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 |
|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|
D9I2G1 | NL1A4_RAT | MGESQSKQESNTRVAQHGSQQDVDPTFQTKRALERERSSPQVEQSFLGQLQSLLGWSSTSKDVPLSQLIREMDHESRRHSHQSKKKLDRSEHISEGTIPEIYEKRKETISHTQSMEQKYLFQNFTKLLLLQKCCPGGSEKLVRESWHPCVPEEGGHMIEIQDLFDPNLDTEKKPQLVIIEGAAGIGKSTLARQVKRAWDEGQLYRDRFQHVFFFSCRELAQCKQLSLAELIAQGQEVPTAPTRQILSRPEKLLFILDGIDEPAWVLEDQNPELCVHWSQAQPVHTLLGSLLGKSILPEASLMLTARTTALQKLVPSLGQP... | 3.4.-.- | null | antiviral innate immune response [GO:0140374]; cellular response to UV-B [GO:0071493]; defense response to bacterium [GO:0042742]; defense response to virus [GO:0051607]; negative regulation of cellular defense response [GO:0051245]; neuron apoptotic process [GO:0051402]; NLRP1 inflammasome complex assembly [GO:1904784... | canonical inflammasome complex [GO:0061702]; cytosol [GO:0005829]; neuronal cell body [GO:0043025]; NLRP1 inflammasome complex [GO:0072558]; nucleus [GO:0005634]; protein-containing complex [GO:0032991] | ATP binding [GO:0005524]; ATP hydrolysis activity [GO:0016887]; cysteine-type endopeptidase activator activity [GO:0140608]; double-stranded DNA binding [GO:0003690]; double-stranded RNA binding [GO:0003725]; enzyme binding [GO:0019899]; molecular condensate scaffold activity [GO:0140693]; pattern recognition receptor ... | PF00619;PF13553;PF13516;PF05729;PF17776;PF17779; | 1.10.533.10;3.40.50.300;3.80.10.10; | NLRP family | PTM: [NACHT, LRR and PYD domains-containing protein 1a allele 4]: Autocatalytically cleaved. Autocatalytic cleavage in FIIND region occurs constitutively, prior to activation signals, and is required for inflammasome activity (IL1B release), possibly by facilitating CASP1 binding. Both N- and C-terminal parts remain as... | SUBCELLULAR LOCATION: Cytoplasm, cytosol {ECO:0000250|UniProtKB:Q9C000}. Cytoplasm {ECO:0000250|UniProtKB:Q9C000}. Nucleus {ECO:0000250|UniProtKB:Q9C000}.; SUBCELLULAR LOCATION: [NACHT, LRR and PYD domains-containing protein 1a, C-terminus]: Inflammasome {ECO:0000250|UniProtKB:Q9C000}. | null | null | null | null | null | FUNCTION: Acts as the sensor component of the Nlrp1a inflammasome, which mediates inflammasome activation in response to various pathogen-associated signals, leading to subsequent pyroptosis (By similarity). Inflammasomes are supramolecular complexes that assemble in the cytosol in response to pathogens and other damag... | Rattus norvegicus (Rat) |
D9I2G3 | NL1A2_RAT | MEESQSKQESNTRVAQHGSQQDVDPTFQTKRALEKERSKPRPRPLPRVQLQSLPGWSSTSKDVPLSQLIREMDHESRRCIHRSKKKLDRSEHISQGTIPEIYEKRKETISHTQSMEQKYLFQNFTKLLLLQKCCPGGSEKLVRESWHPCVPEEGGHMIEIQDLFDPNLDTEKKPQLVIIEGAAGIGKSTLARQVKRAWDEGQLYRDRFQHVFFFSCRELAQCKQLSLAELIAQGQEVPTAPTRQILSRPEKLLFILDGIDEPAWVLEDQNPELCVHWSQAQPVHTLLGSLLGKSILPEASLMLTARTTALQKLVPSLGQP... | 3.4.-.- | null | antiviral innate immune response [GO:0140374]; cellular response to UV-B [GO:0071493]; defense response to bacterium [GO:0042742]; defense response to virus [GO:0051607]; negative regulation of cellular defense response [GO:0051245]; neuron apoptotic process [GO:0051402]; NLRP1 inflammasome complex assembly [GO:1904784... | canonical inflammasome complex [GO:0061702]; cytosol [GO:0005829]; neuronal cell body [GO:0043025]; NLRP1 inflammasome complex [GO:0072558]; nucleus [GO:0005634]; protein-containing complex [GO:0032991] | ATP binding [GO:0005524]; ATP hydrolysis activity [GO:0016887]; cysteine-type endopeptidase activator activity [GO:0140608]; double-stranded DNA binding [GO:0003690]; double-stranded RNA binding [GO:0003725]; enzyme binding [GO:0019899]; molecular condensate scaffold activity [GO:0140693]; pattern recognition receptor ... | PF00619;PF13553;PF13516;PF05729;PF17776;PF17779; | 1.10.533.10;3.40.50.300;3.80.10.10; | NLRP family | PTM: [NACHT, LRR and PYD domains-containing protein 1 allele 2]: Autocatalytically cleaved. Autocatalytic cleavage in FIIND region occurs constitutively, prior to activation signals, and is required for inflammasome activity (IL1B release), possibly by facilitating CASP1 binding. Both N- and C-terminal parts remain ass... | SUBCELLULAR LOCATION: Cytoplasm, cytosol {ECO:0000250|UniProtKB:Q9C000}. Cytoplasm {ECO:0000250|UniProtKB:Q9C000}. Nucleus {ECO:0000250|UniProtKB:Q9C000}.; SUBCELLULAR LOCATION: [NACHT, LRR and PYD domains-containing protein 1a, C-terminus]: Inflammasome {ECO:0000250|UniProtKB:Q9C000}. | null | null | null | null | null | FUNCTION: Acts as the sensor component of the Nlrp1a inflammasome, which mediates inflammasome activation in response to various pathogen-associated signals, leading to subsequent pyroptosis (By similarity). Inflammasomes are supramolecular complexes that assemble in the cytosol in response to pathogens and other damag... | Rattus norvegicus (Rat) |
D9I2G4 | NL1A5_RAT | MGESQSKQESNTRVAQHGSQQDVDPTFQTKRALERERSSPQVEQSFLGQLQSLLGWSSTSKDVPLSQLIREMDHESRRHSHQSKKKLDRSEHISEGTIPEIYEKRKETISHTQSMEQKYLFQNFTKLLLLQKCCPGGSEKLVRESWHPCVPEEGGHMIEIQDLFDPNLDTEKKPQLVIIEGAAGIGKSTLARQVKRAWEEGQLYRDRFQHVFFFSCRELAQCKQLSLAELIAQGQEVLTAPTRQILSRPEKLLFILDGIDEPAWVLEDQNPELCVHWSQAQPVHTLLGSLLGKSILPEASLMLTARTTALQKLIPSLGQP... | 3.4.-.- | null | antiviral innate immune response [GO:0140374]; cellular response to UV-B [GO:0071493]; defense response to bacterium [GO:0042742]; defense response to virus [GO:0051607]; negative regulation of cellular defense response [GO:0051245]; neuron apoptotic process [GO:0051402]; NLRP1 inflammasome complex assembly [GO:1904784... | canonical inflammasome complex [GO:0061702]; cytosol [GO:0005829]; neuronal cell body [GO:0043025]; NLRP1 inflammasome complex [GO:0072558]; nucleus [GO:0005634]; protein-containing complex [GO:0032991] | ATP binding [GO:0005524]; ATP hydrolysis activity [GO:0016887]; cysteine-type endopeptidase activator activity [GO:0140608]; double-stranded DNA binding [GO:0003690]; double-stranded RNA binding [GO:0003725]; enzyme binding [GO:0019899]; molecular condensate scaffold activity [GO:0140693]; pattern recognition receptor ... | PF00619;PF13553;PF13516;PF05729;PF17776;PF17779; | 1.10.533.10;3.40.50.300;3.80.10.10; | NLRP family | PTM: [NACHT, LRR and PYD domains-containing protein 1a allele 5]: Autocatalytically cleaved. Autocatalytic cleavage in FIIND region occurs constitutively, prior to activation signals, and is required for inflammasome activity (IL1B release), possibly by facilitating CASP1 binding. Both N- and C-terminal parts remain as... | SUBCELLULAR LOCATION: Cytoplasm, cytosol {ECO:0000250|UniProtKB:Q9C000}. Cytoplasm {ECO:0000250|UniProtKB:Q9C000}. Nucleus {ECO:0000250|UniProtKB:Q9C000}.; SUBCELLULAR LOCATION: [NACHT, LRR and PYD domains-containing protein 1a, C-terminus]: Inflammasome {ECO:0000250|UniProtKB:Q9C000}. | null | null | null | null | null | FUNCTION: Acts as the sensor component of the Nlrp1a inflammasome, which mediates inflammasome activation in response to various pathogen-associated signals, leading to subsequent pyroptosis (By similarity). Inflammasomes are supramolecular complexes that assemble in the cytosol in response to pathogens and other damag... | Rattus norvegicus (Rat) |
D9I2H0 | NL1A3_RAT | MGESQSKQESNTRVAQHGSQQDVDPTFQTKRALERERSSPQVEQSFLGQLQSLLGWSSTSKDVPLSQLIREMDHESRRHSHQSKKKLDRSEHISEGTIPEIYEKRKETISHTQSMEQKYLFQNFTKLLLLQKCCPGGSEKLVRESWHPCVPEEGGHMIEIQDLFDPNLDTEKKPQLVIIEGAAGIGKSTLARQVKRAWDEGQLYRDRFQHVFFFSCRELAQCKQLSLAELIAQGQEVPTAPTRQILSRPEKLLFILDGIDEPAWVLEDQNPELCVHWSQAQPVHTLLGSLLGKSILPEASLMLTARTTALQKLVPSLGQP... | 3.4.-.- | null | antiviral innate immune response [GO:0140374]; cellular response to UV-B [GO:0071493]; defense response to bacterium [GO:0042742]; defense response to virus [GO:0051607]; negative regulation of cellular defense response [GO:0051245]; neuron apoptotic process [GO:0051402]; NLRP1 inflammasome complex assembly [GO:1904784... | canonical inflammasome complex [GO:0061702]; cytosol [GO:0005829]; neuronal cell body [GO:0043025]; NLRP1 inflammasome complex [GO:0072558]; nucleus [GO:0005634]; protein-containing complex [GO:0032991] | ATP binding [GO:0005524]; ATP hydrolysis activity [GO:0016887]; cysteine-type endopeptidase activator activity [GO:0140608]; double-stranded DNA binding [GO:0003690]; double-stranded RNA binding [GO:0003725]; enzyme binding [GO:0019899]; molecular condensate scaffold activity [GO:0140693]; pattern recognition receptor ... | PF00619;PF13553;PF13516;PF05729;PF17776;PF17779; | 1.10.533.10;3.40.50.300;3.80.10.10; | NLRP family | PTM: [NACHT, LRR and PYD domains-containing protein 1a allele 3]: Autocatalytically cleaved. Autocatalytic cleavage in FIIND region occurs constitutively, prior to activation signals, and is required for inflammasome activity (IL1B release), possibly by facilitating CASP1 binding. Both N- and C-terminal parts remain as... | SUBCELLULAR LOCATION: Cytoplasm, cytosol {ECO:0000250|UniProtKB:Q9C000}. Cytoplasm {ECO:0000250|UniProtKB:Q9C000}. Nucleus {ECO:0000250|UniProtKB:Q9C000}.; SUBCELLULAR LOCATION: [NACHT, LRR and PYD domains-containing protein 1a, C-terminus]: Inflammasome {ECO:0000250|UniProtKB:Q9C000}. | null | null | null | null | null | FUNCTION: Acts as the sensor component of the Nlrp1a inflammasome, which mediates inflammasome activation in response to various pathogen-associated signals, leading to subsequent pyroptosis (By similarity). Inflammasomes are supramolecular complexes that assemble in the cytosol in response to pathogens and other damag... | Rattus norvegicus (Rat) |
D9IA43 | CCON1_STUST | MNTATSTAYSYKVVRQFAIMTVVWGIVGMGLGVFIAAQLAWPFLNFDLPWTSFGRLRPLHTNAVIFAFGGCALFATSYYSVQRTCQTTLFAPKLAAFTFWGWQLVILLAAISLPLGFTSSKEYAELEWPIDILITIVWVAYAVVFFGTLAKRKVKHIYVGNWFFGAFILTVAILHVVNNLEIPVTAMKSYSLYAGATDAMVQWWYGHNAVGFFLTAGFLGIMYYFVPKQAERPVYSYRLSIVHFWALITVYIWAGPHHLHYTALPDWAQSLGMVMSLILLAPSWGGMINGMMTLSGAWHKLRSDPILRFLVVSLAFYGMS... | 7.1.1.9 | COFACTOR: Name=Cu(2+); Xref=ChEBI:CHEBI:29036; Evidence={ECO:0000269|PubMed:20576851}; Note=Binds 1 copper ion per subunit, denoted as copper B. {ECO:0000269|PubMed:20576851}; COFACTOR: Name=heme b; Xref=ChEBI:CHEBI:60344; Evidence={ECO:0000269|PubMed:20576851}; Note=Binds 2 heme b groups per subunit, denoted as high- ... | aerobic electron transport chain [GO:0019646]; aerobic respiration, using ferrous ions as electron donor [GO:0019411]; electron transport coupled proton transport [GO:0015990]; oxidative phosphorylation [GO:0006119]; proton transmembrane transport [GO:1902600] | cytochrome complex [GO:0070069]; plasma membrane [GO:0005886]; plasma membrane respirasome [GO:0070470]; plasma membrane respiratory chain complex IV [GO:0045278] | copper ion binding [GO:0005507]; cytochrome-c oxidase activity [GO:0004129]; heme binding [GO:0020037]; iron ion binding [GO:0005506]; oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen [GO:0016705]; oxygen binding [GO:0019825]; ubiquinol-cytochrome-c reductase activit... | PF00115; | 1.20.210.10; | Heme-copper respiratory oxidase family | null | SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000250|UniProtKB:P0ABI8}; Multi-pass membrane protein {ECO:0000255}. | CATALYTIC ACTIVITY: Reaction=4 Fe(II)-[cytochrome c] + 8 H(+)(in) + O2 = 4 Fe(III)-[cytochrome c] + 4 H(+)(out) + 2 H2O; Xref=Rhea:RHEA:11436, Rhea:RHEA-COMP:10350, Rhea:RHEA-COMP:14399, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, ChEBI:CHEBI:29033, ChEBI:CHEBI:29034; EC=7.1.1.9; Evidence={ECO:0000305}; | null | PATHWAY: Energy metabolism; oxidative phosphorylation. {ECO:0000305}. | null | null | FUNCTION: Cbb3-type cytochrome c oxidase is the component of the respiratory chain that catalyzes the reduction of oxygen to water. Subunits CcoN and CcoO form the functional core of the enzyme complex. Subunits CcoP and CcoQ may optionally bind to the core. CcoN is the catalytic subunit of the enzyme. Electrons origin... | Stutzerimonas stutzeri (Pseudomonas stutzeri) |
