLLMCLLMSLLIFVRGCDSQFVDMSPASNTSECLESQVDAAAFSKLMWPYPIDPSKVDGIIYPLGRTYSNITLAYTGLFPLQGDLGSQYLYSVSHAVGHDGDPTKAYISNYSLLVNDFDNGFVVRIGAAANSTGTIVISPSVNTKIKKAYPAFILGSSLTNTSAGQPLYANYSLTIIPDGCGTVLHAFYCILKPRTVNRCPSGTGYVSYFIYETVHNDCQSTINRNASLNSFKSFFDLVNCTFFNSWDITADETKEWFGITQDTQGVHLYSSRKGDLYGGNMFRFATLPVYEGIKYYTVIPRSFRSKANKREAWAAFYVYKLHQLTYLLDFSVDGYIRRAIDCGHDDLSQLHCSYTSFEVDTGVYSVSSYEASATGTFIEQPNATECDFSPMLTGVAPQVYNFKRLVFSNCNYNLTKLLSLFAVDEFSCNGISPDSIARGCYSTLTVDYFAYPLSMKSYIRPGSAGNIPLYNYKQSFANPTCRVMASVLANVTITKPHAYGYISKCSRLTGANQDVETPLYINPGEYSICRDFSPGGFSEDGQVFKRTLTQFEGGGLLIGVGTRVPMTDNLQMSFIISVQYGTGTDSVCPMLDLGDSLTITNRLGKCVDYSLYGVTGRGVFQNCTAVGVKQQRFVYDSFDNLVGYYSDDGNYYCVRPCVSVPVSVIYDKSTNLHATLFGSVACEHVTTMMSQFSRLTQSNLRRRDSNIPLQTAVGCVIGLSNNSLVVSDCKLPLGQSLCAVPPVSTFRSYSASQFQLAVLNYTSPIVVTPINSSGFTAAIPTNFSFSVTQEYIETSIQKVTVDCKQYVCNGFTRCEKLLVEYGQFCSKINQALHGANLRQDESVYSLYSNIKTTSTQTLEYGLNGDFNLTLLQVPQIGGSSSSYRSAIEDLLFDKVTIADPGYMQGYDDCMKQGPQSARDLICAQYVSGYKVLPPLYDPNMEAAYTSSLLGSIAGAGWTAGLSSFAAIPFAQSMFYRLNGVGITQQVLSENQKLIANKFNQALGAMQTGFTTSNLAFSKVQDAVNANAQALSKLASELSNTFGAISSSISDILARLDTVEQDAQIDRLINGRLISLNAFVSQQLVRSETAARSAQLASDKVNECVKSQSKRNGFCGSGTHIVSFVVNAPNGFYFFHVGYVPTNYTNVTAAYGLCNNNNPPLCIAPIDGYFITNQTTTYSVDTEWYYTGSSFYKPEPITQANSRYVSSDVKFDKLENNLPPPLLENSTDVDFKDELEEFFKNVTSHGPNFAEISKINTTLLDLSDEMAMLQEVVKQLNDSYIDLKELGNYTYYNKWPWYVWLGFIAGLVALLLCVFFLLCCTGCGTSCLGKMKCKNCCDSYEEYDVEKIHVH | null | null | endocytosis involved in viral entry into host cell [GO:0075509]; fusion of virus membrane with host endosome membrane [GO:0039654]; fusion of virus membrane with host plasma membrane [GO:0019064]; receptor-mediated virion attachment to host cell [GO:0046813] | host cell endoplasmic reticulum-Golgi intermediate compartment membrane [GO:0044173]; host cell plasma membrane [GO:0020002]; membrane [GO:0016020]; viral envelope [GO:0019031]; virion membrane [GO:0055036] | null | PF16451;PF09408;PF19209;PF01601;PF19214; | 1.20.5.300;2.20.210.30;3.30.70.1840;2.60.120.960; | Betacoronaviruses spike protein family | PTM: Specific enzymatic cleavages in vivo yield mature proteins. The precursor is processed into S1 and S2 by host cell furin or another cellular protease to yield the mature S1 and S2 proteins. Additionally, a second cleavage leads to the release of a fusion peptide after viral attachment to host cell receptor. {ECO:0000255|HAMAP-Rule:MF_04099}.; PTM: The cytoplasmic Cys-rich domain is palmitoylated. Spike glycoprotein is digested within host endosomes. {ECO:0000255|HAMAP-Rule:MF_04099}. | SUBCELLULAR LOCATION: Virion membrane {ECO:0000255|HAMAP-Rule:MF_04099}; Single-pass type I membrane protein {ECO:0000255|HAMAP-Rule:MF_04099}. Host endoplasmic reticulum-Golgi intermediate compartment membrane {ECO:0000255|HAMAP-Rule:MF_04099}; Single-pass type I membrane protein {ECO:0000255|HAMAP-Rule:MF_04099}. Host cell membrane {ECO:0000255|HAMAP-Rule:MF_04099}; Single-pass type I membrane protein {ECO:0000255|HAMAP-Rule:MF_04099}. Note=Accumulates in the endoplasmic reticulum-Golgi intermediate compartment, where it participates in virus particle assembly. Some S oligomers are transported to the host plasma membrane, where they may mediate cell-cell fusion. {ECO:0000255|HAMAP-Rule:MF_04099}. | null | null | null | null | null | FUNCTION: [Spike protein S1]: Attaches the virion to the cell membrane by interacting with host receptor, initiating the infection. {ECO:0000255|HAMAP-Rule:MF_04099}.; FUNCTION: [Spike protein S2]: Mediates fusion of the virion and cellular membranes by acting as a class I viral fusion protein. Under the current model, the protein has at least three conformational states: pre-fusion native state, pre-hairpin intermediate state, and post-fusion hairpin state. During viral and target cell membrane fusion, the coiled coil regions (heptad repeats) assume a trimer-of-hairpins structure, positioning the fusion peptide in close proximity to the C-terminal region of the ectodomain. The formation of this structure appears to drive apposition and subsequent fusion of viral and target cell membranes. {ECO:0000255|HAMAP-Rule:MF_04099}.; FUNCTION: [Spike protein S2']: Acts as a viral fusion peptide which is unmasked following S2 cleavage occurring upon virus endocytosis. {ECO:0000255|HAMAP-Rule:MF_04099}. | Bat coronavirus HKU4 (BtCoV) (BtCoV/HKU4/2004) |
A3EXD0 | SPIKE_BCHK5 | MIRSVLVLMCSLTFIGNLTRGQSVDMGHNGTGSCLDSQVQPDYFESVHTTWPMPIDTSKAEGVIYPNGKSYSNITLTYTGLYPKANDLGKQYLFSDGHSAPGRLNNLFVSNYSSQVESFDDGFVVRIGAAANKTGTTVISQSTFKPIKKIYPAFLLGHSVGNYTPSNRTGRYLNHTLVILPDGCGTILHAFYCVLHPRTQQNCAGETNFKSLSLWDTPASDCVSGSYNQEATLGAFKVYFDLINCTFRYNYTITEDENAEWFGITQDTQGVHLYSSRKENVFRNNMFHFATLPVYQKILYYTVIPRSIRSPFNDRKAWAAFYIYKLHPLTYLLNFDVEGYITKAVDCGYDDLAQLQCSYESFEVETGVYSVSSFEASPRGEFIEQATTQECDFTPMLTGTPPPIYNFKRLVFTNCNYNLTKLLSLFQVSEFSCHQVSPSSLATGCYSSLTVDYFAYSTDMSSYLQPGSAGAIVQFNYKQDFSNPTCRVLATVPQNLTTITKPSNYAYLTECYKTSAYGKNYLYNAPGAYTPCLSLASRGFSTKYQSHSDGELTTTGYIYPVTGNLQMAFIISVQYGTDTNSVCPMQALRNDTSIEDKLDVCVEYSLHGITGRGVFHNCTSVGLRNQRFVYDTFDNLVGYHSDNGNYYCVRPCVSVPVSVIYDKASNSHATLFGSVACSHVTTMMSQFSRMTKTNLLARTTPGPLQTTVGCAMGFINSSMVVDECQLPLGQSLCAIPPTTSSRVRRATSGASDVFQIATLNFTSPLTLAPINSTGFVVAVPTNFTFGVTQEFIETTIQKITVDCKQYVCNGFKKCEDLLKEYGQFCSKINQALHGANLRQDESIANLFSSIKTQNTQPLQAGLNGDFNLTMLQIPQVTTGERKYRSTIEDLLFNKVTIADPGYMQGYDECMQQGPQSARDLICAQYVAGYKVLPPLYDPYMEAAYTSSLLGSIAGASWTAGLSSFAAIPFAQSIFYRLNGVGITQQVLSENQKIIANKFNQALGAMQTGFTTTNLAFNKVQDAVNANAMALSKLAAELSNTFGAISSSISDILARLDTVEQEAQIDRLINGRLTSLNAFVAQQLVRTEAAARSAQLAQDKVNECVKSQSKRNGFCGTGTHIVSFAINAPNGLYFFHVGYQPTSHVNATAAYGLCNTENPQKCIAPIDGYFVLNQTTSTVADSDQQWYYTGSSFFHPEPITEANSKYVSMDVKFENLTNRLPPPLLSNSTDLDFKEELEEFFKNVSSQGPNFQEISKINTTLLNLNTELMVLSEVVKQLNESYIDLKELGNYTFYQKWPWYIWLGFIAGLVALALCVFFILCCTGCGTSCLGKLKCNRCCDSYDEYEVEKIHVH | null | null | endocytosis involved in viral entry into host cell [GO:0075509]; fusion of virus membrane with host endosome membrane [GO:0039654]; fusion of virus membrane with host plasma membrane [GO:0019064]; receptor-mediated virion attachment to host cell [GO:0046813] | host cell endoplasmic reticulum-Golgi intermediate compartment membrane [GO:0044173]; host cell plasma membrane [GO:0020002]; membrane [GO:0016020]; viral envelope [GO:0019031]; virion membrane [GO:0055036] | null | PF16451;PF09408;PF19209;PF01601;PF19214; | 1.20.5.300;2.20.210.30;3.30.70.1840;2.60.120.960; | Betacoronaviruses spike protein family | PTM: Specific enzymatic cleavages in vivo yield mature proteins. The precursor is processed into S1 and S2 by host cell furin or another cellular protease to yield the mature S1 and S2 proteins. Additionally, a second cleavage leads to the release of a fusion peptide after viral attachment to host cell receptor. {ECO:0000255|HAMAP-Rule:MF_04099}.; PTM: The cytoplasmic Cys-rich domain is palmitoylated. Spike glycoprotein is digested within host endosomes. {ECO:0000255|HAMAP-Rule:MF_04099}. | SUBCELLULAR LOCATION: Virion membrane {ECO:0000255|HAMAP-Rule:MF_04099}; Single-pass type I membrane protein {ECO:0000255|HAMAP-Rule:MF_04099}. Host endoplasmic reticulum-Golgi intermediate compartment membrane {ECO:0000255|HAMAP-Rule:MF_04099}; Single-pass type I membrane protein {ECO:0000255|HAMAP-Rule:MF_04099}. Host cell membrane {ECO:0000255|HAMAP-Rule:MF_04099}; Single-pass type I membrane protein {ECO:0000255|HAMAP-Rule:MF_04099}. Note=Accumulates in the endoplasmic reticulum-Golgi intermediate compartment, where it participates in virus particle assembly. Some S oligomers are transported to the host plasma membrane, where they may mediate cell-cell fusion. {ECO:0000255|HAMAP-Rule:MF_04099}. | null | null | null | null | null | FUNCTION: [Spike protein S1]: Attaches the virion to the cell membrane by interacting with host receptor, initiating the infection. {ECO:0000255|HAMAP-Rule:MF_04099}.; FUNCTION: [Spike protein S2]: Mediates fusion of the virion and cellular membranes by acting as a class I viral fusion protein. Under the current model, the protein has at least three conformational states: pre-fusion native state, pre-hairpin intermediate state, and post-fusion hairpin state. During viral and target cell membrane fusion, the coiled coil regions (heptad repeats) assume a trimer-of-hairpins structure, positioning the fusion peptide in close proximity to the C-terminal region of the ectodomain. The formation of this structure appears to drive apposition and subsequent fusion of viral and target cell membranes. {ECO:0000255|HAMAP-Rule:MF_04099}.; FUNCTION: [Spike protein S2']: Acts as a viral fusion peptide which is unmasked following S2 cleavage occurring upon virus endocytosis. {ECO:0000255|HAMAP-Rule:MF_04099}. | Bat coronavirus HKU5 (BtCoV) (BtCoV/HKU5/2004) |
A3EXG6 | SPIKE_BCHK9 | MLLILVLGVSLAAASRPECFNPRFTLTPLNHTLNYTSIKAKVSNVLLPDPYIAYSGQTLRQNLFMADMSNTILYPVTPPANGANGGFIYNTSIIPVSAGLFVNTWMYRQPASSRAYCQEPFGVAFGDTFENDRIAILIMAPDNLGSWSAVAPRNQTNIYLLVCSNATLCINPGFNRWGPAGSFIAPDALVDHSNSCFVNNTFSVNISTSRISLAFLFKDGDLLIYHSGWLPTSNFEHGFSRGSHPMTYFMSLPVGGNLPRAQFFQSIVRSNAIDKGDGMCTNFDVNLHVAHLINRDLLVSYFNNGSVANAADCADSAAEELYCVTGSFDPPTGVYPLSRYRAQVAGFVRVTQRGSYCTPPYSVLQDPPQPVVWRRYMLYDCVFDFTVVVDSLPTHQLQCYGVSPRRLASMCYGSVTLDVMRINETHLNNLFNRVPDTFSLYNYALPDNFYGCLHAFYLNSTAPYAVANRFPIKPGGRQSNSAFIDTVINAAHYSPFSYVYGLAVITLKPAAGSKLVCPVANDTVVITDRCVQYNLYGYTGTGVLSKNTSLVIPDGKVFTASSTGTIIGVSINSTTYSIMPCVTVPVSVGYHPNFERALLFNGLSCSQRSRAVTEPVSVLWSASATAQDAFDTPSGCVVNVELRNTTIVNTCAMPIGNSLCFINGSIATANADSLPRLQLVNYDPLYDNSTATPMTPVYWVKVPTNFTLSATEEYIQTTAPKITIDCARYLCGDSSRCLNVLLHYGTFCNDINKALSRVSTILDSALLSLVKELSINTRDEVTTFSFDGDYNFTGLMGCLGPNCGATTYRSAFSDLLYDKVRITDPGFMQSYQKCIDSQWGGSIRDLLCTQTYNGIAVLPPIVSPAMQALYTSLLVGAVASSGYTFGITSAGVIPFATQLQFRLNGIGVTTQVLVENQKLIASSFNNALVNIQKGFTETSIALSKMQDVINQHAAQLHTLVVQLGNSFGAISSSINEIFSRLEGLAANAEVDRLINGRMMVLNTYVTQLLIQASEAKAQNALAAQKISECVKAQSLRNDFCGNGTHVLSIPQLAPNGVLFIHYAYTPTEYAFVQTSAGLCHNGTGYAPRQGMFVLPNNTNMWHFTTMQFYNPVNISASNTQVLTSCSVNYTSVNYTVLEPSVPGDYDFQKEFDKFYKNLSTIFNNTFNPNDFNFSTVDVTAQIKSLHDVVNQLNQSFIDLKKLNVYEKTIKWPWYVWLAMIAGIVGLVLAVIMLMCMTNCCSCFKGMCDCRRCCGSYDSYDDVYPAVRVNKKRTV | null | null | endocytosis involved in viral entry into host cell [GO:0075509]; fusion of virus membrane with host endosome membrane [GO:0039654]; fusion of virus membrane with host plasma membrane [GO:0019064]; receptor-mediated virion attachment to host cell [GO:0046813] | host cell endoplasmic reticulum-Golgi intermediate compartment membrane [GO:0044173]; host cell plasma membrane [GO:0020002]; membrane [GO:0016020]; viral envelope [GO:0019031]; virion membrane [GO:0055036] | null | PF16451;PF09408;PF19209;PF01601;PF19214; | 1.20.5.300;3.30.70.1840;1.20.5.790;2.60.120.960; | Betacoronaviruses spike protein family | PTM: Specific enzymatic cleavages in vivo yield mature proteins. The precursor is processed into S1 and S2 by host cell furin or another cellular protease to yield the mature S1 and S2 proteins. Additionally, a second cleavage leads to the release of a fusion peptide after viral attachment to host cell receptor. {ECO:0000255|HAMAP-Rule:MF_04099}.; PTM: The cytoplasmic Cys-rich domain is palmitoylated. Spike glycoprotein is digested within host endosomes. {ECO:0000255|HAMAP-Rule:MF_04099}. | SUBCELLULAR LOCATION: Virion membrane {ECO:0000255|HAMAP-Rule:MF_04099}; Single-pass type I membrane protein {ECO:0000255|HAMAP-Rule:MF_04099}. Host endoplasmic reticulum-Golgi intermediate compartment membrane {ECO:0000255|HAMAP-Rule:MF_04099}; Single-pass type I membrane protein {ECO:0000255|HAMAP-Rule:MF_04099}. Host cell membrane {ECO:0000255|HAMAP-Rule:MF_04099}; Single-pass type I membrane protein {ECO:0000255|HAMAP-Rule:MF_04099}. Note=Accumulates in the endoplasmic reticulum-Golgi intermediate compartment, where it participates in virus particle assembly. Some S oligomers are transported to the host plasma membrane, where they may mediate cell-cell fusion. {ECO:0000255|HAMAP-Rule:MF_04099}. | null | null | null | null | null | FUNCTION: [Spike protein S1]: Attaches the virion to the cell membrane by interacting with host receptor, initiating the infection. {ECO:0000255|HAMAP-Rule:MF_04099}.; FUNCTION: [Spike protein S2]: Mediates fusion of the virion and cellular membranes by acting as a class I viral fusion protein. Under the current model, the protein has at least three conformational states: pre-fusion native state, pre-hairpin intermediate state, and post-fusion hairpin state. During viral and target cell membrane fusion, the coiled coil regions (heptad repeats) assume a trimer-of-hairpins structure, positioning the fusion peptide in close proximity to the C-terminal region of the ectodomain. The formation of this structure appears to drive apposition and subsequent fusion of viral and target cell membranes. {ECO:0000255|HAMAP-Rule:MF_04099}.; FUNCTION: [Spike protein S2']: Acts as a viral fusion peptide which is unmasked following S2 cleavage occurring upon virus endocytosis. {ECO:0000255|HAMAP-Rule:MF_04099}. | Bat coronavirus HKU9 (BtCoV) (BtCoV/HKU9) |
A3EZ55 | HOG1A_WALI9 | MSQEDSSFVKLSVFGNIFQVTTRYTDLQPVGMGAFGLLCSSTDQKSGGPVAIKKVMKPFSAPVLAKRTYRELKLLKHLRHENIISLLDVFISPGEDIYFITELLGTDLHRLLSSRPLERQFVQYFLYQMLRALKFVHPAGVVHRDLKPSNILINENCDLKICDFGLARLQDPQMTGYVSTRYYRAPEIMLTWQEYDSAVDIWSVGCIFAEMIDGRPIFPGKDHVHQLTVITELLGSPPEDVINTITSENTRRFVDALPKRHKISFADRFPNANAEEIDLLEKMLDFNPKKRITAADALAHPYLAPYHDPEDEPTANERFDWSFNDADLPTDQWKVMMYSEILDFHNVDVKSEKDMTPSTTTAGAH | 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: Phosphorylated. Dually phosphorylated on Thr-175 and Tyr-177, which activates the enzyme (By similarity). Rapidly dephosphorylated upon either hypo- or hyperosmotic shock. {ECO:0000250, ECO:0000269|PubMed:23712906}. | 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. {ECO:0000269|PubMed:23712906}. | Wallemia ichthyophaga (strain EXF-994 / CBS 113033) |
A3FBE9 | IL6_MUSPF | MNSLSTSAFSPVAFSLGLLLVMATAFPTPGPLGGDSKDDATSNRPPLTSADKMEDFIRFILGKISALKKEMCEKYNKCEDSKEALAENNLNLPKLAEEDKCFQSQFNQETCLTRITTGLQEFQIHLKYLEANYEGNKNNAHSVYISTKHLLQKLRPMNRVEVTTPDPTTDSSLQALFKSQDKWLKHVTIHLILRSLEDFLQFSLRAIRIM | null | null | acute-phase response [GO:0006953]; cellular response to hydrogen peroxide [GO:0070301]; cellular response to lipopolysaccharide [GO:0071222]; defense response to virus [GO:0051607]; glucose homeostasis [GO:0042593]; hepatic immune response [GO:0002384]; hepatocyte proliferation [GO:0072574]; inflammatory response to wounding [GO:0090594]; interleukin-6-mediated signaling pathway [GO:0070102]; liver regeneration [GO:0097421]; negative regulation of apoptotic process [GO:0043066]; negative regulation of collagen biosynthetic process [GO:0032966]; negative regulation of primary miRNA processing [GO:2000635]; neuron projection development [GO:0031175]; neutrophil apoptotic process [GO:0001781]; positive regulation of acute inflammatory response [GO:0002675]; positive regulation of apoptotic DNA fragmentation [GO:1902512]; positive regulation of apoptotic process [GO:0043065]; positive regulation of B cell activation [GO:0050871]; positive regulation of chemokine production [GO:0032722]; positive regulation of cytokine production involved in inflammatory response [GO:1900017]; positive regulation of epithelial to mesenchymal transition [GO:0010718]; positive regulation of extracellular matrix disassembly [GO:0090091]; positive regulation of glial cell proliferation [GO:0060252]; positive regulation of immunoglobulin production [GO:0002639]; positive regulation of interleukin-1 beta production [GO:0032731]; positive regulation of interleukin-10 production [GO:0032733]; positive regulation of interleukin-6 production [GO:0032755]; positive regulation of interleukin-8 production [GO:0032757]; positive regulation of leukocyte adhesion to vascular endothelial cell [GO:1904996]; positive regulation of MAPK cascade [GO:0043410]; positive regulation of osteoblast differentiation [GO:0045669]; positive regulation of peptidyl-serine phosphorylation [GO:0033138]; positive regulation of platelet aggregation [GO:1901731]; positive regulation of receptor signaling pathway via JAK-STAT [GO:0046427]; positive regulation of receptor signaling pathway via STAT [GO:1904894]; positive regulation of smooth muscle cell proliferation [GO:0048661]; positive regulation of T cell proliferation [GO:0042102]; positive regulation of transcription by RNA polymerase II [GO:0045944]; positive regulation of translation [GO:0045727]; positive regulation of tumor necrosis factor production [GO:0032760]; positive regulation of tyrosine phosphorylation of STAT protein [GO:0042531]; positive regulation of vascular endothelial growth factor production [GO:0010575]; regulation of glucagon secretion [GO:0070092]; regulation of insulin secretion [GO:0050796]; response to activity [GO:0014823]; response to glucocorticoid [GO:0051384]; T-helper 17 cell lineage commitment [GO:0072540]; vascular endothelial growth factor production [GO:0010573] | extracellular space [GO:0005615]; interleukin-6 receptor complex [GO:0005896] | cytokine activity [GO:0005125]; growth factor activity [GO:0008083]; interleukin-6 receptor binding [GO:0005138] | PF00489; | 1.20.1250.10; | IL-6 superfamily | null | SUBCELLULAR LOCATION: Secreted {ECO:0000250|UniProtKB:P05231}. | null | null | null | null | null | FUNCTION: Cytokine with a wide variety of biological functions in immunity, tissue regeneration, and metabolism. Binds to IL6R, then the complex associates to the signaling subunit IL6ST/gp130 to trigger the intracellular IL6-signaling pathway. The interaction with the membrane-bound IL6R and IL6ST stimulates 'classic signaling', whereas the binding of IL6 and soluble IL6R to IL6ST stimulates 'trans-signaling'. Alternatively, 'cluster signaling' occurs when membrane-bound IL6:IL6R complexes on transmitter cells activate IL6ST receptors on neighboring receiver cells. {ECO:0000250|UniProtKB:P05231}.; FUNCTION: IL6 is a potent inducer of the acute phase response. Rapid production of IL6 contributes to host defense during infection and tissue injury, but excessive IL6 synthesis is involved in disease pathology. In the innate immune response, is synthesized by myeloid cells, such as macrophages and dendritic cells, upon recognition of pathogens through toll-like receptors (TLRs) at the site of infection or tissue injury (By similarity). In the adaptive immune response, is required for the differentiation of B cells into immunoglobulin-secreting cells. Plays a major role in the differentiation of CD4(+) T cell subsets. Essential factor for the development of T follicular helper (Tfh) cells that are required for the induction of germinal-center formation. Required to drive naive CD4(+) T cells to the Th17 lineage. Also required for proliferation of myeloma cells and the survival of plasmablast cells (By similarity). {ECO:0000250|UniProtKB:P05231, ECO:0000250|UniProtKB:P08505}.; FUNCTION: Acts as an essential factor in bone homeostasis and on vessels directly or indirectly by induction of VEGF, resulting in increased angiogenesis activity and vascular permeability. Induces, through 'trans-signaling' and synergistically with IL1B and TNF, the production of VEGF. Involved in metabolic controls, is discharged into the bloodstream after muscle contraction increasing lipolysis and improving insulin resistance (By similarity). 'Trans-signaling' in central nervous system also regulates energy and glucose homeostasis. Mediates, through GLP-1, crosstalk between insulin-sensitive tissues, intestinal L cells and pancreatic islets to adapt to changes in insulin demand (By similarity). Also acts as a myokine (By similarity). Plays a protective role during liver injury, being required for maintenance of tissue regeneration (By similarity). Also has a pivotal role in iron metabolism by regulating HAMP/hepcidin expression upon inflammation or bacterial infection (By similarity). Through activation of IL6ST-YAP-NOTCH pathway, induces inflammation-induced epithelial regeneration (By similarity). {ECO:0000250|UniProtKB:P05231, ECO:0000250|UniProtKB:P08505}. | Mustela putorius furo (European domestic ferret) (Mustela furo) |
A3FEW8 | BGAL_ENTAG | MFTASPMSLSKILARRDWENPGVTQWHRLPAHAPFNSWRDEASARADDNASRKRSLNGDWQFSYYAAPEQVPDSWVTEDCADAVTTPVPSNWQMQGFDTPIYTNDTYPIPVNPPFVPAENPTGCYSLTFEVDEQWLESGQTRIVFDGVNSAFYLWCNGKWMGYSQDSRLPAEFDLSAVLRPGTNRLAVLVLRWCDGSYLEDQDMWRMSGIFRDVSLLHKPHTHIADYHAVTELNADYDRAKLQVEVALAGEQFADCEVAVTLWRDGLSVATVSAKPGSAIIDERGNWAERLNVTLPVKDPALWSAETPELYRLTFALRDGQGEILDVEACDVGFRCVEISNGLLKVNGKPLLIRGVNRHEHHPENGQVMDEATMCRDIELMKQHNFNAVRCSHYPNHPLWYTLCDRYGLYVVDEANIETHGMVPMSRLADDPRWLPAMSERVTRMVLRDRNHPSIIIWSLGNESGHGANHDALYRWVKTTDPTRPVQYEGGGANTAATDIVCPMYARVDQDQPFEAVPKWSLKKWIGMPDETRPLILCEYAHAMGNSFGGFAKYWQAFRNHPRLQGGFVWDWVDQALTKKDDNGNAFWAYGGDFGDTPNDRQFCLNGLVFPDRTPHPALFEAQRAQQFFTFTLVSTSPLVIDVHSDYLFRQCDNEQLRWNIARDGEVLASGEVALTIAPQQTQRIEIDAPEFAAAAGEIWLNVDIVQTAATAWSPADHRCAWDQWQLPAPLYIAPPVEGTAKPDLKVKEDVLEVSHQSQRWHFDRASGNLTQWWNNGTATLLAPLSDNFTRAPLDNDIGVSEATRIDPNAWVERWKAAGMYNLTPRLLLCEGEQLAQAVTITTLHAWESNGKALFLSRKVWKIDRAGVLHGDVQVQVANDIPQPARIGLSCQLAQTPQTASWLGLGPDENYPDRKLAARQGRWTLPLDALHTAYIFPTDNGLRCDTRELTFDTHQMQGDFHFSLSRYSQQQLRDTSHHHLLEAEPGCWLNIDAFHMGVGGDDSWSPSVSPEFILQRREMRYAFSWRQD | 3.2.1.23 | COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000305}; Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000305}; Name=Fe cation; Xref=ChEBI:CHEBI:24875; Evidence={ECO:0000305}; Note=Binds 2 magnesium ions per monomer. Can also use manganese and iron. {ECO:0000305}; COFACTOR: Name=Na(+); Xref=ChEBI:CHEBI:29101; Evidence={ECO:0000305}; Name=K(+); Xref=ChEBI:CHEBI:29103; Evidence={ECO:0000305}; Note=Binds 1 sodium ion per monomer. Can also use potassium. {ECO:0000305}; | lactose catabolic process [GO:0005990] | beta-galactosidase complex [GO:0009341] | beta-galactosidase activity [GO:0004565]; carbohydrate binding [GO:0030246]; magnesium ion binding [GO:0000287] | PF02929;PF00703;PF02836;PF02837;PF16353; | 2.70.98.10;2.60.120.260;3.20.20.80;2.60.40.10; | Glycosyl hydrolase 2 family | null | null | CATALYTIC ACTIVITY: Reaction=Hydrolysis of terminal non-reducing beta-D-galactose residues in beta-D-galactosides.; EC=3.2.1.23; | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=0.06 mM for o-nitrophenyl-beta-D-galactopyranoside (at 37 degrees Celsius) {ECO:0000269|PubMed:17336932}; KM=114 mM for lactose (at 37 degrees Celsius) {ECO:0000269|PubMed:17336932}; Vmax=0.43 mmol/min/mg enzyme for o-nitrophenyl-beta-D-galactopyranoside (at 37 degrees Celsius) {ECO:0000269|PubMed:17336932}; Vmax=2.9 mmol/min/mg enzyme for o-nitrophenyl-beta-D-galactopyranoside (at 37 degrees Celsius) {ECO:0000269|PubMed:17336932}; | null | BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 7.5-8.0. Stable between 7.5-10.0. {ECO:0000269|PubMed:17336932}; | BIOPHYSICOCHEMICAL PROPERTIES: Temperature dependence: Optimum temperature is 37-40 degrees Celsius. Stable below 37 degrees Celsius. {ECO:0000269|PubMed:17336932}; | FUNCTION: This beta-galactosidase is also able to catalyze glycosyl transfer to a series of acceptors, including hexose, pentose, beta- or alpha-disaccharides, hexahydroxy alcohol, cyclitol, and aromatic glycosides, resulting in the production of galacto-oligosaccharides (GOS). {ECO:0000269|PubMed:17336932}. | Enterobacter agglomerans (Erwinia herbicola) (Pantoea agglomerans) |
A3FIN4 | AT8B5_MOUSE | MKYVKAFVSEISWDCSWYCSAMQERRNEDRQKEEEERILQANNRRFNSLFEYPDNSIKTSKYGFFNFLPMNLFEQFQRLANAYFLILLFLQLVPQISSLAWYTTVIPLIVVLSITGVKDAIDDVKRHRSDQQINNRSVSILVNGRVEEIKWRNVQVGDIIKLENNHPVTADMLLLSSSEPYGLTYIETADLDGETNLKVKQAISVTSAMEDNLELLSSFNGEVRCDPPNNKLDKFSGTLSYLGNTYLLNHERLLLRGCVIRNTDWCYGLVVYTGQDTKLMQNSGRSTFKRTHIDHLMNVLVVWIFMFLGGMCFLLSIGHGIWENSRGYYFQAFLPWKHYITSSATSSALIFWSYFIVLNTMVPISLYVSVEIIRLGNSYYINWDRKMFYAPKNMPAQARTTTLNEELGQVQYVFSDKTGTLTENVMIFNKCSINGKTYGYSYDDNGEYVPKSPKDKVDFSYNHLADPKFSFYDKTLVEAVKSEDPLVYLFFLCLSLCHTVMSEEKVEGELVYQAQSPDEGALVTATRNFGFVFCSRTPETITVIEMGKIRVYRLLAILDFSNERKRMSVIVRTPEDRVMLFCKGADTIIYELLHPSCASLSEVTMDHLDDFASEGLRTLMVAYRELDKAYFQTWIKKHGEAWLTLENRERKLALVYEEIERDLMLLGATAIEDKLQRGVPETIVTLSKAKIKIWVLTGDKQETAVNIAYSCRIFKDEMDGVFMVEGTDRETVLEELRTARKKMKPESLLESDPINMYLARKPKMPFKSLDEVANGNYGLVISGYSLAYALEGSLEFELLRTACMCKGVVCCRMTPLQKAQVVDLVKRYKKVVTLAIGDGANDISMIKAAHIGVGISNQEGMQATLSSDFSFCQFHFLQRLLLVHGRLSYNRMCKFLSYFFYKNFAFTLVHFWYAFFNGFSAQTVYDIWFITFYNLIYTSLPVLGLSLFEKDVNETWSLCYPELYEPGQHNLYFNKKEFVKCLLHGIYNSFVLFFVPMGTVFNSERNDGKDISDFQSFSLLVQTTLIGVMTMQIALRTTSWTMINHTFTWGSLGLYFCILILLCSDGLCLRYPSIFNFLGVARNSLSQPQIWLCLILSTILCMIPLIGYNFLRPLLWPINADKVLNRIHFCLKHPIPTQVQTKIKHPSLRRSAYAFSHKQGFGALITSGKTLKSSALAKSKRFL | 7.6.2.1 | COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250|UniProtKB:Q9Y2Q0}; | Golgi organization [GO:0007030]; phospholipid translocation [GO:0045332]; phospholipid transport [GO:0015914] | acrosomal membrane [GO:0002080]; acrosomal vesicle [GO:0001669]; membrane [GO:0016020]; plasma membrane [GO:0005886]; trans-Golgi network [GO:0005802] | ATP binding [GO:0005524]; ATP hydrolysis activity [GO:0016887]; ATPase-coupled intramembrane lipid transporter activity [GO:0140326]; magnesium ion binding [GO:0000287]; phosphatidylcholine flippase activity [GO:0140345]; phosphatidylethanolamine flippase activity [GO:0090555] | PF13246;PF16212;PF16209; | 3.40.1110.10;2.70.150.10;3.40.50.1000; | Cation transport ATPase (P-type) (TC 3.A.3) family, Type IV subfamily | null | SUBCELLULAR LOCATION: Cytoplasmic vesicle, secretory vesicle, acrosome membrane {ECO:0000269|PubMed:19657017}; Multi-pass membrane protein {ECO:0000269|PubMed:19657017}. | CATALYTIC ACTIVITY: Reaction=ATP + H2O + phospholipidSide 1 = ADP + phosphate + phospholipidSide 2.; EC=7.6.2.1; | null | null | null | null | FUNCTION: P4-ATPase flippase which catalyzes the hydrolysis of ATP coupled to the transport of aminophospholipids from the outer to the inner leaflet of various membranes and ensures the maintenance of asymmetric distribution of phospholipids. Phospholipid translocation seems also to be implicated in vesicle formation and in uptake of lipid signaling molecules. May play a role in phospholid transport across membranes and in acrosome formation. {ECO:0000269|PubMed:19657017}. | Mus musculus (Mouse) |
