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 |
|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|
G2IQQ5 | LIGJ_SPHSK | MMMIIDCHGHYTVLPKAHDEWREQQKAAFKAGQPAPPYPEISDDEIRETIEANQLRLIKERGADMTIFSPRASAMAPHVGDQSVAVPWAQACNNLIARVVDLFPETFAGVCMLPQSPEADMTSSIAELERCVNELGFIGCNLNPDPGGGHFKHPPLTDRFWYPFYEKMVELDVPAMIHVSGSCNPAMHATGAYYLAADTIAFMQLLQGNLFADFPTLRFIIPHGGGAVPYHWGRFRGLADMLKQPSLDTLLMNNVFFDTCVYHQPGINLLADVIDNKNILFGSEMVGAVRGIDPTTGHYFDDTKRYIDALDISDQERHAI... | 4.2.1.- | COFACTOR: Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000269|PubMed:30207699}; Note=Binds 1 zinc ion per subunit. The metal center contained within the active site of LigJ is not used to activate the water molecule but is utilized to activate the substrate via polarization of the carbonyl oxygen. {ECO:0000269|P... | heterocycle metabolic process [GO:0046483]; lignin catabolic process [GO:0046274] | cytosol [GO:0005829] | carboxy-lyase activity [GO:0016831]; hydrolase activity [GO:0016787]; metal ion binding [GO:0046872] | PF04909; | 3.20.20.140; | Metallo-dependent hydrolases superfamily | null | null | CATALYTIC ACTIVITY: Reaction=(3Z)-2-oxo-4-carboxy-3-hexenedioate + H2O = (2S)-2-hydroxy-4-oxobutane-1,2,4-tricarboxylate; Xref=Rhea:RHEA:58508, ChEBI:CHEBI:15377, ChEBI:CHEBI:142690, ChEBI:CHEBI:142706; Evidence={ECO:0000269|PubMed:29658701, ECO:0000269|PubMed:30207699}; | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=9.8 uM for (3Z)-2-keto-4-carboxy-3-hexenedioate (at pH 8.0) {ECO:0000269|PubMed:30207699}; Note=kcat is 25.6 sec(-1) (at pH 8.0). {ECO:0000269|PubMed:30207699}; | PATHWAY: Secondary metabolite metabolism; lignin degradation. {ECO:0000269|PubMed:11092855, ECO:0000305|PubMed:29658701}. | null | null | FUNCTION: Contributes to the degradation of lignin at the level of the protocatechuate 4,5-cleavage pathway. Catalyzes the hydration of the double bond of (3Z)-2-keto-4-carboxy-3-hexenedioate (KCH) to (4S)-4-carboxy-4-hydroxy-2-oxoadipate (CHA, also named (2S)-2-hydroxy-4-oxobutane-1,2,4-tricarboxylate) (PubMed:2965870... | Sphingobium sp. (strain NBRC 103272 / SYK-6) |
G2IQQ8 | LIGK_SPHSK | MRGAAMGVVVQNIERAPLEVIDGLAACGVATVHEAQGRTGLLASYMRPIYRGARVAGSALTISAPPGDNWMVHVAIEQLKAGDILLLAPTSPCEDGYFGDLLATSAQARGCRGLVIDAGVRDVRDLTEMNFPVWSKAIYAQGTVKNTLGSVNVPVVCANALVNPGDVIVADDDGVCVVPLANAEKVLEAARAREANEGDKREKMANGVLGLDLYKMRERLEKEGLKYV | 4.1.1.112; 4.1.3.17 | COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000269|PubMed:12486039}; | lignin catabolic process [GO:0046274]; protocatechuate catabolic process, meta-cleavage [GO:0019617] | null | 4-hydroxy-4-methyl-2-oxoglutarate aldolase activity [GO:0047443]; metal ion binding [GO:0046872]; oxaloacetate decarboxylase activity [GO:0008948] | PF03737; | 3.50.30.40; | LigK/PcmE family | null | null | CATALYTIC ACTIVITY: Reaction=4-hydroxy-4-methyl-2-oxoglutarate = 2 pyruvate; Xref=Rhea:RHEA:22748, ChEBI:CHEBI:15361, ChEBI:CHEBI:58276; EC=4.1.3.17; Evidence={ECO:0000269|PubMed:29658701}; CATALYTIC ACTIVITY: Reaction=2-hydroxy-4-oxobutane-1,2,4-tricarboxylate = oxaloacetate + pyruvate; Xref=Rhea:RHEA:28935, ChEBI:CHE... | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=11.2 uM for 2-hydroxy-4-oxobutane-1,2,4-tricarboxylate {ECO:0000269|PubMed:12486039}; KM=136 uM for oxaloacetate {ECO:0000269|PubMed:12486039}; Vmax=265 umol/min/mg enzyme for CHA aldol cleavage {ECO:0000269|PubMed:12486039}; Vmax=13.2 umol/min/mg enzyme for oxaloa... | PATHWAY: Secondary metabolite metabolism; lignin degradation. {ECO:0000305|PubMed:12486039}. | BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 8.0 for CHA aldolase activity, and 7.0 for oxaloacetate decarboxylase activity. {ECO:0000269|PubMed:12486039}; | null | FUNCTION: Contributes to the degradation of lignin, being involved in the final step of the protocatechuate 4,5-cleavage pathway. Catalyzes the conversion of 4-carboxy-4-hydroxy-2-oxoadipate (CHA, also named 2-hydroxy-4-oxobutane-1,2,4-tricarboxylate) to pyruvate and oxaloacetate but also the decarboxylation of oxaloac... | Sphingobium sp. (strain NBRC 103272 / SYK-6) |
G2IQS7 | LIGM_SPHSK | MSAPTNLEQVLAAGGNTVEMLRNSQIGAYVYPVVAPEFSNWRTEQWAWRNSAVLFDQTHHMVDLYIRGKDALKLLSDTMINSPKGWEPNKAKQYVPVTPYGHVIGDGIIFYLAEEEFVYVGRAPAANWLMYHAQTGGYNVDIVHDDRSPSRPMGKPVQRISWRFQIQGPKAWDVIEKLHGGTLEKLKFFNMAEMNIAGMKIRTLRHGMAGAPGLEIWGPYETQEKARNAILEAGKEFGLIPVGSRAYPSNTLESGWIPSPLPAIYTGDKLKAYREWLPANSYEASGAIGGSFVSSNIEDYYVNPYEIGYGPFVKFDHDFI... | 2.1.1.341 | null | lignin catabolic process [GO:0046274]; methylation [GO:0032259] | cytosol [GO:0005829] | methyltransferase activity [GO:0008168] | PF01571; | null | GcvT family | null | null | CATALYTIC ACTIVITY: Reaction=(6S)-5,6,7,8-tetrahydrofolate + vanillate = (6S)-5-methyl-5,6,7,8-tetrahydrofolate + 3,4-dihydroxybenzoate; Xref=Rhea:RHEA:52276, ChEBI:CHEBI:16632, ChEBI:CHEBI:18608, ChEBI:CHEBI:36241, ChEBI:CHEBI:57453; EC=2.1.1.341; Evidence={ECO:0000269|PubMed:15743951, ECO:0000269|PubMed:28373573, ECO... | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=0.63 mM for vanillate {ECO:0000269|PubMed:28373573}; KM=0.72 mM for tetrahydrofolate {ECO:0000269|PubMed:28373573}; Note=kcat is 5.76 sec(-1) with vanillate as substrate. {ECO:0000269|PubMed:28373573}; | PATHWAY: Secondary metabolite metabolism; lignin degradation. {ECO:0000305|PubMed:15743951}. | BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 8 with vanillate as substrate. {ECO:0000269|PubMed:28373573}; | BIOPHYSICOCHEMICAL PROPERTIES: Temperature dependence: Optimum temperature is 30 degrees Celsius with vanillate as substrate. {ECO:0000269|PubMed:28373573}; | FUNCTION: Involved in the catabolism of vanillate and syringate. Catalyzes the transfer of a methyl moiety from vanillate or 3-O-methylgallate (3MGA) to tetrahydrofolate, forming protocatechuate (PCA) or gallate, respectively, and methyl-tetrahydrofolate. Has similar activities with both substrates (PubMed:15743951). C... | Sphingobium sp. (strain NBRC 103272 / SYK-6) |
G2NFJ9 | LAM55_STREK | MHVPPTDPARSAPPASPHRRRRPKALGLTALAAAMLMAVPTTQAAFGSDVRPAAAQEVVGGGDLGPNVLVFDPSTPDIQGKVDEVFRKQESNQFGTDRYALMFKPGTYNDINAQIGFYTSIAGLGLNPDDTTFNGDVTVDAGWFDGNATQNFWRSAENLALNPVNGTNRWAVSQAAPFRRMHVKGGLNLAPDGYGWASGGYIADSKIDGEVGPYSQQQWYTRDSSVGGWGNGVWNMTFSGVEGAPAQSFPEPPYTTLETTPVSREKPFLYLDGDDYKVFVPAKRTNARGTSWGNGTPEGESLPLDQFYVVKPGATAETIN... | 3.2.1.58 | null | glucan catabolic process [GO:0009251] | extracellular region [GO:0005576] | glucan exo-1,3-beta-glucosidase activity [GO:0004338] | null | 2.160.20.10; | Glycosyl hydrolase 55 family | null | SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:23301151}. | CATALYTIC ACTIVITY: Reaction=Successive hydrolysis of beta-D-glucose units from the non-reducing ends of (1->3)-beta-D-glucans, releasing alpha-glucose.; EC=3.2.1.58; Evidence={ECO:0000269|PubMed:25752603}; | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=0.93 mg/ml for L.digitata soluble laminarin (at pH 6 and 40 degrees Celsius) {ECO:0000269|PubMed:25752603}; Vmax=128 umol/min/mg enzyme with L.digitata soluble laminarin as substrate (at pH 6 and 40 degrees Celsius) {ECO:0000269|PubMed:25752603}; Note=kcat is 138 s... | null | BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 6. Maintains 70% or more of the maximal activity from pH 6.0 to 9.0. {ECO:0000269|PubMed:25752603}; | BIOPHYSICOCHEMICAL PROPERTIES: Temperature dependence: Optimum temperature is 50 degrees Celsius. Maintains 70% or more of the maximal activity from 35 to 65 degrees Celsius. {ECO:0000269|PubMed:25752603}; | FUNCTION: Exo-beta-1,3-glucanase that specifically hydrolyzes laminarin and laminarioligosaccharides, producing glucose and laminaribiose as end products. {ECO:0000269|PubMed:25752603}. | Streptomyces sp. (strain SirexAA-E / ActE) |
G2Q0E2 | PEX10_THET4 | MATQPPPARPPPPLTSSPYPYAAAPDIIRAHQKDAYFQGVLANRLSDLHRRLRGARSAHAWAAETRTFAAALYLCLTTLLGNRTLGEEYCDLVQVEEAPSKLFASSSSKAADDHIYENGLGGGGDGGPLLPSLPRRAGYILTAIVLPHLASRALPSVRSAIRKRLQSRLATLSRRRQQTGTKSGSGRGGRGGGGGITEYRVLRYLLTHLTPLTSGAHFRAATLAVFYFTGAYYELSKWVWGLRYVFTTRAGRVVDDDHNRHHHSPQHGGGNGGRAGYEVLGVLLVVQMAVRAWLHVREQLSSGSVAGGGGEEEEDGEDGF... | 2.3.2.27 | null | protein import into peroxisome matrix, receptor recycling [GO:0016562]; protein ubiquitination [GO:0016567] | peroxisomal membrane [GO:0005778] | transferase activity [GO:0016740]; zinc ion binding [GO:0008270] | PF04757;PF13923; | 3.30.40.10; | Pex2/pex10/pex12 family | null | SUBCELLULAR LOCATION: Peroxisome membrane {ECO:0000250|UniProtKB:Q05568}; Multi-pass membrane protein {ECO:0000269|PubMed:35768507}. | CATALYTIC ACTIVITY: Reaction=S-ubiquitinyl-[E2 ubiquitin-conjugating enzyme]-L-cysteine + [acceptor protein]-L-lysine = [E2 ubiquitin-conjugating enzyme]-L-cysteine + N(6)-ubiquitinyl-[acceptor protein]-L-lysine.; EC=2.3.2.27; Evidence={ECO:0000250|UniProtKB:Q05568}; | null | PATHWAY: Protein modification; protein ubiquitination. {ECO:0000250|UniProtKB:Q05568}. | null | null | FUNCTION: E3 ubiquitin-protein ligase component of a retrotranslocation channel required for peroxisome organization by mediating export of the PEX5 receptor from peroxisomes to the cytosol, thereby promoting PEX5 recycling (By similarity). The retrotranslocation channel is composed of PEX2, PEX10 and PEX12; each subun... | Thermothelomyces thermophilus (strain ATCC 42464 / BCRC 31852 / DSM 1799) (Sporotrichum thermophile) |
G2Q1C9 | PEX2_THET4 | MSDSDPKPTAAKGAAPTSIPNSTRNPNPTPPNPNPNPNPISTPAPTPTATPSPPIASSSNNGNNSTRSTNIDTNNNTNNAFFQAQQRIAARREAREAAAAARQATQQSASRLRARIAASQSPLLRRLGTSTLSLWDTLTSREGTRPAFRVGQVDAELLDEELVELLRGQVREALRYVGGGGGGGGGGGGGGVGSGVAQDWEAEISLALRAVLFKLTVWDHDATYGAALQNLKYTDARRDGPALAPPSRWQKALYGLVTVGGRYLWAKWEDWLLEQDDGFEGPSPRVKRLARWTSALSTLHASAALVSFLVFLLHGRYRTL... | 2.3.2.36 | null | protein import into peroxisome matrix, receptor recycling [GO:0016562]; protein ubiquitination [GO:0016567] | peroxisomal membrane [GO:0005778] | transferase activity [GO:0016740]; zinc ion binding [GO:0008270] | PF04757; | null | Pex2/pex10/pex12 family | null | SUBCELLULAR LOCATION: Peroxisome membrane {ECO:0000250|UniProtKB:P32800}; Multi-pass membrane protein {ECO:0000269|PubMed:35768507}. | CATALYTIC ACTIVITY: Reaction=[E2 ubiquitin-conjugating enzyme]-S-ubiquitinyl-L-cysteine + [acceptor protein]-L-cysteine = [E2 ubiquitin-conjugating enzyme]-L-cysteine + [acceptor protein]-S-ubiquitinyl-L-cysteine.; EC=2.3.2.36; Evidence={ECO:0000250|UniProtKB:P32800}; | null | PATHWAY: Protein modification; protein ubiquitination. {ECO:0000250|UniProtKB:P32800}. | null | null | FUNCTION: E3 ubiquitin-protein ligase component of a retrotranslocation channel required for peroxisome organization by mediating export of the PEX5 receptor from peroxisomes to the cytosol, thereby promoting PEX5 recycling (By similarity). The retrotranslocation channel is composed of PEX2, PEX10 and PEX12; each subun... | Thermothelomyces thermophilus (strain ATCC 42464 / BCRC 31852 / DSM 1799) (Sporotrichum thermophile) |
G2Q9A5 | MYCA_THET4 | MVQTPRQKKFGNEPIAIIGSACRFPGAASTPSKLWELLRKPKDLLTKIPPNRFNADSFYHPDGAHHGASNVTESYFLEEDPRLFDAAFFNVKPVEAHSIDPQHRMLLEVVYESLEAAGQSIEGLAKSQTGVFVGLMCADFSDHILRDLDAIPTYMATGTARSLISNRISYFFDWHGPSMTIDTACSSSLFAVHQAVQLLRSGDSDLAVAAGSNLILGPELYIGESKLKMLSPTGRSRMWDADADGYARGEGVAAVILKRLSDAIRDGDHIESIIRESGINSDGRTKGLTMPNELAQADLIVRTYQKAGLDPTKEEERCQY... | 2.3.1.-; 6.3.2.- | null | amide biosynthetic process [GO:0043604]; fatty acid biosynthetic process [GO:0006633]; heterocycle biosynthetic process [GO:0018130]; methylation [GO:0032259]; organic cyclic compound biosynthetic process [GO:1901362]; organonitrogen compound biosynthetic process [GO:1901566]; toxin biosynthetic process [GO:0009403] | null | 3-oxoacyl-[acyl-carrier-protein] synthase activity [GO:0004315]; fatty acid synthase activity [GO:0004312]; isomerase activity [GO:0016853]; ligase activity [GO:0016874]; methyltransferase activity [GO:0008168]; oxidoreductase activity [GO:0016491]; phosphopantetheine binding [GO:0031177] | PF00698;PF00501;PF00668;PF16197;PF00109;PF02801;PF08659;PF08242;PF07993;PF21089;PF00550;PF14765; | 3.30.300.30;3.40.47.10;1.10.1200.10;3.30.559.10;3.40.366.10;3.40.50.12780;3.40.50.720;3.30.559.30;3.10.129.110;3.40.50.150; | NRP synthetase family | null | null | CATALYTIC ACTIVITY: Reaction=ATP + 12 H(+) + L-leucine + 8 malonyl-CoA + 9 NADPH + 4 S-adenosyl-L-methionine = (5S)-5-(2-methylpropyl)-3-[(2E,6R,8E,10E,12E)-6,8,10,12-tetramethyltetradeca-2,8,10,12-tetraenoyl]-2,5-dihydro-1H-pyrrol-2-one + AMP + 8 CO2 + 8 CoA + diphosphate + 7 H2O + 9 NADP(+) + 4 S-adenosyl-L-homocyste... | null | PATHWAY: Mycotoxin biosynthesis. {ECO:0000269|PubMed:27960349}. | null | null | FUNCTION: Hybrid PKS-NRPS synthetase; part of the gene cluster that mediates the biosynthesis of myceliothermophins, mycotoxins that contain a trans-fused decalin ring system connected to a conjugated 3-pyrrolin-2-one moiety and that have potential anti-tumor properties (PubMed:27960349). The polyketide synthase module... | Thermothelomyces thermophilus (strain ATCC 42464 / BCRC 31852 / DSM 1799) (Sporotrichum thermophile) |
G2Q9T3 | LP9H_THET4 | MSKASALLAGLTGAALVAAHGHVSHIVVNGVYYRNYDPTTDWYQPNPPTVIGWTAADQDNGFVEPNSFGTPDIICHKSATPGGGHATVAAGDKINIVWTPEWPESHIGPVIDYLAACNGDCETVDKSSLRWFKIDGAGYDKAAGRWAADALRANGNSWLVQIPSDLKAGNYVLRHEIIALHGAQSPNGAQAYPQCINLRVTGGGSNLPSGVAGTSLYKATDPGILFNPYVSSPDYTVPGPALIAGAASSIAQSTSVATATGTATVPGGGGANPTATTTAATSAAPSTTLRTTTTSAAQTTAPPSGDVQTKYGQCGGNGWT... | 3.2.1.4 | COFACTOR: Name=Cu(2+); Xref=ChEBI:CHEBI:29036; Evidence={ECO:0000250|UniProtKB:Q4WP32}; Note=Binds 1 copper ion per subunit. {ECO:0000250|UniProtKB:Q4WP32}; | cellulose catabolic process [GO:0030245] | extracellular region [GO:0005576] | cellulose binding [GO:0030248]; hydrolase activity, acting on glycosyl bonds [GO:0016798]; metal ion binding [GO:0046872]; oxidoreductase activity [GO:0016491] | PF03443;PF00734; | 2.70.50.70; | Polysaccharide monooxygenase AA9 family | null | SUBCELLULAR LOCATION: Secreted {ECO:0000305|PubMed:22342036}. | CATALYTIC ACTIVITY: Reaction=Endohydrolysis of (1->4)-beta-D-glucosidic linkages in cellulose, lichenin and cereal beta-D-glucans.; EC=3.2.1.4; Evidence={ECO:0000269|PubMed:22342036, ECO:0000269|PubMed:35450635}; | null | null | BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 8.0. {ECO:0000269|PubMed:22342036}; | BIOPHYSICOCHEMICAL PROPERTIES: Temperature dependence: Optimum temperature is 65 degrees Celsius. {ECO:0000269|PubMed:22342036}; | FUNCTION: Lytic polysaccharide monooxygenase (LMPO) that depolymerizes crystalline and amorphous polysaccharides via the oxidation of scissile alpha- or beta-(1-4)-glycosidic bonds, yielding C1 or C4 oxidation products (PubMed:22342036, PubMed:35450635). Catalysis by LPMOs requires the reduction of the active-site copp... | Thermothelomyces thermophilus (strain ATCC 42464 / BCRC 31852 / DSM 1799) (Sporotrichum thermophile) |
G2QAB5 | LP9D_THET4 | MYRTLGSIALLAGGAAAHGAVTSYNIAGKDYPGYSGFAPTGQDVIQWQWPDYNPVLSASDPKLRCNGGTGAALYAEAAPGDTITATWAQWTHSQGPILVWMYKCPGDFSSCDGSGAGWFKIDEAGFHGDGTTVFLDTETPSGWDIAKLVGGNKSWSSKIPDGLAPGNYLVRHELIALHQANNPQFYPECAQIKVTGSGTAEPAASYKAAIPGYCQQSDPNISFNINDHSLPQEYKIPGPPVFKGTASAKARAFQA | 3.2.1.4 | COFACTOR: Name=Cu(2+); Xref=ChEBI:CHEBI:29036; Evidence={ECO:0000269|PubMed:28257189}; Note=Binds 1 copper ion per subunit. {ECO:0000269|PubMed:28257189}; | cellulose catabolic process [GO:0030245] | extracellular region [GO:0005576] | hydrolase activity [GO:0016787]; metal ion binding [GO:0046872] | PF03443; | 2.70.50.70; | Polysaccharide monooxygenase AA9 family | null | SUBCELLULAR LOCATION: Secreted {ECO:0000305|PubMed:29196788}. | CATALYTIC ACTIVITY: Reaction=Endohydrolysis of (1->4)-beta-D-glucosidic linkages in cellulose, lichenin and cereal beta-D-glucans.; EC=3.2.1.4; Evidence={ECO:0000269|PubMed:28257189, ECO:0000269|PubMed:29196788}; | null | null | null | null | FUNCTION: Lytic polysaccharide monooxygenase that depolymerizes crystalline and amorphous polysaccharides via the oxidation of scissile alpha- or beta-(1-4)-glycosidic bonds, yielding specifically C1 oxidation product (PubMed:28257189, PubMed:29196788). Catalysis by LPMOs requires the reduction of the active-site coppe... | Thermothelomyces thermophilus (strain ATCC 42464 / BCRC 31852 / DSM 1799) (Sporotrichum thermophile) |
G2QFD0 | LMCO1_THET4 | MLLSKLSILLAKWLSVAVYAGTLVHDEQFIPDHILRVSVAQVPSACENREDVVVNGTSPGPAIHLLPGARTWIRVYNDMNDRNLSMHWHGLSQRFAPFSDGTPSATQWPIPPGHFFDYEILTEPEDAGTYFYHSHVGMQALSCTGPLIVEDCGSSPYHYDDERILLFQDHFQKSDLEMIQGLTSTQFTWTGETRGILLNGRGVSPNQAAVQGRPGEASGFFGSHRFSNFRAGDGTSNSWDGIRGDDQIEPPTDCTLPVIDVEPGKTYRLRFIGATGLSLLTMGFEDHNDLTIVQVDGSEYNAPVTVDHIQLGGGQRFDVL... | 1.-.-.- | null | null | null | copper ion binding [GO:0005507]; ferroxidase activity [GO:0004322] | PF00394;PF07731;PF07732; | 2.60.40.420; | Multicopper oxidase family | PTM: N-glycosylation Asn-55 and Asn-83 is involved in folding, conformational stability and laccase activity. {ECO:0000269|PubMed:37326583}. | null | CATALYTIC ACTIVITY: Reaction=2 2',3,4-trihydroxy-trans-chalcone + 2 H(+) + O2 = 2 3',4'-dihydroxyaurone + 2 H2O; Xref=Rhea:RHEA:63848, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, ChEBI:CHEBI:144744, ChEBI:CHEBI:144745; Evidence={ECO:0000269|PubMed:30529567}; PhysiologicalDirection=left-to-right; Xref=Rhea:... | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=2.37 mM for ABTS {ECO:0000269|PubMed:30529567}; KM=2.41 mM for 2,6-dimethoxyphenol {ECO:0000269|PubMed:30529567}; | null | BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 4.0. {ECO:0000269|PubMed:30529567}; | BIOPHYSICOCHEMICAL PROPERTIES: Temperature dependence: Optimum temperature is 50 degrees Celsius. {ECO:0000269|PubMed:30529567}; | FUNCTION: Yellow laccase-like multicopper oxidase that is able to oxidize a variety of phenolic compounds including standard laccase substrates such as 2'-azino-bis(3-ethylbenzothiazoline-6-sulphonic acid) (ABTS) and 2,6-dimethoxyphenol (2,6-DMP) (PubMed:30529567, PubMed:37326583). The existence of an ortho-hydroxy gro... | Thermothelomyces thermophilus (strain ATCC 42464 / BCRC 31852 / DSM 1799) (Sporotrichum thermophile) |
G2QG48 | XYLO_THET4 | MHLLPLTVSATAVVSAASSPHAKRAAIDECLKNAKVPVTARNSTEWKTDASPFNDRLPYTPAAIAKPATVEHIQAAVLCAAEVGVKANPKSGGHSYASFGLGGEDGHLVVELDRMYNVTLDPETHIATVQPGARLGHIATVLYEEGKRAFSHGTCPGVGVGGHSLHGGFGFSSHSHGLAVDWITSADVVLANGSLVTASETENPDLFWALRGAGSNFGIVASFRFKTFAAPPNVTSYEINLPWTNSSNVVKGWGALQEWLLNGGMPEEMNMRVLGNAFQTQLQGLYHGNASALKTAIQPLLALLDANLSSVQEHDWMEGF... | 1.1.3.- | COFACTOR: Name=FAD; Xref=ChEBI:CHEBI:57692; Evidence={ECO:0000269|PubMed:27629413}; Note=Binds 1 FAD per subunit in a bicovalent manner. {ECO:0000269|PubMed:27629413}; | null | extracellular region [GO:0005576] | FAD binding [GO:0071949]; oxidoreductase activity [GO:0016491] | PF08031;PF01565; | 3.30.465.10;3.40.462.20; | Oxygen-dependent FAD-linked oxidoreductase family | PTM: The FAD cofactor is bound via a bicovalent 6-S-cysteinyl, 8alpha-N1-histidyl FAD linkage. {ECO:0000269|PubMed:27629413}. | SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:27629413}. | CATALYTIC ACTIVITY: Reaction=D-xylobiose + O2 = D-xylobiono-1,5-lactone + H2O2; Xref=Rhea:RHEA:59632, ChEBI:CHEBI:15379, ChEBI:CHEBI:16240, ChEBI:CHEBI:28309, ChEBI:CHEBI:143156; Evidence={ECO:0000269|PubMed:27629413}; CATALYTIC ACTIVITY: Reaction=D-xylotriose + O2 = D-xylotriono-1,5-lactone + H2O2; Xref=Rhea:RHEA:5963... | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=0.13 mM for oxygen {ECO:0000269|PubMed:27629413}; KM=342 mM for cellobiose {ECO:0000269|PubMed:27629413}; KM=532 mM for lactose {ECO:0000269|PubMed:27629413}; KM=359 mM for xylose {ECO:0000269|PubMed:27629413}; KM=1.15 mM for xylobiose {ECO:0000269|PubMed:27629413}... | null | BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 7. {ECO:0000269|PubMed:27629413}; | BIOPHYSICOCHEMICAL PROPERTIES: Temperature dependence: Optimum temperature is 30 degrees Celsius. Stable up to 60 degrees Celsius. {ECO:0000269|PubMed:27629413}; | FUNCTION: Catalyzes the selective oxidation of C1 hydroxyl moieties on mono-, oligo- and polysaccharides with concomitant reduction of molecular oxygen to hydrogen peroxide. This results in the formation of the corresponding lactones, which typically undergo spontaneous hydrolysis. Xylooligosaccharide oxidase is able t... | Thermothelomyces thermophilus (strain ATCC 42464 / BCRC 31852 / DSM 1799) (Sporotrichum thermophile) |
G2QND5 | FAEB_THET4 | MLVRSFLGFAVLAATCLAASLQEVTEFGDNPTNIQMYIYVPDQLDTNPPVIVALHPCGGSAQQWFSGTQLPSYADDNGFILIYPSTPHMSNCWDIQNPDTLTHGQGGDALGIVSMVNYTLDKHSGDSSRVYAMGFSSGGMMTNQLAGSYPDVFEAGAVYSGVAFGCAAGAESATPFSPNQTCAQGLQKTAQEWGDFVRNAYAGYTGRRPRMQIFHGLEDTLVRPQCAEEALKQWSNVLGVELTQEVSGVPSPGWTQKIYGDGTQLQGFFGQGIGHQSTVNEQQLLQWFGLI | 3.1.1.73 | null | xylan catabolic process [GO:0045493] | extracellular region [GO:0005576] | feruloyl esterase activity [GO:0030600] | PF10503; | 3.40.50.1820; | Carbohydrate esterase 1 (CE1) family, Feruloyl esterase type B subfamily | null | SUBCELLULAR LOCATION: Secreted {ECO:0000250}. | CATALYTIC ACTIVITY: Reaction=feruloyl-polysaccharide + H2O = ferulate + polysaccharide.; EC=3.1.1.73; Evidence={ECO:0000269|PubMed:22012339}; | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=0.27 mM for methyl ferulate (MFA) {ECO:0000269|PubMed:22012339}; KM=0.26 mM for methyl p-coumarate (MpCA) {ECO:0000269|PubMed:22012339}; KM=0.18 mM for methyl caffeate (MCA) {ECO:0000269|PubMed:22012339}; KM=0.21 mM for methyl sinapate (MSA) {ECO:0000269|PubMed:220... | null | BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 7.0. {ECO:0000269|PubMed:22012339}; | BIOPHYSICOCHEMICAL PROPERTIES: Temperature dependence: Optimum temperature is 50 degrees Celsius. {ECO:0000269|PubMed:22012339}; | FUNCTION: Feruloyl esterase which acts in synergy with xylanases in degradation of plant cell walls. Hydrolyzes the ester linkage of hydroxycinnamic acids (ferulic acid (FA) and p-coumaric acid) and diferulates present in plant cell walls. Is active on substrates containing ferulic acid ester linked to the C-5 and C-2 ... | Thermothelomyces thermophilus (strain ATCC 42464 / BCRC 31852 / DSM 1799) (Sporotrichum thermophile) |
G2QNH0 | ADT_THET4 | MSNKQETKILGMPPFVVDFLMGGVSAAVSKTAAAPIERIKLLVQNQDEMIKAGRLDRRYNGIIDCFRRTTADEGLMALWRGNTANVIRYFPTQALNFAFRDKFKAMFGYKKDKDGYAKWMAGNLASGGAAGATSLLFVYSLDYARTRLANDAKSAKGGGARQFNGLIDVYRKTLASDGIAGLYRGFGPSVAGIVVYRGLYFGMYDSIKPVVLVGPLANNFLASFLLGWCVTTGAGIASYPLDTVRRRMMMTSGEAVKYKSSIDAFRQIIAKEGVKSLFKGAGANILRGVAGAGVLSIYDQLQILLFGKAFKGGSG | null | null | mitochondrial ADP transmembrane transport [GO:0140021]; mitochondrial ATP transmembrane transport [GO:1990544]; negative regulation of mitochondrial outer membrane permeabilization involved in apoptotic signaling pathway [GO:1901029] | mitochondrial inner membrane [GO:0005743] | ATP:ADP antiporter activity [GO:0005471] | PF00153; | 1.50.40.10; | Mitochondrial carrier (TC 2.A.29) family | null | SUBCELLULAR LOCATION: Mitochondrion inner membrane {ECO:0000250|UniProtKB:P18239}; Multi-pass membrane protein {ECO:0000269|PubMed:30611538}. | CATALYTIC ACTIVITY: Reaction=ADP(in) + ATP(out) = ADP(out) + ATP(in); Xref=Rhea:RHEA:34999, ChEBI:CHEBI:30616, ChEBI:CHEBI:456216; Evidence={ECO:0000269|PubMed:30611538}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:35000; Evidence={ECO:0000269|PubMed:30611538}; | null | null | null | null | FUNCTION: ADP:ATP antiporter that mediates import of ADP into the mitochondrial matrix for ATP synthesis, and export of ATP out to fuel the cell (PubMed:30611538). Cycles between the cytoplasmic-open state (c-state) and the matrix-open state (m-state): operates by the alternating access mechanism with a single substrat... | Thermothelomyces thermophilus (strain ATCC 42464 / BCRC 31852 / DSM 1799) (Sporotrichum thermophile) |
