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 |
|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|
A1B8Z0 | BHCD_PARDP | MLVVAEKEIAGLMTPEAAFEAIEAVFASMARRKAYNFPVVREAIGHEDALYGFKGGFDASALVLGLKAGGYWPNNQKHNLINHQSTVFLFDPDTGRVSAAVGGNLLTALRTAAASAVSIKYLAPKGAKVLGMIGAGHQSAFQMRAAANVHRFEKVIGWNPHPEMLSRLADTAAELGLPFEAVELDRLGAEADVIVSITSSFSPLLMNEHVKGPTHIAAMGTDTKGKQELDPALVARARIFTDEVAQSVSIGECQHAIAAGLIREDQVGELGAVVAGDDPGRGDAEVTIFDGTGVGLQDLAVAQAVVELAKHKGVAQEVEI | 1.4.1.- | null | glycolate catabolic process [GO:0046296]; glyoxylate catabolic process [GO:0009436]; thyroid hormone metabolic process [GO:0042403] | cytoplasm [GO:0005737] | NADH binding [GO:0070404]; oxidoreductase activity, acting on the CH-NH2 group of donors, NAD or NADP as acceptor [GO:0016639]; thyroid hormone binding [GO:0070324] | PF02423; | 3.40.50.720;3.30.1780.10; | Ornithine cyclodeaminase/mu-crystallin family, BhcD subfamily | null | null | CATALYTIC ACTIVITY: Reaction=L-aspartate + NAD(+) = H(+) + iminosuccinate + NADH; Xref=Rhea:RHEA:42440, ChEBI:CHEBI:15378, ChEBI:CHEBI:29991, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945, ChEBI:CHEBI:77875; Evidence={ECO:0000269|PubMed:31723261}; PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:42442; Evidence={ECO:0000269... | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=0.09 mM for iminosuccinate {ECO:0000269|PubMed:31723261}; KM=0.02 mM for NADH {ECO:0000269|PubMed:31723261}; KM=0.33 mM for NADPH {ECO:0000269|PubMed:31723261}; Note=kcat is 201 sec(-1). {ECO:0000269|PubMed:31723261}; | null | null | null | FUNCTION: Imine reductase that catalyzes the NADH-dependent reduction of iminosuccinate to L-aspartate. Is essential for the growth of P.denitrificans in the presence of glycolate and glyoxylate since it functions in glyoxylate assimilation via the beta-hydroxyaspartate cycle (BHAC). Thereby BhcD regenerates the amino ... | Paracoccus denitrificans (strain Pd 1222) |
A1B8Z1 | BHCC_PARDP | MNAKTDFSGYEVGYDIPALPGMDESEIQTPCLILDLDALERNIRKMGDYAKAHGMRHRSHGKMHKSVDVQKLQESLGGSVGVCCQKVSEAEAFARGGIKDVLVTNEVREPAKIDRLARLPKTGATVTVCVDDVQNIADLSAAAQKHGTELGIFVEIDCGAGRCGVTTKEAVVEIAKAAAAAPNLTFKGIQAYQGAMQHMDSFEDRKAKLDAAIAQVKEAVDALEAEGLAPEFVSGGGTGSYYFESNSGIYNELQCGSYAFMDADYGRIHDAEGKRIDQGEWENALFILTSVMSHAKPHLAVVDAGLKAQSVDSGLPFVYG... | 4.1.3.41 | COFACTOR: Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326; Evidence={ECO:0000269|PubMed:31723261}; Note=Binds 1 pyridoxal phosphate per subunit. {ECO:0000269|PubMed:31723261}; COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000269|PubMed:31723261}; | D-serine catabolic process [GO:0036088]; glycolate catabolic process [GO:0046296]; glyoxylate catabolic process [GO:0009436] | null | D-serine ammonia-lyase activity [GO:0008721]; magnesium ion binding [GO:0000287]; oxo-acid-lyase activity [GO:0016833]; pyridoxal phosphate binding [GO:0030170] | PF01168;PF14031; | 3.20.20.10;2.40.37.20; | DSD1 family | null | null | CATALYTIC ACTIVITY: Reaction=(3S)-3-hydroxy-D-aspartate = glycine + glyoxylate; Xref=Rhea:RHEA:27934, ChEBI:CHEBI:36655, ChEBI:CHEBI:57305, ChEBI:CHEBI:60894; EC=4.1.3.41; Evidence={ECO:0000269|PubMed:31723261}; PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:27936; Evidence={ECO:0000269|PubMed:31723261}; CATALYTI... | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=0.23 mM for glyoxylate {ECO:0000269|PubMed:31723261}; KM=4.31 mM for glycine {ECO:0000269|PubMed:31723261}; KM=0.28 mM for (3S)-3-hydroxy-D-aspartate {ECO:0000269|PubMed:31723261}; KM=9.24 mM for D-threonine {ECO:0000269|PubMed:31723261}; Note=kcat is 91 sec(-1) fo... | null | null | null | FUNCTION: Catalyzes the condensation of glyoxylate and glycine into (2R,3S)-beta-hydroxyaspartate ((3S)-3-hydroxy-D-aspartate). Is essential for the growth of P.denitrificans in the presence of glycolate and glyoxylate since it functions in glyoxylate assimilation via the beta-hydroxyaspartate cycle (BHAC). Is also abl... | Paracoccus denitrificans (strain Pd 1222) |
A1B8Z2 | BHCB_PARDP | MYIPTYEDMLAAHERIKPHIRRTPIRTSDYLNELTGAQLFFKCENFQEPGAFKVRGATNAVFGLDDAQAAKGVATHSSGNHASCLSYAAMLRGIPCNVVMPRTAPQAKKDTVRRYGGVITECEPSTSSREETFAKVQAETGGDFVHPYNDPRVIAGQGTCAKELVEQVDGLDAVVAPIGGGGMISGTCLTLSTLAPETRVIAAEPEQADDAYRSFKAGYIIADDAPKTVADGLLVPLKDLTWHFVKNHVSEIYTASDAEIVDAMKLIWKHLRIVMEPSSAVPLATILKNPEAFAGKRVGVIVTGGNVDLDKLPWN | 4.2.1.- | COFACTOR: Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326; Evidence={ECO:0000305|PubMed:31723261}; | D-serine biosynthetic process [GO:0070179]; glycolate catabolic process [GO:0046296]; glyoxylate catabolic process [GO:0009436] | cytoplasm [GO:0005737] | ATP binding [GO:0005524]; D-serine ammonia-lyase activity [GO:0008721]; hydro-lyase activity [GO:0016836]; L-serine ammonia-lyase activity [GO:0003941]; magnesium ion binding [GO:0000287]; pyridoxal phosphate binding [GO:0030170]; serine racemase activity [GO:0030378]; threonine racemase activity [GO:0018114] | PF00291; | 3.40.50.1100; | null | null | null | CATALYTIC ACTIVITY: Reaction=(3S)-3-hydroxy-D-aspartate = H2O + iminosuccinate; Xref=Rhea:RHEA:62112, ChEBI:CHEBI:15377, ChEBI:CHEBI:60894, ChEBI:CHEBI:77875; Evidence={ECO:0000269|PubMed:31723261}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:62113; Evidence={ECO:0000269|PubMed:31723261}; | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=0.2 mM for (3S)-3-hydroxy-D-aspartate {ECO:0000269|PubMed:31723261}; Note=kcat is 35 sec(-1). {ECO:0000269|PubMed:31723261}; | null | null | null | FUNCTION: Catalyzes the dehydration of (2R,3S)-beta-hydroxyaspartate ((3S)-3-hydroxy-D-aspartate) into iminosuccinate. Is essential for the growth of P.denitrificans in the presence of glycolate and glyoxylate since it functions in glyoxylate assimilation via the beta-hydroxyaspartate cycle (BHAC). {ECO:0000269|PubMed:... | Paracoccus denitrificans (strain Pd 1222) |
A1B8Z3 | BHCA_PARDP | MTSQNPIFIPGPTNIPEEMRKAVDMPTIDHRSPVFGRMLHPALEGVKKVLKTTQAQVFLFPSTGTGGWETAITNTLSPGDKVLAARNGMFSHRWIDMCQRHGLDVTFVETPWGEGVPADRFEEILTADKGHEIRVVLATHNETATGVKSDIAAVRRALDAAKHPALLFVDGVSSIGSMDFRMDEWGVDIAVTGSQKGFMLPPGLAIVGFSPKAMEAVETARLPRTFFDIRDMATGYARNGYPYTPPVGLINGLNASCERILAEGLENVFARHHRIASGVRAAVDAWGLKLCAVRPELYSDSVSAIRVPEGFDANLIVSHA... | 2.6.1.35 | COFACTOR: Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326; Evidence={ECO:0000305|PubMed:31723261}; | glycine biosynthetic process, by transamination of glyoxylate [GO:0019265]; glycolate catabolic process [GO:0046296]; glyoxylate catabolic process [GO:0009436] | peroxisome [GO:0005777] | alanine-glyoxylate transaminase activity [GO:0008453]; glycine-oxaloacetate transaminase activity [GO:0047303]; serine-pyruvate transaminase activity [GO:0004760] | PF00266; | 3.90.1150.10;3.40.640.10; | Class-V pyridoxal-phosphate-dependent aminotransferase family | null | null | CATALYTIC ACTIVITY: Reaction=glycine + oxaloacetate = glyoxylate + L-aspartate; Xref=Rhea:RHEA:17141, ChEBI:CHEBI:16452, ChEBI:CHEBI:29991, ChEBI:CHEBI:36655, ChEBI:CHEBI:57305; EC=2.6.1.35; Evidence={ECO:0000269|PubMed:31723261}; PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:17143; Evidence={ECO:0000269|PubMed:... | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=0.43 mM for glyoxylate {ECO:0000269|PubMed:31723261}; KM=2.51 mM for L-aspartate {ECO:0000269|PubMed:31723261}; KM=9.52 mM for glycine {ECO:0000269|PubMed:31723261}; KM=2.9 mM for oxaloacetate {ECO:0000269|PubMed:31723261}; KM=2.1 mM for L-serine {ECO:0000269|PubMe... | null | null | null | FUNCTION: Catalyzes the transamination of glyoxylate into glycine using L-aspartate as the preferred amino group donor. Is essential for the growth of P.denitrificans in the presence of glycolate and glyoxylate since it functions in glyoxylate assimilation via the beta-hydroxyaspartate cycle (BHAC). Can catalyze the re... | Paracoccus denitrificans (strain Pd 1222) |
A1C3L3 | FAP1_STRPA | MGKYKRAGETSRKTRVKMHKSGKNWVRTLISQIGLMHFLGGSISEKKINVDVYEQKNISASTILKGAVALGALTGATVVSGNVFADETVLAKETTLTTTDANEVKLSSENFDSEKAEEKISLSQSESASESVSESISESVSESVSTSESVSESVSESVSESISESVSESISESISESVSESTSTSIVLSESGAASGNKATSKGTEEKQDSVRENLDKMISEAEVLNDMAARKLITLDAEQQLELMKSLVATQSQLEATKNLIGDPNATVADLQIAYTTLGNNTQALGNELIKLNPNGQIYAVLNNTEASRAATLRSTTTG... | null | null | cell adhesion [GO:0007155] | cytoplasm [GO:0005737]; extracellular region [GO:0005576]; pilus [GO:0009289] | null | PF04286;PF00746;PF19258; | 2.60.40.2010;1.20.5.420; | Serine-rich repeat protein (SRRP) family | PTM: Glycosylated; occurs within the cytoplasm (PubMed:16997950, PubMed:20164186, PubMed:9632253). It is probable that most of the Ser residues in SSR1 and SSR2 are O-GlcNAcylated. Sequential glycosylation by sugar transferases are able to generate complex sugar polymorphisms (By similarity). {ECO:0000250|UniProtKB:A0A... | SUBCELLULAR LOCATION: Cytoplasm. Secreted. Secreted, cell wall; Peptidoglycan-anchor. Fimbrium. Note=Primarily but not exclusively exported by the accessory SecA2/SecY2 protein translocation apparatus. | null | null | null | null | null | FUNCTION: The major structural element of fimbriae. Required for adherence to saliva-coated hydroxyapatite beads (SHA), an in vitro tooth model. A Fap1-dependent increase in adherence is seen as the pH is reduced from pH 8 to pH 5. {ECO:0000269|PubMed:10594831, ECO:0000269|PubMed:9632253}. | Streptococcus parasanguinis |
A1C3L9 | GTFA_STRPA | MTIYNINLGIGWASSGVEYAQAYRAQILRSLGMPAKFIFTNMFQSENLEHFTKNIGFEDNEIIWLYGYFTDVKISGTTYKKDDLEATFSQCPTKKEASSDRKLIRYYFENQELYINASLYGENQEYVQRVEYVVKGKLIRKDYYSYTKVFSEFYSPGENGVQLCNRSFYNEDGSIAYEEILSNEKSTFVFSNKICYGLEELLEFMLEDLSLTKSDLILLDRATGIGQVVFENIGAAKLAVVIHAEHFNEKNTDEHNILWNNYYEYQFTNADKVNAFITSTERQKILLEEQFTQYTSLHPKIVAIPVGSLDQLKFPEQSRK... | 2.4.1.- | null | glycolipid biosynthetic process [GO:0009247]; protein O-linked glycosylation via serine [GO:0018242]; sulfolipid biosynthetic process [GO:0046506] | cytoplasm [GO:0005737]; plasma membrane [GO:0005886]; protein N-acetylglucosaminyltransferase complex [GO:0017122] | glycosyltransferase activity [GO:0016757]; nucleotide binding [GO:0000166]; UDP-sulfoquinovose:DAG sulfoquinovosyltransferase activity [GO:0046510] | PF00534; | 3.40.50.2000; | Glycosyltransferase group 1 family, Glycosyltransferase 4 subfamily | null | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_01472, ECO:0000269|PubMed:21862581}. Cell membrane {ECO:0000255|HAMAP-Rule:MF_01472, ECO:0000269|PubMed:21862581}; Peripheral membrane protein {ECO:0000255|HAMAP-Rule:MF_01472, ECO:0000305|PubMed:21862581}. Note=Cell membrane association requires GtfB (Gtf2), p... | CATALYTIC ACTIVITY: Reaction=L-seryl-[protein] + UDP-N-acetyl-alpha-D-glucosamine = 3-O-[N-acetyl-alpha-D-glucosaminyl]-L-seryl-[protein] + H(+) + UDP; Xref=Rhea:RHEA:59872, Rhea:RHEA-COMP:9863, Rhea:RHEA-COMP:15471, ChEBI:CHEBI:15378, ChEBI:CHEBI:29999, ChEBI:CHEBI:57705, ChEBI:CHEBI:58223, ChEBI:CHEBI:143279; Evidenc... | null | PATHWAY: Protein modification; protein glycosylation. {ECO:0000255|HAMAP-Rule:MF_01472}. | null | null | FUNCTION: Required for polymorphic O-glycosylation of serine-rich repeat protein Fap1. Catalyzes the first step in glycosylation by transferring N-acetylglucosamine from UDP-GlcNAc to serine residues in Fap1. Part of the accessory SecA2/SecY2 system specifically required to export Fap1, a serine-rich fimbrial adhesin e... | Streptococcus parasanguinis |
A1C3M0 | GTFB_STRPA | MIRLFEWLTQESLDLHYSLEESGIHGTSIVLNDDGFLPEGIISPYTFFCEVEMDGSPLYFNQLEVPYLWQITGTNIEGEIWNRSSKRGVIHYHEPKYLRFVQSVDWLYPDGSIYMTDHYNKYGWAFARTYFFSDQQVSHKKYYTKSGQEVLSENILTGDILLNWKGKVYHFTKKVDFFLFYFKKSGLDLSSIWYNSLGMPFLISYYLGGEGRDILFWQENLADQLPGNMQIIFSGRTSRTKKVIVQDRSVYKKLLHLVEEKNKEMISFLNIIYPKLRENYSRKEILIVTNSDQIEGIETLTDNLSAYTFHIGALTSMSDK... | null | null | protein glycosylation [GO:0006486]; regulation of protein stability [GO:0031647] | plasma membrane [GO:0005886]; protein N-acetylglucosaminyltransferase complex [GO:0017122] | null | null | null | GtfB family | null | SUBCELLULAR LOCATION: Cell membrane {ECO:0000305|PubMed:21862581}; Peripheral membrane protein {ECO:0000305|PubMed:21862581}. | null | null | PATHWAY: Protein modification; protein glycosylation. {ECO:0000255|HAMAP-Rule:MF_01473, ECO:0000269|PubMed:18083807, ECO:0000269|PubMed:20971868, ECO:0000269|PubMed:21862581}. | null | null | FUNCTION: Required for the polymorphic O-glycosylation of the serine-rich repeat protein Fap1. A stabilizing protein that is part of the accessory SecA2/SecY2 system specifically required to export Fap1, a serine-rich fimbrial adhesin encoded upstream in the same operon. The GtfA-GtfB (Gtf1-Gtf2 in this bacteria) compl... | Streptococcus parasanguinis |
A1C8C3 | OBLA_ASPCL | MACKYSTLIDSSLYDREGLCPGIDLRRHVAGELEEVGAFRAQEDWRRLVGPLPKPYAGLLGPDFSFITGAVPECHPDRMEIVAYALEFGFMHDDVIDTDVNHASLDEVGHTLDQSRTGKIEDKGSDGKRQMVTQIIREMMAIDPERAMTVAKSWASGVRHSSRRKEDTNFKALEQYIPYRALDVGYMLWHGLVTFGCAITIPNEEEEEAKRLIIPALVQASLLNDLFSFEKEKNDANVQNAVLIVMNEHGCSEEEARDILKKRIRLECANYLRNVKETNARADVSDELKRYINVMQYTLSGNAAWSTNCPRYNGPTKFNE... | 2.5.1.29; 2.5.1.81; 4.2.3.145 | COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250|UniProtKB:Q12051, ECO:0000250|UniProtKB:Q40577}; Note=Binds 4 Mg(2+) ions per subunit. {ECO:0000250|UniProtKB:Q12051, ECO:0000250|UniProtKB:Q40577}; | alcohol biosynthetic process [GO:0046165]; ketone biosynthetic process [GO:0042181]; mycotoxin biosynthetic process [GO:0043386]; terpenoid biosynthetic process [GO:0016114] | null | farnesyltranstransferase activity [GO:0004311]; geranylfarnesyl diphosphate synthase activity [GO:0044687]; lyase activity [GO:0016829]; metal ion binding [GO:0046872] | PF00348;PF19086; | 1.10.600.10; | Terpene synthase family; FPP/GGPP synthase family | null | null | CATALYTIC ACTIVITY: Reaction=(2E,6E)-farnesyl diphosphate + isopentenyl diphosphate = (2E,6E,10E)-geranylgeranyl diphosphate + diphosphate; Xref=Rhea:RHEA:17653, ChEBI:CHEBI:33019, ChEBI:CHEBI:58756, ChEBI:CHEBI:128769, ChEBI:CHEBI:175763; EC=2.5.1.29; Evidence={ECO:0000269|PubMed:23324037, ECO:0000269|PubMed:28362483}... | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=0.024 uM for geranylgeranyl diphosphate (GGDP) {ECO:0000269|PubMed:28362483}; | PATHWAY: Secondary metabolite biosynthesis; terpenoid biosynthesis. {ECO:0000269|PubMed:23324037}. | null | null | FUNCTION: Bifunctional sesterterpene synthase; part of the gene cluster that mediates the biosynthesis of the sesterterpenes ophiobolins, fungal phytotoxins with potential anti-cancer activities (PubMed:23324037, PubMed:27116000, PubMed:28362483). The first step of the pathway is performed by the sesterterpene synthase... | Aspergillus clavatus (strain ATCC 1007 / CBS 513.65 / DSM 816 / NCTC 3887 / NRRL 1 / QM 1276 / 107) |
A1C9U5 | SKP1_ASPCL | MSTTVTLTSSDGVDLTVDRDVAERSVLIKNMLEDLGESGEAIPIPNVNEVVLKKVIEWCTHHKNDPPSTGDDDDSRRKTTDIDEWDQKFMQVDQEMLFEIILAANYLDIKALLDVGCKTVANMIKGKSPEEIRKTFNIQNDFTPEEEDQIRRENEWAEE | null | null | exit from mitosis [GO:0010458]; G1/S transition of mitotic cell cycle [GO:0000082]; G2/M transition of mitotic cell cycle [GO:0000086]; kinetochore assembly [GO:0051382]; mitotic nuclear membrane biogenesis [GO:0101026]; negative regulation of cytoplasmic translation [GO:2000766]; negative regulation of mitotic metapha... | CBF3 complex [GO:0031518]; kinetochore [GO:0000776]; nuclear SCF ubiquitin ligase complex [GO:0043224]; RAVE complex [GO:0043291]; single-stranded DNA-dependent ATP-dependent DNA helicase complex [GO:0017117] | cullin family protein binding [GO:0097602]; DNA replication origin binding [GO:0003688]; ubiquitin protein ligase activity [GO:0061630] | PF01466;PF03931; | null | SKP1 family | null | null | null | null | PATHWAY: Protein modification; protein ubiquitination. | null | null | FUNCTION: Essential component of the SCF (SKP1-CUL1-F-box protein) E3 ubiquitin ligase complexes, which mediate the ubiquitination and subsequent proteasomal degradation of target proteins. Controls sulfur metabolite repression, probably by mediating the inactivation or degradation of the metR transcription factor (By ... | Aspergillus clavatus (strain ATCC 1007 / CBS 513.65 / DSM 816 / NCTC 3887 / NRRL 1 / QM 1276 / 107) |
A1CAZ7 | UBA4_ASPCL | MENLEQTCASLRAQIAATEAQLAGLKRDLEVAEQAAAEIKAQDVKSTGIREEGSEKKNPWPLLSEEYKRYGRQMIVPQLGLQGQLKLRSARVLIVGAGGLGCPAALYLAGAGVGTLGLVDGDTVEHSNLHRQVLHRSKNVGKFKVDSAIEYLRELNPHPTYVPYRAHLTPQEAPEIFKDYDIVLDCTDNPATRYLISDTAVLLGKPLVSASALRTEGQLIVLNNPPRPVGDKSGGPCYRCVFPKPPPATSVVSCADGGIIGPVVGTMGVLQAIEAIKVITSSPADETSASPPSLLIFSAYSTPPFRSIKIRSRRANCAVC... | 2.7.7.80; 2.8.1.11 | COFACTOR: Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000255|HAMAP-Rule:MF_03049}; Note=Binds 1 zinc ion per subunit. {ECO:0000255|HAMAP-Rule:MF_03049}; | cell budding [GO:0007114]; cellular response to oxidative stress [GO:0034599]; invasive growth in response to glucose limitation [GO:0001403]; Mo-molybdopterin cofactor biosynthetic process [GO:0006777]; protein urmylation [GO:0032447]; regulation of pseudohyphal growth [GO:2000220]; tRNA wobble position uridine thiola... | cytosol [GO:0005829] | AMPylase activity [GO:0070733]; ATP binding [GO:0005524]; identical protein binding [GO:0042802]; metal ion binding [GO:0046872]; molybdopterin-synthase adenylyltransferase activity [GO:0061605]; molybdopterin-synthase sulfurtransferase activity [GO:0061604]; sulfotransferase activity [GO:0008146]; thiosulfate sulfurtr... | PF00581;PF00899; | 3.40.50.720;3.40.250.10; | HesA/MoeB/ThiF family, UBA4 subfamily | null | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_03049}. | CATALYTIC ACTIVITY: Reaction=[molybdopterin-synthase sulfur-carrier protein]-C-terminal Gly-Gly + ATP + H(+) = [molybdopterin-synthase sulfur-carrier protein]-C-terminal Gly-Gly-AMP + diphosphate; Xref=Rhea:RHEA:43616, Rhea:RHEA-COMP:12159, Rhea:RHEA-COMP:12202, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:33019, ... | null | PATHWAY: tRNA modification; 5-methoxycarbonylmethyl-2-thiouridine-tRNA biosynthesis. {ECO:0000255|HAMAP-Rule:MF_03049}.; PATHWAY: Cofactor biosynthesis; molybdopterin biosynthesis. {ECO:0000255|HAMAP-Rule:MF_03049}. | null | null | FUNCTION: Plays a central role in 2-thiolation of mcm(5)S(2)U at tRNA wobble positions of cytosolic tRNA(Lys), tRNA(Glu) and tRNA(Gln). Also essential during biosynthesis of the molybdenum cofactor. Acts by mediating the C-terminal thiocarboxylation of sulfur carriers urm1 and mocs2a. Its N-terminus first activates urm... | Aspergillus clavatus (strain ATCC 1007 / CBS 513.65 / DSM 816 / NCTC 3887 / NRRL 1 / QM 1276 / 107) |
A1CLY8 | CCSA_ASPCL | MGSFQNSSEPIAIIGTGCRFPGGCDSPSKLWELLRAPRDLLKEIPESRFSVDSFYHPDNAHHGTSNVRHSYFLEEDLRQFDVQFFGIKPIEANAVDPQQRLLLETVYEGLESAGLSIQRLQGSDTAVYVGVMSADFTDLVGRDTETFPTYFATGTARSILSNRLSYFFDWHGPSLTIDTACSSSLIAMHHAVQTLRSGDSSLAIVAGSNLILGPEQYIAESKLQMLSPTGRSRMWDAAADGYARGEGVAAIVLKRLSQAIADGDHIECVIRETGVNQDGKTPGITMPSATAQAALIRSTYAKAGLDLSNRSDRPQYFEAH... | 2.3.1.-; 6.3.2.- | null | amide biosynthetic process [GO:0043604]; fatty acid biosynthetic process [GO:0006633]; heterocycle biosynthetic process [GO:0018130]; methylation [GO:0032259]; organic cyclic compound biosynthetic process [GO:1901362]; organonitrogen compound biosynthetic process [GO:1901566]; toxin biosynthetic process [GO:0009403] | null | 3-oxoacyl-[acyl-carrier-protein] synthase activity [GO:0004315]; fatty acid synthase activity [GO:0004312]; isomerase activity [GO:0016853]; ligase activity [GO:0016874]; methyltransferase activity [GO:0008168]; oxidoreductase activity [GO:0016491]; phosphopantetheine binding [GO:0031177] | PF00698;PF00501;PF00668;PF16197;PF00109;PF02801;PF08659;PF08242;PF07993;PF21089;PF00550;PF14765; | 3.30.300.30;3.40.47.10;1.10.1200.10;3.30.559.10;3.40.366.10;3.40.50.12780;3.40.50.720;3.30.559.30;3.10.129.110;3.40.50.150; | NRP synthetase family | null | null | null | null | PATHWAY: Mycotoxin biosynthesis. {ECO:0000269|PubMed:21983160}. | null | null | FUNCTION: Hybrid PKS-NRPS synthetase; part of the gene cluster that mediates the biosynthesis of the mycotoxins cytochalasins E and K (PubMed:21983160). The hybrid PKS-NRPS synthetase ccsA and the enoyl reductase ccsC are responsible for fusion of phenylalanine with an octaketide backbone and subsequent release of the ... | Aspergillus clavatus (strain ATCC 1007 / CBS 513.65 / DSM 816 / NCTC 3887 / NRRL 1 / QM 1276 / 107) |
A1CP85 | ARO1_ASPCL | MIEPTKISILGQESIVADFGLWRNYVAKDLISGCPSTTYVLITDTNIGSIYTPSFQKSFEEAAAAVTPSPRLLTYYAPPGEVSKSRQTKADIEDWMLSQSPPCGRDTVIIALGGGVIGDLTGFVAATYMRGVRFVQVPTTLLAMVDSSIGGKTAIDTPLGKNLIGAIWQPARIYIDLEFLETLPVREFINGMAEVIKTAAISSEEEFTALEDNAETILAAVRREVKPGQRRFDGIEQILKARILASARHKAFVVSEDEREGGLRNLLNWGHSIGHAIEAILTPQILHGECVAIGMVKEAELARHLGVLKGVAVARIVKCI... | 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}. | Aspergillus clavatus (strain ATCC 1007 / CBS 513.65 / DSM 816 / NCTC 3887 / NRRL 1 / QM 1276 / 107) |
