Entry stringlengths 6 10 | Entry Name stringlengths 5 11 | Sequence stringlengths 2 35.2k | EC number stringlengths 7 118 ⌀ | Cofactor stringlengths 38 1.77k ⌀ | Gene Ontology (biological process) stringlengths 18 11.3k ⌀ | Gene Ontology (cellular component) stringlengths 17 1.75k ⌀ | Gene Ontology (molecular function) stringlengths 24 2.09k ⌀ | Pfam stringlengths 8 232 ⌀ | Gene3D stringlengths 10 250 ⌀ | Protein families stringlengths 9 237 ⌀ | Post-translational modification stringlengths 16 8.52k ⌀ | Subcellular location [CC] stringlengths 29 6.18k ⌀ | Catalytic activity stringlengths 64 35.7k ⌀ | Kinetics stringlengths 69 11.7k ⌀ | Pathway stringlengths 27 908 ⌀ | pH dependence stringlengths 64 955 ⌀ | Temperature dependence stringlengths 70 1.16k ⌀ | Function [CC] stringlengths 17 15.3k ⌀ | Organism stringlengths 8 196 |
|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|
C5H8J1 | EME1B_ARATH | MNDHILISDGEDQTTPLPSLSKRARKYPISAILISDSDPTPQKQPPESSFTPIFVPETPLSDDFSVVKCSFGSRALASNREDKFSGKRIISLDSEFEDSPRPETSKKNESVLAGLREPRFGLEAETSEAYYKNTRIPETNLDDDTSWMHEVSFRSSPTNDTIEVVSDQEKEDISVEKIGRKKKIRTTTLPVPGEALPKKRQSKEDKTSAMEEKKLRKEQERLEKAASKAEEAERKRLEKEKKKWEKGKLALKSIVAEIDTKVLEGSIGGLLLSRFSEKGITIHVGPNPIERSIVWTMTIPEDIAPLFPQGPKIPYLLLVY... | 3.1.22.- | COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000305}; Name=Ca(2+); Xref=ChEBI:CHEBI:29108; Evidence={ECO:0000305}; | cell division [GO:0051301]; DNA recombination [GO:0006310]; DNA repair [GO:0006281]; double-strand break repair [GO:0006302]; mitotic intra-S DNA damage checkpoint signaling [GO:0031573]; replication fork processing [GO:0031297]; resolution of meiotic recombination intermediates [GO:0000712] | Holliday junction resolvase complex [GO:0048476]; nucleus [GO:0005634] | crossover junction DNA endonuclease activity [GO:0008821]; DNA binding [GO:0003677]; endonuclease activity [GO:0004519]; metal ion binding [GO:0046872] | PF21292;PF02732; | 3.40.50.10130;1.10.150.670; | EME1/MMS4 family | null | SUBCELLULAR LOCATION: Nucleus {ECO:0000305}. | null | null | null | null | null | FUNCTION: Interacts with MUS81 to form a DNA structure-specific endonuclease with substrate preference for branched DNA structures with a 5'-end at the branch nick. Typical substrates include 3'-flap structures, D-loops, replication forks, nicked Holliday junctions and also intact Holliday junctions with a reduced effi... | Arabidopsis thaliana (Mouse-ear cress) |
C5I9W9 | WTS_ARATH | METVSAVNQTLPISGGEPVKFTTYSAAVHKVLVMINAGILGLLQLVSQQSSVLETHKAAFLCFCVFILFYAVLRVREAMDVRLQPGLVPRLIGHGSHLFGGLAALVLVSVVSTAFSIVLFLLWFIWLSAVVYLETNKPSACPPQLPPV | null | null | calcium ion transport [GO:0006816]; defense response to fungus [GO:0050832]; monoatomic cation transport [GO:0006812]; protein complex oligomerization [GO:0051259]; response to fungus [GO:0009620]; sodium ion transport [GO:0006814] | endoplasmic reticulum membrane [GO:0005789] | calcium channel activity [GO:0005262]; monoatomic cation channel activity [GO:0005261]; protein self-association [GO:0043621]; sodium channel activity [GO:0005272] | null | null | null | null | SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000269|PubMed:37295403}; Multi-pass membrane protein {ECO:0000255}. | CATALYTIC ACTIVITY: Reaction=Ca(2+)(in) = Ca(2+)(out); Xref=Rhea:RHEA:29671, ChEBI:CHEBI:29108; Evidence={ECO:0000269|PubMed:37295403}; CATALYTIC ACTIVITY: Reaction=Na(+)(in) = Na(+)(out); Xref=Rhea:RHEA:34963, ChEBI:CHEBI:29101; Evidence={ECO:0000269|PubMed:37295403}; | null | null | null | null | FUNCTION: Calcium-permeable cation-selective channel conferring a broad-spectrum clubroot resistance by supporting cytosolic Ca(2+) increase in root pericycle cells (PubMed:37295403). Triggers immunity toward fungal pathogens such as Plasmodiophora brassicae (Pb) and induces defenses (PubMed:37295403). Also permeable t... | Arabidopsis thaliana (Mouse-ear cress) |
C5I9X1 | ALDH1_ARTAN | MSSGANGSSKSASHKIKFTKLFINGEFVDSISGNTFDTINPATEEVLATVAEGRKEDIDLAVKAAREAFDNGPWPRMSGEARRKIMLKFADLIDENADELTTLEVIDGGKLFGPVRHFEVPVSSDTFRYFAGAADKIRGATLKMSSNIQAYTLREPIGVVGHIIPWNGPAFMFATKVAPALAAGCTMVIKPAEHTPLTVLFLAHLSKLAGVPDGVINVVNGFGKTAGAAVSSHMDIDMVTFTGSTEVGRTVMQAAALSNLKPVSLELGGKSPLIVFDDADVDKAAEFAILGNFTNKGEMCVAGSRVFVQEGIHDVFVKKL... | 1.2.1.- | null | null | cytosol [GO:0005829] | aldehyde dehydrogenase (NAD+) activity [GO:0004029] | PF00171; | null | Aldehyde dehydrogenase family | null | SUBCELLULAR LOCATION: Cytoplasm, cytosol {ECO:0000250|UniProtKB:P20000}. | CATALYTIC ACTIVITY: Reaction=(+)-artemisinic aldehyde + H2O + NADP(+) = (+)-artemisinate + 2 H(+) + NADPH; Xref=Rhea:RHEA:60680, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349, ChEBI:CHEBI:64688, ChEBI:CHEBI:64782; Evidence={ECO:0000269|Ref.1}; PhysiologicalDirection=left-to-right; Xref=Rhea... | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=2.58 uM for artemisinic aldehyde (in the presence of NADP, at pH 8.5 and 30 degrees Celsius) {ECO:0000269|Ref.1}; KM=8.79 uM for dihydroartemisinic aldehyde (in the presence of NADP, at pH 8.5 and 30 degrees Celsius) {ECO:0000269|Ref.1}; Vmax=11.1 nmol/min/mg enzym... | PATHWAY: Sesquiterpene biosynthesis. {ECO:0000303|PubMed:30468448}. | BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 8.5. {ECO:0000269|Ref.1}; | null | FUNCTION: Involved in the biosynthesis of the antimalarial endoperoxide artemisinin (PubMed:27488942, Ref.1). Catalyzes the NAD(P)-dependent oxidation of artemisinin precursors, artemisinic and dihydroartemisinic aldehydes, thus producing artemisinic and dihydroartemisinic acids, respectively (Ref.1). Can use both NAD ... | Artemisia annua (Sweet wormwood) |
C5JKE6 | ARO1_BLAGS | MGVPTKISILGRESIVADFGIWRNYVAKDLLNSCSSSTYILISDTNITPLYLDGFQKSFDDAAANLSPKPRLLTYEIPPGESSKSRETKAGIEDWMLTRQPPCGRDTVIIALGGGVIGDLIGFVAATYMRGVRFVQVPTTLLAMVDSSIGGKTAIDTPNGKNLIGAIWQPQRIYLDMEFLNTLPEREFINGMAEVIKTAAISSEEKFAALEDDAEIILAAVKSKNTPERPRFSGIEETLKRTILSSAEFKAQVVSADEREGGLRNLLNFGHSIGHAIEAILAPQVLHGECVAIGMVKEAELARHLGILNNVSVSRISKCL... | 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:000476... | PF01761;PF01487;PF00275;PF08501;PF01202; | 3.40.50.1970;3.20.20.70;1.20.1090.10;3.65.10.10;3.40.50.10860;3.40.50.720;3.40.50.300; | Sugar phosphate cyclases superfamily, Dehydroquinate synthase family; EPSP synthase family; Shikimate kinase family; Type-I 3-dehydroquinase family; Shikimate dehydrogenase family | null | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_03143}. | CATALYTIC ACTIVITY: Reaction=7-phospho-2-dehydro-3-deoxy-D-arabino-heptonate = 3-dehydroquinate + phosphate; Xref=Rhea:RHEA:21968, ChEBI:CHEBI:32364, ChEBI:CHEBI:43474, ChEBI:CHEBI:58394; EC=4.2.3.4; Evidence={ECO:0000255|HAMAP-Rule:MF_03143}; CATALYTIC ACTIVITY: Reaction=3-dehydroquinate = 3-dehydroshikimate + H2O; Xr... | 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: st... | null | null | FUNCTION: The AROM polypeptide catalyzes 5 consecutive enzymatic reactions in prechorismate polyaromatic amino acid biosynthesis. {ECO:0000255|HAMAP-Rule:MF_03143}. | Blastomyces gilchristii (strain SLH14081) (Blastomyces dermatitidis) |
C5M1X2 | ARO1_CANTT | MSIEKVPILGKETIHVGYGIQDHIVTEVVDNLASSTYVIVTDTNVEKTPQFSKLTNDFTKVLNEKRPDSRVLTYSVPPGENNKNRATKAAVEDFLLQQGCTRDTVIIAVGGGVIGDMIGFVAATFMRGVRVVQVPTTLLAMVDSSVGGKTAIDTPLGKNFIGAFHQPQYVFIDVSYLESLPTRQFINGMAEVVKTAAIWNEEEFTRLENFSKQFLSVVTAKNPDLLSIKEELVKTVLESVRVKAEVVSSDEKESSLRNLLNFGHTIGHAIEAIVTPEALHGECVSIGMIKEAELARYLGILPPVAVARLSKCLVAYGLPV... | 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:000476... | 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; Xr... | 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: st... | null | null | FUNCTION: The AROM polypeptide catalyzes 5 consecutive enzymatic reactions in prechorismate polyaromatic amino acid biosynthesis. {ECO:0000255|HAMAP-Rule:MF_03143}. | Candida tropicalis (strain ATCC MYA-3404 / T1) (Yeast) |
C5MSH2 | POLG_SALVA | MEGSNGFSSSLAGLSSSRSSLRLLTHFLSLPTLPVNIYLNARRHSGWYRSPPTLPVNIYLNEQFDNLCLAALRYPGHKLYPSVHTLFPDVSPLKIPHSVPAFAHLVQRQGLRRQGNSITNIYGNGNDVTTDVGANGMSLPIAVGDMPTASTSEAPLGSNKGGSSTSPKSTSNGNVVRGSRYSKWWEPAAARALDRALDHAVDATDAVAGAASKGIKAGAAKLSNKLSGSQTTALLALPGNIAGGAPSATVNANNTSISSQALLPSVNPYPSTPAVSLPNPDAPTQVGPAADRQWLVDTLSWSETIAPLTVFSGPKALTPG... | 2.7.7.48; 3.4.22.28; 3.6.4.13 | null | DNA-templated transcription [GO:0006351]; protein complex oligomerization [GO:0051259]; proteolysis [GO:0006508]; suppression by virus of host mRNA export from nucleus [GO:0039522]; symbiont entry into host cell [GO:0046718]; symbiont-mediated suppression of host gene expression [GO:0039657]; viral RNA genome replicati... | host cell cytoplasmic vesicle membrane [GO:0044162]; host cell Golgi membrane [GO:0044178]; membrane [GO:0016020]; T=pseudo3 icosahedral viral capsid [GO:0039618] | ATP binding [GO:0005524]; ATP hydrolysis activity [GO:0016887]; cysteine-type endopeptidase activity [GO:0004197]; monoatomic ion channel activity [GO:0005216]; RNA binding [GO:0003723]; RNA helicase activity [GO:0003724]; RNA-dependent RNA polymerase activity [GO:0003968]; structural molecule activity [GO:0005198] | PF00680;PF00073;PF00910; | 1.20.960.20;2.60.120.20;3.30.70.270;2.40.10.10; | null | PTM: [Genome polyprotein]: Specific enzymatic cleavages by the viral protease in vivo yield a variety of precursors and mature proteins (By similarity). The leader protein-VP0 junction is cleaved by 3C proteinase (By similarity). The VP1/2A junction is cleaved by the protein 3CD in association with protein 2A (By simil... | SUBCELLULAR LOCATION: [Capsid protein VP0]: Virion {ECO:0000250|UniProtKB:O91464}. Host cytoplasm {ECO:0000250|UniProtKB:P12296}.; SUBCELLULAR LOCATION: [Capsid protein VP3]: Virion {ECO:0000250|UniProtKB:O91464}. Host cytoplasm {ECO:0000250|UniProtKB:P12296}.; SUBCELLULAR LOCATION: [Capsid protein VP1]: Virion {ECO:00... | 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}; CATALYTIC ACTIVITY: Reaction=a ribonucleoside 5'-triphosphate + RNA(n) ... | null | null | null | null | FUNCTION: [Leader protein]: Required for viral RNA replication and viral RNA encapsidation (By similarity). Does not have any proteolytic activity (By similarity). {ECO:0000250|UniProtKB:O91464}.; FUNCTION: [Capsid protein VP1]: Forms an icosahedral capsid of pseudo T=3 symmetry with capsid proteins VP0 and VP3 (By sim... | Salivirus A (isolate Human/Nigeria/NG-J1/2007) (SV-A) |
C5PA86 | ARO1_COCP7 | MAAPTTIKILGRDSIVADFGIWKRHVADDLLTNCSSSTYILISDTTLTPLYVPSFQAAFENAASGLTPKPRLLTYAIPPGELSKSRQTKADIEDWMLSRQPPCGRDTVIIALGGGVIGDLIGYVAATYMRGVRFVQVPTTLLAMVDSSIGGKTAIDTPHGKNLIGAIWQPQKIYLDMEFLNTLPEREFINGMAEVIKTAAISSEEDFAALEKNADAILSAVKSENTPERPRFGGIQEILKLTILASARFKADVVSKDEREGGLRNLLNFGHSIGHAIEGILAPQILHGECVAIGMVKEAELARHLGLLKNVAVPRLVKCL... | 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:000476... | PF01761;PF01487;PF00275;PF18317;PF08501;PF01202; | 3.40.50.1970;3.20.20.70;1.20.1090.10;3.65.10.10;3.40.50.10860;3.40.50.720;3.40.50.300; | Sugar phosphate cyclases superfamily, Dehydroquinate synthase family; EPSP synthase family; Shikimate kinase family; Type-I 3-dehydroquinase family; Shikimate dehydrogenase family | null | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_03143}. | CATALYTIC ACTIVITY: Reaction=7-phospho-2-dehydro-3-deoxy-D-arabino-heptonate = 3-dehydroquinate + phosphate; Xref=Rhea:RHEA:21968, ChEBI:CHEBI:32364, ChEBI:CHEBI:43474, ChEBI:CHEBI:58394; EC=4.2.3.4; Evidence={ECO:0000255|HAMAP-Rule:MF_03143}; CATALYTIC ACTIVITY: Reaction=3-dehydroquinate = 3-dehydroshikimate + H2O; Xr... | 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: st... | null | null | FUNCTION: The AROM polypeptide catalyzes 5 consecutive enzymatic reactions in prechorismate polyaromatic amino acid biosynthesis. {ECO:0000255|HAMAP-Rule:MF_03143}. | Coccidioides posadasii (strain C735) (Valley fever fungus) |
C6DS31 | LYSX_MYCTK | MGVGLHLTVPGLRRDGRGVQSNSHDTSSKTTADISRCPQHTDAGLQRAATPGISRLLGISSRSVTLTKPRSATRGNSRYHWVPAAAGWTVGVIATLSLLASVSPLIRWIIKVPREFINDYLFNFPDTNFAWSFVLALLAAALTARKRIAWLVLLANMVLAAVVNAAEIAAGGNTAAESFGENLGFAVHVVAIVVLVLGYREFWAKVRRGALFRAAAVWLAGAVVGIVASWGLVELFPGSLAPDERLGYAANRVVGFALADPDLFTGRPHVFLNAIFGLFGAFALIGAAIVLFLSQRADNALTGEDESAIRGLLDLYGKDD... | 2.3.2.3; 6.1.1.6 | COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250}; Note=Binds 3 Mg(2+) ions per subunit. {ECO:0000250}; | diadenosine tetraphosphate biosynthetic process [GO:0015966]; lipid metabolic process [GO:0006629]; lysyl-tRNA aminoacylation [GO:0006430]; positive regulation of macrophage activation [GO:0043032]; response to antibiotic [GO:0046677] | aminoacyl-tRNA synthetase multienzyme complex [GO:0017101]; cytosol [GO:0005829]; extracellular space [GO:0005615]; plasma membrane [GO:0005886] | ATP adenylyltransferase activity [GO:0003877]; ATP binding [GO:0005524]; DNA binding [GO:0003677]; lysine-tRNA ligase activity [GO:0004824]; magnesium ion binding [GO:0000287]; phosphatidylglycerol lysyltransferase activity [GO:0050071]; tRNA binding [GO:0000049] | PF09924;PF00152;PF16995;PF01336; | 2.40.50.140; | LPG synthetase family; Class-II aminoacyl-tRNA synthetase family | null | SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}. | CATALYTIC ACTIVITY: Reaction=ATP + L-lysine + tRNA(Lys) = AMP + diphosphate + L-lysyl-tRNA(Lys); Xref=Rhea:RHEA:20792, Rhea:RHEA-COMP:9696, Rhea:RHEA-COMP:9697, ChEBI:CHEBI:30616, ChEBI:CHEBI:32551, ChEBI:CHEBI:33019, ChEBI:CHEBI:78442, ChEBI:CHEBI:78529, ChEBI:CHEBI:456215; EC=6.1.1.6; CATALYTIC ACTIVITY: Reaction=1,2... | null | null | null | null | FUNCTION: Catalyzes the production of L-lysyl-tRNA(Lys)transfer and the transfer of a lysyl group from L-lysyl-tRNA(Lys) to membrane-bound phosphatidylglycerol (PG), which produces lysylphosphatidylglycerol (LPG), one of the components of the bacterial membrane with a positive net charge. LPG synthesis contributes to t... | Mycobacterium tuberculosis (strain KZN 1435 / MDR) |
C6EVG7 | VNHP_HELSC | MNPRLACSTWLPLLLVLFTLDQGRANPVERGQEYRSLSKRFDDDSTELILEPRASEENGPPYQPLVPRASDENVPPAYVPLVPRASDENVPPPPLQMPLIPRASEQKGPPFNPPPFVDYEPRAANENALRKLIKRSFERSPGRNKRLSPGDGCFGQKIDRIGAVSGMGCNSVSSQGKK | null | null | blood vessel diameter maintenance [GO:0097746]; cGMP biosynthetic process [GO:0006182]; cGMP-mediated signaling [GO:0019934]; negative regulation of systemic arterial blood pressure [GO:0003085]; neuropeptide signaling pathway [GO:0007218]; receptor guanylyl cyclase signaling pathway [GO:0007168] | cytoplasm [GO:0005737]; extracellular space [GO:0005615] | hormone activity [GO:0005179]; hormone receptor binding [GO:0051427]; toxin activity [GO:0090729] | PF00212; | null | Natriuretic peptide family | null | SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:19837656}. | null | null | null | null | null | FUNCTION: Helokinestatins antagonize the vasodilatory actions of bradykinin at the B2 bradykinin receptor (BDKRB2), with helokinestatin-1 being the most potent antagonist. {ECO:0000269|PubMed:19837656}.; FUNCTION: [Natriuretic peptide]: exhibits hypotensive and vasodepressor activities, possibly by targeting natriureti... | Heloderma suspectum cinctum (Banded Gila monster) |
C6HCG7 | ARO1_AJECH | MGVPTKISILGRESIVADFGIWRNYVAKDLLSSCSSSTYILISDTNLTPLYLEGFQRSFEDAATNVSPKPRLLTYEIPPGESSKSRETKADIEDWMLARQPPCGRDTVIIALGGGVIGDLIGFVAATYMRGVRFVQVPTTLLAMVDSSIGGKTAIDTPNGKNLIGAIWQPQRIYLDMEFLNTLPEREFINGMAEVIKTAAISSEEKFAALERDAETILAAVKSKNTPERPRFSGIEETLKRTILSSAEFKAQVVTADEREGGLRNLLNFGHSIGHSIEAILAPQVLHGECVSIGMVKEAELARHLGILNNVSVSRISKCL... | 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:000476... | PF01761;PF01487;PF00275;PF08501;PF01202; | 3.40.50.1970;3.20.20.70;1.20.1090.10;3.65.10.10;3.40.50.10860;3.40.50.720;3.40.50.300; | Sugar phosphate cyclases superfamily, Dehydroquinate synthase family; EPSP synthase family; Shikimate kinase family; Type-I 3-dehydroquinase family; Shikimate dehydrogenase family | null | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_03143}. | CATALYTIC ACTIVITY: Reaction=7-phospho-2-dehydro-3-deoxy-D-arabino-heptonate = 3-dehydroquinate + phosphate; Xref=Rhea:RHEA:21968, ChEBI:CHEBI:32364, ChEBI:CHEBI:43474, ChEBI:CHEBI:58394; EC=4.2.3.4; Evidence={ECO:0000255|HAMAP-Rule:MF_03143}; CATALYTIC ACTIVITY: Reaction=3-dehydroquinate = 3-dehydroshikimate + H2O; Xr... | 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: st... | null | null | FUNCTION: The AROM polypeptide catalyzes 5 consecutive enzymatic reactions in prechorismate polyaromatic amino acid biosynthesis. {ECO:0000255|HAMAP-Rule:MF_03143}. | Ajellomyces capsulatus (strain H143) (Darling's disease fungus) (Histoplasma capsulatum) |
C6K2K4 | NETO2_RAT | MALEQLCAVLKVLLITVLVVEGIAVAQKTQDGQNIGIKHVPATQCGIWVRTSNGGHFASPNYPDSYPPNKECIYILEAAPRQRIELTFDERYYIEPSFECRFDHLEVRDGPFGFSPLIDRYCGMKSPALIRSTGRFMWIKFSSDEELEGLGFRAKYSFIPDPDFTYLGGILNPIPDCQFELSGADGIVRSSQVEQEEKTKPGQAVDCIWTIKATPKAKIYLRFLDYQMEHSNECKRNFVAVYDGSSAIENLKAKFCSTVANDVMLKTGVGVIRMWADEGSRLSRFRMLFTSFVEPPCTSSTFFCHSNMCINNSLVCNGVQ... | null | null | neurotransmitter receptor localization to postsynaptic specialization membrane [GO:0099645]; regulation of neurotransmitter receptor localization to postsynaptic specialization membrane [GO:0098696] | glutamatergic synapse [GO:0098978]; postsynaptic density [GO:0014069]; postsynaptic density membrane [GO:0098839]; synapse [GO:0045202] | ionotropic glutamate receptor binding [GO:0035255] | PF00431;PF00057; | 4.10.400.10;2.60.120.290; | null | PTM: N-glycosylated. {ECO:0000269|PubMed:19217376}. | SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Single-pass type I membrane protein {ECO:0000305}. | null | null | null | null | null | FUNCTION: Accessory subunit of neuronal kainate-sensitive glutamate receptors, GRIK2 and GRIK3. Increases kainate-receptor channel activity, slowing the decay kinetics of the receptors, without affecting their expression at the cell surface, and increasing the open probability of the receptor channels. Modulates the ag... | Rattus norvegicus (Rat) |
C6KEF6 | POLG_HKV1 | MMEGSNGFSSSLAGLSSSRSSLRLLTHLLSLPPPNRDARRHSGWYRSPPTLPVNVYLNEQFDNLCLAALRYPGCKLYPSVYTLFPDVSPFKIPQSIPAFAHLVQRQGLRRQGNPTTNIYGNGNEVTTDVGANGMSLPIAVGDMPTASSSEAPLGSNKGGSSTSPKSTSNGNVVRGSRYSKWWEPAAARALDRALDHAVDATDAVAGAASKGIKAGATKLSNKLAGSQTTALLALPGNIAGGAPSATVNANNTSISSQALLPSVNPYPSTPAVSLPNPDAPTQVGPAADRQWLVDTIPWSETTPPLTVFSGPKALTPGTYP... | 2.7.7.48; 3.4.22.28; 3.6.4.13 | null | DNA-templated transcription [GO:0006351]; protein complex oligomerization [GO:0051259]; proteolysis [GO:0006508]; suppression by virus of host mRNA export from nucleus [GO:0039522]; symbiont entry into host cell [GO:0046718]; symbiont-mediated suppression of host gene expression [GO:0039657]; viral RNA genome replicati... | host cell cytoplasmic vesicle membrane [GO:0044162]; host cell Golgi membrane [GO:0044178]; membrane [GO:0016020]; T=pseudo3 icosahedral viral capsid [GO:0039618] | ATP binding [GO:0005524]; ATP hydrolysis activity [GO:0016887]; cysteine-type endopeptidase activity [GO:0004197]; monoatomic ion channel activity [GO:0005216]; RNA binding [GO:0003723]; RNA helicase activity [GO:0003724]; RNA-dependent RNA polymerase activity [GO:0003968]; structural molecule activity [GO:0005198] | PF00680;PF00073;PF00910; | 1.20.960.20;2.60.120.20;3.30.70.270;2.40.10.10; | null | PTM: [Genome polyprotein]: Specific enzymatic cleavages by the viral protease in vivo yield a variety of precursors and mature proteins (By similarity). The leader protein-VP0 junction is cleaved by 3C proteinase (By similarity). The VP1/2A junction is cleaved by the protein 3CD in association with protein 2A (By simil... | SUBCELLULAR LOCATION: [Capsid protein VP0]: Virion {ECO:0000250|UniProtKB:O91464}. Host cytoplasm {ECO:0000250|UniProtKB:P12296}.; SUBCELLULAR LOCATION: [Capsid protein VP3]: Virion {ECO:0000250|UniProtKB:O91464}. Host cytoplasm {ECO:0000250|UniProtKB:P12296}.; SUBCELLULAR LOCATION: [Capsid protein VP1]: Virion {ECO:00... | 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=Selectiv... | null | null | null | null | FUNCTION: [Leader protein]: Required for viral RNA replication and viral RNA encapsidation (By similarity). Does not have any proteolytic activity (By similarity). {ECO:0000250|UniProtKB:O91464}.; FUNCTION: [Capsid protein VP1]: Forms an icosahedral capsid of pseudo T=3 symmetry with capsid proteins VP0 and VP3 (By sim... | Human klassevirus 1 (HKV-1) |