A3FKF7 | G3P_MUSPF | MVKVGVNGFGRIGRLVTRAAFNSGKVDIVAINDPFIDLNYMVYMFQYDSTHGKFHGTVKAENGKLVINGKSISIFQERDPANIKWGDAGAEYVVESTGVFTTMEKAGAHLKGGAKRVIISAPSADAPMFVMGVNHEKYDNSLKIVSNASCTTNCLAPLAKVIHDNFGIVEGLMTTVHAITATQKTVDGPSGKLWRDGRGAAQNIIPASTGAAKAVGKVIPELNGKLTGMAFRVPTPNVSVVDLTCRLEKAAKYDDIKKVVKQASEGPLKGILGYTEDQVVSCDFNSDTHSSTFDAGAGIALNDHFVKLISWYDNEFGYSNRVVDLMVYMASKE | 1.2.1.12; 2.6.99.- | null | glucose metabolic process [GO:0006006]; glycolytic process [GO:0006096]; innate immune response [GO:0045087]; microtubule cytoskeleton organization [GO:0000226]; neuron apoptotic process [GO:0051402]; peptidyl-cysteine S-trans-nitrosylation [GO:0035606]; positive regulation of canonical NF-kappaB signal transduction [GO:0043123]; positive regulation of type I interferon production [GO:0032481]; protein stabilization [GO:0050821]; regulation of translation [GO:0006417] | cytoplasm [GO:0005737]; cytosol [GO:0005829]; GAIT complex [GO:0097452]; microtubule cytoskeleton [GO:0015630]; nucleus [GO:0005634] | glyceraldehyde-3-phosphate dehydrogenase (NAD+) (phosphorylating) activity [GO:0004365]; microtubule binding [GO:0008017]; NAD binding [GO:0051287]; NADP binding [GO:0050661]; peptidyl-cysteine S-nitrosylase activity [GO:0035605] | PF02800;PF00044; | 3.40.50.720; | Glyceraldehyde-3-phosphate dehydrogenase family | PTM: ISGylated. {ECO:0000250|UniProtKB:P04406}.; PTM: S-nitrosylation of Cys-150 leads to interaction with SIAH1, followed by translocation to the nucleus S-nitrosylation of Cys-245 is induced by interferon-gamma and LDL(ox) implicating the iNOS-S100A8/9 transnitrosylase complex and seems to prevent interaction with phosphorylated RPL13A and to interfere with GAIT complex activity (By similarity). {ECO:0000250|UniProtKB:P04406, ECO:0000250|UniProtKB:P04797}.; PTM: Sulfhydration at Cys-150 increases catalytic activity. {ECO:0000250|UniProtKB:P16858}. | SUBCELLULAR LOCATION: Cytoplasm, cytosol {ECO:0000250|UniProtKB:P04797}. Cytoplasm, cytoskeleton {ECO:0000250|UniProtKB:P04797}. Nucleus {ECO:0000250|UniProtKB:P04797}. Note=Translocates to the nucleus following S-nitrosylation and interaction with SIAH1, which contains a nuclear localization signal. Colocalizes with CHP1 to small punctate structures along the microtubules tracks. {ECO:0000250|UniProtKB:P04797}. | CATALYTIC ACTIVITY: Reaction=D-glyceraldehyde 3-phosphate + NAD(+) + phosphate = (2R)-3-phospho-glyceroyl phosphate + H(+) + NADH; Xref=Rhea:RHEA:10300, ChEBI:CHEBI:15378, ChEBI:CHEBI:43474, ChEBI:CHEBI:57540, ChEBI:CHEBI:57604, ChEBI:CHEBI:57945, ChEBI:CHEBI:59776; EC=1.2.1.12; Evidence={ECO:0000250|UniProtKB:P04406, ECO:0000255|PROSITE-ProRule:PRU10009}; CATALYTIC ACTIVITY: Reaction=L-cysteinyl-[protein] + S-nitroso-L-cysteinyl-[GAPDH] = L-cysteinyl-[GAPDH] + S-nitroso-L-cysteinyl-[protein]; Xref=Rhea:RHEA:66684, Rhea:RHEA-COMP:10131, Rhea:RHEA-COMP:17089, Rhea:RHEA-COMP:17090, Rhea:RHEA-COMP:17091, ChEBI:CHEBI:29950, ChEBI:CHEBI:149494; Evidence={ECO:0000250|UniProtKB:P04797}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:66685; Evidence={ECO:0000250|UniProtKB:P04797}; | null | PATHWAY: Carbohydrate degradation; glycolysis; pyruvate from D-glyceraldehyde 3-phosphate: step 1/5. | null | null | FUNCTION: Has both glyceraldehyde-3-phosphate dehydrogenase and nitrosylase activities, thereby playing a role in glycolysis and nuclear functions, respectively. Glyceraldehyde-3-phosphate dehydrogenase is a key enzyme in glycolysis that catalyzes the first step of the pathway by converting D-glyceraldehyde 3-phosphate (G3P) into 3-phospho-D-glyceroyl phosphate (By similarity). Modulates the organization and assembly of the cytoskeleton. Facilitates the CHP1-dependent microtubule and membrane associations through its ability to stimulate the binding of CHP1 to microtubules (By similarity). Component of the GAIT (gamma interferon-activated inhibitor of translation) complex which mediates interferon-gamma-induced transcript-selective translation inhibition in inflammation processes. Upon interferon-gamma treatment assembles into the GAIT complex which binds to stem loop-containing GAIT elements in the 3'-UTR of diverse inflammatory mRNAs (such as ceruplasmin) and suppresses their translation. Also plays a role in innate immunity by promoting TNF-induced NF-kappa-B activation and type I interferon production, via interaction with TRAF2 and TRAF3, respectively (By similarity). Participates in nuclear events including transcription, RNA transport, DNA replication and apoptosis. Nuclear functions are probably due to the nitrosylase activity that mediates cysteine S-nitrosylation of nuclear target proteins such as SIRT1, HDAC2 and PRKDC (By similarity). {ECO:0000250|UniProtKB:P04406, ECO:0000250|UniProtKB:P04797}. | Mustela putorius furo (European domestic ferret) (Mustela furo) |
A3FMB2 | POLG_HAVH2 | MNMSKQGIFQTVGSGLDHILSLADIEEEQMIQSVDRTAVTGASYFTSVDQSSVHTAEVGSHQIEPLKTSVDKPGSKKTQGEKFFLIHSADWLTTHALFHEVAKLDVVKLLYNEQFAVQGLLRYHTYARFGIEIQVQINPTPFQQGGLICAMVPGDQSYGSIASLTVYPHGLLNCNINNVVRIKVPFIYTRGAYHFKDPQYPVWELTIRVWSELNIGTGTSAYTSLNVLARFTDLELHGLTPLSTQMMRNEFRVSTTENVVNLSNYEDARAKMSFALDPEDWKSDPSQGGGIKITHFTTWTSIPTLAAQFPFNASDSVGQQIKVIPVDPYFFQMTNTNPDQKCITALASICQMFCFWRGDLVFDFQVFPTKYHSGRLLFCFVPGNELIDVTGITLKQATTAPCAVMDITGVQSTLRFRVPWISDTPYRVNRYTKSAHQKGEYTAIGKLIVYCYNRLTSPSNVASHVRVNVYLSAINLECFAPLYHAMDVTTQVGDDSGGFSTTVSTEQNVPDPQVGITTMRDLKGKANRGKMDVSGVQAPVGAITTIEDPVLAKKVPETFPELKPGESRHTSDHMSIYKFMGRSHFLCTFTFNSNNKEYTFPITLSSTSNPPHGLPSTLRWFFNLFQLYRGPLDLTIIITGATDVDGMAWFTPVGLAVDTPWVEKESALSIDYKTALGAVRFNTRRTGNIQIRLPWYSYLYAVSGALDGLGDKTDSTFGLVSIQIANYNHSDEYLSFSCYLSVTEQSEFYFPRAPLNSNAMLSTESMMSRIAAGDLESSVDDPRSEEDRRFESHIECRKPYKELRLEVGKQRLKYAQEELSNEVLPPPRKMKGLFSQAKISLFYTEEHEIMKFSWRGVTADTRALRRFGFSMAAGRSVWTLEMDAGVLTGRLVRLNDEKWTEMKDDKIVSLIEKFTSNKYWSKVSFPHGMLDLEEIAANSTDFPNMSETDLCFLLHWLNPKKINLADRMLGLSGVQEIKEQGVGLIAECRTFLDSIAGTLKSMMFGFHHSVTVEIINTVLCFVKSGILLYVIQQLNQDEHSHIIGLLRVMNYADIGCSVISCGKVFSKMLETVFNWQMDSRMMELRTQSFSNWLRDICSGITIFKSFKDAIYWLYTKLKDFYEVNYGKKKDILNILKDNQQKIEKAIEEADNFCILQIQDVEKFDQYQKGVDLIQKLRTVHSMAQVDPNLGVHLSPLRDCIARVHQKLKNLGSINQAMVTRCEPVVCYLYGKRGGGKSLTSIALATKICKHYGVEPEKNIYTKPVASDYWDGYSGQLVCIIDDIGQNTTDEDWSDFCQLVSGCPMRLNMASLEEKGRHFSSPFIIATSNWSNPSPKTVYVKEAIDRRLHFKVEVKPASFFKNPHNDMLNVNLAKTNDAIKDMSCVDLIMDGHNISLMDLLSSLVMTVEIRKQNMSEFMELWSQGISDDDNDSAVAEFFQSFPSGEPSNSKLSSFFQSVTNHKWVAVGAAVGILGVLVGGWFVYKHFSRKEEEPIPAEGVYHGVTKPKQVIKLDADPVESQSTLEIAGLVRKNLVQFGVGEKNGCVRWVMNALGVKDDWLLVPSHAYKFEKDYEMMEFYFNRGGTYYSISAGNVVIQSLDVGFQDVVLMKVPTIPKFRDITQHFIKKGDVPRALNRLATLVTTVNGTPMLISEGPLKMEEKATYVHKKNDGTTVDLTVDQAWRGKGEGLPGMCGGALVSSNQSIQNAILGIHVAGGNSILVAKLVTQEMFQNIDKKIESQRIMKVEFTQCSMNVVSKTLFRKSPIHHHIDKTMINFPAVMPFSKAEVDPMAVMLSKYSLPIVEEPEDYKEASIFYQNKIVGKTQLVDDFLDLDMAITGAPGIDAINMDSSPGFPYVQEKLTKRDLIWLDENGLLLGVHPRLAQRILFNTVMMENCSDLDVVFTTCPKDELRPLEKVLESKTRAIDACPLDYTILCRMYWGPAISYFHLNPGFHTGVAIGIDPDRQWDELFKTMIRFGDVGLDLDFSAFDASLSPFMIREAGRIMSELSGTPSHFGTALINTIIYSKHLLYNCCYHVCGSMPSGSPCTALLNSIINNINLYYVFSKIFGKSPVFFCQALRILCYGDDVLIVFSRDVQIDNLDLIGQKIVDEFKKLGMTATSADKNVPQLKPVSELTFLKRSFNLVEDRIRPAISEKTIWSLIAWQRSNAEFEQNLENAQWFAFMHGYEFYQKFYYFVQSCLEKEMIEYRLKSYDWWRMRFYDQCFICDLS | 2.7.7.48; 3.4.22.28; 3.6.1.15 | null | DNA-templated transcription [GO:0006351]; protein complex oligomerization [GO:0051259]; proteolysis [GO:0006508]; symbiont entry into host cell [GO:0046718]; symbiont-mediated suppression of host cytoplasmic pattern recognition receptor signaling pathway via inhibition of MAVS activity [GO:0039545]; viral RNA genome replication [GO:0039694]; virion attachment to host cell [GO:0019062]; virus-mediated perturbation of host defense response [GO:0019049] | host cell cytoplasmic vesicle membrane [GO:0044162]; host cell mitochondrial outer membrane [GO:0044193]; host multivesicular body [GO:0072494]; membrane [GO:0016020]; T=pseudo3 icosahedral viral capsid [GO:0039618] | ATP binding [GO:0005524]; cysteine-type endopeptidase activity [GO:0004197]; monoatomic ion channel activity [GO:0005216]; ribonucleoside triphosphate phosphatase activity [GO:0017111]; RNA binding [GO:0003723]; RNA helicase activity [GO:0003724]; RNA-dependent RNA polymerase activity [GO:0003968]; structural molecule activity [GO:0005198] | PF20758;PF12944;PF00548;PF00680;PF00073;PF00910; | 1.20.960.20;2.60.120.20;3.30.70.270;2.40.10.10; | Picornaviridae polyprotein family | PTM: [Genome polyprotein]: Specific enzymatic cleavages by viral protease in vivo yield a variety of precursors and mature proteins. Polyprotein processing intermediates are produced, such as P1-2A which is a functional precursor of the structural proteins, VP0 which is a VP4-VP2 precursor, VP1-2A precursor, 3ABC precursor which is a stable and catalytically active precursor of 3A, 3B and 3C proteins, 3AB and 3CD precursors. The assembly signal 2A is removed from VP1-2A by a host protease, possibly host Cathepsin L. This cleavage occurs over a region of 3 amino-acids probably generating VP1 proteins with heterogeneous C-termini. {ECO:0000250|UniProtKB:P08617}.; PTM: [Capsid protein VP0]: During virion maturation, immature virions are rendered infectious following cleavage of VP0 into VP4 and VP2. This maturation seems to be an autocatalytic event triggered by the presence of RNA in the capsid and is followed by a conformational change of the particle. {ECO:0000250|UniProtKB:P03303}.; PTM: [Protein VP1-2A]: The assembly signal 2A is removed from VP1-2A by a host protease, possibly host Cathepsin L in naked virions. This cleavage does not occur in enveloped virions. This cleavage occurs over a region of 3 amino-acids probably generating VP1 proteins with heterogeneous C-termini. {ECO:0000250|UniProtKB:P08617}.; PTM: [Viral protein genome-linked]: VPg is uridylylated prior to priming replication into VPg-pUpU. {ECO:0000250|UniProtKB:P03300}.; PTM: [Capsid protein VP4]: Unlike other picornaviruses, does not seem to be myristoylated. {ECO:0000250|UniProtKB:P08617}. | SUBCELLULAR LOCATION: [Capsid protein VP2]: Virion {ECO:0000250|UniProtKB:P08617}. Host endosome, host multivesicular body {ECO:0000250|UniProtKB:P08617}. Note=The egress of newly formed virions occurs through an exosome-like mechanism involving endosomal budding of viral capsids into multivesicular bodies. {ECO:0000250|UniProtKB:P08617}.; SUBCELLULAR LOCATION: [Capsid protein VP3]: Virion {ECO:0000250|UniProtKB:P08617}. Host endosome, host multivesicular body {ECO:0000250|UniProtKB:P08617}. Note=The egress of newly formed virions occurs through an exosome-like mechanism involving endosomal budding of viral capsids into multivesicular bodies. {ECO:0000250|UniProtKB:P08617}.; SUBCELLULAR LOCATION: [Capsid protein VP1]: Virion {ECO:0000250|UniProtKB:P08617}. Host endosome, host multivesicular body {ECO:0000250|UniProtKB:P08617}. Note=The egress of newly formed virions occurs through an exosome-like mechanism involving endosomal budding of viral capsids into multivesicular bodies. {ECO:0000250|UniProtKB:P08617}.; SUBCELLULAR LOCATION: [Capsid protein VP4]: Virion {ECO:0000250|UniProtKB:P08617}. Note=Present in the full mature virion. The egress of newly formed virions occurs through an exosome-like mechanism involving endosomal budding of viral capsids into multivesicular bodies. {ECO:0000250|UniProtKB:P08617}.; SUBCELLULAR LOCATION: [Protein 2B]: Host membrane {ECO:0000250|UniProtKB:P08617}; Peripheral membrane protein {ECO:0000250|UniProtKB:P08617}. Note=Probably localizes to intracellular membrane vesicles that are induced after virus infection as the site for viral RNA replication. {ECO:0000250|UniProtKB:P08617}.; SUBCELLULAR LOCATION: [Protein 2C]: Host membrane {ECO:0000250|UniProtKB:P08617}; Single-pass membrane protein {ECO:0000250|UniProtKB:P08617}. Note=Probably localizes to intracellular membrane vesicles that are induced after virus infection as the site for viral RNA replication. May associate with membranes through a N-terminal amphipathic helix. {ECO:0000250|UniProtKB:P08617}.; SUBCELLULAR LOCATION: [Protein 3ABC]: Host membrane {ECO:0000250|UniProtKB:P08617}; Single-pass membrane protein {ECO:0000255}. Host mitochondrion outer membrane {ECO:0000250|UniProtKB:P08617}; Single-pass membrane protein {ECO:0000250|UniProtKB:P08617}. Note=Probably localizes to intracellular membrane vesicles that are induced after virus infection as the site for viral RNA replication. {ECO:0000250|UniProtKB:P08617}.; SUBCELLULAR LOCATION: [Protein 3AB]: Host membrane {ECO:0000250|UniProtKB:P08617}; Single-pass membrane protein {ECO:0000255}. Note=Probably localizes to intracellular membrane vesicles that are induced after virus infection as the site for viral RNA replication. {ECO:0000250|UniProtKB:P08617}.; SUBCELLULAR LOCATION: [Protein 3A]: Host membrane {ECO:0000250|UniProtKB:P08617}; Single-pass membrane protein {ECO:0000255}. Note=Probably localizes to intracellular membrane vesicles that are induced after virus infection as the site for viral RNA replication. {ECO:0000250|UniProtKB:P08617}.; SUBCELLULAR LOCATION: [Viral protein genome-linked]: Virion {ECO:0000250|UniProtKB:P08617}.; SUBCELLULAR LOCATION: [Protease 3C]: Host cytoplasm {ECO:0000250|UniProtKB:P08617}.; SUBCELLULAR LOCATION: [RNA-directed RNA polymerase 3D-POL]: Host cytoplasmic vesicle membrane {ECO:0000250|UniProtKB:P08617}; Peripheral membrane protein {ECO:0000250|UniProtKB:P08617}; Cytoplasmic side {ECO:0000250|UniProtKB:P08617}. Note=Interacts with membranes in a complex with viral protein 3AB. Probably localizes to the surface of intracellular membrane vesicles that are induced after virus infection as the site for viral RNA replication. These vesicles are derived from the endoplasmic reticulum. {ECO:0000250|UniProtKB:P08617}. | CATALYTIC ACTIVITY: Reaction=a ribonucleoside 5'-triphosphate + RNA(n) = diphosphate + RNA(n+1); Xref=Rhea:RHEA:21248, Rhea:RHEA-COMP:14527, Rhea:RHEA-COMP:17342, ChEBI:CHEBI:33019, ChEBI:CHEBI:61557, ChEBI:CHEBI:140395; EC=2.7.7.48; Evidence={ECO:0000250|UniProtKB:P08617, ECO:0000255|PROSITE-ProRule:PRU00539}; CATALYTIC ACTIVITY: Reaction=a ribonucleoside 5'-triphosphate + H2O = a ribonucleoside 5'-diphosphate + H(+) + phosphate; Xref=Rhea:RHEA:23680, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:43474, ChEBI:CHEBI:57930, ChEBI:CHEBI:61557; EC=3.6.1.15; Evidence={ECO:0000250|UniProtKB:P08617}; CATALYTIC ACTIVITY: Reaction=Selective cleavage of Gln-|-Gly bond in the poliovirus polyprotein. In other picornavirus reactions Glu may be substituted for Gln, and Ser or Thr for Gly.; EC=3.4.22.28; Evidence={ECO:0000255|PROSITE-ProRule:PRU01222}; | null | null | null | null | FUNCTION: [Capsid protein VP1]: Capsid proteins VP1, VP2, and VP3 form a closed capsid enclosing the viral positive strand RNA genome. All these proteins contain a beta-sheet structure called beta-barrel jelly roll. Together they form an icosahedral capsid (T=3) composed of 60 copies of each VP1, VP2, and VP3, with a diameter of approximately 300 Angstroms. VP1 is situated at the 12 fivefold axes, whereas VP2 and VP3 are located at the quasi-sixfold axes. The naked capsid interacts with the host receptor HAVCR1 to provide virion attachment to and probably entry into the target cell. {ECO:0000250|UniProtKB:P08617}.; FUNCTION: [Capsid protein VP2]: Capsid proteins VP1, VP2, and VP3 form a closed capsid enclosing the viral positive strand RNA genome. All these proteins contain a beta-sheet structure called beta-barrel jelly roll. Together they form an icosahedral capsid (T=3) composed of 60 copies of each VP1, VP2, and VP3, with a diameter of approximately 300 Angstroms. VP1 is situated at the 12 fivefold axes, whereas VP2 and VP3 are located at the quasi-sixfold axes. The naked capsid interacts with the host receptor HAVCR1 to provide virion attachment to and probably entry into the target cell. {ECO:0000250|UniProtKB:P08617}.; FUNCTION: [Capsid protein VP3]: Capsid proteins VP1, VP2, and VP3 form a closed capsid enclosing the viral positive strand RNA genome. All these proteins contain a beta-sheet structure called beta-barrel jelly roll. Together they form an icosahedral capsid (T=3) composed of 60 copies of each VP1, VP2, and VP3, with a diameter of approximately 300 Angstroms. VP1 is situated at the 12 fivefold axes, whereas VP2 and VP3 are located at the quasi-sixfold axes. The naked capsid interacts with the host receptor HAVCR1 to provide virion attachment to and probably entry into the target cell. {ECO:0000250|UniProtKB:P08617}.; FUNCTION: [Capsid protein VP0]: VP0 precursor is a component of the immature procapsids. {ECO:0000250|UniProtKB:P08617}.; FUNCTION: [Capsid protein VP4]: Plays a role in the assembly of the 12 pentamers into an icosahedral structure. Has not been detected in mature virions, supposedly owing to its small size. {ECO:0000250|UniProtKB:P08617}.; FUNCTION: [Protein VP1-2A]: Precursor component of immature procapsids that corresponds to an extended form of the structural protein VP1. After maturation, possibly by the host Cathepsin L, the assembly signal 2A is cleaved to give rise to the mature VP1 protein. {ECO:0000250|UniProtKB:P08617}.; FUNCTION: [Protein 2B]: Functions as a viroporin. Affects membrane integrity and causes an increase in membrane permeability. Involved in host intracellular membrane rearrangements probably to give rise to the viral factories. Does not disrupt calcium homeostasis or glycoprotein trafficking. Antagonizes the innate immune response of the host by suppressing IFN-beta synthesis, which it achieves by interfering with the RIG-I/IFIH1 pathway. {ECO:0000250|UniProtKB:P08617}.; FUNCTION: [Protein 2BC]: Affects membrane integrity and causes an increase in membrane permeability. {ECO:0000250|UniProtKB:P08617}.; FUNCTION: [Protein 2C]: Associates with and induces structural rearrangements of intracellular membranes. Displays RNA-binding activity. {ECO:0000250|UniProtKB:P08617}.; FUNCTION: [Protein 3ABC]: The precursor 3ABC is targeted to the mitochondrial membrane where protease 3C activity cleaves and inhibits the host antiviral protein MAVS, thereby disrupting activation of IRF3 through the IFIH1/MDA5 pathway. In vivo, the protease activity of 3ABC precursor is more efficient in cleaving the 2BC precursor than that of protein 3C. The 3ABC precursor may therefore play a role in the proteolytic processing of the polyprotein. Possible viroporin. {ECO:0000250|UniProtKB:P08617}.; FUNCTION: [Protein 3AB]: Interacts with the 3CD precursor and with RNA structures found at both the 5'- and 3'-termini of the viral genome. Since the 3AB precursor contains the hydrophobic domain 3A, it probably anchors the whole viral replicase complex to intracellular membranes on which viral RNA synthesis occurs. {ECO:0000250|UniProtKB:P08617}.; FUNCTION: [Protein 3A]: May serve as membrane anchor to the 3AB and 3ABC precursors via its hydrophobic domain. May interact with RNA. {ECO:0000250|UniProtKB:P08617}.; FUNCTION: [Viral protein genome-linked]: Acts as a primer for viral RNA replication and remains covalently bound to viral genomic RNA. VPg is uridylylated prior to priming replication into VPg-pUpU. The VPg-pUpU is then used as primer on the genomic RNA poly(A) by the RNA-dependent RNA polymerase to replicate the viral genome. {ECO:0000250|UniProtKB:P03300, ECO:0000250|UniProtKB:P08617}.; FUNCTION: [Protease 3C]: Cysteine protease that generates mature viral proteins from the precursor polyprotein. In addition to its proteolytic activity, it binds to viral RNA, and thus influences viral genome replication. RNA and substrate bind cooperatively to the protease. Cleaves IKBKG/NEMO to impair innate immune signaling. Cleaves host PABPC1 which may participate in the switch of viral translation to RNA synthesis. {ECO:0000250|UniProtKB:P08617}.; FUNCTION: [Protein 3CD]: Interacts with the 3AB precursor and with RNA structures found at both the 5'- and 3'-termini of the viral genome. Disrupts TLR3 signaling by degrading the host adapter protein TICAM1/TRIF. {ECO:0000250|UniProtKB:P08617}.; FUNCTION: RNA-directed RNA polymerase 3D-POL replicates genomic and antigenomic RNA by recognizing replications specific signals. {ECO:0000250|UniProtKB:P08617}. | Human hepatitis A virus genotype IA (isolate H2) (HHAV) (Human hepatitis A virus (isolate Human/China/H2/1982)) |
A3KCL7 | OXDD_PIG | MDTVRIAVVGAGVMGLSTAVCIFKLVPGCSITVISDKFTPETTSDVAAGMLIPPVYPDTPIHKQKQWFKDTFDHLFAIANSAEAKDAGVLLVSGWQIFQSAPTEEVPFWADVVLGFRKMTKNELKKFPQHVCGQAFTTLKCEGPTYLPWLEKRVKGSGGLVLTRRVEDLWELHPSFNIVVNCSGLGSKQLVGDMEIFPVRGQVLKVQAPWVKHFIRDGSGLTYIYPGIANVTLGGTRQKGDWNLSPNAEISKQILSRCCALEPSLRGACDIREKVGLRPSRPGVRLEKELLVQGSQRLPVVHNYGHGSGGIAMHWGTALEAARLVSECVQALRTPAPKSKL | 1.4.3.1 | COFACTOR: Name=FAD; Xref=ChEBI:CHEBI:57692; Evidence={ECO:0000269|PubMed:17234685}; | aspartate catabolic process [GO:0006533]; D-amino acid catabolic process [GO:0019478]; nervous system process [GO:0050877] | cytoplasm [GO:0005737]; cytosol [GO:0005829]; peroxisomal matrix [GO:0005782]; peroxisome [GO:0005777] | D-aspartate oxidase activity [GO:0008445]; D-glutamate oxidase activity [GO:0047821]; FAD binding [GO:0071949] | PF01266; | 3.30.9.10;3.40.50.720; | DAMOX/DASOX family | null | SUBCELLULAR LOCATION: Peroxisome matrix {ECO:0000305|PubMed:20819121, ECO:0000305|PubMed:20976510}. Cytoplasm, cytosol {ECO:0000250|UniProtKB:Q99489}. Note=Active in the peroxisomal matrix. {ECO:0000250|UniProtKB:Q99489}. | CATALYTIC ACTIVITY: Reaction=D-aspartate + H2O + O2 = H2O2 + NH4(+) + oxaloacetate; Xref=Rhea:RHEA:12512, ChEBI:CHEBI:15377, ChEBI:CHEBI:15379, ChEBI:CHEBI:16240, ChEBI:CHEBI:16452, ChEBI:CHEBI:28938, ChEBI:CHEBI:29990; EC=1.4.3.1; Evidence={ECO:0000269|PubMed:16751595, ECO:0000269|PubMed:17234685}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:12513; Evidence={ECO:0000269|PubMed:16751595, ECO:0000269|PubMed:17234685}; CATALYTIC ACTIVITY: Reaction=D-glutamate + H2O + O2 = 2-oxoglutarate + H2O2 + NH4(+); Xref=Rhea:RHEA:10028, ChEBI:CHEBI:15377, ChEBI:CHEBI:15379, ChEBI:CHEBI:16240, ChEBI:CHEBI:16810, ChEBI:CHEBI:28938, ChEBI:CHEBI:29986; Evidence={ECO:0000269|PubMed:17234685}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:10029; Evidence={ECO:0000269|PubMed:17234685}; | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=0.613 mM for D-aspartate (at 37 degrees Celsius and at pH 8.3) {ECO:0000269|PubMed:17234685}; KM=2.2 mM for D-aspartate (at 25 degrees Celsius and at pH 8.3) {ECO:0000269|PubMed:16751595}; KM=0.547 mM for D-glutamate (at 37 degrees Celsius and at pH 8.3) {ECO:0000269|PubMed:17234685}; KM=2.01 mM for N-methyl D-aspartate (at 37 degrees Celsius and at pH 8.3) {ECO:0000269|PubMed:17234685}; Note=kcat is 172 sec(-1) with D-aspartate as substrate (at 37 degrees Celsius and at pH 8.3) (PubMed:17234685). kcat is 46.7 sec(-1) with D-aspartate as substrate (at 25 degrees Celsius and at pH 8.3) (PubMed:16751595). kcat is 30 sec(-1) with D-glutamate as substrate (at 37 degrees Celsius and at pH 8.3) (PubMed:17234685). kcat is 635 sec(-1) with N-methyl D-aspartate as substrate (at 37 degrees Celsius and at pH 8.3) (PubMed:17234685). {ECO:0000269|PubMed:16751595, ECO:0000269|PubMed:17234685}; | null | BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 7.5 to 9.0. {ECO:0000269|PubMed:17234685}; | null | FUNCTION: Selectively catalyzes the oxidative deamination of acidic amino acids (PubMed:16751595, PubMed:17234685). Suppresses the level of D-aspartate in the brain, an amino acid that can act as an agonist for glutamate receptors (By similarity). Protects the organism from the toxicity of D-amino acids (By similarity). May also function in the intestine (By similarity). {ECO:0000250|UniProtKB:D3ZDM7, ECO:0000250|UniProtKB:Q922Z0, ECO:0000269|PubMed:16751595, ECO:0000269|PubMed:17234685}. | Sus scrofa (Pig) |
A3KFM7 | CHD6_MOUSE | MKMKIQKKEKQLSKLRALNHSPMSDASVNFDYKSPSPFDCSPDQGENIEEAANHCLPHKNLYTTEEEADTLFSRKLTSHNGMEDSGGRGTGVKKKRKKKEPGEQEGTKGSKDREPKPKRKREPKEPKEPRRAKEPKRAKEPKETKQKDGVKKPRKHREASGTKEGKEKRSCTDYGSRTKSKKASREQGPTPVERKKKGKRKNETTVESLELDHSLPNPSLQSPEEPSESADSQKRRSGRQVKRRKYNEDLDFKVVDDDGETIAVLGAGRTSALSASTLAWQAEEPPEDDANIIEKILASKTVQEVHPGEPPFDLELFYVKYRNFSYLHCKWATMEELEKDPRIAQKIKRFRNKQAQMKHIFTEPDEDLFNPDYIEIDRILEVAHTKDAETGEEVTHYLVKWCSLPYEESTWELEEDVDPAKVKEFESLQILPEVKHVERPASDAWQKLETSREYRNSNRLREYQLEGMNWLLFNWYNRKNCILADEMGLGKTIQSIAFLSEIFVRGIHGPFLIIAPLSTITNWEREFRTWTEMNAIVYHGSQISRQMIQQYEMVYRDAQGNPLSGVFKFHVVITTFEMILADCPELKKIHWSCVIIDEAHRLKNRNCKLLEGLKLMALEHKVLLTGTPLQNSVEELFSLLNFLEPSQFPSETAFLEEFGDLKTEEQVKKLQSILKPMMLRRLKDDVEKNLAPKQETIIEVELTNIQKKYYRAILEKNFSFLTKGANQHNMPNLINTMMELRKCCNHPYLINGAEEKILEDFRKAHSSEASDFQLQAMIQAAGKLVLIDKLLPKLIAGGHKVLIFSQMVRCLDILEDYLIQRRYTYERIDGRVRGNLRQAAIDRFCKPDSDRFVFLLCTRAGGLGINLTAADTCIIFDSDWNPQNDLQAQARCHRIGQSKAVKVYRLITRNSYEREMFDKASLKLGLDKAILQDINRKGSTNGVQQLSKMEVEDLLRKGAYGALMDEEDEGSKFCEEDIDQILQRRTHTITIQSEGKGSTFAKASFVASGNRTDISLDDPNFWQKWAKIAELDTEANNEKESLVIDRPRVRKQTKHYNSFEEDELMEFSELDSDSDERPTRSRRLSDRARRYLRAECFRVEKNLLIFGWGRWKDILTHGRFKWPLNEKDMEMICRALLVYCVKHYKGDEKIKSFIWELITPSKDGQVQTLQNHSGLSAPVPRGRKGKKTKNQLLLPELKNADWLATCNPEVVLHDDGYKKHLKQHCNKVLLRVRMLYYLKAEILGEAADKAFEGTPARELDVLLPDIDYVEIPVDWWDAEADKSLLIGVFKHGYERYNAMRADPALCFLEKVGMPDEKSLSAEQGVTDGTSDIPERGNIDKEDSAEDKLDGLQKQTASPSDGSDGIFGEKKDDSQAAQDGSDPDKSPWPVSSALTARLRRLVTIYQRCNRKELCRPEILGPGNQGYWVQEEVFRRTSEMDLINKEAQKRWTRREQADFYRTVSSFGVVYDQEKKAFDWTQFRIISRLDKKSDESLEHYFYSFVAMCRNVCRLPAWKDDGPPDASIYVEPITEERAAKTLYRIELLRKVREQVLMCPQLHERLQLCRPSLYLPVWWECGKHDRDLLIGTAKHGLNRTDYYIMNDPQLSFLDAYRNYAQHKRTDTQAPGSLCCLYQSNSKLYESLTYTPVSRTSESLESEPENLMRMESRDDHLCLPEGGLPDITCENFVSKVQEVISLDHDENLLPESLENMIYGKTGLSQEPHSFQEAPTTNTQSRKNTITISASRNESCQPPGIEAEITSASSLMSSLEAGVAKMNIKNGKHLLVSISKEGEPCCSETGRRPETIGHREAKCLVSPTLDTGHESGFVDLCSLSVYDPKRNFSSDQQLIDLLENKSLESKLILNQSDEEEEENEDETLAIVASATEKPEVLDFPKPTVNIPRGKNLSFHQDEAKKGRLEVVSKTAGPQRVFPPPANQCHCKHIERWAHGLGSEDSEVEKPKAYQPDLYRSKANNSTVEGETAVIPTEPFKLKHELLKEPWKESSEGGKSFSMYAPEGSEPKPEDMDFENKDDYEKDGTCLSQDYPGKYSEEESKSSASGIAGDLGEEAQEVRAPTIAQLLQEKTLYSFSEWPKDRVIINRLDNICHVVLKGKWPCSHQYEPSGALPTPVLSSSAGSRSSLSEPEATEHGFSNGAALAAQIQKESFLAPVFTKDEQKHRRPYEFEVERDAKARSLEEYSATHGRPPIVLNGWHGESAIDLSCSSEGSPGATSPFPVSASTPKIGAISSLQGALGMDLSGILQAGLIHPVTGQIVNGSLRRDDAAMRRRRGRRKHIEGGMDLIFLKEQTLQAGILEVHEDAGQTTLSTTHPEVPGATSSAPEPTAAASSQAEKAVPSKSLLDWLRQQADYSLDVPGFGTSFSDKPKQRRPRCKEPGKLDISSLGGEERVPAVPKEPGLRGFLPESKFNHTLAEPVLRDAGPRRRGRRPRNELLKAPAIVADSPSGMGPLFMNGLIAGMDLVGLQNVRNIPGIPLTGLVGFPAGFATMPTGEEVKNTLSMLPMMLPGMAAVPQMFGVGGLLNTPMATTCTTTASASLASTKSGTSATEKSTEDKLSGHDVNTDALVDDKPGPSPFSDQSEPTITTSSPVAFNPFLIPGVSPGLIYPSMFLSPGMGMALPAMQQARHSEMVGLETQKRKKKKTKGDSPTQEPASVCEKEPGSDQNCTESSATVSPEREHVAQAREEGLKDSNEDTN | 3.6.4.12 | null | cell redox homeostasis [GO:0045454]; chromatin remodeling [GO:0006338]; positive regulation of transcription by RNA polymerase II [GO:0045944]; regulation of gene expression [GO:0010468] | chromatin [GO:0000785]; nucleoplasm [GO:0005654]; nucleus [GO:0005634] | ATP binding [GO:0005524]; ATP hydrolysis activity [GO:0016887]; ATP-dependent activity, acting on DNA [GO:0008094]; ATP-dependent chromatin remodeler activity [GO:0140658]; chromatin binding [GO:0003682]; DNA binding [GO:0003677]; helicase activity [GO:0004386]; histone binding [GO:0042393]; transcription coregulator binding [GO:0001221] | PF00385;PF00271;PF00176; | 2.40.50.40;1.10.10.60;3.40.50.300;3.40.50.10810; | SNF2/RAD54 helicase family | null | SUBCELLULAR LOCATION: Nucleus, nucleoplasm {ECO:0000250|UniProtKB:Q8TD26}. Note=Enriched at sites of mRNA synthesis. {ECO:0000250|UniProtKB:Q8TD26}. | CATALYTIC ACTIVITY: Reaction=ATP + H2O = ADP + H(+) + phosphate; Xref=Rhea:RHEA:13065, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:456216; EC=3.6.4.12; Evidence={ECO:0000250|UniProtKB:Q8TD26}; | null | null | null | null | FUNCTION: DNA-dependent ATPase that plays a role in chromatin remodeling. Regulates transcription by disrupting nucleosomes in a largely non-sliding manner which strongly increases the accessibility of chromatin. Activates transcription of specific genes in response to oxidative stress through interaction with NFE2L2. {ECO:0000250|UniProtKB:Q8TD26}. | Mus musculus (Mouse) |