D9IVE5 | ANM2_XENLA | MESSSECSSISDFQDSTEGDDANTLPENLCMREYVVICDYVATDNTQLSLCSGDKVLLLNAVSQDWWWVNHNGTCGYVPASHLHDALNEQEDTEVNDPWQDEEYYGSYKTLKLHLEMLSDVPRTMTYQNVILKNSSSLCGKHILDLGCGTGIISFFCAKFAQPEAVYAVEASKIAEQTCRLVEQNGISSLVHVIRQQAEELDLPTKVDVLVSEWMGTCLLFEFMLESVLQARDRWLKEDGVMWPSTACIHLVPCSAYKEYSNKVLFWDNPYQLDFSLLKPPATKEFFAKPQPDYILQPEDCLSEPCTLFHLNLKTLQVAE... | 2.1.1.319 | null | developmental cell growth [GO:0048588]; methylation [GO:0032259]; negative regulation of DNA-templated transcription [GO:0045892]; negative regulation of G1/S transition of mitotic cell cycle [GO:2000134]; negative regulation of NF-kappaB transcription factor activity [GO:0032088]; positive regulation of apoptotic proc... | cytoplasm [GO:0005737]; nucleus [GO:0005634] | histone H3R8 methyltransferase activity [GO:0140592]; nuclear estrogen receptor binding [GO:0030331]; protein-arginine omega-N asymmetric methyltransferase activity [GO:0035242] | PF13649;PF07653; | 2.70.160.11;2.30.30.40;3.40.50.150; | Class I-like SAM-binding methyltransferase superfamily, Protein arginine N-methyltransferase family | null | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Nucleus {ECO:0000250}. | CATALYTIC ACTIVITY: Reaction=L-arginyl-[protein] + 2 S-adenosyl-L-methionine = 2 H(+) + N(omega),N(omega)-dimethyl-L-arginyl-[protein] + 2 S-adenosyl-L-homocysteine; Xref=Rhea:RHEA:48096, Rhea:RHEA-COMP:10532, Rhea:RHEA-COMP:11991, ChEBI:CHEBI:15378, ChEBI:CHEBI:29965, ChEBI:CHEBI:57856, ChEBI:CHEBI:59789, ChEBI:CHEBI:... | null | null | null | null | FUNCTION: Arginine methyltransferase that methylates the guanidino nitrogens of arginyl residues in proteins such as histones. Involved in growth regulation (By similarity). Involved in embryonic dorsal development. {ECO:0000250, ECO:0000269|PubMed:20708585}. | Xenopus laevis (African clawed frog) |
D9J041 | MERA_LYSSH | MNKFKVNISGMTCTGCEKHVESALEKIGAKNIESSYRRGEAVFELPDDIEVESAIKAIDEANYQAGEIEEVSSLENVALINEDNYDLLIIGSGAAAFSSAIKAIEYGAKVGMIERGTVGGTCVNIGCVPSKTLLRAGEIIHLSKDNPFIGLQTSAGEVDLASLITQKDKLVSELRNQKYMDLIDEYNFDLIKGEAKFVDASTVEVNGAKLSAKRFLIATGASPSLPQISGLEKMDYLTSTTLLELKKIPKRLTVIGSGYIGMELGQLFHHLGSEITLMQRSERLLKEYDPEISESVEKALIEQGINLVKGATFERVEQSG... | 1.16.1.1 | COFACTOR: Name=FAD; Xref=ChEBI:CHEBI:57692; Evidence={ECO:0000255|PIRNR:PIRNR000350, ECO:0000255|PIRSR:PIRSR000350-3, ECO:0000255|RuleBase:RU361223, ECO:0000269|PubMed:28894951}; Note=Binds 1 FAD per subunit. {ECO:0000255|PIRNR:PIRNR000350, ECO:0000255|PIRSR:PIRSR000350-3, ECO:0000255|RuleBase:RU361223}; | detoxification of mercury ion [GO:0050787] | null | flavin adenine dinucleotide binding [GO:0050660]; mercury (II) reductase activity [GO:0016152]; mercury ion binding [GO:0045340]; NADP binding [GO:0050661]; oxidoreductase activity, acting on a sulfur group of donors, NAD(P) as acceptor [GO:0016668] | PF00403;PF07992;PF02852; | 3.30.390.30;3.30.70.100;3.50.50.60; | Class-I pyridine nucleotide-disulfide oxidoreductase family | null | null | CATALYTIC ACTIVITY: Reaction=H(+) + Hg + NADP(+) = Hg(2+) + NADPH; Xref=Rhea:RHEA:23856, ChEBI:CHEBI:15378, ChEBI:CHEBI:16170, ChEBI:CHEBI:16793, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349; EC=1.16.1.1; Evidence={ECO:0000255|PIRNR:PIRNR000350, ECO:0000255|RuleBase:RU361223, ECO:0000269|PubMed:28894951}; | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=231 uM for NADPH {ECO:0000269|PubMed:28894951}; Vmax=18 umol/min/mg enzyme {ECO:0000269|PubMed:28894951}; | null | BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 7-7.5. {ECO:0000269|PubMed:28894951}; | BIOPHYSICOCHEMICAL PROPERTIES: Temperature dependence: Optimum temperature is 25-50 degrees Celsius. Activity is inhibited only slightly at 60 degrees Celsius, but at temperatures of 70 degrees Celsius and above, the activity is reduced to about 14% of normal activity. {ECO:0000269|PubMed:28894951}; | FUNCTION: Resistance to Hg(2+) in bacteria appears to be governed by a specialized system which includes mercuric reductase (By similarity) (PubMed:28894951). MerA protein is responsible for volatilizing mercury as Hg(0) (By similarity) (PubMed:28894951). Catalyzes reduction of Hg(2+) to elemental Hg, which is volatile... | Lysinibacillus sphaericus (Bacillus sphaericus) |
D9N129 | WDR20_CAEEL | MHQHMLGPSTSLGGTNNSALQSSVLSEGVLLSHSQPTREEIKKNFETREGVYRSVPSAEFSRPRPLPQYHMPPGIASAAASQIAAAGSTVRVSFLNGAEKSVESPEAVAPTSSTYEHHKNEPNGARIDMVDEAQADKICFNVGKELYVFSYRGTQTETDLSRPIDKRVYKGTSPTYHAFNQESAKNGSCQLLIGFTLGQLQIIDPLEKSSSSPFSRLYNEDRYIEKTSVTCIRWLPGDSNIFLASYVSGNLYVYDQRISAASSNNNGSSQPPPWTIHKEGDKFAIHTWKGKVQRNPVTRWQIGEGSIHQFSFSGSDGKMM... | null | null | carbon catabolite repression of transcription [GO:0045013]; positive regulation of gene expression [GO:0010628]; positive regulation of locomotion involved in locomotory behavior [GO:0090326]; positive regulation of protein deubiquitination [GO:1903003]; positive regulation of protein localization to cell surface [GO:2... | cell division site [GO:0032153]; cell tip [GO:0051286]; nucleus [GO:0005634] | null | PF00400; | 2.130.10.10; | null | null | null | null | null | null | null | null | FUNCTION: Together with wdr-48, binds to and stimulates the activity of the deubiquitinating enzyme usp-46, leading to deubiquitination and stabilization of the glr-1 glutamate receptor. {ECO:0000269|PubMed:24356955}. | Caenorhabditis elegans |
D9N164 | IRK10_PARME | MTGGMKPPARKPRILNSDGSSNITRLGLEKRGWLDDHYHDLLTVSWPVFITLITGLYLVTNALFALAYLACGDVIENARPGSFTDAFFFSVQTMATIGYGKLIPIGPLANTLVTLEALCGMLGLAVAASLIYARFTRPTAGVLFSSRMVISDFEGKPTLMMRLANLRIEQIIEADVHLVLVRSEISQEGMVFRRFHDLTLTRSRSPIFSLSWTVMHPIDHHSPIYGETDETLRNSHSEFLVLFTGHHEAFAQNVHARHAYSCDEIIWGGHFVDVFTTLPDGRRALDLGKFHEIAQ | null | null | potassium ion import across plasma membrane [GO:1990573]; regulation of monoatomic ion transmembrane transport [GO:0034765] | monoatomic ion channel complex [GO:0034702]; plasma membrane [GO:0005886] | identical protein binding [GO:0042802]; inward rectifier potassium channel activity [GO:0005242] | PF07885;PF17655; | 1.10.287.70;2.60.40.1400; | Inward rectifier-type potassium channel (TC 1.A.2.1) family, KCNJ11 subfamily | null | SUBCELLULAR LOCATION: Membrane {ECO:0000269|PubMed:16216578, ECO:0000269|PubMed:20564790, ECO:0000269|PubMed:20876570, ECO:0000269|PubMed:22231399}; Multi-pass membrane protein {ECO:0000269|PubMed:16216578, ECO:0000269|PubMed:20564790, ECO:0000269|PubMed:20876570, ECO:0000269|PubMed:22231399}. | null | null | null | null | null | FUNCTION: Inward rectifier potassium channel that mediates potassium uptake into the cell. Inward rectifier potassium channels are characterized by a greater tendency to allow potassium to flow into the cell rather than out of it. The inward rectification may be achieved by the blockage of outward current by cytoplasmi... | Paramagnetospirillum magnetotacticum (Aquaspirillum magnetotacticum) |
D9PTN5 | MYRF2_CAEEL | MGDLNPAETPEPKKNPVAKIASNLYSTQIVKPVPSVSNSTNLSPCQNPNMTNLFYITLLQNKLNKYTQQLLKKNEEGLNDPLANVEQFNIIQFLQNDVDFNLPIEAFEQGNMDQNIRIDPILQRQQMANQPMLMPQHMLQQLHQQQIYEQQLASMPMTPAITDLTRHGSSSSPSTTNSDPPYSPEGLNNFGLGTQRPNHGVIPNDISNVPQHINRQFNPRMGPNTSPNPPSFPQFLNSNHPTPGSYVQSISPDSNGQGFAQSNLYNALNVSSDESINGSDDIPNRKRPRMDQNMDPSFIMHAPVSGKLGAEVTEEGGQPN... | 3.4.-.- | null | cell differentiation [GO:0030154]; positive regulation of DNA-templated transcription [GO:0045893]; protein autoprocessing [GO:0016540]; regulation of neuron remodeling [GO:1904799]; regulation of synapse assembly [GO:0051963] | apical plasma membrane [GO:0016324]; endoplasmic reticulum [GO:0005783]; endoplasmic reticulum membrane [GO:0005789]; nucleus [GO:0005634]; transcription regulator complex [GO:0005667] | DNA-binding transcription factor activity [GO:0003700]; peptidase activity [GO:0008233]; sequence-specific DNA binding [GO:0043565] | PF13888;PF13887;PF05224;PF13884; | 2.60.40.1390; | MRF family | PTM: Myelin regulatory factor: Follows autocatalytic cleavage via the peptidase S74 domain. Autoprocessing is apparently constitutive and is essential for transcriptional activity. {ECO:0000250|UniProtKB:G5EFI7}. | SUBCELLULAR LOCATION: [Myelin regulatory factor homolog 2]: Endoplasmic reticulum membrane {ECO:0000269|PubMed:28441531}; Single-pass membrane protein {ECO:0000255}. Nucleus {ECO:0000269|PubMed:33950834}. Apical cell membrane {ECO:0000269|PubMed:33950834}; Single-pass membrane protein {ECO:0000255}. Note=In early L1 la... | null | null | null | null | null | FUNCTION: [Myelin regulatory factor homolog 2]: Constitutes a precursor of the transcription factor (PubMed:28441531). Mediates the autocatalytic cleavage that releases the Myelin regulatory factor homolog 2, N-terminal component that specifically activates transcription of genes involved in synaptic rewiring during ne... | Caenorhabditis elegans |
D9PUX5 | TFRB_METTM | MINVKVLRFEPGVDEKPHLESYDIPSKEKMKVLDALQLINKMYNANIAFRSSCRAGQCGSCAVKMNGEVVLACRAEVEDGAVIEPVDLPVIKDLMVDRSEIEDKVRAMGLYLQSEARGIQRIKPEDYQDTKKLRGCIECFSCISSCPVIKESTEYAGPYFMRYISKFAFDPRDEAERAAGGVEEGLYCCTTCGKCAEVCPKELNVPGDAIEKLRAMACREGAGPLDAHRKIKKLISETGRSVDHIGKGFIESVGQNPGSRIGFFTGCLVDYRMPDVGMALLRVLREHGFEVDVPDGQVCCGSPMIRTGQLDIVEDLVERN... | 1.3.4.1 | COFACTOR: Name=[2Fe-2S] cluster; Xref=ChEBI:CHEBI:190135; Evidence={ECO:0000269|PubMed:9578488}; Note=Binds 1 [2Fe-2S] cluster per subunit. {ECO:0000269|PubMed:9578488}; COFACTOR: Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883; Evidence={ECO:0000269|PubMed:9578488}; Note=Binds 2 [4Fe-4S] clusters per subunit. {ECO:00002... | fumarate metabolic process [GO:0006106]; tricarboxylic acid cycle [GO:0006099] | cytoplasm [GO:0005737] | 2 iron, 2 sulfur cluster binding [GO:0051537]; 4 iron, 4 sulfur cluster binding [GO:0051539]; electron transfer activity [GO:0009055]; iron-sulfur cluster binding [GO:0051536]; metal ion binding [GO:0046872]; oxidoreductase activity, acting on the CH-CH group of donors [GO:0016627] | PF02754;PF13085;PF13183; | 3.10.20.30;1.10.1060.10; | null | null | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000303|PubMed:2499256}. | CATALYTIC ACTIVITY: Reaction=coenzyme B + coenzyme M + fumarate = coenzyme M-coenzyme B heterodisulfide + succinate; Xref=Rhea:RHEA:40235, ChEBI:CHEBI:29806, ChEBI:CHEBI:30031, ChEBI:CHEBI:58319, ChEBI:CHEBI:58411, ChEBI:CHEBI:58596; EC=1.3.4.1; Evidence={ECO:0000269|PubMed:9578488}; | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=0.2 mM for fumarate {ECO:0000269|PubMed:2499256}; | null | BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is7.0. {ECO:0000269|PubMed:2499256}; | BIOPHYSICOCHEMICAL PROPERTIES: Temperature dependence: Optimum temperature is 75 degrees Celsius. {ECO:0000269|PubMed:2499256}; | FUNCTION: Catalyzes the reduction of fumarate with reduced coenzyme M (CoM-S-H) and coenzyme B (CoB-S-H). In vitro, is able to reduces fumarate with reduced benzyl viologen, oxidize CoM-S-H and CoB-S-H to CoM-S-S-CoB with methylene blue, and reduce CoM-S-S-CoB with reduced benzyl viologen. The enzyme has specificity fo... | Methanothermobacter marburgensis (strain ATCC BAA-927 / DSM 2133 / JCM 14651 / NBRC 100331 / OCM 82 / Marburg) (Methanobacterium thermoautotrophicum) |
D9PVP5 | FNO_METTM | MKIAVLGGTGDQGLGLALRLALAGEEVIIGSRDAEKAVSAAQKVLEIAERDDLKVKGATNAEAAEEAEVAILTVPLQAQMATLGSVKEAIKGKVLIDATVPIDSCLGGSAVRYIDLWDGSAAERAARFLEDQGTRVAAAFNNISASALLDITGPVDCDCLIASDHRDALDLASELAEKIDGVRAIDCGGLENARVIEKITPLLINLNIKNRIRNAGIRITNLPE | 1.5.1.40 | null | copper ion import [GO:0015677]; NADPH regeneration [GO:0006740] | plasma membrane [GO:0005886] | 8-hydroxy-5-deazaflavin:NADPH oxidoreductase activity [GO:0102261]; coenzyme F420 binding [GO:0070967]; cupric reductase activity [GO:0008823]; ferric-chelate reductase (NADPH) activity [GO:0052851]; NADP binding [GO:0050661]; oxidoreductase activity, acting on NAD(P)H [GO:0016651]; reduced coenzyme F420:NADP+ oxidored... | PF03807; | 3.40.50.720; | F420-dependent NADP reductase family | null | null | CATALYTIC ACTIVITY: Reaction=NADP(+) + reduced coenzyme F420-(gamma-L-Glu)(n) = 2 H(+) + NADPH + oxidized coenzyme F420-(gamma-L-Glu)(n); Xref=Rhea:RHEA:31363, Rhea:RHEA-COMP:12939, Rhea:RHEA-COMP:14378, ChEBI:CHEBI:15378, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349, ChEBI:CHEBI:133980, ChEBI:CHEBI:139511; EC=1.5.1.40; Eviden... | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=0.3 mM for F420 (at pH 6.0) {ECO:0000269|PubMed:9821972}; KM=50 uM for NADPH (at pH 6.0) {ECO:0000269|PubMed:9821972}; KM=0.15 mM for F420H(2) (at pH 8.0) {ECO:0000269|PubMed:9821972}; KM=70 uM for NADP(+) (at pH 8.0) {ECO:0000269|PubMed:9821972}; Vmax=1500 umol/mi... | null | BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 3.5 for F420 reduction with NADPH, and 8.0 for NADP(+) reduction with F420H(2). {ECO:0000269|PubMed:9821972}; | null | FUNCTION: Catalyzes the reduction of NADP(+) with F420H(2) via hydride transfer, and the reverse reaction, i.e. the reduction of F420 with NADPH. Probably functions in the regeneration of NADPH required in biosynthetic reactions. {ECO:0000269|PubMed:9821972}. | Methanothermobacter marburgensis (strain ATCC BAA-927 / DSM 2133 / JCM 14651 / NBRC 100331 / OCM 82 / Marburg) (Methanobacterium thermoautotrophicum) |