C6KEM4 | AADH2_MAIZE | MAPPQTIPRRGLFIGGAWREPCLGRRLPVVNPATEATIGDIPAGTAEDVEIAVAAARDAFSRDGGRHWSRAPGAVRANFLRAIAAKIKDRKSELALLETLDSGKPLDEASGDMDDVAACFEYYADLAEALDGKQQSPISLPMENFKSYVLKEPIGVVGLITPWNYPLLMATWKVAPALAAGCTTILKPSELASVSCLELGAICMEIGLPPGVLNIITGLGPEAGAPLSSHSHVDKVAFTGSTETGKRIMISAAQMVKPVSLELGGKSPLIVFDDIGDIDKAVEWTMFGIFANAGQVCSATSRLLLHEKIAKKFLDRLVAW... | 1.2.1.-; 1.2.1.19; 1.2.1.47; 1.2.1.54 | null | cellular detoxification of aldehyde [GO:0110095]; cellular response to anoxia [GO:0071454]; glycine betaine biosynthetic process from choline [GO:0019285] | peroxisome [GO:0005777] | 1-pyrroline dehydrogenase activity [GO:0033737]; 4-trimethylammoniobutyraldehyde dehydrogenase activity [GO:0047105]; aminobutyraldehyde dehydrogenase activity [GO:0019145]; betaine-aldehyde dehydrogenase activity [GO:0008802]; gamma-guanidinobutyraldehyde dehydrogenase activity [GO:0047107]; protein homodimerization a... | PF00171; | null | Aldehyde dehydrogenase family | null | null | CATALYTIC ACTIVITY: Reaction=4-aminobutanal + H2O + NAD(+) = 4-aminobutanoate + 2 H(+) + NADH; Xref=Rhea:RHEA:19105, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945, ChEBI:CHEBI:58264, ChEBI:CHEBI:59888; EC=1.2.1.19; Evidence={ECO:0000269|PubMed:23408433}; PhysiologicalDirection=left-to-right... | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=59 uM for 4-aminobutanal {ECO:0000269|PubMed:23408433}; KM=98 uM for 3-aminopropanal {ECO:0000269|PubMed:23408433}; KM=16 uM for 4-(trimethylamino)butanal {ECO:0000269|PubMed:23408433}; KM=11 uM for 4-guanidinobutanal {ECO:0000269|PubMed:23408433}; KM=86 uM for NAD... | PATHWAY: Amine and polyamine biosynthesis; betaine biosynthesis via choline pathway; betaine from betaine aldehyde: step 1/1. {ECO:0000305}. | null | null | FUNCTION: Dehydrogenase that catalyzes the oxidation of several aminoaldehydes (PubMed:23408433). Metabolizes and detoxifies aldehyde products of polyamine degradation to non-toxic amino acids (Probable). Catalyzes the oxidation of 4-aminobutanal and 3-aminopropanal to 4-aminobutanoate and beta-alanine, respectively (P... | Zea mays (Maize) |
C6KFA3 | AGRG6_DANRE | MISFISGRWWRWKFQNTLAVFLLLICLSTSVAQSCQSSTSCNVVLTDSQGSFTSPCYPNDYPPSQSCNWTIQAPAGFIVQITFLDFELEEAQGCIYDRVVVKTGTSDAKFCGLTANGLTLNSTGNVMEVFFNSDFSVQKKGFHISYKQVAVTLRNQKVTMPKSSKTILRVSNSISIPVLTAFTVCFEIARTAQKATETIFTLSDAAGTSILAFEKTSNGMELFIGASYCSVDNLLTSSDITATMKPLCLTWTKSSGLIGVYFGGHYFSSICSASQIYTLQSGGLLQIAGKGSSSVSVDDQNLDGFIYNFRLWDHAMLSSE... | null | null | adenylate cyclase-activating G protein-coupled receptor signaling pathway [GO:0007189]; cAMP-mediated signaling [GO:0019933]; cell surface receptor signaling pathway [GO:0007166]; ear development [GO:0043583]; G protein-coupled receptor signaling pathway [GO:0007186]; heart development [GO:0007507]; heart trabecula for... | plasma membrane [GO:0005886] | collagen binding [GO:0005518]; extracellular matrix binding [GO:0050840]; G protein-coupled receptor activity [GO:0004930]; laminin binding [GO:0043236] | PF00002;PF00431;PF01825;PF00354; | 2.60.120.200;2.60.220.50;1.20.1070.10;2.60.120.290; | G-protein coupled receptor 2 family, Adhesion G-protein coupled receptor (ADGR) subfamily | PTM: Autoproteolytically processed at the GPS region of the GAIN-B domain; this cleavage modulates receptor activity. {ECO:0000255|PROSITE-ProRule:PRU00098}. | SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:25118328}; Multi-pass membrane protein {ECO:0000255}. | null | null | null | null | null | FUNCTION: G-protein coupled receptor which is activated by type IV collagen, a major constituent of the basement membrane. Couples to G(i)-proteins as well as G(s)-proteins (PubMed:25118328). Essential for normal differentiation of promyelinating Schwann cells and for normal myelination of axons (PubMed:19745155). Also... | Danio rerio (Zebrafish) (Brachydanio rerio) |
C6KI89 | CTSG2_MOUSE | MVSRPAMSPVSPVWPRKPNLWAFWVLRLVLLLSLKSWAEDALQHCTWLLVLNKFEKVGLHLSKDRFQDHEPIDTVAKVFQKLTDSPIDPSENYLSFPYYLQINFSCPGQNIEELARKGHLMGMKPMVQINYMYSVNFYRWEMENVQILMEAAPMRSTGYCPAEAMCVLNWYTPMPFKNGSVVSSVDIYTNGIGPFVSKKRFYVNMNGFLKRDASGKSLFAIGYESLVLKSSHFRLSKSRPLWYTVNHAPVFILGGFYDEKSILFSDSNFQDYVLLELSIDSCWVGSFYCPILGFSATIHDAIATESTLFIRQNQLVYYFT... | null | null | cell differentiation [GO:0030154]; spermatogenesis [GO:0007283] | CatSper complex [GO:0036128]; motile cilium [GO:0031514]; sperm principal piece [GO:0097228] | null | PF15064; | null | CATSPERG family | null | SUBCELLULAR LOCATION: Cell projection, cilium, flagellum membrane {ECO:0000305}; Single-pass type I membrane protein {ECO:0000255}. | null | null | null | null | null | FUNCTION: Auxiliary component of the CatSper complex, a complex involved in sperm cell hyperactivation (PubMed:19516020, PubMed:34225353). Sperm cell hyperactivation is needed for sperm motility which is essential late in the preparation of sperm for fertilization (PubMed:19516020). {ECO:0000269|PubMed:19516020, ECO:00... | Mus musculus (Mouse) |
C6KIE6 | XLG2_ARATH | MAAVIRKLLPFPSPNPKRDNRESDDDDETSSGYRIEYSFASEYKGPLIANVPRALPVEVDQIPTALPVSFSSLRSGISYPVAPLVMTKDTKRPPDSGIEKKNGFVDSAAGSSVVLIGRDVVSGSSSSSSSKRLDVPEEVKSPADFRLSPSSPLSASAREEDHLDDDRVSDVGPRAVRFVEPFQSSECDESSYVSDGESIAATHRAERKGKRGSCYRCQLGNRFTEKEVCIVCDAKYCFNCVRRAMGAMPEGRKCQACIGYRIDESKRASLGKCSRMLKRHLTDSELRQVMNAEITCKANQLPSRLIIVNDKPLSEDELYT... | null | COFACTOR: Name=Ca(2+); Xref=ChEBI:CHEBI:29108; Evidence={ECO:0000269|PubMed:22232549}; | defense response to bacterium [GO:0042742]; G protein-coupled receptor signaling pathway [GO:0007186]; response to bacterium [GO:0009617] | nucleus [GO:0005634] | G-protein beta/gamma-subunit complex binding [GO:0031683]; GTP binding [GO:0005525]; GTPase activity [GO:0003924]; metal ion binding [GO:0046872] | PF00503; | 1.10.400.10;3.40.50.300; | G-alpha family, XLG subfamily | null | SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:17999646}. | null | null | null | null | null | FUNCTION: Guanine nucleotide-binding proteins (G proteins) are involved as modulators or transducers in various transmembrane signaling systems (By similarity). Binds GTP with specificity. Plays a role in the root morphogenesis by regulation of the cell proliferation. Acts as a positive regulator in resistance to patho... | Arabidopsis thaliana (Mouse-ear cress) |
C6KRL6 | ZHP3_CAEEL | MDFVHCNKCFNRKPPDGFFISSCFHIFCTKCAKADLAVCLICKKNVRLVRLDGNISSGIKIYFADPIKMVADSLAKIQKKIDFQQSTRDHLVKYLTKEKEKKRQMEVYFRTKGQEFDSQRKKLAEATAWIQMAEKKLQASEEERVKAEREIEECQAKLKSMTNLMSADTLGMNSQTPFPFSLAESQETAPSLVESSANSTFNMVSPLVSSPASSPNSINYNSFFENGSRTRPESLNEEAMFNTMLQSSGQSANANTSESSAFSVAFNNIFTPSRNNMGDSSMINKTTANQTIMDKTSMSLENWRQNRANSFGVHDISKRD... | null | null | chiasma assembly [GO:0051026]; embryo development ending in birth or egg hatching [GO:0009792]; homologous chromosome pairing at meiosis [GO:0007129]; meiotic chromosome segregation [GO:0045132]; protein sumoylation [GO:0016925]; reciprocal meiotic recombination [GO:0007131]; synaptonemal complex disassembly [GO:007019... | chromosome [GO:0005694]; synaptonemal complex [GO:0000795] | metal ion binding [GO:0046872]; SUMO transferase activity [GO:0019789] | PF14634; | null | null | null | SUBCELLULAR LOCATION: Chromosome {ECO:0000269|PubMed:15340062, ECO:0000269|PubMed:18949042, ECO:0000269|PubMed:29521627, ECO:0000269|PubMed:30379819}. Note=Co-localizes with zhp-4 to chromosomes from mitosis to early diakinesis in the germline (PubMed:29521627, PubMed:30379819). Co-localizes with syp-1, a component of ... | null | null | null | null | null | FUNCTION: Recruited co-dependently with zhp-4 to the synaptonemal complex between homologous chromosome pairs to regulate the formation and number of crossover events between homologs during meiotic recombination (PubMed:15340062, PubMed:18949042, PubMed:29521627, PubMed:30379819). In the early stages of pachytene, in ... | Caenorhabditis elegans |
C6KRN1 | SAO1_CAEEL | MHKNGNNGPVIDTKWHYLGPDSEKYGPYMSKDMLFWLQAGYFNDGLQLKTENEPNYHTLGEWSQLLGTHPFSMPVHSLDATIAQMNSMRPHGAMMMVPPGLQNQFQPPMPMRFPPFLPMPLLHQMNQNGPPMGAQMHSQPPSEPIDAGSLSHTPDSENETRLNEQTLQQPPSWLIALGLAGHGRKPHHHQQILAHQHIPQMQHANVATDQVVMKSVECQTEPVEISKEQASRVLSELLGQMVIIN | null | null | negative regulation of Notch signaling pathway [GO:0045746]; Notch signaling pathway [GO:0007219]; regulation of protein deneddylation [GO:0060625] | cell cortex [GO:0005938]; cleavage furrow [GO:0032154]; cytoplasm [GO:0005737] | WD40-repeat domain binding [GO:0071987] | PF02213; | 3.30.1490.40; | null | null | null | null | null | null | null | null | FUNCTION: Involved in negative regulation of early and late embryonic Notch signaling. {ECO:0000269|PubMed:22209900}. | Caenorhabditis elegans |
C6KSX0 | PF12_PLAF7 | MIKLSKKYCLGISFVLYILLSVCEGHKNLTCDFNDVYKLEFHPNQQTSVTKLCNLTPNVLEKVTIKCGSDKLNYNLYPPTCFEEVYASRNMMHLKKIKEFVIGSSMFMRRSLTPNKINEVSFRIPPNMMPEKPIYCFCENKKTITINGSNGNPSSKKDIINRGIVEIIIPSLNEKVKGCDFTTSESTIFSKGYSINEISNKSSNNQQDIVCTVKAHANDLIGFKCPSNYSVEPHDCFVSAFNLSGKNENLENKLKLTNIIMDHYNNTFYSRLPSLISDNWKFFCVCSKDNEKKLVFTVEASISSSNTKLASRDNTYQDYI... | null | null | symbiont entry into host [GO:0044409] | apical part of cell [GO:0045177]; cell surface [GO:0009986]; plasma membrane [GO:0005886]; side of membrane [GO:0098552]; symbiont-containing vacuolar space [GO:0020004] | null | PF07422; | 2.60.40.2860; | null | PTM: Processed into a soluble form. {ECO:0000269|PubMed:22848665}. | SUBCELLULAR LOCATION: [Merozoite surface protein P12]: Cell surface. Cell membrane {ECO:0000305}; Lipid-anchor, GPI-anchor {ECO:0000305}. Note=Present on the surface of merozoite. {ECO:0000269|PubMed:22848665}.; SUBCELLULAR LOCATION: [Merozoite surface protein P12, processed form]: Cell surface. Cell membrane. Note=She... | null | null | null | null | null | null | Plasmodium falciparum (isolate 3D7) |
C6KT50 | PDX1_PLAF7 | MENHKDDAVLLKHGWCEMLKGGVIMDVKSVEQAKIAEEAGAIGVMVLENIPSELRNKEGVARSVDPSKVEEIKKCVSINVLAKVRIGHFVEAQILEELKIDMIDESEVLTIADEMHHIDKHKFKTPFVCGCTNLGEALRRISEGASMIRTKGEAGTGNIIEAIKHIRTVNNEIKYLCSLSDSEVYHFAKKINAPIDLVLLTKKLKRLPVVNFAAGGVATPADAAMCMQLGMDGVFVGSGIFESENPRKMAASIVSAVSNFNNPKILLDVSMNLGKAMCGSTRVSDKWKNKNEEHTKFLTPQ | 4.3.3.6 | null | amino acid metabolic process [GO:0006520]; pyridoxal phosphate biosynthetic process [GO:0042823]; pyridoxine biosynthetic process [GO:0008615]; response to singlet oxygen [GO:0000304]; vitamin B6 biosynthetic process [GO:0042819] | cytosol [GO:0005829] | amine-lyase activity [GO:0016843]; catalytic activity [GO:0003824]; glutaminase activity [GO:0004359]; identical protein binding [GO:0042802]; pyridoxal 5'-phosphate synthase (glutamine hydrolysing) activity [GO:0036381] | PF01680; | 3.20.20.70; | PdxS/SNZ family | null | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:16339145}. | CATALYTIC ACTIVITY: Reaction=aldehydo-D-ribose 5-phosphate + D-glyceraldehyde 3-phosphate + L-glutamine = H(+) + 3 H2O + L-glutamate + phosphate + pyridoxal 5'-phosphate; Xref=Rhea:RHEA:31507, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:29985, ChEBI:CHEBI:43474, ChEBI:CHEBI:58273, ChEBI:CHEBI:58359, ChEBI:CHEBI:5... | null | PATHWAY: Cofactor biosynthesis; pyridoxal 5'-phosphate biosynthesis. | null | null | FUNCTION: Catalyzes the formation of pyridoxal 5'-phosphate from ribose 5-phosphate (RBP), glyceraldehyde 3-phosphate (G3P) and ammonia. The ammonia is provided by Pdx2. Can also use ribulose 5-phosphate and dihydroxyacetone phosphate as substrates, resulting from enzyme-catalyzed isomerization of RBP and G3P, respecti... | Plasmodium falciparum (isolate 3D7) |
C6KT68 | FENR_PLAF7 | MKIRFVFILSVLISGVCCISKNVSRRVANRMTAHSRFLFVHDKYKRNKNFKLKNNKEENNFINLYTVKNPLKCKIVDKINLVRPNSPNEVYHLEINHNGLFKYLEGHTCGIIPYYNELDNNPNNQINKDHNIINTTNHTNHNNIALSHIKKQRCARLYSISSSNNMENLSVAIKIHKYEQTENAPNITNYGYCSGFIKNLKINDDIYLTGAHGYFNLPNDAIQKNTNFIFIATGTGISPYISFLKKLFAYDKNNLYNRNSNYTGYITIYYGVYNEDSILYLNELEYFQKMYPNNINIHYVFSYKQNSDATSFYVQDEIYK... | 1.18.1.2 | COFACTOR: Name=FAD; Xref=ChEBI:CHEBI:57692; Evidence={ECO:0000269|PubMed:17251200, ECO:0000269|PubMed:17258767, ECO:0000269|PubMed:19736991}; | electron transport chain [GO:0022900]; regulation of isopentenyl diphosphate biosynthetic process, methylerythritol 4-phosphate pathway [GO:0010322] | apicoplast [GO:0020011]; chloroplast thylakoid membrane protein complex [GO:0098807] | electron transfer activity [GO:0009055]; FAD binding [GO:0071949]; ferredoxin-NAD(P) reductase activity [GO:0008937]; ferredoxin-NADP+ reductase activity [GO:0004324]; identical protein binding [GO:0042802]; NADPH dehydrogenase activity [GO:0003959] | PF00175; | 3.40.50.80;2.40.30.10; | Ferredoxin--NADP reductase type 1 family | null | SUBCELLULAR LOCATION: Plastid, apicoplast {ECO:0000305}. | CATALYTIC ACTIVITY: Reaction=H(+) + NADP(+) + 2 reduced [2Fe-2S]-[ferredoxin] = NADPH + 2 oxidized [2Fe-2S]-[ferredoxin]; Xref=Rhea:RHEA:20125, Rhea:RHEA-COMP:10000, Rhea:RHEA-COMP:10001, ChEBI:CHEBI:15378, ChEBI:CHEBI:33737, ChEBI:CHEBI:33738, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349; EC=1.18.1.2; Evidence={ECO:0000305|Pu... | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=36 uM for NADPH {ECO:0000269|PubMed:17258767, ECO:0000269|PubMed:19736991}; KM=720 uM for NADH {ECO:0000269|PubMed:17258767}; | null | null | null | FUNCTION: May play a role in the terminal step of the DOXP/MEP pathway for isoprenoid precursor biosynthesis. {ECO:0000269|PubMed:16289098}. | Plasmodium falciparum (isolate 3D7) |
C6KTB8 | PK4_PLAF7 | MCNFIKKGIRFNGDKYIFLFDIFIKKYLLNVFVANILWEEENNICFLNRLKNKRKKSILFLKEEYLRYLMILNKEEKNKKKRLKKIYECIKVFSIKEFRWLINKLEIIYFYFFCHLLLLCIFQNIFLLTYMSKEYFLKNIHDYMINILSNDIKFNTCIEFTHNDKYEQKCITMAYYDFLLNKKGKLKKRNKYYDIKNIEPLTGKDKNLYSYYNFSPFFPMSSSDIINVNTNDKISNILWNDKYIDTLNHVNMKKKDIPLNIHSNNILMNNYAYRKYVRSYMIKKRINDLILYNLKNIFEKINNIEKLTNINNFMNFKKEY... | 2.7.11.1 | null | negative regulation of translation [GO:0017148]; peptidyl-serine phosphorylation [GO:0018105]; protein phosphorylation [GO:0006468]; regulation of translational initiation by eIF2 alpha phosphorylation [GO:0010998] | cytoplasm [GO:0005737]; cytosol [GO:0005829]; endoplasmic reticulum membrane [GO:0005789]; nucleus [GO:0005634] | ATP binding [GO:0005524]; elongation factor-2 kinase activity [GO:0004686]; eukaryotic translation initiation factor 2alpha kinase activity [GO:0004694]; protein serine kinase activity [GO:0106310] | PF00069; | 1.10.510.10; | Protein kinase superfamily, Ser/Thr protein kinase family, GCN2 subfamily | PTM: Auto-phosphorylated. {ECO:0000269|PubMed:29241041}. | SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000250|UniProtKB:A0A509AMC3}; Multi-pass membrane protein {ECO:0000255}. | CATALYTIC ACTIVITY: Reaction=ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-[protein]; Xref=Rhea:RHEA:17989, Rhea:RHEA-COMP:9863, Rhea:RHEA-COMP:11604, ChEBI:CHEBI:15378, ChEBI:CHEBI:29999, ChEBI:CHEBI:30616, ChEBI:CHEBI:83421, ChEBI:CHEBI:456216; EC=2.7.11.1; Evidence={ECO:0000269|PubMed:22355110, ECO:000026... | null | null | null | null | FUNCTION: During the asexual blood stage, phosphorylates translation factor eIF2alpha in late schizonts resulting in protein translation inhibition (PubMed:22355110, PubMed:29241041). Plays a role in trophozoite differentiation into schizonts (PubMed:29241041). {ECO:0000269|PubMed:22355110, ECO:0000269|PubMed:29241041}... | Plasmodium falciparum (isolate 3D7) |
C6XZB6 | HEPB_PEDHD | MKRQLYLYVIFVVVELMVFTTKGYSQTKADVVWKDVDGVSMPIPPKTHPRLYLREQQVPDLKNRMNDPKLKKVWADMIKMQEDWKPADIPEVKDFRFYFNQKGLTVRVELMALNYLMTKDPKVGREAITSIIDTLETATFKPAGDISRGIGLFMVTGAIVYDWCYDQLKPEEKTRFVKAFVRLAKMLECGYPPVKDKSIVGHASEWMIMRDLLSVGIAIYDEFPEMYNLAAGRFFKEHLVARNWFYPSHNYHQGMSYLNVRFTNDLFALWILDRMGAGNVFNPGQQFILYDAIYKRRPDGQILAGGDVDYSRKKPKYYTM... | 4.2.2.7; 4.2.2.8 | null | heparin catabolic process [GO:0030211] | periplasmic space [GO:0042597] | heparin binding [GO:0008201]; heparin lyase activity [GO:0047488]; heparin-sulfate lyase activity [GO:0015021]; metal ion binding [GO:0046872] | PF16332;PF07940;PF18675; | 2.60.40.2750;2.70.98.70;1.50.10.100; | Polysaccharide lyase 12 family | null | SUBCELLULAR LOCATION: Periplasm {ECO:0000269|PubMed:8702264}. | CATALYTIC ACTIVITY: Reaction=Elimination of sulfate, appears to act on linkages between N-acetyl-D-glucosamine and uronate. Product is an unsaturated sugar.; EC=4.2.2.8; Evidence={ECO:0000269|PubMed:8702264}; CATALYTIC ACTIVITY: Reaction=Eliminative cleavage of polysaccharides containing (1->4)-linked D-glucuronate or ... | null | null | null | null | FUNCTION: Cleaves both heparin and heparan sulfate glycosaminoglycans through a beta-elimination mechanism. Cleaves heparin at alpha-D-GlcNp2S6S(1->4) alpha-L-IdoAp2S and heparan sulfate at alpha-D-GlcNp2Ac(or 2S)6OH(1->4)beta-D-GlcAp. {ECO:0000269|PubMed:8702264}. | Pedobacter heparinus (strain ATCC 13125 / DSM 2366 / CIP 104194 / JCM 7457 / NBRC 12017 / NCIMB 9290 / NRRL B-14731 / HIM 762-3) |
C6Y4D0 | DPB3_SCHPO | MEKTYGKTVLPLSRVKRIIKQDEDVHYCSNASALLISVATELFVEKLATEAYQLAKLQKRKGIRYRDVEDVVRKDDQFEFLSDLFSI | null | null | CMG complex assembly [GO:0140529]; DNA strand elongation involved in mitotic DNA replication [GO:1902983]; DNA-templated DNA replication [GO:0006261]; heterochromatin formation [GO:0031507]; mitotic DNA replication initiation [GO:1902975]; regulation of DNA-templated transcription [GO:0006355] | epsilon DNA polymerase complex [GO:0008622]; nuclear replication fork [GO:0043596]; nucleus [GO:0005634] | protein heterodimerization activity [GO:0046982]; transcription cis-regulatory region binding [GO:0000976] | PF00808; | 1.10.20.10; | null | null | SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:P27344}. | null | null | null | null | null | FUNCTION: As accessory component of the DNA polymerase epsilon (DNA polymerase II) participates in chromosomal DNA replication. It is required during synthesis of the leading and lagging DNA strands at the replication fork and binds at/or near replication origins and moves along DNA with the replication fork. It has 3'... | Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast) |
C6ZJZ3 | IF4E1_SOYBN | MVVEDTQKSVITEDQYPSRVVSDNNNDDDDDDLEEGEIPVDGEDSGATATTKPPAALARNPHPLENSWTFWFDNPSSKSKQAAWGSSIRPIYTFATVEEFWSIYNNIHHPSKLGLGADFHCFKHKIEPKWEDPICANGGKWTMTFPRGKSDTSWLYTLLAMIGEQFDHGDEICGAVVNVRSRQDKIAIWTKNASNEAAQVSIGKQWKEFLDYNDTIGFIFHEDAKKLDRGAKNKYVV | null | null | defense response to virus [GO:0051607]; response to virus [GO:0009615]; translational initiation [GO:0006413] | cytoplasm [GO:0005737]; eukaryotic translation initiation factor 4F complex [GO:0016281]; nucleus [GO:0005634] | RNA 7-methylguanosine cap binding [GO:0000340]; RNA binding [GO:0003723]; translation initiation factor activity [GO:0003743] | PF01652; | 3.30.760.10; | Eukaryotic initiation factor 4E family | PTM: According to the redox status, the Cys-135-Cys-173 disulfide bridge may have a role in regulating protein function by affecting its ability to bind capped mRNA. {ECO:0000250|UniProtKB:P29557}. | SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:31860775}. Cytoplasm {ECO:0000269|PubMed:31860775}.; SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:31860775}. Cytoplasm {ECO:0000269|PubMed:31860775}. Note=(Microbial infection) Binds to potyvirus viral genome-linked protein (VPg) in the nucleus and with potyvirus n... | null | null | null | null | null | FUNCTION: Component of the protein complex eIF4F, which is involved in the recognition of the mRNA cap, ATP-dependent unwinding of 5'-terminal secondary structure and recruitment of mRNA to the ribosome (By similarity). Recognizes and binds the 7-methylguanosine-containing mRNA cap during an early step in the initiatio... | Glycine max (Soybean) (Glycine hispida) |
C7A2A0 | BALDH_ANTMA | MAAHRFSSLLSRSVPLLSRGGKQSYLGRGVYRYGTAAAAALEEPIKPPVSVQYDKLLINGQFVDAASGKTFPTLDPRSGEVIAHVAEGDAEDINRAVAAARKAFDEGPWPKMPAYERQKIMLRFADLVEKHNDEVAALEAWDSGKPYEQCAQVEIPMFVRLFRYYAGWADKIHGLTIPADGPHHVQTLHEPIGVAGQIIPWNFPLVMFGWKVGPALACGNSVVLKTAEQTPLSALLVSKLFHEAGLPEGVLNIVSGFGPTAGAALCRHMDVDKLAFTGSTETGKIVLELSAKSNLKPVTLELGGKSPFIVCEDADVDKAV... | 1.2.1.28; 1.2.1.3; 1.2.1.39 | null | circadian rhythm [GO:0007623]; green leaf volatile biosynthetic process [GO:0010597] | mitochondrion [GO:0005739] | acetaldehyde dehydrogenase (acetylating) activity [GO:0008774]; aldehyde dehydrogenase (NAD+) activity [GO:0004029]; benzaldehyde dehydrogenase (NAD+) activity [GO:0018479]; glyceraldehyde-3-phosphate dehydrogenase (NAD+) (non-phosphorylating) activity [GO:0043878]; phenylacetaldehyde dehydrogenase activity [GO:0008957... | PF00171; | null | Aldehyde dehydrogenase family | null | SUBCELLULAR LOCATION: Mitochondrion {ECO:0000269|PubMed:19292760}. | CATALYTIC ACTIVITY: Reaction=an aldehyde + H2O + NAD(+) = a carboxylate + 2 H(+) + NADH; Xref=Rhea:RHEA:16185, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:17478, ChEBI:CHEBI:29067, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945; EC=1.2.1.3; Evidence={ECO:0000269|PubMed:19292760}; PhysiologicalDirection=left-to-right; Xref=... | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=1.37 uM for benzaldehyde {ECO:0000269|PubMed:19292760}; KM=2.01 uM for acetaldehyde {ECO:0000269|PubMed:19292760}; KM=5.35 uM for phenylacetaldehyde {ECO:0000269|PubMed:19292760}; Vmax=1.32 nmol/sec/mg enzyme with benzaldehyde as substrate {ECO:0000269|PubMed:19292... | PATHWAY: Aromatic compound metabolism. {ECO:0000269|PubMed:19292760}. | BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 8. Active in a broad range of pH varying from 6 to 9. {ECO:0000269|PubMed:19292760}; | null | FUNCTION: Component of the floral volatile benzenoid/phenylpropanoid (FVBP) biosynthetic pathway (PubMed:19292760). Catalyzes the oxidation of benzaldehyde to benzoic acid (BA) (PubMed:19292760). Capable of oxidizing a broad spectrum of aliphatic aldehydes; increased carbon chain length results in a decrease in its eff... | Antirrhinum majus (Garden snapdragon) |