A3KFX0 | 5NT1A_MOUSE | MEPGQPREAREPGPGAETAAVPRWEEAKTFYDNLSSKKKPKSPKPQNAVTIAVSSRALFRMDEEQRIYTEQGVEEYVRYQLEHENEPFSPGPAFPFVKALEAVNKRLRELYPDSEDIFDIVLMTNNHAQVGVRLINSINHYDLFIERFCMTGGNSPICYLKAYHTNLYLSADADKVREAIDEGIAAATIFSPSRDVVVSQSQLRVAFDGDAVLFSDESERIVKAHGLDRFFEHEKAHENKPLAQGPLKGFLEALGRLQKKFYSKGLRLECPIRTYLVTARSAASSGARALKTLRSWGLETDEALFLAGAPKGPLLEKIRPHIFFDDQMFHVAGAQEMGTVAAHVPYGVAQNPRRAAAAKQSLGAQ | 3.1.3.5; 3.1.3.89; 3.1.3.99 | COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250|UniProtKB:Q9BXI3}; | adenosine metabolic process [GO:0046085]; allantoin metabolic process [GO:0000255]; amide catabolic process [GO:0043605]; AMP catabolic process [GO:0006196]; dAMP catabolic process [GO:0046059]; dGMP catabolic process [GO:0046055]; IMP catabolic process [GO:0006204]; purine nucleoside monophosphate catabolic process [GO:0009128] | cytosol [GO:0005829] | 5'-nucleotidase activity [GO:0008253]; IMP 5'-nucleotidase activity [GO:0050483]; magnesium ion binding [GO:0000287]; nucleotide binding [GO:0000166]; XMP 5'-nucleosidase activity [GO:0106411] | PF06189; | null | 5'-nucleotidase type 3 family | null | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q9BXI3}. | CATALYTIC ACTIVITY: Reaction=a ribonucleoside 5'-phosphate + H2O = a ribonucleoside + phosphate; Xref=Rhea:RHEA:12484, ChEBI:CHEBI:15377, ChEBI:CHEBI:18254, ChEBI:CHEBI:43474, ChEBI:CHEBI:58043; EC=3.1.3.5; Evidence={ECO:0000250|UniProtKB:Q9BXI3}; CATALYTIC ACTIVITY: Reaction=a 2'-deoxyribonucleoside 5'-phosphate + H2O = a 2'-deoxyribonucleoside + phosphate; Xref=Rhea:RHEA:36167, ChEBI:CHEBI:15377, ChEBI:CHEBI:18274, ChEBI:CHEBI:43474, ChEBI:CHEBI:65317; EC=3.1.3.89; Evidence={ECO:0000250|UniProtKB:Q9BXI3}; CATALYTIC ACTIVITY: Reaction=H2O + IMP = inosine + phosphate; Xref=Rhea:RHEA:27718, ChEBI:CHEBI:15377, ChEBI:CHEBI:17596, ChEBI:CHEBI:43474, ChEBI:CHEBI:58053; EC=3.1.3.99; Evidence={ECO:0000250|UniProtKB:Q9BXI3}; CATALYTIC ACTIVITY: Reaction=AMP + H2O = adenosine + phosphate; Xref=Rhea:RHEA:29375, ChEBI:CHEBI:15377, ChEBI:CHEBI:16335, ChEBI:CHEBI:43474, ChEBI:CHEBI:456215; Evidence={ECO:0000250|UniProtKB:Q9BXI3}; CATALYTIC ACTIVITY: Reaction=dCMP + H2O = 2'-deoxycytidine + phosphate; Xref=Rhea:RHEA:29363, ChEBI:CHEBI:15377, ChEBI:CHEBI:15698, ChEBI:CHEBI:43474, ChEBI:CHEBI:57566; Evidence={ECO:0000250|UniProtKB:Q9BXI3}; | null | null | null | null | FUNCTION: Catalyzes the hydrolysis of ribonucleotide and deoxyribonucleotide monophosphates, releasing inorganic phosphate and the corresponding nucleoside (By similarity). AMP is the major substrate but can also hydrolyze dCMP and IMP (By similarity). {ECO:0000250|UniProtKB:Q9BXI3}. | Mus musculus (Mouse) |
A3KG59 | P20D2_MOUSE | MGPVVERPAEPGTSSAAELELLKRRAAERIDEAAERLGALSRAIWSAPELAYEEHRAHGELTRFFECEPPAASWAVQPHFGLPTAFRAEWAPPESAAGPRALQVAFLCEYDALPALGHACGHNLIAEVGVAAALGLRAALESIAAPPPVKVIVLGTPAEEDGGGKIDLIEAGAFENLDVVFMAHPSQENAAYLPDVAEHDVTVKYYGKASHAAAYPWEGVNALDAAVLAYTNLSVLRQQMKPTWRVHGIIKNGGVKPNIIPSYSELVYYFRAPSMKELQVLTKKAEDCFRAAALATGCTVDIESEAHDYYNVIPNKTLCSAYTENGKKLGMEFISEDAVLNGPSGSTDFGNVSFVVPGIHPYFYIGTDALNHTEQYTEAAGSQAAQLYTLRTAKALAMTALDVIFKPALLEGVRKEFKCKLQEEQLLNTAA | 3.4.13.4 | null | proteolysis [GO:0006508]; regulation of protein metabolic process [GO:0051246] | nucleoplasm [GO:0005654] | carboxypeptidase activity [GO:0004180]; dipeptidase activity [GO:0016805]; identical protein binding [GO:0042802] | PF07687;PF01546; | 3.30.70.360;3.40.630.10; | Peptidase M20A family | null | null | CATALYTIC ACTIVITY: Reaction=beta-alanyl-L-lysine + H2O = beta-alanine + L-lysine; Xref=Rhea:RHEA:59608, ChEBI:CHEBI:15377, ChEBI:CHEBI:32551, ChEBI:CHEBI:57966, ChEBI:CHEBI:143161; EC=3.4.13.4; Evidence={ECO:0000269|PubMed:24891507}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:59609; Evidence={ECO:0000305|PubMed:24891507}; CATALYTIC ACTIVITY: Reaction=beta-alanyl-L-arginine + H2O = beta-alanine + L-arginine; Xref=Rhea:RHEA:59616, ChEBI:CHEBI:15377, ChEBI:CHEBI:32682, ChEBI:CHEBI:57966, ChEBI:CHEBI:143157; EC=3.4.13.4; Evidence={ECO:0000269|PubMed:24891507}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:59617; Evidence={ECO:0000305|PubMed:24891507}; CATALYTIC ACTIVITY: Reaction=beta-alanyl-L-ornithine + H2O = beta-alanine + L-ornithine; Xref=Rhea:RHEA:59612, ChEBI:CHEBI:15377, ChEBI:CHEBI:46911, ChEBI:CHEBI:57966, ChEBI:CHEBI:143162; EC=3.4.13.4; Evidence={ECO:0000269|PubMed:24891507}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:59613; Evidence={ECO:0000305|PubMed:24891507}; CATALYTIC ACTIVITY: Reaction=H2O + N(2)-(4-aminobutanoyl)-L-lysine = 4-aminobutanoate + L-lysine; Xref=Rhea:RHEA:59620, ChEBI:CHEBI:15377, ChEBI:CHEBI:32551, ChEBI:CHEBI:59888, ChEBI:CHEBI:143159; EC=3.4.13.4; Evidence={ECO:0000269|PubMed:24891507}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:59621; Evidence={ECO:0000305|PubMed:24891507}; CATALYTIC ACTIVITY: Reaction=H2O + N(2)-(4-aminobutanoyl)-L-arginine = 4-aminobutanoate + L-arginine; Xref=Rhea:RHEA:59628, ChEBI:CHEBI:15377, ChEBI:CHEBI:32682, ChEBI:CHEBI:59888, ChEBI:CHEBI:143158; EC=3.4.13.4; Evidence={ECO:0000269|PubMed:24891507}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:59629; Evidence={ECO:0000305|PubMed:24891507}; CATALYTIC ACTIVITY: Reaction=H2O + N(2)-(4-aminobutanoyl)-L-ornithine = 4-aminobutanoate + L-ornithine; Xref=Rhea:RHEA:59624, ChEBI:CHEBI:15377, ChEBI:CHEBI:46911, ChEBI:CHEBI:59888, ChEBI:CHEBI:143160; EC=3.4.13.4; Evidence={ECO:0000269|PubMed:24891507}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:59625; Evidence={ECO:0000305|PubMed:24891507}; | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=1.9 mM for beta-alanyl-L-lysine {ECO:0000269|PubMed:24891507}; KM=1.9 mM for beta-alanyl-L-ornithine {ECO:0000269|PubMed:24891507}; KM=6.8 mM for beta-alanyl-L-arginine {ECO:0000269|PubMed:24891507}; KM=2.6 mM for N(2)-(4-aminobutanoyl)-L-lysine {ECO:0000269|PubMed:24891507}; KM=1.35 mM for N(2)-(4-aminobutanoyl)-L-ornithine {ECO:0000269|PubMed:24891507}; Vmax=17.4 umol/min/mg enzyme toward beta-alanyl-L-lysine {ECO:0000269|PubMed:24891507}; Vmax=30.7 umol/min/mg enzyme toward beta-alanyl-L-ornithine {ECO:0000269|PubMed:24891507}; Vmax=27 umol/min/mg enzyme toward N(2)-(4-aminobutanoyl)-L-lysine {ECO:0000269|PubMed:24891507}; Vmax=12.5 umol/min/mg enzyme toward N(2)-(4-aminobutanoyl)-L-ornithine {ECO:0000269|PubMed:24891507}; | null | null | null | FUNCTION: Catalyzes the peptide bond hydrolysis in dipeptides having basic amino acids lysine, ornithine or arginine at C-terminus. Postulated to function in a metabolite repair mechanism by eliminating alternate dipeptide by-products formed during carnosine synthesis. {ECO:0000269|PubMed:24891507}. | Mus musculus (Mouse) |
A3KGF7 | PLCB2_MOUSE | MSLLNPVLLPPNVKAYLSQGERFIKWDDETSIASPVILRVDPKGYYLYWTYQNQEMEFLDVTSIRDTRFGKFAKIPKSQKLREVFNMDFPDNHFLLKTLTVVSGPDMVDLTFYNFVSYKENVGKDWAEDVLALAKHPMTVNAPRSTFLDKILVKLKMQLNPEGKIPVKNFFQMFPADRKRVEAALGACHLAKGKNDAINPEDFPESVYKSFLMSLCPRPEIDEIFTSYHSKAKPYMTKEHLTKFINQKQRDPRLNSLLFPPARPEQVQVLIDKYEPSGINVQRGQLSPEGMVWFLCGPENSVLAHDTLLIHQDMTQPLNHYFINSSHNTYLTAGQFSGLSSAEMYRQVLLSGCRCVELDCWKGKPPDEEPIITHGFTMTTDILFKEAIEAIAESAFKTSPYPVILSFENHVDSPRQQAKMAEYCRSMFGETLLTDPLENFPLKPGIPLPSPEDLRGKILIKNKKNQFSGPASPSKKPGGVAEGSLPSSVPVEEDTGWTAEDRTEVEEEEVVEEEEEEESGNLDEEEIKKMQSDEGTAGLEVTAYEEMSSLVNYIQPTKFISFEFSAQKNRSYVVSSFTELKAYELLSKASMQFVDYNKRQMSRVYPKGTRMDSSNYMPQMFWNAGCQMVALNFQTMDLPMQQNMALFEFNGQSGYLLKHEFMRRLDKQFNPFSVDRIDVVVATTLSITIISGQFLSERSVRTYVEVELFGLPGDPKRRYRTKLSPTANSINPVWKEEPFIFEKILMPELASLRIAVMEEGSKFLGHRIIPINALHSGYHHLCLRSESNMALTMPALFVFLEMKDYIPDTWADLTVALANPIKYFNAQDKKSVKLKGVTGSLPEKLFSGTPVASQSNGAPVSAGNGSTAPGTKATGEEATKEVTEPQTASLEELRELKGVVKLQRRHEKELRELERRGARRWEELLQRGAAQLAELQTQAAGCKLRPGKGSRKKRTLPCEETVVAPSEPHDRADPRVQELKDRLEQELQQQGEEQYRSVLKRKEQHVTEQIAKMMELAREKQAAELKTFKETSETDTKEMKKKLEAKRLERIQAMTKVTTDKVAQERLKREINNSHIQEVVQAVKQMTETLERHQEKLEERQTACLEQIQAMEKQFQEKALAEYEAKMKGLEAEVKESVRAYFKDCFPTEAEDKPERSCEASEESCPQEPLVSKADTQESRL | 3.1.4.11 | COFACTOR: Name=Ca(2+); Xref=ChEBI:CHEBI:29108; Evidence={ECO:0000250}; Note=Binds 1 Ca(2+) ion per subunit. {ECO:0000250}; | detection of chemical stimulus involved in sensory perception of bitter taste [GO:0001580]; G protein-coupled receptor signaling pathway [GO:0007186]; lipid catabolic process [GO:0016042]; phosphatidylinositol metabolic process [GO:0046488]; phosphatidylinositol-mediated signaling [GO:0048015]; phospholipase C-activating G protein-coupled receptor signaling pathway [GO:0007200]; release of sequestered calcium ion into cytosol [GO:0051209]; sensory perception of bitter taste [GO:0050913] | cytoplasm [GO:0005737]; G-protein beta/gamma-subunit complex [GO:0031680]; neuronal dense core vesicle [GO:0098992] | calcium ion binding [GO:0005509]; G-protein beta/gamma-subunit complex binding [GO:0031683]; phosphatidylinositol phospholipase C activity [GO:0004435]; phospholipase C activity [GO:0004629]; phospholipid binding [GO:0005543] | PF00168;PF09279;PF17787;PF00388;PF00387;PF08703; | 2.30.29.240;2.60.40.150;1.10.238.10;3.20.20.190;1.20.1230.10; | null | null | null | CATALYTIC ACTIVITY: Reaction=a 1,2-diacyl-sn-glycero-3-phospho-(1D-myo-inositol-4,5-bisphosphate) + H2O = 1D-myo-inositol 1,4,5-trisphosphate + a 1,2-diacyl-sn-glycerol + H(+); Xref=Rhea:RHEA:33179, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:17815, ChEBI:CHEBI:58456, ChEBI:CHEBI:203600; EC=3.1.4.11; Evidence={ECO:0000250|UniProtKB:Q00722}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:33180; Evidence={ECO:0000250|UniProtKB:Q00722}; CATALYTIC ACTIVITY: Reaction=a 1,2-diacyl-sn-glycero-3-phospho-(1D-myo-inositol) + H2O = 1D-myo-inositol 1-phosphate + a 1,2-diacyl-sn-glycerol + H(+); Xref=Rhea:RHEA:43484, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:17815, ChEBI:CHEBI:57880, ChEBI:CHEBI:58433; Evidence={ECO:0000250|UniProtKB:Q00722}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:43485; Evidence={ECO:0000250|UniProtKB:Q00722}; | null | null | null | null | FUNCTION: The production of the second messenger molecules diacylglycerol (DAG) and inositol 1,4,5-trisphosphate (IP3) is mediated by activated phosphatidylinositol-specific phospholipase C enzymes. {ECO:0000250|UniProtKB:Q00722}. | Mus musculus (Mouse) |
A3KGS3 | RGPA2_MOUSE | MFSRRSHGDVKKSTQKVLDPKKDVLTRLKHLRALLDNVDASDLKQFFETNYSQIYFIFYENFITLENSLKLKGNNKSQREELDSILFLFEKILQFLPERIFFRWHYQSIGSTLKKLLHTGNSIKIRCEGIRLFLLWLQALQTNCAEEQVLIFACLVPGFPAVLSSRGPCTLETLINPSPSIVDAKIYPEEITPLLPAISGEKIAEDQTCFFLQILLKYMVIQAASLEWKNKENQDTGFKFLFTLFRKYYLPHLFPSFTKLTNIYKPVLEIPHLRPKPVYVTVTRDNETIYSTKIPYMAARVVFIKWIVTFFLEKKYLTATQNTKNGVDVLPKIIQTVGGGAIQEKVPELDGAGSTEQDKSHSNSSTLSDRRLSNSSLCSIEEEHRTVYEMVQRILLSTRGYVNFVNEVFRQAFLLPSCEISVTRKVVQVYRKWILQNKPVFMEEPDKKDVAQEDADKLGLSETDSKEASSESSGHKRSSSWGRTYSFTSAMSRGCVTEEDNTNVKAGAQAMLQVFLTNAANVFLLEPCAEVPMLLREQVDASKAVLIIFRRMIMELTMNQKTWEQMLQILLRITEAVMQKPKDKHVKDLFAQSLAGLLFRTLIVAWIRANLCVYISRELWDDFLRVLSSLTEWEELITEWSNIMDSLTAVLARTVYGVEMTNLPLDKLSEQKEKKQRGKGCILEPQKGTAVGRSFSLSWRSHPDVTEPMRFRSATTSGAPGVEKARNTVRQKATEVEEFQQAESTAAADCDYLVVGQQQVPRSSSTSDITERLYSDSSQGQKVEHSQNLSSSEPKSVQESKGHVTHEHEGITMLVRRSSSPAELELKDDLQQAHGRCRQRQTSESTGSDTVVGYSNEAELPVSPWQACEEDPDLSTPTDAVADSDARHWLQLSPTDASNLTDSRECLADDCSIIAGGNLTGWHPDSAAVLWRRVLGILGDVNNIQSPKIHAKVFGYLYELWYKLAKIRDNLAISLDNQSSPSPPLLIPPLRMFASWLFKATTLPNEYKEGKLQAYKLICAMMTRRQDVLPNSDFLVHFYLVMHLGLTSEDQDVLNTIIKNCSPRFFSLGLPGFSMLVGDFITAAARVLSTDMLAAPRSEALTLLGSLVCFPNTYQEIPLLQSVPEVSDVVTGAEDVKHYLINILLKNATEEPNECARCIAICSLGVWICEELAQSASHPQVKDAINVIGVTLKFPNKIVAQVACDVLQLLVSYWEKLQMFETALPRKMAEILVATIAFLLPSAEYSSVETDKKFIVSLLLCLLDWCMALPVSALLHPVSTAVLEELHPSRAPLLDYIYRVLHCCVCGSSTYTQQSHYTLTLADLSSTDYDPFLPLANVRNSEPIQYHSSADLGNLLTVEEEKKRRSVELIPLTARMVMAHLVNHLGHYPLSGGPAVLHSLVSENHDNAHVEGTELSSEVFRSPNLQLFVFNDSTLISYLQTPAEGPAGGTSGGSLSDVRVIVRDISGKYSWDGKVLYGPLEGRLAPNGRNPSFQISGWHHHTCGPQKDLFNGEEGDDVLDKLLENIGHTSPECLLPSQLNLNEPSPTPCAMNWDQEKAIMEVILRQSAQEDEYVQRCNSDSSVTVTSQGQPSPVEPRGPFYFCRLLLDDLGMNSWDRRKNFHLLKKNSKLLRELKNLDSRQCRETHKIAVFYIAEGQEDKCSILANERGSQAYEDFVAGLGWEVDLSTHCGFMGGLQRNGSTGQTAPYYATSTVEVIFHVSTRMPSDSDDSLTKKLRHLGNDEVHIVWSEHSRDYRRGIIPTAFGDVSIIIYPMKNHMFFITITKKPEVPFFGPLFDGAIVSGKLLPSLICATCINASRAVKCLIPLYQSFYEERALYLEAIIQNHREVMTFEDFAAQVFSPSPSYSVSGTD | null | null | activation of GTPase activity [GO:0090630]; Ral protein signal transduction [GO:0032484]; regulation of exocyst localization [GO:0060178]; regulation of protein localization [GO:0032880]; regulation of small GTPase mediated signal transduction [GO:0051056] | cytoplasm [GO:0005737]; cytosol [GO:0005829]; nucleus [GO:0005634] | GTPase activator activity [GO:0005096]; protein heterodimerization activity [GO:0046982] | PF20412;PF02145; | 3.40.50.11210; | null | null | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. | null | null | null | null | null | FUNCTION: Catalytic subunit of the heterodimeric RalGAP2 complex which acts as a GTPase activator for the Ras-like small GTPases RALA and RALB. {ECO:0000250}. | Mus musculus (Mouse) |
A3KGV1 | ODFP2_MOUSE | MSASSSGGSPRFPSCGKNGVTSLTQKKVLRTPCGAPSVTVTKSHKRGMKGDTVNVRRSVRVKTKVPWMPPGKSSARHVGCKWENPPHCLEITPPSSEKLVSVMRLSDLSTEDDDSGHCKMNRYDKKIDSLMNAVGCLKSEVKMQKGERQMAKRFLEERKEELEEVAHELAETEHENTVLRHNIERIKEEKDFTMLQKKHLQQEKECLMSKLVEAEMDGAAAAKQVMALKDTIGKLKTEKQMTCTDINTLTRQKELLLQKLSTFEETNRTLRDLLREQHCKEDSERLMEQQGTLLKRLAEADSEKARLLLLLQDKDKEVEELLQEIQCEKAQAKTASELSKSMESMRGHLQAQLRCKEAENSRLCMQIKNLERSGNQHKAEVEAIMEQLKELKQKGDRDKETLKKAIRAQKERAEKSEEYAEQLHVQLADKDLYVAEALSTLESWRSRYNQVVKDKGDLELEIIVLNDRVTDLVNQQQSLEEKMREDRDSLVERLHRQTAEYSAFKLENERLKASFAPMEDKLNQAHLEVQQLKASVKNYEGMIDNYKSQVMKTRLEADEVAAQLERCDKENKMLKDEMNKEIEAARRQFQSQLADLQQLPDILKITEAKLAECQDQLQGYERKNIDLTAIISDLRSRIEHQGDKLEMAREKHQASQKENKQLSQKVDELERKLEATSAQNVEFLQVIAKREEAIHQAQLRLEEKTRECGSLARQLESAIEDARRQVEQTKEQALSKERAAQSKILDLETQLSRTKTELGQLRRTRDDADRRYQSRLQDLKDRLEQSESTNRSMQNYVQFLKASYANVFGDAPYTSSYLTSSPIRSRSPPA | null | null | cell differentiation [GO:0030154]; regulation of cilium assembly [GO:1902017]; spermatogenesis [GO:0007283] | centriole [GO:0005814]; centrosome [GO:0005813]; ciliary transition fiber [GO:0097539]; cilium [GO:0005929]; cytoplasm [GO:0005737]; intracellular membrane-bounded organelle [GO:0043231]; microtubule [GO:0005874]; outer dense fiber [GO:0001520]; sperm flagellum [GO:0036126]; sperm midpiece [GO:0097225]; sperm principal piece [GO:0097228]; spindle pole [GO:0000922] | structural constituent of cytoskeleton [GO:0005200] | null | 1.20.5.340; | ODF2 family | PTM: Tyrosine phosphorylated (By similarity). Phosphorylated on Ser-95 by TSSK4 (PubMed:26961893). {ECO:0000250|UniProtKB:Q2MJU7, ECO:0000269|PubMed:26961893}. | SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, microtubule organizing center, centrosome {ECO:0000269|PubMed:15852003, ECO:0000269|PubMed:23386061, ECO:0000269|PubMed:31904090}. Cell projection, cilium {ECO:0000269|PubMed:15852003}. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome, centriole {ECO:0000269|PubMed:15852003}. Cytoplasm, cytoskeleton, spindle pole {ECO:0000269|PubMed:15852003}. Cell projection, cilium, flagellum {ECO:0000269|PubMed:27682589, ECO:0000269|PubMed:31904090, ECO:0000269|PubMed:35587122, ECO:0000269|PubMed:37198331, ECO:0000269|PubMed:38038747}. Note=Localized at the microtubule organizing centers in interphase and spindle poles in mitosis. Localized at the distal/subdistal appendages of mother centrioles. {ECO:0000269|PubMed:15852003}. | null | null | null | null | null | FUNCTION: Seems to be a major component of sperm tail outer dense fibers (ODF). ODFs are filamentous structures located on the outside of the axoneme in the midpiece and principal piece of the mammalian sperm tail and may help to maintain the passive elastic structures and elastic recoil of the sperm tail. May have a modulating influence on sperm motility. Functions as a general scaffold protein that is specifically localized at the distal/subdistal appendages of mother centrioles. Component of the centrosome matrix required for the localization of PLK1 and NIN to the centrosomes. Required for the formation and/or maintenance of normal CETN1 assembly (By similarity). {ECO:0000250|UniProtKB:Q5BJF6, ECO:0000269|PubMed:15852003}. | Mus musculus (Mouse) |
A3KMH1 | VWA8_HUMAN | MQSRLLLLGAPGGHGGPASRRMRLLLRQVVQRRPGGDRQRPEVRLLHAGSGADTGDTVNIGDVSYKLKIPKNPELVPQNYISDSLAQSVVQHLRWIMQKDLLGQDVFLIGPPGPLRRSIAMQYLELTKREVEYIALSRDTTETDLKQRREIRAGTAFYIDQCAVRAATEGRTLILEGLEKAERNVLPVLNNLLENREMQLEDGRFLMSAERYDKLLRDHTKKELDSWKIVRVSENFRVIALGLPVPRYSGNPLDPPLRSRFQARDIYYLPFKDQLKLLYSIGANVSAEKVSQLLSFATTLCSQESSTLGLPDFPLDSLAAAVQILDSFPMMPIKHAIQWLYPYSILLGHEGKMAVEGVLKRFELQDSGSSLLPKEIVKVEKMMENHVSQASVTIRIADKEVTIKVPAGTRLLSQPCASDRFIQTLSHKQLQAEMMQSHMVKDICLIGGKGCGKTVIAKNFADTLGYNIEPIMLYQDMTARDLLQQRYTLPNGDTAWRSSPLVNAALEGKLVLLDGIHRVNAGTLAVLQRLIHDRELSLYDGSRLLREDRYMRLKEELQLSDEQLQKRSIFPIHPSFRIIALAEPPVIGSTAHQWLGPEFLTMFFFHYMKPLVKSEEIQVIKEKVPNVPQEALDKLLSFTHKLRETQDPTAQSLAASLSTRQLLRISRRLSQYPNENLHSAVTKACLSRFLPSLARSALEKNLADATIEINTDDNLEPELKDYKCEVTSGTLRIGAVSAPIYNAHEKMKVPDVLFYDNIQHVIVMEDMLKDFLLGEHLLLVGNQGVGKNKIVDRFLHLLNRPREYIQLHRDTTVQTLTLQPSVKDGLIVYEDSPLVKAVKLGHILVVDEADKAPTNVTCILKTLVENGEMILADGRRIVANSANVNGRENVVVIHPDFRMIVLANRPGFPFLGNDFFGTLGDIFSCHAVDNPKPHSELEMLRQYGPNVPEPILQKLVAAFGELRSLADQGIINYPYSTREVVNIVKHLQKFPTEGLSSVVRNVFDFDSYNNDMREILINTLHKYGIPIGAKPTSVQLAKELTLPEQTFMGYWTIGQARSGMQKLLCPVETHHIDIKGPALINIQEYPIERHEERSLNFTEECASWRIPLDEINIICDIATSHENEQNTLYVVTCNPASLYFMNMTGKSGFFVDFFDIFPRTANGVWHPFVTVAPLGSPLKGQVVLHEQQSNVILLLDTTGRALHRLILPSEKFTSKKPFWWNKEEAETYKMCKEFSHKNWLVFYKEKGNSLTVLDVLEGRTHTISLPINLKTVFLVAEDKWLLVESKTNQKYLLTKPAHIESEGSGVCQLYVLKEEPPSTGFGVTQETEFSIPHKISSDQLSSEHLSSAVEQKIASPNRILSDEKNYATIVVGFPDLMSPSEVYSWKRPSSLHKRSGTDTSFYRGKKKRGTPKQSNCVTLLDTNQVVRILPPGEVPLKDIYPKDVTPPQTSGYIEVTDLQSKKLRYIPIPRSESLSPYTTWLSTISDTDALLAEWDKSGVVTVDMGGHIRLWETGLERLQRSLMEWRNMIGQDDRNMQITINRDSGEDVSSPKHGKEDPDNMPHVGGNTWAGGTGGRDTAGLGGKGGPYRLDAGHTVYQVSQAEKDAVPEEVKRAAREMGQRAFQQRLKEIQMSEYDAATYERFSGAVRRQVHSLRIILDNLQAKGKERQWLRHQATGELDDAKIIDGLTGEKAIYKRRGELEPQLGSPQQKPKRLRLVVDVSGSMYRFNRMDGRLERTMEAVCMVMEAFENYEEKFQYDIVGHSGDGYNIGLVPMNKIPKDNKQRLEILKTMHAHSQFCMSGDHTLEGTEHAIKEIVKEEADEYFVIVLSDANLSRYGIHPAKFAQILTRDPQVNAFAIFIGSLGDQATRLQRTLPAGRSFVAMDTKDIPQILQQIFTSTMLSSV | null | null | null | cytoplasm [GO:0005737]; mitochondrion [GO:0005739]; peroxisome [GO:0005777] | ATP binding [GO:0005524]; ATP hydrolysis activity [GO:0016887] | PF07728; | 3.40.50.300;3.40.50.410; | null | null | SUBCELLULAR LOCATION: [Isoform 1]: Mitochondrion {ECO:0000269|PubMed:30204880}.; SUBCELLULAR LOCATION: [Isoform 2]: Mitochondrion {ECO:0000269|PubMed:30204880}. Peroxisome {ECO:0000269|PubMed:30204880}. Note=Localizes to peroxisomes in a PEX7-dependent manner. {ECO:0000269|PubMed:30204880}. | null | null | null | null | null | FUNCTION: Exhibits ATPase activity in vitro. {ECO:0000250|UniProtKB:Q8CC88}. | Homo sapiens (Human) |
A3KNA7 | SRBP2_DANRE | MDASEFMDTMDPSLSELGDEFTLGDIDEMLQFVSNQVDFPDIFEDQMGGGATARTLPQAVPSAILTPPHTPVQTSSQTHTQTLTQAHTQTHTQTHTQTRTPPVLQPRPQPITQVQTQTFPMQTLAVQTQAQPQTVMITPTATPSRFIQNQVICQQNNATSFQVLQPQMQSIMTSPQVQPMTIQHQRVLTPAGQTIQTLSTAPTTVHTMSQQVPVLVHQPQILKTDSLLLTTKPDGTQVLSTVQSPTGITTLTTPIQTTALQMPTLMSSNILTTVPVVMGGGDKLPIKQLSSGPAHNIGGARVGVEQSPVVGPGGVVKEGERRTTHNIIEKRYRSSINDKILELRDLVLGNDAKMHKSGVLRKAIDYIKYLQQVNHKLRQENLTLKMANQKNKSACVSDVDLELKAEVSLISPPPSDSGSSSPAQLSPYCIDSEPGSPLLEHEQLKSEPDSPSCVGVMDRSRLLLCALSFLCLSLNPLPSLLGAEAPAGSPEVAGHGPTRTLFSLPAQTQSFGAWLWCVLPFLLVWVVSGVGVVWGCVRVLYLWEPVTPLHSPTSVRFWRHRKQADLQLYRGDYAGAVLSLQTCLSVLSRVLPVTTLDIMCSLSWNLIRYCLRRPAPLGWLVRLVGGRHEGEESQTSSRDAALVYHKLSQLQLTGQMERRPLWGVCVSLSAVNLCESAEGKLTATQQVQVYVTAAISVRAALGKHLTCLPAYLLSCAEALTCQSDSKPLPDCLRWIFTPLGRQFFLSCDWSVRSESDGQIFTSARDKADPIAQLHRCFCQKLLERATHTLIEPQSREDAGEFTGVLEFLQLLNSCTEDSAPSTAPFPALANQSSTSVRDPVCRWWASVLTAAVHWLQGDDASVRSLLAEAERMPRALHTLDHPLPKAVLALCKAVQMSVCPQKGEGVVSCLSHCQRASAQLHISVCQSHNNTWLHKGVELLVCDLLLTLRTSLWQRGGGSNGEPGPAPGSQLSGFQRDLSSLRRLGQAHRQAQHKLFLHETTVRLMAGASPTRTHQLLRHRTHNYTTTDGECVLGERERAHAILLACRHLPLPLLTPPGHRARLLAEAKRTLERVGDRRSLQDCQHILLRLSGGTTIAAS | null | null | cholesterol metabolic process [GO:0008203]; liver development [GO:0001889]; positive regulation of cholesterol storage [GO:0010886]; positive regulation of transcription by RNA polymerase II [GO:0045944]; regulation of Notch signaling pathway [GO:0008593] | endoplasmic reticulum membrane [GO:0005789]; ER to Golgi transport vesicle membrane [GO:0012507]; Golgi membrane [GO:0000139]; nucleus [GO:0005634] | 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] | PF00010; | 4.10.280.10; | SREBP family | PTM: [Sterol regulatory element-binding protein 2]: Processed in the Golgi apparatus, releasing the protein from the membrane (PubMed:30705153). At low cholesterol the SCAP-SREBP complex is recruited into COPII vesicles for export from the endoplasmic reticulum (By similarity). In the Golgi, complex SREBPs are cleaved sequentially by site-1 (mbtps1, S1P) and site-2 (mbtps2, S2P) protease. The first cleavage by site-1 protease occurs within the luminal loop, the second cleavage by site-2 protease occurs within the first transmembrane domain, releasing the transcription factor from the Golgi membrane (By similarity). {ECO:0000250|UniProtKB:Q12772, ECO:0000269|PubMed:30705153}. | SUBCELLULAR LOCATION: [Sterol regulatory element-binding protein 2]: Endoplasmic reticulum membrane {ECO:0000250|UniProtKB:Q12772}; Multi-pass membrane protein {ECO:0000255}. Golgi apparatus membrane {ECO:0000250|UniProtKB:Q12772}; Multi-pass membrane protein {ECO:0000255}. Cytoplasmic vesicle, COPII-coated vesicle membrane {ECO:0000250|UniProtKB:Q12772}; Multi-pass membrane protein {ECO:0000255}. Note=At high sterol concentrations, the SCAP-SREBP is retained in the endoplasmic reticulum. Low sterol concentrations promote recruitment into COPII-coated vesicles and transport of the SCAP-SREBP to the Golgi, where it is processed. {ECO:0000250|UniProtKB:Q12772}.; SUBCELLULAR LOCATION: [Processed sterol regulatory element-binding protein 2]: Nucleus {ECO:0000250|UniProtKB:Q12772}. | null | null | null | null | null | FUNCTION: [Sterol regulatory element-binding protein 2]: Precursor of the transcription factor form (Processed sterol regulatory element-binding protein 2), which is embedded in the endoplasmic reticulum membrane. Low sterol concentrations promote processing of this form, releasing the transcription factor form that translocates into the nucleus and activates transcription of genes involved in cholesterol biosynthesis. {ECO:0000250|UniProtKB:Q12772}.; FUNCTION: [Processed sterol regulatory element-binding protein 2]: Key transcription factor that regulates expression of genes involved in cholesterol biosynthesis. Binds to the sterol regulatory element 1 (SRE-1) (5'-ATCACCCCAC-3'). Has dual sequence specificity binding to both an E-box motif (5'-ATCACGTGA-3') and to SRE-1 (5'-ATCACCCCAC-3'). Regulates transcription of genes related to cholesterol synthesis pathway (By similarity). Activated by mediated cholesterol efflux, transactivates NOTCH and promotes hematopoietic stem and progenitor cell emergence (PubMed:30705153). {ECO:0000250|UniProtKB:Q12772, ECO:0000269|PubMed:30705153}. | Danio rerio (Zebrafish) (Brachydanio rerio) |
A3KNL5 | ATF1A_DANRE | MARLLLRRGFFSSHIRMSSDQLGELGTGAGKGGGGGGSVRAAGGSFGRREAAEEERYFRQKEREQLAALKNHHEEEIDHHKKEIERLQREIDRHKGKIRKLKHDD | null | null | erythrocyte differentiation [GO:0030218]; heme biosynthetic process [GO:0006783]; negative regulation of hydrolase activity [GO:0051346]; optokinetic behavior [GO:0007634]; protein homotetramerization [GO:0051289]; regulation of neuroinflammatory response [GO:0150077]; visual perception [GO:0007601] | mitochondrion [GO:0005739] | ATPase binding [GO:0051117]; ATPase inhibitor activity [GO:0042030]; protein homodimerization activity [GO:0042803] | PF04568; | 1.20.5.500; | ATPase inhibitor family | null | SUBCELLULAR LOCATION: Mitochondrion {ECO:0000250}. | null | null | null | null | null | FUNCTION: Endogenous F(1)F(o)-ATPase inhibitor limiting ATP depletion when the mitochondrial membrane potential falls below a threshold and the F(1)F(o)-ATP synthase starts hydrolyzing ATP to pump protons out of the mitochondrial matrix. Required to avoid the consumption of cellular ATP when the F(1)F(o)-ATP synthase enzyme acts as an ATP hydrolase (By similarity). Indirectly acts as a regulator of heme synthesis in erythroid tissues: regulates heme synthesis by modulating the mitochondrial pH and redox potential, allowing fech to efficiently catalyze the incorporation of iron into protoporphyrin IX to produce heme (PubMed:23135403). {ECO:0000250|UniProtKB:P01096, ECO:0000269|PubMed:23135403}. | Danio rerio (Zebrafish) (Brachydanio rerio) |
A3KPA0 | JAM3B_DANRE | MALTPLACVLLLLSMQCYISTLAVLLKSTNSKPWVNEFESIELSCMIESITTTKPRIEWKKIKNGDPSYVYFDNQISGDLERRAKIREPATLVILNATRSDSADYRCEVTAPNDQKSFDEILISLTVRVKPVVPRCSVPKSIPVGKPAELHCLEDEGYPKSQYQWFRNKEEIPLDPKSSPKFFNSTYTLDGEMGTLKFSAVRKEDAGEYYCRAKNEAGISECGPQMMEVYDINIAGIILGVVVVVMVLLCITVGIFCAYKRGYFTSQKQTGNNYKPPAKGDGVDYVRTEDEGDFRHKSSFVI | null | null | cell migration [GO:0016477]; cell-cell adhesion [GO:0098609]; myoblast fusion [GO:0007520] | bicellular tight junction [GO:0005923]; cell-cell contact zone [GO:0044291]; desmosome [GO:0030057]; plasma membrane [GO:0005886]; protein complex involved in cell adhesion [GO:0098636] | cell-cell adhesion mediator activity [GO:0098632]; integrin binding [GO:0005178]; protein heterodimerization activity [GO:0046982]; protein homodimerization activity [GO:0042803] | PF13927;PF07686; | 2.60.40.10; | Immunoglobulin superfamily | null | SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:Q9BX67}; Single-pass type I membrane protein {ECO:0000250|UniProtKB:Q9BX67}. Cell junction {ECO:0000250|UniProtKB:Q9BX67}. Cell junction, desmosome {ECO:0000250|UniProtKB:Q9BX67}. Cell junction, tight junction {ECO:0000250|UniProtKB:Q9BX67}. | null | null | null | null | null | FUNCTION: Junctional adhesion protein that mediates heterotypic cell-cell interactions to regulate different cellular processes (By similarity). During myogenesis, it is involved in myocyte fusion through the binding of jam2a on neighboring myocytes (PubMed:22180726). {ECO:0000250|UniProtKB:P57087, ECO:0000269|PubMed:22180726}. | Danio rerio (Zebrafish) (Brachydanio rerio) |
A3KPF2 | ANM14_ARATH | MEIPSLNKQQEFTLASVTDLTSPSSSLSSSPVVATFSCVNEVKELRFQESKSSDGFSFDLSSTQLFKLGPLQFTCVSDGSISSAKEKSSFSRGVVIKFRDEKDSKEFCDSFEECKKDDAVKQGSALPNGTVVSANKSKFDDKIEAASAKMYFHYYGQLLHQQNMLQDYVRTGTYHAAVMENRSDFSGRVVVDVGAGSGILSMFAALAGAKHVYAVEASEMAEYARKLIAGNPLLAERITVIKGKIEDIELPEKADVLISEPMGTLLVNERMLETYVIARDRFLSPNGKMFPTVGRIHMAPFADEFLFVEMANKALFWQQQNYYGVDLTPLYVSAHQGYFSQPVVDAFDPRLLVAPSMFHVIDFTMMTEEQFYEIDIPLKFTASVCTRIHGLACWFDVLFDGSTVQRWFTTAPGAPTTHWYQIRCVLSQPIHVMAGQEITGRLHLIAHSAQSYTINLTLSAKMWGPGANQGGILQTSSCKLDLKEPYYRMSQPQVYPTQEPPAQSQDIHIHSDDLEELELLQQNANAQL | 2.1.1.319 | null | peptidyl-arginine methylation, to asymmetrical-dimethyl arginine [GO:0019919]; regulation of flower development [GO:0009909]; vegetative to reproductive phase transition of meristem [GO:0010228] | chloroplast [GO:0009507]; cytoplasm [GO:0005737]; nucleus [GO:0005634] | histone arginine N-methyltransferase activity [GO:0008469]; protein heterodimerization activity [GO:0046982]; protein homodimerization activity [GO:0042803]; protein-arginine omega-N asymmetric methyltransferase activity [GO:0035242]; protein-arginine omega-N monomethyltransferase activity [GO:0035241] | PF06325; | 2.70.160.11;3.40.50.150; | Class I-like SAM-binding methyltransferase superfamily, Protein arginine N-methyltransferase family | null | SUBCELLULAR LOCATION: Nucleus {ECO:0000250}. Cytoplasm {ECO:0000250}. | CATALYTIC ACTIVITY: Reaction=L-arginyl-[protein] + 2 S-adenosyl-L-methionine = 2 H(+) + N(omega),N(omega)-dimethyl-L-arginyl-[protein] + 2 S-adenosyl-L-homocysteine; Xref=Rhea:RHEA:48096, Rhea:RHEA-COMP:10532, Rhea:RHEA-COMP:11991, ChEBI:CHEBI:15378, ChEBI:CHEBI:29965, ChEBI:CHEBI:57856, ChEBI:CHEBI:59789, ChEBI:CHEBI:61897; EC=2.1.1.319; | null | null | null | null | FUNCTION: Methylates (mono- and asymmetric dimethylation) the guanidino nitrogens of arginyl residues in several proteins involved in DNA packaging, transcription regulation, and mRNA stability. Recruited to promoters upon gene activation, methylates histone H3 and activates transcription via chromatin remodeling. {ECO:0000250}. | Arabidopsis thaliana (Mouse-ear cress) |