A1CQG2 | RSP5_ASPCL | MGSNLPSQPNLRLTIIAADGLYKRDVFRFPDPFAVATVGGEQTQTTSVIKKTLNPYWNEMFDLRVNEESILAIQIFDQKKFKKKDQGFLGVINVRIGDVIDLEMGGDEMLTRDLKKSNDNLVVHGKLIINLSTNLSTPNTNQANGLHRSHIQPSTSSGLVPQVGASAAHPAASPAPIDPAASNPSLHPQRVPSTNRPPSTVAPGAAAGATPTNTQGSRTNLSSFEDSQGRLPAGWERREDNLGRTYYVDHNTRTTTWTRPSSNYNEQTQRTQREANMQLERRAHQSRMLPEDRTGANSPNLPETSQQAPTPPAGGSANAV... | 2.3.2.26 | null | chromatin organization [GO:0006325]; mitochondria-associated ubiquitin-dependent protein catabolic process [GO:0072671]; mitochondrion organization [GO:0007005]; nonfunctional rRNA decay [GO:0070651]; poly(A)+ mRNA export from nucleus [GO:0016973]; positive regulation of fatty acid biosynthetic process [GO:0045723]; po... | cellular bud tip [GO:0005934]; cytosolic ribosome [GO:0022626]; endosome membrane [GO:0010008]; Golgi apparatus [GO:0005794]; nucleus [GO:0005634]; RSP5-BUL ubiquitin ligase complex [GO:1990306]; ubiquitin ligase complex [GO:0000151] | phosphatidylinositol binding [GO:0035091]; ubiquitin binding [GO:0043130]; ubiquitin protein ligase activity [GO:0061630]; ubiquitin-protein transferase activity [GO:0004842] | PF00168;PF00632;PF00397; | 2.20.70.10;2.60.40.150;3.30.2160.10;3.30.2410.10;3.90.1750.10; | RSP5/NEDD4 family | null | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:P39940}. | CATALYTIC ACTIVITY: Reaction=S-ubiquitinyl-[E2 ubiquitin-conjugating enzyme]-L-cysteine + [acceptor protein]-L-lysine = [E2 ubiquitin-conjugating enzyme]-L-cysteine + N(6)-ubiquitinyl-[acceptor protein]-L-lysine.; EC=2.3.2.26; | null | PATHWAY: Protein modification; protein ubiquitination. | null | null | FUNCTION: E3 ubiquitin-protein ligase which accepts ubiquitin from an E2 ubiquitin-conjugating enzyme in the form of a thioester and then directly transfers the ubiquitin to targeted substrates. Probably involved in the regulatory network controlling carbon source utilization. {ECO:0000250|UniProtKB:Q5BDP1}. | Aspergillus clavatus (strain ATCC 1007 / CBS 513.65 / DSM 816 / NCTC 3887 / NRRL 1 / QM 1276 / 107) |
A1CX69 | ATG1_NEOFI | MSIGRYTRLDEIGRGSFATVYQGVHTKTRTYVAIKSVNLSKLNKKLKDNLSSEIHILKGLYHPHIVALIDCHETTSHIHLVMEYCALGDLSLFIKRRDTLGDHRYTRDMIAKYPNPPGGALNEVVVRHFLKQLASALKFLRDRNLIHRDIKPQNLLLCPSPSSYRSGVTQVVPFKGSEDSFNPATGLESLPLLKIADFGFARSLPATSLAETLCGSPLYMAPEILRYEKYDAKADLWSVGTVLYEMVVGKPPFRATNHVELLRKIEKGEDRIKFPEENPASDEIKALIRALLKRNPVERLNFPDFFENGVITSPIPGLVA... | 2.7.11.1 | null | autophagosome assembly [GO:0000045]; axon extension [GO:0048675]; negative regulation of collateral sprouting [GO:0048671]; phosphorylation [GO:0016310]; piecemeal microautophagy of the nucleus [GO:0034727]; positive regulation of autophagy [GO:0010508]; protein transport [GO:0015031]; response to starvation [GO:004259... | Atg1/ULK1 kinase complex [GO:1990316]; autophagosome membrane [GO:0000421]; cytosol [GO:0005829]; phagophore [GO:0061908]; phagophore assembly site membrane [GO:0034045]; vacuole-isolation membrane contact site [GO:0120095] | ATP binding [GO:0005524]; protein serine kinase activity [GO:0106310]; protein serine/threonine kinase activity [GO:0004674] | PF12063;PF21127;PF00069; | 1.10.510.10; | Protein kinase superfamily, Ser/Thr protein kinase family, APG1/unc-51/ULK1 subfamily | null | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:P53104}. Preautophagosomal structure membrane {ECO:0000250|UniProtKB:P53104}; Peripheral membrane protein {ECO:0000250|UniProtKB:P53104}. | CATALYTIC ACTIVITY: Reaction=ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-[protein]; Xref=Rhea:RHEA:17989, Rhea:RHEA-COMP:9863, Rhea:RHEA-COMP:11604, ChEBI:CHEBI:15378, ChEBI:CHEBI:29999, ChEBI:CHEBI:30616, ChEBI:CHEBI:83421, ChEBI:CHEBI:456216; EC=2.7.11.1; Evidence={ECO:0000250|UniProtKB:P53104}; CATALYTI... | null | null | null | null | FUNCTION: Serine/threonine protein kinase involved in the cytoplasm to vacuole transport (Cvt) and found to be essential in autophagy, where it is required for the formation of autophagosomes. Involved in the clearance of protein aggregates which cannot be efficiently cleared by the proteasome. Required for selective a... | Neosartorya fischeri (strain ATCC 1020 / DSM 3700 / CBS 544.65 / FGSC A1164 / JCM 1740 / NRRL 181 / WB 181) (Aspergillus fischerianus) |
A1CZG3 | SKP1_NEOFI | MTTVTLTSSDGVDITVDRDVAERSILIKNMLEDLGESDEAIPIPNVNEVVLKKVIEWCTHHKNDPPSTGDDDDSRRKTTDIDEWDQKFMQVDQEMLFEIILAANYLDIKALLDVGCKTVANMIKGKSPEEIRKTFNIQNDFTPEEEDQIRRENEWAEE | null | null | exit from mitosis [GO:0010458]; G1/S transition of mitotic cell cycle [GO:0000082]; G2/M transition of mitotic cell cycle [GO:0000086]; kinetochore assembly [GO:0051382]; mitotic nuclear membrane biogenesis [GO:0101026]; negative regulation of cytoplasmic translation [GO:2000766]; negative regulation of mitotic metapha... | CBF3 complex [GO:0031518]; kinetochore [GO:0000776]; nuclear SCF ubiquitin ligase complex [GO:0043224]; RAVE complex [GO:0043291]; single-stranded DNA-dependent ATP-dependent DNA helicase complex [GO:0017117] | cullin family protein binding [GO:0097602]; DNA replication origin binding [GO:0003688]; ubiquitin protein ligase activity [GO:0061630] | PF01466;PF03931; | null | SKP1 family | null | null | null | null | PATHWAY: Protein modification; protein ubiquitination. | null | null | FUNCTION: Essential component of the SCF (SKP1-CUL1-F-box protein) E3 ubiquitin ligase complexes, which mediate the ubiquitination and subsequent proteasomal degradation of target proteins. Controls sulfur metabolite repression, probably by mediating the inactivation or degradation of the metR transcription factor (By ... | Neosartorya fischeri (strain ATCC 1020 / DSM 3700 / CBS 544.65 / FGSC A1164 / JCM 1740 / NRRL 181 / WB 181) (Aspergillus fischerianus) |
A1D244 | ARO1_NEOFI | MTGPTKISILGQESIVADFGLWRNYVAKDLISGCPSTTYVLITDTNIGSIYTPGFQKSFEEAAASVSPSPRLLIYNAPPGEVSKSRQTKADIEDWMLSQSPPCGRDTVVIALGGGVIGDLTGFVAATYMRGVRFVQVPTTLLAMVDSSIGGKTAIDTPLGKNLIGAIWQPSRIYIDLEFLETLPVREFINGMAEVIKTAAISSEEEFTALEDNAETILSAVRREVKPGQRRFEGIEEILKARILASARHKAFVVSADEREGGLRNLLNWGHSIGHAIEAILTPQILHGECVAIGMVKEAELARHLGILKGVAVARIVKCI... | 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}. | Neosartorya fischeri (strain ATCC 1020 / DSM 3700 / CBS 544.65 / FGSC A1164 / JCM 1740 / NRRL 181 / WB 181) (Aspergillus fischerianus) |
A1D3C5 | RSP5_NEOFI | MGSNLPAQPNLRLTIIAADGLYKRDVFRFPDPFAVATVGGEQTHTTSVIKKTLNPYWNEMFDLRVNEDSILAIQIFDQKKFKKKDQGFLGVINVRIGDVIDLQMGGDEMLTRDLKKSNDNLVVHGKLIINLSTNLSTPNTNQANGLHRSHVQSSTSSGLVPQVAPSSSHPAASGAAPVDPSASNPSLNPQRVPSTTRPSSTAAPASAAGAAASNTHGSRTNLSSFEDSQGRLPAGWERREDNLGRTYYVDHNTRTTTWTRPSSNYNEHAQRSQREANMQLERRAHQSRMLPEDRTGANSPNLPESSQQAHTPPAGGSANA... | 2.3.2.26 | null | chromatin organization [GO:0006325]; mitochondria-associated ubiquitin-dependent protein catabolic process [GO:0072671]; mitochondrion organization [GO:0007005]; nonfunctional rRNA decay [GO:0070651]; poly(A)+ mRNA export from nucleus [GO:0016973]; positive regulation of fatty acid biosynthetic process [GO:0045723]; po... | cellular bud tip [GO:0005934]; cytosolic ribosome [GO:0022626]; endosome membrane [GO:0010008]; Golgi apparatus [GO:0005794]; nucleus [GO:0005634]; RSP5-BUL ubiquitin ligase complex [GO:1990306]; ubiquitin ligase complex [GO:0000151] | phosphatidylinositol binding [GO:0035091]; ubiquitin binding [GO:0043130]; ubiquitin protein ligase activity [GO:0061630]; ubiquitin-protein transferase activity [GO:0004842] | PF00168;PF00632;PF00397; | 2.20.70.10;2.60.40.150;3.30.2160.10;3.30.2410.10;3.90.1750.10; | RSP5/NEDD4 family | null | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:P39940}. | CATALYTIC ACTIVITY: Reaction=S-ubiquitinyl-[E2 ubiquitin-conjugating enzyme]-L-cysteine + [acceptor protein]-L-lysine = [E2 ubiquitin-conjugating enzyme]-L-cysteine + N(6)-ubiquitinyl-[acceptor protein]-L-lysine.; EC=2.3.2.26; | null | PATHWAY: Protein modification; protein ubiquitination. | null | null | FUNCTION: E3 ubiquitin-protein ligase which accepts ubiquitin from an E2 ubiquitin-conjugating enzyme in the form of a thioester and then directly transfers the ubiquitin to targeted substrates. Probably involved in the regulatory network controlling carbon source utilization. {ECO:0000250|UniProtKB:Q5BDP1}. | Neosartorya fischeri (strain ATCC 1020 / DSM 3700 / CBS 544.65 / FGSC A1164 / JCM 1740 / NRRL 181 / WB 181) (Aspergillus fischerianus) |
A1DED8 | UBA4_NEOFI | MENLEQTCASLRAQIAATEAQLAGLKRELEIAEQAAADVKAQDTTITITADEGRINGTRTWPLLSEEYKRYGRQMIVPQVGLQGQLKLRSARVLIVGAGGLGCPAALYLAGAGVGTLGLVDGDTVENSNLHRQVLHRSKNVGKFKVDSAIEYLREAHLTPQEAPSIFKDYDIILDCTDNPATRYLISDTAVLLGKPLVSASALRTEGQLMVLNYPPRPVGDKSGGPCYRCVFPKPPPANSVVSCADGGILGPVVGTMGVLQALEAIKVITSPAVNPSASPPSLLIFSAYSTPPFRTIRLRARRANCAVCSADASVTLETL... | 2.7.7.80; 2.8.1.11 | COFACTOR: Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000255|HAMAP-Rule:MF_03049}; Note=Binds 1 zinc ion per subunit. {ECO:0000255|HAMAP-Rule:MF_03049}; | cell budding [GO:0007114]; cellular response to oxidative stress [GO:0034599]; invasive growth in response to glucose limitation [GO:0001403]; Mo-molybdopterin cofactor biosynthetic process [GO:0006777]; protein urmylation [GO:0032447]; regulation of pseudohyphal growth [GO:2000220]; tRNA wobble position uridine thiola... | cytosol [GO:0005829] | AMPylase activity [GO:0070733]; ATP binding [GO:0005524]; identical protein binding [GO:0042802]; metal ion binding [GO:0046872]; molybdopterin-synthase adenylyltransferase activity [GO:0061605]; molybdopterin-synthase sulfurtransferase activity [GO:0061604]; sulfotransferase activity [GO:0008146]; thiosulfate sulfurtr... | PF00581;PF00899; | 3.40.50.720;3.40.250.10; | HesA/MoeB/ThiF family, UBA4 subfamily | null | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_03049}. | CATALYTIC ACTIVITY: Reaction=[molybdopterin-synthase sulfur-carrier protein]-C-terminal Gly-Gly + ATP + H(+) = [molybdopterin-synthase sulfur-carrier protein]-C-terminal Gly-Gly-AMP + diphosphate; Xref=Rhea:RHEA:43616, Rhea:RHEA-COMP:12159, Rhea:RHEA-COMP:12202, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:33019, ... | null | PATHWAY: tRNA modification; 5-methoxycarbonylmethyl-2-thiouridine-tRNA biosynthesis. {ECO:0000255|HAMAP-Rule:MF_03049}. | null | null | FUNCTION: Plays a central role in 2-thiolation of mcm(5)S(2)U at tRNA wobble positions of cytosolic tRNA(Lys), tRNA(Glu) and tRNA(Gln). Also essential during biosynthesis of the molybdenum cofactor. Acts by mediating the C-terminal thiocarboxylation of sulfur carriers urm1 and mocs2a. Its N-terminus first activates urm... | Neosartorya fischeri (strain ATCC 1020 / DSM 3700 / CBS 544.65 / FGSC A1164 / JCM 1740 / NRRL 181 / WB 181) (Aspergillus fischerianus) |
A1E280 | TRP6H_STRAO | MDNRIKTVVILGGGTAGWMTAAYLGKALQNTVKIVVLEAPTIPRIGVGEATVPNLQRAFFDYLGIPEEEWMRECNASYKMAVKFINWRTPGEGSPDPRTLDDGHTDTFHHPFGLLPSADQIPLSHYWAAKRLQGETDENFDEACFADTAIMNAKKAPRFLDMRRATNYAWHFDASKVAAFLRNFAVTKQAVEHVEDEMTEVLTDERGFITALRTKSGRILQGDLFVDCSGFRGLLINKAMEEPFIDMSDHLLCNSAVATAVPHDDEKNGVEPYTSSIAMEAGWTWKIPMLGRFGSGHVYSDHFATQDEATLAFSKLWGLD... | 1.14.19.59 | null | null | null | monooxygenase activity [GO:0004497]; nucleotide binding [GO:0000166] | PF04820; | 3.50.50.60; | Flavin-dependent halogenase family, Bacterial tryptophan halogenase subfamily | null | null | CATALYTIC ACTIVITY: Reaction=chloride + FADH2 + L-tryptophan + O2 = 6-chloro-L-tryptophan + FAD + 2 H2O; Xref=Rhea:RHEA:55900, ChEBI:CHEBI:15377, ChEBI:CHEBI:15379, ChEBI:CHEBI:17996, ChEBI:CHEBI:57692, ChEBI:CHEBI:57912, ChEBI:CHEBI:58307, ChEBI:CHEBI:139335; EC=1.14.19.59; Evidence={ECO:0000269|PubMed:33465708, ECO:0... | null | null | null | null | FUNCTION: Involved in the biosynthesis of thienodolin, a plant growth-regulating compound (PubMed:24692213). Catalyzes the chlorination of tryptophan (Trp) at C6 position to yield 6-chloro-tryptophan (PubMed:24692213, PubMed:33465708). It is also able to use bromide ions to generate monobrominated Trp (PubMed:33465708,... | Streptomyces albogriseolus |
A1E959 | ODAM_HUMAN | MKIIILLGFLGATLSAPLIPQRLMSASNSNELLLNLNNGQLLPLQLQGPLNSWIPPFSGILQQQQQAQIPGLSQFSLSALDQFAGLLPNQIPLTGEASFAQGAQAGQVDPLQLQTPPQTQPGPSHVMPYVFSFKMPQEQGQMFQYYPVYMVLPWEQPQQTVPRSPQQTRQQQYEEQIPFYAQFGYIPQLAEPAISGGQQQLAFDPQLGTAPEIAVMSTGEEIPYLQKEAINFRHDSAGVFMPSTSPKPSTTNVFTSAVDQTITPELPEEKDKTDSLREP | null | null | biomineral tissue development [GO:0031214]; inflammatory response [GO:0006954]; odontogenesis of dentin-containing tooth [GO:0042475]; positive regulation of epithelial cell proliferation involved in wound healing [GO:0060054]; positive regulation of gene expression [GO:0010628]; positive regulation of GTPase activity ... | cell periphery [GO:0071944]; cytoplasm [GO:0005737]; cytosol [GO:0005829]; extracellular region [GO:0005576]; extracellular space [GO:0005615]; mitotic spindle [GO:0072686]; nucleoplasm [GO:0005654]; nucleus [GO:0005634]; supramolecular fiber [GO:0099512] | null | PF15424; | null | ODAM family | PTM: O-glycosylated. {ECO:0000250}. | SUBCELLULAR LOCATION: Secreted {ECO:0000250|UniProtKB:Q3HS83}. Cytoplasm {ECO:0000269|PubMed:25911094}. Nucleus {ECO:0000269|PubMed:25911094}. | null | null | null | null | null | FUNCTION: Tooth-associated epithelia protein that probably plays a role in odontogenesis, the complex process that results in the initiation and generation of the tooth. May be incorporated in the enamel matrix at the end of mineralization process. Involved in the induction of RHOA activity via interaction with ARHGEF ... | Homo sapiens (Human) |
A1E960 | ODAM_MOUSE | MKIIILLGLIGASSSAPLISQRLLSASNSHELLLNLNNGQLLPLQFQGAFNSWIPPFPGFLQQQQAQVSGRPQFTLSTLESFAGLFPNQIPLSRQVGLAQGGQAGQPDLSQQQTPPQTQQSASPMSYVVPVKVPQDQTQMFQYYPVYMLLPWEQPQTVTSSPQHTGQQLFEEQIPFYNQFGFAPPQAEPGVPGGQQHLAFDSFVGTAPETPGMPVEGSLLYPQKEPISFKHDNAGVFMPTTSPKPSTDNFFTSGIDPTIAPEQKVKTDSLREP | null | null | biomineral tissue development [GO:0031214]; inflammatory response [GO:0006954]; odontogenesis of dentin-containing tooth [GO:0042475]; positive regulation of epithelial cell proliferation involved in wound healing [GO:0060054]; positive regulation of gene expression [GO:0010628]; positive regulation of protein phosphor... | cell periphery [GO:0071944]; cytoplasm [GO:0005737]; cytosol [GO:0005829]; extracellular region [GO:0005576]; extracellular space [GO:0005615]; mitotic spindle [GO:0072686]; nucleoplasm [GO:0005654]; nucleus [GO:0005634]; supramolecular fiber [GO:0099512] | null | PF15424; | null | ODAM family | PTM: O-glycosylated. {ECO:0000250}. | SUBCELLULAR LOCATION: Secreted {ECO:0000250|UniProtKB:Q3HS83}. Cytoplasm {ECO:0000250|UniProtKB:A1E959}. Nucleus {ECO:0000250|UniProtKB:A1E959}. | null | null | null | null | null | FUNCTION: Tooth-associated epithelia protein that probably plays a role in odontogenesis, the complex process that results in the initiation and generation of the tooth. May be incorporated in the enamel matrix at the end of mineralization process. Involved in the induction of RHOA activity via interaction with ARHGEF ... | Mus musculus (Mouse) |
A1EC31 | TDIF_ZINEL | MDIDLLWSFGGWFFILFPETINYCMAKLRSTSQISHFTNPRSCSSLFFVALLIITILITMLQSSTSMEVTSLPTHQPTSSNSHDESSTSSTATTTTDLHPKRTHHQSHPKPTRSFEAGAHEVPSGPNPISNR | null | null | cell-cell signaling involved in cell fate commitment [GO:0045168]; phloem or xylem histogenesis [GO:0010087]; procambium histogenesis [GO:0010067]; xylem development [GO:0010089] | apoplast [GO:0048046]; plasma membrane [GO:0005886] | receptor serine/threonine kinase binding [GO:0033612] | null | null | CLV3/ESR signal peptide family | PTM: [TDIFp]: The TDIFp peptide contains two hydroxprolines, but hydroxylation had no direct effect on TDIFp activity. {ECO:0000269|PubMed:16902140}.; PTM: [TDIFp]: The O-glycosylation (arabinosylation) of the hydroxyproline Pro-126 enhances binding affinity of the TDIFp peptide for its receptor. {ECO:0000250|UniProtKB... | SUBCELLULAR LOCATION: [TDIFp]: Secreted, extracellular space {ECO:0000269|PubMed:16902140}.; SUBCELLULAR LOCATION: [CLAVATA3/ESR (CLE)-related protein TDIF]: Cell membrane {ECO:0000305}; Single-pass membrane protein {ECO:0000305}. | null | null | null | null | null | FUNCTION: [TDIFp]: Extracellular signal peptide that regulates cell fate. Represses tracheary element differentiation but promotes the formation of procambial cells adjacent to phloem cells in the veins. {ECO:0000269|PubMed:16902140, ECO:0000269|PubMed:18812507}. | Zinnia elegans (Garden zinnia) (Zinnia violacea) |
A1IHE6 | ACMA_GORST | MSTTTLDAAVIGTGVAGLYELHMLREQGLEVRAYDKASGVGGTWYWNRYPGARFDSEAYIYQYLFDEDLYKGWSWSQRFPGQEEIERWLNYVADSLDLRRDISLETEITSAVFDEDRNRWTLTTADGDTIDAQFLITCCGMLSAPMKDLFPGQSDFGGQLVHTARWPKEGIDFAGKRVGVIGNGATGIQVIQSIAADVDELKVFIRTPQYALPMKNPSYGPDEVAWYKSRFGELKDTLPHTFTGFEYDFTDAWEDLTPEQRRARLEDDYENGSLKLWLASFAEIFSDEQVSEEVSEFVREKMRARLVDPELCDLLIPSDY... | 1.14.13.226 | COFACTOR: Name=FAD; Xref=ChEBI:CHEBI:57692; Evidence={ECO:0000269|PubMed:30392152, ECO:0000305|PubMed:17071761}; Note=Binds 1 FAD per subunit. {ECO:0000250|UniProtKB:H3JQW0}; | null | null | flavin adenine dinucleotide binding [GO:0050660]; N,N-dimethylaniline monooxygenase activity [GO:0004499]; NADP binding [GO:0050661] | PF00743; | 3.50.50.60; | FAD-binding monooxygenase family | null | null | CATALYTIC ACTIVITY: Reaction=acetone + H(+) + NADPH + O2 = H2O + methyl acetate + NADP(+); Xref=Rhea:RHEA:49988, ChEBI:CHEBI:15347, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349, ChEBI:CHEBI:77700; EC=1.14.13.226; Evidence={ECO:0000269|PubMed:17071761, ECO:0000269|PubMed:... | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=6.7 uM for NADPH {ECO:0000269|PubMed:30392152}; KM=170 uM for acetone {ECO:0000269|PubMed:30392152}; KM=0.34 uM for butanone {ECO:0000269|PubMed:30392152}; KM=0.37 uM for 2-pentanone {ECO:0000269|PubMed:30392152}; KM=1.5 uM for 2-heptanone {ECO:0000269|PubMed:30392... | null | BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 8.0-8.5 (PubMed:17071761). Optimum pH is 7.0-8.0 (PubMed:30392152). {ECO:0000269|PubMed:17071761, ECO:0000269|PubMed:30392152}; | BIOPHYSICOCHEMICAL PROPERTIES: Temperature dependence: Optimum temperature is 35 degrees Celsius. {ECO:0000269|PubMed:17071761}; | FUNCTION: Plays an important role in the metabolism of acetone derived from propane oxidation (PubMed:17071761). Catalyzes the oxidation of acetone to methyl acetate (PubMed:17071761, PubMed:30392152). Exhibits high catalytic efficiency towards various linear and cyclic ketones, such as butanone, 2-pentanone, 2-heptano... | Gordonia sp. (strain TY-5) |
A1IVT7 | HOG1_BOTFB | MAEFVRAQIFGTTFEITSRYSDLQPVGMGAFGLVCSAKDNLTGSNVAVKKIMKPFSTPVLSKRTYRELKLLKHLKHENVISLSDIFISPLEDIYFVTELLGTDLHRLLTSRPLEKQFIQYFLYQILRGLKYVHSAGVVHRDLKPSNILVNENCDLKICDFGLARIQDPQMTGYVSTRYYRAPEIMLTWQKYDVEVDVWSAGCIFAEMLEGKPLFPGKDHVNQFSIITELLGTPPDDVIHTIASENTLRFVQSLPKRERQPLASKFTQADPLAIDLLEKMLVFDPRARIKAAEGLAHEYLSPYHDPTDEPAAEERFDWSFN... | 2.7.11.24 | COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250}; | cellular response to oxidative stress [GO:0034599]; osmosensory signaling pathway [GO:0007231]; phosphorylation [GO:0016310]; stress-activated MAPK cascade [GO:0051403] | cytoplasm [GO:0005737]; nucleus [GO:0005634] | ATP binding [GO:0005524]; MAP kinase activity [GO:0004707]; protein serine kinase activity [GO:0106310] | PF00069; | 1.10.510.10; | Protein kinase superfamily, Ser/Thr protein kinase family, MAP kinase subfamily. HOG1 sub-subfamily | PTM: Dually phosphorylated on Thr-171 and Tyr-173, which activates the enzyme (By similarity). Phosphorylated under osmotic stress, specific fungicides, and oxidative stress mediated by H(2)O(2) and menadione. {ECO:0000250, ECO:0000269|PubMed:17189492}. | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Nucleus {ECO:0000250}. | CATALYTIC ACTIVITY: Reaction=ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-[protein]; Xref=Rhea:RHEA:17989, Rhea:RHEA-COMP:9863, Rhea:RHEA-COMP:11604, ChEBI:CHEBI:15378, ChEBI:CHEBI:29999, ChEBI:CHEBI:30616, ChEBI:CHEBI:83421, ChEBI:CHEBI:456216; EC=2.7.11.24; CATALYTIC ACTIVITY: Reaction=ATP + L-threonyl-[p... | null | null | null | null | FUNCTION: Mitogen-activated protein kinase involved in a signal transduction pathway that is activated by changes in the osmolarity of the extracellular environment. Controls osmotic regulation of transcription of target genes (By similarity). Involved in vegetative and pathogenic development like conidia formation, sc... | Botryotinia fuckeliana (strain B05.10) (Noble rot fungus) (Botrytis cinerea) |
A1JIG4 | FADB_YERE8 | MLYQSETLQLHWLENGIAELVFDAPGSVNKLDTQTVANLGEALVVLEKQSELKGLLLRSAKAAFIVGADITEFLSLFNEPPEKLHQWLVFANDIFNRLEDLPVPTIAAINGYALGGGCECILATDFRVASPEARIGLPETKLGIMPGFGGSVRLPRLLGADSALEIIAAGKDIIAKDALKVGLVDAVVAPEKLVDAALSILNQAIDGKLDWQAARRPKLEPLKLNPTEAAMCFTIAKGMVMQVAGKHYPAPLTAVKTIEAAAKFGRAEALILETNSFVPLAGSNEARALVGIFLNDQYVKGQAKKLSKGVSAPKQAAVLG... | 1.1.1.35; 4.2.1.17; 5.1.2.3; 5.3.3.8 | null | fatty acid beta-oxidation [GO:0006635] | fatty acid beta-oxidation multienzyme complex [GO:0036125] | 3-hydroxyacyl-CoA dehydrogenase activity [GO:0003857]; 3-hydroxybutyryl-CoA epimerase activity [GO:0008692]; delta(3)-delta(2)-enoyl-CoA isomerase activity [GO:0004165]; enoyl-CoA hydratase activity [GO:0004300]; NAD+ binding [GO:0070403] | PF00725;PF02737;PF00378; | 1.10.1040.50;3.40.50.720; | Enoyl-CoA hydratase/isomerase family; 3-hydroxyacyl-CoA dehydrogenase family | null | null | CATALYTIC ACTIVITY: Reaction=a (3S)-3-hydroxyacyl-CoA + NAD(+) = a 3-oxoacyl-CoA + H(+) + NADH; Xref=Rhea:RHEA:22432, ChEBI:CHEBI:15378, ChEBI:CHEBI:57318, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945, ChEBI:CHEBI:90726; EC=1.1.1.35; Evidence={ECO:0000255|HAMAP-Rule:MF_01621}; CATALYTIC ACTIVITY: Reaction=a (3S)-3-hydroxyacyl-... | null | PATHWAY: Lipid metabolism; fatty acid beta-oxidation. {ECO:0000255|HAMAP-Rule:MF_01621}. | null | null | FUNCTION: Involved in the aerobic and anaerobic degradation of long-chain fatty acids via beta-oxidation cycle. Catalyzes the formation of 3-oxoacyl-CoA from enoyl-CoA via L-3-hydroxyacyl-CoA. It can also use D-3-hydroxyacyl-CoA and cis-3-enoyl-CoA as substrate. {ECO:0000255|HAMAP-Rule:MF_01621}. | Yersinia enterocolitica serotype O:8 / biotype 1B (strain NCTC 13174 / 8081) |