C7AE94 | FAOMT_VITVI | MSSSSHRGILKTEALTKYLLETSAYPREHEQLKGLREATVEKHKYWSLMNVPVDEGLFISMLLKIMNAKKTIELGVFTGYSLLATALALPQDGKIIAVDPDKEAYQTGVPFIKKAGVEHKINFIQSDAMSVLNDLIADGKEEGTLDFAMVDADKENYLNYHELLLKLVRVGGIIAYDNTLWFGSVARSEEEEMMDFERAGRVHLMKLNKFLASDPRVELSHLSIGDGVALCRRLY | 2.1.1.267 | COFACTOR: Name=a divalent metal cation; Xref=ChEBI:CHEBI:60240; Evidence={ECO:0000269|PubMed:19525322, ECO:0000269|PubMed:20580386}; | anthocyanin-containing compound biosynthetic process [GO:0009718]; cyanidin 3-O-glucoside biosynthetic process [GO:0033485]; delphinidin 3-O-glucoside biosynthetic process [GO:0033486]; methylation [GO:0032259]; pigmentation [GO:0043473] | cytoplasm [GO:0005737] | laricitrin 5'-O-methyltransferase activity [GO:0070448]; metal ion binding [GO:0046872]; myricetin 3'-O-methyltransferase activity [GO:0033799]; O-methyltransferase activity [GO:0008171] | PF01596; | 3.40.50.150; | Class I-like SAM-binding methyltransferase superfamily, Cation-dependent O-methyltransferase family, CCoAMT subfamily | null | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:19525322}. | CATALYTIC ACTIVITY: Reaction=S-adenosyl-L-methionine + a 3'-hydroxyflavonoid = S-adenosyl-L-homocysteine + a 3'-methoxyflavonoid.; EC=2.1.1.267; Evidence={ECO:0000269|PubMed:19525322, ECO:0000269|PubMed:20580386}; CATALYTIC ACTIVITY: Reaction=S-adenosyl-L-methionine + a 5'-hydroxy-3'-methoxyflavonoid = S-adenosyl-L-hom... | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=43 uM for cyanidin 3-glucoside {ECO:0000269|PubMed:19525322, ECO:0000269|PubMed:20580386}; KM=7.6 uM for cyanidin 3-glucoside {ECO:0000269|PubMed:19525322, ECO:0000269|PubMed:20580386}; KM=44 uM for delphinidin 3-glucoside {ECO:0000269|PubMed:19525322, ECO:0000269|... | PATHWAY: Pigment biosynthesis; anthocyanin biosynthesis. {ECO:0000269|PubMed:19525322, ECO:0000269|PubMed:20580386}. | BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 8.0-8.8. {ECO:0000269|PubMed:19525322, ECO:0000269|PubMed:20580386}; | BIOPHYSICOCHEMICAL PROPERTIES: Temperature dependence: Optimum temperature is 49 degrees Celsius. {ECO:0000269|PubMed:19525322, ECO:0000269|PubMed:20580386}; | FUNCTION: Mediates O-methylation of anthocyanins. Anthocyanins are major pigments in grapes: at ripening initiation in red grapevine berries, the exocarp turns color from green to red and then to purple due to the accumulation and extent of methylation of anthocyanins. Catalyzes both 3' and 5' O-methylation of anthocya... | Vitis vinifera (Grape) |
C7AJA4 | TUT7_TRYBB | MNVAKREFIRGMMAHYRASLPPPEHSVVIHELQKRVLDIGMLAVNKAHVELFGSHVSGFCTPHSDADISLTYRNFSPWLQGMERVDEQNNKRMTRFGKEASAMGMEDVRYIRARIPVVQFTDGVTGIHCDVSIGNIGGVENSKILCAIRQVFPDFYGAYIHLVKAWGKAREVIAPERSTFNSFTVTTMALMVLQELGLLPVFSKPTGEFGELTVADAEMLLQEFKLPPIYDSLHDDDEKLGEAVFFCLQRFAEYYAKYDFSAGTVSLIHPRRHRTVYERVVRRHLELLGSRKRLEWEKHIAEHKEDGPLDENDFSASMQN... | 2.7.7.52 | COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000269|PubMed:19465686}; Note=Binds 1 Mg(2+) per subunit. {ECO:0000269|PubMed:20403364}; | mRNA processing [GO:0006397]; RNA 3' uridylation [GO:0071076] | mitochondrial matrix [GO:0005759]; mitochondrion [GO:0005739] | metal ion binding [GO:0046872]; nucleotide binding [GO:0000166]; RNA uridylyltransferase activity [GO:0050265] | null | 1.10.1410.10;3.30.460.10; | DNA polymerase type-B-like family | null | SUBCELLULAR LOCATION: Mitochondrion matrix {ECO:0000269|PubMed:19465686}. | CATALYTIC ACTIVITY: Reaction=RNA(n) + UTP = diphosphate + RNA(n)-3'-uridine ribonucleotide; Xref=Rhea:RHEA:14785, Rhea:RHEA-COMP:14527, Rhea:RHEA-COMP:17348, ChEBI:CHEBI:33019, ChEBI:CHEBI:46398, ChEBI:CHEBI:140395, ChEBI:CHEBI:173116; EC=2.7.7.52; Evidence={ECO:0000269|PubMed:19465686, ECO:0000269|PubMed:20403364}; | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=3.6 uM for UTP (with 6(U) single-stranded RNA as substrate) {ECO:0000269|PubMed:19465686}; KM=1 uM for UTP (with double-stranded RNA as substrate) {ECO:0000269|PubMed:19465686}; Note=kcat is 0.18 min(-1) with UTP and 6(U) single-stranded RNA as substrates (PubMed:1... | null | null | null | FUNCTION: Terminal uridylyltransferase which, as part of the mitochondrial RNA editing core-like complex (RECC-like), is involved in the post-transcriptional editing of mitochondrial RNA, a process involving the addition and deletion of uridine (U) nucleotides in the pre-mRNA (PubMed:19465686). Specifically, catalyzes ... | Trypanosoma brucei brucei |
C7ASJ5 | BGAL2_ARTSP | MGKRFPSGWFSPRVHPPRRQRSPMTNQATPGTASVWNNIEGIGFGGDYNPEQWPVSVRLEDLELMQEAGVNFLSVGIFSWALLEPAEGQYDFGWLDDVMDNLHGIGVKVALATATAAPPAWLVRKHPEILPVTADGTTLGPGSRRHYTPSSAVYRKYAAGITRVLAERYKDHPALALWHVDNELGCHVSEFYGEEDAAAFRLWLERRYGTIDALNAAWGTAFWSQHYGSFEEILPPGVAPSTLNPGQQLDFQRFNSWALMDYYRSLVAVLREVTPAVPCTTNLMASSATKSMDYFSWAKDLDVIANDHYLVAADPERHIE... | 3.2.1.23 | null | galactose metabolic process [GO:0006012] | beta-galactosidase complex [GO:0009341] | beta-galactosidase activity [GO:0004565] | PF02449;PF08533;PF08532; | 3.40.50.880;3.20.20.80;2.60.40.1180; | Glycosyl hydrolase 42 family | null | null | CATALYTIC ACTIVITY: Reaction=Hydrolysis of terminal non-reducing beta-D-galactose residues in beta-D-galactosides.; EC=3.2.1.23; Evidence={ECO:0000269|PubMed:19631003}; | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=5.75 mM for ONPG (at 10 degrees Celsius) {ECO:0000269|PubMed:19631003}; KM=4.86 mM for ONPG (at 20 degrees Celsius) {ECO:0000269|PubMed:19631003}; KM=3.46 mM for ONPG (at 30 degrees Celsius) {ECO:0000269|PubMed:19631003}; KM=3.15 mM for ONPG (at 40 degrees Celsius)... | null | BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 6.5 with ONPG as substrate. Over 90% of activity in the pH range 6.5-8.5. Highly efficient at pH range 4.5-9.5. {ECO:0000269|PubMed:19631003}; | BIOPHYSICOCHEMICAL PROPERTIES: Temperature dependence: Optimum temperature is 50 degrees Celsius with ONPG as substrate. Active at 4-8 degrees Celsius. 60% of the maximum activity is detected at 25 degrees Celsius and 15% at 0 degrees Celsius. Over 50% activity at 30 degrees Celsius. {ECO:0000269|PubMed:19631003}; | FUNCTION: Hydrolyzes p-nitrophenyl-beta-D-galactopyranoside (PNPG), o-nitrophenyl-beta-D-galactopyranoside (ONPG) and chromogen 5-bromo-4-chloro-3-indolyl-beta-D-galactopyranoside (X-gal), with highest activity against PNPG. Also acts on p-nitrophenyl-beta-D-glucopyranoside (PNPGlu) and o-nitrophenyl-beta-D-glucopyrano... | Arthrobacter sp |
C7AU21 | D27_ORYSJ | METTTLVLLLPHGGAGGVRPAAAATAKRSYVMRRCCSTVRAVMARPQEAPASAPAKKTETAAMMSTVQTETAAAPPATVYRDSWFDKLAIGYLSRNLQEASGLKNEKDGYESLIDAALAISRIFSLDKQSEIVTQALERALPSYILTMIKVMMPPSRFSREYFAAFTTIFFPWLVGPCEVMESEVEGRKEKNVVYIPKCRFLESTNCVGMCTNLCKIPCQKFIQDSLGMKVYMSPNFEDMSCEMIFGQQPPEDDPALKQPCFRTKCVAKQNHGVNCSI | 5.2.1.14 | COFACTOR: Name=Fe cation; Xref=ChEBI:CHEBI:24875; Evidence={ECO:0000269|PubMed:19470589}; Note=Recombinant protein contains about 1.7 mole of iron per mole of protein. {ECO:0000269|PubMed:19470589}; | secondary shoot formation [GO:0010223]; strigolactone biosynthetic process [GO:1901601] | chloroplast [GO:0009507] | beta-carotene isomerase activity [GO:0106365]; cis-trans isomerase activity [GO:0016859]; iron ion binding [GO:0005506] | PF13225; | null | null | null | SUBCELLULAR LOCATION: Plastid, chloroplast {ECO:0000269|PubMed:19470589}. | CATALYTIC ACTIVITY: Reaction=all-trans-beta-carotene = 9-cis-beta-carotene; Xref=Rhea:RHEA:34455, ChEBI:CHEBI:17579, ChEBI:CHEBI:67188; EC=5.2.1.14; Evidence={ECO:0000269|PubMed:22422982}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:34456; Evidence={ECO:0000269|PubMed:22422982}; | null | null | null | null | FUNCTION: Involved in strigolactones biosynthesis by catalyzing the isomerization of the C9-C10 double bond in all-trans-beta-carotene leading to 9-cis-beta-carotene and providing the substrate for CCD7. Strigolactones are hormones that inhibit tillering and shoot branching through the MAX-dependent pathway, contribute... | Oryza sativa subsp. japonica (Rice) |
C7B178 | VPY_PETHY | MDRLLSLEPSNVVTIRLEPGQKCSGVLTLRNVMYTMPVAFRLQPLNKIRYSIRPQSGIISPLTTITLEIIYHLPPNTTLPDSFPHCDDSFLLHSVVAPGATAKDTSSTLDMVPSDWFTTKRKQVFIDSAIKIMFVGSPVLCYLVRKGYMDEIREVLEKSDTTWKSVDSVNFEGQTLLHLAISQGRPDLVQLLLEFGPNIEAHSRSCSSPLEAASATGEALIVELLLAKKASTERTEFSASGPIHLAAGNGHLEVLKLLLLKGANVNSLTKDGNTALHLAVEERRRDCARLLLANGARADICSTGNGDTPLHIAAGLGDEH... | null | null | arbuscular mycorrhizal association [GO:0036377]; negative regulation of canonical Wnt signaling pathway [GO:0090090]; positive regulation of JNK cascade [GO:0046330]; protein targeting to chloroplast [GO:0045036]; response to inorganic substance [GO:0010035]; response to symbiotic fungus [GO:0009610] | cytosol [GO:0005829]; nucleus [GO:0005634]; plasma membrane [GO:0005886] | chloroplast targeting sequence binding [GO:0030941] | PF00023;PF12796;PF13857;PF00635; | 1.25.40.20;2.60.40.10; | null | null | SUBCELLULAR LOCATION: Cytoplasm, cytosol {ECO:0000269|PubMed:20804456}. Nucleus {ECO:0000269|PubMed:20804456}. Cell membrane {ECO:0000250|UniProtKB:D3J162}; Peripheral membrane protein {ECO:0000305}; Cytoplasmic side {ECO:0000305}. Note=Associated with mobile spherical structures that are associated with the tonoplast ... | null | null | null | null | null | FUNCTION: Required for arbuscular mycorrhizal (AM) symbiosis with AM fungi (e.g. Glomus intraradices, G. mosseae and Gigaspora margarita) both during fungal passage across root epidermis and for arbuscule formation in cortical cells; this symbiosis promotes phosphorus (P) and copper (Cu) uptake (PubMed:17573800, PubMed... | Petunia hybrida (Petunia) |
C7BKP9 | PATOX_PHOAA | MKGIEGVIMLSHDILPEKLLVSEKKHENVGSYFSDDIGEQSEQTEVSHFNLSLDDAFDIYADISIENQQELKNKDNNTNIWSSLGRGDDDHNLKKIINDAFKEKLPQLMEYRRKGYNVIGLDKEGIKKLEGMLKAVPPEIQQPTMKNLYSAAQELLNTLKQHPLLPENQDMIQQSNLVIRNLSDALEAINAVSKVNQVEWWEEVHKTNKAQSDRLIAATLEELFFKVKDKRLPGSNDDYCQQEREETERKIKDLLLYDGYQLTAEHFKFGRLRKSLLAESRVTRLKLAEYLEKKSVGILTAARDAKMYAMKILLAQTRNN... | 2.4.1.-; 3.5.1.44 | COFACTOR: Name=a divalent metal cation; Xref=ChEBI:CHEBI:60240; Evidence={ECO:0000269|PubMed:24141704}; Note=A Ca(2+) ion is seen in the structure. {ECO:0000269|PubMed:24141704}; | mannosyl-inositol phosphorylceramide biosynthetic process [GO:0051999]; symbiont-mediated perturbation of host Rho signal transduction [GO:0044083] | extracellular region [GO:0005576]; host cell plasma membrane [GO:0020002]; membrane [GO:0016020] | calcium ion binding [GO:0005509]; mannosyltransferase activity [GO:0000030]; protein N-acetylglucosaminyltransferase activity [GO:0016262]; protein-glutamine glutaminase activity [GO:0050568]; toxin activity [GO:0090729] | PF04488;PF15645; | 3.90.550.20;3.10.670.10; | null | null | SUBCELLULAR LOCATION: Secreted {ECO:0000305}. Host cell membrane {ECO:0000269|PubMed:25782990}; Peripheral membrane protein {ECO:0000269|PubMed:25782990}; Cytoplasmic side {ECO:0000269|PubMed:25782990}. Note=Associates with the negatively charged inner leaflet of the plasma membrane via interaction with phosphatidylser... | CATALYTIC ACTIVITY: Reaction=L-tyrosyl-[protein] + UDP-N-acetyl-alpha-D-glucosamine = H(+) + O-(N-acetyl-alpha-D-glucosaminyl)-L-tyrosyl-[protein] + UDP; Xref=Rhea:RHEA:51536, Rhea:RHEA-COMP:10136, Rhea:RHEA-COMP:13016, ChEBI:CHEBI:15378, ChEBI:CHEBI:46858, ChEBI:CHEBI:57705, ChEBI:CHEBI:58223, ChEBI:CHEBI:134208; Evid... | null | null | null | null | FUNCTION: Toxin that acts on host cells by modifying Rho proteins by tyrosine GlcNAcylation and heterotrimeric G alpha proteins by deamidation. Catalyzes the mono-O-GlcNAcylation of small GTPases of the Rho family (RhoA, RhoB, RhoC, Rac1, Rac2, Rac3, Cdc42) in eukaryotic host cells at the conserved tyrosine residue loc... | Photorhabdus asymbiotica subsp. asymbiotica (strain ATCC 43949 / 3105-77) (Xenorhabdus luminescens (strain 2)) |
C7C422 | BLAN1_KLEPN | MELPNIMHPVAKLSTALAAALMLSGCMPGEIRPTIGQQMETGDQRFGDLVFRQLAPNVWQHTSYLDMPGFGAVASNGLIVRDGGRVLVVDTAWTDDQTAQILNWIKQEINLPVALAVVTHAHQDKMGGMDALHAAGIATYANALSNQLAPQEGMVAAQHSLTFAANGWVEPATAPNFGPLKVFYPGPGHTSDNITVGIDGTDIAFGGCLIKDSKAKSLGNLGDADTEHYAASARAFGAAFPKASMIVMSHSAPDSRAAITHTARMADKLR | 3.5.2.6 | COFACTOR: Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000269|PubMed:22713171, ECO:0000269|PubMed:25815530}; Note=Binds 2 Zn(2+) ions per subunit. {ECO:0000269|PubMed:22713171, ECO:0000269|PubMed:25815530}; | antibiotic catabolic process [GO:0017001]; response to antibiotic [GO:0046677] | periplasmic space [GO:0042597] | beta-lactamase activity [GO:0008800]; zinc ion binding [GO:0008270] | PF00753; | 3.60.15.10; | Metallo-beta-lactamase superfamily, Class-B beta-lactamase family | null | SUBCELLULAR LOCATION: Periplasm {ECO:0000305}. | CATALYTIC ACTIVITY: Reaction=a beta-lactam + H2O = a substituted beta-amino acid; Xref=Rhea:RHEA:20401, ChEBI:CHEBI:15377, ChEBI:CHEBI:35627, ChEBI:CHEBI:140347; EC=3.5.2.6; Evidence={ECO:0000269|PubMed:19770275}; | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=8 uM for cefuroxime {ECO:0000269|PubMed:19770275}; KM=10 uM for cefotaxime {ECO:0000269|PubMed:19770275}; KM=10 uM for cephalothin {ECO:0000269|PubMed:19770275}; KM=12 uM for piperacillin {ECO:0000269|PubMed:19770275}; KM=16 uM for penicillin G {ECO:0000269|PubMed:... | null | null | null | FUNCTION: Confers resistance to the different beta-lactams antibiotics (penicillin, cephalosporin and carbapenem) via the hydrolysis of the beta-lactam ring. Does not confer resistance to the polymixin colistin or the fluoroquinolone ciprofloxacin. {ECO:0000269|PubMed:19770275}. | Klebsiella pneumoniae |
C7DLJ6 | OLHYD_ELIME | MNPITSKFDKVLNASSEYGHVNHEPDSSKEQQRNTPQKSMPFSDQIGNYQRNKGIPVQSYDNSKIYIIGSGIAGMSAAYYFIRDGHVPAKNITFLEQLHIDGGSLDGAGNPTDGYIIRGGREMDMTYENLWDMFQDIPALEMPAPYSVLDEYRLINDNDSNYSKARLINNKGEIKDFSKFGLNKMDQLAIIRLLLKNKEELDDLTIEDYFSESFLKSNFWTFWRTMFAFENWHSLLELKLYMHRFLHAIDGLNDLSSLVFPKYNQYDTFVTPLRKFLQEKGVNIHLNTLVKDLDIHINTEGKVVEGIITEQDGKEVKIPV... | 4.2.1.53 | COFACTOR: Name=FAD; Xref=ChEBI:CHEBI:57692; Evidence={ECO:0000269|PubMed:26077980}; Note=Binds 1 FAD per subunit. It is presumed that reduced FAD (FADH2) rather than oxidized FAD is involved in OhyA catalysis in vivo. It seems that FAD does not undergo changes in reduction/oxidation state during substrate turnover. {EC... | fatty acid metabolic process [GO:0006631]; response to fatty acid [GO:0070542]; response to toxic substance [GO:0009636] | null | FAD binding [GO:0071949]; fatty acid binding [GO:0005504]; oleate hydratase activity [GO:0050151] | PF06100; | 3.30.9.80;3.50.50.60; | Oleate hydratase family | null | null | CATALYTIC ACTIVITY: Reaction=(R)-10-hydroxyoctadecanoate = (9Z)-octadecenoate + H2O; Xref=Rhea:RHEA:21852, ChEBI:CHEBI:15377, ChEBI:CHEBI:15683, ChEBI:CHEBI:30823; EC=4.2.1.53; Evidence={ECO:0000269|PubMed:19465645, ECO:0000269|PubMed:26077980}; PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:21854; Evidence={ECO:... | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=0.21 mM for oleate (at 30 degrees Celsius) {ECO:0000269|PubMed:19465645}; KM=0.11 mM for oleate (at 25 degrees Celsius) {ECO:0000269|PubMed:26077980}; KM=0.07 mM for oleate (at 25 degrees Celsius) with OhyA harboring two-electron-reduced FAD {ECO:0000269|PubMed:260... | PATHWAY: Lipid metabolism; fatty acid metabolism. {ECO:0000305}. | BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is around 6. {ECO:0000269|PubMed:19465645, ECO:0000269|PubMed:26077980}; | BIOPHYSICOCHEMICAL PROPERTIES: Temperature dependence: Optimum temperature is 25 degrees Celsius. {ECO:0000269|PubMed:26077980}; | FUNCTION: Catalyzes the hydration of oleate at its cis-9-double bond to yield (R)-10-hydroxyoctadecanoate (PubMed:19465645, PubMed:26077980). The hydration of unsaturated fatty acids is suggested to be a detoxification mechanism and a survival strategy for living in fatty acid-rich environments. {ECO:0000269|PubMed:194... | Elizabethkingia meningoseptica (Chryseobacterium meningosepticum) |
C7E9W0 | SCH21_STACH | ASVTFWTLDNVDRTLVFTGNPGSAAIETITVGPAENTTVEFPGSWVGNWYAYPTDAEDVPGMLGEVQFGGWNGLTYFDVSAIVNPTDHDNVKQMWPAESRKPMSGCEVFPCDNAYWLPDDIQTKVTHEVDLWTTLGAGSTGLTF | 3.1.11.- | COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000269|PubMed:21109751}; | DNA metabolic process [GO:0006259] | extracellular region [GO:0005576] | DNA exonuclease activity [GO:0004529]; identical protein binding [GO:0042802]; protein homodimerization activity [GO:0042803] | null | null | null | null | SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:22424314}. | null | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=0.00329 mg/ml for salmon testes dsDNA (at pH 9 and 37 degrees Celsius) {ECO:0000269|PubMed:21109751}; | null | BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 9. No activity between pH 3-6. {ECO:0000269|PubMed:21109751}; | BIOPHYSICOCHEMICAL PROPERTIES: Temperature dependence: Optimum temperature is 45 degrees Celsius. Activity is about 80% of the maximum activity at 35 and 50 degrees Celsius. {ECO:0000269|PubMed:21109751}; | FUNCTION: Has exodeoxyribonuclease activity with lambda-DNA and salmon testes dsDNA. No activity with circular plasmid DNA. The physiological role of this enzyme may be to degrade environmental DNA, and thus mobilize nitrogen for uptake. {ECO:0000269|PubMed:21109751}. | Stachybotrys chartarum (Toxic black mold) (Stilbospora chartarum) |
C7EXK4 | AT8A2_BOVIN | MSRATSVGDQLDVPARTIYLNQPHLNKFCDNQISTAKYSVVTFLPRFLYEQIRRAANAFFLFIALLQQIPDVSPTGRYTTLVPLIIILTIAGIKEIVEDFKRHKADNAVNKKKTIVLRNGMWQTIVWKEVAVGDIVKVVNGQYLPADVVLLSSSEPQAMCYVETANLDGETNLKIRQGLSHTADMQTREVLMKLSGTIECEGPNRHLYDFTGNLNLDGKSPVALGPDQILLRGTQLRNTQWGFGIVVYTGHDTKLMQNSTKAPLKRSNVEKVTNVQILVLFGILLVMALVSSVGALYWNGSQGGKNWYIKKMDATSDNFG... | 7.6.2.1 | COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250|UniProtKB:Q9Y2Q0}; | aminophospholipid translocation [GO:0140331]; neuron development [GO:0048666]; phospholipid translocation [GO:0045332] | endosome membrane [GO:0010008]; Golgi membrane [GO:0000139]; photoreceptor disc membrane [GO:0097381]; plasma membrane [GO:0005886] | ATP binding [GO:0005524]; ATP hydrolysis activity [GO:0016887]; ATPase-coupled intramembrane lipid transporter activity [GO:0140326]; magnesium ion binding [GO:0000287]; phosphatidylethanolamine flippase activity [GO:0090555]; phosphatidylserine flippase activity [GO:0140346]; phosphatidylserine floppase activity [GO:0... | PF13246;PF00122;PF16212;PF16209; | 3.40.1110.10;2.70.150.10;3.40.50.1000; | Cation transport ATPase (P-type) (TC 3.A.3) family, Type IV subfamily | null | SUBCELLULAR LOCATION: Membrane {ECO:0000305|PubMed:19778899, ECO:0000305|PubMed:21454556}; Multi-pass membrane protein {ECO:0000255}. Golgi apparatus membrane {ECO:0000250|UniProtKB:P98200}. Endosome membrane {ECO:0000250|UniProtKB:P98200}. Cell membrane {ECO:0000250|UniProtKB:P98200}. Photoreceptor outer segment membr... | CATALYTIC ACTIVITY: Reaction=ATP + H2O + phospholipidSide 1 = ADP + phosphate + phospholipidSide 2.; EC=7.6.2.1; Evidence={ECO:0000269|PubMed:19778899, ECO:0000269|PubMed:22307598, ECO:0000269|PubMed:24706822, ECO:0000269|PubMed:26592152, ECO:0000269|PubMed:31371510}; CATALYTIC ACTIVITY: Reaction=a 1,2-diacyl-sn-glycer... | null | null | null | null | FUNCTION: Catalytic component of a P4-ATPase flippase complex 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 (PubMed:19778899, PubMed:24706822, PubMed:26... | Bos taurus (Bovine) |
C7F6X3 | IBP_LEUSY | MSLLSIITIGLAGLGGLVNGQRDLSVELGVASNFAILAKAGISSVPDSAILGDIGVSPAAATYITGFGLTQDSSTTYATSPQVTGLIYAADYSTPTPNYLAAAVANAETAYNQAAGFVDPDFLELGAGELRDQTLVPGLYKWTSSVSVPTDLTFEGNGDATWVFQIAGGLSLADGVAFTLAGGANSTNIAFQVGDDVTVGKGAHFEGVLLAKRFVTLQTGSSLNGRVLSQTEVALQKATVNSPFVPAPEVVQKRSNARQWL | null | null | null | extracellular region [GO:0005576] | ice binding [GO:0050825] | PF11999; | null | Ice-binding protein family | PTM: Glycosylated (PubMed:20067781, PubMed:22303017, PubMed:22426061, PubMed:23203635). Glycosylation is not required for the thermal hysteresis (TH) activity (PubMed:22426061). Glycosylation may increase stability and secretion of this protein (Probable). {ECO:0000269|PubMed:20067781, ECO:0000269|PubMed:22303017, ECO:... | SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:20067781, ECO:0000269|PubMed:22426061, ECO:0000269|PubMed:23203635}. | null | null | null | null | null | FUNCTION: Confers freeze tolerance. Binds to the surface of ice crystals and inhibits their growth. Has low thermal hysteresis (TH) activity, which is the ability to lower the freezing point of an aqueous solution below its melting point (PubMed:20067781, PubMed:22303017, PubMed:22426061, PubMed:22622645, PubMed:232036... | Leucosporidium sp. (strain AY30) (Arctic yeast) |