D9TT09 | SUCPP_THETC | MALKNKVQLITYPDSLGGNLKTLNDVLEKYFSDVFGGVHILPPFPSSGDRGFAPITYSEIEPKFGTWYDIKKMAENFDILLDLMVNHVSRRSIYFQDFLKKGRKSEYADMFITLDKLWKDGKPVKGDIEKMFLRRTLPYSTFKIEETGEEEKVWTTFGKTDPSEQIDLDVNSHLVREFLLEVFKTFSNFGVKIVRLDAVGYVIKKIGTSCFFVEPEIYEFLDWAKGQAASYGIELLLEVHSQFEVQYKLAERGFLIYDFILPFTVLYTLINKSNEMLYHYLKNRPINQFTMLDCHDGIPVKPDLDGLIDTKKAKEVVDIC... | 2.4.1.329 | null | carbohydrate metabolic process [GO:0005975] | null | 1,4-alpha-oligoglucan phosphorylase activity [GO:0004645]; hexosyltransferase activity [GO:0016758] | PF00128; | 3.20.20.80; | Glycosyl hydrolase 13 family, Sucrose phosphorylase subfamily | null | null | CATALYTIC ACTIVITY: Reaction=phosphate + sucrose 6(F)-phosphate = alpha-D-glucose 1-phosphate + beta-D-fructose 6-phosphate; Xref=Rhea:RHEA:38863, ChEBI:CHEBI:43474, ChEBI:CHEBI:57634, ChEBI:CHEBI:57723, ChEBI:CHEBI:58601; EC=2.4.1.329; Evidence={ECO:0000269|PubMed:24599311}; PhysiologicalDirection=left-to-right; Xref=... | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=6.9 mM for phosphate (at 55 degrees Celsius and pH 6.5) {ECO:0000269|PubMed:24599311}; KM=12.7 mM for sucrose 6(F)-phosphate (at 55 degrees Celsius and pH 6.5) {ECO:0000269|PubMed:24599311}; KM=76.5 mM for sucrose (at 55 degrees Celsius and pH 6.5) {ECO:0000269|Pub... | null | BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 6 and 6.5 for the synthetic and phosphorolytic reaction, respectively. Thermostable. Has a half-life of 60 hours at 60 degrees Celsius. {ECO:0000269|PubMed:24599311}; | BIOPHYSICOCHEMICAL PROPERTIES: Temperature dependence: Optimum temperature is 55 degrees Celsius. {ECO:0000269|PubMed:24599311}; | FUNCTION: Catalyzes the reversible phosphorolysis of sucrose 6(F)-phosphate into alpha-D-glucose 1-phosphate (Glc1P) and D-fructose 6-phosphate. May be involved in a new pathway for the degradation of sucrose, which could become phosphorylated on its fructose moiety during uptake via a PTS system. To a lesser extent, c... | Thermoanaerobacterium thermosaccharolyticum (strain ATCC 7956 / DSM 571 / NCIMB 9385 / NCA 3814 / NCTC 13789 / WDCM 00135 / 2032) (Clostridium thermosaccharolyticum) |
D9X0I3 | ACNA_STRVT | MSANSFDARSTLQVGDESYEIFRLDKVEGSARLPYSLKVLLENLLRTEDGANITADHIRALGGWDSQAQPSQEIQFTPARVIMQDFTGVPCVVDLATMREAVKELGGDPAKINPLAPAELVIDHSVIADKFGTNDAFKQNVELEYGRNKERYQFLRWGQTAFDEFKVVPPGTGIVHQVNIEHLARTVMVRGGQAYPDTLVGTDSHTTMVNGLGVLGWGVGGIEAEAAMLGQPVSMLIPRVVGFKLTGELKPGTTATDLVLTITEMLRGHGVVGKFVEFYGEGVAATSLANRATIGNMSPEFGSTAAIFPIDDETLNYLRL... | 4.2.1.3 | COFACTOR: Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883; Evidence={ECO:0000250|UniProtKB:P36683}; Note=Binds 1 [4Fe-4S] cluster per subunit. {ECO:0000250|UniProtKB:P36683}; | citrate metabolic process [GO:0006101]; tricarboxylic acid cycle [GO:0006099] | cytosol [GO:0005829] | 2-methylisocitrate dehydratase activity [GO:0047456]; 4 iron, 4 sulfur cluster binding [GO:0051539]; aconitate hydratase activity [GO:0003994]; iron-responsive element binding [GO:0030350]; metal ion binding [GO:0046872] | PF00330;PF00694; | 6.10.190.10;3.30.499.10;3.20.19.10; | Aconitase/IPM isomerase family | null | null | CATALYTIC ACTIVITY: Reaction=citrate = D-threo-isocitrate; Xref=Rhea:RHEA:10336, ChEBI:CHEBI:15562, ChEBI:CHEBI:16947; EC=4.2.1.3; Evidence={ECO:0000269|PubMed:23116164, ECO:0000305|PubMed:10559181}; CATALYTIC ACTIVITY: Reaction=citrate = cis-aconitate + H2O; Xref=Rhea:RHEA:10228, ChEBI:CHEBI:15377, ChEBI:CHEBI:16383, ... | null | PATHWAY: Carbohydrate metabolism; tricarboxylic acid cycle; isocitrate from oxaloacetate: step 2/2. {ECO:0000305|PubMed:10559181}. | null | null | FUNCTION: Catalyzes the reversible isomerization of citrate to isocitrate via cis-aconitate in the tricarboxylic acid (TCA) cycle (PubMed:10559181, PubMed:23116164). Aconitase activity is important for the initiation of morphological and physiological differentiation of S.viridochromogenes (PubMed:10559181, PubMed:2311... | Streptomyces viridochromogenes (strain DSM 40736 / JCM 4977 / BCRC 1201 / Tue 494) |
E0CJS3 | EOBII_PETHY | MDKKPCNSQDAEVRKGPWTMEEDLILINYIANHGEGVWNSLAKSAGLKRTGKSCRLRWLNYLRPDVRRGNITPEEQLLIMELHAKWGNRWSKIAKHLPGRTDNEIKNYWRTRIQKHIKQAETMNGQAASSEQNDHQEACTSQMSNGPNDNTIDQTYSPTSYSGNVDTFQAGPNFLTEANDNMWSMEDIWSMQLLNGD | null | null | circadian rhythm [GO:0007623]; floral organ senescence [GO:0080187]; green leaf volatile biosynthetic process [GO:0010597]; regulation of cell wall organization or biogenesis [GO:1903338]; regulation of DNA-templated transcription [GO:0006355]; regulation of flower development [GO:0009909]; regulation of gene expressio... | nucleus [GO:0005634]; plant-type cell wall [GO:0009505] | DNA-binding transcription factor activity [GO:0003700]; sequence-specific DNA binding [GO:0043565]; transcription cis-regulatory region binding [GO:0000976] | PF00249; | 1.10.10.60; | null | null | SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00625, ECO:0000269|PubMed:20543029}. | null | null | null | null | null | FUNCTION: MYB-type transcription factor controlling the production of volatile organic compounds (VOCs), including floral volatile benzenoids and phenylpropanoids (FVBP), in flowers of fragrant cultivars (e.g. cv. Mitchell and cv. V26) by regulating the expression of ODO1 and EOBI, key regulators of the shikimate pathw... | Petunia hybrida (Petunia) |
E0CX11 | STMP1_HUMAN | MLQFLLGFTLGNVVGMYLAQNYDIPNLAKKLEEIKKDLDAKKKPPSA | null | null | innate immune response [GO:0045087]; mitochondrial cytochrome c oxidase assembly [GO:0033617]; mitochondrial respirasome assembly [GO:0097250]; mitochondrial respiratory chain complex III assembly [GO:0034551]; positive regulation of interleukin-1 beta production [GO:0032731]; positive regulation of NLRP3 inflammasome ... | mitochondrial inner membrane [GO:0005743]; mitochondrial intermembrane space [GO:0005758]; mitochondrial outer membrane [GO:0005741]; mitochondrial respirasome [GO:0005746] | null | PF15054; | null | STMP1 family | null | SUBCELLULAR LOCATION: Mitochondrion inner membrane {ECO:0000269|PubMed:35450818}; Single-pass membrane protein {ECO:0000255}. Mitochondrion outer membrane {ECO:0000250|UniProtKB:P0DP99}; Single-pass membrane protein {ECO:0000255}. Mitochondrion intermembrane space {ECO:0000250|UniProtKB:P0DP99}. | null | null | null | null | null | FUNCTION: Microprotein involved in mitochondrial respiratory chain complex III (ubiquinol-cytochrome c oxidoreductase) and complex IV (mitochondrial cytochrome c oxidase complex) assembly (PubMed:35450818). Required for the formation of mitochondrial supercomplexes (SCs) (PubMed:35450818). Also required for the activat... | Homo sapiens (Human) |
E0CZ16 | KLHL3_MOUSE | MEGESVKPSPQPTAQAEDEEKNRRTVTVNAAHMGKAFKVMNELRSKRLLCDVMIVAEDVEVEAHRVVLAACSPYFCAMFTGDMSESKAKKIEIKDVDGQTLSKLIDYIYTAEIEVTEENVQVLLPAASLLQLMDVRQNCCDFLQSQLHPTNCLGIRAFADVHTCTDLLQQANAYAEQHFPEVMLGEEFLSLSLDQVCSLISSDKLTVSSEEKVFEAVISWINYEKETRLDHMAKLMEHVRLPLLPRDYLVQTVEEEALIKNNNTCKDFLIEAMKYHLLPLDQRLLIKNPRTKPRTPVSLPKVMIVVGGQAPKAIRSVECY... | null | null | distal tubule morphogenesis [GO:0072156]; gene expression [GO:0010467]; monoatomic ion homeostasis [GO:0050801]; potassium ion homeostasis [GO:0055075]; proteasome-mediated ubiquitin-dependent protein catabolic process [GO:0043161]; protein catabolic process [GO:0030163]; protein K48-linked ubiquitination [GO:0070936];... | Cul3-RING ubiquitin ligase complex [GO:0031463]; cytoskeleton [GO:0005856]; cytosol [GO:0005829] | actin binding [GO:0003779]; cullin family protein binding [GO:0097602]; ubiquitin ligase-substrate adaptor activity [GO:1990756] | PF07707;PF00651;PF01344; | 1.25.40.420;2.120.10.80; | KLHL3 family | PTM: Phosphorylation at Ser-433 by PKA or PKC decreases the interaction with WNK1 and WNK4, leading to inhibit their degradation by the BCR(KLHL3) complex (By similarity). Phosphorylated at Ser-433 by PKC in response to angiotensin II signaling, decreasing ability to promote degradation of WNK1 and WNK4, leading to act... | SUBCELLULAR LOCATION: Cytoplasm, cytosol {ECO:0000250|UniProtKB:Q9UH77}. Cytoplasm, cytoskeleton {ECO:0000250|UniProtKB:Q9UH77}. | null | null | PATHWAY: Protein modification; protein ubiquitination. {ECO:0000250|UniProtKB:Q9UH77}. | null | null | FUNCTION: Substrate-specific adapter of a BCR (BTB-CUL3-RBX1) E3 ubiquitin ligase complex that acts as a regulator of ion transport in the distal nephron (PubMed:24821705, PubMed:25831548, PubMed:28052936, PubMed:35621709). The BCR(KLHL3) complex acts by mediating ubiquitination and degradation of WNK1 and WNK4, two ac... | Mus musculus (Mouse) |
E0D877 | APY_AEDAL | MAGKPGIQLFVIFLLLSSFAAVVWAMDNMPADKDVSKLFPLTLIHINDLHARFDETNMKSNACTAKDQCIAGIARVYQKIQDLLKEYKSKNAIYLNAGDNFQGTLWYNLLRWQVTADFITKLKPTAMTLGNHEFDHTPKGLAPYLAELDKAGIPTLVANLVMNDDPDLKSSKIQKSIKVTVGGKTIGIIGVLYDKTHEIAQTGKVTLSNAVETVKREAAALKKDKVDIIVVLSHCSYDEDKKIAKEAGQDIDVIVGAHSHSFLYSKESNKPYDQKDKIEGPYPTIVESNNKRKIPIVQAKSFGKYVGRLTLYFDNEGEVK... | 3.6.1.5 | COFACTOR: Name=a divalent metal cation; Xref=ChEBI:CHEBI:60240; Evidence={ECO:0000250|UniProtKB:P50635}; | AMP catabolic process [GO:0006196] | extracellular region [GO:0005576]; plasma membrane [GO:0005886] | 5'-nucleotidase activity [GO:0008253]; apyrase activity [GO:0004050]; ATP binding [GO:0005524]; metal ion binding [GO:0046872] | PF02872;PF00149; | 3.60.21.10;3.90.780.10; | 5'-nucleotidase family | null | SUBCELLULAR LOCATION: Secreted {ECO:0000250|UniProtKB:P50635}. | CATALYTIC ACTIVITY: Reaction=a ribonucleoside 5'-triphosphate + 2 H2O = a ribonucleoside 5'-phosphate + 2 H(+) + 2 phosphate; Xref=Rhea:RHEA:36795, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:43474, ChEBI:CHEBI:58043, ChEBI:CHEBI:61557; EC=3.6.1.5; Evidence={ECO:0000269|PubMed:21842387}; PhysiologicalDirection=le... | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=11.6 uM for ATP {ECO:0000269|PubMed:21842387}; Vmax=1.02 nmol/sec/ug enzyme toward ATP {ECO:0000269|PubMed:21842387}; | null | null | null | FUNCTION: Facilitates hematophagy by inhibiting ADP-dependent platelet aggregation in the host (PubMed:21842387). Cleaves adenosine triphosphate (ATP) and adenosine diphosphate (ADP) to adenosine monophosphate (AMP) and inorganic phosphate (PubMed:21842387). May reduce probing time by facilitating the speed of locating... | Aedes albopictus (Asian tiger mosquito) (Stegomyia albopicta) |
E0SRA9 | ILVC_IGNAA | MAKIYKDEDISLEPIKNKTIAILGYGSQGRAWALNLRDSGLNVVVGLERQGDSWRRAIDDGFKPMYTKDAVAIADIIVFLVPDMVQKSLWLNSVKDFMKKGADLVFAHGFNIHFKIIEPPKDSDVYMIAPKSPGPIVRRSYEMGGGVPALVAVYQNVSGEALQKALAIAKGIGCARAGVIESTFKEETETDLFGEQVILVGGIMELIKASFETLVEEGYQPEVAYFETVNELKLIVDLIYEKGLTGMLRAVSDTAKYGGITVGKFIIDKSVRDKMKIVLERIRSGEFAREWIKEYERGMPTVFKELSELEGSTIETVGRK... | 1.1.1.383 | COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000255|HAMAP-Rule:MF_00435, ECO:0000269|PubMed:25849365}; Note=Binds 2 magnesium ions per subunit. {ECO:0000255|HAMAP-Rule:MF_00435}; | amino acid biosynthetic process [GO:0008652]; isoleucine biosynthetic process [GO:0009097]; valine biosynthetic process [GO:0009099] | cytosol [GO:0005829] | ketol-acid reductoisomerase activity [GO:0004455]; magnesium ion binding [GO:0000287]; NADP binding [GO:0050661] | PF01450;PF07991; | 6.10.240.10;3.40.50.720; | Ketol-acid reductoisomerase family | null | null | CATALYTIC ACTIVITY: Reaction=(2R)-2,3-dihydroxy-3-methylbutanoate + NAD(+) = (2S)-2-acetolactate + H(+) + NADH; Xref=Rhea:RHEA:30627, ChEBI:CHEBI:15378, ChEBI:CHEBI:49072, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945, ChEBI:CHEBI:58476; EC=1.1.1.383; Evidence={ECO:0000269|PubMed:25172159, ECO:0000269|PubMed:26644020}; CATALYTI... | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=3.1 mM for S2AL (at pH 7 and 85 degrees Celsius) {ECO:0000269|PubMed:26644020}; Note=kcat is 3.3 sec(-1) for reductoisomerase activity with NADPH (at pH 7 and 85 degrees Celsius with S2AL as substrate) (PubMed:26644020). kcat is 0.03 sec(-1) for reductoisomerase ac... | PATHWAY: Amino-acid biosynthesis; L-isoleucine biosynthesis; L-isoleucine from 2-oxobutanoate: step 2/4. {ECO:0000255|HAMAP-Rule:MF_00435}.; PATHWAY: Amino-acid biosynthesis; L-valine biosynthesis; L-valine from pyruvate: step 2/4. {ECO:0000255|HAMAP-Rule:MF_00435}. | null | null | FUNCTION: Involved in the biosynthesis of branched-chain amino acids (BCAA). Catalyzes an alkyl-migration followed by a ketol-acid reduction of (S)-2-acetolactate (S2AL) to yield (R)-2,3-dihydroxy-isovalerate. In the isomerase reaction, S2AL is rearranged via a Mg-dependent methyl migration to produce 3-hydroxy-3-methy... | Ignisphaera aggregans (strain DSM 17230 / JCM 13409 / AQ1.S1) |