A1KI36 | KGD_MYCBP | MANISSPFGQNEWLVEAMYRKFRDDPSSVDPSWHEFLVDYSPEPTSQPAAEPTRVTSPLVAERAAAAAPQAPPKPADTAAAGNGVVAALAAKTAVPPPAEGDEVAVLRGAAAAVVKNMSASLEVPTATSVRAVPAKLLIDNRIVINNQLKRTRGGKISFTHLLGYALVQAVKKFPNMNRHYTEVDGKPTAVTPAHTNLGLAIDLQGKDGKRSLVVAGIKRCETMRFAQFVTAYEDIVRRARDGKLTTEDFAGVTISLTNPGTIGTVHSVPRLMPGQGAIIGVGAMEYPAEFQGASEERIAELGIGKLITLTSTYDHRIIQ... | 1.2.4.2; 2.2.1.5; 2.3.1.61; 4.1.1.71 | COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250}; COFACTOR: Name=thiamine diphosphate; Xref=ChEBI:CHEBI:58937; Evidence={ECO:0000250}; | tricarboxylic acid cycle [GO:0006099] | cytosol [GO:0005829]; oxoglutarate dehydrogenase complex [GO:0045252] | 2-hydroxy-3-oxoadipate synthase activity [GO:0050439]; 2-oxoglutarate decarboxylase activity [GO:0008683]; dihydrolipoyllysine-residue succinyltransferase activity [GO:0004149]; magnesium ion binding [GO:0000287]; oxoglutarate dehydrogenase (succinyl-transferring) activity [GO:0004591]; thiamine pyrophosphate binding [... | PF00198;PF16078;PF00676;PF16870;PF02779; | 3.40.50.12470;3.40.50.970;3.30.559.10;3.40.50.11610;1.10.287.1150; | 2-oxoacid dehydrogenase family, Kgd subfamily | null | null | CATALYTIC ACTIVITY: Reaction=2-oxoglutarate + glyoxylate + H(+) = 2-hydroxy-3-oxoadipate + CO2; Xref=Rhea:RHEA:14341, ChEBI:CHEBI:15378, ChEBI:CHEBI:16526, ChEBI:CHEBI:16810, ChEBI:CHEBI:36655, ChEBI:CHEBI:57712; EC=2.2.1.5; CATALYTIC ACTIVITY: Reaction=2-oxoglutarate + H(+) = CO2 + succinate semialdehyde; Xref=Rhea:RH... | null | PATHWAY: Carbohydrate metabolism; tricarboxylic acid cycle; succinate from 2-oxoglutarate (transferase route): step 1/2.; PATHWAY: Carbohydrate metabolism; tricarboxylic acid cycle; succinyl-CoA from 2-oxoglutarate (dehydrogenase route): step 1/1. | null | null | FUNCTION: Shows three enzymatic activities that share a first common step, the attack of thiamine-PP on 2-oxoglutarate (alpha-ketoglutarate, KG), leading to the formation of an enamine-thiamine-PP intermediate upon decarboxylation. Thus, displays KGD activity, catalyzing the decarboxylation from five-carbon 2-oxoglutar... | Mycobacterium bovis (strain BCG / Pasteur 1173P2) |
A1KJ57 | LYSX_MYCBP | MGLHLTVPGLRRDGRGVQSNSHDTSSKTTADISRCPQHTDAGLQRAATPGISRLLGISSRSVTLTKPRSATRGNSRYHWVPAAAGWTVGVIATLSLLASVSPLIRWIIKVPREFINDYLFNFPDTNFAWSFVLALLAAALTARKRIAWLVLLANMVLAAVVNAAEIAAGGNTAAESFGENLGFAVHVVAIVVLVLGYREFWAKVRRGALFRAAAVWLAGAVVGIVASWGLVELFPGSLAPDERLGYAANRVVGFALADPDLFTGRPHVFLNAIFGLFGAFALIGAAIVLFLSQRADNALTGEDESAIRGLLDLYGKDDSL... | 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 bovis (strain BCG / Pasteur 1173P2) |
A1KPA8 | CH601_MYCBP | MSKLIEYDETARRAMEVGMDKLADTVRVTLGPRGRHVVLAKAFGGPTVTNDGVTVAREIELEDPFEDLGAQLVKSVATKTNDVAGDGTTTATILAQALIKGGLRLVAAGVNPIALGVGIGKAADAVSEALLASATPVSGKTGIAQVATVSSRDEQIGDLVGEAMSKVGHDGVVSVEESSTLGTELEFTEGIGFDKGFLSAYFVTDFDNQQAVLEDALILLHQDKISSLPDLLPLLEKVAGTGKPLLIVAEDVEGEALATLVVNAIRKTLKAVAVKGPYFGDRRKAFLEDLAVVTGGQVVNPDAGMVLREVGLEVLGSARR... | 5.6.1.7 | null | chaperone cofactor-dependent protein refolding [GO:0051085]; mitochondrial unfolded protein response [GO:0034514]; positive regulation of interferon-alpha production [GO:0032727]; positive regulation of interleukin-6 production [GO:0032755]; positive regulation of T cell activation [GO:0050870]; positive regulation of ... | GroEL-GroES complex [GO:1990220] | ATP binding [GO:0005524]; ATP-dependent protein folding chaperone [GO:0140662]; isomerase activity [GO:0016853]; metal ion binding [GO:0046872]; protein-folding chaperone binding [GO:0051087]; unfolded protein binding [GO:0051082] | PF00118; | 3.50.7.10;1.10.560.10;3.30.260.10; | Chaperonin (HSP60) family | null | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00600}. Note=Although thought of as a cytoplasmic chaperone this protein has been found to interact in vitro with a host extracellular protein. {ECO:0000269|PubMed:21203928}. | CATALYTIC ACTIVITY: Reaction=ATP + H2O + a folded polypeptide = ADP + phosphate + an unfolded polypeptide.; EC=5.6.1.7; Evidence={ECO:0000255|HAMAP-Rule:MF_00600}; | null | null | null | null | FUNCTION: Together with its co-chaperonin GroES, plays an essential role in assisting protein folding. The GroEL-GroES system forms a nano-cage that allows encapsulation of the non-native substrate proteins and provides a physical environment optimized to promote and accelerate protein folding. {ECO:0000255|HAMAP-Rule:... | Mycobacterium bovis (strain BCG / Pasteur 1173P2) |
A1KXC4 | FCMR_MOUSE | MDFWLWLLYFLPVSGALRVLPEVQLNVEWGGSIIIECPLPQLHVRMYLCRQMAKPGICSTVVSNTFVKKEYERRVTLTPCLDKKLFLVEMTQLTENDDGIYACGVGMKTDKGKTQKITLNVHNEYPEPFWEDEWTSERPRWLHRFLQHQMPWLHGSEHPSSSGVIAKVTTPAPKTEAPPVHQPSSITSVTQHPRVYRAFSVSATKSPALLPATTASKTSTQQAIRPLEASYSHHTRLHEQRTRHHGPHYGREDRGLHIPIPEFHILIPTFLGFLLLVLLGLVVKRAIQRRRASSRRAGRLAMRRRGRGASRPFPTQRRDA... | null | null | Fc receptor-mediated immune complex endocytosis [GO:0160006]; humoral immune response mediated by circulating immunoglobulin [GO:0002455]; immunoglobulin transcytosis in epithelial cells [GO:0002414]; negative regulation of extrinsic apoptotic signaling pathway [GO:2001237]; negative regulation of lymphocyte apoptotic ... | cell surface [GO:0009986]; early endosome membrane [GO:0031901]; external side of plasma membrane [GO:0009897]; lysosomal membrane [GO:0005765]; plasma membrane [GO:0005886]; trans-Golgi network membrane [GO:0032588] | high-affinity IgM receptor activity [GO:0002172]; IgM binding [GO:0001791]; polymeric immunoglobulin binding [GO:0001790] | PF07686; | 2.60.40.10; | null | PTM: Phosphorylated on both Tyr and Ser residues. {ECO:0000250|UniProtKB:O60667}.; PTM: O-glycosylated. Sialylated. O-linked glycans regulate trafficking to the plasma membrane. {ECO:0000250|UniProtKB:O60667}. | SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:22988094, ECO:0000269|PubMed:25732732, ECO:0000269|PubMed:28135254}; Single-pass membrane protein {ECO:0000255}. Early endosome membrane {ECO:0000250|UniProtKB:O60667}; Single-pass membrane protein {ECO:0000255}. Golgi apparatus, trans-Golgi network membrane {ECO:... | null | null | null | null | null | FUNCTION: High-affinity Fc receptor for immunoglobulin M (IgM), both secreted and membrane-bound IgM (By similarity). Primarily regulates IgM transport and homeostasis. In lymphoid cells, enables exocytosis of membrane-bound IgM on the plasma membrane as well as endocytosis of IgM-antigen complexes toward lysosomes for... | Mus musculus (Mouse) |
A1KXE4 | F168B_HUMAN | MNPVYSPGSSGVPYANAKGIGYPAGFPMGYAAAAPAYSPNMYPGANPTFQTGYTPGTPYKVSCSPTSGAVPPYSSSPNPYQTAVYPVRSAYPQQSPYAQQGTYYTQPLYAAPPHVIHHTTVVQPNGMPATVYPAPIPPPRGNGVTMGMVAGTTMAMSAGTLLTAHSPTPVAPHPVTVPTYRAPGTPTYSYVPPQW | null | null | null | axon [GO:0030424]; extracellular exosome [GO:0070062]; perinuclear region of cytoplasm [GO:0048471]; plasma membrane [GO:0005886] | null | PF14944; | null | FAM168 family | PTM: N-glycosylated. {ECO:0000250|UniProtKB:D4AEP3}. | SUBCELLULAR LOCATION: Cytoplasm, perinuclear region {ECO:0000250|UniProtKB:D4AEP3}. Cell membrane {ECO:0000250|UniProtKB:Q80XQ8}; Multi-pass membrane protein {ECO:0000250|UniProtKB:Q80XQ8}. Cell projection, axon {ECO:0000250|UniProtKB:Q80XQ8}. Note=Expressed in neuronal cell bodies and axonal fibers. {ECO:0000250|UniPr... | null | null | null | null | null | FUNCTION: Inhibitor of neuronal axonal outgrowth. Acts as a negative regulator of CDC42 and STAT3 and a positive regulator of STMN2. Positive regulator of CDC27. {ECO:0000250|UniProtKB:D4AEP3}. | Homo sapiens (Human) |
A1KZ92 | PXDNL_HUMAN | MEPRLFCWTTLFLLAGWCLPGLPCPSRCLCFKSTVRCMHLMLDHIPQVPQQTTVLDLRFNRIREIPGSAFKKLKNLNTLLLNNNHIRKISRNAFEGLENLLYLYLYKNEIHALDKQTFKGLISLEHLYIHFNQLEMLQPETFGDLLRLERLFLHNNKLSKIPAGSFSNLDSLKRLRLDSNALVCDCDLMWLGELLQGFAQHGHTQAAATCEYPRRLHGRAVASVTVEEFNCQSPRITFEPQDVEVPSGNTVYFTCRAEGNPKPEIIWIHNNHSLDLEDDTRLNVFDDGTLMIRNTRESDQGVYQCMARNSAGEAKTQSAM... | 1.-.-.- | COFACTOR: Name=heme b; Xref=ChEBI:CHEBI:60344; Evidence={ECO:0000255|PROSITE-ProRule:PRU00298}; | hydrogen peroxide catabolic process [GO:0042744]; response to oxidative stress [GO:0006979] | endoplasmic reticulum [GO:0005783]; extracellular space [GO:0005615]; plasma membrane [GO:0005886] | endonuclease activity [GO:0004519]; heme binding [GO:0020037]; lactoperoxidase activity [GO:0140825]; metal ion binding [GO:0046872]; peroxidase activity [GO:0004601] | PF03098;PF07679;PF13927;PF13855;PF00093; | 6.20.200.20;1.10.640.10;2.60.40.10;3.80.10.10; | Peroxidase family, XPO subfamily | PTM: Phosphorylation by SRC on tyrosine residues is required for targeting to polysomes. {ECO:0000269|PubMed:22543864}. | SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:24253521}. Endoplasmic reticulum {ECO:0000269|PubMed:24253521}. Cell membrane {ECO:0000269|PubMed:24253521}.; SUBCELLULAR LOCATION: [Isoform PMR1]: Cytoplasm. Note=Associates with polysomes. | null | null | null | null | null | FUNCTION: Probable oxidoreductase (Probable). Lacks peroxidase activity (PubMed:24253521). Inhibits the peroxidase activity of PXDN through its interaction (PubMed:24253521). {ECO:0000269|PubMed:24253521, ECO:0000305|PubMed:24253521}.; FUNCTION: [Isoform PMR1]: Endonuclease selectively degrading some target mRNAs while... | Homo sapiens (Human) |
A1L0T0 | HACL2_HUMAN | METPAAAAPAGSLFPSFLLLACGTLVAALLGAAHRLGLFYQLLHKVDKASVRHGGENVAAVLRAHGVRFIFTLVGGHISPLLVACEKLGIRVVDTRHEVTAVFAADAMARLSGTVGVAAVTAGPGLTNTVTAVKNAQMAQSPILLLGGAASTLLQNRGALQAVDQLSLFRPLCKFCVSVRRVRDIVPTLRAAMAAAQSGTPGPVFVELPVDVLYPYFMVQKEMVPAKPPKGLVGRVVSWYLENYLANLFAGAWEPQPEGPLPLDIPQASPQQVQRCVEILSRAKRPLMVLGSQALLTPTSADKLRAAVETLGVPCFLGGM... | 4.1.2.- | COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250|UniProtKB:Q8CHM7}; Note=Binds 1 Mg(2+) ion per subunit. {ECO:0000250|UniProtKB:Q8CHM7}; COFACTOR: Name=thiamine diphosphate; Xref=ChEBI:CHEBI:58937; Evidence={ECO:0000269|PubMed:28289220}; Note=Binds 1 thiamine pyrophosphate per subunit. {ECO:0000250|... | fatty acid alpha-oxidation [GO:0001561]; isoleucine biosynthetic process [GO:0009097]; valine biosynthetic process [GO:0009099] | acetolactate synthase complex [GO:0005948]; endoplasmic reticulum membrane [GO:0005789]; membrane [GO:0016020] | acetolactate synthase activity [GO:0003984]; flavin adenine dinucleotide binding [GO:0050660]; lyase activity [GO:0016829]; magnesium ion binding [GO:0000287]; thiamine pyrophosphate binding [GO:0030976] | PF02775;PF00205;PF02776; | 3.40.50.970;3.40.50.1220; | TPP enzyme family | null | SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000269|PubMed:28289220}; Single-pass membrane protein {ECO:0000255}. | CATALYTIC ACTIVITY: Reaction=2-hydroxyoctadecanoyl-CoA = formyl-CoA + heptadecanal; Xref=Rhea:RHEA:55196, ChEBI:CHEBI:57376, ChEBI:CHEBI:74116, ChEBI:CHEBI:138631; Evidence={ECO:0000269|PubMed:28289220}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:55197; Evidence={ECO:0000305|PubMed:28289220}; CATALYTIC ACTIVI... | null | null | null | null | FUNCTION: Endoplasmic reticulum 2-OH acyl-CoA lyase involved in the cleavage (C1 removal) reaction in the fatty acid alpha-oxydation in a thiamine pyrophosphate (TPP)-dependent manner. Involved in the phytosphingosine degradation pathway. {ECO:0000269|PubMed:28289220}. | Homo sapiens (Human) |
A1L167 | U2QL1_HUMAN | MKELQDIARLSDRFISVELVDESLFDWNVKLHQVDKDSVLWQDMKETNTEFILLNLTFPDNFPFSPPFMRVLSPRLENGYVLDGGAICMELLTPRGWSSAYTVEAVMRQFAASLVKGQGRICRKAGKSKKSFSRKEAEATFKSLVKTHEKYGWVTPPVSDG | 2.3.2.23 | null | protein polyubiquitination [GO:0000209] | nucleoplasm [GO:0005654]; nucleus [GO:0005634]; plasma membrane [GO:0005886] | ATP binding [GO:0005524]; ubiquitin conjugating enzyme activity [GO:0061631] | PF00179; | 3.10.110.10; | Ubiquitin-conjugating enzyme family | null | SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:24000165}. | CATALYTIC ACTIVITY: Reaction=S-ubiquitinyl-[E1 ubiquitin-activating enzyme]-L-cysteine + [E2 ubiquitin-conjugating enzyme]-L-cysteine = [E1 ubiquitin-activating enzyme]-L-cysteine + S-ubiquitinyl-[E2 ubiquitin-conjugating enzyme]-L-cysteine.; EC=2.3.2.23; Evidence={ECO:0000255|PROSITE-ProRule:PRU00388}; | null | PATHWAY: Protein modification; protein ubiquitination. {ECO:0000255|PROSITE-ProRule:PRU00388}. | null | null | FUNCTION: Probable E2 ubiquitin-protein ligase that catalyzes the covalent attachment of ubiquitin to target proteins. May facilitate the monoubiquitination and degradation of MTOR and CCNE1 through interaction with FBXW7. {ECO:0000269|PubMed:24000165}. | Homo sapiens (Human) |
A1L190 | SYCE3_HUMAN | MDDADPEERNYDNMLKMLSDLNKDLEKLLEEMEKISVQATWMAYDMVVMRTNPTLAESMRRLEDAFVNCKEEMEKNWQELLHETKQRL | null | null | apoptotic process [GO:0006915]; cell division [GO:0051301]; ectopic germ cell programmed cell death [GO:0035234]; positive regulation of apoptotic process [GO:0043065]; positive regulation of developmental process [GO:0051094]; positive regulation of reproductive process [GO:2000243]; reciprocal meiotic recombination [... | central element [GO:0000801]; chromosome [GO:0005694]; nucleus [GO:0005634] | null | PF15191; | null | null | null | SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:B5KM66}. Chromosome {ECO:0000250|UniProtKB:B5KM66}. Note=Colocalizes with SYCE1 in the central elements. {ECO:0000250|UniProtKB:B5KM66}. | null | null | null | null | null | FUNCTION: Major component of the transverse central element of synaptonemal complexes (SCS), formed between homologous chromosomes during meiotic prophase. Required for chromosome loading of the central element-specific SCS proteins, and for initiating synapsis between homologous chromosomes. Chromosome loading appears... | Homo sapiens (Human) |
A1L1K7 | ACBG2_RAT | MTQEKKAEDPDRGMDTTSAAPRLWSTHCDGEVLLRLSKHGPGHETPMTIPELFQESVERFGAYPALASKNGKKWDTLTFSQYYDVCRKAARSLIKLGLQRFHGVGILGFNSVEWVVAALGAILAGGLCVGIYATNSAEACQYVIKQANVNVLIVENDQQLQKILSIPPDKMETVKAIVQYRLPLMENSTNLYSWQDFMELGNAIPNIQLDRVILSQKANQCAVIIYTSGTTGSPKGVMLSHDNITWTAGAMAREIELIHVSGKQDTIVSYLPLSHIAAQLMDIWIPIKVGVLTFFAQPDALRGTLVYTLQEVKPTYFLGV... | 6.2.1.15; 6.2.1.3 | null | cell differentiation [GO:0030154]; fatty acid metabolic process [GO:0006631]; long-chain fatty acid biosynthetic process [GO:0042759]; spermatogenesis [GO:0007283] | cytoplasm [GO:0005737]; cytosol [GO:0005829]; endoplasmic reticulum [GO:0005783]; membrane [GO:0016020]; mitochondrion [GO:0005739] | arachidonate-CoA ligase activity [GO:0047676]; ATP binding [GO:0005524]; fatty acyl-CoA hydrolase activity [GO:0047617]; long-chain fatty acid-CoA ligase activity [GO:0004467] | PF00501; | 3.40.50.12780; | ATP-dependent AMP-binding enzyme family, Bubblegum subfamily | null | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Membrane {ECO:0000250}; Peripheral membrane protein {ECO:0000250}. | CATALYTIC ACTIVITY: Reaction=a long-chain fatty acid + ATP + CoA = a long-chain fatty acyl-CoA + AMP + diphosphate; Xref=Rhea:RHEA:15421, ChEBI:CHEBI:30616, ChEBI:CHEBI:33019, ChEBI:CHEBI:57287, ChEBI:CHEBI:57560, ChEBI:CHEBI:83139, ChEBI:CHEBI:456215; EC=6.2.1.3; Evidence={ECO:0000250|UniProtKB:Q5FVE4}; PhysiologicalD... | null | null | null | null | FUNCTION: Catalyzes the conversion of fatty acids such as long chain and very long-chain fatty acids to their active form acyl-CoAs for both synthesis of cellular lipids, and degradation via beta-oxidation. Can activate diverse saturated, monosaturated and polyunsaturated fatty acids. Has increased ability to activate ... | Rattus norvegicus (Rat) |
A1L1K8 | HABP4_RAT | MKGALGSPVAAAGAAMQETFGCVVANRFHQLLDDESDPFDILREAEHRRQQQLQRKRRDEAAAASGAGHRGGRSPAVASGHRPGAAGRRESQKERKSLAVSSAQQPDSPGGPQPPGQKRTPRRGEQQGWNDNRGTDVVLDRAERRSYREYRPYDTERQAESTAEKFTDEKPVDRFDRDRPLRGRGGPRGGLRNRGRGGPGNRAFDSFDQRGKRDFERYGSSDKANRMEDSMGGCGVRTWGSGKDTSDTEPPAPMEETSMMEECQGVLDEESASKVPELEVEEENQVQEMTLDEWKNLQEQTRPKPEFNIRKPESTVPSKA... | null | null | cellular response to mechanical stimulus [GO:0071260]; mRNA processing [GO:0006397]; negative regulation of DNA binding [GO:0043392]; PML body organization [GO:0030578]; positive regulation of RNA splicing [GO:0033120]; positive regulation of translational initiation [GO:0045948]; ribosome hibernation [GO:0141014]; RNA... | Cajal body [GO:0015030]; cytoplasm [GO:0005737]; cytoplasmic stress granule [GO:0010494]; cytosol [GO:0005829]; Gemini of coiled bodies [GO:0097504]; nuclear membrane [GO:0031965]; nuclear speck [GO:0016607]; nucleolus [GO:0005730]; nucleus [GO:0005634]; sarcomere [GO:0030017]; sarcoplasm [GO:0016528]; synapse [GO:0045... | ribosome binding [GO:0043022]; RNA binding [GO:0003723]; SUMO binding [GO:0032183]; translation elongation factor binding [GO:0061770] | PF04774;PF16174; | null | SERBP1-HABP4 family | PTM: Phosphorylated by phorbol 12-myristate 13-acetate (PMA)-activated PKC isoforms at Thr-352 and Thr-373. {ECO:0000250|UniProtKB:Q5JVS0}.; PTM: Methylated. Methylation is decreased by phorbol 12-myristate 13-acetate (PMA)-activated PKC, in vitro. {ECO:0000250|UniProtKB:Q5JVS0}. | SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:15862299}. Cytoplasm {ECO:0000269|PubMed:15862299}. Cytoplasm, Stress granule {ECO:0000250|UniProtKB:Q5JVS0}. Cytoplasm, sarcoplasm {ECO:0000269|PubMed:15862299}. Nucleus, nuclear body {ECO:0000250|UniProtKB:Q5JVS0}. Nucleus, nucleolus {ECO:0000250|UniProtKB:Q5JVS0}. Nu... | null | null | null | null | null | FUNCTION: Ribosome-binding protein that promotes ribosome hibernation, a process during which ribosomes are stabilized in an inactive state and preserved from proteasomal degradation (By similarity). Acts via its association with EEF2/eEF2 factor at the A-site of the ribosome, promoting ribosome stabilization in an ina... | Rattus norvegicus (Rat) |
A1L1N5 | HN1BA_DANRE | MFANMVSKLTSLQQELLSALLDSGVTKDVLLQALEDLDPSPSAFGVKLDSLQMSPSGSKLSDTDSKPVFHTLTNGHSKGKLSGDEGSEDGDDYDTPPILKELQSQNTEEAAEQRAEIERMLAEDPWRAARMIKGYMQQHNIPQREVVDVTGLNQSHLSQHLNKGTPMKTQKRAALYTWYVRKQREILRQFNQATQGSGATMLDKGNQDQVLLFFSEFSQSGQGMVQPGDDAAIEPACKKLRRNRFKWGPASQQILYQAYERQKNPSKEEREALVEECNRAECLQRGVSPSKAHGLGSNLVTEVRVYNWFANRRKEEAFRQ... | null | null | anterior/posterior pattern specification [GO:0009952]; anterior/posterior pattern specification involved in pronephros development [GO:0034672]; digestive tract morphogenesis [GO:0048546]; embryonic digestive tract development [GO:0048566]; endocrine pancreas development [GO:0031018]; endoderm formation [GO:0001706]; g... | nucleus [GO:0005634] | DNA binding [GO:0003677]; DNA-binding transcription factor activity [GO:0003700]; DNA-binding transcription factor activity, RNA polymerase II-specific [GO:0000981]; protein dimerization activity [GO:0046983]; RNA polymerase II cis-regulatory region sequence-specific DNA binding [GO:0000978] | PF04814;PF04812; | 1.10.10.60;1.10.260.40; | HNF1 homeobox family | null | SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00108}. | null | null | null | null | null | FUNCTION: Transcription factor that binds to the inverted palindrome 5'-GTTAATNATTAAC-3' (By similarity). Required for induction of rhombomere r5/r6 gene expression in the hindbrain. {ECO:0000250|UniProtKB:P35680, ECO:0000269|PubMed:18945197}. | Danio rerio (Zebrafish) (Brachydanio rerio) |
A1L1V4 | LOL2B_DANRE | MLALWSISFVLLCSWRLSYAQYEHLGFAIAYQEPEQDLYTPPELPADTPRIQLRLAGEKRKHNEGRVEVFYEGEWGTVCDDDFTIHAAQVICRELGYFEAISWSPSSKYGKGEGRIWFDNVHCKGKEKSLAQCESNGIGVSDCKHSEDVGVVCSDKRIPGFKFVNTLTNNINSLNIQVEDVRIRPILASYRKRIPVTEGYVEVKDGGKWKQICDDEWTQMNSRVICGMFGFPGQKRYNTRVYKMFARRRKPSYWDYTINCTGKEAHLSSCTLGHTLSNSTCEEGTPVVVSCIPGRAFAPTPMTGYKKAFRQEQPLVRLRG... | 1.4.3.13 | COFACTOR: Name=Cu cation; Xref=ChEBI:CHEBI:23378; Evidence={ECO:0000250|UniProtKB:Q9Y4K0}; COFACTOR: Name=lysine tyrosylquinone residue; Xref=ChEBI:CHEBI:20489; Evidence={ECO:0000250|UniProtKB:Q9Y4K0}; Note=Contains 1 lysine tyrosylquinone. {ECO:0000250|UniProtKB:P33072, ECO:0000250|UniProtKB:Q9Y4K0}; | collagen fibril organization [GO:0030199]; endothelial cell migration [GO:0043542]; endothelial cell proliferation [GO:0001935]; epithelial to mesenchymal transition [GO:0001837]; heterochromatin organization [GO:0070828]; negative regulation of DNA-templated transcription [GO:0045892]; negative regulation of stem cell... | basement membrane [GO:0005604]; chromatin [GO:0000785]; collagen-containing extracellular matrix [GO:0062023]; endoplasmic reticulum [GO:0005783]; extracellular space [GO:0005615]; membrane [GO:0016020]; nucleus [GO:0005634] | calcium ion binding [GO:0005509]; copper ion binding [GO:0005507]; protein-lysine 6-oxidase activity [GO:0004720] | PF01186;PF00530; | 3.10.250.10; | Lysyl oxidase family | PTM: The lysine tyrosylquinone cross-link (LTQ) is generated by condensation of the epsilon-amino group of a lysine with a topaquinone produced by oxidation of tyrosine. {ECO:0000250|UniProtKB:Q9Y4K0}. | SUBCELLULAR LOCATION: Secreted, extracellular space, extracellular matrix, basement membrane {ECO:0000250|UniProtKB:Q9Y4K0}. Nucleus {ECO:0000250|UniProtKB:Q9Y4K0}. Chromosome {ECO:0000250|UniProtKB:Q9Y4K0}. Endoplasmic reticulum {ECO:0000250|UniProtKB:Q9Y4K0}. Note=Associated with chromatin. It is unclear how LOXL2 is... | CATALYTIC ACTIVITY: Reaction=H2O + L-lysyl-[protein] + O2 = (S)-2-amino-6-oxohexanoyl-[protein] + H2O2 + NH4(+); Xref=Rhea:RHEA:24544, Rhea:RHEA-COMP:9752, Rhea:RHEA-COMP:12448, ChEBI:CHEBI:15377, ChEBI:CHEBI:15379, ChEBI:CHEBI:16240, ChEBI:CHEBI:28938, ChEBI:CHEBI:29969, ChEBI:CHEBI:131803; EC=1.4.3.13; Evidence={ECO:... | null | null | null | null | FUNCTION: Mediates the post-translational oxidative deamination of lysine residues on target proteins leading to the formation of deaminated lysine (allysine) (By similarity). Acts as a transcription corepressor and specifically mediates deamination of trimethylated 'Lys-4' of histone H3 (H3K4me3), a specific tag for e... | Danio rerio (Zebrafish) (Brachydanio rerio) |