C7G3A0 | MPPE1_CRIGR | MALVRWRLRRGNFHLLSRVLLLKLTVVIISVLLFCEYFIYHLVIFQCHWPEVKTLAHGDRQKPVLKAMFLADTHLLGEIRGHWLDKLRREWQMERAFQTALWWLQPEVIFILGDIFDEGKWSTTEAWADDVQRFRKIFRHGSHVQLKVVIGNHDIGFHYQMSKYRIKRFEKVFSSERLFSWKGVNFVMVNSVAMEGDGCSICSEAEAELREISRKLNCSREVQGSSQCEGEQRLPFSAPVLLQHYPLYRASDANCSGEDAAPPEERNVPFEEKYDVLSREASQKLLWWLQPRLVLSGHTHSACEVLHPGGVPEVSVPSFS... | 3.1.-.- | COFACTOR: Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000305|PubMed:19837036}; Note=Binds 2 manganese ions per subunit. {ECO:0000305|PubMed:19837036}; | endoplasmic reticulum to Golgi vesicle-mediated transport [GO:0006888]; GPI anchor biosynthetic process [GO:0006506] | cis-Golgi network [GO:0005801]; endoplasmic reticulum exit site [GO:0070971]; endoplasmic reticulum-Golgi intermediate compartment [GO:0005793]; endoplasmic reticulum-Golgi intermediate compartment membrane [GO:0033116]; nucleoplasm [GO:0005654] | GPI anchor binding [GO:0034235]; GPI-mannose ethanolamine phosphate phosphodiesterase activity [GO:0062050]; manganese ion binding [GO:0030145] | PF00149; | 3.60.21.10; | Metallophosphoesterase superfamily, MPPE1 family | null | SUBCELLULAR LOCATION: Endoplasmic reticulum-Golgi intermediate compartment membrane {ECO:0000269|PubMed:19837036}; Multi-pass membrane protein {ECO:0000269|PubMed:19837036}. Golgi apparatus, cis-Golgi network membrane {ECO:0000269|PubMed:19837036}; Multi-pass membrane protein {ECO:0000269|PubMed:19837036}. Note=Also lo... | null | null | null | null | null | FUNCTION: Metallophosphoesterase required for transport of GPI-anchor proteins from the endoplasmic reticulum to the Golgi. Acts in lipid remodeling steps of GPI-anchor maturation by mediating the removal of a side-chain ethanolamine-phosphate (EtNP) from the second Man (Man2) of the GPI intermediate, an essential step... | Cricetulus griseus (Chinese hamster) (Cricetulus barabensis griseus) |
C7G3K3 | KBX2_LIOAU | MAKHLIVMFLVIMVISSLVDCAKKPFVQRVKNAASKAYNKLKGLAMQSQYGCPIISNMCEDHCRRKKMEGQCDLLDCVCS | null | null | defense response to bacterium [GO:0042742] | extracellular region [GO:0005576] | toxin activity [GO:0090729] | PF14866; | null | Long chain scorpion toxin family, Class 2 subfamily | null | SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:19966481}. | null | null | null | null | null | FUNCTION: Dual-function toxin that acts both as an insecticidal and an antimicrobial peptide (PubMed:19966481, PubMed:30393903, PubMed:35490851). May inhibit voltage-gated potassium channels (Kv) (By similarity). This amphipathic peptide causes significant antimicrobial activity against E.coli (MIC=7 uM) but does not s... | Liocheles australasiae (Dwarf wood scorpion) |
C7GIN5 | ARO1_YEAS2 | MVQLAKVPILGNDIIHVGYNIHDHLVETIIKHCPSSTYVICNDTNLSKVPYYQQLVLEFKASLPEGSRLLTYVVKPGETSKSRETKAQLEDYLLVEGCTRDTVMIAIGGGVIGDMIGFVASTFMRGVRVVQVPTSLLAMVDSSIGGKTAIDTPLGKNFIGAFWQPKFVLVDIKWLETLAKREFINGMAEVIKTACIWNADEFTRLESNASLFLNVVNGAKNVKVTNQLTNEIDEISNTDIEAMLDHTYKLVLESIKVKAEVVSSDERESSLRNLLNFGHSIGHAYEAILTPQALHGECVSIGMVKEAELSRYFGILSPTQ... | 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:000476... | 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; Xr... | 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: st... | null | null | FUNCTION: The AROM polypeptide catalyzes 5 consecutive enzymatic reactions in prechorismate polyaromatic amino acid biosynthesis. {ECO:0000255|HAMAP-Rule:MF_03143}. | Saccharomyces cerevisiae (strain JAY291) (Baker's yeast) |
C7IVR4 | PQN41_CAEEL | MKPKKLQQGSDSAHTSDTESTKTCEKTAKKLPKTQKKLQKSKKTAKKRRDEEFRIFFPPPRVNPPIKTPFRLHNTNCEHRDWISDNLCLPKYASYQTGWRISHKSMKSLVLMDKRRAEWLKMHNLYRKSEIRKAIWTIERKGAKKLDEMPGNWRISREKRNSLDLQEFPIKIEQFPVKKREKTAKNWRKIAVLVCFKRKTTTKNRYLRRPKTKNQRKIEFRRPKTSKNRKLRLKIRPRVRFIDRKLIRRRECLVDPQNLISWIRRQEKAENLRIFQEKQKRLQEQQEDAEWEQIEAQRANSDDVIEDKSLKMEVLDIVKH... | null | null | null | cytoplasm [GO:0005737] | null | null | null | null | null | SUBCELLULAR LOCATION: [Isoform d]: Cytoplasm {ECO:0000269|PubMed:22363008}. Note=Forms aggregates. {ECO:0000269|PubMed:22363008}.; SUBCELLULAR LOCATION: [Isoform a]: Cytoplasm {ECO:0000269|PubMed:22363008}. Note=Does not form aggregates. {ECO:0000269|PubMed:22363008}.; SUBCELLULAR LOCATION: [Isoform b]: Cytoplasm {ECO:... | null | null | null | null | null | FUNCTION: [Isoform d]: In males, required for non-apoptotic death of the linker cell once it has finished guiding gonad elongation at the end of larval development. May be involved in nuclear envelope crenellation in the linker cell. {ECO:0000269|PubMed:22363008}.; FUNCTION: [Isoform a]: In males, promotes linker cell ... | Caenorhabditis elegans |
C7IW64 | ROS1A_ORYSJ | MQDFGQWLPQSQTTADLYFSSIPIPSQFDTSIETQTRTSAVVSSEKESANSFVPHNGTGLVERISNDAGLTEVVGSSAGPTECIDLNKTPARKPKKKKHRPKVLKDDKPSKTPKSATPIPSTEKVEKPSGKRKYVRKKTSPGQPPAEQAASSHCRSELKSVKRSLDFGGEVLQESTQSGSQVPVAEICTGPKRQSIPSTIQRDSQSQLACHVVSSTSSIHTSASQMVNAHLFPPDNMPNGVLLDLNNSTSQLQNEHAKFVDSPARLFGSRIRQTSGKNSLLEIYAGMSDRNVPDLNSSISQTHSMSTDFAQYLLSSSQAS... | 3.2.2.- | COFACTOR: Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883; Evidence={ECO:0000250|UniProtKB:P0AB83}; Note=Binds 1 [4Fe-4S] cluster. The cluster does not appear to play a role in catalysis, but is probably involved in the proper positioning of the enzyme along the DNA strand. {ECO:0000250|UniProtKB:P0AB83}; | base-excision repair [GO:0006284]; DNA demethylation [GO:0080111]; epigenetic regulation of gene expression [GO:0040029] | nucleus [GO:0005634] | 4 iron, 4 sulfur cluster binding [GO:0051539]; cytosine C-5 DNA demethylase activity [GO:0051747]; DNA binding [GO:0003677]; DNA demethylase activity [GO:0035514]; DNA N-glycosylase activity [GO:0019104]; metal ion binding [GO:0046872] | PF15629;PF15628; | 1.10.1670.10; | DNA glycosylase family, DEMETER subfamily | null | SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:B8YIE8}. | null | null | null | null | null | FUNCTION: Bifunctional DNA glycosylase/lyase, which excises 5-methylcytosine (5-meC) and 5-hydroxymethylcytosine (5-hmeC), leaving an apyrimidinic (AP) site that is subsequently incised by the lyase activity (Probable). DNA demethylase that is indispensable in both male and female gametophyte development (PubMed:224486... | Oryza sativa subsp. japonica (Rice) |
C7NBY4 | CS13A_LEPBD | MKVTKVGGISHKKYTSEGRLVKSESEENRTDERLSALLNMRLDMYIKNPSSTETKENQKRIGKLKKFFSNKMVYLKDNTLSLKNGKKENIDREYSETDILESDVRDKKNFAVLKKIYLNENVNSEELEVFRNDIKKKLNKINSLKYSFEKNKANYQKINENNIEKVEGKSKRNIIYDYYRESAKRDAYVSNVKEAFDKLYKEEDIAKLVLEIENLTKLEKYKIREFYHEIIGRKNDKENFAKIIYEEIQNVNNMKELIEKVPDMSELKKSQVFYKYYLDKEELNDKNIKYAFCHFVEIEMSQLLKNYVYKRLSNISNDKI... | 3.1.-.- | COFACTOR: Name=a divalent metal cation; Xref=ChEBI:CHEBI:60240; Evidence={ECO:0000269|PubMed:27669025}; Note=Pre-crRNA processing is metal independent, while crRNA-guided target RNA cleavage is dependent on divalent metal (i.e. inhibited by EDTA) (PubMed:27669025). {ECO:0000269|PubMed:27669025}; | defense response to virus [GO:0051607] | null | endonuclease activity [GO:0004519]; RNA binding [GO:0003723] | null | null | CRISPR-associated endoribonuclease Cas13a family | null | null | null | null | null | null | null | FUNCTION: CRISPR (clustered regularly interspaced short palindromic repeat), is an adaptive immune system that provides protection against mobile genetic elements (viruses, transposable elements and conjugative plasmids). CRISPR clusters contain sequences complementary to antecedent mobile elements (spacer sequences) a... | Leptotrichia buccalis (strain ATCC 14201 / DSM 1135 / JCM 12969 / NCTC 10249 / C-1013-b) |
C7S340 | CABC2_PROVU | LPTLSHEAFGDIYLFEGELPNTLTTSNNNQLSLSKQHAKDGEQSLKWQYQPQATLTLNNIVNYQDDKNTATPLTFMMWIYNEKPQSSPLTLAFKQNNKIALSFNAELNFTGWRGIAVPFRDMQGSATGQLDQLVITAPNQAGTLFFDQIIMSVPLDNRWAVPDYQTPYVNNAVNTMVSKNWSALLMYDQMFQAHYPTLNFDTEFRDDQTEMASIYQRFEYYQGIRSDKKITPDMLDKHLALWEKLVLTQHADGSITGKALDHPNRQHFMKVEGVFSEGTQKALLDANMLRDVGKTLLQTAIYLRSDSLSATDRKKLEERY... | 4.2.2.21 | null | carbohydrate metabolic process [GO:0005975]; glycosaminoglycan catabolic process [GO:0006027] | extracellular region [GO:0005576]; periplasmic space [GO:0042597] | carbohydrate binding [GO:0030246]; chondroitin-sulfate-ABC endolyase activity [GO:0034000]; chondroitin-sulfate-ABC exolyase activity [GO:0034001] | PF02278;PF02884;PF09093;PF09092; | 2.70.98.10;1.50.10.100;2.60.120.430;2.60.220.10; | Polysaccharide lyase 8 family | null | null | CATALYTIC ACTIVITY: Reaction=Exolytic removal of Delta(4)-unsaturated disaccharide residues from the non-reducing ends of both polymeric chondroitin/dermatan sulfates and their oligosaccharide fragments.; EC=4.2.2.21; Evidence={ECO:0000269|PubMed:18849565, ECO:0000269|PubMed:9083041}; | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=33 uM for chondroitin 6-sulfate tetrasaccharide {ECO:0000269|PubMed:18849565, ECO:0000269|PubMed:9083041}; KM=80 uM for chondroitin 6-sulfate {ECO:0000269|PubMed:18849565, ECO:0000269|PubMed:9083041}; KM=9.8 uM for chondroitin 6-sulfate {ECO:0000269|PubMed:18849565... | null | BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 8. {ECO:0000269|PubMed:18849565, ECO:0000269|PubMed:9083041}; | BIOPHYSICOCHEMICAL PROPERTIES: Temperature dependence: Optimum temperature is 40 degrees Celsius (PubMed:9083041). Optimum temperature is 37 degrees Celsius (PubMed:18849565). {ECO:0000269|PubMed:18849565, ECO:0000269|PubMed:9083041}; | FUNCTION: Broad-specificity glycosaminoglycan lyase, which acts in an exolytic fashion, and preferentially degrades the tetra- and hexasaccharide derivatives of chondroitin sulfate and dermatan sulfate produced by the chondroitin sulfate ABC endolyase, to yield the respective disaccharides. To a lesser extent, is also ... | Proteus vulgaris |
C7SG33 | IF4E1_CITLA | MVVEETIKATSTEDLSNTIANQNPRGRGGDEDEELEEGEIVGDDDLDSSNLSAAIVHQPHPLEHSWTFWFDNPSAKSKQATWGASIRPIYTFSTVEEFWSVYNNIHHPSKLALRADLYCFKHKIEPKWEDPVCANGGKWTVNFSRGKSDNGWLYTLLAMIGEQFDCGDEICGAVVNVRSGQDKISIWTKNASNEAAQASIGKQWKEFLDYNDSIGFIFHEDAKKFDRHAKNKYSV | null | null | defense response to virus [GO:0051607]; translational initiation [GO:0006413] | cytoplasm [GO:0005737]; eukaryotic translation initiation factor 4F complex [GO:0016281]; nucleus [GO:0005634] | RNA 7-methylguanosine cap binding [GO:0000340]; RNA binding [GO:0003723]; translation initiation factor activity [GO:0003743] | PF01652; | 3.30.760.10; | Eukaryotic initiation factor 4E family | PTM: According to the redox status, the Cys-133-Cys-171 disulfide bridge may have a role in regulating protein function by affecting its ability to bind capped mRNA. {ECO:0000250|UniProtKB:P29557}. | SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:C6ZJZ3}. Cytoplasm {ECO:0000250|UniProtKB:C6ZJZ3}. | null | null | null | null | null | FUNCTION: Component of the protein complex eIF4F, which is involved in the recognition of the mRNA cap, ATP-dependent unwinding of 5'-terminal secondary structure and recruitment of mRNA to the ribosome (By similarity). Recognizes and binds the 7-methylguanosine-containing mRNA cap during an early step in the initiatio... | Citrullus lanatus (Watermelon) (Citrullus vulgaris) |
C7YZ74 | ARO1_FUSV7 | MAEAKKPGPERISILGEANIIVDHGLWLNFVVDDLLQNTPTSTYVLITDTNLFDTYVPAFQAQFEAAAEGKATRLLTYTIPPGEASKSRETKAEIEDWMLSQQCTRDTVIIALGGGVMGDMIGYVAATFMRGVRFVQVPTTLLAMVDSSIGGKTAIDTPMGKNLVGAFWQPKRIYIDLAFLETLPVREFINGMAEVVKTAAIWNETEFTVLEESAAHILECVRSKGEGRLTPIKDVLKRIVIGSAGVKAEVVSSDEREGGLRNLLNFGHSIGHAIEAILTPQLLHGEAVAIGMVKEAELARYLGVLRPGAVARLVKCIAS... | 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:000476... | PF01761;PF01487;PF00275;PF18317;PF08501;PF01202; | 3.40.50.1970;3.20.20.70;1.20.1090.10;3.65.10.10;3.40.50.10860;3.40.50.720;3.40.50.300; | Sugar phosphate cyclases superfamily, Dehydroquinate synthase family; EPSP synthase family; Shikimate kinase family; Type-I 3-dehydroquinase family; Shikimate dehydrogenase family | null | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_03143}. | CATALYTIC ACTIVITY: Reaction=7-phospho-2-dehydro-3-deoxy-D-arabino-heptonate = 3-dehydroquinate + phosphate; Xref=Rhea:RHEA:21968, ChEBI:CHEBI:32364, ChEBI:CHEBI:43474, ChEBI:CHEBI:58394; EC=4.2.3.4; Evidence={ECO:0000255|HAMAP-Rule:MF_03143}; CATALYTIC ACTIVITY: Reaction=3-dehydroquinate = 3-dehydroshikimate + H2O; Xr... | 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: st... | null | null | FUNCTION: The AROM polypeptide catalyzes 5 consecutive enzymatic reactions in prechorismate polyaromatic amino acid biosynthesis. {ECO:0000255|HAMAP-Rule:MF_03143}. | Fusarium vanettenii (strain ATCC MYA-4622 / CBS 123669 / FGSC 9596 / NRRL 45880 / 77-13-4) (Fusarium solani subsp. pisi) |
C8KI33 | SUV2_ARATH | MSGNDEEFNDEFLLAIDSIETTLKKADMYRPLPPPYLPTFLPAPPPSTKISSSLSHPMQLQSSAGQQRKQIQVPDPFLSYSPPRELSQRVVSGFNDALMDYSNSTVVTAAKPISPTTSNRRCDSEKDLEIDRLKKELERVSKQLLDVEQECSQLKKGKSKETESRNLCADDNRGQCSTVHASKRIDLEPDVATSSVNHRENDSRMALDDKRSFKTTGVQADVANHSDLSKKLLDIWRTSNYQDPRKNLISELLLACSTDLQILFSFMKISTPPQELNKQEAKTSSDRQSSKALESEKVYQLYSAVTKISYGFVNLKTLVE... | null | null | DNA damage response [GO:0006974]; positive regulation of cell cycle G2/M phase transition [GO:1902751]; regulation of cell cycle [GO:0051726]; response to aluminum ion [GO:0010044]; response to cisplatin [GO:0072718]; response to gamma radiation [GO:0010332]; response to hydroxyurea [GO:0072710]; response to ionizing r... | cytoplasm [GO:0005737]; nucleus [GO:0005634] | phosphoprotein phosphatase activity [GO:0004721]; protein dimerization activity [GO:0046983] | null | null | Serpin family | PTM: Probably phosphorylated by ATR. {ECO:0000269|PubMed:28556304}. | SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00768, ECO:0000269|PubMed:28556304}. Cytoplasm {ECO:0000269|PubMed:28556304}. | null | null | null | null | null | FUNCTION: Required for tolerance to DNA-damaging and cross-linking agents such as UVB irradiation, gamma-radiation, aphidicolin, ionizing radiation and hydroxyurea (HU), cisplatin (CDDP) and mitomycin C (MMC) (PubMed:19619158, PubMed:19619159, PubMed:28556304). Involved in cell-cycle G2/M arrest in response to DNA dama... | Arabidopsis thaliana (Mouse-ear cress) |
C8V7P4 | IVOA_EMENI | MASPIIQPAGAGIHDIFTQLELWESIDKGLSMITILRDNDVLWKPFLQLTLFNQLNIVRKAWSATIQKASESDKVPTLKDVYTSESSFIAQALLDTKNLQITPPATPRTALSGALLAKTIVIFHHSERAQEELGTELPEEVRSLVNQNAICLKVLYNANQWHIDLHYKRDSLSSAQAGEVAEIFEQYLEEALEAVASAIPPSPPVEDDNAGHGGLCKERTDCPKVNRCIHDLIEEQAIARPDQEGICAYDGSLSYAGLSKLSSVLAEQLKTFGARPEQRVAILMNKSFWYPVVVLAVLKSGAAFVPLDPSHPKNRLKQLI... | 5.1.-.- | null | amino acid activation for nonribosomal peptide biosynthetic process [GO:0043041]; conidium formation [GO:0048315]; pigment biosynthetic process [GO:0046148]; positive regulation of conidium formation [GO:0075307]; secondary metabolic process [GO:0019748]; secondary metabolite biosynthetic process [GO:0044550] | cytoplasm [GO:0005737]; fungal-type cell wall [GO:0009277] | isomerase activity [GO:0016853]; phosphopantetheine binding [GO:0031177] | PF00501;PF00668;PF00550; | 3.30.300.30;1.10.1200.10;3.30.559.10;3.40.50.12780;3.30.559.30; | NRP synthetase family | null | null | CATALYTIC ACTIVITY: Reaction=ATP + H2O + L-tryptophan = AMP + D-tryptophan + diphosphate + H(+); Xref=Rhea:RHEA:63892, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:33019, ChEBI:CHEBI:57719, ChEBI:CHEBI:57912, ChEBI:CHEBI:456215; Evidence={ECO:0000269|PubMed:31573806}; PhysiologicalDirection=left... | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=50 uM for L-tryptophan {ECO:0000269|PubMed:31573806}; | PATHWAY: Pigment biosynthesis. {ECO:0000269|PubMed:2126551, ECO:0000269|PubMed:28108400, ECO:0000269|Ref.3}. | null | null | FUNCTION: Nonribosomal peptide synthetase; part of the pathway that mediates the biosynthesis of the gray-brown conidiophore pigment (PubMed:23617571, PubMed:28108400). The first step of the pathway is performed by the nonribosomal peptide synthetase ivoA that catalyzes ATP-dependent unidirectional stereoinversion of L... | Emericella nidulans (strain FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139) (Aspergillus nidulans) |
C8VBH4 | ESA1_EMENI | MGVRDSHGEAAGTPDPVEKGIATLNTIRIGVKAMVHKDGALRKAEILSIKQRKDGLAFYVHYVDFNKRLDEWVASSRLDLSQEVEWPQPEKPEKKKSGPAKAPSKNKRVRAGSRDVSATPDTLTGKNTNVGKAQRPSKAGGKENRGDETPADLSMLASEAVSADGTPKAVSEDIDMMDASFTDAKEIKEEERALGLMSREEEIEKLRTSGSMTQNPTEVHRVRNLDRLQMGKYDIEPWYFSPYPASFSDAEVVYIDEFCLSYFDNKRAFERHRTKCTLTHPPGNEIYRDDNISFFEVDGRRQRTWCRNLCLLSKLFLDHK... | 2.3.1.-; 2.3.1.48 | null | DNA repair [GO:0006281]; DNA-templated transcription elongation [GO:0006354]; negative regulation of DNA-templated transcription [GO:0045892]; positive regulation of macroautophagy [GO:0016239]; positive regulation of transcription elongation by RNA polymerase II [GO:0032968]; positive regulation of triglyceride biosyn... | NuA4 histone acetyltransferase complex [GO:0035267]; nucleosome [GO:0000786]; nucleus [GO:0005634]; piccolo histone acetyltransferase complex [GO:0032777] | chromatin binding [GO:0003682]; histone crotonyltransferase activity [GO:0140068]; histone H4K12 acetyltransferase activity [GO:0043997]; histone H4K16 acetyltransferase activity [GO:0046972]; peptide 2-hydroxyisobutyryltransferase activity [GO:0106226]; transcription coregulator activity [GO:0003712] | PF01853;PF11717;PF17772; | 2.30.30.140;3.40.630.30;3.30.60.60;1.10.10.10; | MYST (SAS/MOZ) family | PTM: Autoacetylation at Lys-320 is required for proper function. {ECO:0000250|UniProtKB:Q08649}. | SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:O94446}. Chromosome {ECO:0000250|UniProtKB:O94446}. Note=Following DNA damage, localizes to sites of DNA damage, such as double stand breaks (DSBs). {ECO:0000250|UniProtKB:O94446}. | CATALYTIC ACTIVITY: Reaction=acetyl-CoA + L-lysyl-[histone] = CoA + H(+) + N(6)-acetyl-L-lysyl-[histone]; Xref=Rhea:RHEA:21992, Rhea:RHEA-COMP:9845, Rhea:RHEA-COMP:11338, ChEBI:CHEBI:15378, ChEBI:CHEBI:29969, ChEBI:CHEBI:57287, ChEBI:CHEBI:57288, ChEBI:CHEBI:61930; EC=2.3.1.48; Evidence={ECO:0000250|UniProtKB:O94446}; ... | null | null | null | null | FUNCTION: Catalytic component of the NuA4 histone acetyltransferase (HAT) complex which is involved in epigenetic transcriptional activation of selected genes principally by acetylation of nucleosomal histones H4, H3, H2B, H2A and H2A variant H2A.Z (By similarity). Acetylates histone H4 to form H4K5ac, H4K8ac, H4K12ac ... | Emericella nidulans (strain FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139) (Aspergillus nidulans) |
C8VG90 | ACON_EMENI | MITTRLARMGALAPKSRLLFGTRGMATVADLDKKVEMCNLEKGNYINYKKMSENLDVVRRRLTRPLTYAEKILYSHLDDPQNQDIERGKSYLKLRPDRVACQDATAQMAILQFMSAGMPSVATPTTVHCDHLIEAQLGGEKDLARANEINKEVYDFLASSTAKYNIGFWKPGSGIIHQIILENYAFPGGLMIGTDSHTPNAGGLAIAAIGVGGADAVDVMAGLPWELKAPKVIGVRLTGEMSGWTAPKDIILKVAGLLTVKGGTGAIIEYHGPGVNSLSATGMATICNMGAEIGATTSLFPFNDRMYDYLKATKRQQIGD... | 4.2.1.-; 4.2.1.3 | COFACTOR: Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883; Evidence={ECO:0000250}; Note=Binds 1 [4Fe-4S] cluster per subunit. {ECO:0000250}; | lysine biosynthetic process via aminoadipic acid [GO:0019878]; mitochondrial genome maintenance [GO:0000002]; tricarboxylic acid cycle [GO:0006099] | cytosol [GO:0005829]; mitochondrial nucleoid [GO:0042645]; mitochondrion [GO:0005739] | 4 iron, 4 sulfur cluster binding [GO:0051539]; aconitate hydratase activity [GO:0003994]; double-stranded DNA binding [GO:0003690]; metal ion binding [GO:0046872]; single-stranded DNA binding [GO:0003697] | PF00330;PF00694; | 3.40.1060.10;3.30.499.10;3.20.19.10; | Aconitase/IPM isomerase family | null | SUBCELLULAR LOCATION: Mitochondrion {ECO:0000250}. | CATALYTIC ACTIVITY: Reaction=citrate = D-threo-isocitrate; Xref=Rhea:RHEA:10336, ChEBI:CHEBI:15562, ChEBI:CHEBI:16947; EC=4.2.1.3; Evidence={ECO:0000269|PubMed:23106124}; CATALYTIC ACTIVITY: Reaction=(2R)-homocitrate = cis-homoaconitate + H2O; Xref=Rhea:RHEA:26101, ChEBI:CHEBI:15377, ChEBI:CHEBI:58174, ChEBI:CHEBI:5888... | null | PATHWAY: Carbohydrate metabolism; tricarboxylic acid cycle; isocitrate from oxaloacetate: step 2/2.; PATHWAY: Amino-acid biosynthesis; L-lysine biosynthesis via AAA pathway; L-alpha-aminoadipate from 2-oxoglutarate: step 2/5. | null | null | FUNCTION: Catalyzes the isomerization of citrate to isocitrate via cis-aconitate, a step in the citric acid cycle. Also catalyzes the reversible dehydration of (R)-homocitrate to cis-homoaconitate, a step in the alpha-aminoadipate pathway for lysine biosynthesis. {ECO:0000269|PubMed:23106124}. | Emericella nidulans (strain FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139) (Aspergillus nidulans) |