A3KPP3 | MOG1_DANRE | MSRPLFGGALSAVFPSSVMDISELRQIPDNQEVFAHSQTDQSIIIELLEYQSQVQDADAARYHFEDVAGSNKAIENGTWEVRVVEQVPQSEISMQECSSAWLLSGAQLVSKFNEEAKNTVNVHQCLFRLPQFTTDILMTFNDPVFINPLSSSAAGNMEAIPWTLQDFQGVLQSLRLLDSGVFG | null | null | atrioventricular canal morphogenesis [GO:1905222]; heart contraction [GO:0060047]; heart looping [GO:0001947]; protein import into nucleus [GO:0006606]; regulation of heart looping [GO:1901207]; regulation of heart morphogenesis [GO:2000826]; regulation of membrane depolarization [GO:0003254] | nucleus [GO:0005634]; perinuclear region of cytoplasm [GO:0048471]; plasma membrane [GO:0005886] | guanyl-nucleotide exchange factor activity [GO:0005085]; small GTPase binding [GO:0031267]; sodium channel regulator activity [GO:0017080]; transmembrane transporter binding [GO:0044325] | PF04603; | 3.40.1000.10; | MOG1 family | null | SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q9HD47}. Cytoplasm, perinuclear region {ECO:0000250|UniProtKB:Q9HD47}. Cytoplasm {ECO:0000250|UniProtKB:Q9HD47}. Cell membrane {ECO:0000250|UniProtKB:Q9HD47}; Peripheral membrane protein {ECO:0000250|UniProtKB:Q9HD47}; Cytoplasmic side {ECO:0000250|UniProtKB:Q9HD47}. Note=May shuttle between the nucleus and cytoplasm. {ECO:0000250|UniProtKB:Q9HD47}. | null | null | null | null | null | FUNCTION: May regulate the intracellular trafficking of RAN. Promotes guanine nucleotide release from RAN and inhibits binding of new GTP. Plays a role in the regulation of the levels of GTP-bound RAN in the nucleus (By similarity). Required for normal expression of the ion channel hcn4 and for normal expression of the cardiac transcription factors nkx2.5, gata4 and hand2 during embryonic development. Required for normal embryonic heart development and normal heart rate (PubMed:26903377). {ECO:0000250|UniProtKB:Q9HD47, ECO:0000269|PubMed:26903377}. | Danio rerio (Zebrafish) (Brachydanio rerio) |
A3KPQ7 | CEIP2_DANRE | MQVNDGPSSHPIFVAPVNGNAQRSSGYVPGRIVPVRSPPPAKAPPPPPLKPPVPPPARPSVFNLSEDGNRREQAQNQQRKNTYICVGIFFGIFLLILILVLSLTSKDVLDENCPHQNPALRSWKPGHDLKKVVVIHSGEHYRLDSSATLYSITIQAGGSVVFADDKKGSKNITLRTRHILIEDGGALHIGAPKCRYRSLATITLVGRSDETAVTEVPGMGRKFLGVNSGGTLELHGSERMSWTFLTRTVPASGLATGDHAFQKNFSRGINLRVVDQDTAEVLVNERFDTHESQDDSKRLGELLKALPAGRIVALATGDSAVKNLVFETKQTIHDLLGSNYISDLKYRDAWALVSVIGGGNGSCTEDVREHENHDTGGKALARQDFFTVDGVGFTVTAYSEWSNGYPTTGFQVDAVDKVVLNLQDDVSSWNPGDRIVVASTDYSMYQAEEFTLLPCPNCNRKQVQIQGKPQFSHVGEILDGVDMRAEVALLSRNILIHGEMENSCYGGNWCQYFSYDTFGGHIKILGNFTSVHLSHIELKHMGQQREKGRYPLNFHRCGDVDQSGGYSNPAYVDSLSIHHSFSRCVTVHATNGLLVKDTVGYDTLGHCFFLKDGIEQRNIFFHNLGLLTRPGTILPTDRNDSMCTEITDRVYKGYIPIPANECKAVSSFWIAHPNNHLISNSAAGSQDAGIWYVFHNSSTGDSHGMISETKAELTPLGTFFNNRVHSNFKAGLFIDRKVKSTNATAADPREYLCLDNSARFRPHESSDPSRPRVAAIIDTLISFKNNDLGAWIRGGDIIIRNSGDGSYPKDEGSSQEVSQSLFIGESRNRGTNGGQNKYWGIGGVDGKMRTLPRNKTFPIRGFQINDGPVRIFDSTFRAFSPTADRFTMAVGFSLKNIWQLTPRNNLSALAFHPSVTLRAFFGRPGDWFEQNDLDGDKNSIFHDLDGSISGYADTYVARADNFLIRHPQCVDMPQWNGVVCSGKYSQVYIQTQAASNLSLSISRDEYPDKPMVLRGIRTKTSPSQQYQPVLMMGKSYTMHWNGPAPRETVLSLINFDQDDWALLGLCYPNETVFQITSDIYNKQNNGFEGIEDYGPVTSIADLEKRQQERKYFFDKSAGLLWLYARARHRRDGNSYCSSAGCERVKIIATIRANQKTETCNCTANAYPKYSKPASNIVPMPKPNTEPCGACGASQFAFSSDPWNSYLQTQIKSLSVKEEQDNDTQAYITVNAQRFDLSQSGFLLVTVDACSGKVTKNSMFSSLDTKMEQFFKTGIMKRSIVLLATRGQPASFAGVAQYLESLGSAKTPDLQNKVAIAFFGFLGQGGPSPQPWSTLLTCQGAKILGLQERFIPLSLEEYSCPPKKDSPTRMDLELLKKIS | 3.2.1.35 | COFACTOR: Name=Ca(2+); Xref=ChEBI:CHEBI:29108; Evidence={ECO:0000250|UniProtKB:Q9UHN6}; | angiogenesis [GO:0001525]; atrioventricular valve formation [GO:0003190]; cardiac muscle tissue morphogenesis [GO:0055008]; cell migration involved in heart formation [GO:0060974]; cell migration to the midline involved in heart development [GO:0003318]; embryonic heart tube morphogenesis [GO:0003143]; endocardial cushion development [GO:0003197]; heart looping [GO:0001947]; hyaluronan catabolic process [GO:0030214]; muscle attachment [GO:0016203]; muscle tissue morphogenesis [GO:0060415]; positive regulation of extracellular matrix assembly [GO:1901203]; positive regulation of vascular endothelial growth factor signaling pathway [GO:1900748]; regulation of sprouting angiogenesis [GO:1903670]; regulation of Wnt signaling pathway [GO:0030111] | plasma membrane [GO:0005886] | calcium ion binding [GO:0005509]; carbohydrate binding [GO:0030246]; hyalurononglucosaminidase activity [GO:0004415] | PF10162;PF15711; | null | CEMIP family | null | SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:28118600}; Single-pass type II membrane protein {ECO:0000269|PubMed:28118600}. | CATALYTIC ACTIVITY: Reaction=Random hydrolysis of (1->4)-linkages between N-acetyl-beta-D-glucosamine and D-glucuronate residues in hyaluronate.; EC=3.2.1.35; Evidence={ECO:0000305|PubMed:28118600}; | null | null | null | null | FUNCTION: Cell surface hyaluronidase that mediates the initial cleavage of extracellular high-molecular-weight hyaluronan into intermediate-size hyaluronan (PubMed:28118600). Acts as a regulator of angiogenesis in embryos by mediating degradation of extracellular hyaluronan, thereby promoting VEGF signaling (PubMed:28118600). Acts as a regulator of heart development during myocardial and endocardial morphogenesis: involved in the looping stage of heart morphogenesis (PubMed:21896629). Stimulates migration of endocardial cells and increases both myocardial and endocardial fusion (PubMed:21896630). Involved in the restriction of endocardial cushions (ECs) formation to the atrioventricular canal (AVC) (PubMed:21896630). Also required for muscle fiber attachment (PubMed:27471259). Is very specific to hyaluronan; not able to cleave chondroitin sulfate or dermatan sulfate (By similarity). {ECO:0000250|UniProtKB:Q9UHN6, ECO:0000269|PubMed:21896629, ECO:0000269|PubMed:21896630, ECO:0000269|PubMed:27471259, ECO:0000269|PubMed:28118600}. | Danio rerio (Zebrafish) (Brachydanio rerio) |
A3KPW9 | BAG6_DANRE | MEESGVIEVTVKTLDSQSRTFTVRGEWTVKQFKEHIAASVEISVDKQRLIYQGKVLQDERTLTEYNVDGKVIHLVERPPPQSSQPGGGGGGVSGSSGAADGGSSSSQSSAYTTSHDRNANNYVMLGTFNLPVNIMDPQQIQMSVQQMLAGVGEMGRNVRVSTSTGSSGSVDVHINVDQSVQSEPRMRLHLAENLLRETQALIHRLEGQSSEPSQQETPPPQPSSSSFSAHPMDSSPPPPSVSSSASQTEGETQSGPNHPSPLELVEVLSEVRRVEERLRPFMERTHSILGAATSADYNNNTQEREEDQRTLNLIGESLHLLGNTLVALSDLRCNLSAQPPRHLHVVRPMSHYTSPVMMQSGLPHIPIPMNLGSTVTMTSNSRQTSDGQPQPPHSSNQSDQQGQAPPTPANESNQQTGHGQGTPRVIRITHQTMEPVVMMQMNLDGTTVPLHVPGLPPEFMQAIMHQISQQAVTMATAASAGHQGQQQGTAGAGAQNGESPVPPPPQARVVITRPTLSPRVPQPMGTRGTTINLRAAVPPPSGQQTNQMVSGLVGQLLLPLHTGDQTSTTSSSHSFSFSTSSSTSSSSSFSSASPPLSSANTSGQTSTHTTSTASVGQAQESGPGDNLAQLLGSLLGGAAGAGGGVSGATPSITVTVPGVPAFIQGLSEFIQSGQPVFPSPNQQPPPSQATPPSAPSGPAPTTAPSGGAETLSPELFTGIVQGVLSTMMGSLGAGQGNTESIAQFIQRLSQTSNLFTPGAGDAVGFFGDLLSLVCQSFSMVDMVLLLHGNPQPLSRIQPQLTAFFTEHYLQGREPTDANIASASEDLINELEEYIAESFSTVTVREGVDIIQTNMSFLRQQFTRMATHILRCTDNTFGQRLLYLCTQGLFECLALNLYCLRGEQRALTTVINHRIRRMSAEVNPSLVNWLTSMMSMRLHVILEHNPVTEDQIQHYVIYTQSESARRTEAGSQSSQQSQNMNVEEGLSPAPATTAEEALRSTGDTDGDEAPGRPSAEETRGAVAMATTEREESTGEAEPWAATVPPEWVPIIRRDMLTQRKMKAQPPLSDAYMHGMPAKRRKTAQGEGPHLSLTEAVSRAARTAGVRPVTAPDSLQGELETPELQEAYAQQVKSDIKKRLSDDPDYNHQRFPNTHRVFSEDA | null | null | brain development [GO:0007420]; chromatin organization [GO:0006325]; endoplasmic reticulum stress-induced pre-emptive quality control [GO:0061857]; ERAD pathway [GO:0036503]; internal peptidyl-lysine acetylation [GO:0018393]; intrinsic apoptotic signaling pathway in response to DNA damage by p53 class mediator [GO:0042771]; intrinsic apoptotic signaling pathway in response to endoplasmic reticulum stress [GO:0070059]; kidney development [GO:0001822]; lung development [GO:0030324]; negative regulation of proteasomal ubiquitin-dependent protein catabolic process [GO:0032435]; negative regulation of proteolysis [GO:0045861]; proteasomal protein catabolic process [GO:0010498]; protein stabilization [GO:0050821]; regulation of apoptotic process [GO:0042981]; regulation of embryonic development [GO:0045995]; spermatogenesis [GO:0007283]; synaptonemal complex assembly [GO:0007130]; tail-anchored membrane protein insertion into ER membrane [GO:0071816]; ubiquitin-dependent protein catabolic process [GO:0006511] | BAT3 complex [GO:0071818]; cytosol [GO:0005829]; extracellular region [GO:0005576]; nucleus [GO:0005634] | misfolded protein binding [GO:0051787]; polyubiquitin modification-dependent protein binding [GO:0031593]; proteasome binding [GO:0070628]; ribosome binding [GO:0043022] | PF12057;PF20960;PF00240; | null | null | null | SUBCELLULAR LOCATION: Cytoplasm, cytosol {ECO:0000250|UniProtKB:P46379}. Nucleus {ECO:0000250|UniProtKB:P46379}. Secreted, extracellular exosome {ECO:0000250|UniProtKB:P46379}. | null | null | null | null | null | FUNCTION: ATP-independent molecular chaperone preventing the aggregation of misfolded and hydrophobic patches-containing proteins. Functions as part of a cytosolic protein quality control complex, the bag6/bat3 complex, which maintains these client proteins in a soluble state and participates in their proper delivery to the endoplasmic reticulum or alternatively can promote their sorting to the proteasome where they undergo degradation. The bag6/bat3 complex is involved in the post-translational delivery of tail-anchored/type II transmembrane proteins to the endoplasmic reticulum membrane. Similarly, the bag6/bat3 complex also functions as a sorting platform for proteins of the secretory pathway that are mislocalized to the cytosol either delivering them to the proteasome for degradation or to the endoplasmic reticulum. The bag6/bat3 complex also plays a role in the endoplasmic reticulum-associated degradation (ERAD), a quality control mechanism that eliminates unwanted proteins of the endoplasmic reticulum through their retrotranslocation to the cytosol and their targeting to the proteasome. It maintains these retrotranslocated proteins in an unfolded yet soluble state condition in the cytosol to ensure their proper delivery to the proteasome. Also required for selective ubiquitin-mediated degradation of defective nascent chain polypeptides by the proteasome. Also involved in endoplasmic reticulum stress-induced pre-emptive quality control, a mechanism that selectively attenuates the translocation of newly synthesized proteins into the endoplasmic reticulum and reroutes them to the cytosol for proteasomal degradation. May ensure the proper degradation of these proteins and thereby protects the endoplasmic reticulum from protein overload upon stress. By stabilizing a large spectrum of proteins, may indirectly affect different biological processes including apoptosis. By controlling the steady-state expression of the IGF1R receptor, indirectly regulates the insulin-like growth factor receptor signaling pathway. {ECO:0000250|UniProtKB:P46379}.; FUNCTION: When nuclear, may also act as a component of some chromatin regulator complex. {ECO:0000250|UniProtKB:P46379}. | Danio rerio (Zebrafish) (Brachydanio rerio) |
A3KQH2 | DRC9_DANRE | MTSVEELRACALLQDCADQLSVLGNIIRPGAETQQRTELHLKTAQLMAGSSLSNFSGELKSQKHFKIQQTLLASDNLAKVQKDRQFVSDVINALLEELQKKNNFQSLFSAVAEERKKKAELLDIINREEEGRRQIKKLQKQLLDIRKEKTEECERLEEEVAILKDQVQDMRVRTNQQGKFVKSCAEQLVYQESKHNSYKENELEDEVKMLQEKIEEEKNVHFETEAFLKQQHANLKQKLQYWIHRYEKDMEEKEQEITALQNKRNSSQTRIQDLSKKCKDMENVVIEDRIEKEHLRAQMEKEQREKNAATKIQAWWRGTLVRKGPRSKKADKSKKKDGKKGKKKRK | null | null | cilium organization [GO:0044782]; definitive hemopoiesis [GO:0060216]; sperm axoneme assembly [GO:0007288] | cytoplasm [GO:0005737]; cytoskeleton [GO:0005856]; motile cilium [GO:0031514]; sperm flagellum [GO:0036126] | calmodulin binding [GO:0005516] | PF00612; | 1.20.5.190; | DRC9 family | null | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q80W32}. Cell projection, cilium, flagellum {ECO:0000250|UniProtKB:Q80W32}. Cell projection, cilium {ECO:0000250|UniProtKB:Q80W32}. Cytoplasm, cytoskeleton {ECO:0000250|UniProtKB:Q80W32}. Cytoplasm, cytoskeleton, flagellum axoneme {ECO:0000250|UniProtKB:A8HQ54}. | null | null | null | null | null | FUNCTION: Component of the nexin-dynein regulatory complex (N-DRC), a key regulator of ciliary/flagellar motility which maintains the alignment and integrity of the distal axoneme and regulates microtubule sliding in motile axonemes (By similarity). Binds calmodulin when cellular Ca(2+) levels are low and thereby contributes to the regulation of calcium and calmodulin-dependent protein kinase IV (camk4) activity; contributes to the regulation of camk4 signaling cascades. Plays a role in the regulation of definitive hematopoiesis via its effects on camk4 (PubMed:24787902). {ECO:0000250|UniProtKB:A8HQ54, ECO:0000269|PubMed:24787902}. | Danio rerio (Zebrafish) (Brachydanio rerio) |
A3LSZ2 | ARO1_PICST | MTSVEKVSILGAETIHVGYGIQDHIVQEVISHLASSTYVIVTDTNMARTTPFTKLRNKFESKLKELRPESRLLFYSVSPGENNKNRETKAAVEDFLLQQGCTRDTVILAVGGGVIGDMIGFVAATFMRGVRVVQVPTSLLAMVDSSVGGKTAIDTPLGKNFVGAFHQPEYVFADVSFLETLPTRQFINGMAEVVKTAAIWNEEEFTRLEKFSKKFLAVVSAKTPDLISIKEELVKTVLESIRVKAFVVSSDEKETGLRNLLNFGHTIGHAIEAVLTPQALHGECVSIGMIKEAELARYLGVLSPVAVARLSKCLVAYGLPVSIDEKDFLKKVGNKRHNVEIDILLKKMAIDKKNDGSKIRCVILEAIGKCYQLKAHQVSKQDLSFVLTDEVLVHPFDDKLIPKTNVVIPPGSKSISNRALVLAALGTGTVRIKNLLHSDDTKHMLEAVASLKGASISTEDNGETIVVTGNGGKLVSCDEQLYLGNAGTASRFLTSVAPLVGINPQSGEHVVLTGNARMQERPIGPLVDALRANGSEIDYLNKEGSLPLKVKAGKGLNGGRIELAATISSQYVSSILMCAPYANEPVTLSLVGGKPISQLYINMTIAMMKTFGIVVTKSETEEHTYHIPRGSYVNPKEYVIESDASSATYPLAFAALTGTSCTIPNIGSSSLQGDARFAVDVLRPMGCEVVQTATSTTVTGPSVGNLKPLPHVDMEPMTDAFLTASVVAAVAKNGTQSTSITGIANQRVKECNRIAAMVSELAKFGVVANELPDGIEIHGISPNDLVTPSTEKRGIKTFDDHRVAMSFSLLAGLCKDKVLIQERSCTGKTWPGWWDILHTKFKVAIDGYELPLQHEDSTALVEKHGNGKRSIIVIGMRGAGKSTLSKWMASFLGFKLVDLDDVLEEKIGTDIRSFVQQQGWEEFRKQEAIVAKESFIKFSEGCVLSTGGGIVEGEEARESLKSYVKSGGIVLHLHRDLDETVVLLSADTTRPAYVDEIKQVWLRRENWYRECSNYHFYSAHCSSDAEFKHLRNSFTTYIKTITGFHVAQIPKKRSFYTSLTFSDLTEVASSLEDISTGSDAIELRVDLLKETTHTFVADQTAILRKSTNLPIIYTIRTESQGGKFPDNKFEELEELLALGIKLGVQYLDLQLDLPNDLLERILESKKFTKIIASYVDVSGSLRWDNVEWKNRYNQGVSLGADLVKLVGRANSFQDNLSLEVFRGTSTLKPLIAYNVGEKGKLSRVLNPRLTPVTHAKIPAESGNEGALDVAQINKAYTDIGGLSEKHFWIVGNPVGHSRSPNLHNAGYKKLNLPYVFDRFETSDAGEAFQKLIKEDKNFGGLAVTMPLKVDIMKYTDKLSDSAQVIGAVNTVIELEGEQGKYLGENTDWVGISESFVRDGIPNLENVNVNGLVVGGGGTSRAAVYALHQLGCKKIYMLNRTVSKIQEIQKNFPAEYNIEILDSVEAVEAAQPISLIVSCIPADKPIDEQLLNKLERVLYVGGEAKIGGFTPSLLEASYKPRVTPIMKIASEKYEWNVIPGVEMLVNQGITQFQLHTGFVAPYDVVHDAVVNQ | 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;PF01488;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}. | Scheffersomyces stipitis (strain ATCC 58785 / CBS 6054 / NBRC 10063 / NRRL Y-11545) (Yeast) (Pichia stipitis) |
A3MTK6 | CAS4_PYRCJ | MELLSPKPLCSVVNCEDLEKLDHVSALNELRREQEIFKLLPGIYAHRYDFRRVSPSIINDFEYCPRLLWVQHKLGLKLLSEKSVVSIIRGRILHERYERLLSQYENVVAEYKVEIGDLVGVVDLVIKRGGEYIPVEIKTGFSKEAHKTQLQIYISMLKARFGYLVYRNHVEVVHRNDAALDVLKKIREILSAREAPPAKCNSCIFKPICKNLL | 3.1.12.1 | COFACTOR: Name=[2Fe-2S] cluster; Xref=ChEBI:CHEBI:190135; Evidence={ECO:0000269|PubMed:25200083, ECO:0000303|PubMed:24171432}; Note=Binds 1 [2Fe-2S] cluster per subunit. Not required for nuclease activity, since mutation of the Cys residues leads to a colorless but active protein. {ECO:0000269|PubMed:25200083, ECO:0000303|PubMed:24171432}; COFACTOR: Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000269|PubMed:25200083}; Name=Co(2+); Xref=ChEBI:CHEBI:48828; Evidence={ECO:0000269|PubMed:25200083}; Note=Mn(2+) required for ssDNA cleavage activity. Can also utilize Co(2+) and to a lesser extent Mg(2+). {ECO:0000269|PubMed:25200083}; | defense response to virus [GO:0051607]; DNA duplex unwinding [GO:0032508] | null | 2 iron, 2 sulfur cluster binding [GO:0051537]; metal ion binding [GO:0046872]; single-stranded DNA 5'-3' DNA exonuclease activity [GO:0045145]; single-stranded DNA endodeoxyribonuclease activity [GO:0000014] | PF01930; | 3.90.320.10; | CRISPR-associated exonuclease Cas4 family | null | null | CATALYTIC ACTIVITY: Reaction=exonucleolytic cleavage in the 5'- to 3'-direction to yield nucleoside 3'-phosphates.; EC=3.1.12.1; Evidence={ECO:0000269|PubMed:25200083}; | null | null | BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 7-9. {ECO:0000269|PubMed:25200083}; | BIOPHYSICOCHEMICAL PROPERTIES: Temperature dependence: Optimum temperature is 50-70 degrees Celsius. {ECO:0000269|PubMed:25200083}; | FUNCTION: CRISPR (clustered regularly interspaced short palindromic repeat) is an adaptive immune system that provides protection against mobile genetic elements (viruses, transposable elements and conjugative plasmids). CRISPR clusters contain sequences complementary to antecedent mobile elements and target invading nucleic acids. CRISPR clusters are transcribed and processed into CRISPR RNA (crRNA). A ssDNA exonuclease that has 5' to 3' activity, yielding 5'-OH and 3'-phosphate groups. Has Mn(2+)-dependent endonuclease activity on circular ssDNA. Can unwind dsDNA; unwinding does not require ATP. {ECO:0000269|PubMed:24171432, ECO:0000269|PubMed:25200083}. | Pyrobaculum calidifontis (strain DSM 21063 / JCM 11548 / VA1) |
A3MTW6 | THIL_PYRCJ | MSGFGGRGVDEKGFLRWLLGELGVEEDDVAYVDGLVVKVDGAAASTSRLPFQTWADFGWRNVAAAYSDVRVKFAEARLLLASVTAPDLGTAAEVVQGVREASQFFSLAYVGGDLNEGRDVVVDVVLVGWARARVGRAPRPGDVLVTIPQFGYTSLAYRFWQMGGAVVERGVEALKRPKPLWPLPPAECVTAAMDSSDGLGDVLWSMARGVDIVVKELPAPREVLEFAAERGLDVGEIVFNGGEEFLPVFAVRRDCPVESPYVSFAEVVPGEGRVWWRGEELKWRGWAYFRGWG | 2.7.4.16 | null | phosphorylation [GO:0016310]; thiamine biosynthetic process [GO:0009228]; thiamine diphosphate biosynthetic process [GO:0009229] | null | ATP binding [GO:0005524]; magnesium ion binding [GO:0000287]; protein homodimerization activity [GO:0042803]; thiamine-phosphate kinase activity [GO:0009030] | PF00586; | 3.90.650.10;3.30.1330.10; | Thiamine-monophosphate kinase family | null | null | CATALYTIC ACTIVITY: Reaction=ATP + thiamine phosphate = ADP + thiamine diphosphate; Xref=Rhea:RHEA:15913, ChEBI:CHEBI:30616, ChEBI:CHEBI:37575, ChEBI:CHEBI:58937, ChEBI:CHEBI:456216; EC=2.7.4.16; Evidence={ECO:0000255|HAMAP-Rule:MF_02128, ECO:0000269|PubMed:26639844}; | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=0.2 uM for thiamine phosphate (at pH 7.0 and 100 degrees Celsius) {ECO:0000269|PubMed:26639844}; KM=39 uM for ATP (at pH 7.0 and 100 degrees Celsius) {ECO:0000269|PubMed:26639844}; Note=kcat is 0.063 sec(-1) (at pH 7.0 and 100 degrees Celsius). {ECO:0000269|PubMed:26639844}; | PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; thiamine diphosphate from thiamine phosphate: step 1/1. {ECO:0000255|HAMAP-Rule:MF_02128, ECO:0000269|PubMed:26639844}. | BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is around 7.0. Retains about 90% of maximum activity at pH 8.0. {ECO:0000269|PubMed:26639844}; | BIOPHYSICOCHEMICAL PROPERTIES: Temperature dependence: Optimum temperature is 120 degrees Celsius. Activities at 100 and 80 degrees Celsius are about 50% and 10% of that at 120 degrees Celsius, respectively. Is unstable so that the protein loses about 45% of its activity after heating for 15 minutes at 100 degrees Celsius. However, the enzyme is not so intensively inactivated in the presence of ATP. {ECO:0000269|PubMed:26639844}; | FUNCTION: Catalyzes the ATP-dependent phosphorylation of thiamine-monophosphate (TMP) to form thiamine-pyrophosphate (TPP), the active form of vitamin B1. {ECO:0000255|HAMAP-Rule:MF_02128, ECO:0000269|PubMed:26639844}. | Pyrobaculum calidifontis (strain DSM 21063 / JCM 11548 / VA1) |
A3MUY9 | DHE2_PYRCJ | MSTTYIVSDFLINTLLTIKRGVELAGLPPEFYEALEKPKRILVVNIPVKMDDGKIKYFEGYRVQHNDALGPFKGGIRFHPEVTLADDIALAMLMTLKNSLAGLPYGGAKGAVRVDPRRLSRRELEELARGYARAVAPLIGEQLDIPAPDVGTDSQVMAWMVDEYSRLVGRNAPAVFTSKPPELWGNPVREYSTGFGVAVAAREVAKRLWGGIVGKTAAVQGLGNVGRWAAYWLEKMGAKVVAVSDVNGVVYRERGLDVDLIRETKAKGPQLLEMISQKNGVEIVKNPDQIFSLDVDILVPAAIENVVREDNVDGVRARLVVEGANGPTTPGAERRLYERGVVVVPDILANAGGVIMSYLEWVENLQWLFWDEEETRRRLEAIMSNNVARVYARWEKEKSWTMRDAAVVTALERIYNAMKTRGWI | 1.4.1.2 | null | 2-oxoglutarate metabolic process [GO:0006103]; glutamate catabolic process [GO:0006538]; glutamate metabolic process [GO:0006536] | null | glutamate dehydrogenase (NAD+) activity [GO:0004352]; NAD+ binding [GO:0070403]; NADH binding [GO:0070404] | PF00208;PF02812; | 3.40.50.10860;3.40.50.720; | Glu/Leu/Phe/Val dehydrogenases family | null | null | CATALYTIC ACTIVITY: Reaction=H2O + L-glutamate + NAD(+) = 2-oxoglutarate + H(+) + NADH + NH4(+); Xref=Rhea:RHEA:15133, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:16810, ChEBI:CHEBI:28938, ChEBI:CHEBI:29985, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945; EC=1.4.1.2; Evidence={ECO:0000269|PubMed:23508687}; | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=0.028 mM for NAD(+) (at 50 degrees Celsius) {ECO:0000269|PubMed:23508687}; KM=5.3 mM for L-glutamate (at 50 degrees Celsius) {ECO:0000269|PubMed:23508687}; KM=0.01 mM for NADH (at 50 degrees Celsius) {ECO:0000269|PubMed:23508687}; KM=0.92 mM for 2-oxoglutarate (at 50 degrees Celsius) {ECO:0000269|PubMed:23508687}; KM=9.8 mM for ammonia (at 50 degrees Celsius) {ECO:0000269|PubMed:23508687}; Note=kcat is 17 sec(-1) for oxidative deamination of L-glutamate, and 65 sec(-1) for reductive amination of 2-oxoglutarate (at 50 degrees Celsius). {ECO:0000269|PubMed:23508687}; | null | BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 10.5 for oxidative deamination, and 9.5 for reductive amination. Retains more than 80% of its activity after incubation for 30 minutes at pH 4.0-10.5. {ECO:0000269|PubMed:23508687}; | BIOPHYSICOCHEMICAL PROPERTIES: Temperature dependence: Optimum temperature is 80 degrees Celsius for oxidative deamination. Retains full activity after incubation for 10 minutes at temperatures up to 105 degrees Celsius. {ECO:0000269|PubMed:23508687}; | FUNCTION: Catalyzes the reversible oxidative deamination of L-glutamate to 2-oxoglutarate and ammonia, thereby playing a key role at the intersection of the carbon and nitrogen metabolic pathways. Is strictly specific for NAD(+)/NADH as the acceptor/donor, since it cannot use NADP(+)/NADPH. May function in vivo in the catabolic direction. Also catalyzes at low rates the oxidative deamination of L-norvaline, L-2-aminobutyrate, L-valine and L-isoleucine, and the reductive amination of 2-oxovalerate and 2-oxobutyrate. {ECO:0000269|PubMed:23508687}. | Pyrobaculum calidifontis (strain DSM 21063 / JCM 11548 / VA1) |
A3MWK6 | DHE4_PYRCJ | MSQNGQFLEYTLQVIRRGVEMGGFPEDFYKLLSRPKRIIQVSIPVKMDNGSYEVFEGYRVQHNDALGPFKGGIRFHPEVTLADDIALAMLMTLKNSLAGLPYGGAKGAVRVDPRRLSRRELEELARGYARAVAPLIGEQLDIPAPDVGTDSQVMAWMVDEYSKLAGRNAPAVFTSKPPELWGNPVREYSTGFGVAVAAREVAKRLWGGIEGKTVAVHGAGNTGAWAAYWLEKMGAKVVAISDTRGTVVNKAGIPGEQILKVYMEKKRDKSATVLALEGEKIADSNASLYQDVDILVPAAIENVVREDNVGLVRARLVVEGANGPTTPGAERRLYERGVVVVPDILANAGGVIMSYLEWVENLQWLFWDEEETRRRLEAIMSNNVARVYARWEKEKSWTMRDAAVVTALERIYNAMKTRGWI | 1.4.1.4 | null | 2-oxoglutarate metabolic process [GO:0006103]; glutamate catabolic process [GO:0006538]; glutamate metabolic process [GO:0006536] | null | glutamate dehydrogenase (NAD+) activity [GO:0004352]; glutamate dehydrogenase (NADP+) activity [GO:0004354]; NADP+ binding [GO:0070401]; NADPH binding [GO:0070402] | PF00208;PF02812; | 3.40.50.10860;3.40.50.720; | Glu/Leu/Phe/Val dehydrogenases family | null | null | CATALYTIC ACTIVITY: Reaction=H2O + L-glutamate + NADP(+) = 2-oxoglutarate + H(+) + NADPH + NH4(+); Xref=Rhea:RHEA:11612, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:16810, ChEBI:CHEBI:28938, ChEBI:CHEBI:29985, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349; EC=1.4.1.4; Evidence={ECO:0000269|PubMed:23508687}; | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=0.035 mM for NADP(+) (at 50 degrees Celsius) {ECO:0000269|PubMed:23508687}; KM=3.4 mM for L-glutamate (at 50 degrees Celsius) {ECO:0000269|PubMed:23508687}; KM=0.017 mM for NADPH (at 50 degrees Celsius) {ECO:0000269|PubMed:23508687}; KM=1.7 mM for 2-oxoglutarate (at 50 degrees Celsius) {ECO:0000269|PubMed:23508687}; KM=2.2 mM for ammonia (at 50 degrees Celsius) {ECO:0000269|PubMed:23508687}; Note=kcat is 13 sec(-1) for oxidative deamination of L-glutamate, and 95 sec(-1) for reductive amination of 2-oxoglutarate (at 50 degrees Celsius). {ECO:0000269|PubMed:23508687}; | null | BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 9.5 for oxidative deamination, and 9.0 for reductive amination. Retains more than 80% of its activity after incubation for 30 minutes at pH 4.5-9.5. {ECO:0000269|PubMed:23508687}; | BIOPHYSICOCHEMICAL PROPERTIES: Temperature dependence: Optimum temperature is 90 degrees Celsius for oxidative deamination. Retains full activity after incubation for 10 minutes at temperatures up to 90 degrees Celsius. {ECO:0000269|PubMed:23508687}; | FUNCTION: Catalyzes the reversible oxidative deamination of L-glutamate to 2-oxoglutarate and ammonia, thereby playing a key role at the intersection of the carbon and nitrogen metabolic pathways. Shows a high preference for NADP(+)/NADPH as the acceptor/donor over NAD(+)/NADH. May function in vivo in the synthetic direction. Also catalyzes at very low rates the oxidative deamination of L-2-aminobutyrate, and the reductive amination of 2-oxovalerate and 2-oxobutyrate. {ECO:0000269|PubMed:23508687}. | Pyrobaculum calidifontis (strain DSM 21063 / JCM 11548 / VA1) |
A3Q3N5 | KGD_MYCSJ | MSSSPSPFGQNEWLVEEMYRKFREDPSSVDPSWHEFLVDYNPEPTTDSSASENGQQTRTAAPKAPPEPAPAPAPKSQDSKSQAPKQDSKPQESKPQAKAKPAESKSSTKPADAKSEKSGKSGTNGAAKPAAQPADDSDQNQVLRGAAAAVAKNMSASLDVPTATSVRAIPAKLMIDNRVVINNHLKRTRGGKISFTHLIGYAIVAAVKKFPNMNRHFAEVDGKPNAVTPAHTNLGLAIDLQGKDGNRQLVVAAIKKADTMRFGQFIAAYEDIVRRARDGKLTAEDFSGVTISLTNPGTIGTVHSVPRLMRGQGAIIGVGAMEYPAEFQGASEERIADLGIGKLITLTSTYDHRIIQGAESGDFLRTVHQLLLSDDFFDEIFRELGIPYEPVRWRTDNPDSIEDKNARVIELIAAYRNRGHLMADIDPLRLDSNRFRSHPDLDVLTHGLTLWDLDREFKVNGFAGAERKKLRDVLAVLRDAYCRHIGVEYTHILEPEQQQWLQERIEGKHEKPTVAQQKYILSRLNAAEAFETFLQTKYVGQKRFSLEGAETVIPAMDAVIDQCAEHALDEVVIGMPHRGRLNVLANIVGKPYSQIFSEFEGNLNPSQAHGSGDVKYHLGSSGTYLQMFGDNDITVSLTANPSHLEAVDPVMEGLVRAKQDLLDKGDTEDGYTVVPLMLHGDAAFAGQGVVAETLNLALLRGYRTGGTIHLIVNNQIGFTTSPAAAKSSEYCTDVAKMIGAPIFHVNGDDPEAAVWVSRLAVDFRQKFKKDVVIDLLCYRRRGHNEGDDPSMTQPSMYDVIDTKRGVRKSYTEALIGRGDISMKEAEDALRDYQGQLEQVFNEVRELEKHEIEPSESVEADQQIPAKLATAVDKSLLARIGDAHLAVPEGFTVHPRVKPVLEKRREMAYEGKVDWAFAELLALGTMISEGKLVRLSGQDTRRGTFTQRHSVVIDRKTGKEFTPLQLLATDSDGNPTGGKFLVYDSPLSEFAAVGFEYGYSVGNPDAMVLWEAQFGDFINGAQSIIDEFISSGEAKWGQLSDVVLLLPHGHEGQGPDHTSGRIERFLQLWAEGSMTIALPSTPANYFHLLRRHSLDGIQRPLIVFTPKSMLRNKAAVSDIRDFTEQKFRSVLEEPTYTDGDGDRNKVTRILLTSGKIYYELVARKNKESRDDVAIVRIEQLAPLPKRRLAETLDKYPNVDEKFWVQEEPANQGAWPTFGLTLPEMLPDHFTGIKRISRRAMSAPSSGSSKVHAVEQQEILDEAFAP | 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 JLS) |
A3Q8U4 | FADB_SHELP | MIYQSPTIQVELLEDNIARLCFNAEGSVNKFDRETLNSLNDALDALAQTQGVKGLMLTSGKDAFIVGADITEFLGLFAQDDNVLQGWLEDANKVFNKLEDLPFPTISAIKGFALGGGCETILATDLRIADTSARIGLPETKLGIIPGFGGTVRLPRVIGADNALEWITTGKDQRPEAALKVGAIDAVVAPELLETAACQMLQDAISEKIDWQARRQRKLSPLTLPKLEAMMSFATAKGMVFKVAGKHYPAPMAVVEVIEKAALSERAEALQVEHQAFIKLAKTDVAKALIGIFLNDQLVKGKAKKAAKQAQAVNSAAVLGAGIMGGGIAYQSASKGTPIVMKDINQAALDLGLNEAAKLLTAQINRGRSTPAKMAGVLNNITATLDYNALKQADVVVEAVVEHPKVKATVLAEVEQVVGEDAIITSNTSTISINLLAKSLQKPERFCGMHFFNPVHKMPLVEVIRGEHSSEETVASVVAYAAKMGKTPIVVNDCPGFFVNRVLFPYFAGFSGLLEDGADFAAIDKVMEKQFGWPMGPAYLLDVVGLDTGHHAQAVMAEGFPDRMAKEGKDAIDVMFEADRFGQKNGKGFYQYSVDRRGKPKKEVDPLSYELLGNAFGEQKEFSSDEIIARTMIPMIIETVRCLEEGIIATPAEADMGLVYGLGFPPFRGGVFRYLDTLGVANFVALADQYAHLGGLYQVTDKMRELAATNGSYYPA | 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 loihica (strain ATCC BAA-1088 / PV-4) |