G2TRN4 | ERH_SCHPO | MSPPPAESHIILLIQQGSDPKTRIWSDHCSLRSAIEYIVGVYQTNQAVSEKESIDVSRFFNFFDEIYDCVPLVYDRHFRAYIPHEKQWLLHHAQEYLTAARQIP | null | null | nuclear-transcribed mRNA catabolic process, meiosis-specific transcripts [GO:0033621]; regulation of siRNA-independent facultative heterochromatin formation [GO:1902801]; regulatory ncRNA 3'-end processing [GO:0043628] | ascospore-type prospore nucleus [GO:1905754]; cytoplasm [GO:0005737]; heterochromatin island [GO:1990342]; nuclear exosome focus [GO:1990251]; nucleoplasm [GO:0005654]; nucleus [GO:0005634]; rDNA heterochromatin [GO:0033553] | molecular function inhibitor activity [GO:0140678] | PF01133; | 3.30.2260.10; | E(R) family | null | SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:23145069, ECO:0000269|PubMed:26942678}. Cytoplasm {ECO:0000269|PubMed:23145069}. Note=Localizes to chromatin regions during vegetative growth, localizes to mei2 nuclear dots during meiosis. {ECO:0000269|PubMed:26942678}. | null | null | null | null | null | FUNCTION: Forms part of the erh1-mmi1 complex that recruits the CCR4-NOT complex and the NURS complex to target RNAs (PubMed:26942678, PubMed:30651569, PubMed:31974447). Suppresses the meiotic program during vegetative growth and promotes the meiotic program during mating (PubMed:31974447). Recruitment of the NURS comp... | Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast) |
G2WR64 | DMT5_VERDV | MAQKPQQFDVLGDTGARVDRPRDSLALIFKRALELGLDDVSQDGGVRFTVGTMCSGTDAPILALRELQDAALAMGYNHLFDFDHQFSVEIEAYKQAFIERNSKPSGEIYRDVIQVSDPSRKDAITAHGSLAPIPAAPDLLVAGSSCVDFSKLNNKRDILAKHSVLSRLYEEAKNTKNGLDFGTVTPQSQSHDVRMALQDVRDSFHTEGESVKTFGSILQFIYDQRPKLIILENVSHAPWRAFTHFWLPLVGYVALSMKVDSKNFLVPQTRTRGYLVAVDQWHYGTELSTRMARLWSSMMESSNWFPNQYPEVHKFLLSSM... | 3.6.4.- | null | methylation [GO:0032259]; nucleotide-excision repair [GO:0006289] | chromosome [GO:0005694]; nucleus [GO:0005634] | ATP binding [GO:0005524]; ATP-dependent chromatin remodeler activity [GO:0140658]; DNA binding [GO:0003677]; hydrolase activity [GO:0016787]; metal ion binding [GO:0046872]; methyltransferase activity [GO:0008168] | PF00271;PF00176; | 3.40.50.300;3.40.50.10810;3.40.50.150; | Class I-like SAM-binding methyltransferase superfamily, C5-methyltransferase family; SNF2/RAD54 helicase family | null | SUBCELLULAR LOCATION: Nucleus {ECO:0000305|PubMed:33941240}. Chromosome {ECO:0000305|PubMed:33941240}. | CATALYTIC ACTIVITY: Reaction=a 2'-deoxycytidine in DNA + ATP + H2O + S-adenosyl-L-methionine = a 5-methyl-2'-deoxycytidine in DNA + ADP + 2 H(+) + phosphate + S-adenosyl-L-homocysteine; Xref=Rhea:RHEA:68984, Rhea:RHEA-COMP:11369, Rhea:RHEA-COMP:11370, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI... | null | null | null | null | FUNCTION: May play a role in cytosine methylation at palindromic 5'-CG-3' and 5'-C[ACT]G-3' sites in DNA. {ECO:0000269|PubMed:33941240}. | Verticillium dahliae (strain VdLs.17 / ATCC MYA-4575 / FGSC 10137) (Verticillium wilt) |
G2X4G0 | 424Y_VERDV | MVSFTSLLAAFSVVSGVLTSPIAVVPEVNTALAKRTPSSTGTSGGFYYSFWTDTPNSVTYTNGDAGKFSVSWKNNNGNHVGGKGWRTGSARTIKYSGSYKPNGNSYLAIYGWTRSPLIEYYIVESFGTYNPSTGATSKGQFTVDGSVYDLYTSTRTNAPSIEGTRTFTQFWSVRRTKRTSGSVNTGAHFAAWKKAGMNLGSHDYQILAVEGYKSSGSATMTVS | 3.2.1.8 | null | effector-mediated perturbation of host innate immune response by symbiont [GO:0140404]; xylan catabolic process [GO:0045493] | extracellular region [GO:0005576]; host cell nucleus [GO:0042025] | endo-1,4-beta-xylanase activity [GO:0031176] | PF00457; | 2.60.120.180; | Glycosyl hydrolase 11 (cellulase G) family | null | SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:34233072}. Host nucleus {ECO:0000269|PubMed:34233072}. | CATALYTIC ACTIVITY: Reaction=Endohydrolysis of (1->4)-beta-D-xylosidic linkages in xylans.; EC=3.2.1.8; Evidence={ECO:0000255|PROSITE-ProRule:PRU01097}; | null | PATHWAY: Glycan degradation; xylan degradation. {ECO:0000255|PROSITE-ProRule:PRU01097}. | null | null | FUNCTION: Secreted effector that localizes to the host nucleus to contribute to the virulence process (PubMed:34233072). Induces host innate immunity responses; triggers BAK1-and SOBIR1-dependent cell death, salicylic acid signaling and jasmonic acid signaling (PubMed:34233072). {ECO:0000269|PubMed:34233072}. | Verticillium dahliae (strain VdLs.17 / ATCC MYA-4575 / FGSC 10137) (Verticillium wilt) |
G2X4M1 | ISC1_VERDV | MSSFRSMLGVPPSTASTQDSVLVIIDAQGEYAEGKLKISNIEASRPNISSLLEKYRAANAPIVHVVHETPAGAPLFTQGTKLAEIFDELTPKEGEAVVTKHHPGSFADTNLQEILEKSGKKKIVLVGYMAHVCVSTTARQGAQRGWDVIVAEDAVGDRDIPGVDAAQLVKVALAEIADVFGTLVSSKDIN | 3.3.2.1 | null | effector-mediated suppression of host innate immune response [GO:0140403] | extracellular region [GO:0005576]; host cell cytoplasm [GO:0030430]; host cell nucleus [GO:0042025] | isochorismatase activity [GO:0008908] | PF00857; | 3.40.50.850; | Isochorismatase family | null | SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:25156390}. Host cytoplasm {ECO:0000269|PubMed:25156390}. Host nucleus {ECO:0000269|PubMed:25156390}. Note=Lacks a signal peptide and uses an unconventional secretion pathway for delivering effectors which plays an important role in host-pathogen interactions. {ECO:0000... | CATALYTIC ACTIVITY: Reaction=H2O + isochorismate = (2S,3S)-2,3-dihydroxy-2,3-dihydrobenzoate + pyruvate; Xref=Rhea:RHEA:11112, ChEBI:CHEBI:15361, ChEBI:CHEBI:15377, ChEBI:CHEBI:29780, ChEBI:CHEBI:58764; EC=3.3.2.1; Evidence={ECO:0000269|PubMed:25156390}; | null | null | null | null | FUNCTION: Secreted isochorismatase required for full virulence of V.dahliae (PubMed:25156390). Suppresses salicylate-mediated innate immunity of the host by disrupting the plant salicylate metabolism pathway via hydrolysis of its isochorismate precursor (PubMed:25156390). {ECO:0000269|PubMed:25156390}. | Verticillium dahliae (strain VdLs.17 / ATCC MYA-4575 / FGSC 10137) (Verticillium wilt) |
G2X7W6 | ATC3_VERDV | MAGRPTGGPQGAPSHDLLLDLENDQPVYGGGQRSTLNDDDLMRTYTRDQESGQDQGRPSVSYDDFIGAGQSRQHGTGSQPGGPGQSSSSNNNNNNNVSAPYSRSGRQYSQTSDLGNYQRYADDFDDYPADGDSFYQQGGALNGGGADAAARHNARNRNSVLTMGGGFFGKMKNRLGMGQGYSEMDLPLTEPGGGGGGAGGGGHSRADSSGIDPPKRDKKFDMGNFKFGFGRSKPDPSTLGPRIIHLNNPPANAANKYVNNHVSTAKYNIATFLPKFLLEQFSKIANVFFLFTAALQQIPGLSPTNRFTTIIPLVAVLMVS... | 7.6.2.1 | COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250|UniProtKB:P39524}; | endocytic recycling [GO:0032456]; phospholipid translocation [GO:0045332]; post-Golgi vesicle-mediated transport [GO:0006892] | plasma membrane [GO:0005886]; trans-Golgi network membrane [GO:0032588] | ATP binding [GO:0005524]; ATP hydrolysis activity [GO:0016887]; magnesium ion binding [GO:0000287]; phosphatidylethanolamine flippase activity [GO:0090555]; phosphatidylserine floppase activity [GO:0090556] | PF13246;PF00122;PF16212;PF16209; | 3.40.1110.10;2.70.150.10;3.40.50.1000; | Cation transport ATPase (P-type) (TC 3.A.3) family, Type IV subfamily | null | SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:36072318}; Multi-pass membrane protein {ECO:0000255}. Golgi apparatus, trans-Golgi network membrane {ECO:0000269|PubMed:36072318}; Multi-pass membrane protein {ECO:0000255}. | CATALYTIC ACTIVITY: Reaction=ATP + H2O + phospholipidSide 1 = ADP + phosphate + phospholipidSide 2.; EC=7.6.2.1; Evidence={ECO:0000250|UniProtKB:P39524}; CATALYTIC ACTIVITY: Reaction=a 1,2-diacyl-sn-glycero-3-phospho-L-serine(out) + ATP + H2O = a 1,2-diacyl-sn-glycero-3-phospho-L-serine(in) + ADP + H(+) + phosphate; Xr... | null | null | null | null | FUNCTION: Catalytic component of a P4-ATPase flippase complex which catalyzes the hydrolysis of ATP coupled to the transport of phosphatidylserine and small amounts of ethanolamine from the lumen to the cytosolic leaflet of the trans-Golgi network and cell membrane and ensures the maintenance of asymmetric distribution... | Verticillium dahliae (strain VdLs.17 / ATCC MYA-4575 / FGSC 10137) (Verticillium wilt) |
G2XDH0 | SCP41_VERDV | MRTETASLLLLAALSVAEELTPNDVPLACANMCGPIVELSYKCDVDGTDELRKLKRRKLFSPQQQQQQQQQQQQSAPKAKRQADPEPQAPAPVPSSTNNQQAADVIFIPGSIGKFKTIPTPLPPADTGVPSMAVTPAAPAPTLPVLDLRPTTTPTNLNPNLPILATPILPSVPASTPLATASSTQVPLPVGNEADAGDGVDAGPAPSNSLNGNVGDMVDDAGNLWPGQKGRQAASDLETACICSNTSFNVRRVAGLCGDCLEQVSGDQGPMRAILASCNFTTERYEPEKESLVANVRVEATKPSFTQTAAASYSWRVSGP... | null | null | effector-mediated suppression of host innate immune response [GO:0140403] | extracellular region [GO:0005576]; host cell nucleus [GO:0042025] | transcription regulator inhibitor activity [GO:0140416] | null | null | null | null | SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:29757140}. Host nucleus {ECO:0000269|PubMed:29757140}. | null | null | null | null | null | FUNCTION: Effector that binds transcription regulators in the host plant to suppress the host's innate immune response (PubMed:29757140). Inhibits the host plant transcription regulators CBP60G and SARD1 (PubMed:29757140). {ECO:0000269|PubMed:29757140}. | Verticillium dahliae (strain VdLs.17 / ATCC MYA-4575 / FGSC 10137) (Verticillium wilt) |
G2XKQ0 | SUMO5_HUMAN | MSDLEAKPSTEHLGDKIKDEDIKLRVIGQDSSEIHFKVKMTTPLKKLKKSYCQRQGVPVNSLRFLFEGQRIADNHTPEELGMEEEDVIEVYQEQIGGHSTV | null | null | PML body organization [GO:0030578]; protein sumoylation [GO:0016925] | nucleus [GO:0005634]; PML body [GO:0016605] | identical protein binding [GO:0042802]; protein tag activity [GO:0031386]; transcription factor binding [GO:0008134]; ubiquitin-like protein ligase binding [GO:0044389] | PF11976; | null | Ubiquitin family, SUMO subfamily | PTM: Cleavage of precursor form is necessary for function. {ECO:0000250|UniProtKB:P63165}.; PTM: Autosumoylated at Lys-18. {ECO:0000269|PubMed:27211601}. | SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:27211601}. Note=Forms prominent non-membrane-bound structures in the nucleus. {ECO:0000269|PubMed:27211601}. | null | null | null | null | null | FUNCTION: Ubiquitin-like protein that can be covalently attached to proteins as a monomer or as a lysine-linked polymer. Regulates the life cycle of promyelocytic leukemia nuclear bodies (PML-NBs). PolySUMO1P1/SUMO5 conjugation on 'Lys-160' of PML facilitates recruitment of PML-NB components, which enlarges PML-NB. SUM... | Homo sapiens (Human) |
G3C7W6 | S2611_CAVPO | MPSSLKGLGQAWLSSSSMALSACCSVSAWQKRLPVLAWLPRYSLQWLKMDFIAGLSVGLTVIPQALAYAEVAGLPPQYGLYSAFTGCFVYVFLGTSRDVTLGPTAIMSLLVSFYTFHEPAYAVLLTFLSGCIQLAMGLLHLGFLLDFISCPVIKGFTSAAAIIIGFGQIKNLLGLHNIPRQFFLQVYHTFLSVGETRLGDAILGLVCMVLLLVLKLMRDRIPPVHPEMPLCVRLSCGLVWTTATARNALVVSFAALVAYSFEVTGYQPFILTGEIAKGLPPVRVPPFSVTMANGTVSFTRMVQDLGAGLAVVPLIGLLES... | null | null | oxalate transport [GO:0019532]; sulfate transport [GO:0008272] | apical plasma membrane [GO:0016324]; basolateral plasma membrane [GO:0016323]; endoplasmic reticulum [GO:0005783]; Golgi apparatus [GO:0005794]; lysosomal membrane [GO:0005765]; nucleoplasm [GO:0005654]; plasma membrane [GO:0005886] | chloride channel activity [GO:0005254]; chloride:bicarbonate antiporter activity [GO:0140900]; secondary active sulfate transmembrane transporter activity [GO:0008271] | PF01740;PF00916; | 3.30.750.24; | SLC26A/SulP transporter (TC 2.A.53) family | null | SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:Q86WA9}; Multi-pass membrane protein {ECO:0000255}. Lysosome membrane {ECO:0000250|UniProtKB:Q86WA9}; Multi-pass membrane protein {ECO:0000255}. Apical cell membrane {ECO:0000250|UniProtKB:Q80ZD3}; Multi-pass membrane protein {ECO:0000255}. Basolateral cell mem... | CATALYTIC ACTIVITY: Reaction=chloride(out) + hydrogencarbonate(in) = chloride(in) + hydrogencarbonate(out); Xref=Rhea:RHEA:72363, ChEBI:CHEBI:17544, ChEBI:CHEBI:17996; Evidence={ECO:0000269|PubMed:21593449}; CATALYTIC ACTIVITY: Reaction=H(+)(in) + sulfate(in) = H(+)(out) + sulfate(out); Xref=Rhea:RHEA:28574, ChEBI:CHEB... | null | null | null | null | FUNCTION: Sodium-independent anion exchanger mediating bicarbonate, chloride, sulfate and oxalate transport (PubMed:21593449). Exhibits sodium-independent sulfate anion transporter activity that may cooperate with SLC26A2 to mediate DIDS-sensitive sulfate uptake into high endothelial venules endothelial cells (HEVEC) (... | Cavia porcellus (Guinea pig) |
G3ECR1 | CAS9_STRTR | MLFNKCIIISINLDFSNKEKCMTKPYSIGLDIGTNSVGWAVITDNYKVPSKKMKVLGNTSKKYIKKNLLGVLLFDSGITAEGRRLKRTARRRYTRRRNRILYLQEIFSTEMATLDDAFFQRLDDSFLVPDDKRDSKYPIFGNLVEEKVYHDEFPTIYHLRKYLADSTKKADLRLVYLALAHMIKYRGHFLIEGEFNSKNNDIQKNFQDFLDTYNAIFESDLSLENSKQLEEIVKDKISKLEKKDRILKLFPGEKNSGIFSEFLKLIVGNQADFRKCFNLDEKASLHFSKESYDEDLETLLGYIGDDYSDVFLKAKKLYDA... | 3.1.-.- | COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000269|PubMed:22949671}; Note=Endonuclease activity on target DNA requires Mg(2+). {ECO:0000269|PubMed:22949671}; | defense response to virus [GO:0051607]; maintenance of CRISPR repeat elements [GO:0043571] | null | DNA binding [GO:0003677]; endonuclease activity [GO:0004519]; metal ion binding [GO:0046872]; RNA binding [GO:0003723] | PF16593;PF16595;PF16592;PF13395; | 1.10.30.50;3.30.420.10; | CRISPR-associated protein Cas9 family, Subtype II-A subfamily | null | null | null | null | null | null | null | FUNCTION: CRISPR (clustered regularly interspaced short palindromic repeat) is an adaptive immune system that provides protection against mobile genetic elements (viruses, transposable elements and conjugative plasmids). CRISPR clusters contain spacers, sequences complementary to antecedent mobile elements, and target ... | Streptococcus thermophilus |
G3FEX6 | POLG_JAEVM | MTKKPGGPGKNRAINMLKRGLPRVFPLVGVKRVVMSLLDGRGPVRFVLALITFFKFTALAPTKALLGRWRAVEKSVAMKHLTSFKRELGTLIDAVNKRGKKQNKRGGNESSIMWLASLAIVIACAGAMKLSNFQGKLLMTINNTDIADVIVIPTSKGENRCWVRAIDVGYMCEDTITYECPKLAVGNDPEDVDCWCDNQEVYVQYGRCTRTRHSKRSRRSVSVQTHGESSLVNKKEAWLDSTKATRYLMKTENWIIRNPGYAFLAAALGWMLGSNSGQRVVFTILLLLVAPAYSFNCLGMGNRDFIEGASGATWVDLVLE... | 2.1.1.56; 2.1.1.57; 2.7.7.48; 3.4.21.91; 3.6.1.15; 3.6.4.13 | COFACTOR: Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Note=For RNA-directed RNA polymerase NS5 activity; Mn(2+) is more effective than Mg(2+). {ECO:0000250|UniProtKB:P27395}; | clathrin-dependent endocytosis of virus by host cell [GO:0075512]; fusion of virus membrane with host endosome membrane [GO:0039654]; induction by virus of host autophagy [GO:0039520]; proteolysis [GO:0006508]; symbiont-mediated suppression of host JAK-STAT cascade via inhibition of host TYK2 activity [GO:0039574]; sym... | extracellular region [GO:0005576]; host cell endoplasmic reticulum membrane [GO:0044167]; host cell nucleus [GO:0042025]; host cell perinuclear region of cytoplasm [GO:0044220]; host cell surface [GO:0044228]; membrane [GO:0016020]; viral capsid [GO:0019028]; viral envelope [GO:0019031]; virion membrane [GO:0055036] | ATP binding [GO:0005524]; ATP hydrolysis activity [GO:0016887]; double-stranded RNA binding [GO:0003725]; metal ion binding [GO:0046872]; mRNA (nucleoside-2'-O-)-methyltransferase activity [GO:0004483]; mRNA 5'-cap (guanine-N7-)-methyltransferase activity [GO:0004482]; protein dimerization activity [GO:0046983]; RNA he... | PF20907;PF01003;PF07652;PF21659;PF02832;PF00869;PF01004;PF00948;PF01005;PF01002;PF01350;PF01349;PF00972;PF20483;PF01570;PF01728;PF00949; | 1.10.10.930;1.10.260.90;1.20.1280.260;2.40.10.120;2.60.40.350;1.10.8.970;2.60.260.50;3.30.70.2840;3.40.50.300;2.60.98.10;3.40.50.150;3.30.67.10;3.30.387.10; | Class I-like SAM-binding methyltransferase superfamily, mRNA cap 0-1 NS5-type methyltransferase family | PTM: [Genome polyprotein]: Specific enzymatic cleavages in vivo yield mature proteins (By similarity). Cleavages in the lumen of endoplasmic reticulum are performed by host signal peptidase, whereas cleavages in the cytoplasmic side are performed by serine protease NS3. Signal cleavage at the 2K-4B site requires a prio... | SUBCELLULAR LOCATION: [Genome polyprotein]: Host endoplasmic reticulum membrane {ECO:0000255}; Multi-pass membrane protein {ECO:0000255}.; SUBCELLULAR LOCATION: [Capsid protein C]: Virion {ECO:0000250|UniProtKB:P17763}. Host nucleus {ECO:0000250|UniProtKB:P17763}. Host cytoplasm {ECO:0000250|UniProtKB:P06935}. Host cyt... | CATALYTIC ACTIVITY: Reaction=Selective hydrolysis of -Xaa-Xaa-|-Yaa- bonds in which each of the Xaa can be either Arg or Lys and Yaa can be either Ser or Ala.; EC=3.4.21.91; Evidence={ECO:0000250|UniProtKB:P27395}; CATALYTIC ACTIVITY: Reaction=a ribonucleoside 5'-triphosphate + H2O = a ribonucleoside 5'-diphosphate + H... | null | null | null | null | FUNCTION: [Capsid protein C]: Plays a role in virus budding by binding to the cell membrane and gathering the viral RNA into a nucleocapsid that forms the core of a mature virus particle. During virus entry, may induce genome penetration into the host cytoplasm after hemifusion induced by the surface proteins. Can migr... | Japanese encephalitis virus (strain M28) (JEV) |
G3FNQ9 | SPAZ_ORBOL | MLTNGLISLLAIAGLATNAFAGPIRKVSNAGAAGAIADKYIVVLKKGLSDSAVSKHTNRISSFHSNVARDLTGARAHGVGRKFRFSSTGFNGYVGGFDKATLQEILNSPEVDYVEQDTVVTTYAEQTDSTWGLDRISHEDYSAPYTYEYDETAAGAGTTVYVIDTGIRISHDEFQTVNGSSRATWGFNSVDKTDSDGNGHGTHCAGTIAGKTYGVSKKAKVVAVKVLSAGGSGSTAGVVSGMNWVAENATPNFSVASMSLGGSKSTALNAAVDCIFNAGITIVVAAGNENQDAKNVSPASAPNAITVGAIDSSNKIASLS... | 3.4.21.- | null | collagen catabolic process [GO:0030574]; proteolysis [GO:0006508] | extracellular space [GO:0005615] | serine-type endopeptidase activity [GO:0004252] | PF05922;PF00082; | 3.30.70.80;3.40.50.200; | Peptidase S8 family | null | SUBCELLULAR LOCATION: Secreted {ECO:0000250}. | null | null | null | BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 6-8. {ECO:0000269|Ref.1}; | BIOPHYSICOCHEMICAL PROPERTIES: Temperature dependence: Optimum temperature is 45 degrees Celsius. {ECO:0000269|Ref.1}; | FUNCTION: Hydrolyzes gelatin, casein, the chromogenic substrate azocoll and the cuticle of the nematode P.redivivus. Immobilizes P.redivivus. {ECO:0000269|Ref.1}. | Orbilia oligospora (Nematode-trapping fungus) (Arthrobotrys oligospora) |
G3GTP0 | DNLI4_CRIGR | MATSQTSQTVAAHVPFADLCSTLERIQKSKERAEKIRHFKEFLDSWRKFHDALHKNKKDVTDSFYPAMRLILPQLERERMAYGIKETMLAKLYIELLNLPREGKDALKLLNYRTPSGARTDAGDFAVIAYFVLKPRCLQKGSLTIQQVNELLDLVASNNSGKRKDLVKKSLLQLITQSSALEQKWLIRMIIKDLKLGVSQQTILNIFHNDAVELHNVTTDLEKVCRQLHDPAVGLSDISITLFSAFKPMLAAVADVERVEKDMKQQSFYIETKLDGERMQMHKDGSVYQYFSRNGYNYTDQFGASPQEGTLTPFIHDAFR... | 6.5.1.1 | COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250|UniProtKB:P49917}; | cell cycle [GO:0007049]; cell division [GO:0051301]; cellular response to ionizing radiation [GO:0071479]; central nervous system development [GO:0007417]; chromosome organization [GO:0051276]; DN2 thymocyte differentiation [GO:1904155]; DNA biosynthetic process [GO:0071897]; DNA ligation involved in DNA recombination ... | condensed chromosome [GO:0000793]; DNA ligase IV complex [GO:0032807]; DNA-dependent protein kinase-DNA ligase 4 complex [GO:0005958]; nucleoplasm [GO:0005654] | ATP binding [GO:0005524]; DNA binding [GO:0003677]; DNA ligase (ATP) activity [GO:0003910]; magnesium ion binding [GO:0000287] | PF00533;PF04679;PF01068;PF04675;PF11411; | 6.10.250.520;3.40.50.10190;1.10.3260.10;3.30.470.30;2.40.50.140; | ATP-dependent DNA ligase family | null | SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:P49917}. | CATALYTIC ACTIVITY: Reaction=ATP + (deoxyribonucleotide)n-3'-hydroxyl + 5'-phospho-(deoxyribonucleotide)m = (deoxyribonucleotide)n+m + AMP + diphosphate.; EC=6.5.1.1; Evidence={ECO:0000255|PROSITE-ProRule:PRU10135}; | null | null | null | null | FUNCTION: DNA ligase involved in DNA non-homologous end joining (NHEJ); required for double-strand break (DSB) repair and V(D)J recombination. Catalyzes the NHEJ ligation step of the broken DNA during DSB repair by resealing the DNA breaks after the gap filling is completed. Joins single-strand breaks in a double-stran... | Cricetulus griseus (Chinese hamster) (Cricetulus barabensis griseus) |
G3HIK4 | CETP_CRIGR | MLAVTLLSLALLGSTCACSTSTSYEAGIVCRITKAALLVLNQETAKVIQTAFQRASYPDIKGERSMMLLGRVTYGLHNIQISHLSIASSQVELVEAKSVDVSIQNASVIFKGTLNYGYKGAWGLNIEQSVDFEIESAIDLQINTKLTCDSGHVRTDAPDCSISFHKLLLHLQGEREPGWTKQLFTNIISFTLKMVLKGQVCKEINVISNIMADFVQTRAANIISDRDIEVDISLTRSPIITATYLESHHKGHFIYKNISEVLPLPAFSPTLLGDTRMLYFWFSEQVLDSLAKAAFQDGRLQLNLAETELKVVLETWHFNP... | null | null | cholesterol homeostasis [GO:0042632]; cholesterol metabolic process [GO:0008203]; cholesterol transport [GO:0030301]; high-density lipoprotein particle remodeling [GO:0034375]; low-density lipoprotein particle remodeling [GO:0034374]; phosphatidylcholine metabolic process [GO:0046470]; phospholipid homeostasis [GO:0055... | extracellular space [GO:0005615]; high-density lipoprotein particle [GO:0034364] | cholesterol binding [GO:0015485]; cholesterol transfer activity [GO:0120020]; phosphatidylcholine binding [GO:0031210]; phospholipid transporter activity [GO:0005548]; triglyceride binding [GO:0017129] | PF01273;PF02886; | null | BPI/LBP/Plunc superfamily, BPI/LBP family | null | SUBCELLULAR LOCATION: Secreted {ECO:0000250|UniProtKB:P11597}. Note=Secreted in plasma. {ECO:0000250|UniProtKB:P11597}. | CATALYTIC ACTIVITY: Reaction=cholesteryl (9Z-octadecenoate)(in) = cholesteryl (9Z-octadecenoate)(out); Xref=Rhea:RHEA:43348, ChEBI:CHEBI:46898; Evidence={ECO:0000250|UniProtKB:P11597}; CATALYTIC ACTIVITY: Reaction=1,2,3-tri-(9Z-octadecenoyl)-glycerol(in) = 1,2,3-tri-(9Z-octadecenoyl)-glycerol(out); Xref=Rhea:RHEA:43352... | null | null | null | null | FUNCTION: Involved in the transfer of neutral lipids, including cholesteryl ester and triglyceride, among lipoprotein particles. Allows the net movement of cholesteryl ester from high density lipoproteins/HDL to triglyceride-rich very low density lipoproteins/VLDL, and the equimolar transport of triglyceride from VLDL ... | Cricetulus griseus (Chinese hamster) (Cricetulus barabensis griseus) |