C8VJQ3 | ASQI_EMENI | MTCTLRDLNSLLEICCRCPAHNPSTAFAPTTKVRVSSDVRGIFALPVQKDHKPYNGLSPEHLETMKAVSLMLDAAGPKLEDGISKAKELLEERINPELMRDALGIYLTHSKDAQQRKIFPPPLKNHPFFSTKTRRPANVAGEICTADTLHGHALLSYWRDDYDLNDSHYYWHMVYRGAGGDNSKNVGDFDRHGEVFLYVHSQMVARYETESLCWSLPLVRPWNQYDDFLENGYAPISSLIEHYGGYPPFSTWYSIRNPDMPDTLNVTIPRARLEEWRDNIYAAIRKGQFETTSKDKPLVLTRDNCLNFVGGILDAQYPSL... | 4.1.99.27 | COFACTOR: Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000269|PubMed:30026518}; Note=Binds 1 zinc ion per subunit. {ECO:0000269|PubMed:30026518}; | null | null | lyase activity [GO:0016829]; metal ion binding [GO:0046872] | PF03723;PF00372; | 1.10.1280.10;2.60.40.1520; | Tyrosinase family | null | null | CATALYTIC ACTIVITY: Reaction=(-)-cyclopenine = H(+) + methyl isocyanate + viridicatin; Xref=Rhea:RHEA:73415, ChEBI:CHEBI:15378, ChEBI:CHEBI:59059, ChEBI:CHEBI:193522, ChEBI:CHEBI:193553; EC=4.1.99.27; Evidence={ECO:0000269|PubMed:30026518}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:73416; Evidence={ECO:00002... | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=0.068 mM for (-)-Cyclopeptin {ECO:0000269|PubMed:30026518}; KM=2.86 mM for 4'-methoxycyclopenin {ECO:0000269|PubMed:30026518}; | PATHWAY: Secondary metabolite biosynthesis. {ECO:0000269|PubMed:30026518}.; PATHWAY: Alkaloid biosynthesis. {ECO:0000269|PubMed:30026518}.; PATHWAY: Mycotoxin biosynthesis. {ECO:0000269|PubMed:30026518}. | null | null | FUNCTION: Cyclopenase; part of the gene cluster that mediates the biosynthesis of the aspoquinolone mycotoxins (PubMed:25251934, PubMed:30026518). Within the pathway, the cyclopenase asqI catalyzes the conversion of 4'-methoxycyclopenin into 4'-methoxyviridicatin (PubMed:30026518). Cyclopenin can also be converted into... | Emericella nidulans (strain FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139) (Aspergillus nidulans) |
C8VJW0 | HXNR_EMENI | MKAKMKKHACTYPGCSKAFTRAEHLRRHSLNHETISNSQGYTCQRCMTHFSRADLLSRHLDRHAKKDAEAGGFGKGVLETRKRMRRAEDGSIVLRPPKRPSRHQQKTGPPVGAPLSSSGSVSAGSGRSSRSPDVSLHAAQAPVSPPRSASDPVSVSGVSIDDDGTDPDPMLAPMMPGGPFEPYVEPIPGQFDAADGSWGGFDALGDGMMLDTATDFNLPFAATGNYNWLFDVSSLDDAFHHLELPLGPDLVPFANSHGNYASVNTMELSGAGAENVQDSMLNLDLDIDLNGLPAGFVHDQGPDGSSASVLLQAASFVERG... | null | null | DNA-templated transcription [GO:0006351]; regulation of transcription by RNA polymerase II [GO:0006357] | chromatin [GO:0000785]; nucleus [GO:0005634] | DNA-binding transcription factor activity, RNA polymerase II-specific [GO:0000981]; RNA polymerase II cis-regulatory region sequence-specific DNA binding [GO:0000978]; zinc ion binding [GO:0008270] | PF04082; | 3.30.160.60; | null | null | SUBCELLULAR LOCATION: Nucleus {ECO:0000305|PubMed:29212709}. | null | null | null | null | null | FUNCTION: Transcription factor that specifically regulates the expression of the hxn gene cluster that mediates the degradation of nicotinate and related metabolites (PubMed:29212709, PubMed:4581274). {ECO:0000269|PubMed:29212709, ECO:0000269|PubMed:4581274}. | Emericella nidulans (strain FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139) (Aspergillus nidulans) |
C8VQG9 | LAEA_EMENI | MFEMGPVGTRLPAMTSPAHNHYSYHSPTSSDRGRSRQNSDAMDIQSITEREPATRYAVAGGPAPWNRNGSPSMSPMYSNNSERNQFHEENGRTYHGFRRGMYFLPCDEQEQDRLDIFHKLFTVARVSESLIYAPHPTNGRFLDLGCGTGIWAIEVANKYPDAFVAGVDLAPIQPPNHPKNCEFYAPFDFEAPWAMGEDSWDLIHLQMGCGSVMGWPNLYRRIFAHLRPGAWFEQVEIDFEPRCDDRSLDGTALRHWYDCLKQATAETMRPIAHSSRDTIKDLQDAGFTEIDHQIVGLPLNPWHQDEHERKVARWYNLAVS... | 2.1.1.- | null | ascospore formation [GO:0030437]; biological process involved in interaction with host [GO:0051701]; methylation [GO:0032259]; penicillin metabolic process [GO:0042316]; positive regulation of ascospore formation [GO:0075296]; positive regulation of penicillin metabolic process [GO:0033246]; positive regulation of ster... | nucleus [GO:0005634] | methyltransferase activity [GO:0008168] | PF13489; | 3.40.50.150; | Methyltransferase superfamily, LaeA methyltransferase family | PTM: Self-methylates at Met-207. {ECO:0000269|PubMed:23532849}. | SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:18556559}. | CATALYTIC ACTIVITY: Reaction=L-methionyl-[protein] + S-adenosyl-L-methionine = S-adenosyl-L-homocysteine + S-methyl-L-methionyl-[protein]; Xref=Rhea:RHEA:60560, Rhea:RHEA-COMP:12313, Rhea:RHEA-COMP:15592, ChEBI:CHEBI:16044, ChEBI:CHEBI:57856, ChEBI:CHEBI:59789, ChEBI:CHEBI:142742; Evidence={ECO:0000269|PubMed:23532849}... | null | null | null | null | FUNCTION: Methyltransferase that performs automethylation at Met-207 (PubMed:23532849). No other methyl-accepting substrate has been identified yet (PubMed:23532849). Component of the velvet transcription factor complex that acts as a global regulator for secondary metabolite gene expression (PubMed:15075281, PubMed:20... | Emericella nidulans (strain FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139) (Aspergillus nidulans) |
C8VQY7 | YPT7_EMENI | MSSRKKVMLKVIILGDSGVGKTSLMNQYVNKKFSGSYKATIGADFLTKEVLVDDRLVTMQIWDTAGQERFQSLGVAFYRGADCCVLVYDVNNSKSFEALDSWRDEFLIQASPRDPESFPFVVIGNKIDMEESKRMISSKRAMTFCQSKGNIPYFETSAKEAVNVEQAFEVIARSALAQEEAEEYGGDYTDPINIHDTTERDGCAC | null | null | endosome organization [GO:0007032]; endosome to lysosome transport [GO:0008333]; regulation of vacuole fusion, non-autophagic [GO:0032889]; vacuole fusion, non-autophagic [GO:0042144] | fungal-type vacuole membrane [GO:0000329]; late endosome [GO:0005770]; phagocytic vesicle [GO:0045335]; vacuolar membrane [GO:0005774]; vacuole [GO:0005773] | GTP binding [GO:0005525]; GTPase activity [GO:0003924] | PF00071; | 3.40.50.300; | Small GTPase superfamily, Rab family | null | null | null | null | null | null | null | FUNCTION: Ypt/Rab-type GTPases are key regulators of membrane trafficking and intracellular vesicular transport. They act as molecular switches that convert between GTP-bound and GDP-bound states, and regulate virtually all steps of membrane traffic from the formation of the transport vesicle at the donor membrane to i... | Emericella nidulans (strain FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139) (Aspergillus nidulans) |
C8VSZ2 | XANA_EMENI | MPAITVKPLTPPAGSAIDFGAVITDVDLEHLTDGDFSTIRSALYTHLVVVLKNQHQLTPKAQYELTRRFDPSATQYGHGKTLDAKRSILHPDLKTIPHQPQVQVIGHGFIDSYEGLENITLKHPHHRTFHRDPIPQEDDYDSTRFYRWHIDAALYGLNPPIVTTLLAVKVPGGRRQTVRYDDGSGETMDVPLGTTAFASGERMFELLSEEDKEFALSSRVEYAPHPYIWMSPARSLPTGLGLHSDDLELPLSELPPIDESAIQILPMVWKNPATGKPALQIHPSAVRKIHCGDGTVIDDLKKVREIAYKLQRPAISPQYV... | 1.14.11.48 | COFACTOR: Name=Fe(2+); Xref=ChEBI:CHEBI:29033; Evidence={ECO:0000269|PubMed:17429948, ECO:0000269|PubMed:18036331}; Note=Binds 1 Fe(2+) ion per subunit. {ECO:0000250|UniProtKB:P37610}; | heterocycle metabolic process [GO:0046483]; organic cyclic compound metabolic process [GO:1901360] | cytosol [GO:0005829] | alpha-ketoglutarate-dependent xanthine dioxygenase activity [GO:0097641]; metal ion binding [GO:0046872] | PF02668; | 3.60.130.10; | TfdA dioxygenase family | PTM: Glycosylated (PubMed:17429948). Is subject to both N- and O-linked glycosylation (PubMed:17429948). {ECO:0000269|PubMed:17429948}.; PTM: Phosphorylated. {ECO:0000269|PubMed:17429948}. | SUBCELLULAR LOCATION: Cytoplasm, cytosol {ECO:0000269|PubMed:24970358}. | CATALYTIC ACTIVITY: Reaction=2-oxoglutarate + O2 + xanthine = CO2 + succinate + urate; Xref=Rhea:RHEA:43120, ChEBI:CHEBI:15379, ChEBI:CHEBI:16526, ChEBI:CHEBI:16810, ChEBI:CHEBI:17712, ChEBI:CHEBI:17775, ChEBI:CHEBI:30031; EC=1.14.11.48; Evidence={ECO:0000269|PubMed:15948966, ECO:0000269|PubMed:17429948, ECO:0000269|Pu... | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=31.1 uM for 2-oxoglutarate (at 25 degrees Celsius) {ECO:0000269|PubMed:17429948, ECO:0000269|PubMed:18036331}; KM=50 uM for 2-oxoglutarate (at 30 degrees Celsius) {ECO:0000269|PubMed:15948966, ECO:0000269|PubMed:17429948}; KM=45.2 uM for xanthine (at 25 degrees Cel... | null | BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 6.5 to 7.4. {ECO:0000269|PubMed:15948966, ECO:0000269|PubMed:17429948}; | null | FUNCTION: Alpha-ketoglutarate-dependent xanthine dioxygenase is a non-heme mononuclear Fe(2+) enzyme that decarboxylates alpha-ketoglutarate to succinate and CO(2) while hydroxylating xanthine to generate uric acid (PubMed:15948966, PubMed:17429948, PubMed:18036331). Allows xanthine utilization as a nitrogen source (Pu... | Emericella nidulans (strain FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139) (Aspergillus nidulans) |
C8VTS4 | VELB_EMENI | MYAVEDRAHSGHHPPPLSMDRIPPPSTMYPSSAGPSAMVSPAGQPEPESLSTVHDGRIWSLQVVQQPIRARMCGFGDKDRRPITPPPCIRLIVKDAQTQKEVDINSLDSSFYVVMADLWNADGTHEVNLVKHSATSPSISTAMSSSYPPPPHPTSSDYPASYQTNPYGQPVGQPVGQPVGYAGVGNYYGGSTQLQYQNAYPNPQAQYYQPMYGGMAQPQMPAAQPVTPGPGGMFTRNLIGCLSASAYRLYDTEDKIGVWFVLQDLSVRTEGIFRLKFSFVNVGKSVSDLPQSDIAEVINKGTAPILASTFSEPFQVFSAK... | null | null | cellular response to light stimulus [GO:0071482]; conidium formation [GO:0048315]; negative regulation of conidium formation [GO:0075308]; positive regulation of sexual sporulation resulting in formation of a cellular spore [GO:0043941]; positive regulation of sterigmatocystin biosynthetic process [GO:0010914]; sexual ... | cytoplasm [GO:0005737]; nucleus [GO:0005634] | null | PF11754; | 2.60.40.3960; | Velvet family, VelB subfamily | null | SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:18556559}. Cytoplasm {ECO:0000269|PubMed:18556559}. Note=VeA increases the nuclear localization of VelB. {ECO:0000269|PubMed:18556559}. | null | null | null | null | null | FUNCTION: Component of the velvet transcription factor complex that controls sexual/asexual developmental ratio in response to light, promoting sexual development in the darkness while stimulating asexual sporulation under illumination (PubMed:18556559, PubMed:23049895). The velvet complex acts as a global regulator fo... | Emericella nidulans (strain FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139) (Aspergillus nidulans) |
C8VTV4 | VEA_EMENI | MATLAAPPPPLGESGNSNSVSRITREGKKITYKLNIMQQPKRARACGQGSKSHTDRRPVDPPPVIELNIFESDPHDDSNKTDITFVYNANFFLFATLEPERPIATGKLMTNQGSPVLTGVPVAGVAYLDKPNRAGYFIFPDLSVRNEGSYRFSFHLFEQIKDPKDATEGTQPMPSPVPGKLSSPQEFLEFRLEVISNPFIVYSAKKFPGLTTSTPISRMIAEQGCRVRIRRDVRMRRRGDKRTEDYDYDNERGYNNRRPDQYAGSDAYANAPERPRSTSISTNMDPYSYPSRRPSAVEYGQPIAQPYQRPMASTPAPSST... | null | null | sporulation resulting in formation of a cellular spore [GO:0030435] | cytoplasm [GO:0005737]; nucleus [GO:0005634] | null | PF11754; | 2.60.40.3960; | Velvet family, VeA subfamily | PTM: Phosphorylated at Thr-167, Thr-170, Ser-183 and Tyr-254 (PubMed:26564476). Thr-167 should be phosphorylated and T170 and S183 should be dephosphorylated to achieve light induction of conidiation (PubMed:26564476). Phosphorylation of Ser-183 and Tyr-254 influence sterigmatocystin production in a light-independent m... | SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:17163983, ECO:0000269|PubMed:18556559, ECO:0000269|PubMed:19318129, ECO:0000269|PubMed:20816830, ECO:0000269|PubMed:23341778}. Cytoplasm {ECO:0000269|PubMed:17163983, ECO:0000269|PubMed:18556559, ECO:0000269|PubMed:19318129, ECO:0000269|PubMed:20816830, ECO:0000269|PubM... | null | null | null | null | null | FUNCTION: Component of the velvet transcription factor complex that controls sexual/asexual developmental ratio in response to light, promoting sexual development in the darkness while stimulating asexual sporulation under illumination (PubMed:12223191, PubMed:14665453, PubMed:18556559, PubMed:19210625, PubMed:2076818,... | Emericella nidulans (strain FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139) (Aspergillus nidulans) |
C8WLM1 | CGR2_EGGLE | MEYGKCRGIERGMGRRDFLKAATLLGATAAGAGMLAGCAPKSASEAQAQTAPAATGGLDPADVDWKYETDVVIVGSGSGGTCAAIEAAEAGADVVVFEKDKAMYGGNSALCGGYMLAAGWSTQEEITGYAGDTGEAFANQMLRWSQGLGNQDMIREACLRSGEAVDWMMDTGRTYEGASPLPPVWSCGDTEADVVPRSVYNHNAYGATEGHMATLKKRAESLSNIEIEMGCEVAHILKNAEGSVIGVQLADGSFAKARKGVVMACASVDNNLEMSKDLGLMQNVWGLTLEGAGLLAPGNPDMDSNTGDGVRMLREIGAEL... | 1.3.2.- | COFACTOR: Name=FAD; Xref=ChEBI:CHEBI:57692; Evidence={ECO:0000269|PubMed:29761785}; COFACTOR: Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883; Evidence={ECO:0000269|PubMed:29761785}; | response to toxic substance [GO:0009636]; steroid metabolic process [GO:0008202] | plasma membrane [GO:0005886] | 4 iron, 4 sulfur cluster binding [GO:0051539]; metal ion binding [GO:0046872]; steroid dehydrogenase activity, acting on the CH-CH group of donors [GO:0033765] | PF00890; | 3.50.50.60;3.90.700.10; | FAD-dependent oxidoreductase 2 family | PTM: Predicted to be exported by the Tat system. The position of the signal peptide cleavage has not been experimentally proven. {ECO:0000255|PROSITE-ProRule:PRU00648}. | SUBCELLULAR LOCATION: Cell membrane; Peripheral membrane protein; Extracellular side {ECO:0000305|PubMed:29761785}. | CATALYTIC ACTIVITY: Reaction=digoxin + 2 Fe(II)-[cytochrome c] + 3 H(+) = dihydrodigoxin + 2 Fe(III)-[cytochrome c]; Xref=Rhea:RHEA:62528, Rhea:RHEA-COMP:10350, Rhea:RHEA-COMP:14399, ChEBI:CHEBI:15378, ChEBI:CHEBI:29033, ChEBI:CHEBI:29034, ChEBI:CHEBI:71002, ChEBI:CHEBI:145795; Evidence={ECO:0000269|PubMed:29761785, EC... | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=94.6 uM for digoxin {ECO:0000269|PubMed:29761785}; Note=kcat is 0.23 sec(-1) for the reduction of digoxin. {ECO:0000269|PubMed:29761785}; | null | null | null | FUNCTION: Involved in the inactivation of the cardiac medication and plant natural product digoxin, thus decreasing drug efficacy and toxicity. Catalyzes the reduction of the alpha,beta-unsaturated butyrolactone ring of digoxin to the inactive metabolite dihydrodigoxin. Likely uses the cytochrome Cgr1 as the physiologi... | Eggerthella lenta (strain ATCC 25559 / DSM 2243 / CCUG 17323 / JCM 9979 / KCTC 3265 / NCTC 11813 / VPI 0255 / 1899 B) (Eubacterium lentum) |
C8WR67 | ILVC_ALIAD | MEKIYYDADISIQPLADKRIAVIGYGSQGHAHAQNLRDSGFDVVIGLRPGSSWAKAEADGFRVMAVGEAVEESDVIMILLPDERQPAVYEREIRPYLTAGKALAFAHGFNIHFSQIQPPKDVDVFMVAPKGPGHLVRRVYEAGGGVPALIAVHQDASGQAKDLALAYARGIGAGRAGILTTTFREETETDLFGEQAVLCGGLSALIKAGFETLVEAGYQPEIAYFECLHEMKLIVDLIYEGGLEYMRYSISDTAQWGDFTSGPRIINEETKKEMRRILADIQSGAFAKSWILENQANRPMFNAINRRELEHPIEVVGRKL... | 1.1.1.86 | COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000255|HAMAP-Rule:MF_00435, ECO:0000269|PubMed:25849365}; Note=Binds 2 magnesium ions per subunit. {ECO:0000255|HAMAP-Rule:MF_00435, ECO:0000269|PubMed:25849365}; | amino acid biosynthetic process [GO:0008652]; isoleucine biosynthetic process [GO:0009097]; valine biosynthetic process [GO:0009099] | cytosol [GO:0005829] | ketol-acid reductoisomerase activity [GO:0004455]; magnesium ion binding [GO:0000287]; NADP binding [GO:0050661] | PF01450;PF07991; | 6.10.240.10;3.40.50.720; | Ketol-acid reductoisomerase family | null | null | CATALYTIC ACTIVITY: Reaction=(2R)-2,3-dihydroxy-3-methylbutanoate + NADP(+) = (2S)-2-acetolactate + H(+) + NADPH; Xref=Rhea:RHEA:22068, ChEBI:CHEBI:15378, ChEBI:CHEBI:49072, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349, ChEBI:CHEBI:58476; EC=1.1.1.86; Evidence={ECO:0000255|HAMAP-Rule:MF_00435, ECO:0000305|PubMed:25849365}; CAT... | null | PATHWAY: Amino-acid biosynthesis; L-isoleucine biosynthesis; L-isoleucine from 2-oxobutanoate: step 2/4. {ECO:0000255|HAMAP-Rule:MF_00435}.; PATHWAY: Amino-acid biosynthesis; L-valine biosynthesis; L-valine from pyruvate: step 2/4. {ECO:0000255|HAMAP-Rule:MF_00435}. | null | null | FUNCTION: Involved in the biosynthesis of branched-chain amino acids (BCAA). Catalyzes an alkyl-migration followed by a ketol-acid reduction of (S)-2-acetolactate (S2AL) to yield (R)-2,3-dihydroxy-isovalerate. In the isomerase reaction, S2AL is rearranged via a Mg-dependent methyl migration to produce 3-hydroxy-3-methy... | Alicyclobacillus acidocaldarius subsp. acidocaldarius (strain ATCC 27009 / DSM 446 / BCRC 14685 / JCM 5260 / KCTC 1825 / NBRC 15652 / NCIMB 11725 / NRRL B-14509 / 104-IA) (Bacillus acidocaldarius) |
C8XPA8 | POLG_BANV | MVNPKGVNVMAARVKRAAQKTKKKAVQVSRGLRGFVLFVLTQLFMGRKLTPNVRRLWKSSDKNSLIHVLTKIKKIVGNLLMGVSRRKKRRSATTSGTVFMAMLGLTLAASVARHAHHTLINITKDDAHKLLTLRNGNCTVVATDIGNWCPDNVEYDCVTLQDNEDPDDVDCWCYRVNNVRVTYGRCKDGNTPRRSKRAVVITAHLDQGLTTKKETWLGSSHFETQVQKVEKWIIRNPTYAIAAILMSWYIGNSLKQRVVLLLLTLALGPAYATHCVGIPKRDFVQGVQGTTWVNLVLEQGGCVTIMAEGKPSVDVWMDNI... | 2.1.1.56; 2.1.1.57; 2.7.7.48; 3.4.21.91; 3.6.1.15; 3.6.4.13 | null | fusion of virus membrane with host endosome membrane [GO:0039654]; induction by virus of host autophagy [GO:0039520]; proteolysis [GO:0006508]; symbiont entry into host cell [GO:0046718]; symbiont-mediated suppression of host JAK-STAT cascade via inhibition of STAT1 activity [GO:0039563]; symbiont-mediated suppression ... | extracellular region [GO:0005576]; host cell endoplasmic reticulum membrane [GO:0044167]; host cell nucleus [GO:0042025]; host cell perinuclear region of cytoplasm [GO:0044220]; membrane [GO:0016020]; viral capsid [GO:0019028]; virion membrane [GO:0055036] | ATP binding [GO:0005524]; ATP hydrolysis activity [GO:0016887]; double-stranded RNA binding [GO:0003725]; GTP binding [GO:0005525]; metal ion binding [GO:0046872]; mRNA (nucleoside-2'-O-)-methyltransferase activity [GO:0004483]; mRNA 5'-cap (guanine-N7-)-methyltransferase activity [GO:0004482]; protein dimerization act... | PF20907;PF01003;PF07652;PF21659;PF02832;PF00869;PF01004;PF00948;PF01005;PF01002;PF01350;PF01349;PF00972;PF20483;PF01570;PF01728;PF00949; | 1.10.260.90;1.20.1280.260;2.40.10.120;2.60.40.350;1.10.8.970;2.60.260.50;3.30.70.2840;3.40.50.300;2.60.98.10;2.40.10.10;3.40.50.150;3.30.67.10;3.30.387.10; | Class I-like SAM-binding methyltransferase superfamily, mRNA cap 0-1 NS5-type methyltransferase family | PTM: [Genome polyprotein]: Specific enzymatic cleavages in vivo yield mature proteins. The nascent capsid protein C contains a C-terminal hydrophobic domain that act as a signal sequence for translocation of prM into the lumen of the ER. Mature capsid protein C is cleaved at a site upstream of this hydrophobic domain b... | SUBCELLULAR LOCATION: [Capsid protein C]: Virion {ECO:0000250|UniProtKB:P17763}. Host nucleus {ECO:0000250|UniProtKB:P17763}. Host cytoplasm, host perinuclear region {ECO:0000250|UniProtKB:P17763}. Host cytoplasm {ECO:0000250|UniProtKB:P17763}.; SUBCELLULAR LOCATION: [Peptide pr]: Secreted {ECO:0000250|UniProtKB:P17763... | CATALYTIC ACTIVITY: Reaction=Selective hydrolysis of -Xaa-Xaa-|-Yaa- bonds in which each of the Xaa can be either Arg or Lys and Yaa can be either Ser or Ala.; EC=3.4.21.91; CATALYTIC ACTIVITY: Reaction=a ribonucleoside 5'-triphosphate + RNA(n) = diphosphate + RNA(n+1); Xref=Rhea:RHEA:21248, Rhea:RHEA-COMP:14527, Rhea:... | null | null | null | null | FUNCTION: [Capsid protein C]: Plays a role in virus budding by binding to the cell membrane and gathering the viral RNA into a nucleocapsid that forms the core of a mature virus particle. During virus entry, may induce genome penetration into the host cytoplasm after hemifusion induced by the surface proteins. Can migr... | Banzi virus (BANV) |
C8XPB2 | POLG_EHV | MPVRPRNKPKGVNVMAAGKVAQKIKNKLKSKAKAIGNISKGLRGFILFILAQIFWARKLTPRVRTMWKKVDKAKATRVLKGIRNIATQLITGLAGRKKRRSMTHGIILSLGVTMVIGASLHHHGGRYLLNVTHADLGKTFTIGSGNCTANIVEAGSWCSDSMEYECVTLAEAEEPDDIDCWCRGVERVRVTYGRCKNGLDSRRSRRAAVITAHIDKGLTTRQEKWLSTSMGERQIQRIERWMMRNPFYAAISLLLAWWVGSDIKQKVLIAFLVLAIGPAYSTHCVGIPKRDFVQGVQGNTWVNLVLDQGSCVTLSSDNKP... | 2.1.1.56; 2.1.1.57; 2.7.7.48; 3.4.21.91; 3.6.1.15; 3.6.4.13 | null | fusion of virus membrane with host endosome membrane [GO:0039654]; induction by virus of host autophagy [GO:0039520]; proteolysis [GO:0006508]; symbiont entry into host cell [GO:0046718]; symbiont-mediated suppression of host JAK-STAT cascade via inhibition of STAT1 activity [GO:0039563]; symbiont-mediated suppression ... | extracellular region [GO:0005576]; host cell endoplasmic reticulum membrane [GO:0044167]; host cell nucleus [GO:0042025]; host cell perinuclear region of cytoplasm [GO:0044220]; membrane [GO:0016020]; viral capsid [GO:0019028]; virion membrane [GO:0055036] | ATP binding [GO:0005524]; ATP hydrolysis activity [GO:0016887]; double-stranded RNA binding [GO:0003725]; GTP binding [GO:0005525]; metal ion binding [GO:0046872]; mRNA (nucleoside-2'-O-)-methyltransferase activity [GO:0004483]; mRNA 5'-cap (guanine-N7-)-methyltransferase activity [GO:0004482]; protein dimerization act... | PF20907;PF01003;PF07652;PF21659;PF02832;PF00869;PF01004;PF00948;PF01005;PF01002;PF01350;PF01349;PF00972;PF20483;PF01570;PF01728;PF00949; | 1.10.260.90;1.20.1280.260;2.40.10.120;2.60.40.350;1.10.8.970;2.60.260.50;3.30.70.2840;3.40.50.300;2.60.98.10;2.40.10.10;3.40.50.150;3.30.67.10;3.30.387.10; | Class I-like SAM-binding methyltransferase superfamily, mRNA cap 0-1 NS5-type methyltransferase family | PTM: [Genome polyprotein]: Specific enzymatic cleavages in vivo yield mature proteins. The nascent capsid protein C contains a C-terminal hydrophobic domain that act as a signal sequence for translocation of prM into the lumen of the ER. Mature capsid protein C is cleaved at a site upstream of this hydrophobic domain b... | SUBCELLULAR LOCATION: [Capsid protein C]: Virion {ECO:0000250|UniProtKB:P17763}. Host nucleus {ECO:0000250|UniProtKB:P17763}. Host cytoplasm, host perinuclear region {ECO:0000250|UniProtKB:P17763}. Host cytoplasm {ECO:0000250|UniProtKB:P17763}.; SUBCELLULAR LOCATION: [Small envelope protein M]: Virion membrane {ECO:000... | CATALYTIC ACTIVITY: Reaction=Selective hydrolysis of -Xaa-Xaa-|-Yaa- bonds in which each of the Xaa can be either Arg or Lys and Yaa can be either Ser or Ala.; EC=3.4.21.91; CATALYTIC ACTIVITY: Reaction=a ribonucleoside 5'-triphosphate + RNA(n) = diphosphate + RNA(n+1); Xref=Rhea:RHEA:21248, Rhea:RHEA-COMP:14527, Rhea:... | null | null | null | null | FUNCTION: [Capsid protein C]: Plays a role in virus budding by binding to the cell membrane and gathering the viral RNA into a nucleocapsid that forms the core of a mature virus particle. During virus entry, may induce genome penetration into the host cytoplasm after hemifusion induced by the surface proteins. Can migr... | Edge Hill virus (EHV) |