A1L259 | URAD_DANRE | MDINVVNALAYEDFVKLFGNVVEKCPLISAAIWSYRPFKDLADIEARISEFIHSLPDSGKEGILRCHPDLAGRDLQSGTLTPESQEEQSQAGMTTLDSAEIVHMYRLNSEYKERFGFPFVICARLNNKADIVRQLSERLKNRRTAELECAIEEVKKICSLRLHSIVLSDIQTKL | 4.1.1.97 | null | allantoin metabolic process [GO:0000255]; purine nucleobase metabolic process [GO:0006144]; urate catabolic process [GO:0019628] | peroxisome [GO:0005777] | 2-oxo-4-hydroxy-4-carboxy-5-ureidoimidazoline decarboxylase activity [GO:0051997] | PF09349; | 1.10.3330.10; | OHCU decarboxylase family | null | SUBCELLULAR LOCATION: Peroxisome {ECO:0000305}. | CATALYTIC ACTIVITY: Reaction=5-hydroxy-2-oxo-4-ureido-2,5-dihydro-1H-imidazole-5-carboxylate + H(+) = (S)-allantoin + CO2; Xref=Rhea:RHEA:26301, ChEBI:CHEBI:15378, ChEBI:CHEBI:15678, ChEBI:CHEBI:16526, ChEBI:CHEBI:58639; EC=4.1.1.97; | null | PATHWAY: Purine metabolism; urate degradation; (S)-allantoin from urate: step 3/3. | null | null | FUNCTION: Catalyzes the stereoselective decarboxylation of 2-oxo-4-hydroxy-4-carboxy-5-ureidoimidazoline (OHCU) to (S)-allantoin. {ECO:0000269|PubMed:17428786}. | Danio rerio (Zebrafish) (Brachydanio rerio) |
A1L2G3 | BAP1_DANRE | MNKGWLELESDPGLFTLLVEDFGVKGVQVEEIYDLQSKCQSPVYGFIFLFKWIEERRSRRKVSTLVDETSVIDDDIVNDMFFAHQLIPNSCATHALLSVLLNCSGVELGMTLSRMKAFTKGFNPESKGYAIGNAPELAKAHNSHARPEPRHLPEKQNGISAVRTMEAFHFVSYVPIKDRLFELDGLKAYPIDHGPWGEDEEWTDKARRVIMERIGLATAGEPYHDIRFNLMAVVPDRRIKYESKLDILKRNRQIILEGLQQIREKKVIRMTQQESGQDRKQQDSSSSEDTPPVVKKEEVQETPIPSGAEQATPTEAQEGA... | 3.4.19.12 | null | chromatin organization [GO:0006325]; cranial skeletal system development [GO:1904888]; negative regulation of DNA-templated transcription [GO:0045892]; Notch signaling pathway [GO:0007219]; protein deubiquitination [GO:0016579]; protein K48-linked deubiquitination [GO:0071108]; regulation of cell cycle [GO:0051726]; re... | cytoplasm [GO:0005737]; nucleus [GO:0005634]; PR-DUB complex [GO:0035517] | chromatin binding [GO:0003682]; cysteine-type deubiquitinase activity [GO:0004843] | PF01088;PF18031; | 1.20.58.860;3.40.532.10; | Peptidase C12 family, BAP1 subfamily | null | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q92560}. Nucleus {ECO:0000250|UniProtKB:Q92560}. Note=Mainly nuclear. Binds to chromatin. {ECO:0000250|UniProtKB:Q92560}. | CATALYTIC ACTIVITY: Reaction=Thiol-dependent hydrolysis of ester, thioester, amide, peptide and isopeptide bonds formed by the C-terminal Gly of ubiquitin (a 76-residue protein attached to proteins as an intracellular targeting signal).; EC=3.4.19.12; Evidence={ECO:0000250|UniProtKB:Q92560}; | null | null | null | null | FUNCTION: Deubiquitinating enzyme that plays a key role in chromatin by mediating deubiquitination of histone H2A. Catalytic component of the PR-DUB complex, a complex that specifically mediates deubiquitination of histone H2A monoubiquitinated at 'Lys-119' (H2AK119ub1) (By similarity). {ECO:0000250|UniProtKB:Q92560}. | Danio rerio (Zebrafish) (Brachydanio rerio) |
A1L314 | MPEG1_MOUSE | MNSFMALVLIWMIIACAEADKPLGETGTTGFQICKNALKLPVLEVLPGGGWDNLRNVDMGRVMDLTYTNCKTTEDGQYIIPDEVYTIPQKESNLEMNSEVLESWMNYQSTTSLSINTELALFSRVNGKFSTEFQRMKTLQVKDQAVTTRVQVRNRIYTVKTTPTSELSLGFTKALMDICDQLEKNQTKMATYLAELLILNYGTHVITSVDAGAALVQEDHVRSSFLLDNQNSQNTVTASAGIAFLNIVNFKVETDYISQTSLTKDYLSNRTNSRVQSFGGVPFYPGITLETWQKGITNHLVAIDRAGLPLHFFIKPDKLP... | null | null | adaptive immune response [GO:0002250]; antibacterial innate immune response [GO:0140367]; antigen processing and presentation of exogenous peptide antigen [GO:0002478]; antigen processing and presentation of exogenous peptide antigen via MHC class I [GO:0042590]; defense response to bacterium [GO:0042742]; defense resp... | cytoplasmic vesicle [GO:0031410]; endolysosome [GO:0036019]; phagocytic vesicle [GO:0045335]; phagocytic vesicle membrane [GO:0030670]; phagolysosome membrane [GO:0061474] | pore-forming activity [GO:0140911]; wide pore channel activity [GO:0022829] | PF01823; | null | MPEG1 family | PTM: Proteolytically processed in two steps to generate the Macrophage-expressed gene 1 protein, processed form: cleaved by trypsin in proximity of the helical transmembrane domain releases the ectodomain into the lysosomal lumen to orient the pore-forming domain toward the endogenous membranes, and processed by the as... | SUBCELLULAR LOCATION: Cytoplasmic vesicle membrane {ECO:0000269|PubMed:26402460, ECO:0000269|PubMed:26418746, ECO:0000269|PubMed:35471730}; Multi-pass membrane protein {ECO:0000269|PubMed:32064340, ECO:0000269|PubMed:36245269}. Note=Bacterial infection induces translocation of the cytoplasmic vesicles to bacterium-cont... | null | null | null | null | null | FUNCTION: Pore-forming protein involved in both innate and adaptive immunity (PubMed:26402460, PubMed:30249808, PubMed:32064340, PubMed:36028507, PubMed:36245269, PubMed:37347855). Plays a central role in antigen cross-presentation in dendritic cells by forming a pore in antigen-containing compartments, thereby promoti... | Mus musculus (Mouse) |
A1L390 | PKHG3_HUMAN | MPVSTSLHQDGSQERPVSLTSTTSSSGSSCDSRSAMEEPSSSEAPAKNGAGSLRSRHLPNSNNNSSSWLNVKGPLSPFNSRAAAGPAHHKLSYLGRVVREIVETERMYVQDLRSIVEDYLLKIIDTPGLLKPEQVSALFGNIENIYALNSQLLRDLDSCNSDPVAVASCFVERSQEFDIYTQYCNNYPNSVAALTECMRDKQQAKFFRDRQELLQHSLPLGSYLLKPVQRILKYHLLLQEIAKHFDEEEDGFEVVEDAIDTMTCVAWYINDMKRRHEHAVRLQEIQSLLINWKGPDLTTYGELVLEGTFRVHRVRNERTF... | null | null | regulation of cell migration [GO:0030334]; regulation of establishment of cell polarity [GO:2000114]; regulation of small GTPase mediated signal transduction [GO:0051056] | cytoskeleton [GO:0005856]; cytosol [GO:0005829] | actin binding [GO:0003779]; guanyl-nucleotide exchange factor activity [GO:0005085]; small GTPase binding [GO:0031267] | PF00169;PF00621; | 1.20.900.10;2.30.29.30; | null | null | SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton {ECO:0000269|PubMed:27555588}. Note=Colocalizes with actin at the leading edge of polarized cells. {ECO:0000269|PubMed:27555588}. | null | null | null | null | null | FUNCTION: Plays a role in controlling cell polarity and cell motility by selectively binding newly polymerized actin and activating RAC1 and CDC42 to enhance local actin polymerization. {ECO:0000269|PubMed:27555588}. | Homo sapiens (Human) |
A1L3C1 | GAR5A_MOUSE | MKGGRDLKAARGGADRPLAPAYAPCRPGRLQRHLLSGEFDQLRDFPIFESNFVQVTRFGEVANKVTMGVAASSPALELPDLLLLAGPDKENGHLQLLGLFPLQFVQLFVHDESRQQLKVKFRTGRAFYLQLRSPPETRDCEFGRWVRLLYRLRFHSPTCAVPFTHEDTAPEEEEEEEEEEEEEEVKEGQLQPPEFQATEARLDPQVSELWGL | null | null | defense response to virus [GO:0051607]; innate immune response [GO:0045087]; positive regulation of type I interferon production [GO:0032481] | Golgi apparatus [GO:0005794]; nucleus [GO:0005634] | null | PF12480; | null | GARIN family | null | SUBCELLULAR LOCATION: Golgi apparatus {ECO:0000269|PubMed:28930687}. | null | null | null | null | null | FUNCTION: RAB2B effector protein which promotes cytosolic DNA-induced innate immune responses. Regulates IFN responses against DNA viruses by regulating the CGAS-STING signaling axis. {ECO:0000269|PubMed:28930687}. | Mus musculus (Mouse) |
A1L3G9 | NMP1B_XENLA | MAGEVEGRGCGFSLGVLVTLLVLPLPSLCTLSTEKELHVIKLYEGRMVRYNESRNFCYQRTYEPKWSDVWTKIQIRINSTKMIRVTQVDNEEKLKEMETFNMFDFFSSFLKEKLNDTFIYVNLYSNKTCVKVHLTDTDTYYSVALSRGFDPRLFFVFLCGLLLFFYGDTLSRSQLFFYSTGITVGMLASMLILVFMLSKLMPKKSPFFALLLGGWSVSIYVIQLVFRNLQAICSEYWQYLIVYLGIVGFVSFAFCYIYGPLENERSINILNWTLQLIGLLLMYVSVQIQHIAVTIVVIAFCTKQIEYPVQWIYILYRKIK... | null | null | erythrocyte enucleation [GO:0043131]; erythrocyte maturation [GO:0043249]; eye development [GO:0001654] | nuclear envelope [GO:0005635]; nuclear inner membrane [GO:0005637] | protein self-association [GO:0043621] | PF10225; | null | NEMP family | PTM: Phosphorylated. {ECO:0000269|PubMed:25946333}. | SUBCELLULAR LOCATION: Nucleus inner membrane {ECO:0000269|PubMed:19167377, ECO:0000269|PubMed:25946333}; Multi-pass membrane protein {ECO:0000255}; Nucleoplasmic side {ECO:0000269|PubMed:19167377}. Nucleus envelope {ECO:0000269|PubMed:19167377}. Note=Localization in the nuclear membrane is essential for its function. C... | null | null | null | null | null | FUNCTION: In concert with ran, required for proper eye development (PubMed:25946333). May be involved in the expression of early eye marker genes (PubMed:19167377). Contributes to nuclear envelope stiffness in germ cells (By similarity). Required for fertility (By similarity). Essential for normal erythropoiesis (By si... | Xenopus laevis (African clawed frog) |
A1L3P4 | SL9A6_MOUSE | MAGARRGWRLAPVRRGVCGPRARPLMRPLWLLFAVSFFGWTGALDGSGGTTRAMDEEIVSEKQAEESHRQDSANLLIFILLLTLTILTIWLFKHRRARFLHETGLAMIYGLLVGLVLRYGIHVPSDVNNVTLSCEVQSSPTTLLVNVSGKFYEYTLKGEISSHELNNVQDNEMLRKVTFDPEVFFNILLPPIIFYAGYSLKRRHFFRNLGSILAYAFLGTAISCFVIGSIMYGCVTLMKVTGQLAGDFYFTDCLLFGAIVSATDPVTVLAIFHELQVDVELYALLFGESVLNDAVAIVLSSSIVAYQPAGDNSHTFDVTA... | null | null | axon extension [GO:0048675]; brain-derived neurotrophic factor receptor signaling pathway [GO:0031547]; dendrite extension [GO:0097484]; dendritic spine development [GO:0060996]; establishment of cell polarity [GO:0030010]; glial cell activation [GO:0061900]; neuron projection morphogenesis [GO:0048812]; potassium ion ... | axon terminus [GO:0043679]; axonal spine [GO:0044308]; cytoplasmic vesicle [GO:0031410]; dendrite [GO:0030425]; early endosome [GO:0005769]; early endosome membrane [GO:0031901]; endosome [GO:0005768]; glutamatergic synapse [GO:0098978]; late endosome [GO:0005770]; late endosome membrane [GO:0031902]; mitochondrion [GO... | potassium:proton antiporter activity [GO:0015386]; sodium:proton antiporter activity [GO:0015385] | PF00999; | 6.10.140.1330; | Monovalent cation:proton antiporter 1 (CPA1) transporter (TC 2.A.36) family | PTM: Ubiquitinated (in vitro). {ECO:0000250|UniProtKB:Q92581}.; PTM: Glycosylated. {ECO:0000250|UniProtKB:Q92581}. | SUBCELLULAR LOCATION: Endosome membrane {ECO:0000250|UniProtKB:Q92581}; Multi-pass membrane protein {ECO:0000255}. Recycling endosome membrane {ECO:0000269|PubMed:23303939, ECO:0000269|PubMed:24035762}; Multi-pass membrane protein {ECO:0000255}. Early endosome membrane {ECO:0000269|PubMed:23303939, ECO:0000269|PubMed:2... | CATALYTIC ACTIVITY: Reaction=H(+)(out) + Na(+)(in) = H(+)(in) + Na(+)(out); Xref=Rhea:RHEA:29419, ChEBI:CHEBI:15378, ChEBI:CHEBI:29101; Evidence={ECO:0000305|PubMed:21413028}; CATALYTIC ACTIVITY: Reaction=H(+)(out) + K(+)(in) = H(+)(in) + K(+)(out); Xref=Rhea:RHEA:29467, ChEBI:CHEBI:15378, ChEBI:CHEBI:29103; Evidence={... | null | null | null | null | FUNCTION: Endosomal Na(+), K(+)/H(+) antiporter. Mediates the electroneutral exchange of endosomal luminal H(+) for a cytosolic Na(+) or K(+). By facilitating proton efflux, SLC9A6 counteracts the acidity generated by vacuolar (V)-ATPase, thereby limiting luminal acidification. Responsible for alkalizing and maintainin... | Mus musculus (Mouse) |
A1L3X0 | ELOV7_HUMAN | MAFSDLTSRTVHLYDNWIKDADPRVEDWLLMSSPLPQTILLGFYVYFVTSLGPKLMENRKPFELKKAMITYNFFIVLFSVYMCYEFVMSGWGIGYSFRCDIVDYSRSPTALRMARTCWLYYFSKFIELLDTIFFVLRKKNSQVTFLHVFHHTIMPWTWWFGVKFAAGGLGTFHALLNTAVHVVMYSYYGLSALGPAYQKYLWWKKYLTSLQLVQFVIVAIHISQFFFMEDCKYQFPVFACIIMSYSFMFLLLFLHFWYRAYTKGQRLPKTVKNGTCKNKDN | 2.3.1.199 | null | fatty acid elongation, monounsaturated fatty acid [GO:0034625]; fatty acid elongation, polyunsaturated fatty acid [GO:0034626]; fatty acid elongation, saturated fatty acid [GO:0019367]; long-chain fatty-acyl-CoA biosynthetic process [GO:0035338]; sphingolipid biosynthetic process [GO:0030148]; unsaturated fatty acid bi... | endoplasmic reticulum [GO:0005783]; endoplasmic reticulum membrane [GO:0005789] | fatty acid elongase activity [GO:0009922] | PF01151; | null | ELO family, ELOVL7 subfamily | null | SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000255|HAMAP-Rule:MF_03207, ECO:0000269|PubMed:20937905}; Multi-pass membrane protein {ECO:0000255|HAMAP-Rule:MF_03207}. | CATALYTIC ACTIVITY: Reaction=a very-long-chain acyl-CoA + H(+) + malonyl-CoA = a very-long-chain 3-oxoacyl-CoA + CO2 + CoA; Xref=Rhea:RHEA:32727, ChEBI:CHEBI:15378, ChEBI:CHEBI:16526, ChEBI:CHEBI:57287, ChEBI:CHEBI:57384, ChEBI:CHEBI:90725, ChEBI:CHEBI:90736; EC=2.3.1.199; Evidence={ECO:0000255|HAMAP-Rule:MF_03207, ECO... | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=2.6 uM for (9Z,12Z,15Z)-octadecatrienoyl-CoA/C18:3(n-3)-CoA {ECO:0000269|PubMed:21959040}; KM=11.7 uM for malonyl-CoA {ECO:0000269|PubMed:21959040}; Vmax=0.33 pmol/min/ug enzyme with (9Z,12Z,15Z)-octadecatrienoyl-CoA/C18:3(n-3)-CoA as substrate {ECO:0000269|PubMed:... | PATHWAY: Lipid metabolism; fatty acid biosynthesis. {ECO:0000255|HAMAP-Rule:MF_03207, ECO:0000269|PubMed:20937905, ECO:0000269|PubMed:21959040}. | null | null | FUNCTION: Catalyzes the first and rate-limiting reaction of the four reactions that constitute the long-chain fatty acids elongation cycle. This endoplasmic reticulum-bound enzymatic process allows the addition of 2 carbons to the chain of long- and very long-chain fatty acids (VLCFAs) per cycle. Condensing enzyme with... | Homo sapiens (Human) |
A1L4H1 | SRCRL_HUMAN | MRVLACLLAALVGIQAVERLRLADGPHGCAGRLEVWHGGRWGTVCDDGWDLRDAAVACRQLGCGGALAAPGGAFFGEGAGPVWLSELACRGNEGQLGLCHHRGWKAHICSHEEDAGVVCAGQRVANSRDDSTSPLDGAPWPGLLLELSPSTEEPLVTHAPRPAGNPQNASRKKSPRPKQAKSTRAPLLTTGAPRQERLRLVSGPHRCAGRLEVWHGGRWGTVCDDGWDLRDAAVACRELGCGGALAAPGGARFGPGAGPVWMDDVGCGGGEQALRDCPRSPWGRSNCDHSEDAGLVCTGPAPRLRLADGPHGCAGRLEVW... | null | null | defense response [GO:0006952]; defense response to Gram-negative bacterium [GO:0050829]; defense response to Gram-positive bacterium [GO:0050830]; detection of bacterial lipoprotein [GO:0042494]; innate immune response [GO:0045087]; negative regulation of interleukin-8 production [GO:0032717]; zymogen activation [GO:00... | collagen-containing extracellular matrix [GO:0062023]; cytoplasm [GO:0005737]; extracellular matrix [GO:0031012]; extracellular space [GO:0005615]; plasma membrane [GO:0005886] | extracellular matrix binding [GO:0050840]; fibronectin binding [GO:0001968]; laminin binding [GO:0043236]; scavenger receptor activity [GO:0005044]; serine-type endopeptidase activity [GO:0004252] | PF00530; | 3.10.250.10; | null | null | SUBCELLULAR LOCATION: Secreted {ECO:0000250}. Cytoplasm {ECO:0000250}. | null | null | null | null | null | FUNCTION: Binds to extracellular matrix proteins. Binds to pathogen-associated molecular patterns (PAMPs) present on the cell walls of Gram-positive and Gram-negative bacteria and fungi, behaving as a pattern recognition receptor (PRR). Induces bacterial and fungal aggregation and subsequent inhibition of PAMP-induced ... | Homo sapiens (Human) |
A1L4K1 | FSD2_HUMAN | MEEESGEELGLDRSTPKDFHFYHMDLYDSEDRLHLFPEENTRMRKVVQAEMANESRGAGDGKAQRDLQEEVDELVHLYGLEDDHELGDEFVDENIPRTGVSEYPPYMMKRRDPAREQRDWRLSGEAAEAEDLGFGGWGSAGQCQDLREAYRYTHGRASEEYECYVIPEEEDEEEAADVFCVTCKTPIRAFQKVFDEHKEHEVIPLNEALESAKDEIHKNMYKLEKQIIEMENFANHLEEVFITVEENFGKQEQNFESHYNEILETLAQKYEEKIQALGEKKKEKLEALYGQLVSCGENLDTCKELMETIEEMCHEEKVDF... | null | null | null | nucleus [GO:0005634]; perinuclear region of cytoplasm [GO:0048471]; sarcoplasmic reticulum [GO:0016529] | null | PF00041;PF00622; | 2.60.120.920;3.30.160.60;2.60.40.10; | null | null | SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:H0UZ81}. Sarcoplasmic reticulum {ECO:0000250|UniProtKB:H0UZ81}. Cytoplasm, perinuclear region {ECO:0000250|UniProtKB:H0UZ81}. Note=In skeletal muscles and striated muscles flanks Z-disks. Partially colocalizes with RYR2 in the sarcoplasmic reticulum. {ECO:0000250|Uni... | null | null | null | null | null | null | Homo sapiens (Human) |
A1S1I8 | FADB_SHEAM | MIYQSPTIQVELTADKIARLCFNAPGSVNKFDRETLASLNAALDVLKDSDAKAAVLTSGKDTFIVGADITEFLALFAEEDAKLMEWIAQANVVFNKLEDLPFPTVSAIKGFALGGGCEAILATDFRVADTSAKIGLPETKLGLIPGFGGTVRLPRLIGADNALEWITTGKDQRPEDALKVGAIDAVVAPENLEAAAIQMLNDALAGKLDWQARRARKQAPLTLPKLEAMMSFTTAKGMVYAVAGKHYPAPMAAVSVVEQAAGMSRAEALVVEHNAFIKLAKTDVATALIGIFLNDQLVKGKAKKASKLAKDIKHAAVLGA... | 1.1.1.35; 4.2.1.17; 5.1.2.3; 5.3.3.8 | null | fatty acid beta-oxidation [GO:0006635] | fatty acid beta-oxidation multienzyme complex [GO:0036125] | 3-hydroxyacyl-CoA dehydrogenase activity [GO:0003857]; 3-hydroxybutyryl-CoA epimerase activity [GO:0008692]; delta(3)-delta(2)-enoyl-CoA isomerase activity [GO:0004165]; enoyl-CoA hydratase activity [GO:0004300]; NAD+ binding [GO:0070403] | PF00725;PF02737;PF00378; | 1.10.1040.50;3.40.50.720; | Enoyl-CoA hydratase/isomerase family; 3-hydroxyacyl-CoA dehydrogenase family | null | null | CATALYTIC ACTIVITY: Reaction=a (3S)-3-hydroxyacyl-CoA + NAD(+) = a 3-oxoacyl-CoA + H(+) + NADH; Xref=Rhea:RHEA:22432, ChEBI:CHEBI:15378, ChEBI:CHEBI:57318, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945, ChEBI:CHEBI:90726; EC=1.1.1.35; Evidence={ECO:0000255|HAMAP-Rule:MF_01621}; CATALYTIC ACTIVITY: Reaction=a (3S)-3-hydroxyacyl-... | null | PATHWAY: Lipid metabolism; fatty acid beta-oxidation. {ECO:0000255|HAMAP-Rule:MF_01621}. | null | null | FUNCTION: Involved in the aerobic and anaerobic degradation of long-chain fatty acids via beta-oxidation cycle. Catalyzes the formation of 3-oxoacyl-CoA from enoyl-CoA via L-3-hydroxyacyl-CoA. It can also use D-3-hydroxyacyl-CoA and cis-3-enoyl-CoA as substrate. {ECO:0000255|HAMAP-Rule:MF_01621}. | Shewanella amazonensis (strain ATCC BAA-1098 / SB2B) |
A1TDK2 | KGD_MYCVP | MNSPSPFGQNEWLVEEMYRKFREDPSSVDPSWHEFLVDYSPEPTNDAPAGNGKPAAAPTAPPEPASAPAPKPASTNGGAPPAKADTSTTRAPEKKPEEKTSPAPKAKTAAPAGVSDDDETQVLRGAAAAVVKNMSASLDVPTATSVRAIPAKAMIDNRIVINNHLKRTRGGKISFTHLLGYAIVQAVKKFPNMNRHFAEIDGKPVAVTPAHTNLGLAIDLPGKDGKRSLVVAAIKNCETMHFGQFIAAYEDIVRRARDGKLTAEDFAGVTISLTNPGTIGTVHSVPRLMKGQGAIVGAGAMEYPAEFQGASEERIAELGV... | 1.2.4.2; 2.2.1.5; 2.3.1.61; 4.1.1.71 | COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250}; COFACTOR: Name=thiamine diphosphate; Xref=ChEBI:CHEBI:58937; Evidence={ECO:0000250}; | tricarboxylic acid cycle [GO:0006099] | cytosol [GO:0005829]; oxoglutarate dehydrogenase complex [GO:0045252] | 2-hydroxy-3-oxoadipate synthase activity [GO:0050439]; 2-oxoglutarate decarboxylase activity [GO:0008683]; dihydrolipoyllysine-residue succinyltransferase activity [GO:0004149]; magnesium ion binding [GO:0000287]; oxoglutarate dehydrogenase (succinyl-transferring) activity [GO:0004591]; thiamine pyrophosphate binding [... | PF00198;PF16078;PF00676;PF16870;PF02779; | 3.40.50.12470;3.40.50.970;3.30.559.10;3.40.50.11610;1.10.287.1150; | 2-oxoacid dehydrogenase family, Kgd subfamily | null | null | CATALYTIC ACTIVITY: Reaction=2-oxoglutarate + glyoxylate + H(+) = 2-hydroxy-3-oxoadipate + CO2; Xref=Rhea:RHEA:14341, ChEBI:CHEBI:15378, ChEBI:CHEBI:16526, ChEBI:CHEBI:16810, ChEBI:CHEBI:36655, ChEBI:CHEBI:57712; EC=2.2.1.5; CATALYTIC ACTIVITY: Reaction=2-oxoglutarate + H(+) = CO2 + succinate semialdehyde; Xref=Rhea:RH... | null | PATHWAY: Carbohydrate metabolism; tricarboxylic acid cycle; succinate from 2-oxoglutarate (transferase route): step 1/2.; PATHWAY: Carbohydrate metabolism; tricarboxylic acid cycle; succinyl-CoA from 2-oxoglutarate (dehydrogenase route): step 1/1. | null | null | FUNCTION: Shows three enzymatic activities that share a first common step, the attack of thiamine-PP on 2-oxoglutarate (alpha-ketoglutarate, KG), leading to the formation of an enamine-thiamine-PP intermediate upon decarboxylation. Thus, displays KGD activity, catalyzing the decarboxylation from five-carbon 2-oxoglutar... | Mycolicibacterium vanbaalenii (strain DSM 7251 / JCM 13017 / BCRC 16820 / KCTC 9966 / NRRL B-24157 / PYR-1) (Mycobacterium vanbaalenii) |
A1TFU9 | HPXO_MYCVP | MKVVIVGAGMGGMSAAIALRQIGIDTVVYERVTENKPVGAAISVWSNGVKCLNYLGLQEETAELGGKVETMSYVDGHTGDTMCRFSMHPLIEQVGQRPYPIARAELQLMLMKAYGIDDINFGMKMVGVENDTAGSAAKATFADGTTVSADVIIGADGAGSITREYVLGGPVSRRYAGYVNYNGLVSTDDAIGPATEWTTYVGDGKRVSVMPVSDDRFYFFFDVVEPQGSPYEEGRVREVLRAHFAGWTPGVQTLIDTLDPLATNRVEILDLDPFHTWVKGRVAVLGDAAHNTTPDIGQGGCSAMEDAIALQWAFKDHPDD... | 1.14.13.113 | COFACTOR: Name=FAD; Xref=ChEBI:CHEBI:57692; Evidence={ECO:0000269|PubMed:23760935}; | purine nucleobase metabolic process [GO:0006144]; urate catabolic process [GO:0019628] | null | FAD binding [GO:0071949]; FAD-dependent urate hydroxylase activity [GO:0102099]; NADH binding [GO:0070404]; NADPH binding [GO:0070402]; oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen, NAD(P)H as one donor, and incorporation of one atom of oxygen [GO:0016709]; urate... | PF01494; | 3.50.50.60; | FAD-dependent urate hydroxylase family | null | null | CATALYTIC ACTIVITY: Reaction=H(+) + NADH + O2 + urate = 5-hydroxyisourate + H2O + NAD(+); Xref=Rhea:RHEA:27329, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, ChEBI:CHEBI:17775, ChEBI:CHEBI:18072, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945; EC=1.14.13.113; Evidence={ECO:0000269|PubMed:23760935}; | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=413 uM for urate {ECO:0000269|PubMed:23760935}; Note=kcat is 56.0 sec(-1) for the NADH-dependent oxidation of urate. Exhibits a Michaelian behavior only toward urate and a cooperative behavior toward NADH and NADPH. {ECO:0000269|PubMed:23760935}; | PATHWAY: Purine metabolism; urate degradation. {ECO:0000305|PubMed:23760935}. | null | null | FUNCTION: Catalyzes the hydroxylation of urate to 5-hydroxyisourate (HIU). Is likely to be involved in the urate degradation pathway to allantoin. Prefers NADH over NADPH as the electron donor. {ECO:0000269|PubMed:23760935}. | Mycolicibacterium vanbaalenii (strain DSM 7251 / JCM 13017 / BCRC 16820 / KCTC 9966 / NRRL B-24157 / PYR-1) (Mycobacterium vanbaalenii) |