E0VIU9 | PRKN_PEDHC | MSILEWFWNILCGMAQYLTFSKNLTNDNLVNIYVKSNVGGTISVNLDPKSDIKNVKELVAPKLGLEPDDVKIIFAGKELLDSTVIEVLDFFSDILHAVKVNKKIKNVIPDKPLCETLEELHQLNDQKNVESIEESNLKNEGKNKAHFFIYCANPCKKINTGKLRVCCSECKHGAFTVDTDPQSWADVLDKNKITGVCNNVGCEGLYAKFYFKCASHPSQGENDTAVPLNLIKRNHKKIPCLACTDICDPVLVFSCDNRHVTCLECFKNYCGSRLKDRQFLSHPDFGYTLPCPAGCSNSFIEEVHHFRLLTDAQYEQYHRF... | 2.3.2.31 | null | autophagy [GO:0006914]; negative regulation of protein phosphorylation [GO:0001933]; positive regulation of proteasomal ubiquitin-dependent protein catabolic process [GO:0032436]; protein polyubiquitination [GO:0000209]; regulation of apoptotic process [GO:0042981]; regulation of cellular response to oxidative stress [... | cytosol [GO:0005829]; endoplasmic reticulum [GO:0005783]; Golgi apparatus [GO:0005794]; mitochondrion [GO:0005739]; ubiquitin ligase complex [GO:0000151] | ubiquitin conjugating enzyme binding [GO:0031624]; ubiquitin protein ligase activity [GO:0061630]; zinc ion binding [GO:0008270] | PF00240;PF17976;PF17978; | 1.20.120.1750;2.20.25.20; | RBR family, Parkin subfamily | PTM: Auto-ubiquitinates in an E2-dependent manner leading to its own degradation. {ECO:0000250|UniProtKB:Q7KTX7}.; PTM: Phosphorylated (By similarity). Activation requires phosphorylation at Ser-92 by Pink1 and binding to Pink1-phosphorylated polyubiquitin chains (By similarity). Phosphorylation at Thr-176 by Pink1 is ... | SUBCELLULAR LOCATION: Mitochondrion {ECO:0000250|UniProtKB:Q7KTX7}. Cytoplasm, cytosol {ECO:0000250|UniProtKB:Q7KTX7}. Note=Translocates from the cytosol to dysfunctional mitochondria that have lost their mitochondrial membrane potential; recruitment to mitochondria is Pink1-dependent. {ECO:0000250|UniProtKB:Q7KTX7}. | CATALYTIC ACTIVITY: Reaction=[E2 ubiquitin-conjugating enzyme]-S-ubiquitinyl-L-cysteine + [acceptor protein]-L-lysine = [E2 ubiquitin-conjugating enzyme]-L-cysteine + [acceptor protein]-N(6)-ubiquitinyl-L-lysine.; EC=2.3.2.31; Evidence={ECO:0000269|PubMed:26161729}; | null | PATHWAY: Protein modification; protein ubiquitination. {ECO:0000269|PubMed:26161729}. | null | null | FUNCTION: E3 ubiquitin-protein ligase which accepts ubiquitin from E2 ubiquitin-conjugating enzymes in the form of a thioester and then directly transfers the ubiquitin to targeted substrates, such as Marf, Opa1, Sep1, Tom20 and porin (By similarity). Mediates monoubiquitination as well as 'Lys-6', 'Lys-11', 'Lys-48'-l... | Pediculus humanus subsp. corporis (Body louse) |
E0W1I1 | PINK1_PEDHC | MSLLAYTNLLLQNGRIFRYYKKANIKKFIKKIIKLDLKSTPSEASVSRQTFLSTGLNSVKNAVQLQARKLLINNVLERVTPTLNSDLKKKAAKRLFYGDSAPFFALVGVSLASGSGLLTKDDELEGICWEIREAVSKGKWNDSESENVEQLQAANLDELDLGEPIAKGCNAVVYSAKLKNVQSNKLAHQLAVKMMFNYDVESNSTAILKAMYRETVPAMSYFFNQNLFNIENISDFKIRLPPHPNIVRMYSVFADRIPDLQCNKQLYPEALPPRINPEGSGRNMSLFLVMKRYDCTLKEYLRDKTPNMRSSILLLSQLLE... | 2.7.11.1 | COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000269|PubMed:22645651, ECO:0000269|PubMed:29160309}; Note=Binds 2 Mg(2+) ions per subunit. {ECO:0000250|UniProtKB:D6WMX4}; | autophagy [GO:0006914]; phosphorylation [GO:0016310]; positive regulation of mitochondrial fission [GO:0090141]; regulation of apoptotic process [GO:0042981] | cytosol [GO:0005829]; mitochondrial inner membrane [GO:0005743]; mitochondrial outer membrane [GO:0005741] | ATP binding [GO:0005524]; metal ion binding [GO:0046872]; protein kinase activity [GO:0004672]; protein serine/threonine kinase activity [GO:0004674] | PF00069; | 1.10.510.10; | Protein kinase superfamily, Ser/Thr protein kinase family | PTM: Proteolytically cleaved. In healthy cells, the precursor is continuously imported into mitochondria where it is proteolytically cleaved into its short form by the mitochondrial rhomboid protease rho-7 (8231301). The short form is then released into the cytosol where it rapidly undergoes proteasome-dependent degrad... | SUBCELLULAR LOCATION: Mitochondrion outer membrane {ECO:0000250|UniProtKB:Q0KHV6}; Single-pass membrane protein {ECO:0000255}. Mitochondrion inner membrane {ECO:0000250|UniProtKB:Q0KHV6}; Single-pass membrane protein {ECO:0000255}. Cytoplasm, cytosol {ECO:0000250|UniProtKB:Q0KHV6}. Note=Localizes mostly in mitochondrio... | 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:22645651, ECO:000026... | null | null | null | null | FUNCTION: Acts as a serine/threonine-protein kinase (PubMed:22645651, PubMed:26161729, PubMed:29160309). Exhibits a substrate preference for proline at position P+1 and a general preference at several residues for basic residues such as arginine (By similarity). Also exhibits moderate preferences for a phosphotyrosine ... | Pediculus humanus subsp. corporis (Body louse) |
E0W4V5 | PSR2_PHYSO | MRLQCVVLFAALTLVAATHAPPNVKTVLSAEQHDIPVKRLLRPGNPAGKEDEERGINFSSVPGFEKLANLLKPKPGLKKLLKWADAKKPPETVFTRLRLDKTGTQLFDNTDFPVWAAYTRSVAQTDSEASAVMLKTLVSRYSDEVLSGMIAAAKKSSKTESIATKLETEQMRTWLAAKKTPDDMFLVFKLNKAGDDILSSPLLSAWTNYMKLSNKENPKAQTTLIATMTKHYGDSGVSQILAAARKSPATQSTAKRLEAEQVQLWLKKGRTPDDTFTLLSLDRAGDDLLASPQFNTWMKYINYYNKENPDEKTTVLAKLM... | null | null | null | extracellular region [GO:0005576]; host cell [GO:0043657] | null | null | null | RxLR effector family | null | SUBCELLULAR LOCATION: Secreted {ECO:0000305|PubMed:23377181}. Host cell {ECO:0000305|PubMed:23377181}. | null | null | null | null | null | FUNCTION: Secreted effector that possesses RNA silencing suppression activity by inhibiting the biogenesis of small RNAs in the host plant to promote enhanced susceptibility of host to the pathogen during infection (PubMed:23377181, PubMed:25387135, PubMed:30595554). Interferes with secondary siRNA production by associ... | Phytophthora sojae (Soybean stem and root rot agent) (Phytophthora megasperma f. sp. glycines) |
E0W544 | AVH23_PHYSO | MRLTYFLTVIVVATLHAGGTALATAEAPNHAAIVNVASADNVHSLDTTAEIGGRMLRKVKEDTVSKKDHEERGPGAILERQTAFVKKLFSRQNAIVNRAQGAFQRQNAFVNRDQGAFQRQNAFVKRAIQRQNHFKLSDNA | null | null | null | extracellular region [GO:0005576]; host cell cytoplasm [GO:0030430]; host cell nucleus [GO:0042025] | null | PF16810; | null | RxLR effector family | null | SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:28318979}. Host nucleus {ECO:0000269|PubMed:28318979}. Host cytoplasm {ECO:0000269|PubMed:28318979}. Note=Location into the host nucleus is required for virulence. {ECO:0000269|PubMed:28318979}. | null | null | null | null | null | FUNCTION: Effector that suppresses plant defense responses during the early stages of pathogen infection. Suppresses cell death induced by effectors and PAMPs in plant hosts (PubMed:21653195). Acts as a modulator of histone acetyltransferase (HAT) in plants. Avh23 binds to the ADA2 subunit of the HAT complex SAGA and d... | Phytophthora sojae (Soybean stem and root rot agent) (Phytophthora megasperma f. sp. glycines) |
E0WN94 | ODC_NICGL | MAGQTIIVSGLNPAAILQSTIGGGASPTAAAAAENGTRKVIPLSRDALQDFMLSIITQKLQDEKQPFYVLDLGEVVSLMDQWKSALPNIRPFYAVKCNPEPSFLSILSAMGSNFDCASRAEIEYVLALGISPDRIVFANPCKPESDIIFAAKVGVNLTTYDSEDEVYKIRKHHPKSELLLRIKPMFDGNARCPMGPKYGALPEEVEPLLRAAQAARLTVSGVSFHIGSGDADSNAYLGAIAAAKEVFETAAKLGMSKMTVLDVGGGFTSGHQFTAAAVAVKSALKQRFDDEPELTIIAEPGRFFAETAFTLATTIIGKRV... | 4.1.1.17 | COFACTOR: Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326; Evidence={ECO:0000250|UniProtKB:P11926}; | alkaloid metabolic process [GO:0009820]; nicotine biosynthetic process [GO:0042179]; putrescine biosynthetic process from ornithine [GO:0033387]; response to jasmonic acid [GO:0009753]; response to wounding [GO:0009611] | chloroplast [GO:0009507] | ornithine decarboxylase activity [GO:0004586] | PF02784;PF00278; | 3.20.20.10; | Orn/Lys/Arg decarboxylase class-II family | null | SUBCELLULAR LOCATION: Plastid, chloroplast {ECO:0000255}. | CATALYTIC ACTIVITY: Reaction=H(+) + L-ornithine = CO2 + putrescine; Xref=Rhea:RHEA:22964, ChEBI:CHEBI:15378, ChEBI:CHEBI:16526, ChEBI:CHEBI:46911, ChEBI:CHEBI:326268; EC=4.1.1.17; Evidence={ECO:0000250|UniProtKB:P11926}; | null | PATHWAY: Alkaloid biosynthesis; nicotine biosynthesis. {ECO:0000269|PubMed:21232776}.; PATHWAY: Amine and polyamine biosynthesis; putrescine biosynthesis via L-ornithine pathway; putrescine from L-ornithine: step 1/1. {ECO:0000250|UniProtKB:O22616}. | null | null | FUNCTION: Involved in the biosynthesis of pyridine alkaloid natural products, leading mainly to the production of anabasine, anatabine, nicotine and nornicotine, effective deterrents against herbivores with antiparasitic and pesticide properties (neurotoxins); nornicotine serves as the precursor in the synthesis of the... | Nicotiana glauca (Glaucous tobacco) (Tree tobacco) |
E0X9C7 | TODS_PSEPT | MSSLDRKKPQNRSKNNYYNICLKEKGSEELTCEEHARIIFDGLYEFVGLLDAHGNVLEVNQVALEGAGITLEEIRGKPFWKARWWQISKKTEATQKRLVETASSGEFVRCDVEILGKSGGREVIAVDFSLLPICNEEGSIVYLLAEGRNITDKKKAEAMLALKNQELEQSVERIRKLDNAKSDFFAKVSHELRTPLSLILGPLEAVMAAEAGRESPYWKQFEVIQRNAMTLLKQVNTLLDLAKMDARQMGLSYRRANLSQLTRTISSNFEGIAQQKSITFDTKLPVQMVAEVDCEKYERIILNLLSNAFKFTPDGGLIRC... | 2.7.13.3 | null | null | cytoplasm [GO:0005737] | ATP binding [GO:0005524]; identical protein binding [GO:0042802]; phosphorelay sensor kinase activity [GO:0000155] | PF02518;PF00512;PF08448;PF13426;PF00072; | 1.10.287.130;3.40.50.2300;3.30.565.10;3.30.450.20; | null | PTM: Autophosphorylated. Activation requires a sequential transfer of a phosphate group from a His in the primary transmitter domain, to an Asp in the receiver domain and to a His in the secondary transmitter domain. | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:22212183}. | CATALYTIC ACTIVITY: Reaction=ATP + protein L-histidine = ADP + protein N-phospho-L-histidine.; EC=2.7.13.3; Evidence={ECO:0000269|PubMed:16702539, ECO:0000269|PubMed:19240030}; | null | null | null | null | FUNCTION: Member of the two-component regulatory system TodS/TodT involved in the regulation of toluene degradation. Phosphorylates TodT via a four-step phosphorelay in response to toluene. Can also be induced by benzene and ethylbenzene. {ECO:0000269|PubMed:16702539, ECO:0000269|PubMed:19240030, ECO:0000269|PubMed:222... | Pseudomonas putida (strain DOT-T1E) |
E0Y3X1 | NOTF_ASPSM | MTAPELRVDTFRAPEDAPKEPSAQQPRLPSSPSPAQALASYHHFPTNDQERWWEETGSLFSRFLEAGQYGLPQQYQFMFFFMHHLIPALGPYPQKWRSTISRSGLPIEFSLNFQKGSHRLLRIGFEPVSFLSGSSQDPFNRIPITDLLNRLSKLQLSNFDTPFFQHLLSKFQLSLSEVRQLQKQGSGPDAHPLKSQAAFGFDFNPDGAILVKGYVFPYLKAKAADVPVGTLIAEAVRTIDVERNQFTHAFGLINDYMQESTGYNEYTFLSCDFVETSEQRLKIYGAHTEVTWAKIAEMWTLGGRLIEEPEIIAGLARLKQ... | 2.5.1.109 | null | alkaloid metabolic process [GO:0009820] | null | prenyltransferase activity [GO:0004659] | PF11991; | null | Tryptophan dimethylallyltransferase family | null | null | CATALYTIC ACTIVITY: Reaction=brevianamide F + dimethylallyl diphosphate = deoxybrevianamide E + diphosphate; Xref=Rhea:RHEA:35943, ChEBI:CHEBI:33019, ChEBI:CHEBI:57623, ChEBI:CHEBI:64530, ChEBI:CHEBI:72948; EC=2.5.1.109; Evidence={ECO:0000269|PubMed:20722388}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:35944;... | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=4.33 uM for brevianamide F {ECO:0000269|PubMed:20722388}; KM=1.31 uM for dimethylallyl diphosphate (DMAPP) {ECO:0000269|PubMed:20722388}; Vmax=0.89 uM/min/mg enzyme toward brevianamide F {ECO:0000269|PubMed:20722388}; Vmax=1.18 uM/min/mg enzyme toward dimethylallyl... | PATHWAY: Alkaloid biosynthesis. {ECO:0000269|PubMed:20722388}. | BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 6-9. {ECO:0000269|PubMed:20722388}; | BIOPHYSICOCHEMICAL PROPERTIES: Temperature dependence: Optimum temperature is 4 to 42 degrees Celsius. {ECO:0000269|PubMed:20722388}; | FUNCTION: Deoxybrevianamide E synthase; part of the gene cluster that mediates the biosynthesis of notoamide, a fungal indole alkaloid that belongs to a family of natural products containing a characteristic bicyclo[2.2.2]diazaoctane core (PubMed:20722388). The first step of notoamide biosynthesis involves coupling of ... | Aspergillus sp. (strain MF297-2) |