G3HKI1 | XRCC4_CRIGR | MERKVSRISLASEPNITYFLQVSWEETVGSGFVITLTDGHSAWTATVSESEISQEADDMAMEKEKYADELRKALVSGSGSDTYKFIFSRESCHFSLEKELKDVSFRLGSFNLDKVPNSTEVIRELICYCLDTIAEKQAKNEHLQKENDRLLRDWNDVQGRFEKCVIAKEALEADLYQRFILVLNEKKTKIRSLHKLLDEIQQLEKNLKPERETKCSEKTTDQDAIYDGSTDEEAGASVLAEAAVCKEDSLFSSPDVTDIAPSRKRRHHMQKNLGTEPKMAPQEQQLQGKERLASSLPHTLKEEHEHTSAGNMSLETLRNS... | null | null | DNA ligation involved in DNA repair [GO:0051103]; double-strand break repair via nonhomologous end joining [GO:0006303]; immunoglobulin V(D)J recombination [GO:0033152]; response to X-ray [GO:0010165] | cytoplasm [GO:0005737]; DNA ligase IV complex [GO:0032807]; DNA-dependent protein kinase-DNA ligase 4 complex [GO:0005958]; nucleus [GO:0005634]; site of double-strand break [GO:0035861] | DNA binding [GO:0003677] | PF06632; | 1.20.5.370;2.170.210.10; | XRCC4-XLF family, XRCC4 subfamily | PTM: Phosphorylated by PRKDC at the C-terminus in response to DNA damage; Ser-253 constitutes the main phosphorylation sites. Phosphorylations by PRKDC at the C-terminus of XRCC4 and NHEJ1/XLF are highly redundant and regulate ability of the XRCC4-NHEJ1/XLF subcomplex to bridge DNA. Phosphorylation by PRKDC does not pr... | SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q13426}. Chromosome {ECO:0000250|UniProtKB:Q13426}. Note=Localizes to site of double-strand breaks. {ECO:0000250|UniProtKB:Q13426}.; SUBCELLULAR LOCATION: [Protein XRCC4, C-terminus]: Cytoplasm {ECO:0000250|UniProtKB:Q13426}. Note=Translocates from the nucleus to the... | null | null | null | null | null | FUNCTION: [DNA repair protein XRCC4]: DNA non-homologous end joining (NHEJ) core factor, required for double-strand break repair and V(D)J recombination (PubMed:18093953). Acts as a scaffold protein that regulates recruitment of other proteins to DNA double-strand breaks (DSBs). Associates with NHEJ1/XLF to form altern... | Cricetulus griseus (Chinese hamster) (Cricetulus barabensis griseus) |
G3I6Z6 | NOTC1_CRIGR | MGRSDSRAGALLEGGCEQNIDPRRAAHCHHPRLATSSLRCSQPSGTCLNGGRCEVANGTEACVCSGPFVGQRCQDPNPCLSTPCKNAGTCHVVEHGGTVNYACSCPLGFSGPLCLTPLDNACLANPCRNGGTCDLLTLTEYKCRCPPGWSGKSCQQADPCASNPCANGGQCLPFESSYICGCPPGFHGPTCRQDVNECSQNPGLCRHGGTCHNEIGSYRCVCRATHTGPHCELPYVPCSPSPCQNGGTCRPTGDTTHECACLPGFAGQNCEENVDDCPGNNCKNGGACVDGVNTYNCRCPPEWTGQYCTEDVDECQLMPN... | null | null | angiogenesis [GO:0001525]; cell differentiation [GO:0030154]; cilium assembly [GO:0060271]; Notch signaling involved in heart development [GO:0061314]; regulation of developmental process [GO:0050793]; regulation of DNA-templated transcription [GO:0006355] | adherens junction [GO:0005912]; apical plasma membrane [GO:0016324]; Golgi lumen [GO:0005796]; Golgi membrane [GO:0000139]; nucleus [GO:0005634] | calcium ion binding [GO:0005509]; signaling receptor activity [GO:0038023] | PF00023;PF12796;PF00008;PF07645;PF12661;PF06816;PF07684;PF00066; | 3.30.300.320;3.30.70.3310;1.25.40.20;2.10.25.10; | NOTCH family | PTM: Synthesized in the endoplasmic reticulum as an inactive form which is proteolytically cleaved by a furin-like convertase in the trans-Golgi network before it reaches the plasma membrane to yield an active, ligand-accessible form. Cleavage results in a C-terminal fragment N(TM) and a N-terminal fragment N(EC). Foll... | SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:Q01705}; Single-pass type I membrane protein {ECO:0000250|UniProtKB:Q01705}.; SUBCELLULAR LOCATION: [Notch 1 intracellular domain]: Nucleus {ECO:0000250|UniProtKB:Q01705}. Note=Following proteolytical processing NICD is translocated to the nucleus. Nuclear loca... | null | null | null | null | null | FUNCTION: Functions as a receptor for membrane-bound ligands Jagged-1 (JAG1), Jagged-2 (JAG2) and Delta-1 (DLL1) to regulate cell-fate determination. Upon ligand activation through the released notch intracellular domain (NICD) it forms a transcriptional activator complex with RBPJ/RBPSUH and activates genes of the enh... | Cricetulus griseus (Chinese hamster) (Cricetulus barabensis griseus) |
G3I8R9 | BIP_CRIGR | MKFPMVAAALLLLCAVRAEEEDKKEDVGTVVGIDLGTTYSCVGVFKNGRVEIIANDQGNRITPSYVAFTPEGERLIGDAAKNQLTSNPENTVFDAKRLIGRTWNDPSVQQDIKFLPFKVVEKKTKPYIQVDIGGGQTKTFAPEEISAMVLTKMKETAEAYLGKKVTHAVVTVPAYFNDAQRQATKDAGTIAGLNVMRIINEPTAAAIAYGLDKREGEKNILVFDLGGGTFDVSLLTIDNGVFEVVATNGDTHLGGEDFDQRVMEHFIKLYKKKTGKDVRKDNRAVQKLRREVEKAKRALSSQHQARIEIESFFEGEDFSE... | 3.6.4.10 | null | endoplasmic reticulum unfolded protein response [GO:0030968]; negative regulation of apoptotic process [GO:0043066]; negative regulation of cysteine-type endopeptidase activity involved in apoptotic process [GO:0043154]; negative regulation of IRE1-mediated unfolded protein response [GO:1903895]; negative regulation of... | cell surface [GO:0009986]; cytosol [GO:0005829]; endoplasmic reticulum chaperone complex [GO:0034663]; endoplasmic reticulum lumen [GO:0005788]; endoplasmic reticulum membrane [GO:0005789]; melanosome [GO:0042470]; mitochondrion [GO:0005739]; nucleus [GO:0005634]; perinuclear region of cytoplasm [GO:0048471] | ATP binding [GO:0005524]; ATP hydrolysis activity [GO:0016887]; ATP-dependent protein folding chaperone [GO:0140662] | PF00012; | 1.20.1270.10;3.30.420.40; | Heat shock protein 70 family | PTM: In unstressed cells, AMPylation at Thr-518 by FICD inactivates the chaperome activity: AMPylated form is locked in a relatively inert state and only weakly stimulated by J domain-containing proteins (PubMed:26673894, PubMed:27918543, PubMed:29064369, PubMed:29198525). In response to endoplasmic reticulum stress, d... | SUBCELLULAR LOCATION: Endoplasmic reticulum lumen {ECO:0000250|UniProtKB:P11021}. Melanosome {ECO:0000250|UniProtKB:P11021}. Cytoplasm {ECO:0000250|UniProtKB:P20029}. Cell surface. Note=Identified by mass spectrometry in melanosome fractions from stage I to stage IV (By similarity). Localizes to the cell surface in epi... | CATALYTIC ACTIVITY: Reaction=ATP + H2O = ADP + H(+) + phosphate; Xref=Rhea:RHEA:13065, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:456216; EC=3.6.4.10; Evidence={ECO:0000269|PubMed:29198525}; | null | null | null | null | FUNCTION: Endoplasmic reticulum chaperone that plays a key role in protein folding and quality control in the endoplasmic reticulum lumen (By similarity). Involved in the correct folding of proteins and degradation of misfolded proteins via its interaction with DNAJC10/ERdj5, probably to facilitate the release of DNAJC... | Cricetulus griseus (Chinese hamster) (Cricetulus barabensis griseus) |
G3J3K0 | FKS1_CORMM | MSGYQGGHHDQYDQGYGQAGHGDGYYQDDQYYDQGHGDHAAQGDHAAQGDHGAQGTQGDGYYDESGYYHADANNPYHQDGGYYDGHDQYQDDYYNNNQGYYDGEYNQGYAQGGRHPSEEESETFSDFTMRSDMARAAEMDYYGRGDEQYNGYGEGGRGYRPPSSQLSYGGNRSSGASTPNYGMEYGNGLASQRSKEPYPAWTSDAQIPLSKEEIEDIFLDLTSKFGFQRDSMRNMYDHLMTLLDSRASRMTPNQALLSLHADYIGGDNANYRKWYFAAHLDLDDAVGFANASTKNRKRKAKKGKKKGGEAGNEAETLQEL... | 2.4.1.34 | null | (1->3)-beta-D-glucan biosynthetic process [GO:0006075]; cell wall organization [GO:0071555]; fungal-type cell wall polysaccharide biosynthetic process [GO:0051278] | 1,3-beta-D-glucan synthase complex [GO:0000148] | 1,3-beta-D-glucan synthase activity [GO:0003843] | PF14288;PF02364; | null | Glycosyltransferase 48 family | null | SUBCELLULAR LOCATION: Membrane {ECO:0000269|PubMed:35816703}; Multi-pass membrane protein {ECO:0000255}. Cell membrane {ECO:0000250|UniProtKB:P38631}; Multi-pass membrane protein {ECO:0000255}. | CATALYTIC ACTIVITY: Reaction=[(1->3)-beta-D-glucosyl](n) + UDP-alpha-D-glucose = [(1->3)-beta-D-glucosyl](n+1) + H(+) + UDP; Xref=Rhea:RHEA:21476, Rhea:RHEA-COMP:11146, Rhea:RHEA-COMP:14303, ChEBI:CHEBI:15378, ChEBI:CHEBI:37671, ChEBI:CHEBI:58223, ChEBI:CHEBI:58885; EC=2.4.1.34; Evidence={ECO:0000269|PubMed:35816703}; | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=84.3 uM for UDP-glucose (at 37 degrees Celsius and pH 7) {ECO:0000269|PubMed:35816703}; Note=kcat is 1.42 min(-1) for UDP-glucose (at 37 degrees Celsius and pH 7). {ECO:0000269|PubMed:35816703}; | null | BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 7. {ECO:0000269|PubMed:35816703}; | BIOPHYSICOCHEMICAL PROPERTIES: Temperature dependence: Optimum temperature is 37 degrees Celsius. {ECO:0000269|PubMed:35816703}; | FUNCTION: Catalytic subunit of the 1,3-beta-glucan synthase (GS) (PubMed:35816703). Synthesizes 1,3-beta-glucan, a major structural component of the fungal cell wall (PubMed:35816703). Involved in cell wall synthesis, maintenance and remodeling (By similarity). {ECO:0000250|UniProtKB:P38631, ECO:0000269|PubMed:35816703... | Cordyceps militaris (strain CM01) (Caterpillar fungus) |
G3KIM8 | ACRC_ANAPI | MFLLKIKKERMKRMDFSLTREQEMLKKLARQFAEIELEPVAEEIDREHVFPAENFKKMAEIGLTGIGIPKEFGGSGGGTLEKVIAVSEFGKKCMASASILSIHLIAPQAIYKYGTKEQKETYLPRLTKGGELGAFALTEPNAGSDAGAVKTTAILDSQTNEYVLNGTKCFISGGGRAGVLVIFALTEPKKGLKGMSAIIVEKGTPGFSIGKVESKMGIAGSETAELIFEDCRVPAANLLGKEGKGFKIAMEALDGARIGVGAQAIGIAEGAIDLSVKYVHERIQFGKPIANLQGIQWYIADMATKTAAARALVEFAAYLE... | 1.3.1.95 | COFACTOR: Name=FAD; Xref=ChEBI:CHEBI:57692; Evidence={ECO:0000269|PubMed:12603323}; | leucine catabolic process [GO:0006552] | cytoplasm [GO:0005737] | acryloyl-CoA reductase (NADH) activity [GO:0043958]; FAD binding [GO:0071949]; isovaleryl-CoA dehydrogenase activity [GO:0008470]; oxidoreductase activity, acting on the CH-CH group of donors, NAD or NADP as acceptor [GO:0016628] | PF00441;PF02770;PF02771; | 1.10.540.10;2.40.110.10;1.20.140.10; | Acyl-CoA dehydrogenase family | null | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:12603323}. | CATALYTIC ACTIVITY: Reaction=NAD(+) + propanoyl-CoA = acryloyl-CoA + H(+) + NADH; Xref=Rhea:RHEA:34471, ChEBI:CHEBI:15378, ChEBI:CHEBI:57367, ChEBI:CHEBI:57392, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945; EC=1.3.1.95; Evidence={ECO:0000269|PubMed:12603323}; | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=2 uM for acryloyl-CoA (with NADH as electron acceptor at pH 7.5 and 25 degrees Celsius) {ECO:0000269|PubMed:12603323}; KM=8 uM for NADH (at pH 7.5 and 25 degrees Celsius) {ECO:0000269|PubMed:12603323}; KM=50 uM for propionyl-CoA (with of ferricenium hexafluorophosp... | null | BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is between 6.5 and 7. {ECO:0000269|PubMed:12603323}; | BIOPHYSICOCHEMICAL PROPERTIES: Temperature dependence: In the range between 25 and 55 degrees Celsius, the activity increases with rising temperature. Above 55 degrees Celsius, it decreases and becomes almost zero at 65 degrees Celsius. {ECO:0000269|PubMed:12603323}; | FUNCTION: Probable catalytic subunit of the acryloyl-CoA reductase complex involved in the pathway of L-alanine fermentation. Catalyzes the irreversible NADH-dependent formation of propionyl-CoA from acryloyl-CoA. It can also use 3-buten-2-one as substrate. {ECO:0000269|PubMed:12603323}. | Anaerotignum propionicum (Clostridium propionicum) |
G3LSH3 | NBCL_LOTJA | MSLEDSLRSLSLDYLNLLINGQAFSDVTFSVEGRLVHAHRCILAARSLFFRKFFCGPDPPPPSGNLDSPGGPRVNSPRPGGVIPVNSVGYEVFLLMLQFLYSGQVSIVPQKHEPRPNCGERACWHTHCTSAVDLALDTLAAARYFGVEQLALLTQKQLASMVEKASIEDVMKVLLASRKQDMHQLWTTCSHLVAKSGLPPEVLAKHLPIDIVAKIEELRLKSTLARRSLIPHHHHHHHHHGHHDMGAAADLEDQKIRRMRRALDSSDVELVKLMVMGEGLNLDEALALPYAVENCSREVVKALLELGAADVNYPSGPSGK... | null | null | induced systemic resistance, jasmonic acid mediated signaling pathway [GO:0009864]; plant organ development [GO:0099402]; regulation of DNA-templated transcription [GO:0006355] | nucleus [GO:0005634] | transcription cis-regulatory region binding [GO:0000976] | PF12796;PF00651;PF11900; | 1.25.40.20; | Plant 'ANKYRIN-BTB/POZ' family, 'NOOT-BOP-COCH-like' (NBCL) subfamily | null | SUBCELLULAR LOCATION: Nucleus {ECO:0000269|Ref.2}. Cytoplasm {ECO:0000269|Ref.2}. Cell membrane {ECO:0000269|Ref.2}; Peripheral membrane protein {ECO:0000269|Ref.2}; Cytoplasmic side {ECO:0000269|Ref.2}. | null | null | PATHWAY: Protein modification; protein ubiquitination. {ECO:0000250|UniProtKB:O22286}. | null | null | FUNCTION: May act as a substrate-specific adapter of an E3 ubiquitin-protein ligase complex (CUL3-RBX1-BTB) which mediates the ubiquitination and subsequent proteasomal degradation of target proteins (By similarity). Transcriptional co-regulator involved in the promotion of leaf and floral meristem fate and determinacy... | Lotus japonicus (Lotus corniculatus var. japonicus) |
G3MZR2 | FUT7_BOVIN | MQNAGLSPTPSLRALGGLAMAALLSTVWLWWRLGAAPGGAPAPQPTTTILVWHWPFASQPPELPGDTCTRYGVARCRLTVNRSLLAGADAVVFHHRELQTQQARLPLAERPRGQPWVWASMESPSHTRGLGRLRGVFNWVLSYRRDSDIFVPYGRLEPREGPAPPLPAKRGLAAWVVSNFQKRQRRVQLYRQLALHLRVDVFGRAAGQPLCASCLLRAVAGYRFYLSFENSEHRDYITEKFWRNALLAGAVPVVLGPPRAAYEAVAPPDAFVHVDDFGSARELAAFLTSMNESCYRRYFAWRDRFRVRLFSDWRERFCAI... | 2.4.1.- | null | fucosylation [GO:0036065]; inflammatory response [GO:0006954]; leukocyte migration involved in inflammatory response [GO:0002523]; lymphocyte migration into lymph node [GO:0097022]; positive regulation of cell adhesion [GO:0045785]; positive regulation of cell-cell adhesion [GO:0022409]; positive regulation of leukocyt... | membrane [GO:0016020] | 4-galactosyl-N-acetylglucosaminide 3-alpha-L-fucosyltransferase activity [GO:0017083]; alpha-(1->3)-fucosyltransferase activity [GO:0046920] | PF17039;PF00852; | 3.40.50.11660; | Glycosyltransferase 10 family | PTM: N-glycosylated. {ECO:0000250|UniProtKB:Q11130}. | SUBCELLULAR LOCATION: Membrane {ECO:0000255}; Single-pass membrane protein {ECO:0000255}. | CATALYTIC ACTIVITY: Reaction=an N-acetyl-alpha-neuraminyl-(2->3)-beta-D-galactosyl-(1->4)-N-acetyl-beta-D-glucosaminyl derivative + GDP-beta-L-fucose = an alpha-Neu5Ac-(2->3)-beta-D-Gal-(1->4)-[alpha-L-Fuc-(1->3)]-beta-D-GlcNAc derivative + GDP + H(+); Xref=Rhea:RHEA:56076, ChEBI:CHEBI:15378, ChEBI:CHEBI:57273, ChEBI:C... | null | PATHWAY: Protein modification; protein glycosylation. {ECO:0000250|UniProtKB:Q11130}. | null | null | FUNCTION: Catalyzes the transfer of L-fucose, from a guanosine diphosphate-beta-L-fucose, to the N-acetyl glucosamine (GlcNAc) of a distal alpha2,3 sialylated lactosamine unit of a glycoprotein or a glycolipid-linked sialopolylactosamines chain through an alpha-1,3 glycosidic linkage and participates in the final fucos... | Bos taurus (Bovine) |
G3MZY8 | RPB1_BOVIN | MHGGGPPSGDSACPLRTIKRVQFGVLSPDELKRMSVTEGGIKYPETTEGGRPKLGGLMDPRQGVIERTGRCQTCAGNMTECPGHFGHIELAKPVFHVGFLVKTMKVLRCVCFFCSKLLVDSNNPKIKDILAKSKGQPKKRLTHVYDLCKGKNICEGGEEMDNKFGVEQPEGDEDLTKEKGHGGCGRYQPRIRRSGLELYAEWKHVNEDSQEKKILLSPERVHEIFKRISDEECFVLGMEPRYARPEWMIVTVLPVPPLSVRPAVVMQGSARNQDDLTHKLADIVKINNQLRRNEQNGAAAHVIAEDVKLLQFHVATMVDN... | 2.7.7.48; 2.7.7.6; 3.1.13.- | COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000269|PubMed:26789250, ECO:0000269|PubMed:28892040}; Note=Two Mg(2+) ions are coordinated by both the catalytic residues and the nucleic acid substrate to enhance substrate recognition and catalytic efficiency. {ECO:0000250|UniProtKB:P24928, ECO:0000269|Pub... | null | cytoplasm [GO:0005737]; euchromatin [GO:0000791]; RNA polymerase II, core complex [GO:0005665] | core promoter sequence-specific DNA binding [GO:0001046]; DNA-directed 5'-3' RNA polymerase activity [GO:0003899]; DNA/RNA hybrid binding [GO:0071667]; hydrolase activity [GO:0016787]; magnesium ion binding [GO:0000287]; RNA polymerase II activity [GO:0001055]; RNA-dependent RNA polymerase activity [GO:0003968]; zinc i... | PF04997;PF00623;PF04983;PF05000;PF04998;PF04992;PF04990;PF05001; | 1.10.132.30;1.10.150.390;2.40.40.20;3.30.1360.140;6.10.250.2940;6.20.50.80;3.30.1490.180;4.10.860.120;1.10.274.100; | RNA polymerase beta' chain family | PTM: The tandem heptapeptide repeats in the C-terminal domain (CTD) can be highly phosphorylated. The phosphorylation activates Pol II. Phosphorylation occurs mainly at residues 'Ser-2' and 'Ser-5' of the heptapeptide repeat and is mediated, at least, by CDK7 and CDK9. CDK7 phosphorylation of POLR2A associated with DNA... | SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:P24928}. Cytoplasm {ECO:0000250|UniProtKB:P24928}. Chromosome {ECO:0000250|UniProtKB:P24928}. Note=Hypophosphorylated form is mainly found in the cytoplasm, while the hyperphosphorylated and active form is nuclear. Co-localizes with kinase SRPK2 and helicase DDX23 at... | CATALYTIC ACTIVITY: Reaction=a ribonucleoside 5'-triphosphate + RNA(n) = diphosphate + RNA(n+1); Xref=Rhea:RHEA:21248, Rhea:RHEA-COMP:14527, Rhea:RHEA-COMP:17342, ChEBI:CHEBI:33019, ChEBI:CHEBI:61557, ChEBI:CHEBI:140395; EC=2.7.7.6; Evidence={ECO:0000269|PubMed:16769904, ECO:0000269|PubMed:26789250}; PhysiologicalDirec... | null | null | null | null | FUNCTION: Catalytic core component of RNA polymerase II (Pol II), a DNA-dependent RNA polymerase which synthesizes mRNA precursors and many functional non-coding RNAs using the four ribonucleoside triphosphates as substrates (PubMed:16769904, PubMed:26789250). Pol II-mediated transcription cycle proceeds through transc... | Bos taurus (Bovine) |
G3QY98 | APOA1_GORGO | MKAAVLTLAVLFLTGSQARHFWQQDEPPQSPWDRVKDLATVYVDVLKDSGRDYVSQFEGSALGKQLNLKLLDNWDSVTSTFSKLREQLGPVTQEFWDNLEKETEGLRQEMSKDLEEVKAKVQPYLDDFQKKWQEEMELYRQKVEPLRAELQEGARQKLHELQEKLSPLGEEMRDRARAHVDALRTHLAPYSDELRQRLAARLEALKENGGARLAEYHAKATEHLSTLSEKAKPALEDLRQGLLPVLESFKVSFLSALEEYTKKLNTQ | null | null | acylglycerol homeostasis [GO:0055090]; adrenal gland development [GO:0030325]; blood vessel endothelial cell migration [GO:0043534]; cholesterol biosynthetic process [GO:0006695]; cholesterol efflux [GO:0033344]; cholesterol homeostasis [GO:0042632]; cholesterol import [GO:0070508]; cholesterol metabolic process [GO:00... | chylomicron [GO:0042627]; endocytic vesicle [GO:0030139]; extracellular vesicle [GO:1903561]; high-density lipoprotein particle [GO:0034364]; low-density lipoprotein particle [GO:0034362]; spherical high-density lipoprotein particle [GO:0034366]; very-low-density lipoprotein particle [GO:0034361] | amyloid-beta binding [GO:0001540]; apolipoprotein A-I receptor binding [GO:0034191]; chemorepellent activity [GO:0045499]; cholesterol binding [GO:0015485]; cholesterol transfer activity [GO:0120020]; enzyme binding [GO:0019899]; heat shock protein binding [GO:0031072]; high-density lipoprotein particle binding [GO:000... | PF01442; | 1.20.5.20;6.10.140.380;1.20.120.20; | Apolipoprotein A1/A4/E family | PTM: Glycosylated. {ECO:0000250}.; PTM: Palmitoylated. {ECO:0000250}.; PTM: Phosphorylation sites are present in the extracellular medium. {ECO:0000250}. | SUBCELLULAR LOCATION: Secreted. | null | null | null | null | null | FUNCTION: Participates in the reverse transport of cholesterol from tissues to the liver for excretion by promoting cholesterol efflux from tissues and by acting as a cofactor for the lecithin cholesterol acyltransferase (LCAT). As part of the SPAP complex, activates spermatozoa motility (By similarity). {ECO:0000250}. | Gorilla gorilla gorilla (Western lowland gorilla) |
G3UXB3 | NKX11_MOUSE | MSTSGPAAPGDVPALPPPPPGPGSGPAPPAPAATARDTMDGRAELPIFPRAGVPPLAASDTVPAVPEGAGAARPAAPPRPTSFSVLDILDPNKFNSRRRRCVLLGPVVPATCAPCAPAACVAVPAASGRSPRAELERRALSAATGVAAAAGAEPTSAGDSYRADEAEANGYSSGSGRSPTADSEDEAPEDEDEEEAPEVQDAQGTEEPRGGSGGLGARGSGCPGAAEVEASPVDDTAAPGPRGNSPGAPGPPATATGAGSAGSTPQGAAVTTKPKRKRTGSDSKSGKPRRARTAFTYEQLVALENKFKATRYLSVCERLN... | null | null | cell differentiation [GO:0030154]; lipid metabolic process [GO:0006629]; nervous system process [GO:0050877]; regulation of generation of precursor metabolites and energy [GO:0043467]; regulation of glucose metabolic process [GO:0010906]; regulation of transcription by RNA polymerase II [GO:0006357] | nucleus [GO:0005634] | DNA-binding transcription factor activity, RNA polymerase II-specific [GO:0000981]; RNA polymerase II cis-regulatory region sequence-specific DNA binding [GO:0000978] | PF00046; | 1.10.10.60; | NK-1 homeobox family | null | SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00108}. | null | null | null | null | null | FUNCTION: May be required for the coordinated crosstalk of factors involved in the maintenance of energy homeostasis, possibly by regulating the transcription of specific factors involved in energy balance. {ECO:0000269|PubMed:17879320, ECO:0000269|PubMed:21126319}. | Mus musculus (Mouse) |
G3UZ78 | ADGB_MOUSE | MASKQAKRKEVHRINSAHGSDKSKDLYHFGSNVPPGSFEQKKGKFPIWPEWSEADINAEKWDAGKGGKEKDKTAKSPIFHFFEDPEGKIELPQSLKVFSWKRPQDFIFSRTPVVVKNEITFDLFSPNEHLLCSELMRWIISEIYAVWKIFNGGILSNYHKGNLGELPILPWKPWEHIYSLCKAVKGHVPLFNSYGKYVVKLYWMGCWRKITVDDFLPFDEENNLLLPATSYEFELWPMLLSKAIIKLANVDVHVAHRRELGELTVIHALTGWLPEVIPLHPAYVDRVWELLKEILPEFKLTEEPSSESKITTIDNKLKEA... | null | null | proteolysis [GO:0006508]; spermatid development [GO:0007286]; spermatogenesis [GO:0007283] | sperm annulus [GO:0097227]; sperm flagellum [GO:0036126]; sperm midpiece [GO:0097225] | calcium-dependent cysteine-type endopeptidase activity [GO:0004198]; heme binding [GO:0020037]; metal ion binding [GO:0046872]; oxygen binding [GO:0019825] | PF00648; | 1.10.490.10; | Globin family; Peptidase C2 family | null | SUBCELLULAR LOCATION: Cell projection, cilium, flagellum {ECO:0000269|PubMed:35700329}. Note=Expressed within the midpiece and along the whole sperm flagellum (PubMed:35700329). Detected in the annulus of the sperm flagellum in S12 and S15 spermatids and mature sperm (PubMed:35700329). {ECO:0000269|PubMed:35700329}. | null | null | null | null | null | FUNCTION: Probable chimeric globin with a bis-histidyl six-coordinate heme-iron atom through which it could bind dioxygen, carbon monoxide and nitric oxide (By similarity). Required for sperm flagellum formation and maturation of elongating spermatids, thus playing an essential role in male fertility (PubMed:35700329, ... | Mus musculus (Mouse) |
G3V6S8 | SRSF6_RAT | MPRVYIGRLSYNVREKDIQRFFSGYGRLLEIDLKNGYGFVEFEDSRDADDAVYELNSKELCGERVIVEHARGPRRDRDGYSYGSRSGGGGYSSRRTSGRDKYGPPVRTEYRLIVENLSSRCSWQDLKDFMRQAGEVTYADAHKERTNEGVIEFRSYSDMKRALDKLDGTEINGRNIRLIEDKPRTSHRRSYSGSRSRSRSRRRSRSRSRRSSRSRSRSISKSRSRSRSRSKGRSRSRSKGRKSRSKSKSKPKSDRGSHSHSRSRSKDKYGKSRSRSRSRSPKENGKGDIKSKSRSRSQSRSHSPLPAPPSKARSMSPPPK... | null | null | alternative mRNA splicing, via spliceosome [GO:0000380]; mRNA splice site recognition [GO:0006376]; negative regulation of gene expression [GO:0010629]; negative regulation of keratinocyte differentiation [GO:0045617]; negative regulation of mRNA splicing, via spliceosome [GO:0048025]; negative regulation of type B pan... | cytoplasm [GO:0005737]; nuclear speck [GO:0016607]; nucleus [GO:0005634]; ribonucleoprotein complex [GO:1990904] | mRNA binding [GO:0003729]; pre-mRNA binding [GO:0036002]; RNA binding [GO:0003723] | PF00076; | 3.30.70.330; | Splicing factor SR family | PTM: Extensively phosphorylated on serine residues in the RS domain. Phosphorylated by DYRK1A, probably in the RS domain. Phosphorylation by DYRK1A modulates alternative splice site selection and inhibits the expression of MAPT/Tau exon 10 (By similarity). {ECO:0000250}. | SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:12549914}. Nucleus speckle {ECO:0000250|UniProtKB:Q13247}. | null | null | null | null | null | FUNCTION: Plays a role in constitutive splicing and modulates the selection of alternative splice sites. Plays a role in the alternative splicing of MAPT/Tau exon 10. Binds to alternative exons of TNC pre-mRNA and promotes the expression of alternatively spliced TNC. Plays a role in wound healing and in the regulation ... | Rattus norvegicus (Rat) |