C8YUV0 | FFAR4_MACFA | MSPECARAAGDAPLRSLEQANRTRFSFFSDVKGDHRLLLAAVETTVLALIFAVSLLGNVCALVLVARRRRRGTTACLVLNLFCADLLFISAIPLVLAVRWTEAWLLGPVACHLLFYLMTLSGSVTILTLAAVSLERMVCIVHLQRGVRGPGRRARAVLLTLIWGYSAVAALPLCVFFRVVPQRLPGADQEISICTLIWPTIAGEISWDVSFVTLNFLVPGLVIVISYSKILQITKASRKRLTVSLAYSESHQIRVSQQDFRLFRTLFLLMVSFFIMWSPIIITILLILIQNFKQDLVIWPSLFFWVVAFTFANSALNPIL... | null | null | adenylate cyclase-activating G protein-coupled receptor signaling pathway [GO:0007189]; brown fat cell differentiation [GO:0050873]; cellular response to hormone stimulus [GO:0032870]; ghrelin secretion [GO:0036321]; inflammatory response [GO:0006954]; negative regulation of apoptotic process [GO:0043066]; negative reg... | ciliary membrane [GO:0060170]; cilium [GO:0005929]; endosome membrane [GO:0010008]; lysosomal membrane [GO:0005765]; plasma membrane [GO:0005886] | fatty acid binding [GO:0005504]; G protein-coupled receptor activity [GO:0004930]; peptide binding [GO:0042277]; taste receptor activity [GO:0008527] | PF00001; | 1.20.1070.10; | G-protein coupled receptor 1 family | PTM: Phosphorylated at two clusters of Ser and Thr residues located in the intracellular C-terminus. Prerequisite for FFAR4 internalization via an ARRB2-dependent pathway. {ECO:0000250|UniProtKB:Q5NUL3}. | SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:Q7TMA4}; Multi-pass membrane protein {ECO:0000255}. Endosome membrane {ECO:0000250|UniProtKB:Q5NUL3}; Multi-pass membrane protein {ECO:0000255}. Lysosome membrane {ECO:0000250|UniProtKB:Q5NUL3}; Multi-pass membrane protein {ECO:0000255}. Cell projection, cilium... | null | null | null | null | null | FUNCTION: G-protein-coupled receptor for long-chain fatty acids (LCFAs) with a major role in adipogenesis, energy metabolism and inflammation. Signals via G-protein and beta-arrestin pathways. LCFAs sensing initiates activation of phosphoinositidase C-linked G proteins GNAQ and GNA11 (G(q)/G(11)), inducing a variety of... | Macaca fascicularis (Crab-eating macaque) (Cynomolgus monkey) |
C8Z543 | ARO1_YEAS8 | MVQLAKVPILGNDIIHVGYNIHDHLVETIIKHCPSSTYVICNDTNLSKVPYYQQLVLEFKASLPEGSRLLTYVVKPGETSKSRETKAQLEDYLLVEGCTRDTVMVAIGGGVIGDMIGFVASTFMRGVRVVQVPTSLLAMVDSSIGGKTAIDTPLGKNFIGAFWQPKFVLVDIKWLETLAKREFINGMAEVIKTACIWNADEFTRLESNASLFLNVVNGAKNVKVTNQLTNEIDEISNTDIEAMLDHTYKLVLESIKVKAEVVSSDERESSLRNLLNFGHSIGHAYEAILTPQALHGECVSIGMVKEAELSRYFGILSPTQ... | 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:000476... | 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; Xr... | 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: st... | null | null | FUNCTION: The AROM polypeptide catalyzes 5 consecutive enzymatic reactions in prechorismate polyaromatic amino acid biosynthesis. {ECO:0000255|HAMAP-Rule:MF_03143}. | Saccharomyces cerevisiae (strain Lalvin EC1118 / Prise de mousse) (Baker's yeast) |
C9JE40 | PATL2_HUMAN | MNCLEGPGKTCGPLASEEELVSACQLEKEEENEGEEEEEEEDEEDLDPDLDPDLEEEENDLGDPAVLGAVHNTQRALLSSPGVKAPGMLGMSLASLHFLWQTLDYLSPIPFWPTFPSTSSPAQHFGPRLPSPDPTLFCSLLTSWPPRFSHLTQLHPRHQRILQQQQHSQTPSPPAKKPWSQQPDPYANLMTRKEKDWVIKVQMVQLQSAKPRLDDYYYQEYYQKLEKKQADEELLGRRNRVESLKLVTPYIPKAEAYESVVRIEGSLGQVAVSTCFSPRRAIDAVPHGTQEQDIEAASSQRLRVLYRIEKMFLQLLEIEE... | null | null | deadenylation-dependent decapping of nuclear-transcribed mRNA [GO:0000290]; negative regulation of cytoplasmic mRNA processing body assembly [GO:0010607]; negative regulation of translation [GO:0017148]; P-body assembly [GO:0033962] | cytoplasm [GO:0005737]; nucleus [GO:0005634]; P-body [GO:0000932] | RNA binding [GO:0003723] | PF09770; | null | PAT1 family | null | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:20584987, ECO:0000269|PubMed:28965849}. Nucleus {ECO:0000250|UniProtKB:A2ARM1}. | null | null | null | null | null | FUNCTION: RNA-binding protein that acts as a translational repressor. {ECO:0000250|UniProtKB:Q4V7K4}. | Homo sapiens (Human) |
C9JLW8 | MCRI1_HUMAN | MTSSPVSRVVYNGKRTSSPRSPPSSSEIFTPAHEENVRFIYEAWQGVERDLRGQVPGGERGLVEEYVEKVPNPSLKTFKPIDLSDLKRRSTQDAKKS | null | null | regulation of epithelial to mesenchymal transition [GO:0010717] | cytoplasm [GO:0005737]; cytoplasmic stress granule [GO:0010494]; nucleus [GO:0005634] | null | PF14799; | null | MCRIP family | PTM: Phosphorylation by MAPK3/1 (ERK1/2) regulates MCRIP1 binding to CTBP(s) (PubMed:25728771). {ECO:0000269|PubMed:25728771}. | SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:25728771, ECO:0000269|PubMed:26184334}. Cytoplasm, Stress granule {ECO:0000269|PubMed:26184334}. | null | null | null | null | null | FUNCTION: The phosphorylation status of MCRIP1 functions as a molecular switch to regulate epithelial-mesenchymal transition. Unphosphorylated MCRIP1 binds to and inhibits the transcriptional corepressor CTBP(s). When phosphorylated by MAPK/ERK, MCRIP1 releases CTBP(s) resulting in transcriptional silencing of the E-ca... | Homo sapiens (Human) |
C9JR72 | KBTBD_HUMAN | MARGPQTLVQVWVGGQLFQADRALLVEHCGFFRGLFRSGMRETRAAEVRLGVLSAGGFRATLQVLRGDRPALAAEDELLQAVECAAFLQAPALARFLEHNLTSDNCALLCDAAAAFGLRDVFHSAALFICDGERELAAELALPEARAYVAALRPSSYAAVSTHTPAPGFLEDASRTLCYLDEEEDAWRTLAALPLEASTLLAGVATLGNKLYIVGGVRGASKEVVELGFCYDPDGGTWHEFPSPHQPRYDTALAGFDGRLYAIGGEFQRTPISSVERYDPAAGCWSFVADLPQPAAGVPCAQACGRLFVCLWRPADTTAV... | null | null | actin filament organization [GO:0007015]; protein ubiquitination [GO:0016567]; regulation of the force of skeletal muscle contraction [GO:0014728]; relaxation of skeletal muscle [GO:0090076] | cytosol [GO:0005829] | actin filament binding [GO:0051015] | PF00651;PF01344; | 2.120.10.80; | null | PTM: Autoubiquitinated. {ECO:0000269|PubMed:22542517}. | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:21109227, ECO:0000269|PubMed:22542517}. | null | null | PATHWAY: Protein modification; protein ubiquitination. | null | null | FUNCTION: Substrate-specific adapter of a BCR (BTB-CUL3-RBX1) E3 ubiquitin ligase complex. {ECO:0000269|PubMed:22542517}. | Homo sapiens (Human) |
C9JRZ8 | AK1BF_HUMAN | MATFVELSTKAKMPIVGLGTWRSLLGKVKEAVKVAIDAEYRHIDCAYFYENQHEVGEAIQEKIQEKAVMREDLFIVSKVWPTFFERPLVRKAFEKTLKDLKLSYLDVYLIHWPQGFKTGDDFFPKDDKGNMISGKGTFLDAWEAMEELVDEGLVKALGVSNFNHFQIERLLNKPGLKYKPVTNQVECHPYLTQEKLIQYCHSKGITVTAYSPLGSPDRPWAKPEDPSLLEDPKIKEIAAKHKKTTAQVLIRFHIQRNVTVIPKSMTPAHIVENIQVFDFKLSDEEMATILSFNRNWRAFDFKEFSHLEDFPFDAEY | 1.1.1.-; 1.1.1.216; 1.1.1.300; 1.1.1.54; 1.1.1.64 | null | estrogen biosynthetic process [GO:0006703] | cytosol [GO:0005829]; mitochondrial matrix [GO:0005759]; mitochondrion [GO:0005739] | alditol:NADP+ 1-oxidoreductase activity [GO:0004032]; allyl-alcohol dehydrogenase activity [GO:0047655]; estradiol 17-beta-dehydrogenase [NAD(P)] activity [GO:0004303]; farnesol dehydrogenase activity [GO:0047886]; NADP-retinol dehydrogenase activity [GO:0052650]; oxidoreductase activity, acting on the CH-OH group of d... | PF00248; | 3.20.20.100; | Aldo/keto reductase family | null | SUBCELLULAR LOCATION: [Isoform 1]: Mitochondrion {ECO:0000269|PubMed:25577493}.; SUBCELLULAR LOCATION: [Isoform 2]: Cytoplasm, cytosol {ECO:0000269|PubMed:25577493}. | CATALYTIC ACTIVITY: Reaction=17beta-estradiol + NADP(+) = estrone + H(+) + NADPH; Xref=Rhea:RHEA:24616, ChEBI:CHEBI:15378, ChEBI:CHEBI:16469, ChEBI:CHEBI:17263, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349; Evidence={ECO:0000269|PubMed:25577493}; CATALYTIC ACTIVITY: Reaction=NADP(+) + testosterone = androst-4-ene-3,17-dione + ... | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=2.8 uM for androsterone (tested with isoform 1 in the reductive reaction) {ECO:0000269|PubMed:25577493}; KM=1.9 uM for delta-4-androstenedione (tested with isoform 1 in the reductive reaction) {ECO:0000269|PubMed:25577493}; KM=2.5 uM for estrone (tested with isofor... | null | null | null | FUNCTION: [Isoform 1]: Catalyzes the NADPH-dependent reduction of a variety of carbonyl substrates, like aromatic aldehydes, alkenals, ketones and alpha-dicarbonyl compounds (PubMed:21276782, PubMed:26222439). In addition, catalyzes the reduction of androgens and estrogens with high positional selectivity (shows 17-bet... | Homo sapiens (Human) |
C9K4X8 | GSS_PATPE | MTSNNRHLFQATCLVLLLLHAAFHGGALGEKYCDDDFHMAVFRTCAVSKRSQPGMSLSDVLTMNRFRGHNIKRSIDSTLEDNAFFMSGLEKRSEYSGIASYCCLHGCTPSELSVVC | null | null | adenylate cyclase-activating G protein-coupled receptor signaling pathway [GO:0007189]; positive regulation of oocyte maturation [GO:1900195]; positive regulation of ovulation [GO:0060279] | extracellular space [GO:0005615]; plasma membrane [GO:0005886] | hormone activity [GO:0005179] | null | null | Insulin family | null | SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:23829221}. | null | null | null | null | null | FUNCTION: Induces oocyte maturation and ovulation in vitro in ovarian fragments and induces spawning behavior and gamete release in vivo (PubMed:19470645). Probably mediates its effects by binding to a G-protein coupled receptor located in follicle cell membranes (PubMed:21295575, PubMed:21967225, PubMed:24929230). Fol... | Patiria pectinifera (Starfish) (Asterina pectinifera) |
C9SE96 | ARO1_VERA1 | MSCSNNTEPTRIAILGTDNIVVDHGIWLNWVTKDLFDNVKSSTYVLVTDTNLYDTYVPPFKHAFDGATDTTAGPRLLTLAIPPGEISKSRQSKAHIEDWMLSQQCTRDTVIIALGGGVIGDMLGYVAATFMRGIRFVQVPTTLLAMVDSSIGGKTAIDTPMGKNLVGAFWQPSRIYIDLAFLETLPSREFINGMAEVIKTAAIWDENEFATLEANAPSIVAAVNQPTGPGRLSPIREILKRIVLGSARVKAEVVSSDEREGGLRNLLNFGHSIGHAYEALLTPQLLHGEAVAIGMVKEAELARYLGVLRPSAVARLAKCI... | 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:000476... | PF01761;PF01487;PF00275;PF08501;PF01202; | 3.40.50.1970;3.20.20.70;1.20.1090.10;3.65.10.10;3.40.50.10860;3.40.50.720;3.40.50.300; | Sugar phosphate cyclases superfamily, Dehydroquinate synthase family; EPSP synthase family; Shikimate kinase family; Type-I 3-dehydroquinase family; Shikimate dehydrogenase family | null | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_03143}. | CATALYTIC ACTIVITY: Reaction=7-phospho-2-dehydro-3-deoxy-D-arabino-heptonate = 3-dehydroquinate + phosphate; Xref=Rhea:RHEA:21968, ChEBI:CHEBI:32364, ChEBI:CHEBI:43474, ChEBI:CHEBI:58394; EC=4.2.3.4; Evidence={ECO:0000255|HAMAP-Rule:MF_03143}; CATALYTIC ACTIVITY: Reaction=3-dehydroquinate = 3-dehydroshikimate + H2O; Xr... | 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: st... | null | null | FUNCTION: The AROM polypeptide catalyzes 5 consecutive enzymatic reactions in prechorismate polyaromatic amino acid biosynthesis. {ECO:0000255|HAMAP-Rule:MF_03143}. | Verticillium alfalfae (strain VaMs.102 / ATCC MYA-4576 / FGSC 10136) (Verticillium wilt of alfalfa) (Verticillium albo-atrum) |
C9X0M5 | RNC_NEIM8 | MKDDVLKQQAHAAIQKKLGYAFRDISLLRQALTHRSHHAKHNERFEFVGDSILNYTVARMLFDAFPKLTEGELSRLRASLVNEGVLAEMAAEMNVGDGLYLGAGELKSGGFRRPSILADAMEAMFAAVSFDADFNTAEKVVRHLFADRVRRADFQNQAKDGKTALQEALQARRFALPKYRIEEQIGYANDSMFVISCDLGELGFVCRAKGTSRKAAEQEAAKEALKWLEEKLPLKRKKK | 3.1.26.3 | COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000255|HAMAP-Rule:MF_00104}; | mRNA processing [GO:0006397]; pre-miRNA processing [GO:0031054]; rRNA processing [GO:0006364]; siRNA processing [GO:0030422]; tRNA processing [GO:0008033] | cytoplasm [GO:0005737]; RISC complex [GO:0016442] | deoxyribonuclease I activity [GO:0004530]; metal ion binding [GO:0046872]; ribonuclease III activity [GO:0004525]; rRNA binding [GO:0019843] | PF00035;PF14622; | 3.30.160.20;1.10.1520.10; | Ribonuclease III family | null | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00104}. | CATALYTIC ACTIVITY: Reaction=Endonucleolytic cleavage to 5'-phosphomonoester.; EC=3.1.26.3; Evidence={ECO:0000255|HAMAP-Rule:MF_00104}; | null | null | null | null | FUNCTION: Digests double-stranded RNA. Involved in the processing of primary rRNA transcript to yield the immediate precursors to the large and small rRNAs (23S and 16S). Also processes some mRNAs, and tRNAs when they are encoded in the rRNA operon. {ECO:0000269|PubMed:23706818}.; FUNCTION: CRISPR (clustered regularly ... | Neisseria meningitidis serogroup C (strain 8013) |
C9XI63 | TEPS3_ANOGA | MWQFIRSRILTVIIFIGAAHGLLVVGPKFIRANQEYTLVISNFNSQLSKVDLLLKLEGETDNGLSVLNVTKMVDVRRNMNRMINFNMPEDLTAGNYKITIDGQRGFSFHKEAELVYLSKSISGLIQVDKPVFKPGDTVNFRVIVLDTELKPPARVKSVHVTIRDPQRNVIRKWSTAKLYAGVFESDLQIAPTPMLGVWNISVEVEGEELVSKTFEVKEYVLSTFDVQVMPSVIPLEEHQAVNLTIEANYHFGKPVQGVAKVELYLDDDKLNQKKELTVYGKGQVELRFDNFAMDADQQDVRVKVSFIEQYTNRTVVKQSQ... | null | null | antibacterial innate immune response [GO:0140367]; antifungal innate immune response [GO:0061760]; cell aggregation [GO:0098743]; defense response to symbiont [GO:0140546]; positive regulation of melanin biosynthetic process [GO:0048023] | extracellular region [GO:0005576]; extracellular space [GO:0005615] | endopeptidase inhibitor activity [GO:0004866] | PF00207;PF07703;PF07677;PF01835;PF17791;PF17789;PF07678;PF21412; | 1.50.10.20;2.20.130.20;2.60.120.1540;2.60.40.1930;2.60.40.1940;2.60.40.2950;2.60.40.690;2.60.40.10; | null | PTM: In the hemolymph, the full-length protein is cleaved by an unknow protease into a 75kDa N-terminal (TEP1-N) chain and an 80kDa C-terminal (TEP1-C) chain which remain non-covalently linked (PubMed:15006349, PubMed:19286136, PubMed:24039584, PubMed:25012124). The TEP1-C chain contains the thioester bond which covale... | SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:15006349, ECO:0000269|PubMed:19286136, ECO:0000269|PubMed:23166497, ECO:0000269|PubMed:24039584, ECO:0000269|PubMed:25012124}. Note=Secreted as a full-length protein into the hemolymph. {ECO:0000269|PubMed:15006349, ECO:0000269|PubMed:19286136, ECO:0000269|PubMed:23166... | null | null | null | null | null | FUNCTION: Plays an essential role in the innate immune response against bacteria, fungi and protozoa infection (PubMed:15006349, PubMed:23166497, PubMed:24039584, PubMed:25012124, PubMed:30690067). After proteolytic cleavage, the protein C-terminus binds covalently through a thioester bond to the pathogen surface resul... | Anopheles gambiae (African malaria mosquito) |
C9XI66 | TEPR1_ANOGA | MWQFIRSRILTVIIFIGAAHGLLVVGPKFIRANQEYTLVISNFNSQLSKVDLLLKLEGETDNGLSVLNVTKMVDVRRNMNRMINFNMPEDLTAGNYKITIDGQRGFSFHKEAELVYLSKSISGLIQVDKPVFKPGDTVNFRVIVLDTELKPPARVKSVYVTIRDPQRNVIRKWSTAKLYAGVFESDLQIAPTPMLGVWNISVEVEGEELVSKTFEVKEYVLSTFDVQVMPSVIPLEEHQAVNLTIEANYHFGKPVQGVAKVELYLDDDKLKLKKELTVYGKGQVELRFDNFAMDADQQDVPVKVSFVEQYTNRTVVKQSQ... | null | null | defense response to symbiont [GO:0140546]; immune system process [GO:0002376]; positive regulation of melanin biosynthetic process [GO:0048023] | extracellular space [GO:0005615] | endopeptidase inhibitor activity [GO:0004866] | PF00207;PF07703;PF07677;PF01835;PF17791;PF17789;PF07678;PF21412; | 1.50.10.20;2.20.130.20;2.60.120.1540;2.60.40.1930;2.60.40.1940;2.60.40.2950;2.60.40.690;2.60.40.10; | null | PTM: In the hemolymph, the full-length protein is cleaved by an unknow protease into a 75kDa N-terminal (TEP1-N) chain and an 80kDa C-terminal (TEP1-C) chain which remain non-covalently linked (PubMed:19286136, PubMed:23055931). The TEP1-C chain contains the thioester bond which covalently binds to the pathogen surface... | SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:15006349, ECO:0000269|PubMed:19286136}. Note=Secreted as a full-length protein into the hemolymph. {ECO:0000269|PubMed:15006349, ECO:0000269|PubMed:19286136}. | null | null | null | null | null | FUNCTION: Plays an essential role in the innate immune response against bacteria, fungi and protozoa infection (PubMed:15006349). After proteolytic cleavage, the protein C-terminus binds covalently through a thioester bond to the pathogen surface resulting in pathogen clearance either by melanization or lysis (PubMed:1... | Anopheles gambiae (African malaria mosquito) |
D0E0C2 | SCNA1_PERAM | MADNSPLIREERQRLFRPYTRAMLTAPSAQPAKENGKTEENKDNSRDKGRGANKDRDGSAHPDQALEQGSRLPARMRNIFPAELASTPLEDFDPFYKNKKTFVVVTKAGDIFRFSGEKSLWMLDPFTPIRRVAISTMVQPIFSYFIMITILIHCIFMIMPATQTTYILELVFLSIYTIEVVVKVLARGFILHPFAYLRDPWNWLDFLVTLIGYITLVVDLGHLYALRAFRVLRSWRTVTIVPGWRTIVDALSLSITSLKDLVLLLLFSLFVFAVLGLQIYMGVLTQKCVKHFPADGSWGNFTDERWFNYTSNSSHWYIPD... | null | null | membrane depolarization during action potential [GO:0086010]; neuronal action potential [GO:0019228] | axon [GO:0030424]; voltage-gated sodium channel complex [GO:0001518] | voltage-gated sodium channel activity [GO:0005248] | PF16905;PF00520; | 1.10.287.70;1.10.238.10;1.20.120.350; | Sodium channel (TC 1.A.1.10) family | null | SUBCELLULAR LOCATION: Cell membrane {ECO:0000255|RuleBase:RU361132, ECO:0000269|PubMed:28183995}; Multi-pass membrane protein {ECO:0000255|RuleBase:RU361132, ECO:0000269|PubMed:28183995}. | null | null | null | null | null | FUNCTION: Mediates the voltage-dependent sodium ion permeability of excitable membranes. {ECO:0000255|RuleBase:RU361132, ECO:0000305|PubMed:28183995}. | Periplaneta americana (American cockroach) (Blatta americana) |
D0E8I5 | PHNZ_UNCHF | MSLSNSSKVSVLISLLEKSRDLDYIGEAINQLEHSLQCAYFAQRSGADNEMVLAALLHDLGHYCNDTSFEDMGGYGVWQHEKVGADYLRGLGFSERVACLIEGHVAAKRYLVSSKASYLKNLSDASRKTLEYQGGPMDEGERRLFEEREDFKDCLKIRAWDEKGKQTDLKVPGPEHYRKMMEEHLSENQN | 1.13.11.78 | COFACTOR: Name=Fe cation; Xref=ChEBI:CHEBI:24875; Evidence={ECO:0000269|PubMed:22564006, ECO:0000269|PubMed:24198335, ECO:0000269|PubMed:24706911}; Note=Binds 2 iron ions per subunit. During catalysis, PhnZ uses a mixed-valent Fe(2+)/Fe(3+) cofactor. {ECO:0000269|PubMed:24198335, ECO:0000269|PubMed:24706911}; | null | null | hydrolase activity [GO:0016787]; metal ion binding [GO:0046872]; oxidoreductase activity [GO:0016491] | PF01966; | 1.10.3210.10; | null | null | null | CATALYTIC ACTIVITY: Reaction=(1R)-(2-amino-1-hydroxyethyl)phosphonate + O2 = glycine + 2 H(+) + phosphate; Xref=Rhea:RHEA:41444, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, ChEBI:CHEBI:43474, ChEBI:CHEBI:57305, ChEBI:CHEBI:141612; EC=1.13.11.78; Evidence={ECO:0000269|PubMed:22564006, ECO:0000269|PubMed:24198335, ECO:0000269|... | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=0.16 mM for (R,R)-2-amino-1-hydroxypropylphosphonic acid {ECO:0000269|PubMed:24706911}; KM=0.17 mM for (R)-2-amino-1-hydroxyethylphosphonic acid {ECO:0000269|PubMed:24706911}; Note=kcat is 11 min(-1) for (R)-2-amino-1-hydroxyethylphosphonic acid as substrate. kcat ... | null | null | null | FUNCTION: Involved in the degradation of the organophosphonate 2-aminoethylphosphonic acid (2-AEP) (Probable). Catalyzes the cleavage of the carbon-phosphorus bond of (2-amino-1-hydroxyethyl)phosphonic acid to yield glycine and phosphate through an oxidative mechanism (PubMed:22564006, PubMed:24198335, PubMed:24706911)... | Uncultured bacterium HF130_AEPn_1 |