A1UK81 | KGD_MYCSK | MSSSPSPFGQNEWLVEEMYRKFREDPSSVDPSWHEFLVDYNPEPTTDSSASENGQQTRTAAPKAPPEPAPAPAPKTPDSKTPDSKSQAPKQDSKPQESKPQAKAKPAESKSSTKPADAKSEKSGKSGTNGAAKPAAQPADDSDQNQVLRGAAAAVAKNMSASLDVPTATSVRAIPAKLMIDNRVVINNHLKRTRGGKISFTHLIGYAIVAAVKKFPNMNRHFAEVDGKPNAVTPAHTNLGLAIDLQGKDGNRQLVVAAIKKADTMRFGQFIAAYEDIVRRARDGKLTAEDFSGVTISLTNPGTIGTVHSVPRLMRGQGAI... | 1.2.4.2; 2.2.1.5; 2.3.1.61; 4.1.1.71 | COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250}; COFACTOR: Name=thiamine diphosphate; Xref=ChEBI:CHEBI:58937; Evidence={ECO:0000250}; | tricarboxylic acid cycle [GO:0006099] | cytosol [GO:0005829]; oxoglutarate dehydrogenase complex [GO:0045252] | 2-hydroxy-3-oxoadipate synthase activity [GO:0050439]; 2-oxoglutarate decarboxylase activity [GO:0008683]; dihydrolipoyllysine-residue succinyltransferase activity [GO:0004149]; magnesium ion binding [GO:0000287]; oxoglutarate dehydrogenase (succinyl-transferring) activity [GO:0004591]; thiamine pyrophosphate binding [... | PF00198;PF16078;PF00676;PF16870;PF02779; | 3.40.50.12470;3.40.50.970;3.30.559.10;3.40.50.11610;1.10.287.1150; | 2-oxoacid dehydrogenase family, Kgd subfamily | null | null | CATALYTIC ACTIVITY: Reaction=2-oxoglutarate + glyoxylate + H(+) = 2-hydroxy-3-oxoadipate + CO2; Xref=Rhea:RHEA:14341, ChEBI:CHEBI:15378, ChEBI:CHEBI:16526, ChEBI:CHEBI:16810, ChEBI:CHEBI:36655, ChEBI:CHEBI:57712; EC=2.2.1.5; CATALYTIC ACTIVITY: Reaction=2-oxoglutarate + H(+) = CO2 + succinate semialdehyde; Xref=Rhea:RH... | null | PATHWAY: Carbohydrate metabolism; tricarboxylic acid cycle; succinate from 2-oxoglutarate (transferase route): step 1/2.; PATHWAY: Carbohydrate metabolism; tricarboxylic acid cycle; succinyl-CoA from 2-oxoglutarate (dehydrogenase route): step 1/1. | null | null | FUNCTION: Shows three enzymatic activities that share a first common step, the attack of thiamine-PP on 2-oxoglutarate (alpha-ketoglutarate, KG), leading to the formation of an enamine-thiamine-PP intermediate upon decarboxylation. Thus, displays KGD activity, catalyzing the decarboxylation from five-carbon 2-oxoglutar... | Mycobacterium sp. (strain KMS) |
A1X148 | CAV2_ECHTE | MGLESEKADVQLFMDDDAYSRHSGVDFVEAEKFSASGPDRDPHRLNSHLQLGFQDVIAEPETTHSFDKVWICSHALFEISKYVLYKFLTFFLAIPLAFAAGILFAILSCLHIWIIMPFVKTCLMVLPSVQTIWKSVTDVVIAPLCTSVGRSFSSVSLQLSQD | null | null | caveola assembly [GO:0070836]; endoplasmic reticulum organization [GO:0007029]; insulin receptor signaling pathway [GO:0008286]; mitochondrion organization [GO:0007005]; negative regulation of endothelial cell proliferation [GO:0001937]; positive regulation of dopamine receptor signaling pathway [GO:0060161]; positive ... | caveola [GO:0005901]; cytoplasmic vesicle [GO:0031410]; focal adhesion [GO:0005925]; Golgi membrane [GO:0000139]; nucleus [GO:0005634]; perinuclear region of cytoplasm [GO:0048471]; plasma membrane raft [GO:0044853]; sarcolemma [GO:0042383] | D1 dopamine receptor binding [GO:0031748]; molecular adaptor activity [GO:0060090]; protein kinase binding [GO:0019901] | PF01146; | null | Caveolin family | PTM: Phosphorylated on serine and tyrosine residues. CAV1 promotes phosphorylation on Ser-23 which then targets the complex to the plasma membrane, lipid rafts and caveolae. Phosphorylation on Ser-36 appears to modulate mitosis in endothelial cells. Phosphorylation on Tyr-19 is required for insulin-induced phosphorylat... | SUBCELLULAR LOCATION: Nucleus {ECO:0000250}. Golgi apparatus membrane; Peripheral membrane protein. Cell membrane; Peripheral membrane protein. Membrane, caveola; Peripheral membrane protein. Note=Potential hairpin-like structure in the membrane. Membrane protein of caveolae. Tyr-19-phosphorylated form is enriched at s... | null | null | null | null | null | FUNCTION: May act as a scaffolding protein within caveolar membranes. Interacts directly with G-protein alpha subunits and can functionally regulate their activity. Acts as an accessory protein in conjunction with CAV1 in targeting to lipid rafts and driving caveolae formation. The Ser-36 phosphorylated form has a role... | Echinops telfairi (Lesser hedgehog tenrec) |
A1X149 | CAV1_ECHTE | MSGGKYVDSEGHLYTLPIREQGNIYKPNNKAMAEDMNEKQVYDAHTKEIDLVNRDPKHLNDDVVKIDFEDVIAEPEGTHSFDGIWKASFTTFTVTKYWFYRLLSGIFGIPMALIWGVYFAILSFLHIWAVVPCIKSFLIEIQCISRVYSIYVHTFCDPLFEAIGKIFSNIRISTQKEI | null | null | apoptotic signaling pathway [GO:0097190]; canonical Wnt signaling pathway [GO:0060070]; caveola assembly [GO:0070836]; caveolin-mediated endocytosis [GO:0072584]; cell differentiation [GO:0030154]; cellular response to exogenous dsRNA [GO:0071360]; cellular response to hyperoxia [GO:0071455]; cellular response to misfo... | caveola [GO:0005901]; endoplasmic reticulum [GO:0005783]; endosome [GO:0005768]; focal adhesion [GO:0005925]; Golgi membrane [GO:0000139]; membrane raft [GO:0045121]; perinuclear region of cytoplasm [GO:0048471]; protein-containing complex [GO:0032991]; sarcolemma [GO:0042383] | ATPase binding [GO:0051117]; identical protein binding [GO:0042802]; inward rectifier potassium channel inhibitor activity [GO:0070320]; molecular adaptor activity [GO:0060090]; nitric-oxide synthase binding [GO:0050998]; oxysterol binding [GO:0008142]; protein kinase binding [GO:0019901]; protein-containing complex bi... | PF01146; | null | Caveolin family | PTM: Phosphorylated at Tyr-14 by ABL1 in response to oxidative stress. {ECO:0000250|UniProtKB:Q03135}.; PTM: Ubiquitinated. Undergo monoubiquitination and multi- and/or polyubiquitination. Monoubiquitination of N-terminal lysines promotes integration in a ternary complex with UBXN6 and VCP which promotes oligomeric CAV... | SUBCELLULAR LOCATION: Golgi apparatus membrane {ECO:0000250}; Peripheral membrane protein {ECO:0000250}. Cell membrane {ECO:0000250}; Peripheral membrane protein {ECO:0000250}. Membrane, caveola {ECO:0000250|UniProtKB:P49817}; Peripheral membrane protein {ECO:0000250}. Membrane raft {ECO:0000250|UniProtKB:Q03135}. Note... | null | null | null | null | null | FUNCTION: May act as a scaffolding protein within caveolar membranes. Forms a stable heterooligomeric complex with CAV2 that targets to lipid rafts and drives caveolae formation. Mediates the recruitment of CAVIN proteins (CAVIN1/2/3/4) to the caveolae (By similarity). Interacts directly with G-protein alpha subunits a... | Echinops telfairi (Lesser hedgehog tenrec) |
A1X150 | MET_ECHTE | MKAPAALAPGILVLLLTLVQKGGGECREALAKSEMNVNMRYRLPNFTADTPIQNVVVHEGHVFLGAINSIYVLRERDLQQVSEYKTGPVWEHPDCLPCQACGLAGGQWRENVNMALLVETYYDDQLISCGSVHRGTCQRHVLPRDNPADIQAEVHCMHSPRADEDEASQCPDCVVSALGTKVLLAEKQRFVNFFVGNTLNGSSLPGHALHSISVRRIKETQDGFKFLTDKSYIDVLPEFQASYPIKYIHAFESNRFIYFLTVQRETLDSPSFHTRIIRFCSADSGLRSYMEMPLECILTEKRRKRALRSEVFNVLQAAYV... | 2.7.10.1 | null | phosphorylation [GO:0016310]; positive chemotaxis [GO:0050918]; positive regulation of endothelial cell chemotaxis [GO:2001028]; semaphorin-plexin signaling pathway [GO:0071526]; semaphorin-plexin signaling pathway involved in axon guidance [GO:1902287]; transmembrane receptor protein tyrosine kinase signaling pathway ... | membrane [GO:0016020]; semaphorin receptor complex [GO:0002116] | ATP binding [GO:0005524]; semaphorin receptor activity [GO:0017154]; transmembrane receptor protein tyrosine kinase activity [GO:0004714] | PF07714;PF01437;PF01403;PF01833; | 2.60.40.10;1.10.510.10;2.130.10.10; | Protein kinase superfamily, Tyr protein kinase family | PTM: Autophosphorylated in response to ligand binding on Tyr-1233 and Tyr-1234 in the kinase domain leading to further phosphorylation of Tyr-1348 and Tyr-1355 in the C-terminal multifunctional docking site. Dephosphorylated by PTPRJ at Tyr-1348 and Tyr-1364. Dephosphorylated by PTPN1 and PTPN2 (By similarity). {ECO:00... | SUBCELLULAR LOCATION: Membrane {ECO:0000250}; Single-pass type I membrane protein {ECO:0000250}. | CATALYTIC ACTIVITY: Reaction=ATP + L-tyrosyl-[protein] = ADP + H(+) + O-phospho-L-tyrosyl-[protein]; Xref=Rhea:RHEA:10596, Rhea:RHEA-COMP:10136, Rhea:RHEA-COMP:10137, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:46858, ChEBI:CHEBI:82620, ChEBI:CHEBI:456216; EC=2.7.10.1; Evidence={ECO:0000255|PROSITE-ProRule:PRU100... | null | null | null | null | FUNCTION: Receptor tyrosine kinase that transduces signals from the extracellular matrix into the cytoplasm by binding to hepatocyte growth factor/HGF ligand. Regulates many physiological processes including proliferation, scattering, morphogenesis and survival. Ligand binding at the cell surface induces autophosphoryl... | Echinops telfairi (Lesser hedgehog tenrec) |
A1X283 | SPD2B_HUMAN | MPPRRSIVEVKVLDVQKRRVPNKHYVYIIRVTWSSGSTEAIYRRYSKFFDLQMQMLDKFPMEGGQKDPKQRIIPFLPGKILFRRSHIRDVAVKRLIPIDEYCKALIQLPPYISQCDEVLQFFETRPEDLNPPKEEHIGKKKSGGDQTSVDPMVLEQYVVVANYQKQESSEISLSVGQVVDIIEKNESGWWFVSTAEEQGWVPATCLEGQDGVQDEFSLQPEEEEKYTVIYPYTARDQDEMNLERGAVVEVIQKNLEGWWKIRYQGKEGWAPASYLKKNSGEPLPPKPGPGSPSHPGALDLDGVSRQQNAVGREKELLSSQ... | null | null | adipose tissue development [GO:0060612]; bone development [GO:0060348]; cell differentiation [GO:0030154]; extracellular matrix disassembly [GO:0022617]; eye development [GO:0001654]; heart development [GO:0007507]; podosome assembly [GO:0071800]; protein localization to membrane [GO:0072657]; skeletal system developme... | anchoring junction [GO:0070161]; cell projection [GO:0042995]; cytoplasm [GO:0005737]; podosome [GO:0002102] | phosphatidylinositol-3,5-bisphosphate binding [GO:0080025]; phosphatidylinositol-3-phosphate binding [GO:0032266]; phosphatidylinositol-5-phosphate binding [GO:0010314]; SH2 domain binding [GO:0042169]; superoxide-generating NADPH oxidase activator activity [GO:0016176] | PF00787;PF00018;PF07653; | 3.30.1520.10;2.30.30.40; | SH3PXD2 family | PTM: Phosphorylated in SRC-transformed cells. {ECO:0000250}. | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Cell projection, podosome {ECO:0000250}. Note=Cytoplasmic in normal cells and localizes to podosomes in SRC-transformed cells. {ECO:0000250}. | null | null | null | null | null | FUNCTION: Adapter protein involved in invadopodia and podosome formation and extracellular matrix degradation. Binds matrix metalloproteinases (ADAMs), NADPH oxidases (NOXs) and phosphoinositides. Acts as an organizer protein that allows NOX1- or NOX3-dependent reactive oxygen species (ROS) generation and ROS localizat... | Homo sapiens (Human) |
A1XBS5 | CBAR1_HUMAN | MMRRTLENRNAQTKQLQTAVSNVEKHFGELCQIFAAYVRKTARLRDKADLLVNEINAYAATETPHLKLGLMNFADEFAKLQDYRQAEVERLEAKVVEPLKTYGTIVKMKRDDLKATLTARNREAKQLTQLERTRQRNPSDRHVISQAETELQRAAMDASRTSRHLEETINNFERQKMKDIKTIFSEFITIEMLFHGKALEVYTAAYQNIQNIDEDEDLEVFRNSLYAPDYSSRLDIVRANSKSPLQRSLSAKCVSGTGQVSTCRLRKDQQAEDDEDDELDVTEEENFLK | null | null | cilium assembly [GO:0060271]; inner mitochondrial membrane organization [GO:0007007]; limb morphogenesis [GO:0035108]; membrane organization [GO:0061024]; membrane tubulation [GO:0097749]; positive regulation of smoothened signaling pathway [GO:0045880] | centriole [GO:0005814]; ciliary basal body [GO:0036064]; ciliary base [GO:0097546]; ciliary transition zone [GO:0035869]; cytoplasm [GO:0005737]; mitochondrial crista [GO:0030061]; mitochondrial inner membrane [GO:0005743]; mitochondrion [GO:0005739]; nucleus [GO:0005634] | phospholipid binding [GO:0005543] | PF06730; | 1.20.1270.60; | CIBAR family | null | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:27528616, ECO:0000269|PubMed:30404948}. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome, centriole {ECO:0000269|PubMed:27528616}. Cytoplasm, cytoskeleton, cilium basal body {ECO:0000269|PubMed:27528616, ECO:0000269|PubMed:30395363}. Cell projection,... | null | null | null | null | null | FUNCTION: Acts as a positive regulator of ciliary hedgehog signaling (By similarity). Probable regulator of ciliogenesis involved in limb morphogenesis (PubMed:27528616, PubMed:30395363). In cooperation with CBY1 it is involved in the recruitment and fusion of endosomal vesicles at distal appendages during early stages... | Homo sapiens (Human) |
A1XGB4 | PIMP1_CAPAN | MTPPPTSTVPPYVSLIVRILTLICLLISFIVIATNNQTVSTVAGDVKIKFKDFYAYRYLIATVIIGMAYTLLQIAFSISLLTTGNRIGGEGFLLFDFYGDKFISYFLVTGAAASFGMTQDLKQLEGSDNYSKFLNTSNAAASLCLIGFFFAVASSIFSSYNLPKRI | null | null | defense response to bacterium [GO:0042742]; defense response to oomycetes [GO:0002229]; response to abscisic acid [GO:0009737]; response to bacterium [GO:0009617]; response to cold [GO:0009409]; response to ethylene [GO:0009723]; response to jasmonic acid [GO:0009753]; response to salt stress [GO:0009651]; response to ... | plasma membrane [GO:0005886] | null | PF04535; | null | Casparian strip membrane proteins (CASP) family | null | SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:18506481}; Multi-pass membrane protein {ECO:0000269|PubMed:18506481}. | null | null | null | null | null | FUNCTION: Required for defense response to Xanthomonas campestris pv. vesicatoria (Xcv). In heterologous systems, confers resistance to bacterial pathogens such as Pseudomonas syringae pv. tomato but susceptibility to pathogenic oomycetes such as Hylaloperonospora parasitica when expressed in Arabidopsis thaliana. May ... | Capsicum annuum (Capsicum pepper) |
A1XLE2 | TFP_LEPSV | MALTLQGEWIKIEQKGGPAPGPRSSHCMAVVGDKLYMFGGELKPQFHLDKHLYVFDFKTNTWSIAEPKGEAPSLSCLGVRMVAVGTKIYIFGGRDENRNYSDFYSYDTVKKEWKFLTKLDEERVPEARSFPAIAADDNHVYIFGGVSKGGVQSTPFRFKSTIVYNIAEGTWSQLPNPGPDFEPRGGAGLAVIDKKLWVVCGFANSTSGGINDYNSNKVQYYDLVSGKWIEVKTSGVKPSGRSVFAYAVIGKQIVIYGGEIFRDENGHLGPGTMSNEGYALDTETLVWEKLVDGGEPMTPLGWTANCTGTVYGKTGLLMHG... | 4.8.1.7; 4.8.1.8 | COFACTOR: Name=Fe(2+); Xref=ChEBI:CHEBI:29033; Evidence={ECO:0000269|PubMed:17139450}; | glucosinolate metabolic process [GO:0019760]; nitrile biosynthetic process [GO:0080028]; thiocyanate metabolic process [GO:0018969] | cytosol [GO:0005829]; nucleus [GO:0005634] | enzyme regulator activity [GO:0030234]; lyase activity [GO:0016829]; metal ion binding [GO:0046872] | PF01344;PF13418;PF13964; | 2.120.10.80; | null | null | null | CATALYTIC ACTIVITY: Reaction=(Z)-phenyl-N-(sulfonatooxy)methanimidothioate = benzyl thiocyanate + sulfate; Xref=Rhea:RHEA:69312, ChEBI:CHEBI:16017, ChEBI:CHEBI:16189, ChEBI:CHEBI:183061; EC=4.8.1.7; Evidence={ECO:0000269|PubMed:17139450}; CATALYTIC ACTIVITY: Reaction=(Z)-phenyl-N-(sulfonatooxy)methanimidothioate = phen... | null | null | BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 9.5. {ECO:0000269|PubMed:17139450}; | null | FUNCTION: Specifier protein that contributes to constitutive and herbivore-induced simple nitrile formation (By similarity). Catalyzes thiocyanate and simple nitrile formation from benzylglucosinolate in the presence of myrosinase (PubMed:17139450, PubMed:23999604). Converts also aliphatic glucosinolates to both epithi... | Lepidium sativum (Garden cress) |
A1XRN2 | PLIA_ATRNM | MRLILLSGLLLLGTFLANGDEKDSDVQMLNSMIEAVMILQRDFANLRHALMTVHNARSFGRGSERLYVTNKEVSKFEGLEEICSQAGGHIPSPQLENQNKAFEDVLERHNKAAYLVVGDSANFTNWAAGQPNEADGTCVKADTHGSWHSASCDDNLLVVCEFYFIL | null | null | null | extracellular region [GO:0005576] | carbohydrate binding [GO:0030246]; phospholipase A2 inhibitor activity [GO:0019834] | PF00059; | 3.10.100.10; | Alpha-type phospholipase A2 inhibitor family | PTM: N-glycosylated. {ECO:0000269|PubMed:17071122}. | SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:17071122}. Note=Secreted in plasma. {ECO:0000269|PubMed:17071122}. | null | null | null | null | null | FUNCTION: This phospholipase A2 inhibitor neutralizes the activity of basic PLA2 myotoxins of its own and related venoms. The inhibitory profile shows specificity towards group II PLA2, either belonging to the catalytically-active (D49) or -inactive (K49) subtypes. | Atropoides nummifer (Jumping pit viper) (Porthidium nummifer) |
A1XSY8 | EGR2_PIG | MMTAKAVDKIPVTLSGFVHQLSDNIYPVEDLAATSVTIFPNAELGSPFDQMNGVAGDGMINIDMTGEKRSLDLPYPSSFAPVSAPRNQTFTYMGKFSIDPQYPGASCYPEGIINIVSAGILQGVTSPASTTASSNVTSASPNPLATGPLGVCTMSQTQPDLDHLYSPPPPPPYSGCAGDLYQDPSAFLSAATTSTSSSLAYPPPPSYPSPKPATDPGLFPMIPDYPGFFPSQCQRDLHGTAGPDRKPFPCPLDSLRVPPPLTPLSTIRNFTLGGPSAGTTGPGASGGSEGPRLPGSSAAAAAAAYNPHHLPLRPILRPRK... | 2.3.2.- | null | facial nerve structural organization [GO:0021612]; positive regulation of DNA-templated transcription [GO:0045893]; positive regulation of myelination [GO:0031643]; positive regulation of Schwann cell differentiation [GO:0014040]; positive regulation of transcription by RNA polymerase II [GO:0045944]; protein export fr... | cytoplasm [GO:0005737]; nucleus [GO:0005634] | chromatin binding [GO:0003682]; DNA-binding transcription factor activity [GO:0003700]; DNA-binding transcription factor activity, RNA polymerase II-specific [GO:0000981]; metal ion binding [GO:0046872]; RNA polymerase II cis-regulatory region sequence-specific DNA binding [GO:0000978]; sequence-specific DNA binding [G... | PF11928;PF00096; | 3.30.160.60; | EGR C2H2-type zinc-finger protein family | PTM: Ubiquitinated by WWP2 leading to proteasomal degradation. {ECO:0000250|UniProtKB:P08152}.; PTM: Acetylated at Lys-246. May be deacetylated by HDAC6, HDAC10 or SIRT1. {ECO:0000250|UniProtKB:P08152}. | SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:P08152}. | null | null | PATHWAY: Protein modification; protein sumoylation. | null | null | FUNCTION: Sequence-specific DNA-binding transcription factor (By similarity). Plays a role in hindbrain segmentation by regulating the expression of a subset of homeobox containing genes and in Schwann cell myelination by regulating the expression of genes involved in the formation and maintenance of myelin (By similar... | Sus scrofa (Pig) |
A1XWY7 | CFAT_PETHY | MGNTDFHVTVKKKEVVAAVLPMHHEHWLPMSNLDLLLPPLDFGVFFCYKRSKINNDTKDDDETIKKALAETLVSFYALAGEVVFNSLGEPELLCNNRGVDFFHAYADIELNNLDLYHPDVSVHEKLIPIKKHGVLSVQVTGLKCGGIVVGCTFDHRVADAYSANMFLVAWAAIARKDNNINTVIPSFRRSLLNPRRPPQFDDSFIDSTYVFLSSPPKQPNDVLTSRVYYINSQEINLLQSQATRNGSKRSKLECFSAFLWKTIAEGGIDDSKRCKLGIVVDGRQRLRHDSSTTMKNYFGNVLSVPYTEASVGQLKQTPLG... | 2.3.1.-; 2.3.1.224 | null | circadian rhythm [GO:0007623]; green leaf volatile biosynthetic process [GO:0010597]; phenylpropanoid biosynthetic process [GO:0009699]; response to ethylene [GO:0009723] | null | 2-phenylethanol acetyltransferase activity [GO:0102387]; acetyl-coenzyme A:acetyl alcohol acetyltransferase activity [GO:0102720]; alcohol O-acyltransferase activity [GO:0034318] | PF02458; | 3.30.559.10; | Plant acyltransferase family | null | null | CATALYTIC ACTIVITY: Reaction=(E)-coniferol + acetyl-CoA = (E)-coniferyl acetate + CoA; Xref=Rhea:RHEA:64616, ChEBI:CHEBI:17745, ChEBI:CHEBI:47905, ChEBI:CHEBI:57287, ChEBI:CHEBI:57288; Evidence={ECO:0000269|PubMed:17241449}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:64617; Evidence={ECO:0000269|PubMed:172414... | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=56.5 uM for coniferyl alcohol (in the presence of acetyl CoA and at pH 6) {ECO:0000269|PubMed:17241449}; KM=30.6 uM for acetyl CoA (in the presence of coniferyl alcohol and at pH 6) {ECO:0000269|PubMed:17241449}; KM=27.5 uM for coniferyl alcohol (in the presence of... | PATHWAY: Aromatic compound metabolism; phenylpropanoid biosynthesis. {ECO:0000269|PubMed:17241449}. | BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 6. Larger substrate spectrum at pH 7.5, with a lower activity, thought. {ECO:0000269|PubMed:17241449}; | null | FUNCTION: Acyltransferase involved in the biosynthesis of the floral volatile isoeugenol, and which promotes the formation of phenylacetaldehyde, phenylethyl alcohol, phenyl-ethyl acetate, phenylethyl benzoate and benzyl acetate (PubMed:17241449). Catalyzes the acetylation of coniferyl alcohol to produce coniferyl acet... | Petunia hybrida (Petunia) |
A1Y2K1 | FYN_PIG | MGCVQCKDKEATKLTEERDGSLNQSSGFRYGTDPTPQHYPSFGVTSIPNYNNFHAAGGQGLTVFGGVSSSSHTGTLRTRGGTGVTLFVALYDYEARTEDDLSFHKGEKFQILNSSEGDWWEARSLTTGETGYIPSNYVAPVDSIQAEEWYFGKLGRKDAERQLLSFGNPRGTFLIRESETTKGAYSLSIRDWDDMKGDHVKHYKIRKLDNGGYYITTRAQFETLQQLVQHYSERAAGLCCRLVVPCHKGMPRLTDLSVKTKDVWEIPRESLQLIKRLGNGQFGEVWMGTWNGNTKVAIKTLKPGTMSPESFLEEAQIMKK... | 2.7.10.2 | COFACTOR: Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000250|UniProtKB:P06241}; | adaptive immune response [GO:0002250]; cell differentiation [GO:0030154]; innate immune response [GO:0045087]; peptidyl-tyrosine phosphorylation [GO:0018108]; T cell receptor signaling pathway [GO:0050852]; transmembrane receptor protein tyrosine kinase signaling pathway [GO:0007169] | cytoplasm [GO:0005737]; extrinsic component of cytoplasmic side of plasma membrane [GO:0031234]; nucleus [GO:0005634]; perikaryon [GO:0043204] | ATP binding [GO:0005524]; metal ion binding [GO:0046872]; non-membrane spanning protein tyrosine kinase activity [GO:0004715]; protein tyrosine kinase activity [GO:0004713]; signaling receptor binding [GO:0005102] | PF07714;PF00017;PF00018; | 3.30.505.10;2.30.30.40;1.10.510.10; | Protein kinase superfamily, Tyr protein kinase family, SRC subfamily | PTM: Autophosphorylated at Tyr-420 (By similarity). Phosphorylation on the C-terminal tail at Tyr-531 by CSK maintains the enzyme in an inactive state. PTPRC/CD45 dephosphorylates Tyr-531 leading to activation. Ultraviolet B (UVB) strongly increase phosphorylation at Thr-12 and kinase activity, and promotes translocati... | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:P06241}. Nucleus {ECO:0000250|UniProtKB:P06241}. Cell membrane {ECO:0000250|UniProtKB:P06241}. Perikaryon {ECO:0000250|UniProtKB:Q62844}. Note=Present and active in lipid rafts (By similarity). Palmitoylation is crucial for proper trafficking (By similarity). {ECO:... | CATALYTIC ACTIVITY: Reaction=ATP + L-tyrosyl-[protein] = ADP + H(+) + O-phospho-L-tyrosyl-[protein]; Xref=Rhea:RHEA:10596, Rhea:RHEA-COMP:10136, Rhea:RHEA-COMP:10137, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:46858, ChEBI:CHEBI:82620, ChEBI:CHEBI:456216; EC=2.7.10.2; Evidence={ECO:0000250|UniProtKB:P06241, ECO:... | null | null | null | null | FUNCTION: Non-receptor tyrosine-protein kinase that plays a role in many biological processes including regulation of cell growth and survival, cell adhesion, integrin-mediated signaling, cytoskeletal remodeling, cell motility, immune response and axon guidance. Inactive FYN is phosphorylated on its C-terminal tail wit... | Sus scrofa (Pig) |