E0Y419 | VSPBF_MACLB | MVLIRVLANLLLLQLSHAQKSSELVVGGDECNINEHRSLVFLYNSSFGCGGTLINQEWVLSAAHCDMENMRIYLGWHNFSLPNMNQKRRVAKEKFFCLSSKNYTEWDKDIMLIKMNRPVTYSTHVAPLSLPSSPPSVGSVCRIMGWGAITSPNETYPDVPHCANINILNYTVCRAAHPWLPAQSRTLCAGILQGGIDTCKGDSGGPLICNGQIQGIVSWGDNPCAQPLKPGHYTNVFDYTDWIQSIIAGNTTATCPP | 3.4.21.- | null | proteolysis [GO:0006508] | extracellular space [GO:0005615] | serine-type endopeptidase activity [GO:0004252]; toxin activity [GO:0090729] | PF00089; | 2.40.10.10; | Peptidase S1 family, Snake venom subfamily | PTM: Glycosylated. Contains 23.0% of hexoses, 8.3% of hexosamines and 1.0% of sialic acids. {ECO:0000269|PubMed:11602278}. | SUBCELLULAR LOCATION: Secreted {ECO:0000250}. | null | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=77 uM for N-alpha-benzoyl-L-arginine ethyl ester (BAEE) (at pH 8.5 and 25 degrees Celsius) {ECO:0000269|PubMed:2028469}; KM=0.36 mM for Tosyl-L-arginine methyl ester (TAME) (at pH 8.5 and 25 degrees Celsius) {ECO:0000269|PubMed:2028469}; KM=0.18 mM for BAPNA (at pH... | null | null | null | FUNCTION: Snake venom serine protease that has fibrinogenolytic activities by hydrolyzing the beta chain of fibrinogen (FGB). Typical arginine esterase which hydrolyzes esters and amides of arginine. {ECO:0000269|PubMed:11910177, ECO:0000269|PubMed:2028469}. | Macrovipera lebetina (Levantine viper) (Vipera lebetina) |
E0Y421 | VSPY_MACLB | MVLIRVLANLLLLQLSYAQKSSELVVGGDECNINEHRSLVFLYNSSFGCGGTLINQQWVLSAAHCDMENVQIYLGLHNLRLRNQDEQIRVAEEKFFCLSNKSYTKWDKDIMLIRLNSSVTYNTHIAPLSLPSSPPRVGSVCRIMGWGAITSPNETFPNVPHCANINILRYSVCRAAYRGLPAQSRTLCAGILQGGIGSCMGDSGGPLICNGEIQGIVSWGDDICAQPHKPVHYTKVFDYSDWIQSIIAGNTTATCPL | 3.4.21.- | null | proteolysis [GO:0006508] | extracellular space [GO:0005615] | serine-type endopeptidase activity [GO:0004252]; toxin activity [GO:0090729] | PF00089; | 2.40.10.10; | Peptidase S1 family, Snake venom subfamily | PTM: Partial deglycosylation has not effect on enzyme activity. | SUBCELLULAR LOCATION: Secreted. | null | null | null | null | null | FUNCTION: Snake venom serine protease with tyrosine-specific chymotrypsin-like activity. Hydrolyzes the N-acetyl-L-tyrosine ethyl ester (ATEE). Has weak fibrinogenolytic activity. Weakly hydrolyzes azocasein, Aalpha-chain (FGA) and more slowly Bbeta-chain (FGB) of fibrinogen. Optimal substrates are angiotensins I and I... | Macrovipera lebetina (Levantine viper) (Vipera lebetina) |
E1AZ71 | CNGB1_MOUSE | MLGWVQRVLPQPPGTPQKTVETAGPQPETESKPEANPQPEPEPQQEPEPEPEPEPEPEPEPEPEPEPEPEPEPEPVPEEAPPEVQALPPEEPMEGEGEAEAGPSLQETQVADPAQPTSQAQVAVAKVNRPSSWMLSWFWRGMQKVVPQPVCSNGGQNLAAGERDPDQGGAQIPEPCGTGDPGSAEASGTQDTEPSLWLLRWLEQNLEKVLPQPPPPSLAWKVEPEAAVLDPDPPGTPMQMEPTESPSQPNPGPLEPEEEPAAEPQPGFQSSSLPPPGDPVRLIEWLLHRLEMALPQPVLHGKAAEQEPGCPGMCDVQTIS... | null | null | detection of chemical stimulus involved in sensory perception of smell [GO:0050911]; detection of light stimulus involved in visual perception [GO:0050908]; ion channel modulating, G protein-coupled receptor signaling pathway [GO:0099105]; membrane depolarization [GO:0051899]; monoatomic cation transmembrane transport ... | intracellular cyclic nucleotide activated cation channel complex [GO:0017071]; membrane [GO:0016020]; photoreceptor outer segment [GO:0001750]; plasma membrane [GO:0005886]; terminal bouton [GO:0043195] | cAMP binding [GO:0030552]; cGMP binding [GO:0030553]; cyclic nucleotide-activated monoatomic ion channel activity [GO:0043855]; intracellularly cAMP-activated cation channel activity [GO:0005222]; intracellularly cGMP-activated cation channel activity [GO:0005223]; protein-containing complex binding [GO:0044877] | PF00027; | 1.10.287.70;1.10.287.630;2.60.120.10; | Cyclic nucleotide-gated cation channel (TC 1.A.1.5) family, CNGB1 subfamily | null | SUBCELLULAR LOCATION: Cell projection, cilium membrane {ECO:0000269|PubMed:16980309}; Multi-pass membrane protein {ECO:0000255}. | CATALYTIC ACTIVITY: Reaction=Ca(2+)(in) = Ca(2+)(out); Xref=Rhea:RHEA:29671, ChEBI:CHEBI:29108; Evidence={ECO:0000250|UniProtKB:Q28181, ECO:0000305|PubMed:16980309}; CATALYTIC ACTIVITY: Reaction=Na(+)(in) = Na(+)(out); Xref=Rhea:RHEA:34963, ChEBI:CHEBI:29101; Evidence={ECO:0000250|UniProtKB:Q28181}; CATALYTIC ACTIVITY:... | null | null | null | null | FUNCTION: Pore-forming subunit of the rod cyclic nucleotide-gated channel. Mediates rod photoresponses at dim light converting transient changes in intracellular cGMP levels into electrical signals. In the dark, cGMP levels are high and keep the channel open enabling a steady inward current carried by Na(+) and Ca(2+) ... | Mus musculus (Mouse) |
E1B328 | WR52N_ARATH | MTNCEKDEEFVCISCVEEVRYSFVSHLSEALRRKGINNVVVDVDIDDLLFKESQAKIEKAGVSVMVLPGNCDPSEVWLDKFAKVLECQRNNKDQAVVSVLYGDSLLRDQWLSELDFRGLSRIHQSRKECSDSILVEEIVRDVYETHFYVGRIGIYSKLLEIENMVNKQPIGIRCVGIWGMPGIGKTTLAKAVFDQMSSAFDASCFIEDYDKSIHEKGLYCLLEEQLLPGNDATIMKLSSLRDRLNSKRVLVVLDDVCNALVAESFLEGFDWLGPGSLIIITSRDKQVFRLCGINQIYEVQGLNEKEARQLFLLSASIMED... | null | null | defense response [GO:0006952]; signal transduction [GO:0007165] | cytoplasm [GO:0005737]; nucleus [GO:0005634] | ADP binding [GO:0043531]; ATP binding [GO:0005524]; DNA-binding transcription factor activity [GO:0003700]; sequence-specific DNA binding [GO:0043565] | PF07725;PF00931;PF03106; | 1.10.8.430;3.40.50.300;3.80.10.10;3.40.50.10140;2.20.25.80; | null | null | SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:12788974}. Cytoplasm {ECO:0000305|PubMed:12788974}. Note=The nuclear localization is only detected upon interaction with PopP2. {ECO:0000269|PubMed:12788974}. | null | null | null | null | null | FUNCTION: Transcription factor. Interacts specifically with the W box (5'-(T)TGAC[CT]-3'), a frequently occurring elicitor-responsive cis-acting element. Acts also as a disease resistance protein involved in resistance to fungal and bacterial pathogens, including R.solanacearum, P.syringae pv. tomato and C.higginsianum... | Arabidopsis thaliana (Mouse-ear cress) |
E1BB50 | CDK12_BOVIN | MPNPERHGGKKDGSGGASGTLQPSSGGGSSNSRERHRLGSKHKRHKSKHSKDMGLVTPEAAPLGTVIKPLVEYDDISSDSDTFSDDLAFKVDRRENDERRGTDRSDRLHKHRHHQHRRTRDLLKTKQTEKEKNLEASSKSGSTKDRISGSSKRSNEENDDHGKAQISKSSNKESRSSKLHKEKTRKERELKSGHKDRSKSHRKRETPKSYKTVDSPKRRSRSPHRKWSDSPKQDDSPSGASYGQDYDLSPPRSHTSSNYDSYKKSPGSTSRRQSISPPYKEPSAYQSSTRSPSPYSRRQRSVSPYSRRRSSSYERSGSYS... | 2.7.11.22; 2.7.11.23 | null | mRNA processing [GO:0006397]; phosphorylation [GO:0016310]; positive regulation of transcription by RNA polymerase II [GO:0045944]; positive regulation of transcription elongation by RNA polymerase II [GO:0032968]; regulation of MAP kinase activity [GO:0043405]; RNA splicing [GO:0008380] | cyclin/CDK positive transcription elongation factor complex [GO:0008024]; nuclear cyclin-dependent protein kinase holoenzyme complex [GO:0019908]; nuclear speck [GO:0016607]; nucleus [GO:0005634] | ATP binding [GO:0005524]; cyclin binding [GO:0030332]; cyclin-dependent protein serine/threonine kinase activity [GO:0004693]; protein serine kinase activity [GO:0106310]; RNA polymerase II CTD heptapeptide repeat kinase activity [GO:0008353] | PF12330;PF00069; | 1.10.510.10; | Protein kinase superfamily, CMGC Ser/Thr protein kinase family, CDC2/CDKX subfamily | PTM: Phosphorylation at Thr-893 increases kinase activity. {ECO:0000250}. | SUBCELLULAR LOCATION: Nucleus {ECO:0000250}. Nucleus speckle {ECO:0000250}. Note=Colocalized with nuclear speckles throughout interphase. {ECO:0000250}. | CATALYTIC ACTIVITY: Reaction=[DNA-directed RNA polymerase] + ATP = ADP + H(+) + phospho-[DNA-directed RNA polymerase]; Xref=Rhea:RHEA:10216, Rhea:RHEA-COMP:11321, Rhea:RHEA-COMP:11322, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:43176, ChEBI:CHEBI:68546, ChEBI:CHEBI:456216; EC=2.7.11.23; CATALYTIC ACTIVITY: React... | null | null | null | null | FUNCTION: Cyclin-dependent kinase that phosphorylates the C-terminal domain (CTD) of the large subunit of RNA polymerase II (POLR2A), thereby acting as a key regulator of transcription elongation. Regulates the expression of genes involved in DNA repair and is required for the maintenance of genomic stability. Preferen... | Bos taurus (Bovine) |
E1BB52 | CDK13_BOVIN | MPSSSDTALGGGGGLSWAEKKLEERRKRRRFLSPQQPPLLLPLLQPQLLQPPPPPPPLLFLAAPGTAAAAAAAAAASSSCFSPGPPLEVKRLARGKRRAGGRQKRRRGPRAGQEAEKRRVFSLPQPQQDGGGGASSGGGVTPLVEYEDVSSQSEQGLLLGGASAATAATAAGGTGGSGGSPASSSGTQRRGEGSERRPRRDRRSSSGRSKDRHREHRRRDGQRGGGEASKSRSRHGHGGEERAEAGKSGSSSSSGGRRKSASATSSSSSSRKDRDPKAHRSRTKSSKEPPSAYKEPPKAYREDKTEPKAYRRRQRSLSPL... | 2.7.11.22; 2.7.11.23 | null | alternative mRNA splicing, via spliceosome [GO:0000380]; hemopoiesis [GO:0030097]; phosphorylation [GO:0016310]; positive regulation of transcription by RNA polymerase II [GO:0045944]; positive regulation of transcription elongation by RNA polymerase II [GO:0032968] | cyclin/CDK positive transcription elongation factor complex [GO:0008024]; nuclear cyclin-dependent protein kinase holoenzyme complex [GO:0019908]; nuclear speck [GO:0016607]; nucleus [GO:0005634] | ATP binding [GO:0005524]; cyclin binding [GO:0030332]; cyclin-dependent protein serine/threonine kinase activity [GO:0004693]; protein serine kinase activity [GO:0106310]; RNA polymerase II CTD heptapeptide repeat kinase activity [GO:0008353] | PF12330;PF00069; | 1.10.510.10; | Protein kinase superfamily, CMGC Ser/Thr protein kinase family, CDC2/CDKX subfamily | null | SUBCELLULAR LOCATION: Nucleus speckle {ECO:0000250}. | CATALYTIC ACTIVITY: Reaction=[DNA-directed RNA polymerase] + ATP = ADP + H(+) + phospho-[DNA-directed RNA polymerase]; Xref=Rhea:RHEA:10216, Rhea:RHEA-COMP:11321, Rhea:RHEA-COMP:11322, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:43176, ChEBI:CHEBI:68546, ChEBI:CHEBI:456216; EC=2.7.11.23; CATALYTIC ACTIVITY: React... | null | null | null | null | FUNCTION: Cyclin-dependent kinase which displays CTD kinase activity and is required for RNA splicing. Has CTD kinase activity by hyperphosphorylating the C-terminal heptapeptide repeat domain (CTD) of the largest RNA polymerase II subunit RPB1, thereby acting as a key regulator of transcription elongation. Required fo... | Bos taurus (Bovine) |
E1BBQ2 | MGLYR_BOVIN | MGVMAYPFLFCLLLVHFGLGAIGASREAPSRPDPPRERTLRAKQHAQQPARASASDPSAPWSRSTDGTILAQKLAEEVPMDVASYLYTGDSHKLKRANCSSRYELAGLPGKSPALASSHPSLHGALDTLTHATNFLNMMLQSNKSREQNLQDDLEWYQALVRSLLEGEPSISRAAITFSTESLSAPAPQVFLQATREESRILLQDLSSSAHHLANATLETEWFHGLRRKWRTHLHRRGSNQGPRGLGHSWRRRDGLSGDKSHVKWSPPYLECENGSYKPGWLVTLSAAFYGLQPNLVPEFRGVMKVDINLQKVDIDQCSS... | null | null | cognition [GO:0050890]; G protein-coupled receptor signaling pathway [GO:0007186]; protein localization to plasma membrane [GO:0072659]; regulation of G protein-coupled receptor signaling pathway [GO:0008277]; regulation of synapse organization [GO:0050807] | cell projection [GO:0042995]; nucleus [GO:0005634]; plasma membrane [GO:0005886]; postsynaptic membrane [GO:0045211]; presynaptic membrane [GO:0042734] | enzyme activator activity [GO:0008047]; G protein-coupled glycine receptor activity [GO:0160079]; transmembrane signaling receptor activity [GO:0004888] | PF00003; | 3.30.450.20; | G-protein coupled receptor 3 family | null | SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:Q5T848}; Multi-pass membrane protein {ECO:0000250|UniProtKB:Q5T848}. Postsynaptic cell membrane {ECO:0000250|UniProtKB:Q8C419}; Multi-pass membrane protein {ECO:0000250|UniProtKB:Q5T848}. Presynaptic cell membrane {ECO:0000250|UniProtKB:Q8C419}; Multi-pass memb... | null | null | null | null | null | FUNCTION: Metabotropic receptor for glycine that controls synapse formation and function in the brain. Acts as an atypical G-protein coupled receptor that recruits and regulates the RGS7-GNB5 complex instead of activating G proteins. In absence of glycine ligand, promotes the GTPase activator activity of RGS7, increasi... | Bos taurus (Bovine) |