G3V6U9 | SETD3_RAT | MGKKSRVKTQKSGTGATATVSPKEILNLTSELLQKCSSPAPGPGKEWEEYTQIRALVEKIRKKQKGLSVTFDGKREDYFPDLMKWASENGASVEGFEMVNFKEEGFGLRATRDIKAEELFLWVPRKLLMTVESAKNSILGPLYSQDRILQAMGNIALAFHLLCERASPNSFWQPYIQTLPSEYDTPLYFEEEEVRCLQSTQAIHDVFSQYKNTARQYAYFYKVIQTHPHANKLPLKDSFTYEDYRWAVSSVMTRQNQIPTEDGSRVTLALIPLWDMCNHTNGLITTGYNLEDDRCECVALQDFQAGDQIYIFYGTRSNAE... | 2.1.1.85 | null | actin modification [GO:0030047]; bioluminescence [GO:0008218]; peptidyl-histidine methylation [GO:0018021]; positive regulation of muscle cell differentiation [GO:0051149]; positive regulation of transcription by RNA polymerase II [GO:0045944]; regulation of uterine smooth muscle contraction [GO:0070472] | chromatin [GO:0000785]; cytoplasm [GO:0005737]; nucleus [GO:0005634] | actin binding [GO:0003779]; histone H3K36 methyltransferase activity [GO:0046975]; histone H3K4 methyltransferase activity [GO:0042800]; protein-L-histidine N-tele-methyltransferase activity [GO:0018064]; RNA polymerase II-specific DNA-binding transcription factor binding [GO:0061629]; transcription coactivator activit... | PF09273;PF00856; | 3.90.1420.10;3.90.1410.10; | Class V-like SAM-binding methyltransferase superfamily, SETD3 actin-histidine methyltransferase family | PTM: Phosphorylated by GSK3B, which is required for recognition by the SCF(FBXW7) complex and subsequent degradation. {ECO:0000250|UniProtKB:Q86TU7}.; PTM: Ubiquitinated by the SCF(FBXW7) complex following phosphorylation by GSK3B, leading to its degradation by the proteasome. {ECO:0000250|UniProtKB:Q86TU7}. | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q86TU7}. Nucleus {ECO:0000250|UniProtKB:Q91WC0}. Note=Localizes mainly in the cytoplasm. {ECO:0000250|UniProtKB:Q86TU7}. | CATALYTIC ACTIVITY: Reaction=L-histidyl-[protein] + S-adenosyl-L-methionine = H(+) + N(tele)-methyl-L-histidyl-[protein] + S-adenosyl-L-homocysteine; Xref=Rhea:RHEA:19369, Rhea:RHEA-COMP:9745, Rhea:RHEA-COMP:11600, ChEBI:CHEBI:15378, ChEBI:CHEBI:16367, ChEBI:CHEBI:29979, ChEBI:CHEBI:57856, ChEBI:CHEBI:59789; EC=2.1.1.8... | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=2.996 uM for beta-actin {ECO:0000269|PubMed:30526847}; KM=0.109 uM for S-adenosyl-L-methionine {ECO:0000269|PubMed:30526847}; Vmax=11.28 nmol/min/mg enzyme with beta-actin as substrate {ECO:0000269|PubMed:30526847}; Vmax=8.053 nmol/min/mg enzyme with S-adenosyl-L-m... | null | null | null | FUNCTION: Protein-histidine N-methyltransferase that specifically mediates 3-methylhistidine (tele-methylhistidine) methylation of actin at 'His-73' (PubMed:30526847). Histidine methylation of actin is required for smooth muscle contraction of the laboring uterus during delivery (By similarity). Does not have protein-l... | Rattus norvegicus (Rat) |
G3V7L1 | UTRN_RAT | MAKYGHLEASPDDGQNQFSDIIKSRSDEHNDVQKKTFTKWINARFSKSGKPPINDMFSDLKDGRKLLDLLEGLTGTSLPKERGSTRVHALNNVNRVLQVLHQNNVELVNIGGTDIVDGNPKLTLGLLWSIILHWQVKDVMKDIMSDLQQTNSEKILLSWVRQTTRPYSQVNVLNFTTSWTDGLAFNAVLHRHKPDLFSWDRVVKMSPTERLEHAFSKAHTYLGIEKLLDPEDVAVQLPDKKSIIMYLTSLFEVLPQQVTIDAIREVETLPRKYKKECEGEEINIQSAVLTEEGQSPRAETPSTVTEVDMDLDSYQIALEE... | null | null | neuromuscular junction development [GO:0007528]; positive regulation of cell-matrix adhesion [GO:0001954]; response to denervation involved in regulation of muscle adaptation [GO:0014894]; synaptic signaling [GO:0099536] | cortical actin cytoskeleton [GO:0030864]; cytoplasm [GO:0005737]; dystrophin-associated glycoprotein complex [GO:0016010]; filopodium [GO:0030175]; filopodium membrane [GO:0031527]; growth cone [GO:0030426]; neuromuscular junction [GO:0031594]; plasma membrane [GO:0005886]; postsynaptic membrane [GO:0045211]; protein-c... | actin binding [GO:0003779]; actin filament binding [GO:0051015]; integrin binding [GO:0005178]; protein kinase binding [GO:0019901]; vinculin binding [GO:0017166]; zinc ion binding [GO:0008270] | PF00307;PF09068;PF09069;PF00435;PF00569; | 1.20.58.60;2.20.70.10;3.30.60.90;1.10.418.10;1.10.238.10; | null | null | SUBCELLULAR LOCATION: Postsynaptic cell membrane {ECO:0000250|UniProtKB:P46939}; Peripheral membrane protein {ECO:0000250|UniProtKB:P46939}; Cytoplasmic side {ECO:0000250|UniProtKB:P46939}. Cytoplasm, cytoskeleton {ECO:0000250|UniProtKB:P46939}. Note=Neuromuscular junction. {ECO:0000250|UniProtKB:P46939}. | null | null | null | null | null | FUNCTION: May play a role in anchoring the cytoskeleton to the plasma membrane. {ECO:0000250}. | Rattus norvegicus (Rat) |
G3V7L5 | PO4F2_RAT | MMMMSLNSKQAFSMPHAGSLHVEPKYSALHSASPGSSAPAAPSASSPSSSSNAGSGGGGGGGGGGGGGGRSSSSSSSGSGGGGGGGSEAMRRACLPTPPSNIFGGLDESLLARAEALAAVDIVSQSKSHHHHPPHHSPFKPDATYHTMNTIPCTSAASSSSVPISHPSALAGTHHHHHHHHHHHHQPHQALEGELLEHLSPGLALGAMAGPDGTVVSTPAHAPHMATMNPMHQAALSMAHAHGLPSHMGCMSDVDADPRDLEAFAERFKQRRIKLGVTQADVGSALANLKIPGVGSLSQSTICRFESLTLSHNNMIALKP... | null | null | axon extension [GO:0048675]; axon guidance [GO:0007411]; axonogenesis [GO:0007409]; cellular response to cytokine stimulus [GO:0071345]; cellular response to estradiol stimulus [GO:0071392]; cellular response to insulin stimulus [GO:0032869]; cellular response to oxygen levels [GO:0071453]; dorsal root ganglion develop... | cytoplasm [GO:0005737]; euchromatin [GO:0000791]; nuclear speck [GO:0016607]; nucleus [GO:0005634]; transcription regulator complex [GO:0005667] | chromatin binding [GO:0003682]; DNA-binding transcription activator activity, RNA polymerase II-specific [GO:0001228]; DNA-binding transcription factor activity, RNA polymerase II-specific [GO:0000981]; DNA-binding transcription repressor activity, RNA polymerase II-specific [GO:0001227]; p53 binding [GO:0002039]; prom... | PF00046;PF00157; | 1.10.10.60;1.10.260.40; | POU transcription factor family, Class-4 subfamily | null | SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:18368538}. Nucleus speckle {ECO:0000250|UniProtKB:Q12837}. Cytoplasm {ECO:0000250|UniProtKB:Q63934}. | null | null | null | null | null | FUNCTION: Tissue-specific DNA-binding transcription factor involved in the development and differentiation of target cells. Functions either as activator or repressor modulating the rate of target gene transcription through RNA polymerase II enzyme in a promoter-dependent manner. Binds to the consensus octamer motif 5'... | Rattus norvegicus (Rat) |
G3V7P1 | STX12_RAT | MSYGPLDMYRNPGPSGPQPRDFNSIIQTCSGNIQRISQATAQIKNLMSQLGTKQDSSKLQENLQQFQHSTNQLAKETNELLKELGSLPLPLSASEQRQQKLQKERLMNDFSSALNNFQVVQRKVSEKEKESIARARAGSRLSAEDRQREEQLVSFDSHEEWNQMQSQEEEAAITEQDLELIKERETAIQQLEADILDVNQIFKDLAMMIHDQGDLIDSIEANVESSEVHVERASDQLQRAAYYQKKSRKKMCILVLVLSVIVTVLVVVIWVASK | null | null | autophagosome assembly [GO:0000045]; cholesterol efflux [GO:0033344]; endocytic recycling [GO:0032456]; intracellular protein transport [GO:0006886]; protein stabilization [GO:0050821]; regulation of postsynaptic membrane neurotransmitter receptor levels [GO:0099072]; synaptic vesicle to endosome fusion [GO:0016189]; v... | BLOC-1 complex [GO:0031083]; early endosome membrane [GO:0031901]; endomembrane system [GO:0012505]; Golgi membrane [GO:0000139]; membrane raft [GO:0045121]; phagocytic vesicle [GO:0045335]; phagophore assembly site [GO:0000407]; postsynaptic endosome membrane [GO:0098895]; postsynaptic recycling endosome [GO:0098837];... | SNAP receptor activity [GO:0005484]; SNARE binding [GO:0000149] | PF05739;PF14523; | 1.20.5.110;1.20.58.70; | Syntaxin family | null | SUBCELLULAR LOCATION: Endosome membrane; Single-pass type IV membrane protein {ECO:0000269|PubMed:9553086}. Golgi apparatus membrane; Single-pass type IV membrane protein {ECO:0000269|PubMed:9553086}. Endomembrane system {ECO:0000305}; Single-pass type IV membrane protein {ECO:0000305}; Cytoplasmic side {ECO:0000305}. ... | null | null | null | null | null | FUNCTION: SNARE promoting fusion of transport vesicles with target membranes (PubMed:17159904, PubMed:30962439). Together with SNARE STX6, promotes movement of vesicles from endosomes to the cell membrane, and may therefore function in the endocytic recycling pathway (PubMed:30962439). Through complex formation with GR... | Rattus norvegicus (Rat) |
G3V7R4 | FOXO1_RAT | MAEAPQVVETDPDFEPLPRQRSCTWPLPRPEFNQSNSTTSSPAPSGSTAANPDATASLASASAVSTDFMSNLSLLEESEDFARAPGCVAVAAAAAASRGLCGDFQGPEAGCVHSAPPQPPPTGPLSQPPPVPPAAAGPLAGQPRKTSSSRRNAWGNLSYADLITKAIESSAEKRLTLSQIYEWMVKSVPYFKDKGDSNSSAGWKNSIRHNLSLHSKFIRVQNEGTGKSSWWMLNPEGGKSGKSPRRRAASMDNNSKFAKSRGRAAKKKASLQSGQEGPGDSPGSQFSKWPASPGSHSNDDFDNWSTFRPRTSSNASTISG... | null | null | apoptotic process [GO:0006915]; autophagy [GO:0006914]; blood vessel development [GO:0001568]; canonical Wnt signaling pathway [GO:0060070]; cell differentiation [GO:0030154]; cellular response to dexamethasone stimulus [GO:0071549]; cellular response to hydrogen peroxide [GO:0070301]; cellular response to hyperoxia [G... | cytoplasm [GO:0005737]; nucleoplasm [GO:0005654]; nucleus [GO:0005634] | beta-catenin binding [GO:0008013]; chromatin DNA binding [GO:0031490]; DNA binding [GO:0003677]; DNA-binding transcription activator activity, RNA polymerase II-specific [GO:0001228]; DNA-binding transcription factor activity [GO:0003700]; DNA-binding transcription factor activity, RNA polymerase II-specific [GO:000098... | PF00250;PF16676;PF16675; | 1.10.10.10; | null | PTM: Phosphorylation by NLK promotes nuclear export and inhibits the transcriptional activity. In response to growth factors, phosphorylation on Thr-24, Ser-250 and Ser-313 by PKB/AKT1 promotes nuclear export and inactivation of transactivational activity (PubMed:19483080). Phosphorylation on Thr-24 is required for bin... | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:19483080}. Nucleus {ECO:0000250|UniProtKB:Q9R1E0}. Note=Shuttles between the cytoplasm and nucleus (By similarity). Largely nuclear in unstimulated cells (By similarity). In osteoblasts, colocalizes with ATF4 and RUNX2 in the nucleus. Serum deprivation increases local... | null | null | null | null | null | FUNCTION: Transcription factor that is the main target of insulin signaling and regulates metabolic homeostasis in response to oxidative stress (By similarity). Binds to the insulin response element (IRE) with consensus sequence 5'-TT[G/A]TTTTG-3' and the related Daf-16 family binding element (DBE) with consensus seque... | Rattus norvegicus (Rat) |
G3V7W1 | PDCD6_RAT | MAAYSYRPGPGAGPGPAAGAALPDQSFLWNVFQRVDKDRSGVISDNELQQALSNGTWTPFNPVTVRSIISMFDRENKAGVNFSEFTGVWKYITDWQNVFRTYDRDNSGMIDKHELKQALSGFGYRLSDQFHDILIRKFDRQGRGQIAFDDFIQGCIVLQRLTDIFRRYDTDQDGWIQVSYEQYLSMVFSIV | null | null | angiogenesis [GO:0001525]; apoptotic process [GO:0006915]; cellular response to heat [GO:0034605]; COPII vesicle coating [GO:0048208]; endoplasmic reticulum to Golgi vesicle-mediated transport [GO:0006888]; intracellular protein transport [GO:0006886]; negative regulation of phosphatidylinositol 3-kinase/protein kinase... | COPII vesicle coat [GO:0030127]; Cul3-RING ubiquitin ligase complex [GO:0031463]; cytoplasm [GO:0005737]; cytoplasmic vesicle [GO:0031410]; cytosol [GO:0005829]; endoplasmic reticulum [GO:0005783]; endoplasmic reticulum exit site [GO:0070971]; endoplasmic reticulum membrane [GO:0005789]; endosome [GO:0005768]; nucleopl... | calcium ion binding [GO:0005509]; calcium-dependent protein binding [GO:0048306]; identical protein binding [GO:0042802]; magnesium ion binding [GO:0000287]; protein dimerization activity [GO:0046983]; protein homodimerization activity [GO:0042803]; protein-macromolecule adaptor activity [GO:0030674]; protein-membrane ... | PF13499; | 1.10.238.10; | null | null | SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000269|PubMed:27276012}; Peripheral membrane protein {ECO:0000250|UniProtKB:O75340}. Cytoplasmic vesicle, COPII-coated vesicle membrane {ECO:0000250|UniProtKB:O75340}. Cytoplasm {ECO:0000250|UniProtKB:O75340}. Nucleus {ECO:0000250|UniProtKB:O75340}. Endosome {E... | null | null | null | null | null | FUNCTION: Calcium sensor that plays a key role in processes such as endoplasmic reticulum (ER)-Golgi vesicular transport, endosomal biogenesis or membrane repair (By similarity). Acts as an adapter that bridges unrelated proteins or stabilizes weak protein-protein complexes in response to calcium: calcium-binding trigg... | Rattus norvegicus (Rat) |
G3V7X8 | CP26B_RAT | MLFEGLELVSALATLAACLVSVTLLLAVSQQLWQLRWAATRDKSCKLPIPKGSMGFPLIGETGHWLLQGSGFQSSRREKYGNVFKTHLLGRPLIRVTGAENVRKILLGEHQLVSTEWPRSARVLLGPNTVANSIGDIHRNKRKVFSKIFSHEALESYLPKIQLVIQDTLRAWSSQPEAINVYQEAQRLTFRMAVRVLLGFSIPEEDLGNLFEVYQQFVENVFSLPVDLPFSGYRRGIQARQILQKGLEKAIREKLQCTQGKDYSDALDILIESSKEHGKEMTMQELKDGTLELIFAAYATTASASTSLIMQLLKHPAVLE... | 1.14.13.- | COFACTOR: Name=heme; Xref=ChEBI:CHEBI:30413; Evidence={ECO:0000250|UniProtKB:Q9Y6A2}; | bone morphogenesis [GO:0060349]; cell fate determination [GO:0001709]; cellular response to retinoic acid [GO:0071300]; cornification [GO:0070268]; embryonic limb morphogenesis [GO:0030326]; establishment of skin barrier [GO:0061436]; establishment of T cell polarity [GO:0001768]; inflammatory response [GO:0006954]; ki... | cytoplasm [GO:0005737]; endoplasmic reticulum membrane [GO:0005789] | all-trans retinoic acid 18-hydroxylase activity [GO:0062183]; heme binding [GO:0020037]; iron ion binding [GO:0005506]; monooxygenase activity [GO:0004497]; oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen, NAD(P)H as one donor, and incorporation of one atom of oxyge... | PF00067; | 1.10.630.10; | Cytochrome P450 family | null | SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000250|UniProtKB:O43174}; Peripheral membrane protein {ECO:0000250|UniProtKB:O43174}. Microsome membrane {ECO:0000250|UniProtKB:O43174}; Peripheral membrane protein {ECO:0000250|UniProtKB:O43174}. | CATALYTIC ACTIVITY: Reaction=all-trans-retinoate + O2 + reduced [NADPH--hemoprotein reductase] = all-trans-4-hydroxyretinoate + H(+) + H2O + oxidized [NADPH--hemoprotein reductase]; Xref=Rhea:RHEA:51984, Rhea:RHEA-COMP:11964, Rhea:RHEA-COMP:11965, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, ChEBI:CHEBI:352... | null | null | null | null | FUNCTION: A cytochrome P450 monooxygenase involved in the metabolism of retinoates (RAs), the active metabolites of vitamin A, and critical signaling molecules in animals (By similarity). RAs exist as at least four different isomers: all-trans-RA (atRA), 9-cis-RA, 13-cis-RA, and 9,13-dicis-RA, where atRA is considered ... | Rattus norvegicus (Rat) |
G3V893 | ZN335_RAT | MEENEVESSSDAAPRPGQPEEPSESGLGVGTSEAVSADSTDAATAPGLTEADDSGVGQSSDSGSRSVEEVSESISTEPLPQGYLPDSSSVSRGPVAEVPGGPPALVHSSALPDPSMLVSDCTASSSDLGSAIDKIIESTIGPDLIQSCITVTSGEEGGAETTQYLILQGPDDGAPMASSMSTSTLANSLAAIEALADGPTSTSTCLEPAEQPPGEPSSLAQPPAPVVEELDLQGLEAMMEVVVVQQFKCKMCQYRSSTKATLLRHMRERHFRPALAVAAAAAGKRGRVRKWGTSTKTTEEEGPEEEEEDDDIVDAGAIDD... | null | null | brain development [GO:0007420]; brain morphogenesis [GO:0048854]; cerebral cortex neuron differentiation [GO:0021895]; epigenetic regulation of gene expression [GO:0040029]; in utero embryonic development [GO:0001701]; neuron projection morphogenesis [GO:0048812]; positive regulation of lymphocyte proliferation [GO:005... | histone methyltransferase complex [GO:0035097]; nucleus [GO:0005634] | histone methyltransferase binding [GO:1990226]; metal ion binding [GO:0046872]; nuclear receptor coactivator activity [GO:0030374]; RNA polymerase II cis-regulatory region sequence-specific DNA binding [GO:0000978]; transcription cis-regulatory region binding [GO:0000976] | PF00096;PF13912;PF13909; | 3.30.160.60; | Krueppel C2H2-type zinc-finger protein family | null | SUBCELLULAR LOCATION: Nucleus {ECO:0000250}. | null | null | null | null | null | FUNCTION: Component or associated component of some histone methyltransferase complexes may regulate transcription through recruitment of those complexes on gene promoters (By similarity). Enhances ligand-dependent transcriptional activation by nuclear hormone receptors (By similarity). Plays an important role in neura... | Rattus norvegicus (Rat) |
G3V8D4 | APOC2_RAT | MGSRFFLALFLALLVLGNEVQGTEEDDPGSSALLDTVQEHLFSYWNSAKAAAGELYQKTYLTSVDEKLRDMYSKSSAAMTTYAGIFTDQLLTLLKGE | null | null | cholesterol efflux [GO:0033344]; chylomicron remnant clearance [GO:0034382]; high-density lipoprotein particle clearance [GO:0034384]; lipid catabolic process [GO:0016042]; lipoprotein transport [GO:0042953]; negative regulation of cholesterol transport [GO:0032375]; negative regulation of lipid metabolic process [GO:0... | chylomicron [GO:0042627]; extracellular space [GO:0005615]; intermediate-density lipoprotein particle [GO:0034363]; low-density lipoprotein particle [GO:0034362]; spherical high-density lipoprotein particle [GO:0034366]; very-low-density lipoprotein particle [GO:0034361] | lipase inhibitor activity [GO:0055102]; lipid binding [GO:0008289]; lipoprotein lipase activator activity [GO:0060230]; molecular function activator activity [GO:0140677]; phospholipase activator activity [GO:0016004]; phospholipase binding [GO:0043274] | PF05355; | 1.10.1440.10; | Apolipoprotein C2 family | PTM: Proapolipoprotein C-II is synthesized as a sialic acid containing glycoprotein which is subsequently desialylated prior to its proteolytic processing. {ECO:0000250|UniProtKB:P02655}.; PTM: Proapolipoprotein C-II, the major form found in plasma undergoes proteolytic cleavage of its N-terminal hexapeptide to generat... | SUBCELLULAR LOCATION: Secreted {ECO:0000250|UniProtKB:P02655}. | null | null | null | null | null | FUNCTION: Component of chylomicrons, very low-density lipoproteins (VLDL), low-density lipoproteins (LDL), and high-density lipoproteins (HDL) in plasma. Plays an important role in lipoprotein metabolism as an activator of lipoprotein lipase. {ECO:0000250|UniProtKB:P02655}. | Rattus norvegicus (Rat) |
G3V8H4 | CBLC_RAT | MAAATAPQGWQWGEPRALGRAVKLLQRLEEQCRDLRLFVGPPSLRDLLPRTAQLLREVAKARSDKTRGDPEGPGGAGDFLVIYLTNLEAKGRQVAELLPHRGKKDANQDVFPEGSRFRRQLAKLALIFSHMHAELSALFPEGKYCGHLYQITKGSANTFWRENCGVRCVLPWAEFQSLLCSCHPVEPGPIMQALRSTLDLTCSGHVSVFEFDIFTRLFQPWPTLLKNWQLLAVNHPGYMAFLTYDEVQTRLQAYRDKPGSYIFRPSCTRLGQWAIGYVSSNGSILQTIPLNKPLLQVLLKGQKDGIFLYPDGKNHNPDLT... | 2.3.2.27 | null | cell surface receptor signaling pathway [GO:0007166]; negative regulation of epidermal growth factor receptor signaling pathway [GO:0042059]; negative regulation of neuron apoptotic process [GO:0043524]; protein catabolic process [GO:0030163]; protein stabilization [GO:0050821]; protein ubiquitination [GO:0016567]; res... | membrane raft [GO:0045121]; plasma membrane [GO:0005886] | calcium ion binding [GO:0005509]; epidermal growth factor receptor binding [GO:0005154]; phosphotyrosine residue binding [GO:0001784]; receptor tyrosine kinase binding [GO:0030971]; SH3 domain binding [GO:0017124]; ubiquitin protein ligase activity [GO:0061630] | PF02262;PF02761;PF02762;PF13920; | 1.20.930.20;1.10.238.10;3.30.505.10;3.30.40.10; | null | PTM: Phosphorylated on multiple tyrosine residues by SRC. {ECO:0000250}.; PTM: Autoubiquitinated, when phosphorylated at Tyr-341. | null | CATALYTIC ACTIVITY: Reaction=S-ubiquitinyl-[E2 ubiquitin-conjugating enzyme]-L-cysteine + [acceptor protein]-L-lysine = [E2 ubiquitin-conjugating enzyme]-L-cysteine + N(6)-ubiquitinyl-[acceptor protein]-L-lysine.; EC=2.3.2.27; Evidence={ECO:0000250|UniProtKB:Q9ULV8}; | null | null | null | null | FUNCTION: Acts as an E3 ubiquitin-protein ligase, which accepts ubiquitin from specific E2 ubiquitin-conjugating enzymes, and then transfers it to substrates promoting their degradation by the proteasome. Functionally coupled with the E2 ubiquitin-protein ligases UB2D1, UB2D2 and UB2D3. Regulator of EGFR mediated signa... | Rattus norvegicus (Rat) |
G3V8V5 | KCNK4_RAT | MRSTTLLALLALVLLYLVSGALVFQALEQPHEQQVQKDLEDGRDQFLKDHPCVSQKNLEGFIKLVAEALGGGANPETSWTNSSNHSSAWNLGSAFFFSGTIITTIGYGNIALHTDAGRLFCIFYALVGIPLFGMLLAGVGDRLGSSLRRGIGHIEAVFLKWHVPPGLVRMLSAVLFLLIGCLLFVLTPTFVFSYMESWSKLEAIYFVIVTLTTVGFGDYVPGDGTGQNSPAYQPLVWFWILFGLAYFASVLTTIGNWLRAVSRRTRAEMGGLTAQAASWTGTVTARVTQRTGPSAPPPEKEQPLLPSSLPAPPAVAEPAH... | null | null | cellular response to alkaline pH [GO:0071469]; cellular response to fatty acid [GO:0071398]; cellular response to mechanical stimulus [GO:0071260]; cellular response to temperature stimulus [GO:0071502]; detection of mechanical stimulus involved in sensory perception of touch [GO:0050976]; memory [GO:0007613]; potassiu... | plasma membrane [GO:0005886]; potassium channel complex [GO:0034705] | mechanosensitived potassium channel activity [GO:0098782]; outward rectifier potassium channel activity [GO:0015271]; potassium channel activity [GO:0005267]; potassium ion leak channel activity [GO:0022841]; temperature-gated cation channel activity [GO:0097604] | PF07885; | 1.10.287.70; | Two pore domain potassium channel (TC 1.A.1.8) family | null | SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:11374070}; Multi-pass membrane protein {ECO:0000305}. | null | null | null | null | null | FUNCTION: Voltage-insensitive potassium channel (PubMed:11374070, PubMed:15677687). Channel opening is triggered by mechanical forces that deform the membrane, and by raising the intracellular pH to basic levels (PubMed:11374070, PubMed:15677687). The channel is inactive at 24 degrees Celsius (in vitro); raising the te... | Rattus norvegicus (Rat) |
G3V909 | ATF6A_RAT | MESPFSPVLPHGPGEDWESTLFAELGYFTDTDDVQFDAAHETYENNFDHLNFDLDLMPWESDIWSPSSHFCSDIKAEPQPLSPASSSCSVSSPRSTDSCSSTQHVPEELDLLSSSQSPLSLYGDSCHSPSSAEPLKEEKPVTGPGNKTEHGLTPKKKIQMSSKPSVQPKPLLLPAAPKTPANASVPAKTIIIQTLPALMPLAKQQSIISIQPAPTKGQTVLLSQPAVVQLQTPGVLPSAQPVLAVTGGATQLPNHVVNVVPAPVVNSPVNGKLCVTKPVLQSSTRSTGSDIAVLRRQQRMIKNRESACQSRKKKKEYMLG... | null | null | endoplasmic reticulum unfolded protein response [GO:0030968]; eye development [GO:0001654]; positive regulation of apoptotic process [GO:0043065]; positive regulation of ATF6-mediated unfolded protein response [GO:1903893]; positive regulation of autophagy [GO:0010508]; positive regulation of transcription by RNA polym... | endoplasmic reticulum [GO:0005783]; endoplasmic reticulum membrane [GO:0005789]; Golgi apparatus [GO:0005794]; Golgi membrane [GO:0000139]; membrane [GO:0016020]; nucleus [GO:0005634]; RNA polymerase II transcription regulator complex [GO:0090575] | DNA-binding transcription activator activity, RNA polymerase II-specific [GO:0001228]; DNA-binding transcription factor activity [GO:0003700]; DNA-binding transcription factor activity, RNA polymerase II-specific [GO:0000981]; enzyme binding [GO:0019899]; identical protein binding [GO:0042802]; protein heterodimerizati... | PF00170; | 1.20.5.170; | BZIP family, ATF subfamily | PTM: During unfolded protein response, a fragment of approximately 50 kDa containing the cytoplasmic transcription factor domain is released by proteolysis. The cleavage seems to be performed sequentially by site-1 (MBTPS1, S1P) and site-2 (MBTPS2, S2P) proteases (By similarity). {ECO:0000250|UniProtKB:P18850}.; PTM: N... | SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000269|PubMed:22682248}; Single-pass type II membrane protein {ECO:0000255}. Golgi apparatus membrane {ECO:0000250|UniProtKB:P18850}; Single-pass type II membrane protein {ECO:0000255}. Note=Translocates from the endoplasmic reticulum to the Golgi, where it is ... | null | null | null | null | null | FUNCTION: [Cyclic AMP-dependent transcription factor ATF-6 alpha]: Precursor of the transcription factor form (Processed cyclic AMP-dependent transcription factor ATF-6 alpha), which is embedded in the endoplasmic reticulum membrane. Endoplasmic reticulum stress promotes processing of this form, releasing the transcrip... | Rattus norvegicus (Rat) |