A1Y9I9 | TOMT_MOUSE | MSPAIALAFLPLVVTLLVRYRHHFRLLVRTVLLRGFRDCLSGLRIEERAFSYVLTHALPGDPGHILTTLDHWSSCCEYLSHMGPVKGQILMRLVEEKAPACVLELGTYCGYSTLLIARALPPGSRLLTVERDSRTAAVAEKVIRLAGFDEQMVELIAGSSEEVIPRLRAQHQLNRADLVLLAHRPRYYLRDLQLLEAHALLPHGATVLADHVLFPGAPRFLQYTKSCGRYRCRLHHTSLPDFPAIKDGIAQLTYTGPG | 2.1.1.6 | null | auditory receptor cell development [GO:0060117]; catecholamine catabolic process [GO:0042424]; developmental process [GO:0032502]; dopamine metabolic process [GO:0042417]; methylation [GO:0032259]; positive regulation of protein import [GO:1904591]; sensory perception of sound [GO:0007605] | apical part of cell [GO:0045177]; cytoplasm [GO:0005737]; endoplasmic reticulum [GO:0005783] | catechol O-methyltransferase activity [GO:0016206]; L-dopa O-methyltransferase activity [GO:0102084]; orcinol O-methyltransferase activity [GO:0102938] | PF01596; | 3.40.50.150; | Class I-like SAM-binding methyltransferase superfamily, Cation-dependent O-methyltransferase family | null | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:18953341, ECO:0000269|PubMed:28504928}. Endoplasmic reticulum {ECO:0000269|PubMed:28504928}. Note=Localized to the cell body of the cochlear hair cells, but is not present in the stereocilia. Present but not restricted to the apical cistern, Hensen's body and the subs... | CATALYTIC ACTIVITY: Reaction=a catechol + S-adenosyl-L-methionine = a guaiacol + H(+) + S-adenosyl-L-homocysteine; Xref=Rhea:RHEA:17877, ChEBI:CHEBI:15378, ChEBI:CHEBI:33566, ChEBI:CHEBI:57856, ChEBI:CHEBI:59789, ChEBI:CHEBI:134251; EC=2.1.1.6; Evidence={ECO:0000269|PubMed:18794526}; PhysiologicalDirection=left-to-righ... | null | null | null | null | FUNCTION: Catalyzes the O-methylation, and thereby the inactivation, of catecholamine neurotransmitters and catechol hormones (PubMed:18794526). Required for auditory function (PubMed:18794526, PubMed:28504928). Component of the cochlear hair cell's mechanotransduction (MET) machinery. Involved in the assembly of the a... | Mus musculus (Mouse) |
A1YB07 | AMOL2_DANRE | MRTAEESSGTVLHRLIQEQLRYGNPTDPTLLAIQQQALRGGSSGGGAGSPRSSLESLTQEESLSPQLSARQEPQGQEHQGDFQHSESPVCHLYQLHTEELPTYEEAKAHSQYLAYQRGQIGLHQGSLESPGGVGGAEQDDSMWDAKREHARSLSERLLQLSLERNCAHDNIPMSSSHSYPQLSNNHSDTVVNEQSVHQPDQRGPPPEYPFMVRSPGYMLSHSQEHGHYYNEPPPAFHSQHYRLFPTQPQAPRHNGLPTLTPAGQDVNVGGYSIPANNFQMEQLIKENERLKREVDSYSEKAARLQKLEQEIQRISEAYET... | null | null | actin cytoskeleton organization [GO:0030036]; angiogenesis [GO:0001525]; cell migration [GO:0016477]; convergent extension [GO:0060026]; cortical actin cytoskeleton organization [GO:0030866]; dorsal aorta development [GO:0035907]; dorsal aorta morphogenesis [GO:0035912]; embryonic pattern specification [GO:0009880]; en... | bicellular tight junction [GO:0005923]; cell cortex [GO:0005938]; cell junction [GO:0030054]; cell-cell junction [GO:0005911]; cytoplasmic vesicle [GO:0031410]; plasma membrane [GO:0005886]; polymeric cytoskeletal fiber [GO:0099513]; recycling endosome [GO:0055037] | null | PF12240; | null | Angiomotin family | PTM: Phosphorylation at Tyr-103 is necessary for efficient binding to SRC and synergistically functioning with SRC to activate the downstream MAPK pathway. {ECO:0000269|PubMed:21937427}. | SUBCELLULAR LOCATION: Recycling endosome {ECO:0000269|PubMed:22362771}. | null | null | null | null | null | FUNCTION: Regulates the translocation of phosphorylated SRC to peripheral cell-matrix adhesion sites. Required for proper architecture of actin filaments and for cell movements during embryogenesis. Inhibits the Wnt/beta-catenin signaling pathway, probably by recruiting CTNNB1 to recycling endosomes and hence preventin... | Danio rerio (Zebrafish) (Brachydanio rerio) |
A1YER0 | SIX1_GORGO | MSMLPSFGFTQEQVACVCEVLQQGGNLERLGRFLWSLPACDHLHKNESVLKAKAVVAFHRGNFRELYKILESHQFSPHNHPKLQQLWLKAHYVEAEKLRGRPLGAVGKYRVRRKFPLPRTIWDGEETSYCFKEKSRGVLREWYAHNPYPSPREKRELAEATGLTTTQVSNWFKNRRQRDRAAEAKERENTENNNSSSNKQNQLSPLEGGKPLMSSSEEEFSPPQSPDQNSVLLLQGNMGHARSSNYSLPGLTASQPSHGLQTHQHQLQDSLLGPLTSSLVDLGS | null | null | aorta morphogenesis [GO:0035909]; apoptotic process [GO:0006915]; branching involved in ureteric bud morphogenesis [GO:0001658]; cochlea morphogenesis [GO:0090103]; embryonic cranial skeleton morphogenesis [GO:0048701]; embryonic skeletal system morphogenesis [GO:0048704]; endothelin receptor signaling pathway [GO:0086... | cytoplasm [GO:0005737]; nucleolus [GO:0005730]; nucleoplasm [GO:0005654]; nucleus [GO:0005634]; transcription regulator complex [GO:0005667] | chromatin binding [GO:0003682]; DNA-binding transcription activator activity, RNA polymerase II-specific [GO:0001228]; DNA-binding transcription factor activity [GO:0003700]; DNA-binding transcription factor activity, RNA polymerase II-specific [GO:0000981]; RNA polymerase II cis-regulatory region sequence-specific DNA... | PF05920;PF16878; | 1.10.10.60; | SIX/Sine oculis homeobox family | PTM: Phosphorylated during interphase; becomes hyperphosphorylated during mitosis. Hyperphosphorylation impairs binding to promoter elements (By similarity). {ECO:0000250}.; PTM: Ubiquitinated by the anaphase promoting complex (APC), leading to its proteasomal degradation. {ECO:0000250}. | SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00108}. Cytoplasm {ECO:0000250}. | null | null | null | null | null | FUNCTION: Transcription factor that is involved in the regulation of cell proliferation, apoptosis and embryonic development (By similarity). Plays an important role in the development of several organs, including kidney, muscle and inner ear (By similarity). Depending on context, functions as a transcriptional repress... | Gorilla gorilla gorilla (Western lowland gorilla) |
A1YES6 | APEX1_GORGO | MPKRGKKGAVAEDGDELKTEPEAKKSKTAAKKNDKEAAGEGPALYEDPPDQKTSPSGKPATLKICSWNVDGLRAWIKKKGLDWVKEEAPDILCLQETKCSENKLPAELQELPGLSYQYWSAPXXKEGYSGVGLLSRQCPLKVSYGIGEEEHDQEGRVIVAEFDSFVLVTAYVPNAGRGLVRLEYRQRWDEAFRRFLKGLASRKPLVLCGDLNVAHEEIDLRNPKGNKKNAGFTPQERQGFGELLQAVPLADSFRHLYPNTPYAYTFWTYMMNARSKNVGWRLDYFLLSHSLLPALCDSKIRSKALGSDHCPITLYLAL | 3.1.11.2; 3.1.21.- | COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250|UniProtKB:P27695}; Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000250|UniProtKB:P27695}; Note=Probably binds two magnesium or manganese ions per subunit. {ECO:0000250|UniProtKB:P27695}; | base-excision repair [GO:0006284]; DNA recombination [GO:0006310]; DNA repair [GO:0006281]; positive regulation of gene expression via CpG island demethylation [GO:0044029]; regulation of apoptotic process [GO:0042981]; regulation of mRNA stability [GO:0043488] | cytoplasm [GO:0005737]; endoplasmic reticulum [GO:0005783]; mitochondrion [GO:0005739]; nuclear speck [GO:0016607]; nucleolus [GO:0005730]; nucleoplasm [GO:0005654]; nucleus [GO:0005634] | 3'-5' exonuclease activity [GO:0008408]; chromatin DNA binding [GO:0031490]; class II DNA-(apurinic or apyrimidinic site) endonuclease activity [GO:0052720]; damaged DNA binding [GO:0003684]; DNA-(abasic site) binding [GO:0140431]; DNA-(apurinic or apyrimidinic site) endonuclease activity [GO:0003906]; double-stranded ... | PF03372; | 3.60.10.10; | DNA repair enzymes AP/ExoA family | PTM: Phosphorylated. Phosphorylation by kinase PKC or casein kinase CK2 results in enhanced redox activity that stimulates binding of the FOS/JUN AP-1 complex to its cognate binding site. AP-endodeoxyribonuclease activity is not affected by CK2-mediated phosphorylation. Phosphorylation of Thr-233 by CDK5 in response to... | SUBCELLULAR LOCATION: Nucleus. Nucleus, nucleolus {ECO:0000250}. Nucleus speckle {ECO:0000255|PROSITE-ProRule:PRU00764}. Endoplasmic reticulum {ECO:0000250}. Cytoplasm {ECO:0000255|PROSITE-ProRule:PRU00764}. Note=Detected in the cytoplasm of B-cells stimulated to switch. Colocalized with SIRT1 in the nucleus. Colocaliz... | CATALYTIC ACTIVITY: Reaction=Exonucleolytic cleavage in the 3'- to 5'-direction to yield nucleoside 5'-phosphates.; EC=3.1.11.2; Evidence={ECO:0000250|UniProtKB:P27695}; | null | null | null | null | FUNCTION: Multifunctional protein that plays a central role in the cellular response to oxidative stress. The two major activities of APEX1 are DNA repair and redox regulation of transcriptional factors. Functions as an apurinic/apyrimidinic (AP) endodeoxyribonuclease in the DNA base excision repair (BER) pathway of DN... | Gorilla gorilla gorilla (Western lowland gorilla) |
A1YF08 | PDX1_GORGO | MNGEEQYYAATQLYKDPCAFQRGPAPEFSASPPACLYMGRQPPPPPPPHPFPGALGALEQGSPPDISPYEVPPLADDPAVAHLHHHLPAQLALPHPPAGPFPEGAEPGVLEEPNRVQLPFPWMKSTKAHAWKGQWAGGAYAAEPEENKRTRTAYTRAQLLELEKEFLFNKYISRPRRVELAVMLNLTERHIKIWFQNRRMKWKKEEDKKRGGGTAVGGGGVAEPEQDCAVTSGEELLALPPPPPPGGAVPPAAPVAAREGRLPPGLSASPQPSSVAPRRPQEPR | null | null | digestive tract development [GO:0048565]; exocrine pancreas development [GO:0031017]; glucose homeostasis [GO:0042593]; glucose metabolic process [GO:0006006]; insulin secretion [GO:0030073]; intrinsic apoptotic signaling pathway in response to endoplasmic reticulum stress [GO:0070059]; liver development [GO:0001889]; ... | cytosol [GO:0005829]; nuclear speck [GO:0016607]; nucleus [GO:0005634] | chromatin binding [GO:0003682]; DNA-binding transcription factor activity, RNA polymerase II-specific [GO:0000981]; RNA polymerase II cis-regulatory region sequence-specific DNA binding [GO:0000978] | PF00046; | 1.10.10.60; | Antp homeobox family, IPF1/XlHbox-8 subfamily | PTM: Phosphorylated by the SAPK2 pathway at high intracellular glucose concentration. Phosphorylated by HIPK2 on Ser-269 upon glucose accumulation. This phosphorylation mediates subnuclear localization shifting. Phosphorylation by PASK may lead to translocation into the cytosol (By similarity). {ECO:0000250}. | SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00108}. Cytoplasm, cytosol {ECO:0000250}. | null | null | null | null | null | FUNCTION: Activates insulin and somatostatin gene transcription. Key regulator of islet peptide hormone expression but also responsible for the development of the pancreas, most probably by determining maturation and differentiation of common pancreatic precursor cells in the developing gut. Binds the DNA sequence 5'-C... | Gorilla gorilla gorilla (Western lowland gorilla) |
A1YFA7 | PQBP1_GORGO | MPLPVALQTRLAKRGILKHLEPEPEEEIIAEDYDDDPVDYEATRLEGLPPSWYKVFDPSCGLPYYWNADTDLVSWLSPHDPNSVVTKSAKKLRSSNADAEEKLDRSHDKSDRGHDKSDRSHEKLDRGHDKSDRGHDKSDRDRERGYDKVDRERERDRERDRDRGYDKADREEGKERRHHRREELAPYPKSKKAVSRKDEELDPMDPSSYSDAPRGTWSTGLPKRNEAKTGADTTAAGPLFQQRPYPSPGAVLRANAEASRTKQQD | null | null | activation of innate immune response [GO:0002218]; alternative mRNA splicing, via spliceosome [GO:0000380]; cellular response to exogenous dsRNA [GO:0071360]; defense response to virus [GO:0051607]; innate immune response [GO:0045087]; neuron projection development [GO:0031175]; positive regulation of defense response ... | cytoplasm [GO:0005737]; cytoplasmic stress granule [GO:0010494]; cytosol [GO:0005829]; neuronal ribonucleoprotein granule [GO:0071598]; nuclear body [GO:0016604]; nuclear speck [GO:0016607]; plasma membrane [GO:0005886] | double-stranded DNA binding [GO:0003690]; lipid binding [GO:0008289]; ribonucleoprotein complex binding [GO:0043021] | null | 2.20.70.10;3.40.30.10; | null | null | SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:O60828}. Nucleus speckle {ECO:0000250|UniProtKB:Q91VJ5}. Cytoplasmic granule {ECO:0000250|UniProtKB:O60828}. Note=Colocalizes with SRSF2 in nuclear speckles (By similarity). Colocalized with POU3F2. Colocalized with ATXN1 in nuclear inclusion bodies. Localizes to cyt... | null | null | null | null | null | FUNCTION: Intrinsically disordered protein that acts as a scaffold, and which is involved in different processes, such as pre-mRNA splicing, transcription regulation, innate immunity and neuron development. Interacts with splicing-related factors via the intrinsically disordered region and regulates alternative splicin... | Gorilla gorilla gorilla (Western lowland gorilla) |
A1YFZ3 | APEX1_PANPA | MPKRGKKGAVAEDGDELRTEPEAKKSKTAAKKNDKEAAGEGPALYEDPPDQKTSPSGKPATLKICSWNVDGLRAWIKKKGLDWVKEEAPDILCLQETKCSENKLPAELQELPGLSHQYWSAPSDKEGYSGVGLLSRQCPLKVSYGIGEEEHDQEGRVIVAEFDSFVLVTAYVPNAGRGLVRLEYRQRWDEAFRKFLKGLASRKPLVLCGDLNVAHEEIDLRNPKGNKKNAGFTPQERQGFGELLQAVPLADSFRHLYPNTPYAYTFWTYMMNARSKNVGWRLDYFLLSHSLLPALCDSKIRSKALGSDHCPITLYLAL | 3.1.11.2; 3.1.21.- | COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250|UniProtKB:P27695}; Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000250|UniProtKB:P27695}; Note=Probably binds two magnesium or manganese ions per subunit. {ECO:0000250|UniProtKB:P27695}; | base-excision repair [GO:0006284]; DNA recombination [GO:0006310]; DNA repair [GO:0006281]; positive regulation of gene expression via CpG island demethylation [GO:0044029]; regulation of apoptotic process [GO:0042981]; regulation of mRNA stability [GO:0043488] | cytoplasm [GO:0005737]; endoplasmic reticulum [GO:0005783]; mitochondrion [GO:0005739]; nuclear speck [GO:0016607]; nucleolus [GO:0005730]; nucleoplasm [GO:0005654]; nucleus [GO:0005634] | 3'-5' exonuclease activity [GO:0008408]; chromatin DNA binding [GO:0031490]; class II DNA-(apurinic or apyrimidinic site) endonuclease activity [GO:0052720]; damaged DNA binding [GO:0003684]; DNA-(abasic site) binding [GO:0140431]; DNA-(apurinic or apyrimidinic site) endonuclease activity [GO:0003906]; double-stranded ... | PF03372; | 3.60.10.10; | DNA repair enzymes AP/ExoA family | PTM: Phosphorylated. Phosphorylation by kinase PKC or casein kinase CK2 results in enhanced redox activity that stimulates binding of the FOS/JUN AP-1 complex to its cognate binding site. AP-endodeoxyribonuclease activity is not affected by CK2-mediated phosphorylation. Phosphorylation of Thr-233 by CDK5 in response to... | SUBCELLULAR LOCATION: Nucleus. Nucleus, nucleolus {ECO:0000250}. Nucleus speckle {ECO:0000255|PROSITE-ProRule:PRU00764}. Endoplasmic reticulum {ECO:0000250}. Cytoplasm {ECO:0000255|PROSITE-ProRule:PRU00764}. Note=Detected in the cytoplasm of B-cells stimulated to switch. Colocalized with SIRT1 in the nucleus. Colocaliz... | CATALYTIC ACTIVITY: Reaction=Exonucleolytic cleavage in the 3'- to 5'-direction to yield nucleoside 5'-phosphates.; EC=3.1.11.2; Evidence={ECO:0000250|UniProtKB:P27695}; | null | null | null | null | FUNCTION: Multifunctional protein that plays a central role in the cellular response to oxidative stress. The two major activities of APEX1 are DNA repair and redox regulation of transcriptional factors. Functions as an apurinic/apyrimidinic (AP) endodeoxyribonuclease in the DNA base excision repair (BER) pathway of DN... | Pan paniscus (Pygmy chimpanzee) (Bonobo) |
A1YG22 | MYC_PANPA | MPLNVSFTNRNYDLDYDSVQPYFYCDEEENFYQQQQQSELQPPAPSEDIWKKFELLPTPPLSPSRRSGLCSPSYVAVTPFSLRGDNDGGGGSFSTADQLEMVTELLGGDMVNQSFICDPDDETFIKNIIIQDCMWSGFSAAAKLVSEKLASYQAARKDSGSPNPARGHSVCSTSSLYLQDLSAAASECIDPSVVFPYPLNDGSSPKSCPSQDSSAFSPSSDSLLSSTESSPQGSPEPLVLHEETPPTTSSDSEEEQEDEEEIDVVSVEKRQAPGKRSESGSPSAGGHSKPPHSPLVLKRCHVSTHQHNYAAPPSTRKDYP... | null | null | chromatin remodeling [GO:0006338]; chromosome organization [GO:0051276]; DNA damage response [GO:0006974]; G1/S transition of mitotic cell cycle [GO:0000082]; intracellular iron ion homeostasis [GO:0006879]; MAPK cascade [GO:0000165]; negative regulation of apoptotic process [GO:0043066]; negative regulation of cell di... | cytoplasm [GO:0005737]; nucleolus [GO:0005730]; nucleoplasm [GO:0005654]; nucleus [GO:0005634] | DNA binding [GO:0003677]; DNA-binding transcription factor activity, RNA polymerase II-specific [GO:0000981]; E-box binding [GO:0070888]; protein dimerization activity [GO:0046983]; protein-containing complex binding [GO:0044877] | PF00010;PF02344;PF01056; | 4.10.280.10; | null | PTM: Phosphorylated by PRKDC (By similarity). Phosphorylation at Ser-329 by PIM2 leads to the stabilization of MYC (By similarity). Phosphorylation at Ser-62 by CDK2 prevents Ras-induced senescence. Phosphorylated at Ser-62 by DYRK2; this primes the protein for subsequent phosphorylation by GSK3B at Thr-58. Phosphoryla... | SUBCELLULAR LOCATION: Nucleus, nucleoplasm {ECO:0000250|UniProtKB:P01106}. Nucleus, nucleolus {ECO:0000250|UniProtKB:P01106}. Nucleus {ECO:0000250|UniProtKB:P01106}. Cytoplasm {ECO:0000250|UniProtKB:P01106}. | null | null | null | null | null | FUNCTION: Transcription factor that binds DNA in a non-specific manner, yet also specifically recognizes the core sequence 5'-CAC[GA]TG-3'. Activates the transcription of growth-related genes. Binds to the VEGFA promoter, promoting VEGFA production and subsequent sprouting angiogenesis. Regulator of somatic reprogrammi... | Pan paniscus (Pygmy chimpanzee) (Bonobo) |
A1YG32 | S38A2_PANPA | MKKAEMGRFNISPDEDSSSYSSNSDFNYSYPTKQAALKSHYADVDPENQNFLLESNLGKKKYETEFHPGTTSFGMSVFNLSNAIVGSGILGLSYAMANTGIALFIILLTFVSIFSLYSVHLLLKTANEGGSLLYEQLGYKAFGLVGKLAASGSITMQNIGAMSSYLFIVKYELPLVIQALTNIEDKTGLWYLNGNYLVLLVSLVVILPLSLFRNLGYLGYTSGLSLLCMVFFLIVVICKKFQVPCPVEAALIINETINTTLTQPTALVPALSHNVTENDSCRPHYFIFNSQTVYAVPILIFSFVCHPAVLPIYEELKDRS... | null | null | alanine transport [GO:0032328]; amino acid import [GO:0043090]; amino acid transport [GO:0006865]; L-glutamine import across plasma membrane [GO:1903803]; L-proline import across plasma membrane [GO:1904271]; L-serine import across plasma membrane [GO:1903812]; neutral amino acid transport [GO:0015804]; proline transpo... | plasma membrane [GO:0005886] | acidic amino acid transmembrane transporter activity [GO:0015172]; alanine:sodium symporter activity [GO:0015655]; amino acid transmembrane transporter activity [GO:0015171]; amino acid:sodium symporter activity [GO:0005283]; L-glutamine transmembrane transporter activity [GO:0015186]; neutral L-amino acid transmembran... | PF01490; | null | Amino acid/polyamine transporter 2 family | PTM: Polyubiquitination by NEDD4L regulates the degradation and the activity of SLC38A2. {ECO:0000250|UniProtKB:Q8CFE6}. | SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:Q9JHE5}; Multi-pass membrane protein {ECO:0000250|UniProtKB:Q9JHE5}. Note=Insulin promotes recruitment to the plasma membrane from a pool localized in the trans-Golgi network or endosomes. Enriched in the somatodendritic compartment of neurons, it is also detec... | CATALYTIC ACTIVITY: Reaction=L-alanine(in) + Na(+)(in) = L-alanine(out) + Na(+)(out); Xref=Rhea:RHEA:29283, ChEBI:CHEBI:29101, ChEBI:CHEBI:57972; Evidence={ECO:0000250|UniProtKB:Q9JHE5}; PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:29285; Evidence={ECO:0000250|UniProtKB:Q9JHE5}; CATALYTIC ACTIVITY: Reaction=gly... | null | null | null | null | FUNCTION: Symporter that cotransports neutral amino acids and sodium ions from the extracellular to the intracellular side of the cell membrane. The transport is pH-sensitive, Li(+)-intolerant, electrogenic, driven by the Na(+) electrochemical gradient and cotransports of neutral amino acids and sodium ions with a stoi... | Pan paniscus (Pygmy chimpanzee) (Bonobo) |
A1YKT1 | TCP18_ARATH | MNNNIFSTTTTINDDYMLFPYNDHYSSQPLLPFSPSSSINDILIHSTSNTSNNHLDHHHQFQQPSPFSHFEFAPDCALLTSFHPENNGHDDNQTIPNDNHHPSLHFPLNNTIVEQPTEPSETINLIEDSQRISTSQDPKMKKAKKPSRTDRHSKIKTAKGTRDRRMRLSLDVAKELFGLQDMLGFDKASKTVEWLLTQAKPEIIKIATTLSHHGCFSSGDESHIRPVLGSMDTSSDLCELASMWTVDDRGSNTNTTETRGNKVDGRSMRGKRKRPEPRTPILKKLSKEERAKARERAKGRTMEKMMMKMKGRSQLVKVVE... | null | null | regulation of DNA-templated transcription [GO:0006355]; regulation of secondary shoot formation [GO:2000032]; secondary shoot formation [GO:0010223] | nucleus [GO:0005634] | DNA-binding transcription factor activity [GO:0003700]; transcription cis-regulatory region binding [GO:0000976] | PF03634; | null | null | null | SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00701, ECO:0000269|PubMed:17307924}. | null | null | null | null | null | FUNCTION: Transcription factor that prevents axillary bud outgrowth and delays early axillary bud development. Indirectly required for the auxin-induced control of apical dominance. {ECO:0000269|PubMed:17307924, ECO:0000269|PubMed:17452340}. | Arabidopsis thaliana (Mouse-ear cress) |
A1YKW7 | RTXA_KINKI | MNLATTKAKLKSGAQAGVQALNKAGHAAKTGTVAAGKATVAGAKSLYLTIPKDYDIEKGGSLNELIKAADELGIARLQEDANNIESAKKSIDTVEKLLSFTQTGVAVSAKKLDELLQKYSSSQLAKSLGSSANIDSKLTKTNHILSTLSSFLGTALAGMDLDSLVKQGDASATDLAKASLDLINELVNNISNSVQSIEAFSEQLGRLGAAISQTKGLSGLGNKLQNLPNFGKANLALEMISGLLSGISAGFTLADKNASTEKKVAAGFELSNQVIGNVTKAISSYVLAQRAAAGLSTTGAVASLITASIMLAISPLAFMN... | null | null | killing of cells of another organism [GO:0031640] | extracellular region [GO:0005576]; host cell membrane [GO:0033644]; host cell plasma membrane [GO:0020002]; membrane [GO:0016020] | calcium ion binding [GO:0005509]; cholesterol binding [GO:0015485]; monoatomic cation channel activity [GO:0005261]; pore-forming activity [GO:0140911]; toxin activity [GO:0090729] | PF00353;PF02382;PF08339; | 2.150.10.10; | RTX prokaryotic toxin (TC 1.C.11) family | PTM: Myristoylated by RtxC; the toxin only becomes active when modified (PubMed:30405113, PubMed:32461253). Mainly myristoylated; a very minor fraction is acylated with hydroxymyristoyl, lauroyl and palmitoleyl chains fatty acyl groups (PubMed:30405113). Fatty acylation is involved in binding to host membranes and prom... | SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:21443941}. Host cell membrane {ECO:0000269|PubMed:25858109, ECO:0000269|PubMed:30405113, ECO:0000269|PubMed:33260488}; Multi-pass membrane protein {ECO:0000305}. | null | null | null | null | null | FUNCTION: Bacterial cytolysin that attacks host cell membranes and causes cell rupture by forming a pore (PubMed:25858109, PubMed:30405113). Binds and permeabilizes target cells by forming cation-selective pores (PubMed:25858109). Constitutes the key virulence cytotoxin of K.kingae (PubMed:21248099, PubMed:24664507). B... | Kingella kingae |