E1BE10 | PLD6_BOVIN | MRPLRWQVAVVAAAGLALALETLPAVLRWLWVRRRRPRREVLFFPSQVTCTEALLRSPGATPSGCPCSLPHGESSLSRLLSALLAARVSLELCLFAFSSPQLGRAVQLLHQRGVRVRVVTDCDYMALNGSQIGLLRKAGIQVRHDQDLGYMHHKFAIVDRKVLITGSLNWTTQAIQNNRENVLIVEDEEYVRLFLEEFERIWEEFNPTRFSFFPQKERAR | 3.1.4.- | null | lipid catabolic process [GO:0016042]; meiotic cell cycle [GO:0051321]; mitochondrial fusion [GO:0008053]; P granule organization [GO:0030719]; piRNA processing [GO:0034587]; spermatid development [GO:0007286] | Golgi apparatus [GO:0005794]; mitochondrial outer membrane [GO:0005741]; mitochondrion [GO:0005739]; nuclear membrane [GO:0031965]; plasma membrane [GO:0005886] | cardiolipin hydrolase activity [GO:0035755]; metal ion binding [GO:0046872]; protein homodimerization activity [GO:0042803]; RNA endonuclease activity, producing 5'-phosphomonoesters [GO:0016891] | PF13091; | 3.30.870.10; | Phospholipase D family, MitoPLD/Zucchini subfamily | null | SUBCELLULAR LOCATION: Mitochondrion outer membrane {ECO:0000250|UniProtKB:Q5SWZ9}; Single-pass membrane protein {ECO:0000250|UniProtKB:Q5SWZ9}. Nucleus membrane {ECO:0000250|UniProtKB:Q5SWZ9}. Cell membrane {ECO:0000250|UniProtKB:Q5SWZ9}. Golgi apparatus {ECO:0000250|UniProtKB:Q5SWZ9}. Note=Localization in the mitochon... | CATALYTIC ACTIVITY: Reaction=a cardiolipin + H2O = 1,2-diacyl-sn-glycero-3-phospho-(1'-sn-glycerol) + a 1,2-diacyl-sn-glycero-3-phosphate + H(+); Xref=Rhea:RHEA:44884, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:58608, ChEBI:CHEBI:62237, ChEBI:CHEBI:64716; Evidence={ECO:0000250|UniProtKB:Q8N2A8}; PhysiologicalDir... | null | null | null | null | FUNCTION: Presents phospholipase and nuclease activities, depending on the different physiological conditions. Interaction with Mitoguardin (MIGA1 or MIGA2) affects the dimer conformation, facilitating the lipase activity over the nuclease activity. Plays a key role in mitochondrial fusion and fission via its phospholi... | Bos taurus (Bovine) |
E1BF86 | BEST2_BOVIN | MTVTYTARVAKARFGGFSKLLLLWRGSIYKLLWRELLCFLGLFMALSAAYRFVLTEEQKRYFEKLVLYCDRYASLIPVSFVLGFYVTLVVHRWWNQYLSMPLTDALMCVVVGTVHGHDERGRLYRRTLMRYAGLSGVLILRSVSTAVFKRFPTIDHVVEAGFMTREERKKFENLNSSYNKYWVPCVWFCNLAAQARREGRIRDNGAFKLLLEELNVFRSKCGMLFHYDWISVPLVYTQVVTIAVYSYFLACLIGRQFLDPAQGYKDHDLDLCVPIFTLLQFFFYAGWLKVAEQLINPFGEDDDDFETNFLIDRCFQVSML... | null | null | bicarbonate transport [GO:0015701] | basolateral plasma membrane [GO:0016323]; chloride channel complex [GO:0034707]; plasma membrane [GO:0005886] | bicarbonate channel activity [GO:0160133]; chloride channel activity [GO:0005254]; intracellularly ligand-gated monoatomic ion channel activity [GO:0005217]; ligand-gated monoatomic anion channel activity [GO:0099095]; ligand-gated monoatomic cation channel activity [GO:0099094] | PF01062; | null | Anion channel-forming bestrophin (TC 1.A.46) family, Calcium-sensitive chloride channel subfamily | null | SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:32251414}; Multi-pass membrane protein {ECO:0000305|PubMed:32251414, ECO:0000305|PubMed:35789156, ECO:0000305|PubMed:36289327}. Basolateral cell membrane {ECO:0000250|UniProtKB:Q8NFU1}; Multi-pass membrane protein {ECO:0000250|UniProtKB:Q8NFU1}. | CATALYTIC ACTIVITY: Reaction=chloride(in) = chloride(out); Xref=Rhea:RHEA:29823, ChEBI:CHEBI:17996; Evidence={ECO:0000269|PubMed:32251414, ECO:0000269|PubMed:36289327}; CATALYTIC ACTIVITY: Reaction=iodide(out) = iodide(in); Xref=Rhea:RHEA:66324, ChEBI:CHEBI:16382; Evidence={ECO:0000269|PubMed:32251414}; CATALYTIC ACTIV... | null | null | null | null | FUNCTION: Ligand-gated anion channel that allows the movement of anions across cell membranes when activated by calcium (Ca2+) (PubMed:32251414, PubMed:36289327). Transports a large specter of anions, namely mediates the movement of chloride, L-glutamate and iodide (PubMed:32251414, PubMed:36289327). Calcium-binding tr... | Bos taurus (Bovine) |
E1BFR5 | GWL_BOVIN | MEPTMGGEMESGGGAATGECVNRIPVPRPPSIEEFTIVKPISRGAFGKVYLGQKGNRLYAVKVVKKADMINKNMTHQVQAERDALALSKSPFIVHLYYSLQSANNVYLVMEYLIGGDVKSLLHIYGYFDEEMAVKYISEVALALDYLHRHGIIHRDLKPDNMLISNEGHIKLTDFGLSKVTLNRDIDINMMDILTTPSMAKPRQDYSRTPGQVLSLISSLGFHTPVAEGNHDTANVLSTQVSETSPLSQGLTCPMSVDQKDTTPYSSKLLKSCPEMVASHPRMPVKCLTSHLLQSRKRLATSSTSSPSHTFISSMESECH... | 2.7.11.1 | null | cell division [GO:0051301]; DNA damage response [GO:0006974]; G2/M transition of mitotic cell cycle [GO:0000086]; intracellular signal transduction [GO:0035556]; mitotic cell cycle [GO:0000278]; negative regulation of phosphoprotein phosphatase activity [GO:0032515]; phosphorylation [GO:0016310] | centrosome [GO:0005813]; cleavage furrow [GO:0032154]; cytoplasm [GO:0005737]; nucleus [GO:0005634] | ATP binding [GO:0005524]; protein phosphatase 2A binding [GO:0051721]; protein serine kinase activity [GO:0106310]; protein serine/threonine kinase activity [GO:0004674] | PF00069; | 1.10.510.10; | Protein kinase superfamily, AGC Ser/Thr protein kinase family | PTM: Phosphorylation at Thr-745 by CDK1 during M phase activates its kinase activity. Maximum phosphorylation occurs in prometaphase (By similarity). {ECO:0000250}. | SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, microtubule organizing center, centrosome {ECO:0000250}. Nucleus. Note=During interphase is mainly nuclear, upon nuclear envelope breakdown localizes at the cytoplasm and during mitosis at the centrosomes. {ECO:0000250}. | CATALYTIC ACTIVITY: Reaction=ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-[protein]; Xref=Rhea:RHEA:17989, Rhea:RHEA-COMP:9863, Rhea:RHEA-COMP:11604, ChEBI:CHEBI:15378, ChEBI:CHEBI:29999, ChEBI:CHEBI:30616, ChEBI:CHEBI:83421, ChEBI:CHEBI:456216; EC=2.7.11.1; CATALYTIC ACTIVITY: Reaction=ATP + L-threonyl-[pr... | null | null | null | null | FUNCTION: Serine/threonine kinase that plays a key role in M phase by acting as a regulator of mitosis entry and maintenance. Acts by promoting the inactivation of protein phosphatase 2A (PP2A) during M phase: does not directly inhibit PP2A but acts by mediating phosphorylation and subsequent activation of ARPP19 and E... | Bos taurus (Bovine) |
E1BGN7 | CGAS_BOVIN | MAPPRRKATRKASETASGVSAPCVEGGLSAEPSEPAAVPEAPRPGARRCGAAGASGSRREKSRLDPREKPQVRARAARAEDQAEGPAAPTADAEPPAAPGHSLPRASTRSRGTASSARARRPQSGPPEGPGLGPRAPSPHLGRREEAPGAWKPRAVLEKLKLSRQEISVAAEVVNRLGDHLLRRLNSRESEFKGVDLLRTGSYYERVKISAPNEFDLMFTLEVPRIQLEEYCNSSAHYFVKFKRNPKGSPLDQFLEGGILSASKMLFKFRKIIKEEIKHIEDTDVIMERKKRGSPAVTLLIRKPREISVDIILALESKSS... | 2.7.7.86 | COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250|UniProtKB:Q8C6L5}; Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000250|UniProtKB:Q8C6L5}; Note=Binds 1 Mg(2+) per subunit. Is also active with Mn(2+). Mn(2+)-activated enzyme forms an inverted pppGp(2'-5')A intermediate, suggesting a non-canoni... | activation of innate immune response [GO:0002218]; cAMP-mediated signaling [GO:0019933]; cellular response to exogenous dsRNA [GO:0071360]; defense response to virus [GO:0051607]; DNA damage response [GO:0006974]; DNA repair [GO:0006281]; innate immune response [GO:0045087]; negative regulation of double-strand break r... | cytosol [GO:0005829]; nucleus [GO:0005634]; plasma membrane [GO:0005886]; site of double-strand break [GO:0035861] | 2',3'-cyclic GMP-AMP synthase activity [GO:0061501]; ATP binding [GO:0005524]; chromatin binding [GO:0003682]; DNA binding [GO:0003677]; double-stranded DNA binding [GO:0003690]; GTP binding [GO:0005525]; metal ion binding [GO:0046872]; molecular condensate scaffold activity [GO:0140693]; nucleosome binding [GO:0031491... | PF03281;PF20266; | 1.10.1410.40;3.30.460.90; | Mab-21 family | PTM: The N-terminal disordered part (1-146) is phosphorylated by AURKB during the G2-M transition, blocking CGAS liquid phase separation and preventing activation. Phosphorylation at Tyr-204 by BLK promotes cytosolic retention. Localizes into the nucleus following dephosphorylation at Tyr-204 (By similarity). Phosphory... | SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q8C6L5}. Chromosome {ECO:0000250|UniProtKB:Q8C6L5}. Cell membrane {ECO:0000250|UniProtKB:Q8C6L5}; Peripheral membrane protein {ECO:0000250|UniProtKB:Q8C6L5}. Cytoplasm, cytosol {ECO:0000250|UniProtKB:Q8C6L5}. Note=Mainly localizes in the nucleus, and at low level in ... | CATALYTIC ACTIVITY: Reaction=ATP + GTP = 2',3'-cGAMP + 2 diphosphate; Xref=Rhea:RHEA:42064, ChEBI:CHEBI:30616, ChEBI:CHEBI:33019, ChEBI:CHEBI:37565, ChEBI:CHEBI:143093; EC=2.7.7.86; Evidence={ECO:0000250|UniProtKB:Q8C6L5}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:42065; Evidence={ECO:0000250|UniProtKB:Q8C6L... | null | null | null | null | FUNCTION: Nucleotidyltransferase that catalyzes the formation of cyclic GMP-AMP (2',3'-cGAMP) from ATP and GTP and plays a key role in innate immunity. Catalysis involves both the formation of a 2',5' phosphodiester linkage at the GpA step and the formation of a 3',5' phosphodiester linkage at the ApG step, producing c... | Bos taurus (Bovine) |
E1BH29 | ALKB5_BOVIN | MAAASGYTDLREKLKSMTSRDNYKAGSREAAAAAAAAVAAAAAAAAAAEPYAAPGVKRKYPEDSDPERSDFEEQQLQKEEEARKVKSGIRQMRLFSQDECAKIEARIDEVVSRAEKGLYNEHTVDRAPLRNKYFFGEGYTYGAQLQKRGPGQERLYPPGDVDEIPEWVHQLVIQKLVEHRVIPEGFVNSAVINDYQPGGCIVSHVDPIHIFERPIVSVSFFSDSALCFGCKFQFKPIRVSEPVLSLPVRRGSVTVLSGYAADEITHCIRPQDIKERRAVIILRKTRLDAPRLETKSLSSSVLPPSYASDRLSGNNRDPAL... | 1.14.11.53 | COFACTOR: Name=Fe(2+); Xref=ChEBI:CHEBI:29033; Evidence={ECO:0000250|UniProtKB:Q6P6C2}; Note=Binds 1 Fe(2+) ion per subunit. {ECO:0000250|UniProtKB:Q6P6C2}; | cell differentiation [GO:0030154]; mRNA destabilization [GO:0061157]; mRNA export from nucleus [GO:0006406]; mRNA processing [GO:0006397]; non-membrane-bounded organelle assembly [GO:0140694]; oxidative single-stranded RNA demethylation [GO:0035553]; regulation of translation [GO:0006417]; response to hypoxia [GO:00016... | nuclear speck [GO:0016607]; nucleus [GO:0005634]; paraspeckles [GO:0042382] | 2-oxoglutarate-dependent dioxygenase activity [GO:0016706]; metal ion binding [GO:0046872]; molecular condensate scaffold activity [GO:0140693]; mRNA N6-methyladenosine dioxygenase activity [GO:1990931]; oxidative RNA demethylase activity [GO:0035515] | PF13532; | 2.60.120.590; | AlkB family | PTM: Phosphorylated at Ser-87 and Ser-325 in response to reactive oxygen species (ROS), promoting sumoylation and inactivation. {ECO:0000250|UniProtKB:Q6P6C2}.; PTM: Acetylated by KAT8 at Lys-235, promoting interaction with PSPC1, thereby facilitating recognition of N(6)-methyladenosine (m6A) mRNA by ALKBH5. Deacetylat... | SUBCELLULAR LOCATION: Nucleus speckle {ECO:0000250|UniProtKB:Q6P6C2}. Note=Promotes formation and localizes to paraspeckles, a nuclear membraneless organelle. {ECO:0000250|UniProtKB:Q6P6C2}. | CATALYTIC ACTIVITY: Reaction=2-oxoglutarate + an N(6)-methyladenosine in mRNA + O2 = an adenosine in mRNA + CO2 + formaldehyde + succinate; Xref=Rhea:RHEA:49520, Rhea:RHEA-COMP:12414, Rhea:RHEA-COMP:12417, ChEBI:CHEBI:15379, ChEBI:CHEBI:16526, ChEBI:CHEBI:16810, ChEBI:CHEBI:16842, ChEBI:CHEBI:30031, ChEBI:CHEBI:74411, ... | null | null | null | null | FUNCTION: Dioxygenase that specifically demethylates N(6)-methyladenosine (m6A) RNA, the most prevalent internal modification of messenger RNA (mRNA) in higher eukaryotes. Demethylates RNA by oxidative demethylation, which requires molecular oxygen, alpha-ketoglutarate and iron. Demethylation of m6A mRNA affects mRNA p... | Bos taurus (Bovine) |
E1BJS7 | LIN41_BOVIN | MASFPETDFQICLLCKEMCGSPAPLSSNSSASSSSSQTSTSSGGGGGGPGAAARRLHVLPCLAFCRPCLEAHRGGAPGEPLKLRCPVCDQKVVLAEAAGMDARPSSAFLLSNLLDAVVATADEPPPKNGRAGAAAGAGGHGSNHRHHAHHAHPRAAASAPPPPLPPAPPPPAPPRSAPGGPAGSPSALLLRRPHGCSSCDEGNAASSRCLDCQEHLCDNCVRAHQRVRLTKDHYIERGPPGPAAAAAAAAAQQLGLGPPFPGAPFSLLSVFPERLGFCQHHDDEVLHLYCDTCSVPICRECTVGRHGGHSFVYLQEALQD... | 2.3.2.27 | null | fibroblast growth factor receptor signaling pathway [GO:0008543]; G1/S transition of mitotic cell cycle [GO:0000082]; miRNA processing [GO:0035196]; miRNA-mediated gene silencing by inhibition of translation [GO:0035278]; neural tube development [GO:0021915]; post-transcriptional regulation of gene expression [GO:00106... | P-body [GO:0000932] | miRNA binding [GO:0035198]; translation repressor activity [GO:0030371]; ubiquitin protein ligase activity [GO:0061630]; ubiquitin-protein transferase activity [GO:0004842]; zinc ion binding [GO:0008270] | PF00630;PF01436;PF00643; | 4.10.830.40;3.30.160.60;2.60.40.10;2.120.10.30; | TRIM/RBCC family | PTM: Autoubiquitinated. {ECO:0000250|UniProtKB:Q1PSW8}. | SUBCELLULAR LOCATION: Cytoplasm, P-body {ECO:0000250|UniProtKB:Q2Q1W2}. | CATALYTIC ACTIVITY: Reaction=S-ubiquitinyl-[E2 ubiquitin-conjugating enzyme]-L-cysteine + [acceptor protein]-L-lysine = [E2 ubiquitin-conjugating enzyme]-L-cysteine + N(6)-ubiquitinyl-[acceptor protein]-L-lysine.; EC=2.3.2.27; | null | PATHWAY: Protein modification; protein ubiquitination. | null | null | FUNCTION: E3 ubiquitin-protein ligase that cooperates with the microRNAs (miRNAs) machinery and promotes embryonic stem cells proliferation and maintenance (By similarity). Binds to miRNAs and associates with AGO2, participating in post-transcriptional repression of transcripts such as CDKN1A (By similarity). In additi... | Bos taurus (Bovine) |