G3V928 | LRP1_RAT | MLTPPLLLLLPLLSALVAGATMDAPKTCSPKQFACRDQITCISKGWRCDGERDCPDGSDEAPEICPQSKAQRCPPNEHSCLGTELCVPMSRLCNGIQDCMDGSDEGAHCRELRVNCSRMGCQHHCVPTPSGPTCYCNNSFQLQADGKTCKDFDECSVYGTCSQLCTNTDGSFTCGCVEGYLLQPDNRSCKAKNEPVDRPPVLLIANSQNILATYLSGAQVSTITPTSTRQTTAMDFSYANETVCWVHVGDSAAQTQLKCARMPSLKGFVDEHTINISLSLHHVEQMAIDWLTGNFYFVDDIDDRIFVCNRNGDTCVTLLD... | null | null | amyloid-beta clearance [GO:0097242]; amyloid-beta clearance by cellular catabolic process [GO:0150094]; amyloid-beta clearance by transcytosis [GO:0150093]; aorta morphogenesis [GO:0035909]; apoptotic cell clearance [GO:0043277]; astrocyte activation involved in immune response [GO:0002265]; cardiac septum development ... | apical part of cell [GO:0045177]; axonal growth cone [GO:0044295]; basolateral plasma membrane [GO:0016323]; clathrin-coated pit [GO:0005905]; clathrin-coated vesicle [GO:0030136]; dendrite [GO:0030425]; early endosome [GO:0005769]; endosome [GO:0005768]; external side of plasma membrane [GO:0009897]; Golgi apparatus [... | alpha-2 macroglobulin receptor activity [GO:0016964]; apolipoprotein binding [GO:0034185]; calcium ion binding [GO:0005509]; cargo receptor activity [GO:0038024]; clathrin heavy chain binding [GO:0032050]; coreceptor activity [GO:0015026]; low-density lipoprotein particle receptor activity [GO:0005041]; protease bindin... | PF12662;PF16472;PF00008;PF07645;PF14670;PF00057;PF00058; | 4.10.1220.10;2.10.25.10;4.10.400.10;2.120.10.30; | LDLR family | PTM: Cleaved into a 85 kDa membrane-spanning subunit (LRP-85) and a 515 kDa large extracellular domain (LRP-515) that remains non-covalently associated. Gamma-secretase-dependent cleavage of LRP-85 releases the intracellular domain from the membrane. {ECO:0000250|UniProtKB:Q07954}.; PTM: Phosphorylated on serine and th... | SUBCELLULAR LOCATION: [Low-density lipoprotein receptor-related protein 1 85 kDa subunit]: Cell membrane {ECO:0000250|UniProtKB:Q07954}; Single-pass type I membrane protein {ECO:0000250|UniProtKB:Q07954}. Membrane, coated pit {ECO:0000250|UniProtKB:Q07954}.; SUBCELLULAR LOCATION: [Low-density lipoprotein receptor-relat... | null | null | null | null | null | FUNCTION: Endocytic receptor involved in endocytosis and in phagocytosis of apoptotic cells (By similarity). Required for early embryonic development (By similarity). Involved in cellular lipid homeostasis. Involved in the plasma clearance of chylomicron remnants and activated LRPAP1 (alpha 2-macroglobulin), as well as... | Rattus norvegicus (Rat) |
G3V9D0 | PGLT1_RAT | MERLSGCRLRPWMLLLLLFPVQGRQKDSGSKWKVFIDQINRALENYEPCSSQNCSCYHGVIEEDLTPFRGGISRKMMAEVVRRRLGTHYQIIKHRLFREDDCMFPSRCSGVEHFILEVIRRLPDMEMVINVRDYPQVPKWMEPTIPVFSFSKTSEYHDIMYPAWTFWEGGPAVWPLYPTGLGRWDLFREDLLRSAAQWPWEKKNSTAYFRGSRTSPERDPLILLSRKNPKLVDAEYTKNQAWKSMKDTLGKPAAKDVHLIDHCKYKYLFNFRGVAASFRFKHLFLCGSLVFHVGDEWVEFFYPQLKPWVHYIPVKTDLSD... | 2.4.1.376; 2.4.2.63 | null | axial mesoderm development [GO:0048318]; circulatory system development [GO:0072359]; gastrulation [GO:0007369]; muscle tissue development [GO:0060537]; paraxial mesoderm development [GO:0048339]; positive regulation of Notch signaling pathway [GO:0045747]; protein O-linked glycosylation [GO:0006493]; protein O-linked ... | endomembrane system [GO:0012505]; endoplasmic reticulum lumen [GO:0005788] | EGF-domain serine glucosyltransferase activity [GO:0140561]; EGF-domain serine xylosyltransferase activity [GO:0140562]; glucosyltransferase activity [GO:0046527]; UDP-glucosyltransferase activity [GO:0035251]; UDP-xylosyltransferase activity [GO:0035252] | PF05686; | null | Glycosyltransferase 90 family | null | SUBCELLULAR LOCATION: Endoplasmic reticulum lumen {ECO:0000269|PubMed:21949356}. | CATALYTIC ACTIVITY: Reaction=L-seryl-[EGF-like domain protein] + UDP-alpha-D-xylose = 3-O-(beta-D-xylosyl)-L-seryl-[EGF-like domain protein] + H(+) + UDP; Xref=Rhea:RHEA:62016, Rhea:RHEA-COMP:16010, Rhea:RHEA-COMP:16011, ChEBI:CHEBI:15378, ChEBI:CHEBI:29999, ChEBI:CHEBI:57632, ChEBI:CHEBI:58223, ChEBI:CHEBI:132085; EC=... | null | PATHWAY: Protein modification; protein glycosylation. {ECO:0000250|UniProtKB:Q8BYB9}. | null | null | FUNCTION: Dual specificity glycosyltransferase that catalyzes the transfer of glucose and xylose from UDP-glucose and UDP-xylose, respectively, to a serine residue found in the consensus sequence of C-X-S-X-P-C. Specifically targets extracellular EGF repeats of protein such as CRB2, F7, F9 and NOTCH2 (By similarity). A... | Rattus norvegicus (Rat) |
G3V9H8 | RET_RAT | MAKARSGAAGLGLKLFLLLPLLGEAPLGLYFSRDAYWERLYVDQPAGTPLLYVHALRDAPGEVPSFRLGQYLYGVYRTRLHENDWIHIDSGTGLLYLNQSLDHSSWEQLSIRNGGFPLLTVFLQVFLGSTAQREGECHWPGCARVYFSFINDTFPNCSSFKARDLCTPETGVSFRIRENRPPGTFYQFRMLPVQFLCPNISVKYKLLEGDGLPFRCDPDCLEVSTRWALDRELQEKYVLEAECAVAGPGANKEKVAVSFPVTVYDEDDSPPTFSGGVGTASAVVEFKRKEGTVVATLQVFDADVVPASGELVRRYTSTLL... | 2.7.10.1 | COFACTOR: Name=Ca(2+); Xref=ChEBI:CHEBI:29108; Evidence={ECO:0000250|UniProtKB:P07949}; | cellular response to retinoic acid [GO:0071300]; embryonic epithelial tube formation [GO:0001838]; enteric nervous system development [GO:0048484]; glial cell-derived neurotrophic factor receptor signaling pathway [GO:0035860]; homophilic cell adhesion via plasma membrane adhesion molecules [GO:0007156]; innervation [G... | axon [GO:0030424]; dendrite [GO:0030425]; early endosome [GO:0005769]; endosome membrane [GO:0010008]; neuronal cell body [GO:0043025]; plasma membrane [GO:0005886]; plasma membrane protein complex [GO:0098797]; receptor complex [GO:0043235] | ATP binding [GO:0005524]; calcium ion binding [GO:0005509]; transmembrane receptor protein tyrosine kinase activity [GO:0004714] | PF00028;PF07714;PF17756;PF17812;PF17813; | 2.60.40.60;1.10.510.10; | Protein kinase superfamily, Tyr protein kinase family | PTM: Autophosphorylated on C-terminal tyrosine residues upon ligand stimulation. {ECO:0000250|UniProtKB:P07949}.; PTM: Proteolytically cleaved by caspase-3. The soluble RET kinase fragment is able to induce cell death. The extracellular cell-membrane anchored RET cadherin fragment accelerates cell adhesion in sympathet... | SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:P07949}; Single-pass type I membrane protein {ECO:0000250|UniProtKB:P07949}. Endosome membrane {ECO:0000250|UniProtKB:P07949}; Single-pass type I membrane protein {ECO:0000250|UniProtKB:P07949}. Note=Predominantly located on the plasma membrane. In the presence... | 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-protein kinase involved in numerous cellular mechanisms including cell proliferation, neuronal navigation, cell migration, and cell differentiation in response to glia cell line-derived growth family factors (GDNF, NRTN, ARTN, PSPN and GDF15) (By similarity). In contrast to most receptor tyr... | Rattus norvegicus (Rat) |
G3V9M2 | JIP2_RAT | MADRAEMFSLSTFHSLSPPGCRPPQDISLEEFDDEDLSEITDDCGLGLSYDSDHCEKDSLSLGRSEQPHPICSFQDDFQEFEMIDDNEEEEDEEEEEEEEEEEDGDGDGRAGGGSGSQELSGESLIPSPSIEESHKLRPTTLHLTTLGAQDSLNNNSNGGFTSAPPSSWQETVLRSPVQEPLKELPAPLLPAEEEHHEVQSLARPGCDCEGNQPPEPPASGGASPSSDPGIEADLRSHSSGGHEGRRSSQELSSPGSDSEEAGGARLGRMISSISETELELSSDSGSSSGRSSHLTNSIEEASSPASEPEPEPEPEPLHE... | null | null | behavioral fear response [GO:0001662]; dendrite morphogenesis [GO:0048813]; excitatory postsynaptic potential [GO:0060079]; JNK cascade [GO:0007254]; mating behavior [GO:0007617]; negative regulation of apoptotic signaling pathway [GO:2001234]; nonassociative learning [GO:0046958]; positive regulation of stress-activat... | cytoplasm [GO:0005737]; neuronal cell body [GO:0043025]; postsynaptic density [GO:0014069]; protein-containing complex [GO:0032991] | JUN kinase binding [GO:0008432]; kinesin binding [GO:0019894]; MAP-kinase scaffold activity [GO:0005078]; protein kinase binding [GO:0019901]; protein-containing complex binding [GO:0044877] | PF00640;PF14604; | 2.30.29.30;2.30.30.40; | JIP scaffold family | null | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q13387}. Note=Accumulates in cell surface projections. {ECO:0000250|UniProtKB:Q13387}. | null | null | null | null | null | FUNCTION: The JNK-interacting protein (JIP) group of scaffold proteins selectively mediates JNK signaling by aggregating specific components of the MAPK cascade to form a functional JNK signaling module. JIP2 inhibits IL1 beta-induced apoptosis in insulin-secreting cells. {ECO:0000250}. | Rattus norvegicus (Rat) |
G3V9R8 | HNRPC_RAT | MASNVTNKTDPRSMNSRVFIGNLNTLVVKKSDVEAIFSKYGKIVGCSVHKGFAFVQYVNERNARAAVAGEDGRMIAGQVLDINLAAEPKVNRGKAGVKRSAAEMYGSSFDLDYDFQRDYYDRMYSYPARVPPPPPIARAVVPSKRQRVSGNTSRRGKSGFNSKSGQRGSSSKSVKGDDLQAIKKELTQIKQKVDSLLESLEKIEKEQSKQADLSFSSPVEMKNEKSEEEQSSASVKKDETNVKMESEAGADDSAEEGDLLDDDDNEDRGDDQLELKDDEKEPEEGEDDRDSANGEDDS | null | null | 3'-UTR-mediated mRNA stabilization [GO:0070935]; mRNA splicing, via spliceosome [GO:0000398]; negative regulation of mRNA modification [GO:0090367]; negative regulation of telomere maintenance via telomerase [GO:0032211] | actin cytoskeleton [GO:0015629]; catalytic step 2 spliceosome [GO:0071013]; cytosol [GO:0005829]; nucleoplasmic periphery of the nuclear pore complex [GO:1990826]; nucleus [GO:0005634]; pronucleus [GO:0045120]; protein-containing complex [GO:0032991]; spliceosomal complex [GO:0005681]; telomerase holoenzyme complex [GO... | deaminase binding [GO:1990827]; enzyme inhibitor activity [GO:0004857]; identical protein binding [GO:0042802]; mRNA 3'-UTR binding [GO:0003730]; mRNA binding [GO:0003729]; N6-methyladenosine-containing RNA reader activity [GO:1990247]; poly(U) RNA binding [GO:0008266]; protein domain specific binding [GO:0019904]; rib... | PF00076; | 3.30.70.330; | RRM HNRPC family, RALY subfamily | PTM: Phosphorylated on Ser-253 and Ser-291 in resting cells. {ECO:0000250|UniProtKB:P07910}.; PTM: Sumoylated. Sumoylation reduces affinity for mRNA. {ECO:0000250|UniProtKB:P07910}.; PTM: Ubiquitinated and degraded after nucleo-cytoplasmic transport by YWHAE. {ECO:0000250|UniProtKB:P07910}. | SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:P07910}. Note=Component of ribonucleosomes. {ECO:0000250|UniProtKB:P07910}. | null | null | null | null | null | FUNCTION: Binds pre-mRNA and nucleates the assembly of 40S hnRNP particles. Interacts with poly-U tracts in the 3'-UTR or 5'-UTR of mRNA and modulates the stability and the level of translation of bound mRNA molecules. Single HNRNPC tetramers bind 230-240 nucleotides. Trimers of HNRNPC tetramers bind 700 nucleotides. M... | Rattus norvegicus (Rat) |
G3V9T7 | GET3_RAT | MAAGVAGWGVEAEEFEDAPDVEPLEPTLSNIIEQRSLKWIFVGGKGGVGKTTCSCSLAVQLSKGRESVLIISTDPAHNISDAFDQKFSKVPTKVKGYDNLFAMEIDPSLGVAELPDEFFEEDNMLSMGKKMMQEAMSAFPGIDEAMSYAEVMRLVKGMNFSVVVFDTAPTGHTLRLLNFPTIVERGLGRLMQIKNQISPFISQMCNMLGLGDMNADQLASKLEETLPVIRSVSEQFKDPEQTTFICVCIAEFLSLYETERLIQELAKCKIDTHNIIVNQLVFPDPEKPCKMCEARHKIQAKYLDQMEDLYEDFHIVKLPL... | 3.6.-.- | null | post-translational protein targeting to endoplasmic reticulum membrane [GO:0006620]; tail-anchored membrane protein insertion into ER membrane [GO:0071816] | endoplasmic reticulum membrane [GO:0005789]; GET complex [GO:0043529]; nucleolus [GO:0005730]; nucleoplasm [GO:0005654] | ATP binding [GO:0005524]; ATP hydrolysis activity [GO:0016887]; membrane insertase activity [GO:0032977]; metal ion binding [GO:0046872] | PF02374; | 3.40.50.300; | ArsA ATPase family | null | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_03112}. Endoplasmic reticulum {ECO:0000255|HAMAP-Rule:MF_03112}. Nucleus, nucleolus {ECO:0000255|HAMAP-Rule:MF_03112}. | null | null | null | null | null | FUNCTION: ATPase required for the post-translational delivery of tail-anchored (TA) proteins to the endoplasmic reticulum. Recognizes and selectively binds the transmembrane domain of TA proteins in the cytosol. This complex then targets to the endoplasmic reticulum by membrane-bound receptors GET1/WRB and CAMLG/GET2, ... | Rattus norvegicus (Rat) |
G3X745 | GPC1_BOVIN | MELRARGWWLLYAAAVLVACARGDPASKSRSCGEVRQIYGAKGFSLSDVPQAEISGEHLRICPQGYTCCTSEMEENLANRSRAELETALLEGTRALQATLAAQQRGFDDHFQRLLNDSERALQEAFPGAFGELYTQNAKAFRDLYAELRLYYGGANLHLQETLAEFWARLLERLFRQLHPQLLLPDDYLDCLGKQAEPLRPFGEAPRELRLRATRAFVAARTFVQGLGVAGDVVRKVAKVPLSPECSRAVMKLVYCAHCLGVPGARPCPDYCRNVLKGCLANQADLDAEWRNLLDSMVLITDKFWGPSGAESVVGGVHYW... | null | null | cell migration [GO:0016477]; heparan sulfate proteoglycan catabolic process [GO:0030200]; negative regulation of fibroblast growth factor receptor signaling pathway [GO:0040037]; positive regulation of skeletal muscle cell differentiation [GO:2001016]; regulation of protein localization to membrane [GO:1905475] | cell surface [GO:0009986]; collagen-containing extracellular matrix [GO:0062023]; endosome [GO:0005768]; extracellular matrix [GO:0031012]; extracellular region [GO:0005576]; membrane raft [GO:0045121]; plasma membrane [GO:0005886]; side of membrane [GO:0098552]; synapse [GO:0045202] | copper ion binding [GO:0005507]; fibroblast growth factor binding [GO:0017134]; laminin binding [GO:0043236] | PF01153; | null | Glypican family | PTM: S-nitrosylated in a Cu(2+)-dependent manner. Nitric acid (NO) is released from the nitrosylated cysteines by ascorbate or by some other reducing agent, in a Cu(2+) or Zn(2+) dependent manner. This free nitric oxide is then capable of cleaving the heparan sulfate side chains (By similarity). {ECO:0000250}.; PTM: N-... | SUBCELLULAR LOCATION: Cell membrane {ECO:0000250}; Lipid-anchor, GPI-anchor {ECO:0000250}; Extracellular side {ECO:0000250}. Endosome {ECO:0000250}. Note=S-nitrosylated form recycled in endosomes. Localizes to CAV1-containing vesicles close to the cell surface. Cleavage of heparan sulfate side chains takes place mainly... | null | null | null | null | null | FUNCTION: Cell surface proteoglycan that bears heparan sulfate. Binds, via the heparan sulfate side chains, alpha-4 (V) collagen and participates in Schwann cell myelination (By similarity). May act as a catalyst in increasing the rate of conversion of prion protein PRPN (C) to PRNP (Sc) via associating (via the hepara... | Bos taurus (Bovine) |
G3X8Y1 | TRI55_MOUSE | MSTSLNYKSFSKEQQTMDNLEKQLICPICLEMFTKPVVILPCQHNLCRKCASDIFQASNPYLPTRGGTTVASGGRFRCPSCRHEVVLDRHGVYGLQRNLLVENIIDIYKQESTRPEKKLDQPMCEEHEEERINIYCLNCEVPTCSLCKVFGAHKDCQVAPLTHVFQRQKSELSDGIAVLVGSNDRVQGVISQLEDTCKTIEECCRKQKQDLCEKFDHLYGILEERKTEMTQAITRTQEEKLEHVRTLIRKYSDHLENVSKLVESGIQFMDEPEMAVFLQNAKTLLQKIVEASKAFQMEKLEQGYEIMSNFTVNLNREEKI... | 2.3.2.27 | null | diapedesis [GO:0050904]; leukocyte migration involved in inflammatory response [GO:0002523]; macrophage migration [GO:1905517]; positive regulation of non-canonical NF-kappaB signal transduction [GO:1901224]; protein K48-linked ubiquitination [GO:0070936]; protein ubiquitination [GO:0016567] | cytoplasm [GO:0005737]; nucleus [GO:0005634] | identical protein binding [GO:0042802]; protein-macromolecule adaptor activity [GO:0030674]; ubiquitin protein ligase activity [GO:0061630]; zinc ion binding [GO:0008270] | PF00643;PF13445; | 1.20.5.170;3.30.160.60;3.30.40.10; | null | PTM: Targeted for degradation through the proteasomal and lysosomal pathways in the presence of SUMO3. {ECO:0000250|UniProtKB:Q9BYV6}. | SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:29435413}. Cytoplasm {ECO:0000269|PubMed:29435413}. Note=TLR4 signaling pathway promotes nuclear translocation. {ECO:0000269|PubMed:29435413}. | CATALYTIC ACTIVITY: Reaction=S-ubiquitinyl-[E2 ubiquitin-conjugating enzyme]-L-cysteine + [acceptor protein]-L-lysine = [E2 ubiquitin-conjugating enzyme]-L-cysteine + N(6)-ubiquitinyl-[acceptor protein]-L-lysine.; EC=2.3.2.27; Evidence={ECO:0000250|UniProtKB:Q9BYV6}; | null | null | null | null | FUNCTION: E3 ubiquitin ligase that plays an important role in regulating cardiac development and contractility, muscle growth, metabolism, and fiber-type differentiation. Acts as a critical factor that regulates cardiomyocyte size during development in concert with TRIM63 by regulating E2F1-mediated gene expression (Pu... | Mus musculus (Mouse) |
G3X912 | SPRTN_MOUSE | MDEDLVVALRLQEEWDVQMARRAAAAREPVSLVDASWELVDPTPDLQALFLQFNDRFFWGQLEAVEVKWSVRMTLCAGICTYEGRGGMCSIRLSEPLLKLRPRKDLVETLLHEMIHAYLFVTNNDKDREGHGPEFCKHMHRINQLTGANITVYHTFHDEVDEYRRHWWRCNGPCQHRQPYYGYVKRATNRAPSVHDYWWADHQKTCGGTYIKIKEPENYSKKGRGKTKADKQPASAVENKDKLCRGEAQLLIPFSGKGYVLGDASTCPSAGKLNTSYMVNEAKGLSSQDHSVSGLRLNSNAEVKCEQNCLPKKPHLVSPL... | 3.4.24.- | COFACTOR: Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000250|UniProtKB:Q9H040}; | DNA damage response [GO:0006974]; positive regulation of protein ubiquitination [GO:0031398]; protein autoprocessing [GO:0016540]; protein-DNA covalent cross-linking repair [GO:0106300]; proteolysis [GO:0006508]; response to UV [GO:0009411]; translesion synthesis [GO:0019985] | chromatin [GO:0000785]; nuclear speck [GO:0016607]; nucleus [GO:0005634] | double-stranded DNA binding [GO:0003690]; K63-linked polyubiquitin modification-dependent protein binding [GO:0070530]; metal ion binding [GO:0046872]; metalloendopeptidase activity [GO:0004222]; polyubiquitin modification-dependent protein binding [GO:0031593]; single-stranded DNA binding [GO:0003697]; ubiquitin bindi... | PF10263; | 3.30.160.60; | Spartan family | PTM: Autocatalytically cleaved in response to double-stranded DNA-binding: autocatalytic cleavage takes place in trans and leads to inactivation. {ECO:0000250|UniProtKB:Q9H040}.; PTM: Monoubiquitinated; monoubiquitination promotes exclusion from chromatin. Deubiquitinated by VCPIP1: deubiquitination is required for sub... | SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q9H040}. Chromosome {ECO:0000250|UniProtKB:Q9H040}. Note=Localizes to sites of UV damage via the PIP-box. Recruited to stalled replication forks at sites of replication stress following deubiquitination. CHEK1 stimulates recruitment to chromatin. {ECO:0000250|UniProt... | null | null | null | null | null | FUNCTION: DNA-dependent metalloendopeptidase that mediates the proteolytic cleavage of covalent DNA-protein cross-links (DPCs) during DNA synthesis, thereby playing a key role in maintaining genomic integrity (PubMed:27871365, PubMed:28199696). DPCs are highly toxic DNA lesions that interfere with essential chromatin t... | Mus musculus (Mouse) |
G3X939 | SL9A3_MOUSE | MWHRALGPGWKLLLALALTSLQGARGAEEEPSSDGSFQVVTFKWHHVQDPYIIALWILVASLAKIVFHLSHKVTSIVPESALLIVLGLVLGGIVWAADHIASFTLTPTLFFFYLLPPIVLDAGYFMPNRLFFGNLGTILLYAVIGTIWNAATTGLSLYGVFLSGLMGELKIGLLDFLLFGSLIAAVDPVAVLAVFEEVHVNEVLFIIVFGESLLNDAVTVVLYNVFESFVTLGGDAVTGVDCVKGIVSFFVVSLGGTLVGVIFAFLLSLVTRFTKHVRIIEPGFVFVISYLSYLTSEMLSLSSILAITFCGICCQKYVKA... | null | null | potassium ion transmembrane transport [GO:0071805]; receptor-mediated endocytosis [GO:0006898]; regulation of intracellular pH [GO:0051453]; regulation of pH [GO:0006885]; regulation of sodium ion transport [GO:0002028]; sodium ion import across plasma membrane [GO:0098719]; sodium ion transport [GO:0006814] | apical plasma membrane [GO:0016324]; brush border [GO:0005903]; brush border membrane [GO:0031526]; early endosome membrane [GO:0031901]; plasma membrane [GO:0005886]; recycling endosome membrane [GO:0055038]; vesicle [GO:0031982] | identical protein binding [GO:0042802]; PDZ domain binding [GO:0030165]; phosphatidylinositol binding [GO:0035091]; potassium:proton antiporter activity [GO:0015386]; sodium:proton antiporter activity [GO:0015385] | PF00999; | 6.10.140.1330; | Monovalent cation:proton antiporter 1 (CPA1) transporter (TC 2.A.36) family | PTM: Phosphorylated by PKA, which inhibits activity. Phosphorylation at Ser-659 by SGK1 is associated with increased abundance at the cell membrane. Phosphorylation at Ser-714 by CSNK2A1 regulates SLC9A3 activity through the formation of multiple signaling complexes (By similarity). {ECO:0000250|UniProtKB:P26432, ECO:0... | SUBCELLULAR LOCATION: Apical cell membrane {ECO:0000250|UniProtKB:P48764}; Multi-pass membrane protein {ECO:0000250|UniProtKB:P48764}. Cell membrane {ECO:0000250|UniProtKB:P48764}; Multi-pass membrane protein {ECO:0000250|UniProtKB:P48764}. Recycling endosome membrane {ECO:0000250|UniProtKB:P48764}; Multi-pass membrane... | CATALYTIC ACTIVITY: Reaction=H(+)(out) + Na(+)(in) = H(+)(in) + Na(+)(out); Xref=Rhea:RHEA:29419, ChEBI:CHEBI:15378, ChEBI:CHEBI:29101; Evidence={ECO:0000250|UniProtKB:P48764}; | null | null | null | null | FUNCTION: Plasma membrane Na(+)/H(+) antiporter. Exchanges intracellular H(+) ions for extracellular Na(+) in 1:1 stoichiometry, playing a key role in salt and fluid absorption and pH homeostasis (By similarity). Major apical Na(+)/H(+) exchanger in kidney and intestine playing an important role in renal and intestine ... | Mus musculus (Mouse) |
G3X943 | S39A2_MOUSE | MEVLLGVKIGCLLALLVLTLGCGLTPIYVKWFQMDAATGHHHRVLSLLGCTSAGVFLGAGLMHMTAEALEGIESEIQKFVEQNSTGSKGNSSRDAASSYVEYPYGELVISLGFFFVFLLESLALQCCHGAAGGSTVQEEEWGGTHAFGFHKHPAVPSPSRGPLRALVLLLSLSFHSVFEGLAVGLQATVAATIQLCVAVLAHKGLVVFSVGLRLGKIGTGPRWATFCILSLALMSPVGLALGLTVAGGASGQTQGLAQAVLEGIAAGTFLYVTFLEILPRELACPEAPLAKYSCVAAGFAFMALIALWA | null | null | cadmium ion transmembrane transport [GO:0070574]; keratinocyte differentiation [GO:0030216]; zinc ion transmembrane transport [GO:0071577]; zinc ion transport [GO:0006829] | cytoplasmic ribonucleoprotein granule [GO:0036464]; cytoplasmic vesicle [GO:0031410]; plasma membrane [GO:0005886] | metal ion binding [GO:0046872]; zinc ion transmembrane transporter activity [GO:0005385] | PF02535; | null | ZIP transporter (TC 2.A.5) family | null | SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:Q9NP94}; Multi-pass membrane protein {ECO:0000255}. | CATALYTIC ACTIVITY: Reaction=Zn(2+)(in) = Zn(2+)(out); Xref=Rhea:RHEA:29351, ChEBI:CHEBI:29105; Evidence={ECO:0000269|PubMed:14525987}; PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:29353; Evidence={ECO:0000305|PubMed:14525987}; CATALYTIC ACTIVITY: Reaction=Cd(2+)(in) = Cd(2+)(out); Xref=Rhea:RHEA:28707, ChEBI:C... | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=1.6 uM for Zn(2+) {ECO:0000269|PubMed:14525987}; | null | null | null | FUNCTION: Transporter for the divalent cation Zn(2+). Mediates the influx of Zn(2+) into cells from extracellular space (PubMed:14525987). The Zn(2+) uniporter activity is independent of H(+)-driving force, but is modulated by extracellular pH and membrane potential. Transports also other divalent cations Zn(2+), Cd2(+... | Mus musculus (Mouse) |