A3QJU3 | COQ8B_DANRE | MLLSEVLQVLRGAGKVGAAFTSTQGEQLRLMACNSTFGAGMKAAAEAVEGVMGTVMGGGDMTSKTDEFAGIEKWEEMDLDEAAKWSVASEMPPDFSSKDGRGETSETPVGAATGTIKGAGWPAQNTRFLHVSASQHHFRFVHDSIVARLSPEDIQRAREAKQNIARPVRQKLNERAKERKVPATRISRLANFGGLAVGLGIGAIAEVAKQSFGGKRSEVGALLDSPLLSEANAERIVNTLCKVRGAALKIGQMLSIQDNSFINPQLQKIFERVRQSADFMPAWQMHKVLEEELGSGWREKLSSIEEKPFAAASIGQVHHGVLPGGKEIAMKIQYPGVAESIHSDINNLMSVLKMSVVLPDGLFADSSLEVLQRELAWECDYEREAKCAKRFRNLLKGDPVFVVPEVFDELSARRVITMELVNGVPLDRCVDLDQETRNEICFNILQLCLRELFEFRFMQTDPNWSNFFYNSEQNKIFLLDFGACRDYPELFTDHYIEVVHAASVGDRATVLKKSKDLKFLTGFEAKAFEDAHVEAVMILGEAFASAEAFDFGTQSTTQRIQSLIPVMLRHRLTPPPEESYSLHRKMAGSFLICSKLKARFSCRNMFLDVYNAYKRQQQERRSQV | 2.7.-.- | null | cerebellar Purkinje cell layer morphogenesis [GO:0021692]; glomerular basement membrane development [GO:0032836]; phosphorylation [GO:0016310]; podocyte development [GO:0072015]; ubiquinone biosynthetic process [GO:0006744] | cytosol [GO:0005829]; mitochondrial membrane [GO:0031966]; plasma membrane [GO:0005886] | ATP binding [GO:0005524]; kinase activity [GO:0016301] | PF03109; | null | Protein kinase superfamily, ADCK protein kinase family | null | SUBCELLULAR LOCATION: Mitochondrion membrane {ECO:0000250|UniProtKB:Q96D53}; Single-pass membrane protein {ECO:0000250|UniProtKB:Q96D53}. Cytoplasm, cytosol {ECO:0000250|UniProtKB:Q96D53}. Cell membrane {ECO:0000250|UniProtKB:Q96D53}. | null | null | null | null | null | FUNCTION: Atypical kinase involved in the biosynthesis of coenzyme Q, also named ubiquinone, an essential lipid-soluble electron transporter for aerobic cellular respiration. Its substrate specificity is unclear: does not show any protein kinase activity. Probably acts as a small molecule kinase, possibly a lipid kinase that phosphorylates a prenyl lipid in the ubiquinone biosynthesis pathway. Required for podocyte migration. {ECO:0000250|UniProtKB:Q8NI60, ECO:0000250|UniProtKB:Q96D53}. | Danio rerio (Zebrafish) (Brachydanio rerio) |
A3QM97 | CNNM1_CAEEL | MSASCLRLLTLSLFILGQCNVTAAQNGVDDEVTTVTAILDSATTAAADNSTVPTQSASNNNTSQSSKIPTIFGMRVELPADDPFGYDKHGVCSVTPEEEFKVVIYGNHLDKIHQIIWTFTNNCSEPAYVIDALNHFKVHFNHKATFHLTLKLLPEMVHAYKMCVKPKVAPGSPPLGEIYPLDDISTWLTTERPPKEYFLPLPLQIACIGFLLCLSALFSGLTLGLMSLTPQELELVIKSGAIKEQKCAAKILPVRKKGNLLLCSLLLGNVIVNSAISILMGELTTGIYALIGSTMGIVIFGEILPQSICVKKGLEVGAHTISITQLFIFLTFPIAWPVSKLLDCLLGDEYQAYDRKRLMELIKMSITDNGQVSNELKIAVGAMEIADKVVKDVMTKIEDVFMLPDTTVLNAKTVMEIVKMGYTRIPVYQYGDKNNVTDMLFVKDLALLDPDDNFTVKTVCGYHKHPVKFVMNDTPLPNLLEAFKKGEGHLAMVKRLINTDDKHDPSYVLVGVVTLEDIVEEILQAEINDEFDIVSDNVNKVKIKKEQNRDATKYFGDHEAPQTMISMQLQMVALQWLVSNERGFRQEFLDTNVLERLIRSSARRVDVSALMAMGDDAINVPRLAKVYTKDELSDKYILILEGRIQVTIGASGMMFEAGPWHHFGGEIMAKLVDGAATLGRSMSIVGTSELSARRPDLMFKPDYSAVVKEDCTYLEISVSAYINAYKASLMQRERPLNDLSDVSHNSSAHNSNLSLVEKPGPITDPSAMLVPENVRKPSVVSMDSPKILVGLGQHPVAPVAEEEEMALLDQP | null | null | determination of adult lifespan [GO:0008340]; intracellular manganese ion homeostasis [GO:0030026]; magnesium ion homeostasis [GO:0010960]; magnesium ion transport [GO:0015693]; positive regulation of gonad development [GO:1905941]; positive regulation of multicellular organism growth [GO:0040018]; positive regulation of vulval development [GO:0040026]; response to magnesium ion [GO:0032026] | basolateral plasma membrane [GO:0016323]; cytoplasm [GO:0005737]; plasma membrane [GO:0005886] | transmembrane transporter activity [GO:0022857] | PF01595; | 3.10.580.10; | ACDP family | null | SUBCELLULAR LOCATION: Basolateral cell membrane {ECO:0000269|PubMed:27564576}; Multi-pass membrane protein {ECO:0000255}. | null | null | null | null | null | FUNCTION: Probable metal transporter. Probably acts redundantly with the other metal transport proteins cnnm-2, cnnm-3, cnnm-4 and cnnm-5 to regulate Mg(2+) homeostasis. Promotes postembryonic gonad development by regulating Mg(2+) levels, probably via AMPK signaling. {ECO:0000269|PubMed:27564576}. | Caenorhabditis elegans |
A3R052 | PILR1_LINPE | MKPCSVLVVGGTGYIGKRIVSASLYLGHDTYVLKRPGTGLDIEKLQLLLSFKKRGAHLVEASFSDHDSLVRAVRLVDVVICTMSGVHFRSHNILLQLKLVEAIKEAGNVKRFIPSEFGMDPARMGQAMEPGRETFDQKMVVRKAIEEANIPHTYISANCFAGYFVGNLSQLGTLTPPSDKVIIYGDGNVKVVYVDEDDVAKYTIKAIEDDRTVNKTVYLRPPENMMSQRELVAVWEKLSGNQLEKIELPPQDFLALMEGTTVAEQAGIGHFYHIFYEGCLTNFEINAENGEEEASRLYPEVEYTRVHDYLKIYL | 1.23.1.1; 1.23.1.4 | null | (+)-lariciresinol biosynthetic process [GO:1902132]; (+)-pinoresinol catabolic process [GO:1902125]; (+)-secoisolariciresinol biosynthetic process [GO:1902135]; (-)-lariciresinol catabolic process [GO:1902128]; lignan biosynthetic process [GO:0009807] | null | lariciresinol reductase activity [GO:0010284]; pinoresinol reductase activity [GO:0010283] | PF05368; | 3.40.50.720;3.90.25.10; | NmrA-type oxidoreductase family, Isoflavone reductase subfamily | null | null | CATALYTIC ACTIVITY: Reaction=(+)-lariciresinol + NADP(+) = (+)-pinoresinol + H(+) + NADPH; Xref=Rhea:RHEA:34419, ChEBI:CHEBI:40, ChEBI:CHEBI:15378, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349, ChEBI:CHEBI:67246; EC=1.23.1.1; Evidence={ECO:0000269|PubMed:17257599}; CATALYTIC ACTIVITY: Reaction=(+)-secoisolariciresinol + NADP(+) = (-)-lariciresinol + H(+) + NADPH; Xref=Rhea:RHEA:34431, ChEBI:CHEBI:15378, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349, ChEBI:CHEBI:67244, ChEBI:CHEBI:67247; EC=1.23.1.4; Evidence={ECO:0000269|PubMed:17257599}; | null | null | null | null | FUNCTION: Reductase involved in the lignan justicidin B biosynthesis. Catalyzes the enantioselective conversion of (+)-pinoresinol into (+)-lariciresinol and of (-)-lariciresinol into (+)-secoisolariciresinol. Low activity with the other enantiomers. Abstracts the 4R-hydride from the NADPH cofactor during catalysis. {ECO:0000269|PubMed:17257599}. | Linum perenne (Perennial flax) |
A3R064 | DOK3_CHICK | MERPVKDGIIYVQHCKFGKRTWRKIRAQLFAASPFGVARMEKFDARDHGTVSDISLQRCARRVIRLSDCVSVGPMGTESCPKATAAFYLTTTEKNYVLAAEQRDEWIEQLCQLAFQGKKEAEQSSSTGLQPIPMEENCLYSSWQDLTEFPVLVLRTEAAARCELHGHYVLAALPHSLTLKDAQSQQPLLTWPYPFLRKFGQDQNIFSFEAGRRSDSGEGTFTFSTPRAAELCRAVAAAIACQQQGQESPQPSAQGLSNQPWGAEAEDPQCSPTLGRAHSGSHSASYPSLNLLRFPPVEPEAPAPIVYASIARGQQPHFRPCPGQPLPEHLYENIFTAQPRPLAEEEAEEEEGRWELGCRQAPEGHSSEAAVPYPARSAPQPHTQRWAPGGSRGGAEEPSRPKPQRTLRAKLVRLLSRDGPGARDWS | null | null | positive regulation of MAPK cascade [GO:0043410]; Ras protein signal transduction [GO:0007265]; transmembrane receptor protein tyrosine kinase signaling pathway [GO:0007169] | cytoplasm [GO:0005737]; plasma membrane [GO:0005886] | null | PF02174; | 2.30.29.30; | DOK family, Type A subfamily | PTM: Tyrosine-phosphorylated in the presence of GRB2. {ECO:0000269|PubMed:17290227}. | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:17290227}. Cell membrane {ECO:0000269|PubMed:17290227}; Peripheral membrane protein {ECO:0000269|PubMed:17290227}; Cytoplasmic side {ECO:0000269|PubMed:17290227}. | null | null | null | null | null | FUNCTION: DOK proteins are enzymatically inert adaptor or scaffolding proteins. They provide a docking platform for the assembly of multimolecular signaling complexes. Plays a role as negative regulator of the mobilization of calcium ions and of calcium signaling. {ECO:0000269|PubMed:17290227}. | Gallus gallus (Chicken) |
A3R0T9 | VM3_OPHHA | MIQVLLVTICLVVFPYQGSSIILESGKVNDYEVVYPQKIPVLPKSKIQRREQKMYEDTMKYEFKVNGEPVVLHLERNKELFSKDYTETHYSPDGREITTSPPVEDHCYYHGYIQSDIDSTAILNACNGLKGYFRHHGEAYHIEPLKFSDSEAHAVYKYENIEKEDETPKICGVKHSTWESDEPIEKISQKKDFLEEKKYLELYIVADYVMFRKYGRNVTTIRMRVFDMVNYITVVYKALNIHVALIGFEIWSLKDKFVINASTKNNLLHFSIWRSTVLRKRNDNAQLLTGVDLNGYTLGSAYLKAMCDVLQSVGIVQDYSKSPYLVGAAMAHEIGHNLGMEHDTKTCSCMRGNCIMSPEEEGSDFPMEFSSCSLYDFQNYMLTDTPQCLINKPSNTSIIKNAVCGNYVEEEGEECDCGSPEQCENNCCEAATCKLKPGAKCAKGACCKKCQFKKAGAECRAARNECDLPEFCIGQSAECPMDRFHKNGHSCQNDQGYCFRGYCPTLAKQCITLWGSDAKVAPDECFQNNTNGNEYDYCKKTNNVIIPCKPTDVKCGRLYCTGGTENPSEGEKISSDPCKASYSEIEDIGMVDHRTKCGEKMVCSDGKCIPL | 3.4.24.- | COFACTOR: Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000250}; Note=Binds 1 zinc ion per subunit. {ECO:0000250}; | envenomation resulting in fibrinogenolysis in another organism [GO:0044485]; envenomation resulting in hemorrhagic damage in another organism [GO:0044358]; envenomation resulting in negative regulation of platelet aggregation in another organism [GO:0044477]; proteolysis [GO:0006508] | extracellular region [GO:0005576]; host extracellular space [GO:0043655]; plasma membrane [GO:0005886] | metalloendopeptidase activity [GO:0004222]; toxin activity [GO:0090729]; zinc ion binding [GO:0008270] | PF08516;PF00200;PF01562;PF01421; | 3.40.390.10;4.10.70.10; | Venom metalloproteinase (M12B) family, P-III subfamily, P-IIIa sub-subfamily | null | SUBCELLULAR LOCATION: Secreted. | null | null | null | null | null | FUNCTION: Snake venom zinc metalloproteinase that has hemorrhagic activity. Inhibits ADP-, TMVA- and stejnulxin-induced platelet aggregation in a dose-dependent manner (on washed platelet, but not on platelet rich plasm). Also specifically degrades alpha-chain of fibrinogen (FGA). {ECO:0000269|PubMed:17337026}. | Ophiophagus hannah (King cobra) (Naja hannah) |
A3RF67 | BAGBG_DALNI | MHAMTFKAILLLGLLALVSTSASIAFAKEVRATITEVPPFNRNSFPSDFIFGTAASSYQYEGEGRVPSIWDNFTHQYPEKIADGSNGDVAVDQFHHYKEDVAIMKYMNLDAYRLSISWPRILPTGRASGGINSTGVDYYNRLINELLANDITPFVTIFHWDLPQALEDEYGGFLNHTIVNDFRDYADLCFNLFGDRVKHWITVNEPSIFTMNGYAYGIFAPGRCSPSYNPTCTGGDAGTEPDLVAHNLILSHAATVQVYKKKYQEHQNGIIGISLQIIWAVPLSNSTSDQKAAQRYLDFTGGWFLDPLTAGQYPESMQYLVGDRLPKFTTDEAKLVKGSFDFVGINYYTSSYLTSSDASTCCPPSYLTDSQVTFSSQRNGVFIGPVTPSGWMCIYPKGLRDLLLYIKEKYNNPLVYITENGMDELDDPSQSLEESLIDTYRIDSYYRHLFYVRSAIGSGANVKGFFAWSLLDNFEWNEGFTSRFGLNFVNYTTLTRYHKLSATWFKYFLARDQEIAKLDISAPKARWSSSTMIKEEKRKPKWAIQAF | 3.2.1.161 | null | carbohydrate metabolic process [GO:0005975] | null | beta-apiosyl-beta-glucosidase activity [GO:0033956] | PF00232; | 3.20.20.80; | Glycosyl hydrolase 1 family | null | null | CATALYTIC ACTIVITY: Reaction=7-[beta-D-apiofuranosyl-(1->6)-beta-D-glucopyranosyloxy]isoflavonoid + H2O = a 7-hydroxyisoflavonoid + beta-D-apiofuranosyl-(1->6)-D-glucose.; EC=3.2.1.161; Evidence={ECO:0000269|PubMed:16098548}; | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=14.7 mM for pNP-beta-D-glucoside {ECO:0000269|PubMed:16098548}; KM=1.8 mM for pNP-beta-D-fucoside {ECO:0000269|PubMed:16098548}; KM=0.5 mM for dalpatein 7-O-beta-D-apiofuranosyl-(1->6)-beta-D-glucopyranoside {ECO:0000269|PubMed:16098548}; KM=0.7 mM for dalnigrein 7-O-beta-D-apiofuranosyl-(1->6)-beta-D-glucopyranoside {ECO:0000269|PubMed:16098548}; KM=0.11 mM for daidzin {ECO:0000269|PubMed:16098548}; KM=0.09 mM for genistin {ECO:0000269|PubMed:16098548}; | null | BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 5.0-6.0. Half maximum activity is seen at pH 3.5 and 6.5. {ECO:0000269|PubMed:16098548}; | BIOPHYSICOCHEMICAL PROPERTIES: Temperature dependence: Optimum temperature is 65 degrees Celsius. {ECO:0000269|PubMed:16098548}; | FUNCTION: Hydrolyzes dalpatein 7-O-beta-D-apiofuranosyl-(1->6)-beta-D-glucopyranoside and dalnigrein 7-O-beta-D-apiofuranosyl-(1->6)-beta-D-glucopyranoside. Also has activity towards pNP-beta-D-fucoside and pNP-beta-D-glucoside, but not pNP-beta-cellobioside. {ECO:0000269|PubMed:16098548}. | Dalbergia nigrescens (Thai blackwood) |
A3RFZ7 | FCG3A_MACMU | MWQLLLPTALLLLVSAGMRAEDLPKAVVFLEPQWYRVLEKDSVTLKCQGAYSPEDNSTRWFHNESLISSQTSSYFIAAARVNNSGEYRCQTSLSTLSDPVQLEVHIGWLLLQAPRWVFKEEESIHLRCHSWKNTLLHKVTYLQNGKGRKYFHQNSDFYIPKATLKDSGSYFCRGLIGSKNVSSETVNITITQDLAVSSISSFFPPGYQVSFCLVMVLLFAVDTGLYFSVKKSVPSSTRDWEDHKFKWSKDPQDK | null | null | antibody-dependent cellular cytotoxicity [GO:0001788]; calcium-mediated signaling [GO:0019722]; cell surface receptor signaling pathway [GO:0007166]; Fc-gamma receptor signaling pathway [GO:0038094]; natural killer cell activation [GO:0030101]; natural killer cell degranulation [GO:0043320]; natural killer cell mediated cytotoxicity [GO:0042267]; phosphatidylinositol 3-kinase/protein kinase B signal transduction [GO:0043491] | external side of plasma membrane [GO:0009897]; extracellular space [GO:0005615]; plasma membrane [GO:0005886] | IgG binding [GO:0019864]; IgG receptor activity [GO:0019770] | PF13895; | 2.60.40.10; | null | PTM: Glycosylated. Glycosylation plays an inhibitory role in the interaction with IgG1 and IgG2. {ECO:0000250|UniProtKB:P08637}.; PTM: Undergoes rapid ectodomain shedding upon NK cell stimulation. The soluble form is produced by a proteolytic cleavage mediated by ADAM17. Repeated stimulation causes receptor shedding, a mechanism that allows for increased NK cell motility and detachment from opsonized target cells while avoiding activation-induced NK cell apoptosis. {ECO:0000250|UniProtKB:P08637}. | SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:33208458}; Single-pass type I membrane protein {ECO:0000255}. Secreted {ECO:0000250|UniProtKB:P08637}. Note=Exists also as a soluble receptor. {ECO:0000250|UniProtKB:P08637}. | null | null | null | null | null | FUNCTION: Receptor for the invariable Fc fragment of immunoglobulin gamma (IgG). Optimally activated upon binding of clustered antigen-IgG complexes displayed on cell surfaces, triggers lysis of antibody-coated cells, a process known as antibody-dependent cellular cytotoxicity (ADCC). Does not bind free monomeric IgG, thus avoiding inappropriate effector cell activation in the absence of antigenic trigger (PubMed:33208458). Mediates IgG effector functions on natural killer (NK) cells. Binds antigen-IgG complexes generated upon infection and triggers NK cell-dependent cytokine production and degranulation to limit viral load and propagation. Involved in the generation of memory-like adaptive NK cells capable to produce high amounts of IFNG and to efficiently eliminate virus-infected cells via ADCC. Regulates NK cell survival and proliferation, in particular by preventing NK cell progenitor apoptosis (By similarity). Fc-binding subunit that associates with CD247 and/or FCER1G adapters to form functional signaling complexes. Following the engagement of antigen-IgG complexes, triggers phosphorylation of immunoreceptor tyrosine-based activation motif (ITAM)-containing adapters with subsequent activation of phosphatidylinositol 3-kinase signaling and sustained elevation of intracellular calcium that ultimately drive NK cell activation. The ITAM-dependent signaling coupled to receptor phosphorylation by PKC mediates robust intracellular calcium flux that leads to production of pro-inflammatory cytokines, whereas in the absence of receptor phosphorylation it mainly activates phosphatidylinositol 3-kinase signaling leading to cell degranulation (By similarity). Costimulates NK cells and trigger lysis of target cells independently of IgG binding (By similarity). Mediates the antitumor activities of therapeutic antibodies. Upon ligation on monocytes triggers TNFA-dependent ADCC of IgG-coated tumor cells (By similarity). Mediates enhanced ADCC in response to afucosylated IgGs (PubMed:34485821). {ECO:0000250|UniProtKB:P08637, ECO:0000269|PubMed:33208458, ECO:0000269|PubMed:34485821}. | Macaca mulatta (Rhesus macaque) |
A3RL54 | SL9C1_STRPU | MKKRVVKLRELVPAVAALAVAVLIQSATGSSGGSGHTPTTQATHADDHDLTTHNGTEEHDDGHDDGHDDLHAHAPKVIVFISGSCLFGAISRSLFKKLPIPYTVVLLILGAILGVVASNVPLVEEHTRDVAHMDPHVLLQIFLPVLIFESAFAMDVHTFMRSFSQVCILALFGLVVASVLTAVLAMNLFNYNWNFSEAMMFGAIMSATDPVAVVALLKDLGASKQLGTIIEGESLLNDGCAIVIFNVFMKMVFFPQLTSTVGQNVLYFLQVAVAGPLWGYAVAKVTVFFLSHIFNDALVEITITLAATYLTYYIGDIWLEVSGVLAVVVLGLIVNAEKTSISPEVEVFLHRFWEMLAYLANTLIFMMVGVVVTQKALVAVDKMDWFYLIILYLAITIIRGMVISLFSPILSRIGYGLTWRNAVIMTWGGLRGAVGLALALVVENLAGNDVIGSKFLFHTAGIVVLTLVINATTIQTLLRILGMSDISIPKRLAMAGAVRRIHEGQNRTLNMLKSDRFLADADWDIATAACEISDPYSALSDDENAPADELTLGERKSVCPGCKAMVPNEPSPREFADMMEEARLRMLKAEKISYWKQFEHGMLAREALRLLVQHAEVAADEKDQFILVDDLKKSWQIKGIYPWLKRKLEDLISEKKIAAIPMPKYKLGKLMYKICHHMAFEVTINIAIVLNIVPIIMEFVVQDKMASVSTMAAPGSTVSSEPSSLQKIEDALRISNYVFFVIYAIEAIVKILGLGRHYIVSHWNKFDAFILVVALVDIIIAETLLKGSITINLSSIKVVKLFRLLRGLRMLRLTKALIPKLILVVNGKINNQLSLGYDVGKGYIIGEEEVGKIIDRMVDNKKILRELKHISETGRLQVVKELGLLQREHPGIAVSVKTRQAIRTILNHSRETIHELQGAGLLDEMEAHKLELTVEIKMKRLMNAPSSIPPPPPENLLKNVSWLAGDMKLIDFIKARASLLHFDYGEVIVREGDESDGLFLIVSGLVKLYGKSAFLDHDNPPVTAGSEENEVFEDYLTVGNVIGEMGVLTKKPRNATVTCETTVQVYFITAEDMNIAIDTFTLYPSLEYRLWRVVAIRIATPLIMEQMAFQGWTQEKVKLHLERGYLVDLAESHFQFNIDATLEDVILINGTAYNAHTREEIRSPCLISRTVHKLTFQYTATEEPRLFVVRNAEYNGPILDGRLDVDSKRSLISITEISSNMCLKHAAELRQKNSKVMLSRKSSGAAAKEEEDCIPNTSDVEQAAGVSPSVPTKTTPKPKSFLPSLGLSMSKERVNGEAVEESPVKTKQGEETPETEEGAAPRVNV | null | null | cAMP-mediated signaling [GO:0019933]; potassium ion transmembrane transport [GO:0071805]; regulation of intracellular pH [GO:0051453]; single fertilization [GO:0007338]; sodium ion import across plasma membrane [GO:0098719] | plasma membrane [GO:0005886]; sperm flagellum [GO:0036126]; sperm head [GO:0061827] | cAMP binding [GO:0030552]; cGMP binding [GO:0030553]; potassium:proton antiporter activity [GO:0015386]; protein homodimerization activity [GO:0042803]; sodium:proton antiporter activity [GO:0015385] | PF00027;PF00999; | 6.10.140.1330;2.60.120.10;1.20.120.350; | Monovalent cation:proton antiporter 1 (CPA1) transporter (TC 2.A.36) family | null | SUBCELLULAR LOCATION: Cell projection, cilium, flagellum membrane {ECO:0000269|PubMed:30022052}; Multi-pass membrane protein. Note=Observed primarily in sperm flagellum and at the tip of the sperm head. {ECO:0000269|PubMed:30022052}. | CATALYTIC ACTIVITY: Reaction=H(+)(out) + Na(+)(in) = H(+)(in) + Na(+)(out); Xref=Rhea:RHEA:29419, ChEBI:CHEBI:15378, ChEBI:CHEBI:29101; Evidence={ECO:0000269|PubMed:30022052, ECO:0000269|PubMed:37880360}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:29420; Evidence={ECO:0000305|PubMed:30022052}; PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:29421; Evidence={ECO:0000305|PubMed:30022052}; | null | null | BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 6.5. {ECO:0000269|PubMed:37880360}; | null | FUNCTION: Electroneutral sodium:proton antiporter that regulates intracellular pH of sperm along with capacitation and fertility. Activated in response to egg-derived chemoattractants, couples membrane voltage to sodium:proton exchange and transduces membrane hyperpolarization to cytoplasmic alkalization to cAMP signaling and ultimately to sperm motility. {ECO:0000269|PubMed:30022052, ECO:0000269|PubMed:37880360, ECO:0000269|PubMed:37880361}. | Strongylocentrotus purpuratus (Purple sea urchin) |
A3RM20 | PHOSP_RABVI | MSKIFVNPSAIRAGLADLEMAEETVDLINKNIEDNQAHLQGEPIEVDNLPEDMRRLHLDDEKPSGLGGMAKAGEVKYREDFQMDEGEDPNLLFQSYLDNVGVQIVRQMRSGERFLKIWSQTVEEIISYVTVNFPNPPGRSSEDKSTQTTGRELKKETTSASYQRDSQSSKARMAAQTASGPPALEWSATNEEDDLSVEAEIAHQIAESFSKKHKFPSRSSGIFLYNFEQLKMNLDDIVKEAKNVPGVTRLAHDGSKLPLRCVLGWVGLANSKKFQLLVEPDKLNKIMQDDLNRYTSS | null | null | microtubule-dependent intracellular transport of viral material towards nucleus [GO:0075521]; symbiont entry into host cell [GO:0046718]; symbiont-mediated suppression of host cytoplasmic pattern recognition receptor signaling pathway via inhibition of TBK1 activity [GO:0039723]; symbiont-mediated suppression of host JAK-STAT cascade via inhibition of STAT1 activity [GO:0039563]; symbiont-mediated suppression of host JAK-STAT cascade via inhibition of STAT2 activity [GO:0039564]; symbiont-mediated suppression of host toll-like receptor signaling pathway [GO:0039722]; symbiont-mediated suppression of host type I interferon-mediated signaling pathway [GO:0039502]; viral transcription [GO:0019083]; virus-mediated perturbation of host defense response [GO:0019049] | host cell [GO:0043657]; host cell cytoplasm [GO:0030430]; host cell nucleus [GO:0042025]; virion component [GO:0044423] | RNA-dependent RNA polymerase activity [GO:0003968] | PF03012; | 6.10.140.1560;1.20.120.820; | Lyssavirus protein P family | PTM: Phosphorylated by host PKC and by an unknown kinase. {ECO:0000250}. | SUBCELLULAR LOCATION: [Phosphoprotein]: Virion. Host cytoplasm {ECO:0000250}.; SUBCELLULAR LOCATION: [Isoform P2]: Host cytoplasm {ECO:0000250}.; SUBCELLULAR LOCATION: [Isoform P3]: Host nucleus {ECO:0000250}.; SUBCELLULAR LOCATION: [Isoform P4]: Host nucleus {ECO:0000250}.; SUBCELLULAR LOCATION: [Isoform P5]: Host nucleus {ECO:0000250}. | null | null | null | null | null | FUNCTION: Non catalytic polymerase cofactor and regulatory protein that plays a role in viral transcription and replication. Stabilizes the RNA polymerase L to the N-RNA template and binds the soluble protein N, preventing it from encapsidating non-genomic RNA. Also inhibits host IFN-alpha and IFN-beta signaling by binding and retaining phosphorylated STAT1 in the cytoplasm or by inhibiting the DNA binding of STAT1 in the nucleus. Might be involved, through interaction with host dynein, in intracellular microtubule-dependent virus transport of incoming virus from the synapse toward the cell body (By similarity). Inhibits interferon induction pathways by interacting with host TBK1 and preventing the formation of dynamic cytoplasmic condensates that have liquid properties and that are essential for interferon production (By similarity). {ECO:0000250, ECO:0000250|UniProtKB:P16286}. | Rabies virus (strain India) (RABV) |
A3RM23 | L_RABVI | MLDPGEVYDDPVDPIESDAEPRGAPTVPNILRNSDYNLNSPLIEDPARLMLEWLTTGNRPYRMTLTDNCSRSYKVLKDYFKKVDLGSLKVGGTAAQSMISLWLYGAHSESNRSRKCITELAHFYSKSSPIEKLLNCTLGNRGLRIPPEGVLSCLERVDYDKAFGRYLANTYSSYLFFHVITLYMNALDWDEEKTILALWKELTSVDIGKDLVKFKDQIWGLLIVTKDFVYSHSSNCLFDRNYTLMLKDLFLSRFNSLMILLSPPEPRYSDDLISQLCQLYIAGDQVLSMCGNSGYEVIKILEPYVVNSLVQRAERFRPLIHSLGDFPVFIKDKVSQLEGTFGPSAKRFFGVLDQFDNIHDLVFVYGCYRHWGHPYIDYRKGLSKLYDQVHIKKVIDKSYQECLASDLARRILRWGFDKYSKWYLDSRLLTRDHPLTPYIKTQTWPPKHIVDLVGDTWHKLPITQIFEIPEPMDPSEILDDKSHSFTRARLASWLSENRGGPAPSEKVIITALSKPPVNPREFLKTIDLGGLPDEDLIIGLKPKERELKIEGRFFALMSWNLRLYFVITEKLLANYILPLFDALTMTDNLNKVFKKLIDRVTGQGLLDYSRVTYAFHLDYEKWNNHQRLESTEDVFSVLDHVFGLKRVFSRTHEFFQKSWIYYSDRSDLIGLWEDQIYCLDMSNGPTCWNGQDGGLEGLRQKGWSLVSLLMIDRESQTRNTRTKILAQGDNQVLCPTYMLSPGLSREGLLYELESISRNALSIYRAIEEGASKLGLIIKKEETMCSYDFLIYGKTPLFRGNILVPESKRWARVSCISNDQIVNLANIMSTVSTNALTVAQHSQSLIKPMRDFLLMSVQAVFHYLLFSPILKGRVYKILSAEGESFLLAMSRIIYLDPSLGGVSGMSLGRFHIRQFSDPVSEGLSFWREIWLSSHESWIHALCQEAGNPDLGERTLESFTRLLEDPTTLNIKGGASPTILLKDAIRKALYDEVDKVENSEFREAILLSKTHRDNFILFLKSVEPLFPRFLSELFSSSFLGIPESIIGLIQNSRTIRRQFRRSLSRTLEESFYNSEIHGINRMTQTPQRVGRVWPCSSERADLLREISWGRKVVGTTVPHPSEMLGLLPKSSISCPCGATGGGNPRVSVSVLPSFDQSFFSRGPLKGYLGSSTSMSTQLFHAWEKVTNVHVVKRALSLKESINWFITRNSNLAQTLIRNIMSLTGPDFPLEEAPVFKRTGSALHRFKSARYSEGGYSSVCPNLLSHISVSTDTMSDLTQDGKNYDFMFQPLMLYAQTWTSELVQKDTRLRDSTFHWHLRCNRCVRPIDDITLETSQIFEFPDVSKRISRMVSGAVPHFQKLPDIRLKPGDFESLSGREKSRHIGSAQGLLYSILVAIHDSGYNDGTIFPVNIYGKVSPRDYLRGLARGVLIGSSICFLTRMTNININRPLELISGVISYILLRLDNHPSLYIMLREPSLRGEIFSIPQKIPAAYPTTMKEGNRSILCYLQHVLRYEREVITASPENDWLWIFSDFRSAKMTYLTLITYQSHLLLQRVERNLSKSMRANLRQMSSLMRQVLGGHGEDTLESDDDVQRLLKDSLRRTRWVDQEVRHAARTMTGDYSPNKKLSRKAGGSEWVCSAQQVAVSTSANPAPVLELDIRALSKRFQNPLISGLRVVQWATGAHYKLKPILDDLNVFPSLCLVVGDGSGGISRAVLNMFPDAKLVFNSLLEVNDLMASGTHPLPPSAIMSGGDDIVSRVIDFDSIWEKPSDLRNLTTWKYFQSVQKQVNMSYDLIICDAEVTDIASINRITLLMSDFALSIDGPLYLVFKTYGTMLVNPDYKAIQHLSRAFPSVTGFITQVTSSFSSELYLRFSKRGKFFRDAEYLTSSTLREMSLVLFNCSSPRSEMQRARSLNYQDLVRGFPEEIISNPYNEMIITLIDSDVESFLVHKMVDDLELQRRTLSKVAIIIAIMIVFSNRVFNVSKPLTDPLFYPPSDPKILRHFNICCSTMMYLSTALGDVPSFARLHDLYNRPITYYFRKQVIRGNIYLSWSWSDDTAVFKRVACNSSLSLSSHWIRLIYKIVKTTRLVGSIEDLSGEIERHLRGYNRWITLEDIRCRSSLLDYSCL | 2.1.1.375; 2.7.7.48; 2.7.7.88; 3.6.1.- | null | negative stranded viral RNA replication [GO:0039689] | host cell cytoplasm [GO:0030430]; virion component [GO:0044423] | ATP binding [GO:0005524]; GTPase activity [GO:0003924]; mRNA 5'-cap (guanine-N7-)-methyltransferase activity [GO:0004482]; RNA-dependent RNA polymerase activity [GO:0003968] | PF21080;PF14314;PF21081;PF14318;PF00946; | null | Rhabdoviruses protein L family | null | SUBCELLULAR LOCATION: Virion {ECO:0000250|UniProtKB:P03523}. Host cytoplasm {ECO:0000250|UniProtKB:P03523}. Note=L and P are packaged asymmetrically towards the blunt end of the virus. {ECO:0000250|UniProtKB:P03523}. | CATALYTIC ACTIVITY: Reaction=a ribonucleoside 5'-triphosphate + RNA(n) = diphosphate + RNA(n+1); Xref=Rhea:RHEA:21248, Rhea:RHEA-COMP:14527, Rhea:RHEA-COMP:17342, ChEBI:CHEBI:33019, ChEBI:CHEBI:61557, ChEBI:CHEBI:140395; EC=2.7.7.48; Evidence={ECO:0000255|PROSITE-ProRule:PRU00539}; CATALYTIC ACTIVITY: Reaction=a 5'-end (5'-triphosphoguanosine)-adenylyl-adenylyl-cytidylyl-adenosine in mRNA + 2 S-adenosyl-L-methionine = a 5'-end (N(7)-methyl 5'-triphosphoguanosine)-(2'-O-methyladenylyl)-adenylyl-cytidylyl-adenosine in mRNA + H(+) + 2 S-adenosyl-L-homocysteine; Xref=Rhea:RHEA:65376, Rhea:RHEA-COMP:16797, Rhea:RHEA-COMP:16798, ChEBI:CHEBI:15378, ChEBI:CHEBI:57856, ChEBI:CHEBI:59789, ChEBI:CHEBI:156483, ChEBI:CHEBI:156484; EC=2.1.1.375; Evidence={ECO:0000250|UniProtKB:P03523}; CATALYTIC ACTIVITY: Reaction=a 5'-end (5'-triphosphoguanosine)-adenylyl-adenylyl-cytidylyl-adenosine in mRNA + S-adenosyl-L-methionine = a 5'-end (5'-triphosphoguanosine)-(2'-O-methyladenylyl)-adenylyl-cytidylyl-adenosine in mRNA + H(+) + S-adenosyl-L-homocysteine; Xref=Rhea:RHEA:65380, Rhea:RHEA-COMP:16797, Rhea:RHEA-COMP:16801, ChEBI:CHEBI:15378, ChEBI:CHEBI:57856, ChEBI:CHEBI:59789, ChEBI:CHEBI:156482, ChEBI:CHEBI:156484; Evidence={ECO:0000250|UniProtKB:P03523}; CATALYTIC ACTIVITY: Reaction=a 5'-end triphospho-adenylyl-adenylyl-cytidylyl-adenosine in mRNA + GDP + H(+) = a 5'-end (5'-triphosphoguanosine)-adenylyl-adenylyl-cytidylyl-adenosine in mRNA + diphosphate; Xref=Rhea:RHEA:65436, Rhea:RHEA-COMP:16797, Rhea:RHEA-COMP:16799, ChEBI:CHEBI:15378, ChEBI:CHEBI:33019, ChEBI:CHEBI:58189, ChEBI:CHEBI:156484, ChEBI:CHEBI:156503; EC=2.7.7.88; Evidence={ECO:0000250|UniProtKB:P28887}; CATALYTIC ACTIVITY: Reaction=a 5'-end (5'-triphosphoguanosine)-(2'-O-methyladenylyl)-adenylyl-cytidylyl-adenosine in mRNA + S-adenosyl-L-methionine = a 5'-end (N(7)-methyl 5'-triphosphoguanosine)-(2'-O-methyladenylyl)-adenylyl-cytidylyl-adenosine in mRNA + S-adenosyl-L-homocysteine; Xref=Rhea:RHEA:65440, Rhea:RHEA-COMP:16798, Rhea:RHEA-COMP:16801, ChEBI:CHEBI:57856, ChEBI:CHEBI:59789, ChEBI:CHEBI:156482, ChEBI:CHEBI:156483; Evidence={ECO:0000250|UniProtKB:P03523}; CATALYTIC ACTIVITY: Reaction=GTP + H2O = GDP + H(+) + phosphate; Xref=Rhea:RHEA:19669, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:37565, ChEBI:CHEBI:43474, ChEBI:CHEBI:58189; Evidence={ECO:0000250|UniProtKB:P28887}; | null | null | null | null | FUNCTION: RNA-directed RNA polymerase that catalyzes the transcription of viral mRNAs, their capping and polyadenylation. The template is composed of the viral RNA tightly encapsidated by the nucleoprotein (N). The viral polymerase binds to the genomic RNA at the 3' leader promoter, and transcribes subsequently all viral mRNAs with a decreasing efficiency. The first gene is the most transcribed, and the last the least transcribed. The viral phosphoprotein acts as a processivity factor. Capping is concommitant with initiation of mRNA transcription. Indeed, a GDP polyribonucleotidyl transferase (PRNTase) adds the cap structure when the nascent RNA chain length has reached few nucleotides. Ribose 2'-O methylation of viral mRNA cap precedes and facilitates subsequent guanine-N-7 methylation, both activities being carried by the viral polymerase. Polyadenylation of mRNAs occur by a stuttering mechanism at a slipery stop site present at the end viral genes. After finishing transcription of a mRNA, the polymerase can resume transcription of the downstream gene. {ECO:0000250|UniProtKB:P03523}.; FUNCTION: RNA-directed RNA polymerase that catalyzes the replication of viral genomic RNA. The template is composed of the viral RNA tightly encapsidated by the nucleoprotein (N). The replicase mode is dependent on intracellular N protein concentration. In this mode, the polymerase replicates the whole viral genome without recognizing transcriptional signals, and the replicated genome is not caped or polyadenylated. {ECO:0000250|UniProtKB:P03523}. | Rabies virus (strain India) (RABV) |