D0EM77 | KLY_TANFA | MKRFILLFFLSTIAIFKVYSQRLYDNGPLTGDNNYVLQGSKWNKTTLKYYIYNSSSHLTTTERENAIRSAFALWSDKSTLSFIQVYNPNQADIKIKWEKGNHGDGYPFDGNTGILAHAFYPPPAGGNYAGHLHFDGDENWSINGSGIDLITVAAHEIGHLLGIEHSNVSSALMYPYYTGIKRQLDNDDCLAVWDLYGYPFSISGPSSVCDQATYTVENLLSGATVQWSVSNPNIATINSSNGVLTCRGNGICEVRATINNSSVALTPLKICLGTPISQDITLTVESLNSNGTLCTDNPNAIMADHPGGNHLGYIREYEWR... | 3.4.24.- | COFACTOR: Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000269|PubMed:21166898, ECO:0000269|PubMed:23695557}; Note=Binds 2 Zn(2+) ions per subunit. {ECO:0000269|PubMed:21166898, ECO:0000269|PubMed:23695557}; | collagen catabolic process [GO:0030574]; extracellular matrix organization [GO:0030198]; proteolysis [GO:0006508] | extracellular matrix [GO:0031012]; extracellular space [GO:0005615] | metalloendopeptidase activity [GO:0004222]; zinc ion binding [GO:0008270] | PF00413;PF18962; | 2.60.40.1080;3.40.390.10; | Peptidase M10A family | PTM: Processes itself into the mature 18-kDa enzyme (Kly18) through sequential autoproteolytic cleavage at both the N- and C-termini. However, the maturation intermediate Kly38 is found to be more active than Kly18 and the rate for its processing is slow, which raises the question as to whether Kly38 is a physiological... | SUBCELLULAR LOCATION: Secreted {ECO:0000305}. | null | null | null | BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 8 for casein degradation. Active in the broad pH range from 6.5 to 8.5. {ECO:0000269|PubMed:19919176}; | BIOPHYSICOCHEMICAL PROPERTIES: Temperature dependence: In the presence of CaCl(2), the enzyme is fully stable for up to 40 minutes at 70 degrees Celsius, whereas karilysin incubated without calcium loses 50% of its activity within 30 minutes. {ECO:0000269|PubMed:19919176}; | FUNCTION: Metalloprotease able to cleave casein, gelatin, elastin, fibrinogen and fibronectin. Shows exclusive preference for hydrophobic residues, especially Leu, Tyr and Met, at the P1' position of substrates, and for Pro or Ala at P3. Can efficiently cleave the antimicrobial peptide LL-37 which is a component of the... | Tannerella forsythia (strain ATCC 43037 / JCM 10827 / CCUG 21028 A / KCTC 5666 / FDC 338) (Bacteroides forsythus) |
D0EZM8 | NS1_HBOC1 | MAFNPPVIRAFSQPAFTYVFKFPYPQWKEKEWLLHALLAHGTEQSMIQLRNCAPHPDEDIIRDDLLISLEDRHFGAVLCKAVYMATTTLMSHKQRNMFPRCDIIVQSELGEKNLHCHIIVGGEGLSKRNAKSSCAQFYGLILAEIIQRCKSLLATRPFEPEEADIFHTLKKAEREAWGGVTGGNMQILQYRDRRGDLHAQTVDPLRFFKNYLLPKNRCISSYSKPDVCTSPDNWFILAEKTYSHTLINGLPLPEHYRKNYHATLDNEVIPGPQTMAYGGRGPWEHLPEVGDQRLAASSVSTTYKPNKKEKLMLNLLDKCK... | 3.1.21.-; 3.6.4.12 | COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250|UniProtKB:P03134}; Note=The endonuclease active site can probably bind other divalent cations. {ECO:0000250|UniProtKB:P03134}; | DNA replication [GO:0006260]; viral DNA genome replication [GO:0039693] | host cell nucleus [GO:0042025] | ATP binding [GO:0005524]; ATP hydrolysis activity [GO:0016887]; DNA binding [GO:0003677]; endonuclease activity [GO:0004519]; helicase activity [GO:0004386]; metal ion binding [GO:0046872] | PF01057; | 3.40.1310.20;3.40.50.300; | Parvoviruses initiator protein NS1 family | null | SUBCELLULAR LOCATION: Host nucleus {ECO:0000269|PubMed:20457462}. | 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:P03134}; | null | null | null | null | FUNCTION: Multifunctional protein which displays endonuclease and helicase activities required for initiating and directing viral DNA replication. Also plays a role in viral packaging and transactivation of several promoters. Binds site-specifically to 2-3 approximate tandem copies within the origins of replication (Or... | Primate bocaparvovirus 1 (strain Human bocavirus 1 type 1) (HBoV1) (Human bocavirus type 1) |
D0FH76 | VPS4_BOMMO | MTSSNTLQKAIDLVTKATEEDKNKNYEEALRLYEHGVEYFLHAVKYEAQGERAKESIRAKCLQYLDRAEKLKEYLKKDQKKKPVKDGESKSDDKKSDSDSDSDDPEKKKLQGKLEGAIVVEKPHVKWSDVAGLEAAKEALKEAVILPIKFPHLFTGKRIPWKGILLFGPPGTGKSYLAKAVATEANNSTFFSVSSSDLVSKWLGESEKLVKNLFDLARQHKPSIIFIDEIDSLCSSRSDNESESARRIKTEFLVQMQGVGNDMDGILVLGATNIPWVLDSAIRRRFEKRIYIALPEEHARLDMFKLHLGNTRHQLSEQDM... | 3.6.4.6 | null | cell cycle [GO:0007049]; cell division [GO:0051301]; endosomal transport [GO:0016197]; instar larval or pupal development [GO:0002165]; metamorphosis [GO:0007552]; protein complex oligomerization [GO:0051259]; protein transport [GO:0015031]; ubiquitin-dependent protein catabolic process via the multivesicular body sort... | cytoplasm [GO:0005737]; endosome membrane [GO:0010008]; late endosome membrane [GO:0031902]; midbody [GO:0030496]; vacuolar membrane [GO:0005774] | ATP binding [GO:0005524]; ATP hydrolysis activity [GO:0016887]; ATP-dependent protein disaggregase activity [GO:0140545]; protein self-association [GO:0043621] | PF00004;PF17862;PF04212;PF09336; | 1.10.8.60;3.40.50.300;1.20.58.80; | AAA ATPase family | null | SUBCELLULAR LOCATION: Prevacuolar compartment membrane {ECO:0000250|UniProtKB:Q8VEJ9}; Peripheral membrane protein {ECO:0000250|UniProtKB:Q8VEJ9}. Late endosome membrane {ECO:0000250|UniProtKB:Q9UN37}; Peripheral membrane protein {ECO:0000250|UniProtKB:Q9UN37}. Midbody {ECO:0000250|UniProtKB:Q9UN37}. Cytoplasm {ECO:000... | 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=3.6.4.6; Evidence={ECO:0000269|PubMed:23053938}; | null | null | null | null | FUNCTION: Involved in late steps of the endosomal multivesicular bodies (MVB) pathway. Recognizes membrane-associated ESCRT-III assemblies and catalyzes their disassembly, possibly in combination with membrane. {ECO:0000250|UniProtKB:Q9UN37}. | Bombyx mori (Silk moth) |
D0G895 | ACE3_MOUSE | MNLPWALLLVLLSHRQLLPWLRTVGETSLNDFYSEAQAKLFLQFYEQTAQVVLNEFMEATWNYVTNITKQNQKNMLQKEADRSQFMLYFSTRARMFRTDHFLNQDVKRMLRKLQNIDKSALPTEDLLEYNRLLTYMETAYNRAEVCLDEGPCLTLEPDLQEIMATSRDQKELLWAWQGWRDAVGRQLRPVFEDYVRLSNKAAQYNGYKDMGALWRSKYESDTLEEDLEQLYKELQPLYLNLHAYVRRSLYRYYGPELIDLRGPIPAHLLGNMWAQSWNNILDLVLPYPTKAPEDITAIMKIQHWRPEKMFEEANLFFTSM... | null | COFACTOR: Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000255|PROSITE-ProRule:PRU01355}; | positive regulation of systemic arterial blood pressure [GO:0003084]; proteolysis [GO:0006508]; regulation of systemic arterial blood pressure by renin-angiotensin [GO:0003081] | acrosomal membrane [GO:0002080]; acrosomal vesicle [GO:0001669]; plasma membrane [GO:0005886] | metal ion binding [GO:0046872]; metallopeptidase activity [GO:0008237]; peptidyl-dipeptidase activity [GO:0008241] | PF01401; | null | Peptidase M2 family | null | SUBCELLULAR LOCATION: Cytoplasmic vesicle, secretory vesicle, acrosome membrane {ECO:0000269|PubMed:20421979}; Multi-pass membrane protein {ECO:0000255}. Note=Disappears from acrosome reacted sperm. Co-localizes with IZUMO1 at acrosomal cap area. {ECO:0000269|PubMed:20421979}. | null | null | null | null | null | null | Mus musculus (Mouse) |
D0KN27 | HELS_SACS9 | MSLELEWMPIEDLKLPSNVIEIIKKRGIKKLNPPQTEAVKKGLLEGNRLLLTSPTGSGKTLIAEMGIISFLLKNGGKAIYVTPLRALTNEKYLTFKDWELIGFKVAMTSGDYDTDDAWLKNYDIIITTYEKLDSLWRHRPEWLNEVNYFVLDELHYLNDPERGPVVESVTIRAKRRNLLALSATISNYKQIAKWLGAEPVATNWRPVPLIEGVIYPERKKKEYNVIFKDNTTKKVHGDDAIIAYTLDSLSKNGQVLVFRNSRKMAESTALKIANYMNFVSLDENALSEILKQLDDIEEGGSDEKELLKSLISKGVAYHHA... | 5.6.2.4 | null | DNA repair [GO:0006281] | null | 3'-5' DNA helicase activity [GO:0043138]; ATP binding [GO:0005524]; ATP hydrolysis activity [GO:0016887]; DNA binding [GO:0003677]; isomerase activity [GO:0016853] | PF00270;PF00271;PF21280; | 1.10.3380.30;1.10.150.20;3.40.50.300; | Helicase family, Hel308 subfamily | null | null | CATALYTIC ACTIVITY: Reaction=Couples ATP hydrolysis with the unwinding of duplex DNA by translocating in the 3'-5' direction.; EC=5.6.2.4; Evidence={ECO:0000255|HAMAP-Rule:MF_00442, ECO:0000269|Ref.2}; CATALYTIC ACTIVITY: Reaction=ATP + H2O = ADP + H(+) + phosphate; Xref=Rhea:RHEA:13065, ChEBI:CHEBI:15377, ChEBI:CHEBI:... | null | null | null | null | FUNCTION: DNA-dependent ATPase and 3'-5' DNA helicase that may be involved in repair of stalled replication forks. A low processivity 3'-5' helicase. Unwinds short dsDNA substrates with 3'-overhangs (25 bp dsDNA with 25 base overhang), less active on longer dsDNA substrates. Also unwinds the lagging strand of a stalled... | Saccharolobus solfataricus (strain 98/2) (Sulfolobus solfataricus) |
D0LB45 | LYSX_GORB4 | MALDTPSSDLPVSTDDTAEHQPTPAHRPPSAADRRSVDLLEKIRRPRGFGAGAPKIAGTVVGVLAGIALLSSIFPLFRRLIHYPRDFIDNYIVSLPNTSLAWAFVLALVAIALSSRKRIAWWIATIYLVLFMVSNALLLVDPVATDFGVDTDERIQIWIGLGIDAAALIFLIVTYRQFYTRVRRGALFRALGVLIVGLTAATLVGWGLVWAWPGSLERTERLPYAFNRVVTFGSIDSRTFDGHHTHIVIDSALGLLGALALIAAATVLFRSQRLESLMTSDDEKLIRALITRFNDDDSLAYFSTRRDKAVVFSPDGRAAI... | 2.3.2.3; 6.1.1.6 | COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250}; Note=Binds 3 Mg(2+) ions per subunit. {ECO:0000250}; | diadenosine tetraphosphate biosynthetic process [GO:0015966]; lipid metabolic process [GO:0006629]; lysyl-tRNA aminoacylation [GO:0006430]; positive regulation of macrophage activation [GO:0043032]; response to antibiotic [GO:0046677] | aminoacyl-tRNA synthetase multienzyme complex [GO:0017101]; cytosol [GO:0005829]; extracellular space [GO:0005615]; plasma membrane [GO:0005886] | ATP adenylyltransferase activity [GO:0003877]; ATP binding [GO:0005524]; DNA binding [GO:0003677]; lysine-tRNA ligase activity [GO:0004824]; magnesium ion binding [GO:0000287]; phosphatidylglycerol lysyltransferase activity [GO:0050071]; tRNA binding [GO:0000049] | PF09924;PF00152;PF16995;PF01336; | 2.40.50.140; | LPG synthetase family; Class-II aminoacyl-tRNA synthetase family | null | SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}. | CATALYTIC ACTIVITY: Reaction=ATP + L-lysine + tRNA(Lys) = AMP + diphosphate + L-lysyl-tRNA(Lys); Xref=Rhea:RHEA:20792, Rhea:RHEA-COMP:9696, Rhea:RHEA-COMP:9697, ChEBI:CHEBI:30616, ChEBI:CHEBI:32551, ChEBI:CHEBI:33019, ChEBI:CHEBI:78442, ChEBI:CHEBI:78529, ChEBI:CHEBI:456215; EC=6.1.1.6; CATALYTIC ACTIVITY: Reaction=1,2... | null | null | null | null | FUNCTION: Catalyzes the production of L-lysyl-tRNA(Lys)transfer and the transfer of a lysyl group from L-lysyl-tRNA(Lys) to membrane-bound phosphatidylglycerol (PG), which produces lysylphosphatidylglycerol (LPG), one of the components of the bacterial membrane with a positive net charge. LPG synthesis contributes to t... | Gordonia bronchialis (strain ATCC 25592 / DSM 43247 / BCRC 13721 / JCM 3198 / KCTC 3076 / NBRC 16047 / NCTC 10667) (Rhodococcus bronchialis) |
D0N4K2 | CRE5_PHYIT | MQTIQLIIFVAFVLSRAAASISSFSDPTSIVNINHDANRLSRALAAGQNQTQRSLRQHEGEDRGAIDKADEVVSKMKALMGTAKNVPNNLAALIAKRSKTAGEFVRRPFLVSKLSKRYNIADQLSFSTLKQLDKIDNMRIVDIKNGIKGNKKTPNGMRRKIKHFEGMKTAPQKFLESHVGRDMQRYGKDGSRWLSAGVVTRTTDQGERQILLISSSNPARGDFLLPKGGWDRGEKIKKAALREVMEEGGVCRAL | 3.6.1.- | null | adenosine 5'-(hexahydrogen pentaphosphate) catabolic process [GO:1901911]; diadenosine hexaphosphate catabolic process [GO:1901909]; diadenosine pentaphosphate catabolic process [GO:1901907]; diphosphoinositol polyphosphate metabolic process [GO:0071543] | cytoplasm [GO:0005737]; extracellular region [GO:0005576]; host cell cytoplasm [GO:0030430]; host cell nucleolus [GO:0044196]; nucleus [GO:0005634] | bis(5'-adenosyl)-hexaphosphatase activity [GO:0034431]; bis(5'-adenosyl)-pentaphosphatase activity [GO:0034432]; diphosphoinositol-polyphosphate diphosphatase activity [GO:0008486]; endopolyphosphatase activity [GO:0000298]; metal ion binding [GO:0046872] | PF00293; | 3.90.79.10; | RxLR effector family; Nudix hydrolase family | null | SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:30329083}. Host cytoplasm {ECO:0000269|PubMed:30329083}. Host nucleus, host nucleolus {ECO:0000269|PubMed:30329083}. Host nucleus {ECO:0000269|PubMed:30329083}. | null | null | null | null | null | FUNCTION: Effector that is involved in host plant infection. Contributes to virulence during the early infection stage, by inhibiting plant defense responses induced by both PAMP-triggered immunity (PTI) and effector-triggered immunity (ETI). {ECO:0000269|PubMed:29312401, ECO:0000269|PubMed:30329083}. | Phytophthora infestans (strain T30-4) (Potato late blight agent) |
D0NPN8 | A3AEM_PHYIT | MRLAIMLSATAVAINFATSSAIDQTKVLVYGTPAHYIHDSAGRRLLRKNEENEETSEERAPNFNLANLNEEMFNVAALTERADAKKLAKQLMGNDKLADAAYMWWQHNRVTLDQIDTFLKLASRKTQGAKYNQIYNSYMMHLGLTGY | null | null | effector-mediated activation of plant hypersensitive response by symbiont [GO:0080185] | extracellular region [GO:0005576]; host cell cytoplasm [GO:0030430] | null | PF16810; | 1.10.10.2460; | RxLR effector family | PTM: Proteolytically cleaved. The cleavage site directly after the RxLR sequence and the high conservation among other effector proteins suggest that the RxLR motif might play a crucial role in the intracellular processing before secretion. {ECO:0000269|PubMed:28522546}.; PTM: glycosylated. {ECO:0000269|PubMed:28522546... | SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:15894622, ECO:0000269|PubMed:16965554, ECO:0000269|PubMed:17914356, ECO:0000269|PubMed:29312401}. Host cytoplasm {ECO:0000269|PubMed:15894622, ECO:0000269|PubMed:16965554, ECO:0000269|PubMed:17914356, ECO:0000269|PubMed:29312401}. | null | null | null | null | null | FUNCTION: Multifunctional effector that can suppress host BAK1/SERK3-mediated immunity through at least two different pathways (PubMed:19794118, PubMed:20457921, PubMed:21348873, PubMed:26348328). Manipulates plant immunity by targeting and stabilizing host E3 ligase CMPG1. By preventing the normal 26S proteasome-depen... | Phytophthora infestans (strain T30-4) (Potato late blight agent) |
D0P3S7 | ABLB1_PHYIT | MRSLLLTVLLNLVVLLATTGAVSSNLNTAVNYASTSKIRFLSTEYNADEKRSLRGDYNNEVTKEPNTSDEERAFSISKSAEYVKMVLYGFKLGFSPRTQSKTVLRYEDKLFTALYKSGETPRSLRTKHLDKASASVFFNRFKKWYDKNVGPS | null | null | null | extracellular region [GO:0005576]; host cell nucleolus [GO:0044196]; host cell plasma membrane [GO:0020002]; membrane [GO:0016020] | null | null | null | RxLR effector family | null | SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:30329083}. Host nucleus, host nucleolus {ECO:0000269|PubMed:30329083}. Host nucleus {ECO:0000269|PubMed:30329083}. Host cell membrane {ECO:0000269|PubMed:14999409}. | null | null | null | null | null | FUNCTION: Secreted effector that acts as an elicitor of hypersensitive response (HR) specifically on plants carrying defense protein RGA2/Rpi-blb1 (PubMed:18682852, PubMed:19794118, PubMed:19888819, PubMed:20479869, PubMed:21483488). Enhances P.infestans colonization of plant hosts Nicotiana benthamiana and potato Sola... | Phytophthora infestans (strain T30-4) (Potato late blight agent) |
D0PRN2 | NRX1B_CHICK | MGGFLRGSPEPGPAGGSGGSAGGRLALLWIVPLTLSGLLGVAWGASSLGAHHIHHFHGSSKHHSVPIAIYRSPASLRGGHAGTTYIFSKGGGQITYTWPPNDRPSTRADRLAIGFSTVQKEAVLVRVDSSTGLGDYLELHIHQGKIGVKFNVGTDDIAIEEINAIINDGKYHVVRFTRSGGNATLQVDNWPVIERYPAGNNDNERLAIARQRIPYRLGRVVDEWLLDKGRQLTIFNSQATIKIGGKERGHPFQGQLSGLYYNGLKVLNMAAENDANIVIEGNVRLVGEVPSSMTTESTATAMQSEMSTSVMETTTTLATS... | null | null | angiogenesis [GO:0001525]; cell adhesion [GO:0007155] | membrane [GO:0016020] | null | PF02210;PF01034; | 2.60.120.200; | Neurexin family | null | SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Single-pass type I membrane protein {ECO:0000305}. | null | null | null | null | null | FUNCTION: Neuronal cell surface protein that may be involved in cell recognition and cell adhesion by forming intracellular junctions through binding to neuroligins. May play a role in formation or maintenance of synaptic junctions. May mediate intracellular signaling (By similarity). Plays a role in angiogenesis. {ECO... | Gallus gallus (Chicken) |
D0PV95 | DDX3_CAEEL | MESNQSNNGGSGNAALNRGGRYVPPHLRGGDGGAAAAASAGGDDRRGGAGGGGYRRGGGNSGGGGGGGYDRGYNDNRDDRDNRGGSGGYGRDRNYEDRGYNGGGGGGGNRGYNNNRGGGGGGYNRQDRGDGGSSNFSRGGYNNRDEGSDNRGSGRSYNNDRRDNGGDGQNTRWNNLDAPPSRGTSKWENRGARDERIEQELFSGQLSGINFDKYEEIPVEATGDDVPQPISLFSDLSLHEWIEENIKTAGYDRPTPVQKYSIPALQGGRDLMSCAQTGSGKTAAFLVPLVNAILQDGPDAVHRSVTSSGGRKKQYPSALV... | 3.6.4.13 | null | cell differentiation [GO:0030154]; gamete generation [GO:0007276]; masculinization of hermaphroditic germ-line [GO:0042006]; negative regulation of gene expression [GO:0010629]; positive regulation of embryonic development [GO:0040019]; positive regulation of fertilization [GO:1905516]; regulation of translation [GO:00... | canonical inflammasome complex [GO:0061702]; cell leading edge [GO:0031252]; cytoplasm [GO:0005737]; cytoplasmic stress granule [GO:0010494]; lamellipodium [GO:0030027]; nucleus [GO:0005634]; P granule [GO:0043186]; plasma membrane [GO:0005886] | ATP binding [GO:0005524]; ATP hydrolysis activity [GO:0016887]; identical protein binding [GO:0042802]; molecular condensate scaffold activity [GO:0140693]; mRNA binding [GO:0003729]; RNA helicase activity [GO:0003724]; RNA strand annealing activity [GO:0033592] | PF00270;PF00271; | 3.40.50.300; | DEAD box helicase family, DDX3/DED1 subfamily | null | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:19361491, ECO:0000269|PubMed:26015579}. Cytoplasmic granule {ECO:0000269|PubMed:19361491, ECO:0000269|PubMed:26015579}. Nucleus {ECO:0000250|UniProtKB:O00571}. Cytoplasm, Stress granule {ECO:0000250|UniProtKB:O00571}. Inflammasome {ECO:0000250|UniProtKB:Q62167}. Cell ... | 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:27546789}; | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=1.3156 mM for ATP {ECO:0000269|PubMed:27546789}; | null | null | null | FUNCTION: Multifunctional ATP-dependent RNA helicase (PubMed:27546789). Plays a role in RNA remodeling, but is not required for RNA unwinding (PubMed:27546789). Binds to RNA in a concentration-dependent manner to stimulate annealing between two complementary strands of RNA (PubMed:26015579, PubMed:27546789). This proce... | Caenorhabditis elegans |
D0Q0Y7 | CNIH3_RAT | MAFTFAAFCYMLSLVLCAALIFFAIWHIIAFDELRTDFKSPIDQCNPVHARERLRNIERICFLLRKLVLPEYSIHSLFCVMFLCAQEWLTLGLNVPLLFYHFWRYFHCPADSSELAYDPPVVMNADTLSYCQKEAWCKLAFYLLSFFYYLYCMIYTLVSS | null | null | endoplasmic reticulum to Golgi vesicle-mediated transport [GO:0006888]; neurotransmitter receptor localization to postsynaptic specialization membrane [GO:0099645]; regulation of AMPA receptor activity [GO:2000311]; regulation of membrane potential [GO:0042391]; synaptic transmission, glutamatergic [GO:0035249] | AMPA glutamate receptor complex [GO:0032281]; COPII-coated ER to Golgi transport vesicle [GO:0030134]; dendrite [GO:0030425]; dendritic shaft [GO:0043198]; endoplasmic reticulum membrane [GO:0005789]; glutamatergic synapse [GO:0098978]; postsynaptic membrane [GO:0045211]; synapse [GO:0045202] | channel regulator activity [GO:0016247] | PF03311; | null | Cornichon family | null | SUBCELLULAR LOCATION: Postsynaptic cell membrane {ECO:0000269|PubMed:19265014}; Multi-pass membrane protein {ECO:0000269|PubMed:19265014}. Note=Also localizes to the cell membrane of extrasynaptic sites (dendritic shafts, spines of pyramidal cells). | null | null | null | null | null | FUNCTION: Regulates the trafficking and gating properties of AMPA-selective glutamate receptors (AMPARs). Promotes their targeting to the cell membrane and synapses and modulates their gating properties by regulating their rates of activation, deactivation and desensitization. {ECO:0000269|PubMed:19265014}. | Rattus norvegicus (Rat) |
D0QMC3 | MNDAL_MOUSE | MAEYKKIVLLKGLESMEDYQFRTVKSLLRKELKLTKKLQEDYDRIQLADWMEDKFPKYAGLDKLIKVCEHIKDLKDLAKKLKTEKAKVQKKKQGKCKTAVKKKGQDELSSSESLFINKESYKSVPSSKKKGKAIAKTEGEKKNKLTQDQDHLPETSGTDIKTEEDCLQNSPKPPPTSPSSSSNKKKRKEITKTEGGKKKKLTQEQAQLPEPLGTDIKKDEDCLQTPPKPPPTPPSSSLNKKRKSRREEETGVKKSKAAKEPDQPPCCEEPTARCQSPILHSSSSASSNIPSATNQKPQPQNQNIPRGAVLHSEPLTVMVL... | null | null | activation of innate immune response [GO:0002218]; cellular response to interferon-beta [GO:0035458]; negative regulation of cell growth [GO:0030308] | cytosol [GO:0005829]; nucleolus [GO:0005730]; nucleoplasm [GO:0005654]; nucleus [GO:0005634] | double-stranded DNA binding [GO:0003690] | PF02760;PF02758; | 1.10.533.10;2.40.50.140; | HIN-200 family | null | SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:19654412}. | null | null | null | null | null | FUNCTION: Suppresses cell growth when expressed ectopically. {ECO:0000269|PubMed:19654412}. | Mus musculus (Mouse) |
D0TZF0 | ISOA1_ORYSJ | MASLPHCLSARPLVVAAAPGRPGPGPGPWLRGGARRRNAAFSAGNAGRRVGLRRSVASAVEVGVGEDEEEGVEEEEEEVEAVVMPERYALGGACRVLAGMPAPLGATALDGGVNFAVYSAGASAASLCLFTPDDLEADEVTEEVPLDPLFNRTGNVWHVFIEGELHNMLYGYRFDGMFAPHCGQYFDVSNVVVDPYAKAVISRGEYGVPGPGGDCWPQMAGMIPLPYSTFDWQGDLPLRYPQKDLVIYEMHLRGFTKHSSSNVEHPGTYIGAISKLDYLKELGVNCVELMPCHEFNELEYFSCSSKMNFWGYSTINFFSP... | 3.2.1.68 | null | amylopectin biosynthetic process [GO:0010021]; starch biosynthetic process [GO:0019252]; starch catabolic process [GO:0005983] | chloroplast isoamylase complex [GO:0010368]; isoamylase complex [GO:0043033] | isoamylase activity [GO:0019156] | PF00128;PF02922;PF21156; | 3.20.20.80;2.60.40.1180;2.60.40.10; | Glycosyl hydrolase 13 family | null | SUBCELLULAR LOCATION: Plastid, chloroplast {ECO:0000255}. | CATALYTIC ACTIVITY: Reaction=Hydrolysis of (1->6)-alpha-D-glucosidic branch linkages in glycogen, amylopectin and their beta-limit dextrins.; EC=3.2.1.68; Evidence={ECO:0000269|PubMed:10333591}; | null | PATHWAY: Glycan biosynthesis; starch biosynthesis. {ECO:0000305}. | BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 6.5 at 30 degrees Celsius. {ECO:0000269|PubMed:10333591}; | null | FUNCTION: Starch-debranching enzyme involved in amylopectin biosynthesis in endosperm. Functions by removing excess branches or improper branches that interfere with the formation of double helices of the cluster chains of amylopectin and crystallization of starch (PubMed:10517831, PubMed:15618430, PubMed:16953433, Pub... | Oryza sativa subsp. japonica (Rice) |