E1BMF7 | UBP13_BOVIN | MQRRGALFGMPGGSGSRKMAAGDIGELLVPHMPTIRVPRSGDRVYKNECAFSYDSPNSEGGLYVCMNTFLAFGREHVERHFRKTGQSVYMHLKRHVREKVRGASGGALPKRRNSKMFLDLDTDDDLNSDDYEYEDEAKLVIFPDHYEIALPNIEELPALVTIACDAVLSSKSPYRKQDPDTWENELPVSKYANNLTQLDNGVRIPPSGWKCARCDLRENLWLNLTDGSVLCGKWFFDSSGGNGHALEHYRDTGYPLAVKLGTITPDGADVYSFQEEEAVLDPHLAKHLAHFGIDMLHMHGTENGLQDNDIKPRVSEWEVI... | 3.4.19.12 | null | autophagy [GO:0006914]; cell population proliferation [GO:0008283]; protein K63-linked deubiquitination [GO:0070536]; protein stabilization [GO:0050821]; proteolysis [GO:0006508]; regulation of autophagy [GO:0010506]; regulation of DNA-templated transcription [GO:0006355] | cytosol [GO:0005829]; nucleus [GO:0005634] | cysteine-type deubiquitinase activity [GO:0004843]; cysteine-type endopeptidase activity [GO:0004197]; ubiquitin binding [GO:0043130]; zinc ion binding [GO:0008270] | PF00627;PF00443;PF02148;PF17807; | 3.90.70.10;1.10.8.10;3.30.40.10; | Peptidase C19 family | null | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q92995}. | CATALYTIC ACTIVITY: Reaction=Thiol-dependent hydrolysis of ester, thioester, amide, peptide and isopeptide bonds formed by the C-terminal Gly of ubiquitin (a 76-residue protein attached to proteins as an intracellular targeting signal).; EC=3.4.19.12; Evidence={ECO:0000250|UniProtKB:Q92995}; | null | null | null | null | FUNCTION: Deubiquitinase that mediates deubiquitination of target proteins such as BECN1, MITF, SKP2 and USP10 and is involved in various processes such as autophagy, endoplasmic reticulum-associated degradation (ERAD), cell cycle progression or DNA damage response. Component of a regulatory loop that controls autophag... | Bos taurus (Bovine) |
E1BMN8 | NLK_BOVIN | MPNVFQNLVSCKRVFRELKMAAYNGGTSAAAAGHHHHHHHHLPHLPPPHLHHHHHPQHHLHPGSAAAVHPVQQHTSSAAAAAAAAAAAAAMLNPGQQQPYFPSPAPGQAPGPAAAAPAQVQAAAAATVKAHHHQHSHHPQQQLDIEPDRPIGYGAFGVVWSVTDPRDGKRVALKKMPNVFQNLVSCKRVFRELKMLCFFKHDNVLSALDILQPPHIDYFEEIYVVTELMQSDLHKIIVSPQPLSSDHVKVFLYQILRGLKYLHSAGILHRDIKPGNLLVNSNCVLKICDFGLARVEELDESRHMTQEVVTQYYRAPEILM... | 2.7.11.24 | COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250|UniProtKB:O54949}; | intracellular signal transduction [GO:0035556]; negative regulation of TORC1 signaling [GO:1904262]; phosphorylation [GO:0016310]; protein stabilization [GO:0050821]; Wnt signaling pathway [GO:0016055] | cytoplasm [GO:0005737]; nucleus [GO:0005634] | ATP binding [GO:0005524]; MAP kinase activity [GO:0004707]; metal ion binding [GO:0046872]; protein serine kinase activity [GO:0106310]; protein serine/threonine kinase activity [GO:0004674] | PF00069; | 1.10.510.10; | Protein kinase superfamily, CMGC Ser/Thr protein kinase family, MAP kinase subfamily | PTM: Phosphorylated on Thr-305. Intermolecular autophosphorylation on Thr-305 activates the enzyme. {ECO:0000250|UniProtKB:O54949}. | SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:O54949}. Cytoplasm {ECO:0000250|UniProtKB:O54949}. Note=Predominantly nuclear. A smaller fraction is cytoplasmic. {ECO:0000250|UniProtKB:O54949}. | 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:0000250|UniProtKB:O54949}; CATALYT... | null | null | null | null | FUNCTION: Serine/threonine-protein kinase that regulates a number of transcription factors with key roles in cell fate determination. Positive effector of the non-canonical Wnt signaling pathway, acting downstream of WNT5A, MAP3K7/TAK1 and HIPK2. Negative regulator of the canonical Wnt/beta-catenin signaling pathway. B... | Bos taurus (Bovine) |
E1BPK6 | MYO6_BOVIN | MEDGRPVWAPHPTEGFQMGNIVDIGPDSLTIEPLGQKGKTFLALINQVFPAEEDSKKDVEDNCSLMYLNEATLLHNIKVRYSKDRIYTYVANILIAVNPYFDIPKIYSSDSIKSYQGKSLGTMPPHVFAIADKAFRDMKVLKMSQSIIVSGESGAGKTENTKFVLRYLTESYGSGQDIDDRIVEANPLLEAFGNAKTVRNNNSSRFGKFVEIHFNEKSSVVGGFVSHYLLEKSRICVQGKEERNYHIFYRLCAGASEDIRERLHLSSPDNFRYLNRGCTRYFANKETDKQILQNRKTPEHLKAGSLKDPLLDDHGDFVRM... | null | null | actin filament organization [GO:0007015]; actin filament-based movement [GO:0030048]; DNA damage response, signal transduction by p53 class mediator [GO:0030330]; endocytosis [GO:0006897]; inner ear auditory receptor cell differentiation [GO:0042491]; inner ear morphogenesis [GO:0042472]; protein localization [GO:00081... | actin cytoskeleton [GO:0015629]; clathrin-coated endocytic vesicle [GO:0045334]; clathrin-coated pit [GO:0005905]; cytoplasm [GO:0005737]; cytosol [GO:0005829]; endocytic vesicle [GO:0030139]; filamentous actin [GO:0031941]; filopodium [GO:0030175]; Golgi apparatus [GO:0005794]; microvillus [GO:0005902]; myosin complex... | actin filament binding [GO:0051015]; ATP binding [GO:0005524]; calmodulin binding [GO:0005516]; microfilament motor activity [GO:0000146] | PF21521;PF16521;PF00063; | 1.10.10.820;1.20.58.530;3.30.70.1590;6.10.220.10;3.40.850.10;2.30.30.360;1.20.120.720; | TRAFAC class myosin-kinesin ATPase superfamily, Myosin family | PTM: Phosphorylation in the motor domain, induced by EGF, results in translocation of MYO6 from the cell surface to membrane ruffles and affects F-actin dynamics. Phosphorylated in vitro by p21-activated kinase (PAK). {ECO:0000250|UniProtKB:Q29122}. | SUBCELLULAR LOCATION: Golgi apparatus, trans-Golgi network membrane {ECO:0000250|UniProtKB:Q9UM54}; Peripheral membrane protein {ECO:0000250|UniProtKB:Q9UM54}. Golgi apparatus {ECO:0000250|UniProtKB:Q9UM54}. Nucleus {ECO:0000250|UniProtKB:Q9UM54}. Cytoplasm, perinuclear region {ECO:0000250|UniProtKB:Q9UM54}. Membrane, ... | null | null | null | null | null | FUNCTION: Myosins are actin-based motor molecules with ATPase activity. Unconventional myosins serve in intracellular movements (By similarity). Myosin 6 is a reverse-direction motor protein that moves towards the minus-end of actin filaments (By similarity). Has slow rate of actin-activated ADP release due to weak ATP... | Bos taurus (Bovine) |
E1BPQ1 | FOXO1_BOVIN | MAEAPQVVEIDPDFEPLPRPRSCTWPLPRPEFSQSNSATSSPAPSGGAAANPDGAAGLPSASAAAVNADFMSNLSLLEESGDFQQAPGSVAAAAPLSQHPPVPPAAAAAAAGGQLAGQPRKSSSSRRNAWGNLSYADLITKAIESSAEKRLTLSQIYEWMVKSVPYFKDKGDSNSSAGWKNSIRHNLSLHSKFIRVQNEGTGKSSWWMLNPEGGKSGKSPRRRAASMDNNSKFAKSRGRAAKKKASLQSGQEGAGDSPGSQFSKWPASPGSHSNDDFDNWSTFRPRTSSNASTISGRLSPIMTEQDDLGDGDVHSMVYPP... | null | null | apoptotic process [GO:0006915]; autophagy [GO:0006914]; cell differentiation [GO:0030154]; cellular response to hyperoxia [GO:0071455]; cellular response to insulin stimulus [GO:0032869]; cellular response to nitric oxide [GO:0071732]; cellular response to oxidative stress [GO:0034599]; cellular response to starvation ... | cytoplasm [GO:0005737]; nucleus [GO:0005634] | 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]; protein phosphatase 2A binding [GO:0051721]; RNA polymerase II cis-regulatory region sequence... | 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-226 and Ser-292 by PKB/AKT1 promotes nuclear export and inactivation of transactivational activity. Phosphorylation on Thr-24 is required for binding 14-3-3 protei... | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q9R1E0}. 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 loca... | 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. 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 sequence 5'-TT[G/A]TT... | Bos taurus (Bovine) |
E1BPW0 | ENTP5_BOVIN | MALYQGAAFFMLVASCVCSTVFHREQQTWFEGVFLSSMCPVNVSAGTLYGIMFDAGSTGTRIHVYTFVQKVPDNTGQLPVLEGEIFDSVKPGLSAFVDQPKQGAETVQELLEVAKDSIPPSHWKRTPVVLKATAGLRLLPEEKAEALLFEVKEIFKKSPFLVPDDSVSIMDGSYEGILAWVTVNFLTGQLHGHNQETVGTLDLGGASTQITFLPQFEKTLEQTPRDYLTSFEMFNSTYKLYTHSYLGFGLKAARLATLGALETAGIDGYTFRSACLPRWLEAEWIFGGVKYQYGGNQEAGEVGFEPCYAEVLRVVQGKLH... | 3.6.1.6 | COFACTOR: Name=Ca(2+); Xref=ChEBI:CHEBI:29108; Evidence={ECO:0000250|UniProtKB:O75356}; Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250|UniProtKB:O75356}; | 'de novo' post-translational protein folding [GO:0051084]; nucleoside diphosphate catabolic process [GO:0009134]; protein N-linked glycosylation [GO:0006487]; UDP catabolic process [GO:0006256]; UDP-glucose metabolic process [GO:0006011] | endoplasmic reticulum [GO:0005783]; extracellular region [GO:0005576]; membrane [GO:0016020] | ADP phosphatase activity [GO:0043262]; CDP phosphatase activity [GO:0036384]; GDP phosphatase activity [GO:0004382]; IDP phosphatase activity [GO:1990003]; ribonucleoside triphosphate phosphatase activity [GO:0017111]; UDP phosphatase activity [GO:0045134] | PF01150; | 3.30.420.40;3.30.420.150; | GDA1/CD39 NTPase family | PTM: N-glycosylated; high-mannose type. {ECO:0000250|UniProtKB:Q9WUZ9}. | SUBCELLULAR LOCATION: Endoplasmic reticulum {ECO:0000250|UniProtKB:Q9WUZ9}. Secreted {ECO:0000250|UniProtKB:O75356}. | CATALYTIC ACTIVITY: Reaction=a ribonucleoside 5'-diphosphate + H2O = a ribonucleoside 5'-phosphate + H(+) + phosphate; Xref=Rhea:RHEA:36799, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:43474, ChEBI:CHEBI:57930, ChEBI:CHEBI:58043; EC=3.6.1.6; Evidence={ECO:0000250|UniProtKB:O75356}; PhysiologicalDirection=left-to-... | null | PATHWAY: Protein modification; protein glycosylation. {ECO:0000250|UniProtKB:Q9WUZ9}. | null | null | FUNCTION: Hydrolyzes nucleoside diphosphates with a preference for GDP, IDP and UDP compared to ADP and CDP (By similarity). In the lumen of the endoplasmic reticulum, hydrolyzes UDP that acts as an end-product feedback inhibitor of the UDP-Glc:glycoprotein glucosyltransferases. UMP can be transported back by an UDP-su... | Bos taurus (Bovine) |
E1BPX4 | MCM8_BOVIN | MNGKYRGRGFGQGRFQSWKSGRGGRGFSGKWREREHRPDLNKATGKHPEQTPQSLLLQSTLDHFIPYKGWKLYFSEVYSDSIPFIEKIEAFESFFTERIELYDKDEIERKGSILVDFKELINDDEIIKLIPNIANELRDTPEKTLACMGLAIHQVLTKDLERHAAELQAQEGLSRNGETVVNVPHIHARVYNYEPLTQLKNVRANYYGKYIALRGTVVRVSNTKPLCTKMAFLCAACGEIQSLSLPDGKYNLPTKCPVPACRGKSFTALRSSPLTVTMDWQSIKIQELMSDDQREAGRIPRTIECELVHDLVDSCVPGDT... | 3.6.4.12 | null | cell cycle [GO:0007049]; DNA damage response [GO:0006974]; DNA replication [GO:0006260]; double-strand break repair via homologous recombination [GO:0000724]; female gamete generation [GO:0007292]; male gamete generation [GO:0048232]; protein localization to chromatin [GO:0071168]; protein stabilization [GO:0050821]; r... | chromosome [GO:0005694]; MCM complex [GO:0042555]; MCM8-MCM9 complex [GO:0097362]; nucleus [GO:0005634]; organelle membrane [GO:0031090] | ATP binding [GO:0005524]; ATP hydrolysis activity [GO:0016887]; chromatin binding [GO:0003682]; enzyme binding [GO:0019899]; MutLbeta complex binding [GO:0032406]; MutSalpha complex binding [GO:0032407]; MutSbeta complex binding [GO:0032408]; single-stranded DNA binding [GO:0003697]; single-stranded DNA helicase activi... | PF00493;PF17855;PF17207; | 2.20.28.10;2.40.50.140;3.40.50.300; | MCM family | null | SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q9UJA3}. Chromosome {ECO:0000250|UniProtKB:Q9UJA3}. Note=Localizes to nuclear foci. Localizes to double-stranded DNA breaks. Binds chromatin throughout the cell cycle. {ECO:0000250|UniProtKB:Q9UJA3}. | CATALYTIC ACTIVITY: Reaction=ATP + H2O = ADP + H(+) + phosphate; Xref=Rhea:RHEA:13065, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:456216; EC=3.6.4.12; Evidence={ECO:0000250|UniProtKB:Q9UJA3}; | null | null | null | null | FUNCTION: Component of the MCM8-MCM9 complex, a complex involved in the repair of double-stranded DNA breaks (DBSs) and DNA interstrand cross-links (ICLs) by homologous recombination (HR). Required for DNA resection by the MRE11-RAD50-NBN/NBS1 (MRN) complex by recruiting the MRN complex to the repair site and by promot... | Bos taurus (Bovine) |