A3SI50 | DMDC_ROSNI | MTRYTAPTQDIQYLLHDVLDVANDPTPGYAELEPDFTSAVLEEAGKIAGEVLHPLNAVGDQEGCVLENGVVRPPKGFKEAFDQVREGGWTALDLPEQYGGQNMPYLLGTAVGEMFSGANQAFTMYQGLTHGAASAILVHGTDQQKDTYLPKMFSCDWTGTMNLTEPHCGTDLGLMRSKAVPQDDGSYAISGQKIFISAGEHDMAENIIHLVLAKIPGGPEGIKGVSLFIVPKFLVKEDGSLGERNGVKCSKIEEKMGIHGNSTCVMDYDGAKGWLLGEEHKGMRAMFTMMNEARIGVGMQGLAQAEVAYQNALDYARDRLQGRSVTGVENPDGPADPLIVHPDIRRNLLDQKSFIEGARAFLLWGAQMIDRAERGKDEAAHGMVSLLTPVIKGFLTDEGYDMTVQAQQVYGGHGYIEETGMSQFTRDARIAMIYEGANGVQALDLVGRKLAQDGGKHVMAFFDLVKGFIKEAGTDGAMAEFTEPLKSASKDLQSAGMFFMQNGMKNPNAALAGSYDFMHLFGHVCLGLMWGRMAEASLKALAEGRGDANFHETKLATARFYMTRRLPATKLHLARIESGADPVMALDADRF | 1.3.99.41 | COFACTOR: Name=FAD; Xref=ChEBI:CHEBI:57692; Evidence={ECO:0000269|PubMed:30677184}; | null | plasma membrane [GO:0005886] | flavin adenine dinucleotide binding [GO:0050660]; oxidoreductase activity, acting on the CH-CH group of donors [GO:0016627] | PF00441;PF12806;PF02770;PF02771; | 1.10.540.10;2.40.110.10;1.20.140.10; | Acyl-CoA dehydrogenase family | null | null | CATALYTIC ACTIVITY: Reaction=3-(methylsulfanyl)propanoyl-CoA + H(+) + oxidized [electron-transfer flavoprotein] = 3-(methylsulfanyl)acryloyl-CoA + reduced [electron-transfer flavoprotein]; Xref=Rhea:RHEA:52612, Rhea:RHEA-COMP:10685, Rhea:RHEA-COMP:10686, ChEBI:CHEBI:15378, ChEBI:CHEBI:57692, ChEBI:CHEBI:58307, ChEBI:CHEBI:82815, ChEBI:CHEBI:84994; EC=1.3.99.41; Evidence={ECO:0000269|PubMed:30677184}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:52613; Evidence={ECO:0000269|PubMed:30677184}; | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=1.4 mM for MMPA-CoA {ECO:0000269|PubMed:30677184}; KM=6.3 uM for FAD {ECO:0000269|PubMed:30677184}; | null | BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 9.0. {ECO:0000269|PubMed:30677184}; | BIOPHYSICOCHEMICAL PROPERTIES: Temperature dependence: Optimum temperature is 40 degrees Celsius. {ECO:0000269|PubMed:30677184}; | FUNCTION: Involved in the assimilation of dimethylsulphoniopropionate (DMSP), an important compound in the fixation of carbon in marine phytoplankton, by mediating the conversion of 3-(methylthio)propanoyl-CoA (MMPA-CoA) to 3-(methylthio)acryloyl-CoA (MTA-CoA). {ECO:0000269|PubMed:30677184}. | Roseovarius nubinhibens (strain ATCC BAA-591 / DSM 15170 / ISM) |
A4D0H5 | TRP5H_STRRG | MIRSVVIVGGGTAGWMTASYLKAAFDDRIDVTLVESGNVRRIGVGEATFSTVRHFFDYLGLDEREWLPRCAGGYKLGIRFENWSEPGEYFYHPFERLRVVDGFNMAEWWLAVGDRRTSFSEACYLTHRLCEAKRAPRMLDGSLFASQVDESLGRSTLAEQRAQFPYAYHFDADEVARYLSEYAIARGVRHVVDDVQHVGQDERGWISGVHTKQHGEISGDLFVDCTGFRGLLINQTLGGRFQSFSDVLPNNRAVALRVPRENDEDMRPYTTATAMSAGWMWTIPLFKRDGNGYVYSDEFISPEEAERELRSTVAPGRDDLEANHIQMRIGRNERTWINNCVAVGLSAAFVEPLESTGIFFIQHAIEQLVKHFPGERWDPVLISAYNERMAHMVDGVKEFLVLHYKGAQREDTPYWKAAKTRAMPDGLARKLELSASHLLDEQTIYPYYHGFETYSWITMNLGLGIVPERPRPALLHMDPAPALAEFERLRREGDELIAALPSCYEYLASIQ | 1.14.19.58 | null | antibiotic biosynthetic process [GO:0017000] | 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 = 5-chloro-L-tryptophan + FAD + 2 H2O; Xref=Rhea:RHEA:55896, ChEBI:CHEBI:15377, ChEBI:CHEBI:15379, ChEBI:CHEBI:17996, ChEBI:CHEBI:57692, ChEBI:CHEBI:57912, ChEBI:CHEBI:58307, ChEBI:CHEBI:139332; EC=1.14.19.58; Evidence={ECO:0000269|PubMed:15850981, ECO:0000269|PubMed:33465708}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:55897; Evidence={ECO:0000269|PubMed:15850981}; | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=0.15 mM for L-tryptophan {ECO:0000269|PubMed:15850981}; KM=0.109 mM for L-tryptophan {ECO:0000269|PubMed:19501593}; Note=kcat is 3.56 min(-1). {ECO:0000269|PubMed:19501593}; | PATHWAY: Antibiotic biosynthesis. {ECO:0000269|PubMed:15850981, ECO:0000305|PubMed:23062149}. | null | null | FUNCTION: Involved in the biosynthesis of the antibiotic compound pyrroindomycin B (PubMed:15850981). Catalyzes the chlorination of tryptophan (Trp) at C5 position to yield 5-chloro-L-tryptophan (PubMed:15850981, PubMed:33465708). It is also able to use bromide ions to generate monobrominated Trp, but the brominating activity is only about 75% of the chlorinating activity (PubMed:15850981). {ECO:0000269|PubMed:15850981, ECO:0000269|PubMed:33465708}. | Streptomyces rugosporus |
A4D0S4 | LAMB4_HUMAN | MQFQLTLFLHLGWLSYSKAQDDCNRGACHPTTGDLLVGRNTQLMASSTCGLSRAQKYCILSYLEGEQKCFICDSRFPYDPYDQPNSHTIENVIVSFEPDREKKWWQSENGLDHVSIRLDLEALFRFSHLILTFKTFRPAAMLVERSTDYGHNWKVFKYFAKDCATSFPNITSGQAQGVGDIVCDSKYSDIEPSTGGEVVLKVLDPSFEIENPYSPYIQDLVTLTNLRINFTKLHTLGDALLGRRQNDSLDKYYYALYEMIVRGSCFCNGHASECRPMQKMRGDVFSPPGMVHGQCVCQHNTDGPNCERCKDFFQDAPWRPAADLQDNACRSCSCNSHSSRCHFDMTTYLASGGLSGGVCEDCQHNTEGQHCDRCRPLFYRDPLKTISDPYACIPCECDPDGTISGGICVSHSDPALGSVAGQCLCKENVEGAKCDQCKPNHYGLSATDPLGCQPCDCNPLGSLPFLTCDVDTGQCLCLSYVTGAHCEECTVGYWGLGNHLHGCSPCDCDIGGAYSNVCSPKNGQCECRPHVTGRSCSEPAPGYFFAPLNFYLYEAEEATTLQGLAPLGSETFGQSPAVHVVLGEPVPGNPVTWTGPGFARVLPGAGLRFAVNNIPFPVDFTIAIHYETQSAADWTVQIVVNPPGGSEHCIPKTLQSKPQSFALPAATRIMLLPTPICLEPDVQYSIDVYFSQPLQGESHAHSHVLVDSLGLIPQINSLENFCSKQDLDEYQLHNCVEIASAMGPQVLPGACERLIISMSAKLHDGAVACKCHPQGSVGSSCSRLGGQCQCKPLVVGRCCDRCSTGSYDLGHHGCHPCHCHPQGSKDTVCDQVTGQCPCHGEVSGRRCDRCLAGYFGFPSCHPCPCNRFAELCDPETGSCFNCGGFTTGRNCERCIDGYYGNPSSGQPCRPCLCPDDPSSNQYFAHSCYQNLWSSDVICNCLQGYTGTQCGECSTGFYGNPRISGAPCQPCACNNNIDVTDPESCSRVTGECLRCLHNTQGANCQLCKPGHYGSALNQTCRRCSCHASGVSPMECPPGGGACLCDPVTGACPCLPNVTGLACDRCADGYWNLVPGRGCQSCDCDPRTSQSSHCDQLTGQCPCKLGYGGKRCSECQENYYGDPPGRCIPCDCNRAGTQKPICDPDTGMCRCREGVSGQRCDRCARGHSQEFPTCLQCHLCFDQWDHTISSLSKAVQGLMRLAANMEDKRETLPVCEADFKDLRGNVSEIERILKHPVFPSGKFLKVKDYHDSVRRQIMQLNEQLKAVYEFQDLKDTIERAKNEADLLLEDLQEEIDLQSSVLNASIADSSENIKKYYHISSSAEKKINETSSTINTSANTRNDLLTILDTLTSKGNLSLERLKQIKIPDIQILNEKVCGDPGNVPCVPLPCGGALCTGRKGHRKCRGPGCHGSLTLSTNALQKAQEAKSIIRNLDKQVRGLKNQIESISEQAEVSKNNALQLREKLGNIRNQSDSEEENINLFIKKVKNFLLEENVPPEDIEKVANGVLDIHLPIPSQNLTDELVKIQKHMQLCEDYRTDENRLNEEADGAQKLLVKAKAAEKAANILLNLDKTLNQLQQAQITQGRANSTITQLTANITKIKKNVLQAENQTREMKSELELAKQRSGLEDGLSLLQTKLQRHQDHAVNAKVQAESAQHQAGSLEKEFVELKKQYAILQRKTSTTGLTKETLGKVKQLKDAAEKLAGDTEAKIRRITDLERKIQDLNLSRQAKADQLRILEDQVVAIKNEIVEQEKKYARCYS | null | null | animal organ morphogenesis [GO:0009887]; substrate adhesion-dependent cell spreading [GO:0034446]; tissue development [GO:0009888] | basement membrane [GO:0005604]; extracellular region [GO:0005576] | null | PF00053;PF21199;PF00055; | 2.60.120.260;2.10.25.10;2.170.300.10; | null | null | SUBCELLULAR LOCATION: Secreted, extracellular space, extracellular matrix, basement membrane. | null | null | null | null | null | FUNCTION: Binding to cells via a high affinity receptor, laminin is thought to mediate the attachment, migration and organization of cells into tissues during embryonic development by interacting with other extracellular matrix components. | Homo sapiens (Human) |
A4D126 | ISPD_HUMAN | MEAGPPGSARPAEPGPCLSGQRGADHTASASLQSVAGTEPGRHPQAVAAVLPAGGCGERMGVPTPKQFCPILERPLISYTLQALERVCWIKDIVVAVTGENMEVMKSIIQKYQHKRISLVEAGVTRHRSIFNGLKALAEDQINSKLSKPEVVIIHDAVRPFVEEGVLLKVVTAAKEHGAAGAIRPLVSTVVSPSADGCLDYSLERARHRASEMPQAFLFDVIYEAYQQCSDYDLEFGTECLQLALKYCCTKAKLVEGSPDLWKVTYKRDLYAAESIIKERISQEICVVMDTEEDNKHVGHLLEEVLKSELNHVKVTSEALGHAGRHLQQIILDQCYNFVCVNVTTSDFQETQKLLSMLEESSLCILYPVVVVSVHFLDFKLVPPSQKMENLMQIREFAKEVKERNILLYGLLISYPQDDQKLQESLRQGAIIIASLIKERNSGLIGQLLIA | 2.7.7.40 | null | axon guidance [GO:0007411]; isoprenoid biosynthetic process [GO:0008299]; protein O-linked mannosylation [GO:0035269] | cytosol [GO:0005829] | cytidylyltransferase activity [GO:0070567]; D-ribitol-5-phosphate cytidylyltransferase activity [GO:0047349]; protein homodimerization activity [GO:0042803] | PF01128;PF18706; | null | IspD/TarI cytidylyltransferase family, IspD subfamily | null | SUBCELLULAR LOCATION: Cytoplasm, cytosol {ECO:0000269|PubMed:26687144}. | CATALYTIC ACTIVITY: Reaction=CTP + D-ribitol 5-phosphate + H(+) = CDP-L-ribitol + diphosphate; Xref=Rhea:RHEA:12456, ChEBI:CHEBI:15378, ChEBI:CHEBI:33019, ChEBI:CHEBI:37563, ChEBI:CHEBI:57608, ChEBI:CHEBI:57695; EC=2.7.7.40; Evidence={ECO:0000269|PubMed:26687144, ECO:0000269|PubMed:26923585, ECO:0000269|PubMed:27130732}; CATALYTIC ACTIVITY: Reaction=CTP + D-ribose 5-phosphate + H(+) = CDP-D-ribose + diphosphate; Xref=Rhea:RHEA:53872, ChEBI:CHEBI:15378, ChEBI:CHEBI:33019, ChEBI:CHEBI:37563, ChEBI:CHEBI:78346, ChEBI:CHEBI:137525; Evidence={ECO:0000269|PubMed:26687144, ECO:0000269|PubMed:27130732}; CATALYTIC ACTIVITY: Reaction=CTP + D-ribulose 5-phosphate + H(+) = CDP-D-ribulose + diphosphate; Xref=Rhea:RHEA:53612, ChEBI:CHEBI:15378, ChEBI:CHEBI:33019, ChEBI:CHEBI:37563, ChEBI:CHEBI:58121, ChEBI:CHEBI:137524; Evidence={ECO:0000269|PubMed:26687144}; | null | PATHWAY: Protein modification; protein glycosylation. {ECO:0000269|PubMed:26687144, ECO:0000269|PubMed:26923585, ECO:0000269|PubMed:27130732}. | null | null | FUNCTION: Cytidylyltransferase required for protein O-linked mannosylation (PubMed:22522420, PubMed:22522421, PubMed:26687144, PubMed:26923585, PubMed:27130732, PubMed:27601598). Catalyzes the formation of CDP-ribitol nucleotide sugar from D-ribitol 5-phosphate (PubMed:26687144, PubMed:26923585, PubMed:27130732). CDP-ribitol is a substrate of FKTN during the biosynthesis of the phosphorylated O-mannosyl trisaccharide (N-acetylgalactosamine-beta-3-N-acetylglucosamine-beta-4-(phosphate-6-)mannose), a carbohydrate structure present in alpha-dystroglycan (DAG1), which is required for binding laminin G-like domain-containing extracellular proteins with high affinity (PubMed:26687144, PubMed:26923585, PubMed:27130732). Shows activity toward other pentose phosphate sugars and mediates formation of CDP-ribulose or CDP-ribose using CTP and ribulose-5-phosphate or ribose-5-phosphate, respectively (PubMed:26687144). Not Involved in dolichol production (PubMed:26687144). {ECO:0000269|PubMed:22522420, ECO:0000269|PubMed:22522421, ECO:0000269|PubMed:26687144, ECO:0000269|PubMed:26923585, ECO:0000269|PubMed:27130732, ECO:0000269|PubMed:27601598}. | Homo sapiens (Human) |
A4D161 | F221A_HUMAN | MERLTLPLGGAAAVDEYLEYRRIVGEDDGGKLFTPEEYEEYKRKVLPLRLQNRLFVSWRSPTGMDCKLVGPETLCFCTHRYKQHKTDLEAIPQQCPIDLPCQVTGCQCRAYLYVPLNGSQPIRCRCKHFADQHSAAPGFTCNTCSKCSGFHSCFTCACGQPAYAHDTVVETKQERLAQEKPVGQDIPYAAMGGLTGFSSLAEGYMRLDDSGIGVPSVEFLESPITAVDSPFLKAFQASSSSSPETLTDVGTSSQVSSLRRPEEDDMAFFERRYQERMKMEKAAKWKGKAPLPSATKPS | null | null | null | null | null | PF14753; | null | FAM221 family | null | null | null | null | null | null | null | null | Homo sapiens (Human) |
A4D1B5 | GSAP_HUMAN | MALRLVADFDLGKDVLPWLRAQRAVSEASGAGSGGADVLENDYESLHVLNVERNGNIIYTYKDDKGNVVFGLYDCQTRQNELLYTFEKDLQVFSCSVNSERTLLAASLVQSTKEGKRNELQPGSKCLTLLVEIHPVNNVKVLKAVDSYIWVQFLYPHIESHPLPENHLLLISEEKYIEQFRIHVAQEDGNRVVIKNSGHLPRDRIAEDFVWAQWDMSEQRLYYIDLKKSRSILKCIQFYADESYNLMFEVPLDISLSNSGFKLVNFGCDYHQYRDKFSKHLTLCVFTNHTGSLCVCYSPKCASWGQITYSVFYIHKGHSKTFTTSLENVGSHMTKGITFLNLDYYVAVYLPGHFFHLLNVQHPDLICHNLFLTGNNEMIDMLPHCPLQSLSGSLVLDCCSGKLYRALLSQSSLLQLLQNTCLDCEKMAALHCALYCGQGAQFLEAQIIQWISENVSACHSFDLIQEFIIASSYWSVYSETSNMDKLLPHSSVLTWNTEIPGITLVTEDIALPLMKVLSFKGYWEKLNSNLEYVKYAKPHFHYNNSVVRREWHNLISEEKTGKRRSAAYVRNILDNAVKVISNLEARNLGPRLTPLLQEEDSHQRLLMGLMVSELKDHFLRHLQGVEKKKIEQMVLDYISKLLDLICHIVETNWRKHNLHSWVLHFNSRGSAAEFAVFHIMTRILEATNSLFLPLPPGFHTLHTILGVQCLPLHNLLHCIDSGVLLLTETAVIRLMKDLDNTEKNEKLKFSIIVRLPPLIGQKICRLWDHPMSSNIISRNHVTRLLQNYKKQPRNSMINKSSFSVEFLPLNYFIEILTDIESSNQALYPFEGHDNVDAEFVEEAALKHTAMLLGL | null | null | positive regulation of amyloid-beta formation [GO:1902004]; regulation of proteolysis [GO:0030162] | trans-Golgi network [GO:0005802] | amyloid-beta binding [GO:0001540] | PF14959; | null | GSAP family | PTM: The protein is first synthesized as a holoprotein form of 98 kDa and rapidly processed into the gamma-secretase-activating protein 16 kDa C-terminal form, which constitutes the predominant form. {ECO:0000269|PubMed:20811458}. | SUBCELLULAR LOCATION: Golgi apparatus, trans-Golgi network {ECO:0000269|PubMed:20811458}. | null | null | null | null | null | FUNCTION: Regulator of gamma-secretase activity, which specifically activates the production of amyloid-beta protein (amyloid-beta protein 40 and amyloid-beta protein 42), without affecting the cleavage of other gamma-secretase targets such has Notch. The gamma-secretase complex is an endoprotease complex that catalyzes the intramembrane cleavage of integral membrane proteins such as Notch receptors and APP (amyloid-beta precursor protein). Specifically promotes the gamma-cleavage of APP CTF-alpha (also named APP-CTF) by the gamma-secretase complex to generate amyloid-beta, while it reduces the epsilon-cleavage of APP CTF-alpha, leading to a low production of AICD. {ECO:0000269|PubMed:20811458}. | Homo sapiens (Human) |
A4D1E9 | GTPBA_HUMAN | MVHCSCVLFRKYGNFIDKLRLFTRGGSGGMGYPRLGGEGGKGGDVWVVAQNRMTLKQLKDRYPRKRFVAGVGANSKISALKGSKGKDCEIPVPVGISVTDENGKIIGELNKENDRILVAQGGLGGKLLTNFLPLKGQKRIIHLDLKLIADVGLVGFPNAGKSSLLSCVSHAKPAIADYAFTTLKPELGKIMYSDFKQISVADLPGLIEGAHMNKGMGHKFLKHIERTRQLLFVVDISGFQLSSHTQYRTAFETIILLTKELELYKEELQTKPALLAVNKMDLPDAQDKFHELMSQLQNPKDFLHLFEKNMIPERTVEFQHIIPISAVTGEGIEELKNCIRKSLDEQANQENDALHKKQLLNLWISDTMSSTEPPSKHAVTTSKMDII | null | null | ribosome biogenesis [GO:0042254] | chromosome [GO:0005694]; mitochondrion [GO:0005739]; nucleolus [GO:0005730] | GTP binding [GO:0005525]; GTPase activity [GO:0003924]; magnesium ion binding [GO:0000287]; RNA binding [GO:0003723] | PF01018;PF01926; | 2.70.210.12;3.40.50.300; | TRAFAC class OBG-HflX-like GTPase superfamily, OBG GTPase family | null | SUBCELLULAR LOCATION: Nucleus, nucleolus {ECO:0000269|PubMed:17054726}. Chromosome {ECO:0000269|PubMed:17054726}. Note=Found in the dense fibrillar compartment region of the nucleolus. At the onset of mitosis moves to the chromosome surface and remains there until anaphase. Gradually re-assembles into the nucleolus at late anaphase to telophase. | null | null | null | null | null | FUNCTION: May be involved in the ribosome maturation process. Complements an ObgE(CgtA) function in E.coli ribosome maturation. Plays a role of GTPase in vitro. When missing, disorganization of the nucleolar architecture is observed. {ECO:0000269|PubMed:17054726}. | Homo sapiens (Human) |
A4D1P6 | WDR91_HUMAN | MAEAVERTDELVREYLLFRGFTHTLRQLDAEIKADKEKGFRVDKIVDQLQQLMQVYDLAALRDYWSYLERRLFSRLEDIYRPTIHKLKTSLFRFYLVYTIQTNRNDKAQEFFAKQATELQNQAEWKDWFVLPFLPSPDTNPTFATYFSRQWADTFIVSLHNFLSVLFQCMPVPVILNFDAECQRTNQVQEENEVLRQKLFALQAEIHRLKKEEQQPEEEEALVQHKLPPYVSNMDRLGDSELAMVCSQRNASLSQSPRVGFLSSLLPQSKKSPSRLSPAQGPPQPQSSAKKESFGGQGTKGKDPTSGAKDGKSLLSGLATGESGWSQHRQRRLQDHGKERKELFSTTTSQCAEKKPEASGPEAEPCPELHTEPVEPLTRASSAGPEGGGVRPEQPFIVLGQEEYGEHHSSIMHCRVDCSGRRVASLDVDGVIKVWSFNPIMQTKASSISKSPLLSLEWATKRDRLLLLGSGVGTVRLYDTEAKKNLCEININDNMPRILSLACSPNGASFVCSAAAPSLTSQVDFSAPDIGSKGMNQVPGRLLLWDTKTMKQQLQFSLDPEPIAINCTAFNHNGNLLVTGAADGVIRLFDMQQHECAMSWRAHYGEVYSVEFSYDENTVYSIGEDGKFIQWNIHKSGLKVSEYSLPSDATGPFVLSGYSGYKQVQVPRGRLFAFDSEGNYMLTCSATGGVIYKLGGDEKVLESCLSLGGHRAPVVTVDWSTAMDCGTCLTASMDGKIKLTTLLAHKA | null | null | early endosome to late endosome transport [GO:0045022]; negative regulation of phosphatidylinositol 3-kinase/protein kinase B signal transduction [GO:0051898]; regulation of protein catabolic process [GO:0042176] | cytosol [GO:0005829]; early endosome membrane [GO:0031901]; endosome membrane [GO:0010008]; extrinsic component of endosome membrane [GO:0031313]; late endosome membrane [GO:0031902] | phosphatidylinositol 3-kinase inhibitor activity [GO:0141039]; phosphatidylinositol 3-kinase regulator activity [GO:0035014] | PF12894;PF00400; | 2.130.10.10; | WD repeat WDR91 family | null | SUBCELLULAR LOCATION: Early endosome membrane {ECO:0000269|PubMed:26783301}; Peripheral membrane protein {ECO:0000269|PubMed:26783301}. Late endosome membrane {ECO:0000269|PubMed:26783301, ECO:0000269|PubMed:28404643}. | null | null | null | null | null | FUNCTION: Functions as a negative regulator of the PI3 kinase/PI3K activity associated with endosomal membranes via BECN1, a core subunit of the PI3K complex. By modifying the phosphatidylinositol 3-phosphate/PtdInsP3 content of endosomal membranes may regulate endosome fusion, recycling, sorting and early to late endosome transport (PubMed:26783301). It is for instance, required for the delivery of cargos like BST2/tetherin from early to late endosome and thereby participates indirectly to their degradation by the lysosome (PubMed:27126989). May play a role in meiosis (By similarity). {ECO:0000250|UniProtKB:Q7TMQ7, ECO:0000269|PubMed:26783301, ECO:0000269|PubMed:27126989}. | Homo sapiens (Human) |
A4D1T9 | PRS37_HUMAN | MKYVFYLGVLAGTFFFADSSVQKEDPAPYLVYLKSHFNPCVGVLIKPSWVLAPAHCYLPNLKVMLGNFKSRVRDGTEQTINPIQIVRYWNYSHSAPQDDLMLIKLAKPAMLNPKVQPLTLATTNVRPGTVCLLSGLDWSQENSGRHPDLRQNLEAPVMSDRECQKTEQGKSHRNSLCVKFVKVFSRIFGEVAVATVICKDKLQGIEVGHFMGGDVGIYTNVYKYVSWIENTAKDK | null | null | binding of sperm to zona pellucida [GO:0007339]; cell migration [GO:0016477]; germ cell migration [GO:0008354]; positive regulation of acrosome reaction [GO:2000344]; positive regulation of fertilization [GO:1905516]; protein maturation [GO:0051604]; proteolysis [GO:0006508]; regulation of protein processing [GO:0070613] | acrosomal vesicle [GO:0001669]; extracellular region [GO:0005576]; nucleus [GO:0005634] | serine-type endopeptidase activity [GO:0004252] | PF00089; | 2.40.10.10; | Peptidase S1 family | null | SUBCELLULAR LOCATION: Cytoplasmic vesicle, secretory vesicle, acrosome {ECO:0000269|PubMed:27649891}. Secreted {ECO:0000305}. | null | null | null | null | null | FUNCTION: Plays a role in male fertility (By similarity). May have a role in sperm migration or binding to zona-intact eggs (By similarity). Involved in the activation of the proacrosin/acrosin system (PubMed:27649891). {ECO:0000250|UniProtKB:Q9DAA4, ECO:0000269|PubMed:27649891}. | Homo sapiens (Human) |
A4D256 | CC14C_HUMAN | MRSSTLQDPRRRDPQDDVYVDITDRLRFAILYSRPKSASNVHYFSIDNELEYENFSEDFGPLNLAMVYRYCCKINKKLKSITMLRKKIVHFTGSDQRKQANAAFLVGCYMVIYLGRTPEAAYRILIFGDTPYIPFRDAAYGSCNFYITLLDCFHAVKKAMQYGFLNFNSFNLDEYEHYEKAENGDLNWIIPDRFIAFCGPHSRARLESGYHQHSPETYIQYFKNHNVTTIIRLNKRMYDAKRFTDAGFDHHDLFFADGSTPTDAIVKRFLDICENAEGAIAVHCKAGLGRTGTLIACYIMKHYRMTAAETIAWVRICRPGLVIGPQQQFLVMKQTSLWLEGDYFRQRLKGQENGQHRAAFSKLLSGVDDISINGVENQDQQEPKPYSDDDEINGVTQGDRSRALKRRRQSKTNDILLPSPLAVLTFTLCSVVIWWIVCDYILPILLF | 3.1.3.16; 3.1.3.48 | null | cilium assembly [GO:0060271]; dephosphorylation [GO:0016311]; microtubule cytoskeleton organization [GO:0000226]; positive regulation of cytokinesis [GO:0032467]; regulation of exit from mitosis [GO:0007096] | centrosome [GO:0005813]; cytoplasm [GO:0005737]; endoplasmic reticulum membrane [GO:0005789]; mitotic spindle [GO:0072686]; nucleolus [GO:0005730]; spindle pole [GO:0000922] | myosin phosphatase activity [GO:0017018]; protein serine/threonine phosphatase activity [GO:0004722]; protein tyrosine phosphatase activity [GO:0004725]; protein tyrosine/serine/threonine phosphatase activity [GO:0008138] | PF00782;PF14671; | 3.90.190.10; | Protein-tyrosine phosphatase family, Non-receptor class CDC14 subfamily | null | SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000269|PubMed:18547142}; Single-pass membrane protein {ECO:0000255}. Note=Retains its endoplasmic reticulum localization during mitosis. {ECO:0000269|PubMed:18547142}. | CATALYTIC ACTIVITY: Reaction=H2O + O-phospho-L-tyrosyl-[protein] = L-tyrosyl-[protein] + phosphate; Xref=Rhea:RHEA:10684, Rhea:RHEA-COMP:10136, Rhea:RHEA-COMP:10137, ChEBI:CHEBI:15377, ChEBI:CHEBI:43474, ChEBI:CHEBI:46858, ChEBI:CHEBI:82620; EC=3.1.3.48; Evidence={ECO:0000255|PROSITE-ProRule:PRU10044}; CATALYTIC ACTIVITY: Reaction=H2O + O-phospho-L-seryl-[protein] = L-seryl-[protein] + phosphate; Xref=Rhea:RHEA:20629, Rhea:RHEA-COMP:9863, Rhea:RHEA-COMP:11604, ChEBI:CHEBI:15377, ChEBI:CHEBI:29999, ChEBI:CHEBI:43474, ChEBI:CHEBI:83421; EC=3.1.3.16; CATALYTIC ACTIVITY: Reaction=H2O + O-phospho-L-threonyl-[protein] = L-threonyl-[protein] + phosphate; Xref=Rhea:RHEA:47004, Rhea:RHEA-COMP:11060, Rhea:RHEA-COMP:11605, ChEBI:CHEBI:15377, ChEBI:CHEBI:30013, ChEBI:CHEBI:43474, ChEBI:CHEBI:61977; EC=3.1.3.16; | null | null | null | null | FUNCTION: Dual-specificity phosphatase. Preferentially dephosphorylates proteins modified by proline-directed kinases (By similarity). {ECO:0000250}. | Homo sapiens (Human) |
A4D2B0 | MBLC1_HUMAN | MRTEPLCGASPLLVPGDPYSVVVLLQGYAEPEGVGDAVRADGSVTLVLPQTRGPASSHRESPRGSGGAEAALEEAARGPILVDTGGPWAREALLGALAGQGVAPGDVTLVVGTHGHSDHIGNLGLFPGAALLVSHDFCLPGGRYLPHGLGEGQPLRLGPGLEVWATPGHGGQRDVSVVVAGTALGTVVVAGDVFERDGDEDSWQALSEDPAAQERSRKRVLVVADVVVPGHGPPFRVLREASQPETEGGGNSQQEPVVGDEEPALH | 3.1.27.- | COFACTOR: Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000269|PubMed:30507380}; Note=Binds 2 Zn(2+) ions per subunit. {ECO:0000305|PubMed:30507380}; | histone mRNA metabolic process [GO:0008334]; mRNA 3'-end processing [GO:0031124]; positive regulation of G1/S transition of mitotic cell cycle [GO:1900087] | cytoplasm [GO:0005737]; cytosol [GO:0005829]; nucleus [GO:0005634] | metal ion binding [GO:0046872]; RNA endonuclease activity [GO:0004521] | PF00753; | 3.60.15.10; | Metallo-beta-lactamase superfamily, Glyoxalase II family | null | SUBCELLULAR LOCATION: Cytoplasm, cytosol {ECO:0000269|PubMed:30507380}. Nucleus {ECO:0000269|PubMed:30507380}. Note=Localizes in the nucleus during early S-phase of the cell cycle. {ECO:0000269|PubMed:30507380}. | CATALYTIC ACTIVITY: Reaction=a ribonucleotidyl-ribonucleotide-RNA + H2O = a 3'-end ribonucleotide-RNA + a 5'-end 5'-phospho-ribonucleoside-RNA + H(+); Xref=Rhea:RHEA:68096, Rhea:RHEA-COMP:15179, Rhea:RHEA-COMP:17355, Rhea:RHEA-COMP:17428, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:74896, ChEBI:CHEBI:138282, ChEBI:CHEBI:173118; Evidence={ECO:0000269|PubMed:30507380}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:68097; Evidence={ECO:0000305|PubMed:30507380}; | null | null | null | null | FUNCTION: Endoribonuclease that catalyzes the hydrolysis of histone-coding pre-mRNA 3'-end. Involved in histone pre-mRNA processing during the S-phase of the cell cycle, which is required for entering/progressing through S-phase (PubMed:30507380). Cleaves histone pre-mRNA at a major and a minor cleavage site after the 5'-ACCCA-3' and the 5'-ACCCACA-3' sequence, respectively, and located downstream of the stem-loop (PubMed:30507380). May require the presence of the HDE element located at the histone pre-RNA 3'-end to avoid non-specific cleavage (PubMed:30507380). {ECO:0000269|PubMed:30507380}. | Homo sapiens (Human) |
A4D2B8 | PM2P1_HUMAN | MVTMCGGHRPENFLHQVLTEFGEELAGEGKSEVGGGAPRSYLQVASAECWAAAPAVHVGEPVHAGGLHTERGADPVIGLYLVHRGGACQTPTVGNRQTPTLGIHARPRRRATTSLLTLLLAFGKNAVRCALIGPGSLTSRTRPLTEPLGEKERREVFFPPRPERVEHNVESSRWEPRRRGACGSRGGNFPSPRGGSGVASLERAESSSTEPAKAIKPIDRKSVHQICSGPVVPSLSTAVKELVENSLDAGATNIDLKLKDYGVDLIEVSGNGCGVEEENFEGLTLKHHTSKIQEFADLPQVETFGFRGEALSSLCALSDVTISTCHVSAKVGTRLVFDHYGKIIQKTPYPHPRGMTVSVKQLFSTLPVHHKEFQRNIKKKRACFPFAFCRDCQFPEASPAMLPVQPAELTPRSTPPHPCSLEDNVITVFSSVKNGPGSSR | null | null | mismatch repair [GO:0006298]; phosphorylation [GO:0016310]; somatic hypermutation of immunoglobulin genes [GO:0016446] | MutLalpha complex [GO:0032389] | ATP hydrolysis activity [GO:0016887]; ATP-dependent DNA damage sensor activity [GO:0140664]; kinase activity [GO:0016301] | PF13589; | 3.30.565.10; | DNA mismatch repair MutL/HexB family | null | null | null | null | null | null | null | null | Homo sapiens (Human) |
A4ECA9 | HSDHB_COLAA | MNLREKYGEWGLILGATEGVGKAFCEKIAAGGMNVVMVGRREEKLNVLAGEIRETYGVETKVVRADFSQPGAAETVFAATEGLDMGFMSYVACLHSFGKIQDTPWEKHEAMINVNVVTFLKCFHHYMRIFAAQDRGAVINVSSMTGISSSPWNGQYGAGKAFILKMTEAVACECEGTGVDVEVITLGTTLTPSLLSNLPGGPQGEAVMKIALTPEECVDEAFEKLGKELSVIAGQRNKDSVHDWKANHTEDEYIRYMGSFYRD | 1.1.1.201 | null | bile acid catabolic process [GO:0030573]; lipid catabolic process [GO:0016042] | null | 7-beta-hydroxysteroid dehydrogenase (NADP+) activity [GO:0047022]; ketoreductase activity [GO:0045703]; nucleotide binding [GO:0000166] | PF00106; | 3.40.50.720; | Short-chain dehydrogenases/reductases (SDR) family | null | null | CATALYTIC ACTIVITY: Reaction=a 7beta-hydroxysteroid + NADP(+) = a 7-oxosteroid + H(+) + NADPH; Xref=Rhea:RHEA:20233, ChEBI:CHEBI:15378, ChEBI:CHEBI:35349, ChEBI:CHEBI:47789, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349; EC=1.1.1.201; Evidence={ECO:0000269|PubMed:21181147, ECO:0000269|PubMed:27006087, ECO:0000269|PubMed:6954878}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:20234; Evidence={ECO:0000269|PubMed:21181147}; PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:20235; Evidence={ECO:0000269|PubMed:21181147}; CATALYTIC ACTIVITY: Reaction=7-oxolithocholate + H(+) + NADPH = NADP(+) + ursodeoxycholate; Xref=Rhea:RHEA:47540, ChEBI:CHEBI:15378, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349, ChEBI:CHEBI:78604, ChEBI:CHEBI:78605; Evidence={ECO:0000269|PubMed:21181147, ECO:0000269|PubMed:27006087, ECO:0000269|PubMed:6954878}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:47541; Evidence={ECO:0000269|PubMed:21181147}; PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:47542; Evidence={ECO:0000269|PubMed:21181147}; CATALYTIC ACTIVITY: Reaction=7beta-hydroxy-3,12-dioxo-5beta-cholan-24-oate + NADP(+) = dehydrocholate + H(+) + NADPH; Xref=Rhea:RHEA:53860, ChEBI:CHEBI:15378, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349, ChEBI:CHEBI:137881, ChEBI:CHEBI:137882; Evidence={ECO:0000269|PubMed:21181147}; CATALYTIC ACTIVITY: Reaction=NADP(+) + ursocholate = 3alpha,12alpha-dihydroxy-7-oxo-5beta-cholanate + H(+) + NADPH; Xref=Rhea:RHEA:53856, ChEBI:CHEBI:11893, ChEBI:CHEBI:15378, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349, ChEBI:CHEBI:137880; Evidence={ECO:0000269|PubMed:27006087}; | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=5.32 uM for NADP(+) {ECO:0000269|PubMed:21181147}; KM=4.5 uM for NADPH {ECO:0000269|PubMed:21181147}; KM=6.23 uM for ursodeoxycholate {ECO:0000269|PubMed:21181147}; KM=5.2 uM for 7-oxolithocholate {ECO:0000269|PubMed:21181147}; KM=9.23 uM for dehydrocholate {ECO:0000269|PubMed:21181147}; KM=0.108 mM for ursodeoxycholate {ECO:0000269|PubMed:6954878}; KM=0.909 mM for glycoursodeoxycholate {ECO:0000269|PubMed:6954878}; KM=1.639 mM for tauroursodeoxycholate {ECO:0000269|PubMed:6954878}; KM=0.4 mM for NADP(+) {ECO:0000269|PubMed:6954878}; Vmax=38.17 umol/min/mg enzyme for the oxidation of ursodeoxycholate {ECO:0000269|PubMed:21181147}; Vmax=30.77 umol/min/mg enzyme for the reduction of 7-oxolithocholate {ECO:0000269|PubMed:21181147}; Vmax=28.33 umol/min/mg enzyme for the reduction of dehydrocholate {ECO:0000269|PubMed:21181147}; Vmax=0.2 umol/min/mg enzyme for the oxidation of ursodeoxycholate {ECO:0000269|PubMed:6954878}; Vmax=0.25 umol/min/mg enzyme for the oxidation of glycoursodeoxycholate {ECO:0000269|PubMed:6954878}; Vmax=0.24 umol/min/mg enzyme for the oxidation of tauroursodeoxycholate {ECO:0000269|PubMed:6954878}; Note=kcat is 1179 min(-1) for the oxidation of ursodeoxycholate. kcat is 951 min(-1) for the reduction of 7-oxolithocholate. kcat is 875 min(-1) for the reduction of dehydrocholate. {ECO:0000269|PubMed:21181147}; | null | BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 9-10 for the oxidation of ursodeoxycholate. Optimum pH is 4-6 for the reduction of 7-oxo-LCA and dehydrocholate. {ECO:0000269|PubMed:21181147}; | BIOPHYSICOCHEMICAL PROPERTIES: Temperature dependence: Is not very thermostable. The enzyme is completely inactivated at 50 degrees Celsius within 5 minutes and at 40 degrees Celsius within 400 minutes. {ECO:0000269|PubMed:21181147}; | FUNCTION: 7beta-hydroxysteroid dehydrogenase that catalyzes the reduction of the 7-oxo group of 7-oxo-lithocholate (7-oxo-LCA), to yield ursodeoxycholate (UDCA) (PubMed:21181147, PubMed:27006087, PubMed:6954878). As C.aerofaciens is an intestinal bacterium, this enzyme probably contributes to the formation of UDCA in the human colon. UDCA is regarded as a chemopreventive beneficial secondary bile acid due to its low hydrophobicity; it protects hepatocytes and bile duct epithelial cells against necrosis and apoptosis induced by more hydrophobic secondary bile acids like deoxycholate (DCA) (Probable). This enzyme is also able to catalyze the reverse reaction, i.e. the oxidation of the 7beta-hydroxy group of UDCA to 7-oxo-LCA (PubMed:21181147, PubMed:6954878). To a lesser extent, is also active on the taurine- and glycine-conjugates of ursodeoxycholate. It is specific for NADPH/NADP(+) as the electron acceptor/donor since it is not active with NADH/NAD(+) (PubMed:6954878). In the presence of NADPH, 7beta-HSDH can also reduce dehydrocholate (PubMed:21181147). And is also able to oxidize ursocholate (PubMed:27006087). {ECO:0000269|PubMed:21181147, ECO:0000269|PubMed:27006087, ECO:0000269|PubMed:6954878, ECO:0000305}. | Collinsella aerofaciens (strain ATCC 25986 / DSM 3979 / JCM 10188 / KCTC 3647 / NCTC 11838 / VPI 1003) |