G3X982 | AOXC_MOUSE | MSPSKESDELIFFVNGKKVTERNADPEVNLLFYLRKVIRLTGTKYGCGGGDCGACTVMISRYDPISKRISHFSATACLVPICSLHGAAVTTVEGIGSTKTRIHPVQERIAKGHGTQCGFCTPGMVMSIYTLLRNHPEPSTEQIMETLGGNLCRCTGYRPIVESAKSFCPSSTCCQMNGEGKCCLDEEKNEPERKNSVCTKLYEKKEFQPLDPTQELIFPPELMRMAEESQNTVLTFRGERTTWIAPGTLNDLLELKMKHPSAPLVIGNTYLGLHMKFTDVSYPIIISPARILELFVVTNTKQGLTLGAGLSLTQVKNVLS... | 1.17.3.-; 1.2.3.1 | COFACTOR: Name=[2Fe-2S] cluster; Xref=ChEBI:CHEBI:190135; Evidence={ECO:0000269|PubMed:11562361}; Note=Binds 2 [2Fe-2S] clusters per subunit. {ECO:0000269|PubMed:11562361}; COFACTOR: Name=FAD; Xref=ChEBI:CHEBI:57692; Evidence={ECO:0000269|PubMed:11562361}; Note=Binds 1 FAD per subunit. {ECO:0000269|PubMed:11562361}; CO... | xenobiotic metabolic process [GO:0006805] | cytosol [GO:0005829] | 2 iron, 2 sulfur cluster binding [GO:0051537]; aldehyde oxidase activity [GO:0004031]; electron transfer activity [GO:0009055]; FAD binding [GO:0071949]; flavin adenine dinucleotide binding [GO:0050660]; iron ion binding [GO:0005506]; molybdenum ion binding [GO:0030151]; molybdopterin cofactor binding [GO:0043546]; NAD... | PF01315;PF03450;PF00941;PF00111;PF01799;PF02738;PF20256; | 3.10.20.30;3.30.465.10;1.10.150.120;3.90.1170.50;3.30.365.10;3.30.390.50;3.30.43.10; | Xanthine dehydrogenase family | null | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:11562361, ECO:0000269|PubMed:15383531}. | CATALYTIC ACTIVITY: Reaction=an aldehyde + H2O + O2 = a carboxylate + H(+) + H2O2; Xref=Rhea:RHEA:16829, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, ChEBI:CHEBI:16240, ChEBI:CHEBI:17478, ChEBI:CHEBI:29067; EC=1.2.3.1; Evidence={ECO:0000269|PubMed:11562361, ECO:0000269|PubMed:21705476, ECO:0000269|PubMed:23... | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=2.3 uM for phthalazine {ECO:0000269|PubMed:11562361, ECO:0000269|PubMed:21705476, ECO:0000269|PubMed:23019336}; KM=1.4 uM for phthalazine (at 37 degrees Celsius and pH 8) {ECO:0000269|PubMed:11562361, ECO:0000269|PubMed:21705476, ECO:0000269|PubMed:23019336}; KM=2.... | null | null | null | FUNCTION: Oxidase with broad substrate specificity, oxidizing aromatic azaheterocycles, such as N1-methylnicotinamide and phthalazine, as well as aldehydes, such as benzaldehyde, retinal and pyridoxal. Plays a key role in the metabolism of xenobiotics and drugs containing aromatic azaheterocyclic substituents. Is proba... | Mus musculus (Mouse) |
G3X9J0 | SI1L3_MOUSE | MTTYRPLPNDGVDLAASCGARSTDILPGPHPGDYTPMGFWAQNGSMPQPLGESPAATTTRPSPTTPAMPKMGVRARVADWPPKRDALREQSNPSPSQDTDGVKTTKVAHSMRNLQNGQLPSSTPASSGSRAFHRLSRRRSKDVEFQDGWPRSPGRAFLPLRHRSSSEITLSECDVEEPGDPRGTRHPGVLPLFREYGSTSSIDVQGVPEQSFFDILNEFRSEQPEARGSQNLRELLQVDPGALSGGSCGTKGDPRNGQPTKDSLQSLQPLKEKEKSRKKPVRGLGSGDTVDSSIFRKLRSSKPEGEVGRPLGETEESRSP... | null | null | cytoskeleton organization [GO:0007010]; epithelial cell morphogenesis [GO:0003382]; establishment of epithelial cell polarity [GO:0090162]; eye development [GO:0001654]; hematopoietic progenitor cell differentiation [GO:0002244]; regulation of small GTPase mediated signal transduction [GO:0051056] | apical part of cell [GO:0045177]; apical plasma membrane [GO:0016324]; cytoplasm [GO:0005737]; Golgi apparatus [GO:0005794]; nucleoplasm [GO:0005654]; plasma membrane [GO:0005886]; stress fiber [GO:0001725]; tricellular tight junction [GO:0061689] | GTPase activator activity [GO:0005096] | PF21022;PF02145;PF11881; | 2.30.42.10;6.10.140.210;3.40.50.11210; | null | null | SUBCELLULAR LOCATION: Apical cell membrane {ECO:0000250|UniProtKB:O60292}. Note=Detected in tricellular junctions. Colocalizes with apical F-actin. {ECO:0000250|UniProtKB:O60292}. | null | null | null | null | null | FUNCTION: Plays a critical role in epithelial cell morphogenesis, polarity, adhesion and cytoskeletal organization in the lens (PubMed:26231217). {ECO:0000269|PubMed:26231217}. | Mus musculus (Mouse) |
G3X9K3 | BIG1_MOUSE | MYEGKKTKNMFLTRALEKILADKEVKKAHHSQLRKACEVALEEIKVETEKQSPPHGEAKAGSGTLPPVKSKTNFIEADKYFLPFELACQSKCPRIVSTSLDCLQKLIAYGHLTGRAPDSTTPGKKLIDRIIETICGCFQGPQTDEGVQLQIIKALLTAVTSQHIEIHEGTVLQAVRTCYNIYLASKNLINQTTAKATLTQMLNVIFARMENQALQEAKQMERERHRQQQHLLQSPVSHHEPESPHLRYLPPQTVDHINQEHEGDLEPQTHDVDKSLQDDTEPENGSDISSAENEQTEADQATAAETLSKNDILYDGDYEE... | null | null | endomembrane system organization [GO:0010256]; Golgi organization [GO:0007030]; negative regulation of actin filament polymerization [GO:0030837]; negative regulation of GTPase activity [GO:0034260]; neuron projection development [GO:0031175]; positive regulation of phosphatidylinositol 3-kinase/protein kinase B signal... | cytosol [GO:0005829]; Golgi membrane [GO:0000139]; nuclear matrix [GO:0016363]; nucleolus [GO:0005730]; nucleoplasm [GO:0005654]; perinuclear region of cytoplasm [GO:0048471]; small nuclear ribonucleoprotein complex [GO:0030532]; trans-Golgi network [GO:0005802] | guanyl-nucleotide exchange factor activity [GO:0005085]; myosin binding [GO:0017022]; protein kinase A regulatory subunit binding [GO:0034237] | PF20252;PF16213;PF01369;PF09324;PF12783; | 1.10.220.20;1.10.1000.11;1.25.10.10; | null | PTM: Phosphorylated. In vitro phosphorylated by PKA reducing its GEF activity and dephosphorylated by phosphatase PP1 (By similarity). {ECO:0000250}. | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Cytoplasm, perinuclear region {ECO:0000250}. Golgi apparatus {ECO:0000250}. Golgi apparatus, trans-Golgi network {ECO:0000250}. Nucleus {ECO:0000250}. Nucleus, nucleolus {ECO:0000250}. Nucleus matrix {ECO:0000250}. Membrane {ECO:0000250}. Note=Translocates from cytoplasm t... | null | null | null | null | null | FUNCTION: Promotes guanine-nucleotide exchange on ARF1 and ARF3. Promotes the activation of ARF1/ARF3 through replacement of GDP with GTP. Involved in vesicular trafficking. Required for the maintenance of Golgi structure; the function may be independent of its GEF activity. Required for the maturaion of integrin beta-... | Mus musculus (Mouse) |
G3X9X1 | KBTB2_MOUSE | MSTQEERQINTEYAVSLLEQLKLFYEQQLFTDIVLIVEGTEFPCHKMVLATCSSYFRAMFMSGLSESKQTHVHLRNVDAAALQMIIAYAYTGNLAVNDSTVEQLYETACFLQVEDVLQRCREYLIKKINAENCVRLLSFADLFSCEELKQSAKRMVEHKFTAVYRQEAFMQLSHDLLIDILSSDNLNVEKEETVREAAMLWLEYNTESRSQYLSSVLSQIRIDALSEVTQRAWFQGLPPNDKSVVVQGLYKSMPKFFKPRLGMTKEEMMIFIEASSENPCSLYSSVCYSPQAEKVYKLCSPPADLHKVGTVVTPDNDIYI... | null | null | gene expression [GO:0010467]; glucose metabolic process [GO:0006006]; lipid metabolic process [GO:0006629]; phosphatidylinositol 3-kinase/protein kinase B signal transduction [GO:0043491]; protein ubiquitination [GO:0016567]; response to insulin [GO:0032868] | null | null | PF07707;PF00651;PF01344; | 1.25.40.420;2.120.10.80; | null | null | null | null | null | PATHWAY: Protein modification; protein ubiquitination. {ECO:0000269|PubMed:27708159}. | null | null | FUNCTION: Substrate-specific adapter of a BCR (BTB-CUL3-RBX1) E3 ubiquitin ligase complex that acts as a regulator of the insulin signaling pathway, modulating insulin sensitivity by limiting PIK3R1/p85alpha abundance in adipocytes. Targets PIK3R1, the regulatory subunit of phosphatidylinositol 3-kinase (PI3K), for 'Ly... | Mus musculus (Mouse) |
G3XA57 | RFIP2_MOUSE | MMLSEQAQKWFPTHVQVTVLQAKDLKPKGKSGTNDTYTIIQLGKEKYSTSVAEKTLEPVWKEEASFELPGLLMQGSPEKYILFLIVMHRSLVGLDKFLGQVAINLNDIFEDKQRRKTEWFRLESKQGKRIKNRGEIKVNIQFMRNNMTASMFDLSMKDKTRSPFAKLKDKMKGRKSDGVFSDTSSAIVPSTHMPDANPEFSSGEMQMKSKPKKPFLLGPQRLSSAHSMSDLTGSHLSSEKLKSSTVGPTHLLSRQIDSFGVVPESGSLKSPHRRTLSFDTSKLNQPGSIVDEGEHSFGRQSDPFTNVTASLPQKFATLPR... | null | null | establishment of cell polarity [GO:0030010]; insulin secretion involved in cellular response to glucose stimulus [GO:0035773]; phagocytosis [GO:0006909]; positive regulation of protein localization to plasma membrane [GO:1903078]; regulated exocytosis [GO:0045055]; TRAM-dependent toll-like receptor 4 signaling pathway ... | endosome [GO:0005768]; nucleoplasm [GO:0005654]; phagocytic cup [GO:0001891]; recycling endosome membrane [GO:0055038] | protein homodimerization activity [GO:0042803]; protein kinase binding [GO:0019901]; small GTPase binding [GO:0031267] | PF00168;PF09457; | 1.20.5.2440;2.60.40.150; | null | PTM: Phosphorylation at Ser-227 by MARK2 regulates epithelial cell polarity. | SUBCELLULAR LOCATION: Cell membrane; Peripheral membrane protein. Recycling endosome membrane {ECO:0000250}; Peripheral membrane protein {ECO:0000250}. Note=Translocates with RAB11A from the vesicles of the endocytic recycling compartment (ERC) to the plasma membrane. {ECO:0000250}. | null | null | null | null | null | FUNCTION: A Rab11 effector binding preferentially phosphatidylinositol 3,4,5-trisphosphate (PtdInsP3) and phosphatidic acid (PA) and acting in the regulation of the transport of vesicles from the endosomal recycling compartment (ERC) to the plasma membrane. Involved in insulin granule exocytosis. Also involved in recep... | Mus musculus (Mouse) |
G3XA59 | LRC32_MOUSE | MSHQILLLLAMLTLGLAISQRREQVPCRTVNKEALCHGLGLLQVPSVLSLDIQALYLSGNQLQSILVSPLGFYTALRHLDLSDNQISFLQAGVFQALPYLEHLNLAHNRLATGMALNSGGLGRLPLLVSLDLSGNSLHGNLVERLLGETPRLRTLSLAENSLTRLARHTFWGMPAVEQLDLHSNVLMDIEDGAFEALPHLTHLNLSRNSLTCISDFSLQQLQVLDLSCNSIEAFQTAPEPQAQFQLAWLDLRENKLLHFPDLAVFPRLIYLNVSNNLIQLPAGLPRGSEDLHAPSEGWSASPLSNPSRNASTHPLSQLLN... | null | null | negative regulation of activated T cell proliferation [GO:0046007]; negative regulation of cytokine production [GO:0001818]; positive regulation of gene expression [GO:0010628]; regulation of transforming growth factor beta3 activation [GO:1901398]; secondary palate development [GO:0062009]; transforming growth factor ... | cell surface [GO:0009986]; external side of plasma membrane [GO:0009897]; extracellular matrix [GO:0031012]; extracellular space [GO:0005615]; nucleoplasm [GO:0005654] | transforming growth factor beta binding [GO:0050431] | PF13855; | 3.80.10.10; | LRRC32/LRRC33 family | null | SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:Q14392}; Single-pass type I membrane protein {ECO:0000255}. Cell surface {ECO:0000250|UniProtKB:Q14392}. | null | null | null | null | null | FUNCTION: Key regulator of transforming growth factor beta (TGFB1, TGFB2 and TGFB3) that controls TGF-beta activation by maintaining it in a latent state during storage in extracellular space (PubMed:25127859). Associates specifically via disulfide bonds with the Latency-associated peptide (LAP), which is the regulator... | Mus musculus (Mouse) |
G3XAP7 | LP9A_THEAU | HGFVQNIVIDGKNYGGYLVNQYPYMSNPPEVIAWSTTATDLGFVDGTGYQTPDIICHRGAKPGALTAPVSPGGTVELQWTPWPDSHHGPVINYLAPCNGDCSTVDKTQLEFFKIAESGLINDDNPPGIWASDNLIAANNSWTVTIPTTIAPGNYVLRHEIIALHSAQNQDGAQNYPQCINLQVTGGGSDNPAGTLGTALYHDTDPGILINIYQKLSSYIIPGPPLYTG | 3.2.1.4 | COFACTOR: Name=Cu(2+); Xref=ChEBI:CHEBI:29036; Evidence={ECO:0000269|PubMed:21876164, ECO:0000269|PubMed:29971843, ECO:0000269|PubMed:35204695, ECO:0000269|PubMed:36071795, ECO:0000269|Ref.4}; Note=Binds 1 copper ion per subunit. {ECO:0000269|PubMed:21876164, ECO:0000269|PubMed:29971843, ECO:0000269|PubMed:35204695, EC... | cellulose catabolic process [GO:0030245] | extracellular region [GO:0005576] | cellulase activity [GO:0008810]; cellulose binding [GO:0030248]; metal ion binding [GO:0046872] | PF03443; | 2.70.50.70; | Polysaccharide monooxygenase AA9 family | PTM: The catalytically essential N-terminal histidine His-22 is post-translationally modified by methylation to prevent protonation of the histidine side chain, and protect the critical active site of the enzyme from oxidative damage. {ECO:0000269|PubMed:21876164, ECO:0000269|PubMed:29971843}. | SUBCELLULAR LOCATION: Secreted {ECO:0000305|PubMed:21876164}. | CATALYTIC ACTIVITY: Reaction=Endohydrolysis of (1->4)-beta-D-glucosidic linkages in cellulose, lichenin and cereal beta-D-glucans.; EC=3.2.1.4; Evidence={ECO:0000269|PubMed:21876164, ECO:0000269|Ref.4}; | null | null | null | null | FUNCTION: Lytic polysaccharide monooxygenase that depolymerizes crystalline and amorphous polysaccharides via the oxidation of scissile alpha- or beta-(1-4)-glycosidic bonds, yielding C1 and C4 oxidation product (PubMed:21876164, PubMed:29971843, Ref.4). Catalysis by LPMOs requires the reduction of the active-site copp... | Thermoascus aurantiacus |
G3XCV0 | FLEQ_PSEAE | MWRETKLLLIDDNLDRSRDLAVILNFLGEDQLTCNSEDWREVAAGLSNSREALCVLLGSVESKGGAVELLKQLASWDEYLPILLIGEPAPADWPEELRRRVLASLEMPPSYNKLLDSLHRAQVYREMYDQARERGRSREPNLFRSLVGTSRAIQQVRQMMQQVADTDASVLILGESGTGKEVVARNLHYHSKRREGPFVPVNCGAIPAELLESELFGHEKGAFTGAITSRAGRFELANGGTLFLDEIGDMPLPMQVKLLRVLQERTFERVGSNKTQNVDVRIIAATHKNLEKMIEDGTFREDLYYRLNVFPIEMAPLRER... | null | null | DNA-templated transcription [GO:0006351]; negative regulation of extracellular matrix assembly [GO:1901202]; positive regulation of cell-substrate adhesion [GO:0010811]; positive regulation of cilium-dependent cell motility [GO:2000155]; regulation of bacterial-type flagellum-dependent cell motility [GO:1902021]; regul... | protein-DNA complex [GO:0032993] | ATP binding [GO:0005524]; ATP hydrolysis activity [GO:0016887]; cis-regulatory region sequence-specific DNA binding [GO:0000987]; cyclic-di-GMP binding [GO:0035438]; DNA-binding transcription activator activity [GO:0001216]; DNA-binding transcription repressor activity [GO:0001217]; transcription cis-regulatory region ... | PF06490;PF02954;PF00158; | 1.10.8.60;3.40.50.2300;1.10.10.60;3.40.50.300; | null | null | null | null | null | null | null | null | FUNCTION: AAA+ ATPase enhancer-binding protein that acts as a transcription regulator and plays a role in the modulation of mucin adhesion and flagellar gene expression (PubMed:11673434, PubMed:26362077, PubMed:9287015). In addition to flagella genes, regulates also expression of biofilm-related genes (PubMed:22581773)... | Pseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C / PRS 101 / PAO1) |
G3XCX3 | PILU_PSEAE | MEFEKLLRLMVEKGGSDLFITAGVPPSMKVNGRVMPVTKTPLSPEQTRETVLGVMNEQQRRDFAENHECNFAISARGIGRFRVSAFYQRNLVGMVLRRIETNIPTLEELKLPEILKKLALTKRGLVIFVGATGTGKSTSLAAMIGYRNKNSTGHIISIEDPIEYIHQHQGCIVTQREVGLDTDSFEVALKNTLRQAPDVIMIGEVRSRETMDHAVAFAETGHLCLATLHANNANQALERIIHFFPADRHGQVWMDLSLNLKAIVAQQLVPTPDGKGRRAVIEVLLNTPLAADLIRKGEVHELKPLMKRSTEQGMQTFDQA... | null | null | type IV pilus-dependent motility [GO:0043107] | cytoplasm [GO:0005737] | ATP binding [GO:0005524]; endodeoxyribonuclease activity, producing 5'-phosphomonoesters [GO:0016888] | PF00437; | 3.30.450.90;3.40.50.300; | GSP E family | null | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:15659660}. Note=Localizes only to the piliated pole. {ECO:0000269|PubMed:15659660}. | null | null | null | null | null | FUNCTION: ATPase component of the type IV pilus (T4P) that plays a role in surface and host cell adhesion, colonization, biofilm maturation, virulence, and twitching, a form of surface-associated motility facilitated by cycles of extension, adhesion, and retraction of T4P fibers (PubMed:10377148, PubMed:15659660, PubMe... | Pseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C / PRS 101 / PAO1) |
G3XCY4 | AMRZ_PSEAE | MRPLKQATPTYSSRTADKFVVRLPEGMREQIAEVARSHHRSMNSEIIARLEQSLLQEGALQDNLGVRLDSPELSLHERELLQRFRQLTHRQQNALVALIAHDAELAQA | null | null | bacterial-type flagellum assembly [GO:0044780]; negative regulation of bacterial-type flagellum-dependent cell motility [GO:1902201]; negative regulation of DNA-templated transcription [GO:0045892]; negative regulation of single-species biofilm formation on inanimate substrate [GO:1900232]; positive regulation of cell ... | protein-DNA complex [GO:0032993] | DNA binding [GO:0003677]; DNA-binding transcription repressor activity [GO:0001217]; sequence-specific DNA binding [GO:0043565]; transcription cis-regulatory region binding [GO:0000976] | PF03869; | 1.10.1220.10; | null | null | null | null | null | null | null | null | FUNCTION: Functions both as a transcriptional activator and a repressor of multiple genes encoding virulence factors as well as genes involved in environmental adaptation (PubMed:16352829, PubMed:22511872, PubMed:26549743). Plays a role in alginate production via the activation of AlgD which is the first gene in the al... | Pseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C / PRS 101 / PAO1) |
G3XCY6 | GLTR_PSEAE | MSANGRSILLVDDDQEIRELLETYLSRAGFQVRSVSRGADFRQALCEEEASLAILDVMLPDEDGFSLCRWIRSHQRLACMPIIMLTASSDEADRVIGLELGADDYLGKPFSPRELLARIKALLRRAQFTQVRGGDVLAFEDWRLDTVSHRLFHEDGEEFFLSGADFALLKLFLDHPQQILDRDTIANATRGREVLPLERIVDMAVSRLRQRLRDTGKAPRLIQTVRGSGYLLAAQVRPHLQP | null | null | positive regulation of glucose transmembrane transport [GO:0010828]; regulation of DNA-templated transcription [GO:0006355] | cytosol [GO:0005829]; protein-DNA complex [GO:0032993] | phosphorelay response regulator activity [GO:0000156]; transcription cis-regulatory region binding [GO:0000976] | PF00072;PF00486; | 3.40.50.2300;6.10.250.690;1.10.10.10; | null | PTM: Phosphorylated by GtrS. {ECO:0000269|PubMed:24920832}. | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305}. | null | null | null | null | null | FUNCTION: Member of the two-component regulatory system GtrS/GltR involved in the regulation of glucose metabolism and transport, as well as regulation of the exotoxin A gene expression (PubMed:24920832). GltR controls the transcription of genes involved in glucose metabolism (glk and edd/gap-1) and transport (oprB) as... | Pseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C / PRS 101 / PAO1) |
G3XD01 | WBPD_PSEAE | MSYYQHPSAIVDDGAQIGSDSRVWHFVHICAGARIGAGVSLGQNVFVGNKVVIGDRCKIQNNVSVYDNVTLEEGVFCGPSMVFTNVYNPRSLIERKDQYRNTLVKKGATLGANCTIVCGVTIGEYAFVGAGAVINKNVPSYALMVGVPARQIGWMSEFGEQLQLNEQGEAVCSHSGARYVLNGKILSKVDV | 2.3.1.201 | null | cell wall organization [GO:0071555]; O antigen biosynthetic process [GO:0009243]; polysaccharide biosynthetic process [GO:0000271]; protein trimerization [GO:0070206]; UDP-glucuronate biosynthetic process [GO:0006065] | null | acetyltransferase activity [GO:0016407]; acyltransferase activity [GO:0016746] | PF00132; | 2.20.70.110;2.160.10.10; | Transferase hexapeptide repeat family | null | null | CATALYTIC ACTIVITY: Reaction=acetyl-CoA + UDP-2-acetamido-3-amino-2,3-dideoxy-alpha-D-glucuronate = CoA + H(+) + UDP-2,3-diacetamido-2,3-dideoxy-alpha-D-glucuronate; Xref=Rhea:RHEA:33587, ChEBI:CHEBI:15378, ChEBI:CHEBI:57287, ChEBI:CHEBI:57288, ChEBI:CHEBI:58745, ChEBI:CHEBI:62245; EC=2.3.1.201; Evidence={ECO:0000269|P... | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=107 uM for UDP-D-GlcNAc3NA {ECO:0000269|PubMed:19348502}; Note=kcat is 2900 min(-1).; | PATHWAY: Bacterial outer membrane biogenesis; LPS O-antigen biosynthesis. {ECO:0000269|PubMed:16102001, ECO:0000269|PubMed:19282284, ECO:0000269|PubMed:19348502, ECO:0000269|PubMed:8939432}. | null | null | FUNCTION: Plays a role in the biosynthesis of B-band O antigen for serotype O5. Catalyzes the transfer of an acetyl group to the C-3 amino position of UDP-2-acetamido-3-amino-2,3-dideoxy-alpha-D-glucuronate (UDP-D-GlcNAc3NA). {ECO:0000269|PubMed:16102001, ECO:0000269|PubMed:19282284, ECO:0000269|PubMed:19348502}. | Pseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C / PRS 101 / PAO1) |
G3XD23 | WBPB_PSEAE | MKNFALIGAAGYIAPRHMRAIKDTGNCLVSAYDINDSVGIIDSISPQSEFFTEFEFFLDHASNLKRDSATALDYVSICSPNYLHYPHIAAGLRLGCDVICEKPLVPTPEMLDQLAVIERETDKRLYNILQLRHHQAIIALKDKVAREKSPHKYEVDLTYITSRGNWYLKSWKGDPRKSFGVATNIGVHFYDMLHFIFGKLQRNVVHFTSEYKAAGYLEYEQARVRWFLSVDANDLPESVKGKKPTYRSITVNGEEMEFSEGFTDLHTTSYEEILAGRGYGIDDARHCVETVNTIRSAVIVPASDNEGHPFVAALAR | 1.1.1.335 | null | cell wall organization [GO:0071555]; lipopolysaccharide biosynthetic process [GO:0009103]; O antigen biosynthetic process [GO:0009243]; polysaccharide biosynthetic process [GO:0000271]; protein tetramerization [GO:0051262]; UDP-glucuronate biosynthetic process [GO:0006065] | null | NAD+ binding [GO:0070403]; NADH binding [GO:0070404]; NADH dehydrogenase activity [GO:0003954]; phosphoglycerate dehydrogenase activity [GO:0004617] | PF01408;PF02894; | 3.40.50.720; | Gfo/Idh/MocA family | null | null | CATALYTIC ACTIVITY: Reaction=NAD(+) + UDP-N-2-acetamido-2-deoxy-alpha-D-glucuronate = H(+) + NADH + UDP-2-acetamido-2-deoxy-alpha-D-ribo-hex-3-uluronate; Xref=Rhea:RHEA:33579, ChEBI:CHEBI:15378, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945, ChEBI:CHEBI:62250, ChEBI:CHEBI:65040; EC=1.1.1.335; Evidence={ECO:0000269|PubMed:192822... | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=0.25 mM for UDP-GlcNAcA {ECO:0000269|PubMed:19348502, ECO:0000269|PubMed:20690587}; KM=1.35 mM for 2-oxoglutarate {ECO:0000269|PubMed:19348502, ECO:0000269|PubMed:20690587}; Vmax=28 umol/min/ug enzyme {ECO:0000269|PubMed:19348502, ECO:0000269|PubMed:20690587}; | PATHWAY: Bacterial outer membrane biogenesis; LPS O-antigen biosynthesis. {ECO:0000269|PubMed:18621892, ECO:0000269|PubMed:19282284, ECO:0000269|PubMed:19348502, ECO:0000269|PubMed:8939432}. | BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 8.0 for the coupled WbpB/WbpE reaction. {ECO:0000269|PubMed:19348502}; | BIOPHYSICOCHEMICAL PROPERTIES: Temperature dependence: Optimum temperature is 30 degrees Celsius for the coupled WbpB/WbpE reaction. {ECO:0000269|PubMed:19348502}; | FUNCTION: Plays a role in the biosynthesis of B-band O antigen for serotype O5. Catalyzes the NAD-dependent oxidation of UDP-N-acetylglucosaminuronic acid (UDP-D-GlcNAcA) to UDP-2-acetamido-2-deoxy-3-oxo-D-glucuronic acid (UDP-3-oxo-D-GlcNAcA). Cannot use UDP-GlcNAc or UDP-GalNAc as the nucleotide sugar substrate, and ... | Pseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C / PRS 101 / PAO1) |
G3XD24 | PCTA_PSEAE | MIKSLKFSHKILLAASLVVFAAFALFTLYNDYLQRNAIREDLESYLREMGDVTSSNIQNWLGGRLLLVEQTAQTLARDHSPETVSALLEQPALTSTFSFTYLGQQDGVFTMRPDSPMPAGYDPRSRPWYKDAVAAGGLTLTEPYVDAATQELIITAATPVKAAGNTLGVVGGDLSLKTLVQIINSLDFSGMGYAFLVSGDGKILVHPDKEQVMKTLSEVYPQNTPKIATGFSEAELHGHTRILAFTPIKGLPSVTWYLALSIDKDKAYAMLSKFRVSAIAAALISIVAILVLLGLLIRLLMQPLHLMGRAMQDIAQGEGD... | null | null | chemotaxis [GO:0006935]; response to amino acid [GO:0043200]; signal transduction [GO:0007165] | plasma membrane [GO:0005886] | amino acid binding [GO:0016597]; transmembrane signaling receptor activity [GO:0004888] | PF02743;PF00672;PF00015; | 1.10.287.950;3.30.450.20; | Methyl-accepting chemotaxis (MCP) protein family | null | SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000255}. | null | null | null | null | null | FUNCTION: Chemotactic-signal transducers respond to changes in the concentration of attractants and repellents in the environment, transduce a signal from the outside to the inside of the cell, and facilitate sensory adaptation through the variation of the level of methylation. Major receptor that responds to all natur... | Pseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C / PRS 101 / PAO1) |