A1YYW7 | ALPH_SPHSX | MLKHVAAALLLATAMPVVAQSPAPAAAPAPAARSIAATPPKLIVAISVDQFSADLFSEYRQYYTGGLKRLTSEGAVFPRGYQSHAATETCPGHSTILTGSRPSRTGIIANNWFDLDAKREDKNLYCAEDESQPGSSSDKYEASPLHLKVPTLGGRMKAANPATRVVSVAGKDRAAIMMGGATADQVWWLGGPQGYVSYKGVAPTPLVTQVNQAFAQRLAQPNPGFELPAQCVSKDFPVQAGNRTVGTGRFARDAGDYKGFRISPEQDAMTLAFAAAAIENMQLGKQAQTDIISIGLSATDYVGHTFGTEGTESCIQVDRL... | 3.1.3.1 | COFACTOR: Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000269|PubMed:21829507}; Note=Binds 2 Zn(2+) ions. {ECO:0000269|PubMed:21829507}; | dephosphorylation [GO:0016311]; nucleoside triphosphate metabolic process [GO:0009141] | extracellular region [GO:0005576]; vacuole [GO:0005773] | alkaline phosphatase activity [GO:0004035]; metal ion binding [GO:0046872]; nucleoside triphosphate diphosphatase activity [GO:0047429]; ribonucleoside triphosphate phosphatase activity [GO:0017111]; zinc ion binding [GO:0008270] | PF01663; | 3.30.1360.150;3.40.720.10; | null | null | SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:18641147}. | CATALYTIC ACTIVITY: Reaction=a phosphate monoester + H2O = an alcohol + phosphate; Xref=Rhea:RHEA:15017, ChEBI:CHEBI:15377, ChEBI:CHEBI:30879, ChEBI:CHEBI:43474, ChEBI:CHEBI:67140; EC=3.1.3.1; Evidence={ECO:0000269|PubMed:18641147, ECO:0000269|PubMed:21829507}; | null | null | BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 9.0. {ECO:0000269|PubMed:18641147}; | null | FUNCTION: Alkaline phosphatase with broad substrate specificity. Precipitates uranium from alkaline solutions. {ECO:0000269|PubMed:18641147, ECO:0000269|PubMed:21829507}. | Sphingomonas sp |
A1Z0M0 | HEPC_LARCR | MKTFSVAVAVAVVLAFICLQESSAVPANEEQELEQQIYFADPEMPVESCKMPYYMRENRQGSPARCRFCCRCCPRMRGCGICCRF | null | null | defense response to fungus [GO:0050832]; defense response to Gram-negative bacterium [GO:0050829]; defense response to Gram-positive bacterium [GO:0050830]; intracellular iron ion homeostasis [GO:0006879]; negative regulation of iron ion transmembrane transport [GO:0034760] | extracellular region [GO:0005576]; extracellular space [GO:0005615] | hormone activity [GO:0005179] | PF06446; | null | Hepcidin family | null | SUBCELLULAR LOCATION: Secreted {ECO:0000250|UniProtKB:Q9EQ21}. | null | null | null | null | null | FUNCTION: Seems to act as a signaling molecule involved in the maintenance of iron homeostasis. Seems to be required in conjunction with HFE to regulate both intestinal iron absorption and iron storage in macrophages (By similarity). {ECO:0000250|UniProtKB:Q9EQ21}.; FUNCTION: Has very strong antibacterial activity agai... | Larimichthys crocea (Large yellow croaker) (Pseudosciaena crocea) |
A1Z198 | NL1B2_MOUSE | MEESQYKQEHNKKVAQDEGQEDKDTIFETIEAIEAKLMELKTNPESTFNYGIFPEVYMNQGEEILYPAWSLKEENLFQTFKSLRLFQKLCPRGSGNLVKKSWYPCVPEEGGHIINIQDLFGPNIGTQKEPQLVIIEGAAGIGKSTLARQVKRAWMEGELYRDHFQHVFFFSCRELAQCKKLSLAELITQGQDVPTAPINQILSHPEKLLFILDGIDEPAWVLADQNPELCLYWSQTQPVHTLLGSLLGKSILPEASFLLTTRTTALQKFIPSLPQSCQVEVLGFSDFEQEIYIYKYFAKQIFGIKALMMVESNPVLLTLC... | 3.4.-.- | null | inflammatory response [GO:0006954]; innate immune response [GO:0045087]; pattern recognition receptor signaling pathway [GO:0002221]; positive regulation of inflammatory response [GO:0050729]; positive regulation of interleukin-1 beta production [GO:0032731]; protein catabolic process [GO:0030163]; protein homooligomer... | canonical inflammasome complex [GO:0061702]; cytoplasm [GO:0005737]; NLRP1 inflammasome complex [GO:0072558] | ATP binding [GO:0005524]; cysteine-type endopeptidase activator activity [GO:0140608]; peptidase activity [GO:0008233]; protein self-association [GO:0043621] | PF00619;PF13553;PF13516;PF05729;PF17776;PF17779; | 1.10.533.10;3.40.50.300;3.80.10.10; | NLRP family | PTM: [NACHT, LRR and PYD domains-containing protein 1b allele 2]: Autocatalytically cleaved. Autocatalytic cleavage in FIIND region occurs constitutively, prior to activation signals, and is required for inflammasome activity (IL1B release), possibly by facilitating CASP1 binding. Both N- and C-terminal parts remain as... | SUBCELLULAR LOCATION: Cytoplasm, cytosol {ECO:0000250|UniProtKB:Q2LKW6}.; SUBCELLULAR LOCATION: [NACHT, LRR and PYD domains-containing protein 1b, C-terminus]: Inflammasome {ECO:0000250|UniProtKB:Q2LKW6}. | null | null | null | null | null | FUNCTION: Acts as the sensor component of the Nlrp1b inflammasome, which mediates inflammasome activation in response to various pathogen-associated signals, leading to subsequent pyroptosis (By similarity). Inflammasomes are supramolecular complexes that assemble in the cytosol in response to pathogens and other damag... | Mus musculus (Mouse) |
A1Z1Q3 | MACD2_HUMAN | MYPSNKKKKVWREEKERLLKMTLEERRKEYLRDYIPLNSILSWKEEMKGKGQNDEENTQETSQVKKSLTEKVSLYRGDITLLEVDAIVNAANASLLGGGGVDGCIHRAAGPCLLAECRNLNGCDTGHAKITCGYDLPAKYVIHTVGPIARGHINGSHKEDLANCYKSSLKLVKENNIRSVAFPCISTGIYGFPNEPAAVIALNTIKEWLAKNHHEVDRIIFCVFLEVDFKIYKKKMNEFFSVDDNNEEEEDVEMKEDSDENGPEEKQSVEEMEEQSQDADGVNTVTVPGPASEEAVEDCKDEDFAKDENITKGGEVTDHS... | 3.2.2.-; 3.5.1.- | null | brain development [GO:0007420]; DNA damage response [GO:0006974]; peptidyl-glutamate ADP-deribosylation [GO:0140291]; protein de-ADP-ribosylation [GO:0051725]; purine nucleoside metabolic process [GO:0042278]; response to bacterium [GO:0009617] | nucleolus [GO:0005730]; nucleoplasm [GO:0005654]; nucleus [GO:0005634] | ADP-ribosylglutamate hydrolase activity [GO:0140293]; deacetylase activity [GO:0019213]; hydrolase activity, acting on glycosyl bonds [GO:0016798]; O-acetyl-ADP-ribose deacetylase activity [GO:0061463] | PF01661; | 3.40.220.10; | null | null | SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:23474712}. Note=Recruited to DNA lesions, probably via mono-APD-ribosylated proteins. {ECO:0000269|PubMed:23474712}. | CATALYTIC ACTIVITY: Reaction=2''-O-acetyl-ADP-D-ribose + H2O = acetate + ADP-D-ribose + H(+); Xref=Rhea:RHEA:57060, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30089, ChEBI:CHEBI:57967, ChEBI:CHEBI:83767; Evidence={ECO:0000305|PubMed:21257746}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:57061; Evidence=... | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=107 uM for O-acetyl-ADP-ribose {ECO:0000269|PubMed:21257746}; | null | null | null | FUNCTION: Removes ADP-ribose from aspartate and glutamate residues in proteins bearing a single ADP-ribose moiety (PubMed:23474712, PubMed:23474714). Inactive towards proteins bearing poly-ADP-ribose (PubMed:23474712, PubMed:23474714). Deacetylates O-acetyl-ADP ribose, a signaling molecule generated by the deacetylatio... | Homo sapiens (Human) |
A1Z651 | POL_XMRV6 | MGQTVTTPLSLTLQHWGDVQRIASNQSVDVKKRRWVTFCSAEWPTFNVGWPQDGTFNLGVISQVKSRVFCPGPHGHPDQVPYIVTWEALAYDPPPWVKPFVSPKPPPLPTAPVLPPGPSAQPPSRSALYPALTPSIKSKPPKPQVLPDSGGPLIDLLTEDPPPYGAQPSSSARENNEEEAATTSEVSPPSPMVSRLRGRRDPPAADSTTSQAFPLRMGGDGQLQYWPFSSSDLYNWKNNNPSFSEDPGKLTALIESVLITHQPTWDDCQQLLGTLLTGEEKQRVLLEARKAVRGNDGRPTQLPNEVNAAFPLERPDWDYT... | 2.7.7.-; 2.7.7.49; 2.7.7.7; 3.1.-.-; 3.1.26.4; 3.4.23.- | COFACTOR: [Reverse transcriptase/ribonuclease H p80]: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250}; Note=Binds 2 magnesium ions for reverse transcriptase polymerase activity. {ECO:0000250}; COFACTOR: [Reverse transcriptase/ribonuclease H p80]: Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000305|Pu... | DNA integration [GO:0015074]; DNA recombination [GO:0006310]; establishment of integrated proviral latency [GO:0075713]; proteolysis [GO:0006508]; symbiont entry into host cell [GO:0046718]; viral genome integration into host DNA [GO:0044826]; virion assembly [GO:0019068] | host cell plasma membrane [GO:0020002]; membrane [GO:0016020]; viral nucleocapsid [GO:0019013] | aspartic-type endopeptidase activity [GO:0004190]; DNA binding [GO:0003677]; DNA-directed DNA polymerase activity [GO:0003887]; identical protein binding [GO:0042802]; RNA binding [GO:0003723]; RNA-directed DNA polymerase activity [GO:0003964]; RNA-DNA hybrid ribonuclease activity [GO:0004523]; structural constituent o... | PF01140;PF01141;PF02093;PF18697;PF00075;PF17919;PF00665;PF00077;PF00078;PF00098;PF16721; | 1.10.340.70;2.30.30.850;3.10.20.370;3.30.70.270;2.40.70.10;1.10.150.180;3.10.10.10;1.10.375.10;3.30.420.10;4.10.60.10; | null | PTM: [Gag-Pol polyprotein]: Specific enzymatic cleavages by the viral protease yield mature proteins. The protease is released by autocatalytic cleavage. The polyprotein is cleaved during and after budding, this process is termed maturation (By similarity). {ECO:0000250}.; PTM: [Capsid protein p30]: Sumoylated. Require... | SUBCELLULAR LOCATION: [Gag-Pol polyprotein]: Host cell membrane {ECO:0000305}; Lipid-anchor {ECO:0000305}.; SUBCELLULAR LOCATION: [Matrix protein p15]: Virion {ECO:0000305}.; SUBCELLULAR LOCATION: [Capsid protein p30]: Virion {ECO:0000305}.; SUBCELLULAR LOCATION: [Nucleocapsid protein p10]: Virion {ECO:0000305}. | CATALYTIC ACTIVITY: [Reverse transcriptase/ribonuclease H p80]: Reaction=a 2'-deoxyribonucleoside 5'-triphosphate + DNA(n) = diphosphate + DNA(n+1); Xref=Rhea:RHEA:22508, Rhea:RHEA-COMP:17339, Rhea:RHEA-COMP:17340, ChEBI:CHEBI:33019, ChEBI:CHEBI:61560, ChEBI:CHEBI:173112; EC=2.7.7.49; Evidence={ECO:0000255|PROSITE-ProR... | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=10.4 nM for RNA/DNA duplex {ECO:0000269|PubMed:22724525}; | null | null | null | FUNCTION: [Gag-Pol polyprotein]: Plays a role in budding and is processed by the viral protease during virion maturation outside the cell. During budding, it recruits, in a PPXY-dependent or independent manner, Nedd4-like ubiquitin ligases that conjugate ubiquitin molecules to Gag, or to Gag binding host factors. Inter... | Xenotropic MuLV-related virus (isolate VP62) (XMRV) |
A1Z6E0 | GUS_DROME | MGQKISGGVKTVSRNDSQSTFKPIIPRELQADFVKPARIDILLDMPPASRDLQLKHSWNSEDRSLNIFVKEDDKLTFHRHPVAQSTDCIRGKVGLTKGLHIWEIYWPTRQRGTHAVVGVCTADAPLHSVGYQSLVGSTEQSWGWDLGRNKLYHDSKNCAGVTYPAILKNDEAFLVPDKFLVALDMDEGTLSFIVDQQYLGIAFRGLRGKKLYPIVSAVWGHCEITMRYIGGLDPEPLPLMDLCRRTIRQKIGRTNLEEHIQQLQLPLSMKTYLLYKNRR | null | null | cuticle pattern formation [GO:0035017]; dorsal appendage formation [GO:0046843]; germ cell development [GO:0007281]; intracellular signal transduction [GO:0035556]; oocyte anterior/posterior axis specification [GO:0007314]; pole cell migration [GO:0007280]; pole plasm assembly [GO:0007315]; positive regulation of prote... | cell cortex [GO:0005938]; Cul5-RING ubiquitin ligase complex [GO:0031466]; cytoplasm [GO:0005737]; elongin complex [GO:0070449]; nucleus [GO:0005634]; perinuclear region of cytoplasm [GO:0048471]; pole plasm [GO:0045495]; SCF ubiquitin ligase complex [GO:0019005] | null | PF07525;PF00622; | 2.60.120.920;1.10.750.20; | SPSB family | null | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:12479811, ECO:0000269|PubMed:20123973}. Nucleus {ECO:0000269|PubMed:12479811, ECO:0000269|PubMed:20123973}. Note=Component of the cytoplasmic ribonucleoprotein (RNP) bodies which concentrate at the perinuclear region of the nurse cell and in punctate aggregates throug... | null | null | null | null | null | FUNCTION: Involved in the localization of vas to the posterior pole of the oocyte. Required maternally in the germ line for efficient primordial germ cell formation. {ECO:0000269|PubMed:12479811, ECO:0000269|PubMed:20123973}. | Drosophila melanogaster (Fruit fly) |
A1Z6H7 | PO210_DROME | MDSILCMILLILVRNHASEAARLNHPRVLLPIFEDKAINFTLEVDEPNCYKWSSSRQDLISVMPIYKGFSECAYQAVVTVRTHDRRRNTAIVFAEEVQTGETLRSDVIVDVIASLNVRTATRQLYLEEAPAMFELHAFDEQGNEFFTLEGIEFDWEILEPGSKRPTAMRYLTFTDSPYHTVPPTIEKFEADGKKGHMILLEGINTGTAKVTIAMPQAEYKHVRPVEVYISVLANIIIEPSEVTIMAGDSVSFRILQLKMDRLHVIDNNQYYLEVEDSSIAYLRGNSATGAALGRTQVFLRDRNMADSDEVQKGPSALLTV... | null | null | mRNA transport [GO:0051028]; nuclear pore organization [GO:0006999]; protein import into nucleus [GO:0006606] | cytoplasm [GO:0005737]; nuclear membrane [GO:0031965]; nuclear pore [GO:0005643]; nuclear pore inner ring [GO:0044611]; nuclear pore nuclear basket [GO:0044615]; nuclear pore transmembrane ring [GO:0070762] | null | null | null | NUP210 family | PTM: Glycosylated. {ECO:0000269|PubMed:3919018}. | SUBCELLULAR LOCATION: Nucleus membrane {ECO:0000269|PubMed:2517292, ECO:0000269|PubMed:3919018}; Single-pass type I membrane protein {ECO:0000255}. Nucleus, nuclear pore complex {ECO:0000269|PubMed:17682050, ECO:0000269|PubMed:7641726}. Cytoplasm {ECO:0000269|PubMed:2517292}. Note=During mitosis diffusively localized t... | null | null | null | null | null | FUNCTION: Component of the nuclear pore complex. {ECO:0000269|PubMed:17682050, ECO:0000269|PubMed:7641726}. | Drosophila melanogaster (Fruit fly) |
A1Z6J5 | TBCE_DROME | MVGIIDEVQLFYPLGTRIKIGDNYGTVRYVGEVSGHMGSWLGIEWDDGLRGKHNGIVDGKRYFQTQTPTGGSFIRPGKVGPCATLEDAARERYLNYDSSNVDESLIREAQASLQASLFEVVGMDKIARKQSKFEQLEEVSVDQTPVNAAGYLKELTHLTTLNVSHTLIWNWEIVASIAQQLPSLTNLNLSSNRLVLPTSSQITELEPSFRQLKRINLRSCGFSDWKDVMHTALLWPNILSLGLQENSLGQLAEVDRTKIFKQLHELDLHRTNIMDFDQVTKLGNLTTLRLLNIMENGIEEIKLPDCDSQEKLNIFVSLEQ... | null | null | microtubule cytoskeleton organization [GO:0000226]; microtubule polymerization [GO:0046785]; nervous system development [GO:0007399]; neuromuscular synaptic transmission [GO:0007274]; post-chaperonin tubulin folding pathway [GO:0007023]; regulation of synaptic assembly at neuromuscular junction [GO:0008582]; signal tra... | cytoplasm [GO:0005737]; synapse [GO:0045202] | alpha-tubulin binding [GO:0043014] | PF01302; | 2.30.30.190;3.80.10.10; | TBCE family | null | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:19297412}. | null | null | null | null | null | FUNCTION: Tubulin-folding protein which is required for the development of the neuronal microtubule network. Essential for the development and function of neuromuscular synapses. Likely to promote microtubule formation by acting in the negative regulation of the microtubule-severing protein spas. {ECO:0000269|PubMed:19... | Drosophila melanogaster (Fruit fly) |
A1Z6S7 | GDS1_DROME | MATAEIDDLIEKLKTTSVSPANTTNLLCEISATKDPKLFDKHELAECFLGLTKCDDTNVRKEAAKCIAEITKSEVQRKKFTKRNIIAAFLECLRQVPTSDGSMELPIQICRALGNICYLNDEARDLILELEGDAVLLRLLDITTIEDVANAAQFIKVRGGLLSNYLLGGEGLAKRAMELGVMKKLQGIIDIGASNVEQHEDLLLNTLPLLSILTENVSDLNFDSSLNIQLSRILAASTNPDLAEMCLELLHYQAESDEVKLILAKDGLCETIYNLLEKYKTLASTSEARALMKLACELIVLILTGDDSMHYLYTTPLLKN... | null | null | muscle cell cellular homeostasis [GO:0046716]; regulation of mitochondrion organization [GO:0010821]; rhabdomere development [GO:0042052] | cytosol [GO:0005829]; endoplasmic reticulum [GO:0005783]; mitochondrial outer membrane [GO:0005741]; mitochondrion [GO:0005739]; plasma membrane [GO:0005886] | guanyl-nucleotide exchange factor activity [GO:0005085] | null | 1.25.10.10; | null | null | SUBCELLULAR LOCATION: Endoplasmic reticulum {ECO:0000269|PubMed:27716788}. Mitochondrion {ECO:0000269|PubMed:27716788}. Cytoplasm, cytosol {ECO:0000269|PubMed:27716788}. | null | null | null | null | null | FUNCTION: Probably acts as a GEF (guanine nucleotide exchange factor) for the Rho family of small GTP-binding proteins (G proteins) that stimulates the dissociation of GDP to enable subsequent binding of GTP (By similarity). May also chaperone the processing and/or trafficking of small GTPases independently of GEF acti... | Drosophila melanogaster (Fruit fly) |
A1Z6W3 | PRIC1_DROME | MSSLSTGGGAGGSSGGPGGADAAAAPAAGQATVTATGNMEPAMVPRTANLLACKQWWRVCFLYGDQQKYYRQLYSKAAAQRLADANQEPDNARDREYDTVDCDLIAGQLDAVEDADDGIDLGDHSSTPKGGATTAGRPLFPHSSSPRRSKKLLRSLRAHVRGEKLPKNDTTTANESSEVTQRNARVTVLDDPFLFGIDADHLGDLVVRGKRYSTLDATENMARFYAEQEATAQVLEIIEQEEESPEQEAPKPALPPKQKQQRPVPPLPPPPANRVTQDQGTQPAAPQVPLQPLTAGDLQFLNLSLRQRSLPRSMKPFKDA... | null | null | anterior/posterior axis specification [GO:0009948]; axonal transport [GO:0098930]; establishment of imaginal disc-derived wing hair orientation [GO:0001737]; establishment of ommatidial planar polarity [GO:0042067]; establishment of planar polarity [GO:0001736]; establishment of protein localization [GO:0045184]; estab... | axon [GO:0030424]; cytoplasm [GO:0005737]; cytosol [GO:0005829]; plasma membrane [GO:0005886] | zinc ion binding [GO:0008270] | PF00412;PF06297; | 2.10.110.10; | Prickle / espinas / testin family | null | SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:12015986, ECO:0000269|PubMed:12642492, ECO:0000269|PubMed:12941693, ECO:0000269|PubMed:15937478}; Peripheral membrane protein {ECO:0000269|PubMed:12015986, ECO:0000269|PubMed:12642492, ECO:0000269|PubMed:12941693, ECO:0000269|PubMed:15937478}; Cytoplasmic side {EC... | null | null | null | null | null | FUNCTION: Acts in a planar cell polarity (PCP) complex; polarization along the apical/basal axis of epithelial cells. Correct expression of the alternative isoforms is required for PCP signaling in imaginal disks. PCP signaling in the wing disk requires the receptor fz and the cytoplasmic proteins dsh and pk. These act... | Drosophila melanogaster (Fruit fly) |
A1Z7A6 | ASAP_DROME | MPPSLIAVSEFVEETRSDYSSPTTSTFASRMPDCRHTIGVLEERLEFDREGLTKLKKAVKAIHNSGNTHVDNEMFMVRALERLGGKVIEQDEPDIGAAFLKFSVVTKELSALMKTLMQNINNIVMFPVDSMLKSELRGVKGDMKRPFDKAAKDYEAKFIKIEKEKKAQAKEAGMVRTEIDAAVVAEEMEKERRLYQLQTCEYLLKYKDIKTKTGIELLQHLIEYYHALSNYFKDGLQTIEHFGTYIGDLSEKLHEIKQKQDEDRRSLLDLRTVLRSTPDFERVDNVPSSESRSGGAGYSLHQLQGDKHHGVTRQGHLLKK... | null | null | compound eye morphogenesis [GO:0001745]; mitotic cleavage furrow ingression [GO:1990386]; positive regulation of protein localization [GO:1903829]; regulation of Golgi organization [GO:1903358]; regulation of GTPase activity [GO:0043087] | apical part of cell [GO:0045177]; cytoplasm [GO:0005737]; microvillus [GO:0005902]; nucleus [GO:0005634]; plasma membrane [GO:0005886] | GTPase activator activity [GO:0005096]; metal ion binding [GO:0046872]; phosphatidylinositol phosphate binding [GO:1901981] | PF12796;PF01412;PF16746;PF00169;PF14604; | 1.25.40.950;1.25.40.20;1.10.220.150;1.20.1270.60;2.30.29.30;2.30.30.40; | null | null | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:21976699, ECO:0000269|PubMed:27535433}. Nucleus {ECO:0000269|PubMed:27535433}. Cell membrane; Peripheral membrane protein {ECO:0000269|PubMed:21976699, ECO:0000269|PubMed:27535433}. Cell projection, microvillus {ECO:0000269|PubMed:27535433}. Note=Detected in large pun... | null | null | null | null | null | FUNCTION: Probable GTPase-activating protein (GAP) for Arf family proteins (Probable). Involved in Golgi apparatus organization by targeting Arf1 to the Golgi, which may be important for membrane trafficking during epithelial morphogenesis (PubMed:27535433). Regulates the positioning of interommatidial precursor cells ... | Drosophila melanogaster (Fruit fly) |
A1Z7A8 | COIL_DROME | MQHSSMKVDLSNFFKDERRNSLVFIDAAWNNIKDLQDHIQNLFSLKDISLLTSDGCYLPPRESIKVLNSAEGLKAFRFASHDSDTFVSPAPVKSSKKRKNRSVEEQVHLTASTPLRPSKRSKNQNNSEWINIAENPSRVRKKELLDMAPGPSVQSKLLTNKGTPKAPETQTEVSNMSANIETENKESAPQIKNKSKNKKPTKSPEASDQVENEPAPKSISRCTLKEGKMSESKNQETSPDILSEKSGVVTKENETREEQQDKTHLESNKIPDKLSQLKAGDQIEKSPGIAASLLSISFRSPLLEMPFNVPRIFQFPTKKQ... | null | null | Cajal body organization [GO:0030576] | Cajal body [GO:0015030]; chromosome, centromeric region [GO:0000775]; cytoplasm [GO:0005737]; histone locus body [GO:0035363]; nuclear body [GO:0016604]; nucleoplasm [GO:0005654]; spindle [GO:0005819] | null | PF15862; | null | Coilin family | null | SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:19158395}. Nucleus, nucleoplasm {ECO:0000269|PubMed:19158395}. Nucleus, Cajal body {ECO:0000269|PubMed:19158395, ECO:0000269|PubMed:23885126}. Chromosome, centromere {ECO:0000269|PubMed:19158395}. Cytoplasm, cytoskeleton, spindle {ECO:0000269|PubMed:19158395}. Note=Dete... | null | null | null | null | null | FUNCTION: Component of nuclear coiled bodies, also known as Cajal bodies or CBs, which are involved in the modification and assembly of nucleoplasmic snRNPs (PubMed:19846657). Required for Cajal body formation (PubMed:19158395, PubMed:19846657). {ECO:0000269|PubMed:19158395, ECO:0000269|PubMed:19846657}. | Drosophila melanogaster (Fruit fly) |
A1Z7G7 | LPHN_DROME | MILSKYQTAYACEGKKLTIECDPGDVINLIRANYGRFSITICNDHGNVEWSVNCMFPKSLSVLNSRCAHKQSCGVLAATSMFGDPCPGTHKYLEAHYQCISAAQTSTTTNRPSPPPWVLSNGPPIFGNGSGLIHPPGVGAGAPPPPRLPTLPGVVGISGNPGLFNVPPQHTAVTHSTPSSSTTAVGGGRLKGGATSTTTTKHPAGRHDGLPPPPQLHHHHNHHGEDTASPTKPSSKLPAGGNATSPSNTRILTGVGGSGTDDGTLLTTKSSPNRPPGTAASGSVVPGNGSVVRTINNINLNAAGMSGGDDESKLFCGPTH... | null | null | adenylate cyclase-activating G protein-coupled receptor signaling pathway [GO:0007189]; adult locomotory behavior [GO:0008344]; cell surface receptor signaling pathway [GO:0007166]; proprioception [GO:0019230] | plasma membrane [GO:0005886] | carbohydrate binding [GO:0030246]; G protein-coupled receptor activity [GO:0004930]; mechanoreceptor activity [GO:0140897]; transmembrane signaling receptor activity [GO:0004888] | PF00002;PF16489;PF02140;PF01825; | 1.25.40.610;2.60.120.740;2.60.220.50;4.10.1240.10;1.20.1070.10; | G-protein coupled receptor 2 family, LN-TM7 subfamily | PTM: Proteolytically cleaved into 2 subunits, an extracellular subunit and a seven-transmembrane subunit. {ECO:0000250|UniProtKB:O88923}. | SUBCELLULAR LOCATION: Cell membrane {ECO:0000255}; Multi-pass membrane protein {ECO:0000250|UniProtKB:O88923, ECO:0000255}. | null | null | null | null | null | null | Drosophila melanogaster (Fruit fly) |