A4F2N8 | LTHAD_PSESP | MQLSSYHDVIKAAERLEGFANRTPVFTSRTLDAETGAQVFIKCENLQRTGSFKFRGAFNALSRFDEAQRKAGVVAFSSGNHAQGIALAARLLQMPATIVMPTDAPAAKVAATREYGATVVFYDRITEDREQIGRTLAEQHGMTLIPSYDHPDVLAGQGTAAKELLEFTGPLDALFVGLGGGGMLSGTALATRALSPDCLLYGVEPEAGNDGQRSFQTGSIVHIDTPATIADGAQTQHLGNHTFPIIRENVNDILTVSDAELVESMRFFMQRMKMVVEPTGCLGLAALRNLKQQFRGQRVGIIVTGGNVDIEKYASLLKG | 4.3.1.16 | COFACTOR: Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326; Evidence={ECO:0000269|PubMed:10481099, ECO:0000269|PubMed:19193709}; COFACTOR: Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000269|PubMed:10481099, ECO:0000269|PubMed:19193709}; Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000269|PubMed:10481099, ECO:0000269|PubMed:19193709}; Name=Ca(2+); Xref=ChEBI:CHEBI:29108; Evidence={ECO:0000269|PubMed:10481099, ECO:0000269|PubMed:19193709}; Note=Requires a divalent metal cation such as Mn(2+), Mg(2+), or Ca(2+). {ECO:0000269|PubMed:10481099, ECO:0000269|PubMed:19193709}; | cellular modified amino acid catabolic process [GO:0042219]; D-serine biosynthetic process [GO:0070179] | cytoplasm [GO:0005737] | ATP binding [GO:0005524]; D-serine ammonia-lyase activity [GO:0008721]; L-serine ammonia-lyase activity [GO:0003941]; magnesium ion binding [GO:0000287]; pyridoxal phosphate binding [GO:0030170]; serine racemase activity [GO:0030378]; threo-3-hydroxyaspartate ammonia-lyase activity [GO:0030848]; threonine racemase activity [GO:0018114] | PF00291; | 3.40.50.1100; | Serine/threonine dehydratase family | null | null | CATALYTIC ACTIVITY: Reaction=(3S)-3-hydroxy-L-aspartate = NH4(+) + oxaloacetate; Xref=Rhea:RHEA:12424, ChEBI:CHEBI:16452, ChEBI:CHEBI:28938, ChEBI:CHEBI:57251; EC=4.3.1.16; Evidence={ECO:0000269|PubMed:10481099, ECO:0000269|PubMed:19193709}; | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=0.54 mM for L-threo-3-hydroxyaspartate {ECO:0000269|PubMed:19193709}; KM=0.74 mM for L-threo-3-hydroxyaspartate {ECO:0000269|PubMed:10481099}; Vmax=39 umol/min/mg enzyme {ECO:0000269|PubMed:19193709}; Vmax=37.5 umol/min/mg enzyme {ECO:0000269|PubMed:10481099}; | null | BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 9.0. {ECO:0000269|PubMed:19193709}; | BIOPHYSICOCHEMICAL PROPERTIES: Temperature dependence: Optimum temperature is 35 degrees Celsius. {ECO:0000269|PubMed:19193709}; | FUNCTION: Catalyzes the deamination of L-threo-3-hydroxyaspartate to oxaloacetate and ammonia. Shows a high specificity towards L-threo-3-hydroxyaspartate as other 3-hydroxyaminoacids, i.e. D,L-erythro- and D-threo-3-hydroxyaspartate, D-threonine, L-threonine, D,L-allothreonine, D,L-threo-3-phenylserine, D-serine, and L-serine, are not substrates for this enzyme (PubMed:10481099, PubMed:19193709). Exhibits no detectable serine and aspartate racemase activity (PubMed:19193709). Might play a role in the detoxification of naturally occurring 3-hydroxyaspartate in Pseudomonas sp. T62 cells (PubMed:19193709). {ECO:0000269|PubMed:10481099, ECO:0000269|PubMed:19193709}. | Pseudomonas sp |
A4F4L0 | TYOBP_PANTR | MGGLEPCSRLLLLPLLLAVGGLRPVQAQAQSDCSCSTVSPGVLAGIVMGDLVLTVLIALAVYFLGRLVHRGRGAAEAATRKQRITETESPYQELQGQRSDVYSDLNMQRPYYK | null | null | apoptotic cell clearance [GO:0043277]; microglial cell activation involved in immune response [GO:0002282]; negative regulation of B cell proliferation [GO:0030889]; negative regulation of transforming growth factor beta1 production [GO:0032911]; neutrophil activation involved in immune response [GO:0002283]; positive regulation of macrophage fusion [GO:0034241]; positive regulation of microglial cell mediated cytotoxicity [GO:1904151]; positive regulation of natural killer cell activation [GO:0032816]; stimulatory C-type lectin receptor signaling pathway [GO:0002223]; stimulatory killer cell immunoglobulin-like receptor signaling pathway [GO:0002222] | cell surface [GO:0009986]; plasma membrane [GO:0005886] | metal ion binding [GO:0046872]; protein homodimerization activity [GO:0042803]; signaling receptor binding [GO:0005102] | null | 1.10.287.770; | TYROBP family | PTM: Following ligand binding by associated receptors, tyrosine phosphorylated in the ITAM domain which leads to activation of additional tyrosine kinases and subsequent cell activation. {ECO:0000250|UniProtKB:O43914}. | SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:O43914}; Single-pass type I membrane protein {ECO:0000255}. | null | null | null | null | null | FUNCTION: Adapter protein which non-covalently associates with activating receptors found on the surface of a variety of immune cells to mediate signaling and cell activation following ligand binding by the receptors (By similarity). TYROBP is tyrosine-phosphorylated in the ITAM domain following ligand binding by the associated receptors which leads to activation of additional tyrosine kinases and subsequent cell activation (By similarity). Also has an inhibitory role in some cells (By similarity). Non-covalently associates with activating receptors of the CD300 family to mediate cell activation (By similarity). Also mediates cell activation through association with activating receptors of the CD200R family (By similarity). Required for neutrophil activation mediated by integrin (By similarity). Required for the activation of myeloid cells mediated by the CLEC5A/MDL1 receptor (By similarity). Associates with natural killer (NK) cell receptors such as the KLRD1/KLRC2 heterodimer to mediate NK cell activation (By similarity). Associates with TREM1 to mediate activation of neutrophils and monocytes (By similarity). Associates with TREM2 on monocyte-derived dendritic cells to mediate up-regulation of chemokine receptor CCR7 and dendritic cell maturation and survival (By similarity). Association with TREM2 mediates cytokine-induced formation of multinucleated giant cells which are formed by the fusion of macrophages (By similarity). Stabilizes the TREM2 C-terminal fragment (TREM2-CTF) produced by TREM2 ectodomain shedding which suppresses the release of pro-inflammatory cytokines (By similarity). In microglia, required with TREM2 for phagocytosis of apoptotic neurons (By similarity). Required with ITGAM/CD11B in microglia to control production of microglial superoxide ions which promote the neuronal apoptosis that occurs during brain development (By similarity). Promotes pro-inflammatory responses in microglia following nerve injury which accelerates degeneration of injured neurons (By similarity). Positively regulates the expression of the IRAK3/IRAK-M kinase and IL10 production by liver dendritic cells and inhibits their T cell allosimulatory ability (By similarity). Negatively regulates B cell proliferation (By similarity). Required for CSF1-mediated osteoclast cytoskeletal organization (By similarity). Positively regulates multinucleation during osteoclast development (By similarity). {ECO:0000250|UniProtKB:O43914, ECO:0000250|UniProtKB:O54885}. | Pan troglodytes (Chimpanzee) |
A4FV08 | GNPI1_BOVIN | MKLIILDHYSQASEWAAKYIRNRIIQFNPGPDKYFTLGLPTGSTPLGCYKKLIEYYKNGDLSFKYVKTFNMDEYVGLPRDHPESYHSFMWNNFFKHIDIHPENTHILDGNAADLQAECDAFEEKIKAAGGIELFVGGIGPDGHIAFNEPGSSLVSRTRVKTLAMDTILANARFFDGDLAKVPTMALTVGVGTVMDAREVMILITGAHKAFALYKAIEEGVNHMWTVSAFQQHPRTVFVCDEDATLELKVKTVKYFKGLMLVHNKLVDPLYSIKEKEIEKSQSSKKPYSD | 3.5.99.6 | null | carbohydrate metabolic process [GO:0005975]; glucosamine catabolic process [GO:0006043]; N-acetylglucosamine catabolic process [GO:0006046]; N-acetylneuraminate catabolic process [GO:0019262]; UDP-N-acetylglucosamine biosynthetic process [GO:0006048] | cytoplasm [GO:0005737] | glucosamine-6-phosphate deaminase activity [GO:0004342]; identical protein binding [GO:0042802]; isomerase activity [GO:0016853] | PF01182; | 3.40.50.1360; | Glucosamine/galactosamine-6-phosphate isomerase family | null | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. | CATALYTIC ACTIVITY: Reaction=alpha-D-glucosamine 6-phosphate + H2O = beta-D-fructose 6-phosphate + NH4(+); Xref=Rhea:RHEA:12172, ChEBI:CHEBI:15377, ChEBI:CHEBI:28938, ChEBI:CHEBI:57634, ChEBI:CHEBI:75989; EC=3.5.99.6; Evidence={ECO:0000269|PubMed:9774701}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:12173; Evidence={ECO:0000305|PubMed:9774701}; PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:12174; Evidence={ECO:0000305|PubMed:9774701}; | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=0.65 mM for alpha-D-glucosamine 6-phosphate (in the absence of GlcNAc6P); KM=5.9 mM for beta-D-fructose 6-phosphate (in the presence of GlcNAc6P) {ECO:0000269|PubMed:9774701}; KM=3.7 mM for NH4(+) (in the presence of GlcNAc6P) {ECO:0000269|PubMed:9774701}; Note=kcat is 61.6 sec(-1) for conversion of alpha-D-glucosamine 6-phosphate into beta-D-fructose 6-phosphate (in the presence of GlcNAc6P). kcat is 0.37 sec(-1) for conversion of alpha-D-glucosamine 6-phosphate into beta-D-fructose 6-phosphate (in the absence of GlcNAc6P). kcat is 5.8 sec(-1) for conversion of beta-D-fructose 6-phosphate into alpha-D-glucosamine 6-phosphate (in the presence of GlcNAc6P).; | PATHWAY: Nucleotide-sugar biosynthesis; UDP-N-acetyl-alpha-D-glucosamine biosynthesis; alpha-D-glucosamine 6-phosphate from D-fructose 6-phosphate: step 1/1. {ECO:0000250|UniProtKB:P46926}. | null | null | FUNCTION: Catalyzes the reversible conversion of alpha-D-glucosamine 6-phosphate (GlcN-6P) into beta-D-fructose 6-phosphate (Fru-6P) and ammonium ion, a regulatory reaction step in de novo uridine diphosphate-N-acetyl-alpha-D-glucosamine (UDP-GlcNAc) biosynthesis via hexosamine pathway. Deamination is coupled to aldo-keto isomerization mediating the metabolic flux from UDP-GlcNAc toward Fru-6P. At high ammonium level can drive amination and isomerization of Fru-6P toward hexosamines and UDP-GlcNAc synthesis (PubMed:9774701). Has a role in fine tuning the metabolic fluctuations of cytosolic UDP-GlcNAc and their effects on hyaluronan synthesis that occur during tissue remodeling (By similarity). Seems to trigger calcium oscillations in mammalian eggs. These oscillations serve as the essential trigger for egg activation and early development of the embryo (By similarity). {ECO:0000250|UniProtKB:P46926, ECO:0000250|UniProtKB:Q64422, ECO:0000269|PubMed:9774701}. | Bos taurus (Bovine) |
A4FV52 | VGLU1_BOVIN | MEFRQEEFRKLAGRALGKLHRLLEKRQEGAETLELSADGRPVTTQTRDPPVVDCTCFGLPRRYIIAIMSGLGFCISFGIRCNLGVAIVSMVNNSTTHRGGHVVMQKAQFNWDPETVGLIHGSFFWGYIVTQIPGGFICQKFAANRVFGFAIVATSTLNMLIPSAARVHYGCVIFVRILQGLVEGVTYPACHGIWSKWAPPLERSRLATTAFCGSYAGAVVAMPLAGVLVQYSGWSSVFYVYGSFGIFWYLFWLLVSYESPALHPSISEEERKYIEDAIGESAKLMNPVTKFNTPWRRFFTSMPVYAIIVANFCRSWTFYLLLISQPAYFEEVFGFEISKVGLVSALPHLVMTIIVPIGGQIADFLRSRRIMSTTNVRKLMNCGGFGMEATLLLVVGYSHSKGVAISFLVLAVGFSGFAISGFNVNHLDIAPRYASILMGISNGVGTLSGMVCPIIVGAMTKHKTREEWQYVFLIASLVHYGGVIFYGVFASGEKQPWAEPEEMSEEKCGFVGHDQLAGSDESEMEDEAEPPGAPPAPPPSYGATHSTVQPPRPPPPVRDY | null | null | chloride transport [GO:0006821]; L-glutamate transmembrane transport [GO:0015813]; monoatomic anion transport [GO:0006820]; neurotransmitter loading into synaptic vesicle [GO:0098700]; phosphate ion transport [GO:0006817]; potassium ion transport [GO:0006813]; regulation of synapse structure or activity [GO:0050803]; sodium-dependent phosphate transport [GO:0044341]; synaptic transmission, glutamatergic [GO:0035249] | chloride channel complex [GO:0034707]; excitatory synapse [GO:0060076]; neuron projection [GO:0043005]; plasma membrane [GO:0005886]; synaptic vesicle membrane [GO:0030672] | chloride channel activity [GO:0005254]; L-glutamate transmembrane transporter activity [GO:0005313]; L-glutamate uniporter activity [GO:0140788]; neurotransmitter transmembrane transporter activity [GO:0005326]; phosphate ion uniporter activity [GO:0140787]; potassium:proton antiporter activity [GO:0015386]; sodium:phosphate symporter activity [GO:0005436] | PF07690; | 1.20.1250.20; | Major facilitator superfamily, Sodium/anion cotransporter family, VGLUT subfamily | null | SUBCELLULAR LOCATION: Cytoplasmic vesicle, secretory vesicle, synaptic vesicle membrane {ECO:0000250|UniProtKB:Q62634}. Cell membrane {ECO:0000250|UniProtKB:Q62634}; Multi-pass membrane protein {ECO:0000250|UniProtKB:Q62634}. Synapse, synaptosome {ECO:0000250|UniProtKB:Q62634}. | CATALYTIC ACTIVITY: Reaction=L-glutamate(out) = L-glutamate(in); Xref=Rhea:RHEA:66336, ChEBI:CHEBI:29985; Evidence={ECO:0000250|UniProtKB:Q62634}; CATALYTIC ACTIVITY: Reaction=chloride(in) = chloride(out); Xref=Rhea:RHEA:29823, ChEBI:CHEBI:17996; Evidence={ECO:0000250|UniProtKB:Q62634}; CATALYTIC ACTIVITY: Reaction=3 Na(+)(out) + phosphate(out) = 3 Na(+)(in) + phosphate(in); Xref=Rhea:RHEA:71255, ChEBI:CHEBI:29101, ChEBI:CHEBI:43474; Evidence={ECO:0000250|UniProtKB:Q62634}; CATALYTIC ACTIVITY: Reaction=phosphate(in) = phosphate(out); Xref=Rhea:RHEA:32823, ChEBI:CHEBI:43474; Evidence={ECO:0000250|UniProtKB:Q62634}; CATALYTIC ACTIVITY: Reaction=H(+)(out) + K(+)(in) = H(+)(in) + K(+)(out); Xref=Rhea:RHEA:29467, ChEBI:CHEBI:15378, ChEBI:CHEBI:29103; Evidence={ECO:0000250|UniProtKB:Q62634}; | null | null | null | null | FUNCTION: Multifunctional transporter that transports L-glutamate as well as multiple ions such as chloride, proton, potassium, sodium and phosphate. At the synaptic vesicle membrane, mainly functions as an uniporter which transports preferentially L-glutamate but also phosphate from the cytoplasm into synaptic vesicles at presynaptic nerve terminals of excitatory neural cells. The L-glutamate or phosphate uniporter activity is electrogenic and is driven by the proton electrochemical gradient, mainly by the electrical gradient established by the vacuolar H(+)-ATPase across the synaptic vesicle membrane. In addition, functions as a chloride channel that allows a chloride permeation through the synaptic vesicle membrane that affects the proton electrochemical gradient and promotes synaptic vesicles acidification. Moreover, may function as a K(+)/H(+) antiport allowing to maintain the electrical gradient and to decrease chemical gradient and therefore sustain vesicular glutamate uptake. The vesicular K(+)/H(+) antiport activity is electroneutral. At the plasma membrane, following exocytosis, functions as a symporter of Na(+) and phosphate from the extracellular space to the cytoplasm allowing synaptic phosphate homeostasis regulation. The symporter activity is driven by an inside negative membrane potential and is electrogenic (By similarity). Is necessary for synaptic signaling of visual-evoked responses from photoreceptors (By similarity). {ECO:0000250|UniProtKB:Q3TXX4, ECO:0000250|UniProtKB:Q62634}. | Bos taurus (Bovine) |
A4FV54 | RAB8A_BOVIN | MAKTYDYLFKLLLIGDSGVGKTCVLFRFSEDAFNSTFISTIGIDFKIRTIELDGKRIKLQIWDTAGQERFRTITTAYYRGAMGIMLVYDITNEKSFDNIRNWIRNIEEHASADVEKMILGNKCDVNDKRQVSKERGEKLALDYGIKFMETSAKANINVENAFYTLARDIKAKMDKKLEGNSPQGSNQGVKITPDQQKRSSFFRCVLL | 3.6.5.2 | null | autophagy [GO:0006914]; axonogenesis [GO:0007409]; cellular response to insulin stimulus [GO:0032869]; cilium assembly [GO:0060271]; endocytic recycling [GO:0032456]; Golgi organization [GO:0007030]; Golgi vesicle fusion to target membrane [GO:0048210]; neurotransmitter receptor transport to postsynaptic membrane [GO:0098969]; protein localization to cilium [GO:0061512]; protein localization to plasma membrane [GO:0072659]; protein secretion [GO:0009306]; regulation of autophagy [GO:0010506]; regulation of exocytosis [GO:0017157]; vesicle docking involved in exocytosis [GO:0006904] | centriole [GO:0005814]; centrosome [GO:0005813]; ciliary basal body [GO:0036064]; cilium [GO:0005929]; dendritic spine [GO:0043197]; endosome [GO:0005768]; endosome membrane [GO:0010008]; Golgi apparatus [GO:0005794]; midbody [GO:0030496]; phagocytic vesicle [GO:0045335]; phagocytic vesicle membrane [GO:0030670]; plasma membrane [GO:0005886]; recycling endosome membrane [GO:0055038]; synaptic vesicle [GO:0008021]; trans-Golgi network transport vesicle [GO:0030140] | GDP binding [GO:0019003]; GTP binding [GO:0005525]; GTPase activity [GO:0003924]; small GTPase binding [GO:0031267] | PF00071; | 3.40.50.300; | Small GTPase superfamily, Rab family | PTM: Phosphorylation of Thr-72 in the switch II region by LRRK2 prevents the association of RAB regulatory proteins, including CHM, CHML and RAB GDP dissociation inhibitors GDI1 and GDI2. {ECO:0000250|UniProtKB:P61006}. | SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:P55258}; Lipid-anchor {ECO:0000250|UniProtKB:P55258}; Cytoplasmic side {ECO:0000250|UniProtKB:P55258}. Golgi apparatus {ECO:0000250|UniProtKB:P61006}. Endosome membrane {ECO:0000250|UniProtKB:P61006}. Recycling endosome membrane {ECO:0000250|UniProtKB:P61006}. Cell projection, cilium {ECO:0000250|UniProtKB:P61006}. Cytoplasmic vesicle, phagosome membrane {ECO:0000250|UniProtKB:P61006, ECO:0000250|UniProtKB:Q92930}; Lipid-anchor {ECO:0000250|UniProtKB:Q92930}; Cytoplasmic side {ECO:0000250|UniProtKB:Q92930}. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome, centriole {ECO:0000250|UniProtKB:P55258}. Cytoplasm, cytoskeleton, cilium basal body {ECO:0000250|UniProtKB:P55258}. Midbody {ECO:0000250|UniProtKB:P61006}. Cytoplasm {ECO:0000250|UniProtKB:P61006}. Note=Colocalizes with OPTN at the Golgi complex and in vesicular structures close to the plasma membrane. In the GDP-bound form, present in the perinuclear region. Shows a polarized distribution to distal regions of cell protrusions in the GTP-bound form. Colocalizes with PARD3, PRKCI, EXOC5, OCLN, PODXL and RAB11A in apical membrane initiation sites (AMIS) during the generation of apical surface and lumenogenesis. Localizes to tubular recycling endosome. Recruited to phagosomes containing S.aureus or Mycobacterium (By similarity). Non-phosphorylated RAB8A predominantly localizes to the cytoplasm whereas phosphorylated RAB8A localizes to the membrane (By similarity). {ECO:0000250|UniProtKB:P61006}. | CATALYTIC ACTIVITY: Reaction=GTP + H2O = GDP + H(+) + phosphate; Xref=Rhea:RHEA:19669, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:37565, ChEBI:CHEBI:43474, ChEBI:CHEBI:58189; EC=3.6.5.2; Evidence={ECO:0000250|UniProtKB:P61006}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:19670; Evidence={ECO:0000250|UniProtKB:P61006}; | null | null | null | null | FUNCTION: The small GTPases Rab are key regulators of intracellular membrane trafficking, from the formation of transport vesicles to their fusion with membranes. Rabs cycle between an inactive GDP-bound form and an active GTP-bound form that is able to recruit to membranes different sets of downstream effectors directly responsible for vesicle formation, movement, tethering and fusion. That Rab is involved in polarized vesicular trafficking and neurotransmitter release. Together with RAB11A, RAB3IP, the exocyst complex, PARD3, PRKCI, ANXA2, CDC42 and DNMBP promotes transcytosis of PODXL to the apical membrane initiation sites (AMIS), apical surface formation and lumenogenesis. Regulates the compacted morphology of the Golgi (By similarity). Together with MYO5B and RAB11A participates in epithelial cell polarization. Also involved in membrane trafficking to the cilium and ciliogenesis (By similarity). Together with MICALL2, may also regulate adherens junction assembly (By similarity). May play a role in insulin-induced transport to the plasma membrane of the glucose transporter GLUT4 and therefore play a role in glucose homeostasis (By similarity). Involved in autophagy (By similarity). Participates in the export of a subset of neosynthesized proteins through a Rab8-Rab10-Rab11-dependent endososomal export route (By similarity). {ECO:0000250|UniProtKB:P35280, ECO:0000250|UniProtKB:P55258, ECO:0000250|UniProtKB:P61006}. | Bos taurus (Bovine) |
A4FVP2 | TPS03_ARATH | MPKRQAQRRFTRKTDSKTPSQPLVSRRSANYQPSLWQHEYLLSLGNTYVKEDNVERVTLLKQEVSKMLNETEGLLEQLELIDTLQRLGVSYHFEQEIKKTLTNVHVKNVRAHKNRIDRNRWGDLYATALEFRLLRQHGFSIAQDVFDGNIGVDLDDKDIKGILSLYEASYLSTRIDTKLKESIYYTTKRLRKFVEVNKNETKSYTLRRMVIHALEMPYHRRVGRLEARWYIEVYGERHDMNPILLELAKLDFNFVQAIHQDELKSLSSWWSKTGLTKHLDFVRDRITEGYFSSVGVMYEPEFAYHRQMLTKVFMLITTIDDIYDIYGTLEELQLFTTIVEKWDVNRLEELPNYMKLCFLCLVNEINQIGYFVLRDKGFNVIPYLKESWADMCTTFLKEAKWYKSGYKPNFEEYMQNGWISSSVPTILLHLFCLLSDQTLDILGSYNHSVVRSSATILRLANDLATSSEELARGDTMKSVQCHMHETGASEAESRAYIQGIIGVAWDDLNMEKKSCRLHQGFLEAAANLGRVAQCVYQYGDGHGCPDKAKTVNHVRSLLVHPLPLN | 4.2.3.106; 4.2.3.46 | COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250|UniProtKB:A0A1C9J6A7}; Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000250|UniProtKB:A0A1C9J6A7}; Note=Binds 3 Mg(2+) or Mn(2+) ions per subunit. {ECO:0000250|UniProtKB:A0A1C9J6A7}; COFACTOR: Name=K(+); Xref=ChEBI:CHEBI:29103; Evidence={ECO:0000250|UniProtKB:Q84LB2}; | diterpenoid biosynthetic process [GO:0016102]; response to herbivore [GO:0080027]; response to insect [GO:0009625]; response to jasmonic acid [GO:0009753]; response to wounding [GO:0009611]; sesquiterpenoid biosynthetic process [GO:0016106] | chloroplast stroma [GO:0009570]; cytosol [GO:0005829] | (E)-beta-ocimene synthase activity [GO:0034768]; alpha-farnesene synthase activity [GO:0052578]; magnesium ion binding [GO:0000287]; myrcene synthase activity [GO:0050551]; terpene synthase activity [GO:0010333]; tricyclene synthase activity [GO:0102701] | PF01397;PF03936; | 1.10.600.10;1.50.10.130; | Terpene synthase family, Tpsb subfamily | null | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:20463089}. Plastid, chloroplast stroma {ECO:0000269|PubMed:20463089}. | CATALYTIC ACTIVITY: Reaction=(2E,6E)-farnesyl diphosphate = (3E,6E)-alpha-farnesene + diphosphate; Xref=Rhea:RHEA:27421, ChEBI:CHEBI:10280, ChEBI:CHEBI:33019, ChEBI:CHEBI:175763; EC=4.2.3.46; Evidence={ECO:0000269|PubMed:20463089}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:27422; Evidence={ECO:0000269|PubMed:20463089}; CATALYTIC ACTIVITY: Reaction=(2E)-geranyl diphosphate = (E)-beta-ocimene + diphosphate; Xref=Rhea:RHEA:32691, ChEBI:CHEBI:33019, ChEBI:CHEBI:58057, ChEBI:CHEBI:64280; EC=4.2.3.106; Evidence={ECO:0000269|PubMed:12624761, ECO:0000269|PubMed:20463089}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:32692; Evidence={ECO:0000269|PubMed:12624761, ECO:0000269|PubMed:20463089}; | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=6.7 uM for (2E)-geranyl diphosphate {ECO:0000269|PubMed:20463089}; KM=2.6 uM for (2E,6E)-farnesyl diphosphate {ECO:0000269|PubMed:20463089}; Vmax=539 pmol/sec/mg enzyme with (2E)-geranyl diphosphate as substrate {ECO:0000269|PubMed:20463089}; Vmax=69 pmol/sec/mg enzyme with (2E,6E)-farnesyl diphosphate as substrate {ECO:0000269|PubMed:20463089}; Note=kcat is 3.5x10(-2) sec(-1) with (2E)-geranyl diphosphate as substrate (PubMed:20463089). kcat is 4.5x10(-3) sec(-1) with (2E,6E)-farnesyl diphosphate as substrate (PubMed:20463089). {ECO:0000269|PubMed:20463089}; | PATHWAY: Secondary metabolite biosynthesis; terpenoid biosynthesis. {ECO:0000269|PubMed:20463089}. | null | null | FUNCTION: Predominantly involved in sesquiterpenes (C15) biosynthesis. Using FPP as substrate, the major product is (E,E)-alpha-farnesene with minor amounts of (Z,E)-alpha-farnesene and (E,E)-beta-farnesene. Using GPP as substrate, could also be able in vitro to synthesize monoterpene (C10) with (E)-beta-ocimene as the major product and with (Z)-beta-ocimene and myrcene as minor products. {ECO:0000269|PubMed:12624761, ECO:0000269|PubMed:20463089}. | Arabidopsis thaliana (Mouse-ear cress) |
A4FVP6 | NAC16_ARATH | MVDSSRDSCFKAGKFSAPGFRFHPTDEELVVYYLKRKICCKKLRVNAIGVVDVYKVDPSELPGLSMLKTGDRQWFFFTPRNRKYPNAARSSRGTATGYWKATGKDRVIEYNSRSVGLKKTLVFYRGRAPNGERTDWVMHEYTMDEEELGRCKNAKEYYALYKLYKKSGAGPKNGEQYGAPFQEEEWVDSDSEDADSVAVPDYPVVRYENGPCVDDTKFCNPVKLQLEDIEKLLNEIPDAPGVNQRQFDEFVGVPQGNSAEVIQSTLLNNSSGEYIDPRTNGMFLPNGQLYNRDSSFQSHLNSFEATSGMAPLLDNEKEEYIEMNDLLIPELGASSTEKSTEFLNHGEFGDVNEYDQLFNDISVFQGTSTDLSCLSNFTNNTSGQRQQLLYEQFQYQTPENQLNNYMHPSTTLNQFTDNMWFKDDQAALYVQPPQSSSGAFTSQSTGVMPESMNPTMSVNPQYKEGQNGGGTRSQFSSALWELLESIPSTPASACEGPLNQTFVRMSSFSRIRFNGTSVTSRKVTVAKKRISNRGFLLLSIMGALCAIFWVFKATVGVMGRPLLS | null | null | positive regulation of DNA-templated transcription [GO:0045893]; positive regulation of leaf senescence [GO:1900057] | membrane [GO:0016020]; nucleus [GO:0005634] | DNA-binding transcription factor activity [GO:0003700]; transcription cis-regulatory region binding [GO:0000976] | PF02365; | 2.170.150.80; | null | null | SUBCELLULAR LOCATION: Membrane {ECO:0000250|UniProtKB:Q949N0}; Single-pass membrane protein {ECO:0000255}. Nucleus {ECO:0000250|UniProtKB:Q949N0, ECO:0000255|PROSITE-ProRule:PRU00353}. Note=Localized primarily in plasma membrane or endoplasmic reticulum membrane as dormant form and, upon specific stress or signal, is processed into a transcriptionally active and nuclear form after a proteolytic cleavage through regulated intramembrane proteolysis (RIP). {ECO:0000250|UniProtKB:Q949N0}. | null | null | null | null | null | FUNCTION: Transcriptional activator activated by proteolytic cleavage through regulated intramembrane proteolysis (RIP) (By similarity). Transcriptional activator that promotes leaf senescence by up-regulating senescence-associated genes in response to developmental and stress-induced senescence signals. Functions in salt and oxidative stress-responsive signaling pathways. Binds to the promoter of NAC029/NAP and NAC059/ORS1 genes (PubMed:23926065). {ECO:0000250|UniProtKB:Q949N0, ECO:0000269|PubMed:23926065}. | Arabidopsis thaliana (Mouse-ear cress) |