G3XD94 | UGND_PSEAE | MIDVNTVVEKFKSRQALIGIVGLGYVGLPLMLRYNAIGFDVLGIDIDDVKVDKLNAGQCYIEHIPQAKIAKARASGFEATTDFSRVSECDALILCVPTPLNKYREPDMSFVINTTDALKPYLRVGQVVSLESTTYPGTTEEELLPRVQEGGLVVGRDIYLVYSPEREDPGNPNFETRTIPKVIGGHTPQCLEVGIALYEQAIDRVVPVSSTKAAEMTKLLENIHRAVNIGLVNEMKIVADRMGIDIFEVVDAAATKPFGFTPYYPGPGLGGHCIPIDPFYLTWKAREYGLHTRFIELSGEVNQAMPEYVLGKLMDGLNEA... | 1.1.1.136 | COFACTOR: Name=K(+); Xref=ChEBI:CHEBI:29103; Evidence={ECO:0000269|PubMed:15226302}; Name=NH4(+); Xref=ChEBI:CHEBI:28938; Evidence={ECO:0000269|PubMed:15226302}; Note=A monovalent cation. NH4(+) and K(+) are the most effective. {ECO:0000269|PubMed:15226302}; | cell wall organization [GO:0071555]; O antigen biosynthetic process [GO:0009243]; polysaccharide biosynthetic process [GO:0000271] | membrane [GO:0016020] | NAD binding [GO:0051287]; NADH dehydrogenase activity [GO:0003954]; oxidoreductase activity, acting on the CH-CH group of donors, NAD or NADP as acceptor [GO:0016628]; UDP-N-acetylglucosamine 6-dehydrogenase activity [GO:0047004] | PF00984;PF03720;PF03721; | 3.40.50.720; | UDP-glucose/GDP-mannose dehydrogenase family | null | SUBCELLULAR LOCATION: Membrane {ECO:0000255}; Single-pass membrane protein {ECO:0000255}. | CATALYTIC ACTIVITY: Reaction=H2O + 2 NAD(+) + UDP-N-acetyl-alpha-D-glucosamine = 3 H(+) + 2 NADH + UDP-N-2-acetamido-2-deoxy-alpha-D-glucuronate; Xref=Rhea:RHEA:13325, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:57540, ChEBI:CHEBI:57705, ChEBI:CHEBI:57945, ChEBI:CHEBI:65040; EC=1.1.1.136; Evidence={ECO:0000269|Pu... | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=0.094 mM for UDP-D-GlcNAc {ECO:0000269|PubMed:15226302}; KM=0.22 mM for NAD(+) {ECO:0000269|PubMed:15226302}; Vmax=2.9 nmol/min/ug enzyme {ECO:0000269|PubMed:15226302}; | PATHWAY: Bacterial outer membrane biogenesis; LPS O-antigen biosynthesis. {ECO:0000269|PubMed:10930727, ECO:0000269|PubMed:15226302, ECO:0000269|PubMed:18621892, ECO:0000269|PubMed:8939432}. | BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 8.0-9.0. {ECO:0000269|PubMed:15226302}; | BIOPHYSICOCHEMICAL PROPERTIES: Temperature dependence: Optimum temperature is 33-37 degrees Celsius. Active from temperatures ranging from 0 degrees Celsius to 65 degrees Celsius. {ECO:0000269|PubMed:15226302}; | FUNCTION: Plays a role in the biosynthesis of B-band O antigen for serotype O5. Catalyzes the C-6 dehydrogenation of UDP-D-GlcNAc to UDP-N-acetylglucosaminuronic acid (UDP-D-GlcNAcA). {ECO:0000269|PubMed:10930727, ECO:0000269|PubMed:15226302, ECO:0000269|PubMed:18621892}. | Pseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C / PRS 101 / PAO1) |
G3XD97 | PTXS_PSEAE | MNGSVLPSRGRVTINQVAEAAGVSKASVSRYIGGDRQLLADATARRIERAIDQLDYRPNQMARGLKRGRTRLIGMLVADILNPYSVAVMHGVETACREHGYSLVVCNTDRDDEQERHHLAALQSYNVEGLIVNTLGHHPGELRALHRELPMVLVDRQLAELDTDLVGLDNADAVEQALDHLQHRGFRDILLVTEPLDGTSSRIERVQAFNASIGRRPALKGQVLQTDDFFRDGLRAFLSASGPGPKALFTCNGVATLCATRQLRDLGCRLFDEVGLLALDELDWYPLVGSGITALAQPTDEIGRTAFERLLARLEGDREP... | null | null | negative regulation of DNA-templated transcription [GO:0045892]; regulation of DNA-templated transcription [GO:0006355] | protein-DNA complex [GO:0032993] | DNA-binding transcription factor activity [GO:0003700]; DNA-binding transcription repressor activity [GO:0001217]; transcription cis-regulatory region binding [GO:0000976] | PF00356;PF00532; | 3.40.50.2300;1.10.260.40; | null | null | null | null | null | null | null | null | FUNCTION: Negatively regulates glucose metabolism by binding directly to the promoter region of the kgu and gad operons (PubMed:22844393, PubMed:24019239). It also negatively regulates its own synthesis (PubMed:10438759, PubMed:10894751, PubMed:22844393). {ECO:0000269|PubMed:10438759, ECO:0000269|PubMed:10894751, ECO:0... | Pseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C / PRS 101 / PAO1) |
G3XDA8 | PSTS_PSEAE | MKLKRLMAALTFVAAGVGAASAVAAIDPALPEYQKASGVSGNLSSVGSDTLANLMTMWAEEYKRLYPNVNIQIQAAGSSTAPPALTEGTANLGPMSRKMKDVELQAFEQKYGYKPTAVPVAVDALAIFVHKDNPIKGLTMQQVDAIFSATRLCGSKQDVKTWGDLGLTGDWAKKPVQLFGRNSVSGTYGYFKEEALCKGDFRPNVNEQPGSASVVQSVSQSLNGIGYSGIGYKTASVKTVALAKKEGAAFVEDNEQNALNGTYPLSRFLYVYVNKAPNKPLDPLEAQFLKLVLSKTGQQVVVKDGYIPLPAKVAEKAIKE... | null | null | cell adhesion [GO:0007155]; phosphate ion transport [GO:0006817]; single-species biofilm formation [GO:0044010] | extracellular region [GO:0005576]; periplasmic space [GO:0042597] | phosphate ion binding [GO:0042301] | PF12849; | 3.40.190.10; | PstS family | null | SUBCELLULAR LOCATION: Periplasm {ECO:0000269|PubMed:6436026, ECO:0000269|Ref.5}. Secreted {ECO:0000269|PubMed:18282104}. Note=In some strains (e.g. non-MDR PAO1 and virulent clinical strain MDR25) forms long appendages distinct from flagella or pili on the cell surface: cell surface expression depends on type II secret... | null | null | null | null | null | FUNCTION: Binds 1 inorganic phosphate per subunit with a KD of 0.34 uM (PubMed:6436026). Required for phosphate transport (Ref.5). In strain PAO1 implicated in host cell adhesion; in some virulent strains (e.g. MDR25 which expresses very high levels of this protein) antibody fragments against this protein decrease host... | Pseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C / PRS 101 / PAO1) |
G3XP38 | OTASE_ASPNA | MVRRIASATPMVQSPMSPLGTTYCVRPNSVSMNLQRRPLVIASTDEAKVTIIYAGLLIPGDGEPLRNAALVISDKIIAFVGSEADIPKKYLRSTQSTHRVPVLMPGLWDCHMHFGGDDDYYNDYTSGLATHPASSGARLARGCWEALQNGYTSYRDLAGYGCEVAKAINDGTIVGPNVYSSGAALSQTAGHGDIFALPAGEVLGSYGVMNPRPGYWGAGPLCIADGVEEVRRAVRLQIRRGAKVIKVMASGGVMSRDDNPNFAQFSPEELKVIVEEAARQNRIVSAHVHGKAGIMAAIKAGCKSLEHVSYADEEVWELMK... | 3.4.17.- | COFACTOR: Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000269|PubMed:24947135}; | proteolysis [GO:0006508] | extracellular region [GO:0005576] | carboxypeptidase activity [GO:0004180]; hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds [GO:0016810]; metal ion binding [GO:0046872]; metallopeptidase activity [GO:0008237] | PF01979; | 3.20.20.140; | Metallo-dependent hydrolases superfamily, Ochratoxinase amidase 2 family | null | SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:24947135}. | CATALYTIC ACTIVITY: Reaction=H2O + ochratoxin A = L-phenylalanine + ochratoxin alpha; Xref=Rhea:RHEA:72751, ChEBI:CHEBI:15377, ChEBI:CHEBI:58095, ChEBI:CHEBI:166829, ChEBI:CHEBI:192527; Evidence={ECO:0000269|PubMed:24947135}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:72752; Evidence={ECO:0000269|PubMed:24947... | null | null | BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 6. {ECO:0000269|PubMed:24947135}; | BIOPHYSICOCHEMICAL PROPERTIES: Temperature dependence: Optimum temperature is 66 degrees Celsius. {ECO:0000269|PubMed:24947135}; | FUNCTION: Carboxypeptidase that catalyzes the release of a C-terminal amino acid with specific catalytic activity for aromatic amino acids such as phenylalanine (PubMed:24947135, PubMed:33647354). Is able to degrade ochratoxin A, one of the five major mycotoxins most harmful to humans and animals that is produced by As... | Aspergillus niger (strain ATCC 1015 / CBS 113.46 / FGSC A1144 / LSHB Ac4 / NCTC 3858a / NRRL 328 / USDA 3528.7) |
G3Y419 | YANA_ASPNA | MSASRSSTKFSTPAEGSDNGKEFTTPATSTEGHEVPDRPGDALADVAIIGMACRTPGDVRSPDSLWQYLLKKGDASGSLPDWRWEPYRQRHPRNAALLAQTTAKGYFLDDIDHFDAAFFSISPREAEQMDPQQRLALEVAWEALENAGISPPQLAGSNTSVYMGVNSDDYAKLLLEDLPNVDAHMGVGTAYCGIPSRISYILDLMGPSVALDAACASSLVAVHHARQAIRAGETDLAIAGGVNALLGPGLTRVLDEAGAISTDGKCRSFDETASGYGRGEGAGVVILKRLDKALADGDHVLAVLKGSAVASDGKTLGIMA... | 2.3.1.165 | null | fatty acid biosynthetic process [GO:0006633]; heterocycle biosynthetic process [GO:0018130]; methylation [GO:0032259]; organic cyclic compound biosynthetic process [GO:1901362]; secondary metabolite biosynthetic process [GO:0044550]; terpenoid biosynthetic process [GO:0016114] | null | 3-oxoacyl-[acyl-carrier-protein] synthase activity [GO:0004315]; 6-methylsalicylic acid synthase activity [GO:0050641]; fatty acid synthase activity [GO:0004312]; methyltransferase activity [GO:0008168]; phosphopantetheine binding [GO:0031177] | PF00698;PF00109;PF02801;PF08659;PF21089;PF00550; | 3.40.47.10;1.10.1200.10;3.30.70.250;3.40.366.10;3.40.50.720;3.10.129.110; | null | null | null | CATALYTIC ACTIVITY: Reaction=acetyl-CoA + 3 H(+) + 3 malonyl-CoA + NADPH = 6-methylsalicylate + 3 CO2 + 4 CoA + H2O + NADP(+); Xref=Rhea:RHEA:12240, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:16526, ChEBI:CHEBI:36658, ChEBI:CHEBI:57287, ChEBI:CHEBI:57288, ChEBI:CHEBI:57384, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349; ... | null | PATHWAY: Secondary metabolite biosynthesis; terpenoid biosynthesis. {ECO:0000269|PubMed:24684908}. | null | null | FUNCTION: Non-reducing polyketide synthase; part of the gene cluster that mediates the biosynthesis of yanuthone D, a fungal isoprenoid epoxycyclohexenone that acts as an antibiotic against fungi and bacteria (PubMed:24684908). The first step of the pathway is the synthesis of 6-methylsalicylic acid (6-MSA) by the poly... | Aspergillus niger (strain ATCC 1015 / CBS 113.46 / FGSC A1144 / LSHB Ac4 / NCTC 3858a / NRRL 328 / USDA 3528.7) |
G4FEF4 | AGAL_THEMA | MEIFGKTFREGRFVLKEKNFTVEFAVEKIHLGWKISGRVKGSPGRLEVLRTKAPEKVLVNNWQSWGPCRVVDAFSFKPPEIDPNWRYTASVVPDVLERNLQSDYFVAEEGKVYGFLSSKIAHPFFAVEDGELVAYLEYFDVEFDDFVPLEPLVVLEDPNTPLLLEKYAELVGMENNARVPKHTPTGWCSWYHYFLDLTWEETLKNLKLAKNFPFEVFQIDDAYEKDIGDWLVTRGDFPSVEEMAKVIAENGFIPGIWTAPFSVSETSDVFNEHPDWVVKENGEPKMAYRNWNKKIYALDLSKDEVLNWLFDLFSSLRKMG... | 3.2.1.22 | null | carbohydrate metabolic process [GO:0005975]; glycoside catabolic process [GO:0016139] | null | alpha-galactosidase activity [GO:0004557]; carbohydrate binding [GO:0030246]; protein homodimerization activity [GO:0042803] | PF02065; | 2.60.40.2760;3.20.20.70; | Glycosyl hydrolase 36 family | null | null | CATALYTIC ACTIVITY: Reaction=Hydrolysis of terminal, non-reducing alpha-D-galactose residues in alpha-D-galactosides, including galactose oligosaccharides, galactomannans and galactolipids.; EC=3.2.1.22; Evidence={ECO:0000269|PubMed:17323919, ECO:0000269|PubMed:24237145, ECO:0000269|PubMed:25486100, ECO:0000269|PubMed:... | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=0.075 mM for p-nitrophenol-alpha-galactoside (at pH 5.0 and 75 degrees Celsius) {ECO:0000269|PubMed:9741105}; KM=2.1 mM for raffinose (at pH 5.0 and 75 degrees Celsius) {ECO:0000269|PubMed:9741105}; KM=0.11 mM for p-nitrophenyl-alpha-D-galactopyranoside (at pH 5.0 ... | null | BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 5.0-5.5 when using synthetic substrate p-nitrophenyl-alpha-D-galactopyranoside. {ECO:0000269|PubMed:9741105}; | BIOPHYSICOCHEMICAL PROPERTIES: Temperature dependence: Optimum temperature is 90-95 degrees Celsius when using synthetic substrate p-nitrophenyl-alpha-D-galactopyranoside. The half-life of thermoinactivation is 6.5 h at 85 degrees Celsius. {ECO:0000269|PubMed:9741105}; | FUNCTION: Hydrolyzes the short-chain alpha-galactosaccharides raffinose, melibiose and stachyose. {ECO:0000269|PubMed:25486100, ECO:0000269|PubMed:9741105}. | Thermotoga maritima (strain ATCC 43589 / DSM 3109 / JCM 10099 / NBRC 100826 / MSB8) |
G4MQX3 | MIP11_PYRO7 | MAEQLILKGTLEGHNGWVTSLATSMENPNMLLSSSRDKTLIIWNLTRDETSYGYPKRSLKGHSHIVSDCVISSDGAYALSASWDKTLRLWELATGTTTRRFVGHTNDVLSVSFSADNRQIVSGSRDRSIKLWNTLGDCKYTITEKGHSEWVSCVRFSPNPQNPVIVSSGWDKLVKVWELSSCKLQTDHIGHTGYINTVTISPDGSLCASGGKDGTTMLWDLNESKHLYSLNANDEIHALVFSPNRYWLCAATASSIIIFDLEKKSKVDELKPEFAAVGKKSREPECISLAWSADGQTLFAGYTDNIIRAWGVMSRA | null | null | G protein-coupled receptor signaling pathway [GO:0007186]; GCN2-mediated signaling [GO:0140469]; mRNA destabilization [GO:0061157]; negative regulation of cell wall integrity MAPK cascade [GO:1903138]; negative regulation of glucose mediated signaling pathway [GO:1902660]; negative regulation of p38MAPK cascade [GO:190... | cytosolic small ribosomal subunit [GO:0022627]; nucleus [GO:0005634] | G-protein alpha-subunit binding [GO:0001965]; GDP-dissociation inhibitor activity [GO:0005092]; protein kinase C binding [GO:0005080]; ribosome binding [GO:0043022]; translation regulator activity [GO:0045182] | PF00400; | 2.130.10.10; | WD repeat G protein beta family, Ribosomal protein RACK1 subfamily | null | null | null | null | null | null | null | FUNCTION: Involved in regulating the cell wall integrity and MPS1 activation via its interaction with the MAPKKK MCK1. {ECO:0000269|PubMed:28244240}. | Pyricularia oryzae (strain 70-15 / ATCC MYA-4617 / FGSC 8958) (Rice blast fungus) (Magnaporthe oryzae) |
G4MVZ2 | ACE1_PYRO7 | MRDEMWNTATEPIAIIGSGCKFPGGSTTPSKLWELLKDPKDIVSEIRPDRFDVDKYFHPDHKHHGTSNVRHSYFLEENFKHFDAKFFGIRPQEAMAMDPQQRFLLETVYESLEAAGITISDLKGSQAGVFVGNMGVDYSELLSQDIDAFPTYFAPGTARSILSNRISYFFDLHGPSVTVDTACSSSLVAVHQAVQSLRLGETPVAIVCGANLLLGPAQYIAESKLQMLSPNGRSRMWDASADGYARGEGFASIVLKPLSVALANGDHIECIIRETGCNQDGRTKGITMPSPLAQCKLIQETYKRAGLDLSKSSDRPQYFE... | 2.3.1.-; 6.3.2.- | null | amide biosynthetic process [GO:0043604]; fatty acid biosynthetic process [GO:0006633]; heterocycle biosynthetic process [GO:0018130]; methylation [GO:0032259]; organic cyclic compound biosynthetic process [GO:1901362]; organonitrogen compound biosynthetic process [GO:1901566]; toxin biosynthetic process [GO:0009403] | cytoplasm [GO:0005737] | 3-oxoacyl-[acyl-carrier-protein] synthase activity [GO:0004315]; fatty acid synthase activity [GO:0004312]; isomerase activity [GO:0016853]; ligase activity [GO:0016874]; methyltransferase activity [GO:0008168]; oxidoreductase activity [GO:0016491]; phosphopantetheine binding [GO:0031177] | PF00698;PF00501;PF00668;PF16197;PF00109;PF02801;PF08659;PF08242;PF07993;PF21089;PF00550;PF14765; | 3.30.300.30;3.40.47.10;1.10.1200.10;3.30.559.10;3.40.366.10;3.40.50.12780;3.40.50.720;3.30.559.30;3.10.129.110;3.40.50.150; | NRP synthetase family | null | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:15319478}. Note=Localizes in the cytoplasm of the appressorium. {ECO:0000269|PubMed:15319478}. | null | null | PATHWAY: Secondary metabolite biosynthesis. {ECO:0000269|PubMed:29142718}. | null | null | FUNCTION: Hybrid PKS-NRPS synthetase; part of the gene cluster that mediates the biosynthesis of a tyrosine-derived cytochalasan acting as a fungal signal recognized by resistant rice plants and leads to avirulence in Pi33 resistant rice cultivars (PubMed:12838393, PubMed:15319478, PubMed:17142568, PubMed:18433432, Pub... | Pyricularia oryzae (strain 70-15 / ATCC MYA-4617 / FGSC 8958) (Rice blast fungus) (Magnaporthe oryzae) |
G4MY67 | FNTB_PYRO7 | MRHHTKNLRRRAIFLRTTPRGNMDSSSSVATSTSSSSNHRLVRSSEGSPSAGGDDIEEVIMTPGIATGRVQPAVSVAIPDLFTQLPPVKDDLATSTSKTQDETVAICLPYLAGSDANADVEHNAHGVPHIDRKKHVRFLRNMLRQLPAPFIAADASRPWFLYWSLNAMAILGENVKEDYAESLADTARSMQNESGGFSGGHGQTSHLATTYAVVLALAVVGDEEGLSLIDRRALWKWLCDLKEADGGFRMSLGGEEDVRGAYCAAVIISLLNLPLDLCKDSEAYIRDPTANLFTGLGDYVRKCQTFEGGISGQPDAEAHG... | 2.5.1.58 | COFACTOR: Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000250|UniProtKB:P49356}; Note=Binds 1 zinc ion per subunit. {ECO:0000250|UniProtKB:P49356}; | establishment of protein localization to plasma membrane [GO:0061951] | cytoplasm [GO:0005737]; protein farnesyltransferase complex [GO:0005965] | metal ion binding [GO:0046872]; protein farnesyltransferase activity [GO:0004660] | PF00432; | 1.50.10.20; | Protein prenyltransferase subunit beta family | null | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:31250536}. | CATALYTIC ACTIVITY: Reaction=(2E,6E)-farnesyl diphosphate + L-cysteinyl-[protein] = diphosphate + S-(2E,6E)-farnesyl-L-cysteinyl-[protein]; Xref=Rhea:RHEA:13345, Rhea:RHEA-COMP:10131, Rhea:RHEA-COMP:11535, ChEBI:CHEBI:29950, ChEBI:CHEBI:33019, ChEBI:CHEBI:86019, ChEBI:CHEBI:175763; EC=2.5.1.58; Evidence={ECO:0000250|Un... | null | null | null | null | FUNCTION: Catalyzes the transfer of a farnesyl moiety from farnesyl diphosphate to a cysteine at the fourth position from the C-terminus of several proteins having the C-terminal sequence Cys-aliphatic-aliphatic-X. The beta subunit is responsible for peptide-binding. {ECO:0000269|PubMed:31250536}. | Pyricularia oryzae (strain 70-15 / ATCC MYA-4617 / FGSC 8958) (Rice blast fungus) (Magnaporthe oryzae) |
G4N0Z0 | PMK1_PYRO7 | MSRANPPSNSSGSRKISFNVSEQYDIQDVVGEGAYGVVCSAIHKPSGQKVAIKKITPFDHSMFCLRTLREMKLLRYFNHENIISILDIQKPRSYETFNEVYLIQELMETDMHRVIRTQDLSDDHCQYFIYQTLRALKAMHSANVLHRDLKPSNLLLNANCDLKVCDFGLARSAASQEDNSGFMTEYVATRWYRAPEIMLTFKEYTKAIDVWSVGCILAEMLSGKPLFPGKDYHHQLTLILDVLGTPTMEDYYGIKSRRAREYIRSLPFKKKVPFRTLFPKTSDLALDLLEKLLAFNPVKRITVEEALKHPYLEPYHDPDD... | 2.7.11.24 | COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000255|RuleBase:RU361165}; | cell-to-cell migration by invasive hypha [GO:0140649]; hyphal growth [GO:0030448]; MAPK cascade [GO:0000165]; pheromone-dependent signal transduction involved in conjugation with cellular fusion [GO:0000750]; phosphorylation [GO:0016310]; positive regulation of appressorium formation [GO:0075018]; septin ring assembly ... | cytoplasm [GO:0005737]; nucleus [GO:0005634] | ATP binding [GO:0005524]; MAP kinase activity [GO:0004707]; protein serine kinase activity [GO:0106310] | PF00069; | 1.10.510.10; | Protein kinase superfamily, CMGC Ser/Thr protein kinase family, MAP kinase subfamily | PTM: Phosphorylated by MST7. {ECO:0000269|PubMed:15749760}. | null | CATALYTIC ACTIVITY: Reaction=ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-[protein]; Xref=Rhea:RHEA:17989, Rhea:RHEA-COMP:9863, Rhea:RHEA-COMP:11604, ChEBI:CHEBI:15378, ChEBI:CHEBI:29999, ChEBI:CHEBI:30616, ChEBI:CHEBI:83421, ChEBI:CHEBI:456216; EC=2.7.11.24; Evidence={ECO:0000269|PubMed:8946911}; Physiolog... | null | null | null | null | FUNCTION: Mitogen-activated protein kinase; part of the MST11-MST7-PMK1 MAP kinase (MAPK) cascade that is essential for appressorium formation, penetration and invasive growth (PubMed:11952120, PubMed:15749760, PubMed:21283781, PubMed:23085322, PubMed:23454094, PubMed:27059015, PubMed:8946911). Central regulator of app... | Pyricularia oryzae (strain 70-15 / ATCC MYA-4617 / FGSC 8958) (Rice blast fungus) (Magnaporthe oryzae) |
G4N137 | TAS1_PYRO7 | MYNRCCRKVWIQGRVAYRPAYIRQSPPQQTLYRGIDLLPFTTIVMDHQSGFQNPSPSGGLMFSASAKRFISRIVGFVGRGAEVQQKAVGLCPLKTERRRAAAGGLLLPTGLRMGRSIIMSVRPLPFLTGPAPSPDTAAGFKPSPPTGNLVSVSPLSKAQMALWFDYLQHPTSTHYFLTLKVELDKQPLSLDKIIQVIRGLGKQHAMLRTTFHVDTDTDDMSKSYMAVHDDSWDQEIHVLMNDAQLYEALRKPFQLSSESPVRWVVQMKLQPGSARSTYTVYAAGHHIGVDGASMSVLSNQLLEAVASEVEDQPDHSGPHY... | 6.3.2.50 | COFACTOR: Name=pantetheine 4'-phosphate; Xref=ChEBI:CHEBI:47942; Evidence={ECO:0000255|PROSITE-ProRule:PRU00258}; | amino acid activation for nonribosomal peptide biosynthetic process [GO:0043041]; fatty acid biosynthetic process [GO:0006633]; secondary metabolite biosynthetic process [GO:0044550] | cytosol [GO:0005829] | 3-oxoacyl-[acyl-carrier-protein] synthase activity [GO:0004315]; ligase activity [GO:0016874]; phosphopantetheine binding [GO:0031177] | PF00501;PF00668;PF00109;PF02801;PF00550; | 3.30.300.30;3.40.47.10;1.10.1200.10;3.30.559.10;3.40.50.12780;3.30.559.30; | NRP synthetase family | null | null | CATALYTIC ACTIVITY: Reaction=acetoacetyl-CoA + ATP + L-isoleucine = AMP + CoA + diphosphate + 2 H(+) + tenuazonic acid; Xref=Rhea:RHEA:52800, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:33019, ChEBI:CHEBI:57286, ChEBI:CHEBI:57287, ChEBI:CHEBI:58045, ChEBI:CHEBI:136842, ChEBI:CHEBI:456215; EC=6.3.2.50; Evidence={E... | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=44.3 mM for isoleucine {ECO:0000269|PubMed:26503170}; KM=1.2 mM for acetoacetyl-CoA {ECO:0000269|PubMed:26503170}; KM=8.1 mM for ATP {ECO:0000269|PubMed:26503170}; KM=0.34 mM for N-acetoacetyl-L-Ile-SNAC (for the KS domain) {ECO:0000269|PubMed:32565425}; | null | null | null | FUNCTION: Hybrid PKS-NRPS synthetase that mediates the biosynthesis of the toxin tenuazonic acid (TeA), an inhibitor of protein biosynthesis on ribosomes by suppressing the release of new protein (PubMed:26503170, PubMed:28820236, PubMed:32565425, PubMed:32765467). TAS1 alone is sufficient for TeA synthesis via the con... | Pyricularia oryzae (strain 70-15 / ATCC MYA-4617 / FGSC 8958) (Rice blast fungus) (Magnaporthe oryzae) |
G4N2X9 | OXEAS_PYRO7 | MDGAVRLDWTGLDLTGHEIHDGVPIASRVQVMVSFPLFKDQHIIMSSKESPSRKSSTIGQSTRNGSCQADTQKGQLPPVGEKPKPVKENPMKKLKEMSQRPLPTQHGDGTYPTEKKLTGIGEDLKHIRGYDVKTLLAMVKSKLKGEKLKDDKTMLMERVMQLVARLPTESKKRAELTDSLINELWESLDHPPLNYLGPEHSYRTPDGSYNHPFNPQLGAAGSRYARSVIPTVTPPGALPDPGLIFDSIMGRTPNSYRKHPNNVSSILWYWATIIIHDIFWTDPRDINTNKSSSYLDLAPLYGNSQEMQDSIRTFKDGRMK... | 1.-.-.-; 1.13.11.-; 1.13.11.62 | COFACTOR: Name=heme b; Xref=ChEBI:CHEBI:60344; Evidence={ECO:0000255|PROSITE-ProRule:PRU00298}; COFACTOR: Name=heme; Xref=ChEBI:CHEBI:30413; Evidence={ECO:0000250|UniProtKB:P04798}; | fatty acid metabolic process [GO:0006631]; response to oxidative stress [GO:0006979] | null | dioxygenase activity [GO:0051213]; heme binding [GO:0020037]; iron ion binding [GO:0005506]; monooxygenase activity [GO:0004497]; oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen [GO:0016705]; peroxidase activity [GO:0004601] | PF03098;PF00067; | 1.10.630.10;1.10.640.10; | Peroxidase family; Cytochrome P450 family | null | null | CATALYTIC ACTIVITY: Reaction=(9Z)-octadecenoate + O2 = (8R)-hydroperoxy-(9Z)-octadecenoate; Xref=Rhea:RHEA:75655, ChEBI:CHEBI:15379, ChEBI:CHEBI:30823, ChEBI:CHEBI:194403; Evidence={ECO:0000269|PubMed:25121983}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:75656; Evidence={ECO:0000269|PubMed:25121983}; CATALYTI... | null | null | null | null | FUNCTION: Bifunctional dioxygenase (DOX)-epoxy alcohol synthase (EAS) that converts linoleic acid (18:2n-6) sequentially to 10(R)-hydroperoxy-8(E),12(Z)-octadecadienoic acid (10R-HPODE) and 10R-HPODE further to 12 S(13R)-epoxy-10(R)-hydroxy-8(E)-octadecenoic acid as the end product (PubMed:25121983). Oxygenation at C-1... | Pyricularia oryzae (strain 70-15 / ATCC MYA-4617 / FGSC 8958) (Rice blast fungus) (Magnaporthe oryzae) |
G4N374 | MPS1_PYRO7 | MSDLQGRKIFKVFNQDFIVDERYTVTKELGQGAYGIVCAAVNNQTSEGVAIKKVTNVFSKKILAKRALREIKLLQHFRGHRNITCLYDMDIPRPDNFNETYLYEELMECDLAAIIRSGQPLTDAHFQSFIYQILCGLKYIHSANVLHRDLKPGNLLVNADCELKICDFGLARGFSVDPEENAGYMTEYVATRWYRAPEIMLSFQSYTKAIDVWSVGCILAELLGGRPFFKGRDYVDQLNQILHILGTPNEETLSRIGSPRAQEYVRNLPFMAKKPFPTLFPNANPDALDLLDRMLAFDPSSRISVEQALEHPYLHIWHDA... | 2.7.11.24 | COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000255|RuleBase:RU361165}; | negative regulation of glucose mediated signaling pathway [GO:1902660]; negative regulation of mitotic cytokinesis [GO:1902413]; phosphorylation [GO:0016310]; positive regulation of calcium ion import across plasma membrane [GO:1905665]; positive regulation of calcium-mediated signaling [GO:0050850]; positive regulatio... | cytoplasm [GO:0005737]; nucleus [GO:0005634] | ATP binding [GO:0005524]; MAP kinase activity [GO:0004707]; protein serine kinase activity [GO:0106310] | PF00069; | 1.10.510.10; | Protein kinase superfamily, Ser/Thr protein kinase family, MAP kinase subfamily | null | null | CATALYTIC ACTIVITY: Reaction=ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-[protein]; Xref=Rhea:RHEA:17989, Rhea:RHEA-COMP:9863, Rhea:RHEA-COMP:11604, ChEBI:CHEBI:15378, ChEBI:CHEBI:29999, ChEBI:CHEBI:30616, ChEBI:CHEBI:83421, ChEBI:CHEBI:456216; EC=2.7.11.24; Evidence={ECO:0000305|PubMed:9770551}; Physiolog... | null | null | null | null | FUNCTION: Mitogen-activated protein kinase; part of the MCK1-MKK2-MPS1 MAP kinase (MAPK) signal transduction cascade that is essential for cell wall integrity and plant infection, but not for plant defense responses (PubMed:18344407, PubMed:22321443, PubMed:28424497, PubMed:28799700, PubMed:9770551). Beside its role in... | Pyricularia oryzae (strain 70-15 / ATCC MYA-4617 / FGSC 8958) (Rice blast fungus) (Magnaporthe oryzae) |