D0VWM8 | TADBP_CAEEL | MADETPKVKTEPAAEVKSPLDEVKEIRKEAELTQTGSDEKKTTDPEFITVQDPNGDEPIELPTVDGVVLMTTLQASFPGATGLKYKNPKTGANRAVQVDPSGLKLIAPADGWENKTFFVIVAPQSERVRALSSADATSAKRRKVGSSDDSDSDDGRDGRSGRKRAVERDSQPVDLIVLGVDFKTTDECFQKYFEDIGTVVFCEIKRKSDGNSKGFGFVRMSSVGEQNKVLAIPQHMIDGRRCDVKVPDGRSLQDKQGRPSISRIFVGRLTDKVDEHQLRKVFGDEAKSYIETAVVTDVFIPKPFRGFAFVTLSSAEAAER... | null | null | determination of adult lifespan [GO:0008340]; hyperosmotic response [GO:0006972]; mRNA processing [GO:0006397]; positive regulation of gene expression [GO:0010628]; regulation of gene expression [GO:0010468]; response to oxidative stress [GO:0006979]; RNA splicing [GO:0008380] | cytoplasm [GO:0005737]; nucleoplasm [GO:0005654]; nucleus [GO:0005634] | chromatin binding [GO:0003682]; RNA binding [GO:0003723]; single-stranded RNA binding [GO:0003727] | PF00076;PF18694; | 3.30.70.330; | null | null | SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:22792076}. Cytoplasm {ECO:0000269|PubMed:22792076}. Note=Shuttles from the nucleus to the cytoplasm under stress conditions. {ECO:0000269|PubMed:22792076}. | null | null | null | null | null | FUNCTION: RNA-binding protein which regulates transcription, splicing and RNA-editing (PubMed:25391662). Limits the accumulation of double-stranded RNA by maintaining the abundance of the mature RNA transcripts that are formed from double-stranded precursor RNAs (PubMed:25391662). Stress response protein that acts down... | Caenorhabditis elegans |
D0VWR8 | PSBD_THEVL | ERGWFDILDDWLKRDRFVFVGWSGILLFPCAYLALGGWLTGTTFVTSWYTHGLASSYLEGCNFLTVAVSTPANSMGHSLLLLWGPEAQGDFTRWCQLGGLWTFIALHGAFGLIGFMLRQFEIARLVGVRPYNAIAFSAPIAVFVSVFLIYPLGQSSWFFAPSFGVAAIFRFLLFFQGFHNWTLNPFHMMGVAGVLGGALLCAIHGATVENTLFQDGEGASTFRAFNPTQAEETYSMVTANRFWSQIFGIAFSNKRWLHFFMLFVPVTGLWMSAIGVVGLALNLRSYDFISQEIRAAEDPEFETFYTKNLLLNEGIRAWMA... | 1.10.3.9 | COFACTOR: Note=The D1/D2 heterodimer binds P680, chlorophylls that are the primary electron donor of PSII, and subsequent electron acceptors. It shares a non-heme iron and each subunit binds pheophytin, quinone, additional chlorophylls, carotenoids and lipids. There is also a Cl(-1) ion associated with D1 and D2, which... | photosynthetic electron transport in photosystem II [GO:0009772] | photosystem II [GO:0009523]; plasma membrane-derived thylakoid membrane [GO:0031676] | chlorophyll binding [GO:0016168]; electron transporter, transferring electrons within the cyclic electron transport pathway of photosynthesis activity [GO:0045156]; metal ion binding [GO:0046872]; oxygen evolving activity [GO:0010242] | PF00124; | 1.20.85.10; | Reaction center PufL/M/PsbA/D family | null | SUBCELLULAR LOCATION: Cellular thylakoid membrane {ECO:0000255|HAMAP-Rule:MF_01383, ECO:0000269|PubMed:12518057, ECO:0000269|PubMed:19433803, ECO:0000269|PubMed:21499260, ECO:0000269|PubMed:23426624}; Multi-pass membrane protein {ECO:0000255|HAMAP-Rule:MF_01383, ECO:0000269|PubMed:12518057, ECO:0000269|PubMed:19433803,... | CATALYTIC ACTIVITY: Reaction=2 a plastoquinone + 2 H2O + 4 hnu = 2 a plastoquinol + O2; Xref=Rhea:RHEA:36359, Rhea:RHEA-COMP:9561, Rhea:RHEA-COMP:9562, ChEBI:CHEBI:15377, ChEBI:CHEBI:15379, ChEBI:CHEBI:17757, ChEBI:CHEBI:30212, ChEBI:CHEBI:62192; EC=1.10.3.9; Evidence={ECO:0000255|HAMAP-Rule:MF_01383}; | null | null | null | null | FUNCTION: Photosystem II (PSII) is a light-driven water:plastoquinone oxidoreductase that uses light energy to abstract electrons from H(2)O, generating O(2) and a proton gradient subsequently used for ATP formation. It consists of a core antenna complex that captures photons, and an electron transfer chain that conver... | Thermostichus vulcanus (Synechococcus vulcanus) |
D0VWU3 | LAC1_TRAMX | AVGPVADNTITDAATSPDGFSRQAVVVNGVTPGPLVAGNIGDRFQLNVIDNLTNHTMLKTTSVHWHGFFQQGTNWADGPAFINQCPISPGHSFLYDFQVPNQAGTFWYHSHLSTQYCDGLRGPFVVYDPNDPHASRYDVDNDDTVITLADWYHTAAKLGPRFPAGADATLINGKGRAPSDTSAELSVIKVTKGKRYRFRLVSLSCDPNFTFSIDGHNLTIIEVDSSNSQPLSVDSIQIFAAQRYSFVLNANQAVDNYWIRANPNFGNVGFNGGINSAILRYDGAPAVEPTTNQTTSVKPLNEVNLHPLVSTPVPGSPSSG... | 1.10.3.2 | COFACTOR: Name=Cu cation; Xref=ChEBI:CHEBI:23378; Evidence={ECO:0000269|PubMed:16944230, ECO:0000269|PubMed:17012782}; Note=Binds 4 Cu cations per monomer. {ECO:0000269|PubMed:16944230, ECO:0000269|PubMed:17012782}; | lignin catabolic process [GO:0046274] | extracellular region [GO:0005576] | copper ion binding [GO:0005507]; hydroquinone:oxygen oxidoreductase activity [GO:0052716]; oxidoreductase activity [GO:0016491] | PF00394;PF07731;PF07732; | 2.60.40.420; | Multicopper oxidase family | null | SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:16944230, ECO:0000269|PubMed:17012782}. | CATALYTIC ACTIVITY: Reaction=4 hydroquinone + O2 = 4 benzosemiquinone + 2 H2O; Xref=Rhea:RHEA:11276, ChEBI:CHEBI:15377, ChEBI:CHEBI:15379, ChEBI:CHEBI:17594, ChEBI:CHEBI:17977; EC=1.10.3.2; Evidence={ECO:0000269|PubMed:16944230, ECO:0000269|PubMed:17012782}; | null | null | null | null | FUNCTION: Lignin degradation and detoxification of lignin-derived products. {ECO:0000269|PubMed:16944230, ECO:0000269|PubMed:17012782, ECO:0000305}. | Trametes maxima (White-rot fungus) (Cerrena maxima) |
D0VWV4 | C560_PIG | MAALLLRHVGRHCLRAHLSPQLCIRNAVPLGTTAKEEMERFWNKNLGSNRPLSPHITIYRWSLPMAMSICHRGTGIALSAGVSLFGLSALLLPGNFESHLELVKSLCLGPTLIYTAKFGIVFPLMYHTWNGIRHLIWDLGKGLTIPQLTQSGVVVLILTVLSSVGLAAM | null | COFACTOR: Name=heme b; Xref=ChEBI:CHEBI:60344; Evidence={ECO:0000269|PubMed:15989954}; Note=The heme b is bound between the two transmembrane subunits SDHC and SDHD. {ECO:0000269|PubMed:15989954}; | mitochondrial electron transport, succinate to ubiquinone [GO:0006121]; tricarboxylic acid cycle [GO:0006099] | mitochondrial inner membrane [GO:0005743]; mitochondrial respiratory chain complex II, succinate dehydrogenase complex (ubiquinone) [GO:0005749]; plasma membrane [GO:0005886] | electron transfer activity [GO:0009055]; heme binding [GO:0020037]; metal ion binding [GO:0046872]; oxidoreductase activity, acting on the CH-CH group of donors [GO:0016627] | PF01127; | 1.20.1300.10;1.20.5.540; | Cytochrome b560 family | null | SUBCELLULAR LOCATION: Mitochondrion inner membrane {ECO:0000269|PubMed:17480203}; Multi-pass membrane protein {ECO:0000269|PubMed:17480203}. | null | null | PATHWAY: Carbohydrate metabolism; tricarboxylic acid cycle. | null | null | FUNCTION: Membrane-anchoring subunit of succinate dehydrogenase (SDH) that is involved in complex II of the mitochondrial electron transport chain and is responsible for transferring electrons from succinate to ubiquinone (coenzyme Q). {ECO:0000269|PubMed:17480203}. | Sus scrofa (Pig) |
D0VWY5 | GASHR_MARGR | MTQHFDLIAIGGGSGGLAVAEKAAAFGKRVALIESKALGGTCVNVGCVPKKVMWYASHLAEAVRDAPGFGVQASGGTLDWPRLVAGRDRYIGAINSFWDGYVERLGITRVDGHARFVDAHTIEVEGQRLSADHIVIATGGRPIVPRLPGAELGITSDGFFALQQQPKRVAIIGAGYIGIELAGLLRSFGSEVTVVALEDRLLFQFDPLLSATLAENMHAQGIETHLEFAVAALERDAQGTTLVAQDGTRLEGFDSVIWAVGRAPNTRDLGLEAAGIEVQSNGMVPTDAYQNTNVPGVYALGDITGRDQLTPVAIAAGRRL... | 1.8.1.16 | COFACTOR: Name=FAD; Xref=ChEBI:CHEBI:57692; Evidence={ECO:0000269|PubMed:11399772, ECO:0000269|PubMed:17977556}; Note=Binds 1 FAD per subunit. {ECO:0000269|PubMed:11399772, ECO:0000269|PubMed:17977556}; | cell redox homeostasis [GO:0045454]; cellular response to oxidative stress [GO:0034599]; glutathione metabolic process [GO:0006749] | cytosol [GO:0005829] | flavin adenine dinucleotide binding [GO:0050660]; glutathione-disulfide reductase (NADP) activity [GO:0004362]; metal ion binding [GO:0046872]; NADP binding [GO:0050661] | PF07992;PF02852; | 3.30.390.30;3.50.50.60; | Class-I pyridine nucleotide-disulfide oxidoreductase family | null | null | CATALYTIC ACTIVITY: Reaction=2 glutathione amide + NAD(+) = glutathione amide disulfide + H(+) + NADH; Xref=Rhea:RHEA:27433, ChEBI:CHEBI:15378, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945, ChEBI:CHEBI:59895, ChEBI:CHEBI:59896; EC=1.8.1.16; Evidence={ECO:0000269|PubMed:11399772}; | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=97 uM for glutathione amide disulfide (GASSAG) for the reverse reaction (in the presence of 100 uM NADH) {ECO:0000269|PubMed:11399772}; KM=6.9 mM for glutathione disulfide (GSH) for the reverse reaction {ECO:0000269|PubMed:11399772}; KM=13.2 uM for NADH for the rev... | null | null | null | FUNCTION: Catalyzes the reduction of glutathione amide disulfide (GASSAG) to restore glutathione amide (GASH) in the presence of NADH. May play a role in GASH metabolism under anaerobic conditions as a sulfide carrier necessary for cytoplasmic sulfide oxidation. {ECO:0000269|PubMed:11399772}. | Marichromatium gracile (Chromatium gracile) |
D0VYS2 | HSF3_MOUSE | MEQFRKTMVPHFLTKLWILVDDAVLDHVIRWGKDGHSFQIVNEETFAREVLPKYFKHNKITSFIRQLNMYGSRKVFALQTEKTSQENKISIEFQHPLFKRGEACLLANIKRKVPTIKIEGASLYSDEFQKIVTEMQEFKDMQRKMDAKYTQMKQDYSNLYHEVTNLRKKYCAQQQLLTRVLHFILDLMSENHTVLKKRKRSLSFISEDSDSEWDHQYFRIPEDKKEAMEILKDGYELVEDKYKSLLDRVMPILKESKKLISSGDQPSGDDGEHPKVPVQDKPMNEESLTIQLDLTIPVLPEQITEESVEQEPKDISLELD... | null | null | cellular response to heat [GO:0034605]; positive regulation of transcription by RNA polymerase II [GO:0045944]; regulation of transcription by RNA polymerase II [GO:0006357] | cytoplasm [GO:0005737]; nucleus [GO:0005634] | chromatin DNA binding [GO:0031490]; DNA-binding transcription factor activity [GO:0003700]; RNA polymerase II cis-regulatory region sequence-specific DNA binding [GO:0000978]; sequence-specific DNA binding [GO:0043565] | PF00447; | 1.10.10.10; | HSF family | null | SUBCELLULAR LOCATION: [Isoform 1]: Cytoplasm {ECO:0000269|PubMed:19864465}. Nucleus {ECO:0000269|PubMed:19864465}. Note=Cytoplasmic under normal conditions. Translocates to the nucleus in response to heat shock. {ECO:0000269|PubMed:19864465}.; SUBCELLULAR LOCATION: [Isoform 2]: Cytoplasm {ECO:0000269|PubMed:19864465}. ... | null | null | null | null | null | FUNCTION: DNA-binding protein that specifically binds heat shock promoter elements (HSE) and activates transcription of non-classical heat-shock genes such as PDZD2 and PROM2. Protects cells against heat shock and proteotoxic stress. {ECO:0000269|PubMed:19864465}. | Mus musculus (Mouse) |
D0WGK0 | ILVC_SLAES | MSVKTKEKEMAVTILYEQDVDPKVIQGLKVGIIGYGSQGHAHALNLMDSGVDVRVGLREGSSSWKTAEEAGLKVTDMDTAAEEADVIMVLVPDEIQPKVYQEHIAAHLKAGNTLAFAHGFNIHYGYIVPPEDVNVIMCAPKGPGHIVRRQFTEGSGVPDLACVQQDATGNAWDIVLSYCWGVGGARSGIIKATFAEETEEDLFGEQAVLCGGLVELVKAGFETLTEAGYPPELAYFECYHEMKMIVDLMYESGIHFMNYSISNTAEYGEYYAGPKVINEQSREAMKEILKRIQDGSFAQEFVDDCNNGHKRLLEQREAIN... | 1.1.1.86 | COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000255|HAMAP-Rule:MF_00435, ECO:0000269|PubMed:23776225}; Note=Binds 2 magnesium ions per subunit. {ECO:0000255|HAMAP-Rule:MF_00435}; | amino acid biosynthetic process [GO:0008652]; isoleucine biosynthetic process [GO:0009097]; valine biosynthetic process [GO:0009099] | cytosol [GO:0005829] | ketol-acid reductoisomerase activity [GO:0004455]; magnesium ion binding [GO:0000287]; NADP binding [GO:0050661] | PF01450;PF07991; | 6.10.240.10;3.40.50.720; | Ketol-acid reductoisomerase family | null | null | CATALYTIC ACTIVITY: Reaction=(2R)-2,3-dihydroxy-3-methylbutanoate + NADP(+) = (2S)-2-acetolactate + H(+) + NADPH; Xref=Rhea:RHEA:22068, ChEBI:CHEBI:15378, ChEBI:CHEBI:49072, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349, ChEBI:CHEBI:58476; EC=1.1.1.86; Evidence={ECO:0000255|HAMAP-Rule:MF_00435, ECO:0000269|PubMed:23776225}; CAT... | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=1 uM for NADPH (at pH 7) {ECO:0000269|PubMed:23776225}; KM=45 uM for NADH (at pH 7) {ECO:0000269|PubMed:23776225}; Note=kcat is 0.8 sec(-1) for reductoisomerase activity with NADPH as substrate (at pH 7). kcat is 0.41 sec(-1) for reductoisomerase activity with NADH... | PATHWAY: Amino-acid biosynthesis; L-isoleucine biosynthesis; L-isoleucine from 2-oxobutanoate: step 2/4. {ECO:0000255|HAMAP-Rule:MF_00435}.; PATHWAY: Amino-acid biosynthesis; L-valine biosynthesis; L-valine from pyruvate: step 2/4. {ECO:0000255|HAMAP-Rule:MF_00435}. | null | null | FUNCTION: Involved in the biosynthesis of branched-chain amino acids (BCAA). Catalyzes an alkyl-migration followed by a ketol-acid reduction of (S)-2-acetolactate (S2AL) to yield (R)-2,3-dihydroxy-isovalerate. In the isomerase reaction, S2AL is rearranged via a Mg-dependent methyl migration to produce 3-hydroxy-3-methy... | Slackia exigua (strain ATCC 700122 / DSM 15923 / CIP 105133 / JCM 11022 / KCTC 5966 / S-7) |
D0Z5N4 | E2AKB_CAEEL | MTKENQIVLDERVKENQHLQEEEKLALDAVYLNQITYIKAHWHVWVPTNCHILLKALDSCFLNGDPLGKSKLSVILHVKCSEDYPQRKPAVDLLDPQGLSKEDVQNLLTILRQMADTWEGCVVIAELAHRVREFLTDHTPRPAGSFHDDMLANKVRTEAEKQRKRLDTEQKELELLEEEMRQRNAIEMEKTLNGTRQENETRIIGGRRIVVLSNMPNTQLLISEWTFRFSSNRNPAEGKRKDFAPFLQKLDAVYNEIQKLCEIKGLDQNLVEYAFVHLQKISVSPDQILIQLNVAQKIFSSEENMQDTYELIVQKSNLLR... | 2.7.11.1 | null | cellular homeostasis [GO:0019725]; determination of adult lifespan [GO:0008340]; mitochondrial unfolded protein response [GO:0034514]; negative regulation of cytoplasmic translational initiation in response to stress [GO:1990625]; negative regulation of gene expression [GO:0010629]; positive regulation of gene expressi... | cytoplasm [GO:0005737]; cytosol [GO:0005829]; nucleus [GO:0005634] | ATP binding [GO:0005524]; eukaryotic translation initiation factor 2alpha kinase activity [GO:0004694]; protein serine kinase activity [GO:0106310] | PF00069;PF05773;PF13393; | 1.10.510.10;3.10.110.10; | Protein kinase superfamily, Ser/Thr protein kinase family, GCN2 subfamily | null | null | CATALYTIC ACTIVITY: Reaction=ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-[protein]; Xref=Rhea:RHEA:17989, Rhea:RHEA-COMP:9863, Rhea:RHEA-COMP:11604, ChEBI:CHEBI:15378, ChEBI:CHEBI:29999, ChEBI:CHEBI:30616, ChEBI:CHEBI:83421, ChEBI:CHEBI:456216; EC=2.7.11.1; Evidence={ECO:0000250|UniProtKB:Q19192}; CATALYTI... | null | null | null | null | FUNCTION: Serine/threonine-protein kinase which phosphorylates the alpha subunit of eukaryotic translation-initiation factor 2 (eIF2alpha), leading to its inactivation and thus to a rapid reduction of translational initiation and repression of global protein synthesis (By similarity). Involved in the unfolded protein r... | Caenorhabditis elegans |
D0ZKX9 | RSEP_SALT1 | MLSILWNLAAFIIALGVLITVHEFGHFWVARRCGVRVERFSIGFGKALWRRTDRYGTEYVIALIPLGGYVKMLDERAEPVAPELRRHAFNNKTVGQRAAIIAAGPVANFIFAIFAYWLVFIIGVPGVRPVIGEITPNSIAAQAQIAPGTELKAVDGIETPDWDAVRLQLVSKIGDQQTTVSVAPFGSDQRQDKTLDLRHWAFEPDKQDPVSSLGIRPRGPQIEPVLSEVQANSAASKAGLQAGDRIVKVDGQPLTQWMKFVTFVRDNPGKPLALEIERQGSALSLTLTPDTKSVNGKAEGFAGVVPKIIPLPEEYKTIRQ... | 3.4.24.- | COFACTOR: Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000250}; | cellular stress response to acid chemical [GO:0097533]; proteolysis [GO:0006508]; response to temperature stimulus [GO:0009266] | plasma membrane [GO:0005886] | metal ion binding [GO:0046872]; metalloendopeptidase activity [GO:0004222] | PF17820;PF02163; | 2.30.42.10; | Peptidase M50B family | null | SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}. | null | null | null | null | null | FUNCTION: A site-2 regulated intramembrane protease that cleaves the peptide bond between 'Ala-108' and 'Cys-109' in the transmembrane region of RseA. Part of a regulated intramembrane proteolysis (RIP) cascade. Acts on DegS-cleaved RseA to release the cytoplasmic domain of RseA. This provides the cell with sigma-E (Rp... | Salmonella typhimurium (strain 14028s / SGSC 2262) |
D0ZPH9 | SSPH2_SALT1 | MPFHIGSGCLPATISNRRIYRIAWSDTPPEMSSWEKMKEFFCSTHQTEALECIWTICHPPAGTTREDVINRFELLRTLAYAGWEESIHSGQHGENYFCILDEDSQEILSVTLDDAGNYTVNCQGYSETHRLTLDTAQGEEGTGHAEGASGTFRTSFLPATTAPQTPAEYDAVWSAWRRAAPAEESRGRAAVVQKMRACLNNGNAVLNVGESGLTTLPDCLPAHITTLVIPDNNLTSLPALPPELRTLEVSGNQLTSLPVLPPGLLELSIFSNPLTHLPALPSGLCKLWIFGNQLTSLPVLPPGLQELSVSDNQLASLPAL... | 2.3.2.27 | null | protein secretion by the type III secretion system [GO:0030254]; protein ubiquitination [GO:0016567] | extracellular region [GO:0005576]; host cell cytoplasm [GO:0030430]; host cell plasma membrane [GO:0020002]; membrane [GO:0016020] | ubiquitin-protein transferase activity [GO:0004842] | PF14496; | 1.20.58.90;3.80.10.10;3.30.2440.10;1.20.58.360;1.20.1270.130; | LRR-containing bacterial E3 ligase family | PTM: Ubiquitinated in the presence of host E1 ubiquitin-activating enzyme UBA1, E2 ubiquitin-conjugating enzyme UBE2D2 and ubiquitin. {ECO:0000269|PubMed:19273841}. | SUBCELLULAR LOCATION: Secreted. Host cytoplasm. Host apical cell membrane; Peripheral membrane protein; Cytoplasmic side. Note=Secreted via type III secretion system 2 (SPI-2 T3SS), and delivered into the host cytoplasm. Localizes at the periphery of the host cell, specifically in areas of actin polymerization. Localiz... | CATALYTIC ACTIVITY: Reaction=S-ubiquitinyl-[E2 ubiquitin-conjugating enzyme]-L-cysteine + [acceptor protein]-L-lysine = [E2 ubiquitin-conjugating enzyme]-L-cysteine + N(6)-ubiquitinyl-[acceptor protein]-L-lysine.; EC=2.3.2.27; | null | null | null | null | FUNCTION: Effector proteins function to alter host cell physiology and promote bacterial survival in host tissues. This protein is an E3 ubiquitin ligase that interferes with host's ubiquitination pathway. Contributes to virulence in calves. {ECO:0000269|PubMed:10564523, ECO:0000269|PubMed:19273841}. | Salmonella typhimurium (strain 14028s / SGSC 2262) |
D0ZV89 | PHOQ_SALT1 | MNKFARHFLPLSLRVRFLLATAGVVLVLSLAYGIVALVGYSVSFDKTTFRLLRGESNLFYTLAKWENNKISVELPENLDMQSPTMTLIYDETGKLLWTQRNIPWLIKSIQPEWLKTNGFHEIETNVDATSTLLSEDHSAQEKLKEVREDDDDAEMTHSVAVNIYPATARMPQLTIVVVDTIPIELKRSYMVWSWFVYVLAANLLLVIPLLWIAAWWSLRPIEALAREVRELEDHHREMLNPETTRELTSLVRNLNQLLKSERERYNKYRTTLTDLTHSLKTPLAVLQSTLRSLRNEKMSVSKAEPVMLEQISRISQQIGY... | 2.7.13.3; 3.1.3.- | COFACTOR: Name=Ca(2+); Xref=ChEBI:CHEBI:29108; Evidence={ECO:0000269|PubMed:16096064}; Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000269|PubMed:16096064}; Note=Binds up to 3 divalent cations (Ca(2+) or Mg(2+)); their binding site probably overlaps with that of cationic antimicrobial peptides that induce the op... | null | plasma membrane [GO:0005886] | ATP binding [GO:0005524]; metal ion binding [GO:0046872]; phosphoprotein phosphatase activity [GO:0004721]; phosphorelay sensor kinase activity [GO:0000155] | PF02518;PF08918; | 1.10.287.130;3.30.450.140;3.30.565.10; | null | null | SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000250}; Multi-pass membrane protein {ECO:0000250}. | CATALYTIC ACTIVITY: Reaction=ATP + protein L-histidine = ADP + protein N-phospho-L-histidine.; EC=2.7.13.3; | null | null | null | null | FUNCTION: Member of the two-component regulatory system PhoP/PhoQ which regulates the expression of genes involved in virulence, adaptation to acidic and low Mg(2+) environments and resistance to host defense antimicrobial peptides. Essential for intramacrophage survival of S.typhimurium. In low periplasmic Mg(2+), Pho... | Salmonella typhimurium (strain 14028s / SGSC 2262) |
D0ZVG2 | SSPH1_SALT1 | MFNIRNTQPSVSMQAIAGAAAPEASPEEIVWEKIQVFFPQENYEEAQQCLAELCHPARGMLPDHISSQFARLKALTFPAWEENIQCNRDGINQFCILDAGSKEILSITLDDAGNYTVNCQGYSEAHDFIMDTEPGEECTEFAEGASGTSLRPATTVSQKAAEYDAVWSKWERDAPAGESPGRAAVVQEMRDCLNNGNPVLNVGASGLTTLPDRLPPHITTLVIPDNNLTSLPELPEGLRELEVSGNLQLTSLPSLPQGLQKLWAYNNWLASLPTLPPGLGDLAVSNNQLTSLPEMPPALRELRVSGNNLTSLPALPSGLQ... | 2.3.2.27 | null | protein secretion by the type III secretion system [GO:0030254]; protein ubiquitination [GO:0016567] | extracellular region [GO:0005576]; host cell cytoplasm [GO:0030430]; host cell nucleus [GO:0042025] | ubiquitin-protein transferase activity [GO:0004842] | PF00560;PF14496; | 1.20.58.90;3.80.10.10;3.30.2440.10;1.20.58.360;1.20.1270.130; | LRR-containing bacterial E3 ligase family | PTM: Ubiquitinated in the presence of host E1 ubiquitin-activating enzyme, E2 ubiquitin-conjugating enzyme and ubiquitin. {ECO:0000250|UniProtKB:D0ZPH9}. | SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:10564523, ECO:0000269|PubMed:10861017}. Host cytoplasm {ECO:0000269|PubMed:10564523, ECO:0000269|PubMed:10861017}. Host nucleus {ECO:0000269|PubMed:16611232}. Note=Secreted via type III secretion systems 1 and 2 (SPI-1 and SPI-2 T3SS), and delivered into the host cytop... | CATALYTIC ACTIVITY: Reaction=S-ubiquitinyl-[E2 ubiquitin-conjugating enzyme]-L-cysteine + [acceptor protein]-L-lysine = [E2 ubiquitin-conjugating enzyme]-L-cysteine + N(6)-ubiquitinyl-[acceptor protein]-L-lysine.; EC=2.3.2.27; Evidence={ECO:0000269|PubMed:18005683}; | null | null | null | null | FUNCTION: Effector proteins function to alter host cell physiology and promote bacterial survival in host tissues (PubMed:10564523, PubMed:16611232, PubMed:18005683, PubMed:24248594). This protein is an E3 ubiquitin-protein ligase that interferes with the host's ubiquitination pathway and targets host proteins for prot... | Salmonella typhimurium (strain 14028s / SGSC 2262) |
Subsets and Splits
No community queries yet
The top public SQL queries from the community will appear here once available.