A4GBX8 | M2_I77AA | MSLLTEVETPIRNEWGCRCNDSSDPLVVAASIIGILHLILWILDRLFFKCIYRLFKHGLKRGPSTEGVPESMREEYRKEQQNAVDADDSHFVNIELE | null | null | protein complex oligomerization [GO:0051259]; suppression by virus of host autophagy [GO:0039521] | host cell plasma membrane [GO:0020002]; membrane [GO:0016020]; virion membrane [GO:0055036] | monoatomic ion channel activity [GO:0005216]; proton transmembrane transporter activity [GO:0015078] | PF00599; | 6.10.250.1640; | Influenza viruses matrix protein M2 family | null | SUBCELLULAR LOCATION: Virion membrane {ECO:0000255|HAMAP-Rule:MF_04069}. Host apical cell membrane {ECO:0000255|HAMAP-Rule:MF_04069}; Single-pass type III membrane protein {ECO:0000255|HAMAP-Rule:MF_04069}. Note=Abundantly expressed at the apical plasma membrane in infected polarized epithelial cells, in close proximity to budding and assembled virions. Minor component of virions (only 16-20 molecules/virion). {ECO:0000255|HAMAP-Rule:MF_04069}. | null | null | null | null | null | FUNCTION: Forms a proton-selective ion channel that is necessary for the efficient release of the viral genome during virus entry. After attaching to the cell surface, the virion enters the cell by endocytosis. Acidification of the endosome triggers M2 ion channel activity. The influx of protons into virion interior is believed to disrupt interactions between the viral ribonucleoprotein (RNP), matrix protein 1 (M1), and lipid bilayers, thereby freeing the viral genome from interaction with viral proteins and enabling RNA segments to migrate to the host cell nucleus, where influenza virus RNA transcription and replication occur. Also plays a role in viral proteins secretory pathway. Elevates the intravesicular pH of normally acidic compartments, such as trans-Golgi network, preventing newly formed hemagglutinin from premature switching to the fusion-active conformation. {ECO:0000255|HAMAP-Rule:MF_04069}. | Influenza A virus (strain A/Brazil/11/1978 H1N1) |
A4GCH6 | M2_I83A1 | MSLLTEVETPIRNEWGCRCNDSSDPLVVAASIIGILHLILWILDRLFFKCIYRLFKHGLKRGPSTEGVPESMREEYREEQQNAVDADDGHFVSIELE | null | null | protein complex oligomerization [GO:0051259]; suppression by virus of host autophagy [GO:0039521] | host cell plasma membrane [GO:0020002]; membrane [GO:0016020]; virion membrane [GO:0055036] | monoatomic ion channel activity [GO:0005216]; proton transmembrane transporter activity [GO:0015078] | PF00599; | 6.10.250.1640; | Influenza viruses matrix protein M2 family | null | SUBCELLULAR LOCATION: Virion membrane {ECO:0000255|HAMAP-Rule:MF_04069}. Host apical cell membrane {ECO:0000255|HAMAP-Rule:MF_04069}; Single-pass type III membrane protein {ECO:0000255|HAMAP-Rule:MF_04069}. Note=Abundantly expressed at the apical plasma membrane in infected polarized epithelial cells, in close proximity to budding and assembled virions. Minor component of virions (only 16-20 molecules/virion). {ECO:0000255|HAMAP-Rule:MF_04069}. | null | null | null | null | null | FUNCTION: Forms a proton-selective ion channel that is necessary for the efficient release of the viral genome during virus entry. After attaching to the cell surface, the virion enters the cell by endocytosis. Acidification of the endosome triggers M2 ion channel activity. The influx of protons into virion interior is believed to disrupt interactions between the viral ribonucleoprotein (RNP), matrix protein 1 (M1), and lipid bilayers, thereby freeing the viral genome from interaction with viral proteins and enabling RNA segments to migrate to the host cell nucleus, where influenza virus RNA transcription and replication occur. Also plays a role in viral proteins secretory pathway. Elevates the intravesicular pH of normally acidic compartments, such as trans-Golgi network, preventing newly formed hemagglutinin from premature switching to the fusion-active conformation. {ECO:0000255|HAMAP-Rule:MF_04069}. | Influenza A virus (strain A/Chile/1/1983 H1N1) |
A4GCI7 | M2_I36A0 | MSLLTEVETPIRNEWGCRCNGSSDPLVIAANIIGILHLILWILDRLFFKCIYRLFEYGLKRGPSTEGVPESMREEYRKEQQSAVDADDGHFVSIELE | null | null | protein complex oligomerization [GO:0051259]; suppression by virus of host autophagy [GO:0039521] | host cell plasma membrane [GO:0020002]; membrane [GO:0016020]; virion membrane [GO:0055036] | monoatomic ion channel activity [GO:0005216]; proton transmembrane transporter activity [GO:0015078] | PF00599; | 6.10.250.1640; | Influenza viruses matrix protein M2 family | null | SUBCELLULAR LOCATION: Virion membrane {ECO:0000255|HAMAP-Rule:MF_04069}. Host apical cell membrane {ECO:0000255|HAMAP-Rule:MF_04069}; Single-pass type III membrane protein {ECO:0000255|HAMAP-Rule:MF_04069}. Note=Abundantly expressed at the apical plasma membrane in infected polarized epithelial cells, in close proximity to budding and assembled virions. Minor component of virions (only 16-20 molecules/virion). {ECO:0000255|HAMAP-Rule:MF_04069}. | null | null | null | null | null | FUNCTION: Forms a proton-selective ion channel that is necessary for the efficient release of the viral genome during virus entry. After attaching to the cell surface, the virion enters the cell by endocytosis. Acidification of the endosome triggers M2 ion channel activity. The influx of protons into virion interior is believed to disrupt interactions between the viral ribonucleoprotein (RNP), matrix protein 1 (M1), and lipid bilayers, thereby freeing the viral genome from interaction with viral proteins and enabling RNA segments to migrate to the host cell nucleus, where influenza virus RNA transcription and replication occur. Also plays a role in viral proteins secretory pathway. Elevates the intravesicular pH of normally acidic compartments, such as trans-Golgi network, preventing newly formed hemagglutinin from premature switching to the fusion-active conformation. {ECO:0000255|HAMAP-Rule:MF_04069}. | Influenza A virus (strain A/Henry/1936 H1N1) |
A4GCJ8 | M2_I80AA | MSLLTEVETPIRNEWGCRCNDSSDPLVVAASIIGILHLILWILDRLFFKCIYRLFKHGLKRGPSTEGVPESMREEYREEQQNAVDADDGHFVSIELE | null | null | protein complex oligomerization [GO:0051259]; suppression by virus of host autophagy [GO:0039521] | host cell plasma membrane [GO:0020002]; membrane [GO:0016020]; virion membrane [GO:0055036] | monoatomic ion channel activity [GO:0005216]; proton transmembrane transporter activity [GO:0015078] | PF00599; | 6.10.250.1640; | Influenza viruses matrix protein M2 family | null | SUBCELLULAR LOCATION: Virion membrane {ECO:0000255|HAMAP-Rule:MF_04069}. Host apical cell membrane {ECO:0000255|HAMAP-Rule:MF_04069}; Single-pass type III membrane protein {ECO:0000255|HAMAP-Rule:MF_04069}. Note=Abundantly expressed at the apical plasma membrane in infected polarized epithelial cells, in close proximity to budding and assembled virions. Minor component of virions (only 16-20 molecules/virion). {ECO:0000255|HAMAP-Rule:MF_04069}. | null | null | null | null | null | FUNCTION: Forms a proton-selective ion channel that is necessary for the efficient release of the viral genome during virus entry. After attaching to the cell surface, the virion enters the cell by endocytosis. Acidification of the endosome triggers M2 ion channel activity. The influx of protons into virion interior is believed to disrupt interactions between the viral ribonucleoprotein (RNP), matrix protein 1 (M1), and lipid bilayers, thereby freeing the viral genome from interaction with viral proteins and enabling RNA segments to migrate to the host cell nucleus, where influenza virus RNA transcription and replication occur. Also plays a role in viral proteins secretory pathway. Elevates the intravesicular pH of normally acidic compartments, such as trans-Golgi network, preventing newly formed hemagglutinin from premature switching to the fusion-active conformation. {ECO:0000255|HAMAP-Rule:MF_04069}. | Influenza A virus (strain A/India/6263/1980 H1N1) |
A4GCK9 | M2_I43A0 | MSLLTEVETPIRNEWGCRCNDSSDPLVVAASIIGILHLILWILDRLFFKCIYRLFKHGLKRGPSTEGVPESMREEYRKEQQSAVDADDSHFVNIELE | null | null | protein complex oligomerization [GO:0051259]; suppression by virus of host autophagy [GO:0039521] | host cell plasma membrane [GO:0020002]; membrane [GO:0016020]; virion membrane [GO:0055036] | monoatomic ion channel activity [GO:0005216]; proton transmembrane transporter activity [GO:0015078] | PF00599; | 6.10.250.1640; | Influenza viruses matrix protein M2 family | null | SUBCELLULAR LOCATION: Virion membrane {ECO:0000255|HAMAP-Rule:MF_04069}. Host apical cell membrane {ECO:0000255|HAMAP-Rule:MF_04069}; Single-pass type III membrane protein {ECO:0000255|HAMAP-Rule:MF_04069}. Note=Abundantly expressed at the apical plasma membrane in infected polarized epithelial cells, in close proximity to budding and assembled virions. Minor component of virions (only 16-20 molecules/virion). {ECO:0000255|HAMAP-Rule:MF_04069}. | null | null | null | null | null | FUNCTION: Forms a proton-selective ion channel that is necessary for the efficient release of the viral genome during virus entry. After attaching to the cell surface, the virion enters the cell by endocytosis. Acidification of the endosome triggers M2 ion channel activity. The influx of protons into virion interior is believed to disrupt interactions between the viral ribonucleoprotein (RNP), matrix protein 1 (M1), and lipid bilayers, thereby freeing the viral genome from interaction with viral proteins and enabling RNA segments to migrate to the host cell nucleus, where influenza virus RNA transcription and replication occur. Also plays a role in viral proteins secretory pathway. Elevates the intravesicular pH of normally acidic compartments, such as trans-Golgi network, preventing newly formed hemagglutinin from premature switching to the fusion-active conformation. {ECO:0000255|HAMAP-Rule:MF_04069}. | Influenza A virus (strain A/USA:Iowa/1943 H1N1) |
A4GCM0 | M2_I35A3 | MSLLTEVETPIRNEWGCRCNGSSDPLVIAASIIGILHLILWILDRLLFKCIYRRFKYGLKRGPSTEGVPESMREEYRKEQQSAVDADDGHFVNIEPE | null | null | protein complex oligomerization [GO:0051259]; suppression by virus of host autophagy [GO:0039521] | host cell plasma membrane [GO:0020002]; membrane [GO:0016020]; virion membrane [GO:0055036] | monoatomic ion channel activity [GO:0005216]; proton transmembrane transporter activity [GO:0015078] | PF00599; | 6.10.250.1640; | Influenza viruses matrix protein M2 family | null | SUBCELLULAR LOCATION: Virion membrane {ECO:0000255|HAMAP-Rule:MF_04069}. Host apical cell membrane {ECO:0000255|HAMAP-Rule:MF_04069}; Single-pass type III membrane protein {ECO:0000255|HAMAP-Rule:MF_04069}. Note=Abundantly expressed at the apical plasma membrane in infected polarized epithelial cells, in close proximity to budding and assembled virions. Minor component of virions (only 16-20 molecules/virion). {ECO:0000255|HAMAP-Rule:MF_04069}. | null | null | null | null | null | FUNCTION: Forms a proton-selective ion channel that is necessary for the efficient release of the viral genome during virus entry. After attaching to the cell surface, the virion enters the cell by endocytosis. Acidification of the endosome triggers M2 ion channel activity. The influx of protons into virion interior is believed to disrupt interactions between the viral ribonucleoprotein (RNP), matrix protein 1 (M1), and lipid bilayers, thereby freeing the viral genome from interaction with viral proteins and enabling RNA segments to migrate to the host cell nucleus, where influenza virus RNA transcription and replication occur. Also plays a role in viral proteins secretory pathway. Elevates the intravesicular pH of normally acidic compartments, such as trans-Golgi network, preventing newly formed hemagglutinin from premature switching to the fusion-active conformation. {ECO:0000255|HAMAP-Rule:MF_04069}. | Influenza A virus (strain A/USA:Phila/1935 H1N1) |
A4GG66 | CXG1_RAT | MSWSFLTRLLEEIHNHSTFVGKIWLTVLIVFRIVLTAVGGESIYYDEQSKFVCNTEQPGCENVCYDAFAPLSHVRFWVFQIILVATPSVMYLGYAIHKIAKMEHGEADKKAARSKPYAMRWKQHRALEETEEDHEEDPMMYPEMELESEKENKEQSQPKPKHDGRRRIREDGLMKIYVLQLLARTVFEVGFLIGQYFLYGFQVHPFYVCSRLPCPHKIDCFISRPTEKTIFLLIMYGVTGLCLLLNIWEMLHLGFGTIRDSLNSKRRELDDPGAYNYPFTWNTPSAPPGYNIAVKPDQIQYTELSNAKIAYKQNKANIAQEQQYGSHEEHLPADLETLQREIRMAQERLDLAIQAYHHQNNPHGPREKKAKVGSKSGSNKSSISSKSGDGKTSVWI | null | null | AV node cell to bundle of His cell communication by electrical coupling [GO:0086053]; cardiac muscle tissue development [GO:0048738]; cell development [GO:0048468]; cell-cell signaling [GO:0007267]; chemical synaptic transmission [GO:0007268]; gap junction assembly [GO:0016264]; heart development [GO:0007507]; vasculogenesis [GO:0001570]; visual perception [GO:0007601] | connexin complex [GO:0005922]; endoplasmic reticulum [GO:0005783]; gap junction [GO:0005921]; nucleoplasm [GO:0005654]; synapse [GO:0045202] | gap junction channel activity [GO:0005243]; gap junction channel activity involved in AV node cell-bundle of His cell electrical coupling [GO:0086077]; monoatomic ion channel activity [GO:0005216] | PF00029; | 1.20.1440.80; | Connexin family, Gamma-type subfamily | null | SUBCELLULAR LOCATION: Cell membrane {ECO:0000250}; Multi-pass membrane protein {ECO:0000250}. Cell junction, gap junction {ECO:0000250}. | null | null | null | null | null | FUNCTION: One gap junction consists of a cluster of closely packed pairs of transmembrane channels, the connexons, through which materials of low MW diffuse from one cell to a neighboring cell. {ECO:0000250}. | Rattus norvegicus (Rat) |
A4GNA8 | PSD3_ARATH | MGNGNSTETKESRRSKMRKKIQNFRSRRRLSRPGSGSVSGLASQRSVSADDFAGIALLTLIGAEMKFKDKWLACVSFGEQTFRSEISDSTEKPIWNSEKKLLLEKNGPSLARISVFETNRLLKNNIVGYCELDLLDFVVQEPDSTCKSFDLLDPASSNVVGSMFVSCSVEDPVETETCFAKRILSIVDYDEDGKLSFSEFSDLMNAFGNVVAANKKEELFKAADLNGDGVVTIDELAALLAVQQEQEPIINSCPVCGEALQLDKLNAMIHMTLCFDEGTGNQMTGGFLTDRQASYGWMFKLSEWTHLSTYDVGLNTGSSASHIVVIDRKTKRLVEELIDSKIVMSMRAIYQSKIGLRLMDQGAKEILQNLSEKQGKKMNSVESAQNIPSFLEFFKDQINMAEVKYPLDHFKTFNEFFVRELKPGARPIACMDQDDVAVSAADCRLMAFQSVDDSTRFWIKGRKFSIKGLLGNDVQSDAFLDGSLVIFRLAPQDYHRFHSPVSGVIEKFVNVSGSLYTVNPIAVNSKYCNVFTENKRTIVIISTAEFGKVAFVAIGATMVGSISFVRQEGDHVKKGDELGYFSFGGSTVICVFEKDSIKIDEDLLANSARSLETLVTVGMQLGVSFPKLENCVLEP | 4.1.1.65 | COFACTOR: Name=pyruvate; Xref=ChEBI:CHEBI:15361; Evidence={ECO:0000255|HAMAP-Rule:MF_03209}; Note=Binds 1 pyruvoyl group covalently per subunit. {ECO:0000255|HAMAP-Rule:MF_03209}; | phosphatidylethanolamine biosynthetic process [GO:0006646]; protein autoprocessing [GO:0016540] | cytosol [GO:0005829]; endoplasmic reticulum [GO:0005783]; endoplasmic reticulum membrane [GO:0005789] | calcium ion binding [GO:0005509]; phosphatidylserine decarboxylase activity [GO:0004609] | PF00168;PF13499;PF02666; | 2.60.40.150;1.10.238.10; | Phosphatidylserine decarboxylase family, PSD-B subfamily, Eukaryotic type II sub-subfamily | PTM: Is synthesized initially as an inactive proenzyme. Formation of the active enzyme involves a self-maturation process in which the active site pyruvoyl group is generated from an internal serine residue via an autocatalytic post-translational modification. Two non-identical subunits are generated from the proenzyme in this reaction, and the pyruvate is formed at the N-terminus of the alpha chain, which is derived from the carboxyl end of the proenzyme. The autoendoproteolytic cleavage occurs by a canonical serine protease mechanism, in which the side chain hydroxyl group of the serine supplies its oxygen atom to form the C-terminus of the beta chain, while the remainder of the serine residue undergoes an oxidative deamination to produce ammonia and the pyruvoyl prosthetic group on the alpha chain. During this reaction, the Ser that is part of the protease active site of the proenzyme becomes the pyruvoyl prosthetic group, which constitutes an essential element of the active site of the mature decarboxylase. {ECO:0000255|HAMAP-Rule:MF_03209}. | SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000305|PubMed:17449644}; Lipid-anchor {ECO:0000305}. | CATALYTIC ACTIVITY: Reaction=a 1,2-diacyl-sn-glycero-3-phospho-L-serine + H(+) = a 1,2-diacyl-sn-glycero-3-phosphoethanolamine + CO2; Xref=Rhea:RHEA:20828, ChEBI:CHEBI:15378, ChEBI:CHEBI:16526, ChEBI:CHEBI:57262, ChEBI:CHEBI:64612; EC=4.1.1.65; Evidence={ECO:0000255|HAMAP-Rule:MF_03209}; | null | PATHWAY: Phospholipid metabolism; phosphatidylethanolamine biosynthesis; phosphatidylethanolamine from CDP-diacylglycerol: step 2/2. {ECO:0000255|HAMAP-Rule:MF_03209}. | null | null | FUNCTION: Catalyzes the formation of phosphatidylethanolamine (PtdEtn) from phosphatidylserine (PtdSer). Plays a central role in phospholipid metabolism and in the interorganelle trafficking of phosphatidylserine. Contributes only to a minor proportion of PtdEtn production. {ECO:0000255|HAMAP-Rule:MF_03209, ECO:0000269|PubMed:17449644}. | Arabidopsis thaliana (Mouse-ear cress) |
A4GRC6 | HAP2_CHLRE | MCRAIAVALIVYLAQHYILAHAEVIASGRLEKCVVDGVTEELDCQEKVVVTLTVGNGQSLQTEALEFSLSCLNSPDGRCPCSCSAADPTCACRDLAAPLRVSLTKSPLWASYPLQYLSSFNWKPLEVILRPSNKVCKDGDWEDSPTCGWFSQGGVRVADSQGFCCECSSSQVWDDTFGSSKERTRANLDCDFWSDPLDILIGRKPVSAHCLTFDPQWYSGYELGAASLQFEIAITVEVPTAPSPTTATTSATPRTNNSSSANSTNSTNSPAPQFLSPPAPSTREVLHLGPSVPLASSASRLLSAKLLGDLAMYTQLPAISNQVLMVPQPPAAAAATGSPLDATLATNRSAWMLLDKTMLSMDGLACDKVGTGFSAFRYQPSGCGRAPQACLSGQLKDLWEADLARIADGRVPLYMITRFTGGSDTTLQSFSGGPLSFALPVTSHSQSLVTLSVAADGVRLVTNRSPGKITGAAVCRFAGTSCGGFEAVAARGYIYVNITNTGRLDSDYTLTVSNCSSNVRPIEARTLAVRAGSAASLDPPMELYVEDQAAAAARTCTVSLYDSVGAVTDSLTLSFYTNATQLVVKPSGGYNGTGDGAGVKRNGTDCSTACTNPIDVLCFVTKKCWSKFGRLLGIIGGALVGLGLLAVALKFGWLASLAASCCGGGGGAAAGGAGGGMGLGTGGGGGCFGGGQQQQQLPPAASHAMSPPQQQQRSHAEVAAGAAVAGAGAAGAAAAVLGAKHGGGGGGARGKQQHADTRHLQDRDSRAIDGGASIGSSSAGGSSSLSSYSQPREAGGRLLQPPAAAVFVPEGGGGGAAGDEGARAQSSDWDARGRSPRVADEHGSPRQRYDGVRQSPYMVSANPYDGWYDGGSGGGGGGGGGGYGREAPPPQGPPPHPVGAPPPPPRRRSLWERMWLQRPGGGGGGGGGGGGGGGGGSGGGVDQHGGRSCADAARRGGGGPGGMRGVEGLMSNGGRPNGPHPHAPPPPPPPQQQQQQQRQRRSFLESLTAMMTLPWGGGREEEAGGDRRGGGRGGAAAAHGGRGAGGGRGHPPSIGSPPPGPLQPPEYGPQGGQARRWGAGGGRGGVGGDGGGGGVGAAAYVQLSTGGRGGGGGGGRGRGGGREGPTWHNPVYDWQAPPK | null | null | fusion of sperm to egg plasma membrane involved in single fertilization [GO:0007342]; protein insertion into membrane [GO:0051205] | cell projection membrane [GO:0031253]; cytoplasmic vesicle [GO:0031410]; cytoplasmic vesicle membrane [GO:0030659]; plasma membrane [GO:0005886] | lipid binding [GO:0008289] | PF10699; | null | HAP2/GCS1 family | PTM: The protein present at the cell membrane is rapidly degraded after fusion between male (minus) and female (plus) gametes, contrary to the protein present in intracellular pools (PubMed:20335357). This may represent a mechanism to avoid fusion of several male gametes with a single female gamete (Probable). {ECO:0000269|PubMed:20335357, ECO:0000305}.; PTM: N-glycosylated. {ECO:0000269|PubMed:20335357}. | SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:20335357, ECO:0000269|PubMed:25655701, ECO:0000269|PubMed:28235200}; Single-pass type I membrane protein {ECO:0000269|PubMed:28235200, ECO:0000305|PubMed:20335357, ECO:0000305|PubMed:25655701}. Cell projection {ECO:0000269|PubMed:25655701, ECO:0000269|PubMed:28235200}. Cytoplasmic vesicle membrane {ECO:0000269|PubMed:25655701}. Note=In male gametes, detected both in cytoplasmic vesicles and on cell projections called mating structures at the cell membrane. {ECO:0000269|PubMed:25655701}. | null | null | null | null | null | FUNCTION: During fertilization, required on male (minus) gametes for their fusion with female (plus) gametes (PubMed:18367645, PubMed:20335357, PubMed:25655701, PubMed:28235200). Required for membrane fusion, but not for the initial adhesion between gametes (PubMed:18367645, PubMed:25655701, PubMed:28235200). Inserts (via its extracellular domain) into lipid membranes (in vitro) (PubMed:28235200). Probably initiates the fusion of gamete cell membranes by inserting its extracellular domain into the cell membrane of a female gamete (PubMed:28235200). {ECO:0000269|PubMed:18367645, ECO:0000269|PubMed:20335357, ECO:0000269|PubMed:25655701, ECO:0000269|PubMed:28235200}. | Chlamydomonas reinhardtii (Chlamydomonas smithii) |
A4GSN8 | NUA_ARATH | MPLFMPDEELARLSSDAASVVAERADEYIRKIYAELDSVRAKADAASITAEQTCSLLEQKYLSLSQDFSSLESQNAKLQSDFDDRLAELAQSQAQKHQLHLQSIEKDGEVERMSTEMSELHKSKRQLMELLEQKDAEISEKNSTIKSYLDKIVKLTDTSSEKEARLAEATAELARSQAMCSRLSQEKELTERHAKWLDEELTAKVDSYAELRRRHSDLESEMSAKLVDVEKNYIECSSSLNWHKERLRELETKIGSLQEDLSSCKDAATTTEEQYTAELFTANKLVDLYKESSEEWSRKAGELEGVIKALEARLSQVESSYKERLDKEVSTKQLLEKENGDLKQKLEKCEAEIEKTRKTDELNLIPFSNFTRRVDNSGTSNMIEESQAVISKVPAGVSGTALAASLLRDGWSLAKIYEKYQEAVDAMRHEQLGRKEAEMILQRVLSELEEKAGFIQEERGEYERVVEAYCLVNQKLQDSVSEQSNMEKFIMELKADLRRRERENTLLQKDISDLQKQVTILLKECRDVQLRCGAARDDDEDDYPLLSDVEMEMESEADKIISEHLLKFKDINGLVEQNVKLRNLVRSLSEQIESRETELKETFEVDLKNKTDEASAKVATVLKRAEEQGQMIESLHTSVAMYKRLYEEEQKLHSSDSRSSDLSPAVVPGRKNFLHLLEDSEEATKRAQEKAFERIRILEEDFAKARSEVIAIRSERDKLAMEANFAREKLEGIMKESERKREEMNSVLARNIEFSQLIIDHQRKLRESSESLHAAEEISRKLSMEVSVLKQEKELLSNAEKRASDEVSALSQRVYRLQATLDTVQSTEEVREETRAAERRKQEEHIKQLQREWAEAKKELQEERSNARDFTSDRNQTLNNAVMQVEEMGKELANALKAVSVAESRASVAEARLSDLEKKIRSSDPKTLDMDSGGIVSLSDKEMSIELRTAKEEIEKLRGEVESSKSHMLQYKSIAQVNETALKQMESAHENFRLEAEKRQRSLEAELVSLRERVSELENDCIQKSEQLATAAAGKEDALLSASAEIASLREENLVKKSQIEAMNIQMSTLKNDLETEHEKWRVAQRNYERQVILLSETIQELTKTSQALAALQEEASELRKLADARGIENSELNAKWSEEKLMLEQQKNLAEKKYHELNEQNKLLHSRLEAKHLNSAEKNSRSGTISSGSTDSDHLEDSGLQRVVHYLRRTKEIAETEISLMRQEKLRLQSQLESALKMAESARGSLTAERASTRASLLTDDGIKSLQLQVSEMNLLRESNMQLREENKHNFEKCQEMREVAQKARMESENFENLLKTKQTELDLCMKEMEKLRMETDLHKKRVDELRETYRNIDIADYNRLKDEVRQLEEKLKAKDAHAEDCKKVLLEKQNKISLLEKELTNCKKDLSEREKRLDDAQQAQATMQSEFNKQKQELEKNKKIHYTLNMTKRKYEKEKDELSKQNQSLAKQLEEAKEEAGKRTTTDAVVEQSVKEREEKEKRIQILDKYVHQLKDEVRKKTEDLKKKDEELTKERSERKSVEKEVGDSLTKIKKEKTKVDEELAKLERYQTALTHLSEELEKLKHADGNLPEGTSAVQVLSGSILNDQAAAYVSAVEYFERVARSIASNSQVSTKPTDMVTEPSSGIPAAEPSTMTRVPSSTPLIKSPVATTQQLPKVASDNKEKRLISQKPSTEFRRPSGRRIVRPQLVKPEESPKVDVDMPEAEGTGDEGKQPAAHEPESQVTTSVRPVQTLVRKRQADSLVSEPQQDSLTQGETSSEIAPPASKKAKGSESHPDTSEGENLAKEPAIDELMDATTTTDGDNEETEAENAEEKTEEYVEAQQDNEADEPVEESPTETETIPTEEESRDQTEEENQEPLTDMESDKEEGELDLDTLEDLEEGTDVASMMRSPEKEEVQPETLATPTQSPSRMETAMEEAETTIETPVEDDKTDEGGDAAEEAADIPNNANDQQEAPETDIKPETSAATTSPVSTAPTTSSTLASAITSSGAPETEDPKRAPSPGGGSSTIVTLADRAQMKRRERIANIVVSRAPNPATRGARGRTVNLRGGGRLLPRGGRAPRGGRGQSPSPP | null | null | negative regulation of flower development [GO:0009910]; negative regulation of protein sumoylation [GO:0033234]; poly(A)+ mRNA export from nucleus [GO:0016973]; protein import into nucleus [GO:0006606]; regulation of mitotic spindle assembly [GO:1901673]; stamen development [GO:0048443] | mitochondrion [GO:0005739]; nuclear envelope [GO:0005635]; nuclear membrane [GO:0031965]; nuclear pore [GO:0005643]; nucleolus [GO:0005730]; plasmodesma [GO:0009506] | structural constituent of nuclear pore [GO:0017056] | PF07926; | null | null | null | SUBCELLULAR LOCATION: Nucleus envelope {ECO:0000269|PubMed:17513499, ECO:0000269|PubMed:19704557, ECO:0000269|PubMed:21189294}. Nucleus membrane {ECO:0000269|PubMed:19704557}; Peripheral membrane protein {ECO:0000269|PubMed:19704557}; Nucleoplasmic side {ECO:0000269|PubMed:19704557}. Nucleus, nuclear pore complex {ECO:0000269|PubMed:19704557}. Note=Located at the inner surface of the nuclear envelope during interphase and in the vicinity of the spindle during prometaphase. {ECO:0000269|PubMed:17513499, ECO:0000269|PubMed:19704557}. | null | null | null | null | null | FUNCTION: Component of the nuclear pore complex. Acts as a docking site for activities required for desumoylation and mRNA export. Required for the proper expression or localization of a subset of miRNAs. Plays a role in meristematic cell division by interacting with spindle assembly checkpoint proteins. {ECO:0000269|PubMed:17513499, ECO:0000269|PubMed:17535820, ECO:0000269|PubMed:19704557, ECO:0000269|PubMed:19704774, ECO:0000303|PubMed:20872268}. | Arabidopsis thaliana (Mouse-ear cress) |
A4GTP4 | ELK1_RAT | MDPSVTLWQFLLQLLREQGNGHIISWTSRDGGEFKLVDAEEVARLWGLRKNKTNMNYDKLSRALRYYYDKNIIRKVSGQKFVYKFVSYPEVAGCSTEDCPPQPEVSVTSAVAMAPATVHSGPGDNATGKPGTPKGAGMTGQGGLARSSRNEYMRSGLYSTFTIQSLQPQPPLHPRPASVLPNTTPAGVPAPPSGSRSTSPNPLEACLEAEEAGLPLQVILTPPEAPNQKSEELSLNPGFGRPQPPEVKVEGPKEELEVTEVGGFSPEAVKAEQEVSPSEGLLARLPAILTENTAQVCGLSTSTTEITQPQKGRKPRDLELPLSPSLLGGQGPERTPGSGTSSGLQAQGPALTPSLLPTHTLTPVLLTPSSLPPSIHFWSTLSPIAPRSPAKLSFQFPSSGSAQVHIPSISVDGLSTPVVLSPGPQKP | null | null | cell differentiation [GO:0030154]; cellular response to gamma radiation [GO:0071480]; cellular response to lipid [GO:0071396]; cellular response to testosterone stimulus [GO:0071394]; gene expression [GO:0010467]; hippocampal neuron apoptotic process [GO:0110088]; liver development [GO:0001889]; lung development [GO:0030324]; positive regulation of DNA-templated transcription [GO:0045893]; positive regulation of transcription by RNA polymerase II [GO:0045944]; regulation of DNA-templated transcription [GO:0006355]; regulation of transcription by RNA polymerase II [GO:0006357]; response to ethanol [GO:0045471]; response to fibroblast growth factor [GO:0071774]; response to light stimulus [GO:0009416] | axon terminus [GO:0043679]; dendrite [GO:0030425]; mitochondrial membrane [GO:0031966]; neuronal cell body [GO:0043025]; nucleoplasm [GO:0005654]; nucleus [GO:0005634] | 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]; double-stranded DNA binding [GO:0003690]; nuclear receptor coactivator activity [GO:0030374]; RNA polymerase II cis-regulatory region sequence-specific DNA binding [GO:0000978]; RNA polymerase II-specific DNA-binding transcription factor binding [GO:0061629]; sequence-specific double-stranded DNA binding [GO:1990837]; transcription cis-regulatory region binding [GO:0000976] | PF00178; | 1.10.10.10; | ETS family | PTM: Sumoylation represses transcriptional activator activity as it results in recruitment of HDAC2 to target gene promoters which leads to decreased histone acetylation and reduced transactivator activity. It also regulates nuclear retention. {ECO:0000250|UniProtKB:P19419}.; PTM: On mitogenic stimulation, phosphorylated on C-terminal serine and threonine residues by MAPK1. Ser-382 and Ser-388 are the preferred sites for MAPK1. In vitro, phosphorylation by MAPK1 potentiates ternary complex formation with the serum responses factors, SRE and SRF. Also phosphorylated on Ser-382 by MAPK8 and/or MAKP9. Phosphorylation leads to loss of sumoylation and restores transcriptional activator activity. Phosphorylated and activated by CAMK4, MAPK11, MAPK12 and MAPK14 (By similarity). Upon bFGF stimulus, phosphorylated by PAK1 (PubMed:17156131). Phosphorylated by PRP4K at Thr-416; phosphorylation activation ELK1 transcriptional activity (By similarity). {ECO:0000250|UniProtKB:P19419, ECO:0000269|PubMed:17156131}. | SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:P19419}. | null | null | null | null | null | FUNCTION: Transcription factor that binds to purine-rich DNA sequences. Forms a ternary complex with SRF and the ETS and SRF motifs of the serum response element (SRE) on the promoter region of immediate early genes such as FOS and IER2 (By similarity) (PubMed:17156131). Induces target gene transcription upon JNK and MAPK-signaling pathways stimulation (PubMed:17156131). {ECO:0000250|UniProtKB:P19419, ECO:0000269|PubMed:17156131}. | Rattus norvegicus (Rat) |
Subsets and Splits