G4N4J5 | LIDS_PYRO7 | MASSSSSGSSTRSSSPSDPPSSFFQKLGAFLGLFSKPQPPRPDYPHAPGNSAREEQTDITEDIQKLGFKDVETLLLYLNSSVKGVNDDKQLLLERLIQLLSKLPPTSTNGKKVTDGLITGLWESLDHPPVSSLGEKYRFREADGSNNNIHNPTLGVAGSHYARSAKPMVYQNPNPPAPETIFDTLMARDPAKFRPHPNQISSVLFYFATIITHDIFQTSSRDPSINLTSSYLDLSPLYGRNLEEQLSVRAMKDGLLKPDTFCSKRVHGFPPGVGVLLIMFNRFHNYVVTSLAKINEGNRFKKPVGDDTAAWEKYDNDLFQ... | 1.13.11.60; 5.4.4.6 | COFACTOR: Name=heme b; Xref=ChEBI:CHEBI:60344; Evidence={ECO:0000255|PROSITE-ProRule:PRU00298}; COFACTOR: Name=Ca(2+); Xref=ChEBI:CHEBI:29108; Evidence={ECO:0000255|PROSITE-ProRule:PRU00298}; COFACTOR: Name=heme; Xref=ChEBI:CHEBI:30413; Evidence={ECO:0000250|UniProtKB:P04798}; | fatty acid metabolic process [GO:0006631]; response to oxidative stress [GO:0006979] | null | dioxygenase activity [GO:0051213]; heme binding [GO:0020037]; iron ion binding [GO:0005506]; isomerase activity [GO:0016853]; monooxygenase activity [GO:0004497]; oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen [GO:0016705]; peroxidase activity [GO:0004601] | PF03098; | 1.10.630.10;1.10.640.10; | Peroxidase family; Cytochrome P450 family | null | null | CATALYTIC ACTIVITY: Reaction=(9Z,12Z)-octadecadienoate + O2 = (8R,9Z,12Z)-8-hydroperoxyoctadeca-9,12-dienoate; Xref=Rhea:RHEA:25395, ChEBI:CHEBI:15379, ChEBI:CHEBI:30245, ChEBI:CHEBI:58659; EC=1.13.11.60; Evidence={ECO:0000269|PubMed:20023302, ECO:0000269|PubMed:25121983}; PhysiologicalDirection=left-to-right; Xref=Rhe... | null | null | null | null | FUNCTION: 7,8-linoleate diol synthase is a bifunctional enzyme that converts linoleic acid (18:2n-6) into 8-hydroperoxy-8(E),12(Z)-octadecadienoic acid (8-HPODE) and then catalyzes the isomerization of the resulting hydroperoxide to 7,8-dihydroxy-9(Z),12(Z)-octadecadienoic acid (7,8-DiHODE). {ECO:0000269|PubMed:2002330... | Pyricularia oryzae (strain 70-15 / ATCC MYA-4617 / FGSC 8958) (Rice blast fungus) (Magnaporthe oryzae) |
G4N4W3 | MSB2_PYRO7 | MHNFSKLAVAFVAAASFASAEPETKAKVERPIIYFPRHIKRQFANTTTPASEASSSTSRPPPIPVPETSSFSSSASSSSAQELTASRQPTSIDEFFSTLSDALTTDSTPFSQRPATSGAGRSSATGDVTPIIVPSSASPPSTAVKPGSVSALTTSQNSTSAATSESVTSPGSTSGPAGTPESSSASDFTSAVATSRASTATSNTGLIPETTILPTTATSNTGLIPETTILPTTASLSTAESAVTPSITSSASSSGILIAPTGVVTPTSSSSTEDPVFDGIGTLISSIVSSVSTVLQPNGTAPVTTTPNTSVDVATTPVDI... | null | null | cellular bud site selection [GO:0000282]; fungal-type cell wall organization [GO:0031505]; hyperosmotic response [GO:0006972]; osmosensory signaling pathway via Sho1 osmosensor [GO:0007232]; signal transduction involved in filamentous growth [GO:0001402] | cell surface [GO:0009986]; extracellular region [GO:0005576]; plasma membrane [GO:0005886]; site of polarized growth [GO:0030427]; vacuolar membrane [GO:0005774] | osmosensor activity [GO:0005034] | null | null | HKR1/MSB2 family | null | SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:21283781}; Single-pass membrane protein {ECO:0000255}. Vacuole membrane {ECO:0000269|PubMed:21283781}; Single-pass membrane protein {ECO:0000255}. Note=During conidium germination and appressorium formation, localizes at the cell membrane and in vacuoles (PubMed:2... | null | null | null | null | null | FUNCTION: MSB2 and SHO1 have overlapping functions in recognizing various surface signals for MAPK PMK1 activation and appressorium formation (PubMed:21283781). While MSB2 is critical for sensing surface hydrophobicity and cutin monomers, SHO1 may play a more important role in recognizing rice leaf waxes (PubMed:212837... | Pyricularia oryzae (strain 70-15 / ATCC MYA-4617 / FGSC 8958) (Rice blast fungus) (Magnaporthe oryzae) |
G4N6Z6 | MKK2_PYRO7 | MHDQEAANGGETATNPISSLDVPTPPATTIPTLSSPAPLLRPAIPGARSAGARTPRLGLAIPPSPNVKPVGGAPGRPPLPTLHLATPMGSSVTPHEQPPGRPSIVTQQGQSASGGSESSAAHSRSGSFGPLDGRTSNPTSAGSQYSALSFASHFGIGSTRPQGTPDPASAVGSIYSERSDGGAGMDKDGNLKGLENFDKLTIDKARTADVEDLDVEGWKIASMEKRIVELGGLGEGAGGAVTRCKLTGGKTVFALKVITANPDPDVKKQIMRELDFNIQCASEHICRYYGAFEDPSTATISIAMEFCEGGSLDSIYKEVK... | 2.7.11.24 | null | MAPK cascade [GO:0000165]; phosphorylation [GO:0016310]; positive regulation of appressorium formation [GO:0075018]; positive regulation of calcium-mediated signaling [GO:0050850] | cytoplasm [GO:0005737]; division septum [GO:0000935] | ATP binding [GO:0005524]; MAP kinase activity [GO:0004707]; MAP kinase kinase activity [GO:0004708] | PF00069; | 1.10.510.10; | Protein kinase superfamily, STE Ser/Thr protein kinase family, MAP kinase kinase subfamily | null | null | CATALYTIC ACTIVITY: Reaction=ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-[protein]; Xref=Rhea:RHEA:17989, Rhea:RHEA-COMP:9863, Rhea:RHEA-COMP:11604, ChEBI:CHEBI:15378, ChEBI:CHEBI:29999, ChEBI:CHEBI:30616, ChEBI:CHEBI:83421, ChEBI:CHEBI:456216; EC=2.7.11.24; Evidence={ECO:0000305|PubMed:28244240}; Physiolo... | null | null | null | null | FUNCTION: Mitogen-activated protein kinase kinase; part of the MCK1-MKK2-MPS1 MAP kinase (MAPK) signal transduction cascade that is essential for appressorium formation, penetration and invasive growth (PubMed:28244240). Beside its role in pathogenesis, the MPS1 cascade is active in conidiation and cellular stress resp... | Pyricularia oryzae (strain 70-15 / ATCC MYA-4617 / FGSC 8958) (Rice blast fungus) (Magnaporthe oryzae) |
G4N7S6 | HAT1_PYRO7 | MAESDLWSVDANSALELSLVEPTEDGLTTVTRFHPRFTYPLFGEEEQIFGYQDLKINLQYHAPDMRPNVKITHSKKFKSIGETQPTDLDALLQGYLPPVAFAKKREFEDAIRLMPADWTPPGEILSEFDGVDGAKFEIRRSNLADDASRQIIDRVQLLILLFIEGGSYIGTDTTDSLDRWDIFFLYNIKPSTTDGTSRYQFAGYSTVYKFFPLQRFPLEPKEAHENLELPSGEFPFSNLRSRTRISQFLILPPFQKSGNGSRLYRTIYDYCLRDPNVIEVTVEDPNEAFDDMRDVADLDFLRQKSEFTDLRINTDIHIPK... | 2.3.1.48 | null | autophagy [GO:0006914]; DNA repair [GO:0006281]; subtelomeric heterochromatin formation [GO:0031509] | chromosome, telomeric region [GO:0000781]; nucleus [GO:0005634]; phagophore assembly site [GO:0000407] | histone H4 acetyltransferase activity [GO:0010485] | PF10394; | 3.40.630.30;3.90.360.10; | HAT1 family | PTM: Phosphorylated at Ser-8 by GSK1 in the nucleus which impairs its translocation to the cytoplasm through interfering the interaction between HAT1 and SSB1. Dephosphorylation under nutrient starvation conditions promotes the interaction between HAT1 and SSB1 and results in the translocation of HAT1 from the nucleus ... | SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:30776962}. Cytoplasm {ECO:0000269|PubMed:30776962}. Preautophagosomal structure {ECO:0000269|PubMed:30776962}. Note=Is only present in the nucleus under nutrient-rich condition, and translocates from the nucleus to the cytoplasm with the assistance of SSB1 during germin... | CATALYTIC ACTIVITY: Reaction=acetyl-CoA + L-lysyl-[protein] = CoA + H(+) + N(6)-acetyl-L-lysyl-[protein]; Xref=Rhea:RHEA:45948, Rhea:RHEA-COMP:9752, Rhea:RHEA-COMP:10731, ChEBI:CHEBI:15378, ChEBI:CHEBI:29969, ChEBI:CHEBI:57287, ChEBI:CHEBI:57288, ChEBI:CHEBI:61930; EC=2.3.1.48; Evidence={ECO:0000269|PubMed:30776962}; | null | null | null | null | FUNCTION: Catalytic component of the histone acetylase B (HAT-B) complex. Has intrinsic substrate specificity that modifies lysine in recognition sequence GXGKXG (By similarity). Involved in DNA double-strand break repair (PubMed:30776962). Required for appressorium turgor pressure, autophagy and conidial nuclear degra... | Pyricularia oryzae (strain 70-15 / ATCC MYA-4617 / FGSC 8958) (Rice blast fungus) (Magnaporthe oryzae) |
G4NAP4 | MNLOX_PYRO7 | MRVLVWIAGLAPLAVAVPSSSYRVAVAARADNTSASVAPSQNVSGAAPPELVVYTLPCEDGNSTARTAEIRLKQATLLYGPSLLGNASYFPGGPLGDAISLRDQTVWEGAAVVQSLRAFTDAAKVAANIKQNGGLNSLDDFKVLYQDGWKGSVPQGIARGQSENYTSDLLFSMERLSVNPYILKRLHPTEDALPFQVDRATVKQLTKTSLKALHAAGRLFVADHSYQRNYTRLANRYSAACTALFYLDPRSNQFLPLAIKTNVGADLTYTPLDTDNNNWLLAKIMFNNNDLFHGQIFHVAYPHAIAEIVHLAALRTMSAR... | 1.13.11.-; 1.13.11.45; 1.13.11.58 | COFACTOR: Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000269|PubMed:26783260}; Note=Three His residues, the carboxyl oxygen of the C-terminal Ile or Val residue, and a fifth residue, usually Asn, ligate the metal, which binds water to form a catalytic base Mn(2+)OH(2) for hydrogen abstraction. {ECO:0000250|UniP... | arachidonic acid metabolic process [GO:0019369]; hepoxilin biosynthetic process [GO:0051122]; linoleic acid metabolic process [GO:0043651]; lipid oxidation [GO:0034440]; lipoxygenase pathway [GO:0019372] | extracellular region [GO:0005576] | linoleate 11-lipoxygenase activity [GO:0050584]; linoleate 9S-lipoxygenase activity [GO:1990136]; metal ion binding [GO:0046872] | PF00305; | 3.10.450.60; | Lipoxygenase family, Manganese lipoxygenase subfamily | null | SUBCELLULAR LOCATION: Secreted {ECO:0000250|UniProtKB:Q8X151}. | CATALYTIC ACTIVITY: Reaction=(9Z,12Z)-octadecadienoate + O2 = (9S)-hydroperoxy-(10E,12Z)-octadecadienoate; Xref=Rhea:RHEA:30291, ChEBI:CHEBI:15379, ChEBI:CHEBI:30245, ChEBI:CHEBI:60955; EC=1.13.11.58; Evidence={ECO:0000269|PubMed:26264916}; CATALYTIC ACTIVITY: Reaction=(9Z,12Z)-octadecadienoate + O2 = (11S)-hydroperoxy... | null | null | null | null | FUNCTION: Lipoxygenase that metabolizes linoleic and alpha-linolenic acids to 9S-, 11- and 13R-hydroperoxy fatty acids. At the end of lipoxygenation, the intermediate product 11S-HPODE from linoleic acid is then transformed into 9S-HPODE and 13R-HPODE as the final products. The intermediate product 11R-HPOTrE from alph... | Pyricularia oryzae (strain 70-15 / ATCC MYA-4617 / FGSC 8958) (Rice blast fungus) (Magnaporthe oryzae) |
G4NEB8 | MST7_PYRO7 | MADPFAPRTMKRRNVKGLALTPAAPKPPPTAENAPIHRDSDQHAQLEIGIEFNLDLRPEDLEVIKDLGSGNGGTVSKVRHIPTNTVMARKVIHVEAKREMRKRIVRELQIMHSCNSEYIVTFYGAFLNENNDVIMCMEYADVGSLDRVSRVFGPIRVDVLGKIAEATLGGLTYLYAKHHIMHRDIKPSNILVNSRGSIKLCDFGVSGELINSIADTFVGTSTYMAPERIQGEKYTVKSDVWSFGLSIMELAIGKFPFAASEQLSDAESAPAGILDLLQQIVHEPAPKLPKSDAFPQILEDMIQKCLYKNPDDRPTPEELF... | 2.7.11.24 | null | MAPK cascade [GO:0000165]; phosphorylation [GO:0016310]; positive regulation of appressorium formation [GO:0075018] | null | ATP binding [GO:0005524]; MAP kinase activity [GO:0004707]; MAP kinase kinase activity [GO:0004708] | PF00069; | 1.10.510.10; | Protein kinase superfamily, STE Ser/Thr protein kinase family, MAP kinase kinase subfamily | null | null | CATALYTIC ACTIVITY: Reaction=ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-[protein]; Xref=Rhea:RHEA:17989, Rhea:RHEA-COMP:9863, Rhea:RHEA-COMP:11604, ChEBI:CHEBI:15378, ChEBI:CHEBI:29999, ChEBI:CHEBI:30616, ChEBI:CHEBI:83421, ChEBI:CHEBI:456216; EC=2.7.11.24; Evidence={ECO:0000269|PubMed:15749760}; Physiolo... | null | null | null | null | FUNCTION: Mitogen-activated protein kinase kinase; part of the MST11-MST7-PMK1 MAP kinase (MAPK) cascade that is essential for appressorium formation, penetration and invasive growth (PubMed:15749760, PubMed:21283781, PubMed:23454094, PubMed:27059015). The MST11-MST7-PMK1 MAP kinase cascade transduces signals from the ... | Pyricularia oryzae (strain 70-15 / ATCC MYA-4617 / FGSC 8958) (Rice blast fungus) (Magnaporthe oryzae) |
G4NH08 | GSK1_PYRO7 | MSQNRPAAFNTLRMGEVIREKVQDGITGETRDLQYTQCKIVGNGSFGVVFQTKLSPSNEDAAIKRVLQDKRFKNRELQIMRIVRHPNIVQLKAFYYSNGERKDEVYLNLVQEFVPETVYRASRFFNKMKTTMPILEVKLYIYQLFRALAYIHSQGICHRDIKPQNLLLDPTTGILKLCDFGSAKILVENEPNVSYICSRYYRAPELIFGATNYTTKIDVWSTGCVMAELMLGQPLFPGESGIDQLVEIIKVLGTPTREQIRTMNPNYMEHKFPQIKPHPFNRVLRKADNNAIDLIARLLEYTPTERLGAIDAMVHPFFDD... | 2.7.11.1 | null | extrinsic apoptotic signaling pathway in absence of ligand [GO:0097192]; negative regulation of canonical Wnt signaling pathway [GO:0090090]; phosphorylation [GO:0016310]; positive regulation of chromosome segregation [GO:0051984]; positive regulation of developmental process [GO:0051094]; positive regulation of protei... | cytosol [GO:0005829]; nucleus [GO:0005634] | ATP binding [GO:0005524]; protein serine kinase activity [GO:0106310]; protein serine/threonine kinase activity [GO:0004674]; protein serine/threonine/tyrosine kinase activity [GO:0004712]; protein tyrosine kinase activity [GO:0004713] | PF00069; | 1.10.510.10; | Protein kinase superfamily, CMGC Ser/Thr protein kinase family, GSK-3 subfamily | null | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:28424497}. Note=Mainly localizes to the cytoplasm at the conidial stage. {ECO:0000269|PubMed:28424497}. | CATALYTIC ACTIVITY: Reaction=ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-[protein]; Xref=Rhea:RHEA:17989, Rhea:RHEA-COMP:9863, Rhea:RHEA-COMP:11604, ChEBI:CHEBI:15378, ChEBI:CHEBI:29999, ChEBI:CHEBI:30616, ChEBI:CHEBI:83421, ChEBI:CHEBI:456216; EC=2.7.11.1; Evidence={ECO:0000269|PubMed:30776962}; | null | null | null | null | FUNCTION: Protein kinase that acts downstream of the MPS1 MAPK cascade as a highly conservative signal modulator that dictates growth, conidiation and pathogenicity (PubMed:28424497). Phosphorylates HAT1 at 'Ser-8' to block its translocation from the nucleus to the cytoplasm where HAT1 positively regulates appressorium... | Pyricularia oryzae (strain 70-15 / ATCC MYA-4617 / FGSC 8958) (Rice blast fungus) (Magnaporthe oryzae) |
G4RK16 | PFP_THETK | MKIGVLTGGGDAPGLNIAVYTFVKLAERKHEVYAIYHGWRGLLNKEVKRVSSRDLLDFAFSGGTYIRTSRTNPFKDEERARLLESNVKELGLDVVVAIGGDDTLGAAGEAQRRGILDAVGIPKTIDNDVYGTDYTIGFDSAVNAAIEATESFKTTLISHERIGVVEVMGREAGWIALFTGLSTMADAVLIPERPASWDSVAKRVKEAYNERRWALVVVSEGIKEYGGPKDEYGHSRLGGVGNELAEYIERSTGIEARAVVLGHTIRGVPPTAFDRILAVRYATAAYEAVENGRYGVMVAYSNGDIAYVPIVDVVGKNRLV... | 2.7.1.90 | COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000255|HAMAP-Rule:MF_01976}; | canonical glycolysis [GO:0061621]; fructose 1,6-bisphosphate metabolic process [GO:0030388]; fructose 6-phosphate metabolic process [GO:0006002] | 6-phosphofructokinase complex [GO:0005945] | 6-phosphofructokinase activity [GO:0003872]; AMP binding [GO:0016208]; ATP binding [GO:0005524]; diphosphate-fructose-6-phosphate 1-phosphotransferase activity [GO:0047334]; fructose-6-phosphate binding [GO:0070095]; identical protein binding [GO:0042802]; metal ion binding [GO:0046872]; monosaccharide binding [GO:0048... | PF00365; | 3.40.50.450;3.40.50.460; | Phosphofructokinase type A (PFKA) family, Mixed-substrate PFK group III subfamily | null | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_01976}. | CATALYTIC ACTIVITY: Reaction=beta-D-fructose 6-phosphate + diphosphate = beta-D-fructose 1,6-bisphosphate + H(+) + phosphate; Xref=Rhea:RHEA:13613, ChEBI:CHEBI:15378, ChEBI:CHEBI:32966, ChEBI:CHEBI:33019, ChEBI:CHEBI:43474, ChEBI:CHEBI:57634; EC=2.7.1.90; Evidence={ECO:0000255|HAMAP-Rule:MF_01976, ECO:0000269|PubMed:95... | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=0.023 mM for diphosphate {ECO:0000269|PubMed:9555897}; KM=0.053 mM for D-fructose 6-phosphate {ECO:0000269|PubMed:9555897}; KM=1.43 mM for phosphate {ECO:0000269|PubMed:9555897}; KM=0.033 mM for D-fructose 1,6-bisphosphate {ECO:0000269|PubMed:9555897}; | PATHWAY: Carbohydrate degradation; glycolysis; D-glyceraldehyde 3-phosphate and glycerone phosphate from D-glucose: step 3/4. {ECO:0000255|HAMAP-Rule:MF_01976}. | null | null | FUNCTION: Catalyzes the phosphorylation of D-fructose 6-phosphate, the first committing step of glycolysis. Uses inorganic phosphate (PPi) as phosphoryl donor instead of ATP like common ATP-dependent phosphofructokinases (ATP-PFKs), which renders the reaction reversible, and can thus function both in glycolysis and glu... | Thermoproteus tenax (strain ATCC 35583 / DSM 2078 / JCM 9277 / NBRC 100435 / Kra 1) |
G4RK44 | TPSP_THETK | MRLIVVSNRLPVTISPSGEIRESVGGLATAMKSFLGAVNGGRELGLEEVVWVGWSGVPSERESNDLRERLRGMGLEPVPLSSEEVEGFYEGFSNSTLWPLFHGFSEYATYEEKHWRAYRGVNEKYAKAVVALARPGDLVWIHDYHLMLAPAIVREAAEVGVGFFLHIPFPPAELLQLLPSEWRREILEGLLGSDLVGFHTYEYSANFSRSVVRFLGYKVEMGAIAVGHRRVRVGVFPIGIDFDRFYNSSQDPSVVEEMAKLREMLGRAKVVFSIDRLDYTKGVLRRVAAWERFLREHPEWRGRAVFVLVVVPSRTGVPMY... | 2.4.1.15; 3.1.3.12 | COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250|UniProtKB:P31678, ECO:0000269|PubMed:23626675}; | cellular response to heat [GO:0034605]; trehalose biosynthetic process [GO:0005992]; trehalose metabolism in response to stress [GO:0070413] | alpha,alpha-trehalose-phosphate synthase complex (UDP-forming) [GO:0005946]; cytosol [GO:0005829] | alpha,alpha-trehalose-phosphate synthase (UDP-forming) activity [GO:0003825]; metal ion binding [GO:0046872]; trehalose-phosphatase activity [GO:0004805] | PF00982;PF02358; | 3.40.50.2000;3.40.50.1000; | Glycosyltransferase 20 family; Trehalose phosphatase family | null | null | CATALYTIC ACTIVITY: Reaction=D-glucose 6-phosphate + UDP-alpha-D-glucose = alpha,alpha-trehalose 6-phosphate + H(+) + UDP; Xref=Rhea:RHEA:18889, ChEBI:CHEBI:15378, ChEBI:CHEBI:58223, ChEBI:CHEBI:58429, ChEBI:CHEBI:58885, ChEBI:CHEBI:61548; EC=2.4.1.15; Evidence={ECO:0000269|PubMed:23626675}; CATALYTIC ACTIVITY: Reactio... | null | PATHWAY: Glycan biosynthesis; trehalose biosynthesis. {ECO:0000269|PubMed:23626675}. | null | BIOPHYSICOCHEMICAL PROPERTIES: Temperature dependence: Active at 80 degrees Celsius. {ECO:0000269|PubMed:23626675}; | FUNCTION: Bifunctional enzyme which catalyzes the transfer of glucose from UDP-alpha-D-glucose to glucose-6-phosphate to form trehalose-6-phosphate (Tre6P) and removes the phosphate from Tre6P to produce free trehalose. {ECO:0000269|PubMed:23626675}. | Thermoproteus tenax (strain ATCC 35583 / DSM 2078 / JCM 9277 / NBRC 100435 / Kra 1) |
G4SLH0 | TTN1_CAEEL | MEGNEKKGGGLPPTQQRHLNIDTTVGGSISQPVSPSMSYSTDRETVMRSASGHATVAETHLIRSIGSQSQSYTEEHWSSEITSFVALAPPKFIQVIKAYRVHSTDTISLVVEVASDPPAIFEWFYNEKSVLQDRDRFQVGHGINISRLKVSRPEQGVYKCVTRNPAGVSTSYGYITVNADREHLSSSKEDMRLQRQHSVTYHQAPRFLTQVPNLFVTAGSNVIIDVEVDANPPARFSWFVNGKEYRDSIHGVEMFSPDVNRSVVRFSIPVAGEYKVVASNVHGSAMSCGHVDIQKVIELEESTLTTSTTAFDPMTTSMRA... | 2.7.11.1 | COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000269|PubMed:18390597}; | phosphorylation [GO:0016310] | A band [GO:0031672]; I band [GO:0031674]; nuclear membrane [GO:0031965] | actin filament binding [GO:0051015]; ATP binding [GO:0005524]; metal ion binding [GO:0046872]; myosin binding [GO:0017022]; protein serine kinase activity [GO:0106310]; protein serine/threonine kinase activity [GO:0004674] | PF00041;PF07679;PF00069; | 2.60.40.10;1.10.510.10; | Protein kinase superfamily, CAMK Ser/Thr protein kinase family | null | SUBCELLULAR LOCATION: Cytoplasm, myofibril, sarcomere, A band {ECO:0000269|PubMed:20346955}. Cytoplasm, myofibril, sarcomere, I band {ECO:0000269|PubMed:20346955}. Nucleus membrane {ECO:0000269|PubMed:16410549}; Peripheral membrane protein {ECO:0000269|PubMed:16410549}. Note=Localizes throughout the I-band except for d... | CATALYTIC ACTIVITY: Reaction=ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-[protein]; Xref=Rhea:RHEA:17989, Rhea:RHEA-COMP:9863, Rhea:RHEA-COMP:11604, ChEBI:CHEBI:15378, ChEBI:CHEBI:29999, ChEBI:CHEBI:30616, ChEBI:CHEBI:83421, ChEBI:CHEBI:456216; EC=2.7.11.1; Evidence={ECO:0000269|PubMed:12381307, ECO:000026... | null | null | null | null | FUNCTION: Serine/threonine-protein kinase (PubMed:18390597, PubMed:20346955). Key component in the assembly and functioning of muscles. By providing connections at the level of individual microfilaments, it contributes to the fine balance of forces between the two halves of the sarcomere. The size and extensibility of ... | Caenorhabditis elegans |
G4STG9 | PFP_META2 | MNKPKKVAILTAGGLAPCLSSAIGSLIERYTEIDPSIEIICYRSGYKGLLLGDSYAVTPKIRENAALLHKFGGSPIGNSRVKLTNVKDCIKRGLVQEGQDPQKVAADQLVKDGVDVLHTIGGDDTNTAAADLAAFLAKNDYGLTVIGLPKTIDNDVFPIKQSLGAWTAAEQGAQYFQNVVAEYNANPRMLIVHEVMGRNCGWLTAATAMEYRKLLDRSEWLPEIGLDRAAYEVHGVFVPEMEIDLAAEAKRLREVMDKVDCVNIFVSEGAGVDAIVAEMQAKGQEVPRDAFGHIKLDAVNPGKWFGEQFAEMIGAEKTLI... | 2.7.1.90 | COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000255|HAMAP-Rule:MF_01977, ECO:0000269|PubMed:20868748}; | fructose 6-phosphate metabolic process [GO:0006002] | cytoplasm [GO:0005737] | 6-phosphofructokinase activity [GO:0003872]; diphosphate-fructose-6-phosphate 1-phosphotransferase activity [GO:0047334]; metal ion binding [GO:0046872] | PF00365; | 3.40.50.450; | Phosphofructokinase type A (PFKA) family, PPi-dependent PFK group II subfamily, Clade 'P' sub-subfamily | null | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_01977}. | CATALYTIC ACTIVITY: Reaction=beta-D-fructose 6-phosphate + diphosphate = beta-D-fructose 1,6-bisphosphate + H(+) + phosphate; Xref=Rhea:RHEA:13613, ChEBI:CHEBI:15378, ChEBI:CHEBI:32966, ChEBI:CHEBI:33019, ChEBI:CHEBI:43474, ChEBI:CHEBI:57634; EC=2.7.1.90; Evidence={ECO:0000255|HAMAP-Rule:MF_01977, ECO:0000269|PubMed:20... | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=3.4 mM for phosphate {ECO:0000269|PubMed:20868748}; KM=0.118 mM for diphosphate {ECO:0000269|PubMed:20868748}; KM=0.64 mM for fructose 6-phosphate {ECO:0000269|PubMed:20868748}; KM=0.095 mM for fructose 1,6-bisphosphate {ECO:0000269|PubMed:20868748}; KM=1.01 mM for... | PATHWAY: Carbohydrate degradation; glycolysis; D-glyceraldehyde 3-phosphate and glycerone phosphate from D-glucose: step 3/4. {ECO:0000255|HAMAP-Rule:MF_01977}. | BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 7.5. {ECO:0000269|PubMed:20868748}; | BIOPHYSICOCHEMICAL PROPERTIES: Temperature dependence: Optimum temperature is 30 degrees Celsius. {ECO:0000269|PubMed:20868748}; | FUNCTION: Catalyzes the phosphorylation of D-fructose 6-phosphate, the first committing step of glycolysis. Uses inorganic phosphate (PPi) as phosphoryl donor instead of ATP like common ATP-dependent phosphofructokinases (ATP-PFKs), which renders the reaction reversible, and can thus function both in glycolysis and glu... | Methylotuvimicrobium alcaliphilum (strain DSM 19304 / NCIMB 14124 / VKM B-2133 / 20Z) (Methylomicrobium alcaliphilum) |
G4SW86 | ERG_META2 | MSEQESRDNAAVDAVRQKYGFGFSWLVLMIALPPLVYYLWICVTYYQGELVFTSDAAAWRRFWSHVAPPTWHAAGLYAAWFLGQAALQVWAPGPTVQGMKLPDGSRLDYRMNGIFSFLFTLAVVFGLVTMGWLDATVLYDQLGPLLTVVNIFTFVFAGFLYFWGLNGKQWERPTGRPFYDYFMGTALNPRIGSLDLKLFCEARPGMIFWLLMNLSMAAKQYELHGTVTVPMLLVVGFQSFYLIDYFIHEEAVLTTWDIKHEKFGWMLCWGDLVWLPFTYTLQAQYLVHHTHDLPVWGIIAIVALNLAGYAIFRGANIQKH... | 1.3.1.70 | null | ergosterol biosynthetic process [GO:0006696]; sterol biosynthetic process [GO:0016126] | plasma membrane [GO:0005886] | delta14-sterol reductase activity [GO:0050613]; NADP binding [GO:0050661] | PF01222; | 1.20.120.1630; | ERG4/ERG24 family | null | SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000305|PubMed:25307054}; Multi-pass membrane protein {ECO:0000269|PubMed:25307054}. | CATALYTIC ACTIVITY: Reaction=4,4-dimethyl-5alpha-cholesta-8,24-dien-3beta-ol + NADP(+) = 4,4-dimethyl-5alpha-cholesta-8,14,24-trien-3beta-ol + H(+) + NADPH; Xref=Rhea:RHEA:18561, ChEBI:CHEBI:15378, ChEBI:CHEBI:17813, ChEBI:CHEBI:18364, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349; EC=1.3.1.70; Evidence={ECO:0000269|PubMed:2530... | null | PATHWAY: Steroid biosynthesis; zymosterol biosynthesis; zymosterol from lanosterol. {ECO:0000305}. | null | null | FUNCTION: Reduces the C14=C15 double bond of 4,4-dimethyl-cholesta-8,14,24-trienol to produce 4,4-dimethyl-cholesta-8,24-dienol. Complements the deletion of the Delta(14)-sterol reductase gene ERG24 in yeast. {ECO:0000269|PubMed:25307054}. | Methylotuvimicrobium alcaliphilum (strain DSM 19304 / NCIMB 14124 / VKM B-2133 / 20Z) (Methylomicrobium alcaliphilum) |
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