A1Z7K9 | PAN2_DROME | MDYVYCGTDPIGASEDILSVYDAGSAPGNGHFSPSFNGFNIGTTDPEYVELVPVLADGGEHFGVSSVAFDDYEELLWMGNQGGHVTSYYTNSMQKYTSFQVHATDIVRDISTLDSGVLALTQTSLRHQIRRGLPKFTFKSNNMKEMVSMLQLSPHRLVMAGLQDELIDFDLRTLKETRIEHVGAGGCTVLRKNSRYLFAGDQLGTVTLRDLNSLSVQHTIKTHTNILSDFSVQGNLLISCGYSGRQNNLAIDRFLMVYDLRMLRLIAPIQVMIDPQMLKFLPSLTSQLAVVSSYGQVQLVDTVELSEPRVSMYQINTNGS... | 3.1.13.4 | COFACTOR: Name=a divalent metal cation; Xref=ChEBI:CHEBI:60240; Evidence={ECO:0000255|HAMAP-Rule:MF_03182}; Note=Binds 2 metal cations per subunit in the catalytic exonuclease domain. {ECO:0000255|HAMAP-Rule:MF_03182}; | mRNA processing [GO:0006397]; nuclear-transcribed mRNA poly(A) tail shortening [GO:0000289]; positive regulation of cytoplasmic mRNA processing body assembly [GO:0010606] | nucleus [GO:0005634]; P-body [GO:0000932]; PAN complex [GO:0031251] | metal ion binding [GO:0046872]; mRNA regulatory element binding translation repressor activity [GO:0000900]; poly(A)-specific ribonuclease activity [GO:0004535] | PF20770;PF00929;PF13423; | 3.90.70.10;3.30.420.10;2.130.10.10; | Peptidase C19 family, PAN2 subfamily | null | SUBCELLULAR LOCATION: Cytoplasm, P-body {ECO:0000255|HAMAP-Rule:MF_03182}. Nucleus {ECO:0000255|HAMAP-Rule:MF_03182}. Note=Shuttles between nucleus and cytoplasm. {ECO:0000255|HAMAP-Rule:MF_03182}. | CATALYTIC ACTIVITY: Reaction=Exonucleolytic cleavage of poly(A) to 5'-AMP.; EC=3.1.13.4; Evidence={ECO:0000255|HAMAP-Rule:MF_03182, ECO:0000269|PubMed:24880343}; | null | null | null | null | FUNCTION: Catalytic subunit of the poly(A)-nuclease (PAN) deadenylation complex, one of two cytoplasmic mRNA deadenylases involved in general and miRNA-mediated mRNA turnover. PAN specifically shortens poly(A) tails of RNA and the activity is stimulated by poly(A)-binding protein (PABP). PAN deadenylation is followed b... | Drosophila melanogaster (Fruit fly) |
A1Z7R6 | S46_DROME | MNEEPHAHENLVAKAQRSGDADPEVASTASEKQRSSGASAIAVGTEFPGNPQASRPQSLGMYLLEPFILILLFAYNFSSTVLKNEVIYQSCTAGFGYPDSVCQLLGTKNITNETKRIEEQVQPYAAQVTLAMRLVECFIPAFCGLFAGSWADHYGRKPLLMCSFLGYGLQYLISAAIAYCAMYTQGLVSPWWYVLSIVPLSCLGSSVTYSVAAVCFIADVSGGKVRSYRMIAYELAIYVGLLLGSLGSGYAYEATDAYIVFSISAVCIFTALFLMALLLPESLPARNRTLSTPTTDTSVVSMLKSLWSTCSKPREHQNRF... | null | null | innate immune response [GO:0045087]; peptidoglycan transport [GO:0015835]; positive regulation of antimicrobial humoral response [GO:0002760]; positive regulation of peptidoglycan recognition protein signaling pathway [GO:0061059]; transmembrane transport [GO:0055085] | membrane [GO:0016020]; phagocytic vesicle membrane [GO:0030670] | peptidoglycan transmembrane transporter activity [GO:0015647]; transmembrane transporter activity [GO:0022857] | PF07690; | 1.20.1250.20; | Major facilitator superfamily, SLC46 family | null | SUBCELLULAR LOCATION: Cytoplasmic vesicle, phagosome membrane {ECO:0000305|PubMed:28539433}; Multi-pass membrane protein {ECO:0000255}. | CATALYTIC ACTIVITY: Reaction=n H(+)(out) + N-acetyl-beta-D-glucosaminyl-(1->4)-1,6-anhydro-N-acetyl-beta-D-muramoyl-L-alanyl-gamma-D-glutamyl-meso-diaminoheptanedioate-D-alanine(out) = n H(+)(in) + N-acetyl-beta-D-glucosaminyl-(1->4)-1,6-anhydro-N-acetyl-beta-D-muramoyl-L-alanyl-gamma-D-glutamyl-meso-diaminoheptanedioa... | null | null | null | null | FUNCTION: Putative proton-coupled transporter that delivers pathogen-associated molecular patterns to cytosolic pattern recognition receptors as part of the innate immune response to microbes. Likely transports anhydro-muropeptides that contain the amino acid diaminopimelic acid (DAP-type peptidoglycan muropeptides) su... | Drosophila melanogaster (Fruit fly) |
A1Z7T0 | PKN_DROME | MSDSYYQGEYIKHPVLYELSHKYGFTENLPESCMSIRLEEIKEAIRREIRKELKIKEGAEKLREVAKDRRSLSDVAVLVKKSKSKLAELKSELQELESQILLTSANTAVNSNGQESITACIDPNGGFLVSGAVGGLGGGNTALEGGAPATANDKVLASLEKQLQIEMKVKTGAENMIQSLGIGCDKKLLAEAHQMLADSKAKIEFLRLRIIKVKQNREQADRLKASRQMIDEHGQTIGGNNSSQPQSLETTLEERIEELRHRLRIEAAVVDGAKNVIRTLQTANRAPDKKALQEAHGRLSESSRKLDLLRYSLDLRRQEL... | 2.7.11.13 | null | actin cytoskeleton organization [GO:0030036]; cell adhesion [GO:0007155]; dorsal closure [GO:0007391]; intracellular signal transduction [GO:0035556]; mitotic cytokinesis, division site positioning [GO:1902408]; positive regulation of wound healing [GO:0090303]; protein autophosphorylation [GO:0046777]; wing disc morph... | anchoring junction [GO:0070161]; apical cortex [GO:0045179]; cleavage furrow [GO:0032154]; cytoplasm [GO:0005737]; cytoskeleton [GO:0005856]; cytosol [GO:0005829]; lamellipodium [GO:0030027]; midbody [GO:0030496]; nucleus [GO:0005634] | ATP binding [GO:0005524]; diacylglycerol-dependent serine/threonine kinase activity [GO:0004697]; protein kinase activity [GO:0004672]; protein serine kinase activity [GO:0106310]; protein serine/threonine kinase activity [GO:0004674]; small GTPase binding [GO:0031267] | PF02185;PF00069;PF00433; | 1.10.287.160;1.10.510.10; | Protein kinase superfamily, Ser/Thr protein kinase family | PTM: Phosphorylated (By similarity). Autophosphorylated; autophosphorylation is stimulated by GTP-bound Rho/Rac GTPases. {ECO:0000250}. | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:17507675}. Nucleus {ECO:0000250}. Membrane {ECO:0000250}. Cell projection, lamellipodium {ECO:0000250}. Cytoplasm, cytoskeleton {ECO:0000250}. Cleavage furrow {ECO:0000250}. Midbody {ECO:0000250}. Cell junction {ECO:0000250}. | CATALYTIC ACTIVITY: Reaction=ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-[protein]; Xref=Rhea:RHEA:17989, Rhea:RHEA-COMP:9863, Rhea:RHEA-COMP:11604, ChEBI:CHEBI:15378, ChEBI:CHEBI:29999, ChEBI:CHEBI:30616, ChEBI:CHEBI:83421, ChEBI:CHEBI:456216; EC=2.7.11.13; CATALYTIC ACTIVITY: Reaction=ATP + L-threonyl-[p... | null | null | null | null | FUNCTION: Pkc-related serine/threonine-protein kinase and Rho/Rac effector protein that participates in specific signal transduction responses in the cell. May play a role in the regulation of cell cycle progression, actin cytoskeleton assembly, cell migration, cell adhesion and transcription activation signaling proce... | Drosophila melanogaster (Fruit fly) |
A1Z7Z9 | CP131_DROME | MDLCLKGSQINLATRQKTKPKYTSRSLTTLHNPCPHFRPRSANFLQQRSRSSPFLGRPQSADPKFGRRLSNYFVEKELRNGGKRQVSSNDLLKSLLEEPIKRSWLCRSTCNSSESDYSLHKRTPDSSEEGEQFLVNMPVGEKVKSYSSYSGNQGLSNGALLQRTAKPDLPGRVSFSKPNMHADLDSSDCDNDKQEVRPSISAPGPLTLPSFLSKVEQADPVGQKKSVHFGSTAAEGEVLAETYEYPKCPSENCTCSTRSSSTTSTNEASASDVKCACDAPSCRFMESSKQVEPTSPTPTLPKAPSSELDVIREYKQAVEG... | null | null | adult locomotory behavior [GO:0008344]; axoneme assembly [GO:0035082]; ciliary basal body-plasma membrane docking [GO:0097711]; ciliary transition zone assembly [GO:1905349]; cilium assembly [GO:0060271]; intraciliary transport [GO:0042073]; intraciliary transport involved in cilium assembly [GO:0035735]; non-motile ci... | centriolar satellite [GO:0034451]; centriole [GO:0005814]; ciliary basal body [GO:0036064]; ciliary cap [GO:0061822]; ciliary transition zone [GO:0035869]; cytoplasm [GO:0005737]; pericentriolar material [GO:0000242] | null | null | null | CEP131 family | null | SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, microtubule organizing center, centrosome {ECO:0000269|PubMed:21750193}. Cytoplasm, cytoskeleton, cilium basal body {ECO:0000269|PubMed:21750193, ECO:0000269|PubMed:27646273}. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome, centriole {ECO:0000269|PubMed... | null | null | null | null | null | FUNCTION: Cilium-specific protein with a role in cilium/flagellum formation (PubMed:21750193, PubMed:27646273). May be involved in transport of components into the growing cilium (PubMed:21750193). In germ cells and sensory neurons, plays a role with Cby in the building of the transition zone necessary for the formatio... | Drosophila melanogaster (Fruit fly) |
A1Z877 | NDG_DROME | MPTFGSKLLACLLLSSVILVSGQFEHYLDSLRASELYEFEDGSLGSIHLLPKGDSETIVLQLEQPIHFYGEQYEQLYINTNGILTFNSEFPEYLNQPFPLEYASIAAFYSNVDTSFSDEGTSISLFESKEQSILDRASSLVRYAFSSQSEFEARQVIVATWRNVGYFDSKTDRLNTFQVALIANEQSTFVQFIYPDGGLNWLQGETAGLGLPDIRAQAGFVAEDGRFYTLNGSGSENARFLSESTNLGVPGVWLFEVAPIENEQNVRSPDNAESLTESPALALSCQAHAHQCHEKAECHDKAEGYCCVCGSGFYGNGKSC... | null | null | basement membrane assembly involved in embryonic body morphogenesis [GO:2001197]; basement membrane organization [GO:0071711]; cell-matrix adhesion [GO:0007160]; regulation of basement membrane organization [GO:0110011] | basement membrane [GO:0005604]; extracellular space [GO:0005615] | calcium ion binding [GO:0005509]; extracellular matrix structural constituent [GO:0005201] | PF12947;PF07645;PF07474;PF00058;PF06119; | 2.40.155.10;2.10.25.10;2.120.10.30; | null | null | SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:30260959}. Secreted, extracellular space, extracellular matrix, basement membrane {ECO:0000269|PubMed:30260959, ECO:0000269|PubMed:30567930}. Note=Secreted in the hemolymph (PubMed:30260959). Localization to the basal membranes depends on laminin (PubMed:30260959, PubM... | null | null | null | null | null | FUNCTION: Cell adhesion glycoprotein which is widely distributed in basement membranes (PubMed:30260959, PubMed:30567930). Involved in cell-extracellular matrix (ECM) interactions probably by connecting the laminin and collagen IV networks (PubMed:30260959, PubMed:30567930). Required for permeability and mechanical sta... | Drosophila melanogaster (Fruit fly) |
A1Z8D0 | PWP1_DROME | MAEEGPPEPSIDFVPALCFVPRGVAKDRPDKIVLTQAELARIIGDTQQELDEESDDDAEEGENAEEDQNDMDVDDHADANSENRDPQDEFQFQEYDNEANANVTSLANIVDAGEQIPDEDEDSEAEDEVIKPSDNLILVGHVQDDAASMEVWVFNQEEEALYTHHDFLLPSFPLCIEWMNHDAGSEKAGNMCAIGCMDPIITVWDLDIQDAIEPTFKLGSKGSRKQNKEQYGHKDAVLDLSWNTNFEHILASGSVDQTVILWDMDEGQPHTTITAFGKQIQSLEFHPQEAQSILTGCADGYVRLFDCRDAEGVNSSSIEW... | null | null | cellular response to insulin stimulus [GO:0032869]; follicle cell of egg chamber development [GO:0030707]; germ cell development [GO:0007281]; male germ-line stem cell population maintenance [GO:0036098]; male gonad development [GO:0008584]; ovarian fusome organization [GO:0030723]; positive regulation of ribosome biog... | chromosome [GO:0005694]; nucleolus [GO:0005730]; nucleoplasm [GO:0005654]; nucleus [GO:0005634] | chromatin DNA binding [GO:0031490] | PF00400; | 2.130.10.10; | WD repeat PWP1 family | PTM: Phosphorylated in response to nutrient-activated TORC1 signaling. {ECO:0000269|PubMed:29065309}. | SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:21752937}. Nucleus, nucleolus {ECO:0000269|PubMed:29065309}. Chromosome {ECO:0000269|PubMed:21752937}. Nucleus, nucleoplasm {ECO:0000269|PubMed:29065309}. Note=Co-localizes with active forms of RNA polymerase II (PubMed:21752937). Associates with open chromatin and chro... | null | null | null | null | null | FUNCTION: Chromatin-associated factor that regulates transcription (PubMed:21752937). Regulates Pol I-mediated rRNA biogenesis and, probably, Pol III-mediated transcription (PubMed:29065309). Regulates the localization to the nucleolus of Cdk7, a regulator of the Pol I-elongation factor TFIIH (PubMed:29065309). Acts as... | Drosophila melanogaster (Fruit fly) |
A1Z8N1 | TRE11_DROME | MSGRDNRGAGGGGGGHQPLSNAMGKLKEKLTRVGDELGYHRVESNLSTSNTATSLDTILPEDPFLFPQVSPQRHPQNTVRTQRLLEDEPPLSFRPLLEDDDINEPPTQQQQRTPLRASGSLELTPLPPPPTSLEIREHRDRQQRGAQGDELQRSKQSLKGSRVSFERRDTGNSNTNSNKAAESSDEDSFEEKRTGFQQQKATSVDHKGILKDLKHILANDNRRQFQAKKHVSLDVKGTRFLQDLLKESSSEEEFHKTRREFQGRKHQSLDPRVTFKLDKVLQGSSTDSDEEGEDAEHKRLIHRPKDITKPVIIDLKDLES... | null | null | glucose transmembrane transport [GO:1904659]; transmembrane transport [GO:0055085]; trehalose transport [GO:0015771] | membrane [GO:0016020]; plasma membrane [GO:0005886] | glucose transmembrane transporter activity [GO:0005355]; transmembrane transporter activity [GO:0022857]; trehalose transmembrane transporter activity [GO:0015574] | PF00083; | 1.20.1250.20; | Major facilitator superfamily, Sugar transporter (TC 2.A.1.1) family, Trehalose transporter subfamily | null | SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:20035867}; Multi-pass membrane protein {ECO:0000255, ECO:0000269|PubMed:20035867}. | null | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=10.94 mM for trehalose {ECO:0000269|PubMed:20035867}; | null | null | null | FUNCTION: Low-capacity facilitative transporter for trehalose. Does not transport maltose, sucrose or lactose. Mediates the bidirectional transfer of trehalose. Responsible for the transport of trehalose synthesized in the fat body and the incorporation of trehalose into other tissues that require a carbon source, ther... | Drosophila melanogaster (Fruit fly) |
A1Z8P9 | TPR_DROME | MDLSGPQTLNNILQPDELKLVPEDVQKKLSEYINNFSDEYCKNRAAANRLAEAEQKKEELENKMEDYLVKFTSFELNVNELRTHLDQMSSERVNLMDTIAKGEQTISQLRKEKASVVEERDSMMKVIERQQAELERLKQDLHTYQQQLSSAIAAKCEAIARVDEIQSKEVALELKENRMESERDMLHKEILLISGDLNKSNAELQNIRREHTINTMQLQSCLKEKTESLKLMQEQYEQAVKTIGELTSKIEMQNDTAFKQNQATEEYVGKLKKELDAKEKLFEIFKSTESDHLIQREELLQGISEIKRLLEEAEEQCAQL... | null | null | chromatin organization [GO:0006325]; chromatin remodeling [GO:0006338]; germ-line stem-cell niche homeostasis [GO:0060250]; male germ-line stem cell asymmetric division [GO:0048133]; mitotic spindle assembly checkpoint signaling [GO:0007094]; mitotic spindle elongation [GO:0000022]; mRNA export from nucleus [GO:0006406... | chromosome, centromeric region [GO:0000775]; cytoplasm [GO:0005737]; euchromatin [GO:0000791]; metaphase plate [GO:0070090]; midbody [GO:0030496]; mitotic spindle [GO:0072686]; nuclear envelope [GO:0005635]; nuclear inclusion body [GO:0042405]; nuclear lamina [GO:0005652]; nuclear matrix [GO:0016363]; nuclear membrane ... | chromatin DNA binding [GO:0031490]; histone acetyltransferase binding [GO:0035035]; ribonucleoprotein complex binding [GO:0043021]; structural constituent of nuclear pore [GO:0017056] | PF07926; | null | TPR family | PTM: Mps1-mediated phosphorylation disrupts interaction with Mad1 during mitosis. {ECO:0000269|PubMed:31913420}. | SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:12027452, ECO:0000269|PubMed:15356261, ECO:0000269|PubMed:20174442, ECO:0000269|PubMed:22855526}. Nucleus matrix {ECO:0000269|PubMed:9152019}. Nucleus lamina {ECO:0000269|PubMed:15356261}. Nucleus envelope {ECO:0000269|PubMed:18562695, ECO:0000269|PubMed:9152019}. Nucle... | null | null | null | null | null | FUNCTION: Component of the nuclear pore complex (NPC), a complex required for the trafficking across the nuclear envelope (PubMed:9152019). Functions as a scaffolding element in the nuclear phase of the NPC (PubMed:12027452, PubMed:15356261). Plays a role in chromosomal organization and gene expression regulation; stim... | Drosophila melanogaster (Fruit fly) |
A1Z8R8 | PARL_DROME | MLMSRALCRSWLPQVARRCHANVNVPILRINSGHPAARSCRQIHSNRKQSSNLKPTTGEPAAAEQNTPVPVNNVIKAVAFTGAFTVGCFAGATILEYENTRSLILEKARQARFGWWQSRSLADRDYWTQIKQDIRRHWDSLTPGDKMFAPILLCNLVAFAMWRVPALKSTMITYFTSNPAAKVVCWPMFLSTFSHYSAMHLFANMYVMHSFANAAAVSLGKEQFLAVYLSAGVFSSLMSVLYKAATSQAGMSLGASGAIMTLLAYVCTQYPDTQLSILFLPALTFSAGAGIKVLMGIDFAGVVMGWKFFDHAAHLGGAMF... | 3.4.21.105 | null | mitochondrial fusion [GO:0008053]; protein processing [GO:0016485]; signal peptide processing [GO:0006465] | mitochondrial inner membrane [GO:0005743]; mitochondrion [GO:0005739] | endopeptidase activity [GO:0004175]; serine-type endopeptidase activity [GO:0004252] | PF01694; | 1.20.1540.10; | Peptidase S54 family | null | SUBCELLULAR LOCATION: Mitochondrion inner membrane {ECO:0000305|PubMed:16713954}; Multi-pass membrane protein {ECO:0000255}. | CATALYTIC ACTIVITY: Reaction=Cleaves type-1 transmembrane domains using a catalytic dyad composed of serine and histidine that are contributed by different transmembrane domains.; EC=3.4.21.105; Evidence={ECO:0000250|UniProtKB:P20350}; | null | null | null | null | FUNCTION: Mitochondrial intramembrane protease which plays a critical role in the regulation of mitochondrial function (PubMed:16713954, PubMed:21945938). Essential for mitochondrial development and fusion during spermatogenesis and the development of neurons and muscles (PubMed:16713954, PubMed:21945938). Essential fo... | Drosophila melanogaster (Fruit fly) |
A1Z8X3 | RTTN_DROME | MSTKQSPALQLAEGQLTKLTSESEEIRMRALDQIETRFIRCLQLGEPIQFKPVLLLKQLIRWFGYTPPLVPDRVLAMIMELLRSEYAEAVIRKIPYERFKAELQKVRRVLHKQESKRVSELLDDMNLLLLEKYNIDRVTPSVSSLSSNDIPSQATESADSSSNQIYDNLKPEDYEPSWSHPCLDDVATMKSMIDLPRNSVELQLQLTELIIRMGDYPTEYFLQPPFVFLHLVQLQTMTDGSLIHVNRALIACLRLLQQRILLRRNTLSYADRFDPPSRPKQVKVVSALVILLENCMKLIRPLLFSCTNDNWHIMELIVEI... | null | null | centriole assembly [GO:0098534]; centriole replication [GO:0007099]; centriole-centriole cohesion [GO:0010457]; centrosome cycle [GO:0007098]; ciliary basal body organization [GO:0032053] | centriole [GO:0005814]; centrosome [GO:0005813]; ciliary basal body [GO:0036064]; cytoplasm [GO:0005737]; ring centriole [GO:0061823] | null | PF14726; | null | Rotatin family | null | SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, microtubule organizing center, centrosome, centriole {ECO:0000269|PubMed:19948479, ECO:0000269|PubMed:32543652}. Note=Associated with the daughter centriole on mitotic entry (PubMed:32543652). Ana3 recruitment to the procentriole in interphase precedes the Rcd4 one (PubMed... | null | null | null | null | null | FUNCTION: Participes in the structural integrity of both centrioles and basal bodies and in centriole cohesion (PubMed:19948479). Participates in the later stages of centriole assembly through the interaction with Rcd4 leading to the centriole to centrosome conversion (PubMed:32543652). {ECO:0000269|PubMed:19948479, EC... | Drosophila melanogaster (Fruit fly) |
A1Z9E2 | LIN54_DROME | MDTSGGNLDSLDDTEPLPELSFEDFLEPTSEKSSQHMEIEALDSEEDNIGGEDLADPANDSLNTPQFKKNVVHILEDKRLNSSGLTVLKSHAIKMVTAGGTPPAKAQVTDVKILNKLKPIPSSTLKIGSTTIATKSTPGSITKTLGNLTQIRTKDGQVIFVQKSVPGTQSSTAVTGSPSGGIRRLVAPSGIQKAVLSKGVTMASTGLVKAAVPAKASTSVPGSAITLKGIQPLAGGTAKASTSSTTATTSPSLAQPNKIQVVRTADGKIIKINQAGPSLLVNAKQGTGTTVTPGGSAATSVKLSPSTGNVVLNKPVGQVV... | null | null | cell cycle [GO:0007049]; determination of adult lifespan [GO:0008340]; eggshell chorion gene amplification [GO:0007307]; flagellated sperm motility [GO:0030317]; negative regulation of transcription by RNA polymerase II [GO:0000122]; oogenesis [GO:0048477]; regulation of DNA-templated transcription [GO:0006355] | chromatin [GO:0000785]; Myb complex [GO:0031523]; nucleus [GO:0005634]; polytene chromosome [GO:0005700] | DNA binding [GO:0003677] | PF03638; | null | Lin-54 family | null | SUBCELLULAR LOCATION: Nucleus {ECO:0000305}. | null | null | null | null | null | FUNCTION: Component of the DREAM complex, a multiprotein complex that can both act as a transcription activator or repressor depending on the context. In follicle cells, the complex plays a central role in the site-specific DNA replication at the chorion loci. During development, the complex represses transcription of ... | Drosophila melanogaster (Fruit fly) |
A1Z9G2 | SYF1_DROME | MVTKTIKSLNLEINFEVEDVPYEEEILRNAYSVKHWLRYIDHKAKAPNNGVNMVYERALKELPGSYKIWHNYLRTRRKQVRGKIPTDPMYEEVNSAFERALVFMHKMPRIWMDYGAFMTSQCKITRTRHVFDRALRALPITQHGRIWPLYLQFVRRFEMPETALRVYRRYLKLFPEDTEEYVDYLQEADRLDEAAQQLAHIVDNEHFVSKHGKSNHQLWNELCDLISKNPHKVHSLNVDAIIRGGLRRYTDQLGHLWNSLADYYVRSGLFDRARDIYEEAIQTVTTVRDFTQVFDEYAQFEELSLNRRMEQVAANEAATE... | null | null | cardioblast cell fate determination [GO:0007510]; generation of catalytic spliceosome for first transesterification step [GO:0000349]; Malpighian tubule morphogenesis [GO:0007443]; morphogenesis of an epithelium [GO:0002009]; mRNA splicing, via spliceosome [GO:0000398]; regulation of alternative mRNA splicing, via spli... | catalytic step 2 spliceosome [GO:0071013]; nucleus [GO:0005634]; post-mRNA release spliceosomal complex [GO:0071014]; precatalytic spliceosome [GO:0071011]; Prp19 complex [GO:0000974]; U2-type catalytic step 2 spliceosome [GO:0071007] | null | PF13181; | 1.25.40.10; | Crooked-neck family | null | SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:24755291}. | null | null | null | null | null | FUNCTION: Subunit of the NTC(Nineteen)/Prp19 complex, which is part of the spliceosome (PubMed:24755291, PubMed:28087625). The complex participates in spliceosome assembly, its remodeling and is required for efficient spliceosome activation (PubMed:24755291, PubMed:28087625). Essential for efficient pre-mRNA splicing (... | Drosophila melanogaster (Fruit fly) |
A1Z9J4 | DJ1A_DROME | MLSVLRKSFPNGVTHAHRVIRCKSNQDKCAKNALIILAPGAEEMEFTISADVLRRGKILVTVAGLHDCEPVKCSRSVVIVPDTSLEEAVTRGDYDVVVLPGGLAGNKALMNSSAVGDVLRCQESKGGLIAAICAAPTALAKHGIGKGKSITSHPDMKPQLKELYCYIDDKTVVQDGNIITSRGPGTTFDFALKITEQLVGAEVAKEVAKAMLWTYKP | null | null | dopamine metabolic process [GO:0042417]; glycolate biosynthetic process [GO:0046295]; glyoxal metabolic process [GO:1903189]; mitochondrial ATP synthesis coupled electron transport [GO:0042775]; neuron cellular homeostasis [GO:0070050]; positive regulation of phosphatidylinositol 3-kinase/protein kinase B signal transd... | cytoplasm [GO:0005737]; mitochondrion [GO:0005739]; nucleus [GO:0005634] | peroxiredoxin activity [GO:0051920]; protein deglycase activity [GO:0036524] | PF01965; | 3.40.50.880; | null | null | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:16203113}. Nucleus {ECO:0000269|PubMed:16203113}. Mitochondrion {ECO:0000269|PubMed:16203113}. | null | null | null | null | null | FUNCTION: Plays an important role in cell protection against oxidative stress and cell death acting as oxidative stress sensor (PubMed:16139213, PubMed:16139214, PubMed:20457924). Does not play a role in methylglyoxal detoxification (By similarity). {ECO:0000250|UniProtKB:Q99497, ECO:0000250|UniProtKB:Q9VA37, ECO:00002... | Drosophila melanogaster (Fruit fly) |
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