E1BSI0 | PARP3_CHICK | MAPKRRAPPASQPADGGKKAKGGQEEEEDAWSSALNALKTAPREKPPATIDGQCPLSAGPDAKVYEDYDCTLNQTNISANNNKFYIIQLIEHGGTYSTWNRWGRVGEVGQSKLLPFTSLEAAKKDFEKKFWEKTKNRWAARDNFVAQPGKYTLIEVQPGAGQEVALRVDGAGDEKVSKRRVLPCALDETTQKLVALIFSSDMFRHAMQAMNIDVKKMPLGKLSKQQIARGFEALEELEAALGEQPRSMSRLEELSSRFYTIVPHNFGRARPPPIDSPELLRAKKDMLLVLADIEVAQSLQAQKVEEEEVVAHPLDRDYAL... | 2.4.2.- | null | double-strand break repair [GO:0006302] | centriole [GO:0005814]; centrosome [GO:0005813]; cytoplasm [GO:0005737]; nucleolus [GO:0005730]; site of double-strand break [GO:0035861] | NAD+ ADP-ribosyltransferase activity [GO:0003950]; NAD+- protein-lysine ADP-ribosyltransferase activity [GO:0140804]; NAD+-protein ADP-ribosyltransferase activity [GO:1990404]; nucleotidyltransferase activity [GO:0016779] | PF00644;PF02877;PF05406; | 3.90.228.10;1.20.142.10;2.20.140.10; | ARTD/PARP family | null | SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q9Y6F1}. Chromosome {ECO:0000269|PubMed:27530147}. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome {ECO:0000250|UniProtKB:Q9Y6F1}. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome, centriole {ECO:0000250|UniProtKB:Q9Y6F1}. Note=Al... | CATALYTIC ACTIVITY: Reaction=L-aspartyl-[protein] + NAD(+) = 4-O-(ADP-D-ribosyl)-L-aspartyl-[protein] + nicotinamide; Xref=Rhea:RHEA:54424, Rhea:RHEA-COMP:9867, Rhea:RHEA-COMP:13832, ChEBI:CHEBI:17154, ChEBI:CHEBI:29961, ChEBI:CHEBI:57540, ChEBI:CHEBI:138102; Evidence={ECO:0000250|UniProtKB:Q9Y6F1}; PhysiologicalDirect... | null | null | null | null | FUNCTION: Mono-ADP-ribosyltransferase that mediates mono-ADP-ribosylation of target proteins and plays a key role in the response to DNA damage (PubMed:27530147). Mediates mono-ADP-ribosylation of glutamate, aspartate or lysine residues on target proteins (By similarity). In contrast to PARP1 and PARP2, it is not able ... | Gallus gallus (Chicken) |
E1BSW7 | CENPS_CHICK | MEAAGGEQRELLIQRLRAAVHYTTGCLCQDVAEDKGVLFSKQTVAAISEITFRQCENFARDLEMFARHAKRSTITSEDVKLLARRSNSLLKYITQKSDELASSNMEQKEKKKKKSSAAKGRKTEENETPVTESEDSNMA | null | null | cell division [GO:0051301]; DNA repair [GO:0006281]; replication fork processing [GO:0031297]; resolution of meiotic recombination intermediates [GO:0000712] | FANCM-MHF complex [GO:0071821]; Fanconi anaemia nuclear complex [GO:0043240]; kinetochore [GO:0000776] | chromatin binding [GO:0003682]; DNA binding [GO:0003677]; protein heterodimerization activity [GO:0046982] | PF15630; | 1.10.20.10; | TAF9 family, CENP-S/MHF1 subfamily | null | SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:19620631}. Chromosome, centromere {ECO:0000269|PubMed:19620631}. Chromosome, centromere, kinetochore {ECO:0000269|PubMed:19620631}. Note=Assembly of CENPS and CENPX and its partner subunits CENPT and CENPW at centromeres occurs through a dynamic exchange mechanism. Alth... | null | null | null | null | null | FUNCTION: DNA-binding component of the Fanconi anemia (FA) core complex. Required for the normal activation of the FA pathway, leading to monoubiquitination of the FANCI-FANCD2 complex in response to DNA damage, cellular resistance to DNA cross-linking drugs, and prevention of chromosomal breakage (PubMed:20347428). In... | Gallus gallus (Chicken) |
E1BTG2 | LMOD2_CHICK | MSTFGYRRELSKYEDIDEDELLASLTEEELKELERELEDIEPDRNLPVGQRQKSLTEKTPTGTFSREALMAYWERETRKLLEKERLGACEKDSEQEEDNSEDIQEECFTESNSEVSEEAYTEEDDEEEEEEEEEEEDEDDSDDEDEEKQNSAASERPVNCEDGRSSSHVRHKKCSNAKNSENLFNGHDGKDTENLSFKSSAIHPCGNPTVIEDALEKVRSNDPETTEVNLNNIENITSQMLIQFSQALRDNTVVKSFSLANTHADDNVAIAIAGMLKVNQHITSLNIESNFITGKGVLAIMRALQHNKVLTELRFHNQRH... | null | null | actin filament organization [GO:0007015]; actin filament polymerization [GO:0030041]; muscle contraction [GO:0006936]; myofibril assembly [GO:0030239]; pointed-end actin filament capping [GO:0051694] | actin filament [GO:0005884]; cytoskeleton [GO:0005856]; M band [GO:0031430]; myofibril [GO:0030016]; striated muscle thin filament [GO:0005865] | actin binding [GO:0003779]; tropomyosin binding [GO:0005523] | PF03250; | 3.80.10.10; | Tropomodulin family | null | SUBCELLULAR LOCATION: Cytoplasm, myofibril, sarcomere {ECO:0000269|PubMed:20736303}. Cytoplasm, myofibril {ECO:0000269|PubMed:20736303}. Cytoplasm, myofibril, sarcomere, M line {ECO:0000269|PubMed:20736303}. Cytoplasm, cytoskeleton {ECO:0000269|PubMed:20736303}. Note=Colocalizes with actin filament pointed ends in sarc... | null | null | null | null | null | FUNCTION: Mediates nucleation of actin filaments and thereby promotes actin polymerization (By similarity). Plays a role in the regulation of actin filament length (PubMed:20736303). Required for normal sarcomere organization in the heart, and for normal heart function (By similarity). {ECO:0000250|UniProtKB:Q3UHZ5, EC... | Gallus gallus (Chicken) |
E1BY77 | UBP13_CHICK | MQRAALFGGGDAQMAAGDLGELLVPYMPTIRVPKSGDRVYKTECAFSYDSPDSEGGLYVCMNTFLGFGREHIERHYRKTGQCVYLHLKRHVIEKVPGASGGALPKRRNAKLFLDLEANGDLSSDDFEYEDEAKLVIFPDHYEISLPNIEELPALVTIASDALLSAKSPYRKQDPDSWEEELQASKHAKSLVQLDNGVRIPPSGWKCSKCDLRENLWLNLTDGSVLCGKWFFDGSGGNGHAMEHYKETGYPLAVKLGTITPDGADVYSFDEEEPVLDPHIAKHLAHFGIDMLQMQVAENGLRDNDIKPRVSEWEVIQEAGV... | 3.4.19.12 | null | autophagy [GO:0006914]; cell population proliferation [GO:0008283]; maintenance of unfolded protein [GO:0036506]; positive regulation of ERAD pathway [GO:1904294]; protein K63-linked deubiquitination [GO:0070536]; protein stabilization [GO:0050821]; proteolysis [GO:0006508]; regulation of autophagy [GO:0010506]; regula... | cytosol [GO:0005829]; nucleus [GO:0005634] | BAT3 complex binding [GO:1904288]; cysteine-type deubiquitinase activity [GO:0004843]; cysteine-type endopeptidase activity [GO:0004197]; K48-linked deubiquitinase activity [GO:1990380]; proteasome binding [GO:0070628]; protein-folding chaperone binding [GO:0051087]; ubiquitin binding [GO:0043130]; ubiquitin protein li... | PF00627;PF00443;PF02148;PF17807; | 3.90.70.10;1.10.8.10;3.30.40.10; | Peptidase C19 family | null | null | CATALYTIC ACTIVITY: Reaction=Thiol-dependent hydrolysis of ester, thioester, amide, peptide and isopeptide bonds formed by the C-terminal Gly of ubiquitin (a 76-residue protein attached to proteins as an intracellular targeting signal).; EC=3.4.19.12; | null | null | null | null | FUNCTION: Deubiquitinase that mediates deubiquitination of target proteins and is involved in various processes such as autophagy and endoplasmic reticulum-associated degradation (ERAD). {ECO:0000250|UniProtKB:Q92995}. | Gallus gallus (Chicken) |
E1C1L6 | ENTP5_CHICK | MTSSRLPVLLALVFSSLSPVLSHSNREMWFQDLFPPNTCPINAKTKTFYGIMFDAGSTGTRIHIYTFVQKSPEILPELEGEIFESVKPGLSAYADQPEKGAESVKRLLDMAIDAVPPHLWKKTPVVLKATAGLRLLSEEKAQALLSEVKEVFEESPFLVPEDSVSIMDGSYEGILAWITVNFLTGQLSGQNQHTVGTLDLGGASTQITFLPRFEETLKESPTDFLTSFEMFNSTYKLYTHSYLGFGLKAARLATLGALNTEVADRQMFRSSCLPKQLEAEWHFGGVKYRYGGNKEGETGFKPCYLEVLKVVKGKLHQPDE... | 3.6.1.6 | COFACTOR: Name=Ca(2+); Xref=ChEBI:CHEBI:29108; Evidence={ECO:0000250|UniProtKB:O75356}; Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250|UniProtKB:O75356}; | 'de novo' post-translational protein folding [GO:0051084]; nucleoside diphosphate catabolic process [GO:0009134]; protein N-linked glycosylation [GO:0006487]; UDP catabolic process [GO:0006256]; UDP-glucose metabolic process [GO:0006011] | endoplasmic reticulum [GO:0005783]; extracellular region [GO:0005576]; membrane [GO:0016020] | ADP phosphatase activity [GO:0043262]; CDP phosphatase activity [GO:0036384]; GDP phosphatase activity [GO:0004382]; IDP phosphatase activity [GO:1990003]; ribonucleoside triphosphate phosphatase activity [GO:0017111]; UDP phosphatase activity [GO:0045134] | PF01150; | 3.30.420.40;3.30.420.150; | GDA1/CD39 NTPase family | null | SUBCELLULAR LOCATION: Endoplasmic reticulum {ECO:0000250|UniProtKB:Q9WUZ9}. Secreted {ECO:0000250|UniProtKB:O75356}. | CATALYTIC ACTIVITY: Reaction=a ribonucleoside 5'-diphosphate + H2O = a ribonucleoside 5'-phosphate + H(+) + phosphate; Xref=Rhea:RHEA:36799, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:43474, ChEBI:CHEBI:57930, ChEBI:CHEBI:58043; EC=3.6.1.6; Evidence={ECO:0000250|UniProtKB:O75356}; PhysiologicalDirection=left-to-... | null | PATHWAY: Protein modification; protein glycosylation. {ECO:0000250|UniProtKB:Q9WUZ9}. | null | null | FUNCTION: Hydrolyzes nucleoside diphosphates with a preference for GDP, IDP and UDP compared to ADP and CDP (By similarity). In the lumen of the endoplasmic reticulum, hydrolyzes UDP that acts as an end-product feedback inhibitor of the UDP-Glc:glycoprotein glucosyltransferases. UMP can be transported back by an UDP-su... | Gallus gallus (Chicken) |
E1C2I2 | GWL_CHICK | MSTVEPLSDEGVAAGPRRIEVPRPPSIEEFTIVKPISRGAFGKVYLGRKAGRLYAVKVMKKADMINKNMVHQVQAERDALALSKSPFIVHLYYSLQSANNVYLVMEYLIGGDVKSLLHIYGYFDEEMAVKYISEAALALDYLHRHGIIHRDLKPDNMLISNQGHIKLTDFGLSRVTLNREINMIDILTTPSMAKPKHDYSRTPGQLLSLISSLGFYTPVGMKMPINPNSGGASDSLHEVISPLSMIEKENTPLSTKLFKTGLDTSPLTPVMPVRSLTPALLQSRERFGASTASSQSCMYLSSMESECCSSPRLEKDVKQT... | 2.7.11.1 | null | cell division [GO:0051301]; DNA damage response [GO:0006974]; G2/M transition of mitotic cell cycle [GO:0000086]; intracellular signal transduction [GO:0035556]; mitotic cell cycle [GO:0000278]; negative regulation of phosphoprotein phosphatase activity [GO:0032515]; phosphorylation [GO:0016310] | centrosome [GO:0005813]; cleavage furrow [GO:0032154]; cytoplasm [GO:0005737]; nucleus [GO:0005634] | ATP binding [GO:0005524]; protein phosphatase 2A binding [GO:0051721]; protein serine kinase activity [GO:0106310]; protein serine/threonine kinase activity [GO:0004674] | PF00069; | 1.10.510.10; | Protein kinase superfamily, AGC Ser/Thr protein kinase family | PTM: Phosphorylation at Thr-743 by CDK1 during M phase activates its kinase activity. Maximum phosphorylation occurs in prometaphase (By similarity). {ECO:0000250}. | SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, microtubule organizing center, centrosome {ECO:0000250}. Nucleus. Note=During interphase is mainly nuclear, upon nuclear envelope breakdown localizes at the cytoplasm and during mitosis at the centrosomes. {ECO:0000250}. | CATALYTIC ACTIVITY: Reaction=ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-[protein]; Xref=Rhea:RHEA:17989, Rhea:RHEA-COMP:9863, Rhea:RHEA-COMP:11604, ChEBI:CHEBI:15378, ChEBI:CHEBI:29999, ChEBI:CHEBI:30616, ChEBI:CHEBI:83421, ChEBI:CHEBI:456216; EC=2.7.11.1; CATALYTIC ACTIVITY: Reaction=ATP + L-threonyl-[pr... | null | null | null | null | FUNCTION: Serine/threonine kinase that plays a key role in M phase by acting as a regulator of mitosis entry and maintenance. Acts by promoting the inactivation of protein phosphatase 2A (PP2A) during M phase: does not directly inhibit PP2A but acts by mediating phosphorylation and subsequent activation of ARPP19 and E... | Gallus gallus (Chicken) |
E1C3P4 | CBPC1_CHICK | MKVKKNLTCSVSTSSRTMSLLSQLEKINLDSVLGEADNARYVTAKILHLVQSQEKTKKEMTSKGSSAIEVILSTLENTRDPQTILNILSILIELVSVGGGRRASVLVTKGGTQILLQLLLNASKESPPNEELMVLLHTLLAKIGPKDKKIGMKARINGALNISLNLVKQNLQNHRLILPCLQVLRVYSTNSVNAVSLGKNGVVELMFKIIGPFSKKNTSLMKVALDTLAALLKSKTNARRAVDRGYVHMLLTIYVDWHRHDSRHRYMLIRKGVLQCIKSVTNIKLGRKAFIDANGMKILYNTSQECLAVRTLDPLVNTSS... | 3.4.17.-; 3.4.17.24 | COFACTOR: Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000250}; Note=Binds 1 zinc ion per subunit. {ECO:0000250}; | C-terminal protein deglutamylation [GO:0035609]; cerebellar Purkinje cell differentiation [GO:0021702]; eye photoreceptor cell differentiation [GO:0001754]; mitochondrion organization [GO:0007005]; neuromuscular process [GO:0050905]; olfactory bulb development [GO:0021772]; protein side chain deglutamylation [GO:003561... | cytoplasm [GO:0005737]; cytosol [GO:0005829]; mitochondrion [GO:0005739]; nucleus [GO:0005634] | metallocarboxypeptidase activity [GO:0004181]; tubulin binding [GO:0015631]; zinc ion binding [GO:0008270] | PF18027;PF00246; | 2.60.40.3120;1.25.10.10;3.40.630.10; | Peptidase M14 family | null | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q9UPW5}. Cytoplasm, cytosol {ECO:0000250|UniProtKB:Q641K1}. Nucleus {ECO:0000250|UniProtKB:Q641K1}. Mitochondrion {ECO:0000250|UniProtKB:Q641K1}. | CATALYTIC ACTIVITY: Reaction=(L-glutamyl)(n+1)-gamma-L-glutamyl-L-glutamyl-[protein] + H2O = (L-glutamyl)(n)-gamma-L-glutamyl-L-glutamyl-[protein] + L-glutamate; Xref=Rhea:RHEA:60004, Rhea:RHEA-COMP:15519, Rhea:RHEA-COMP:15675, ChEBI:CHEBI:15377, ChEBI:CHEBI:29985, ChEBI:CHEBI:143623; Evidence={ECO:0000250|UniProtKB:Q6... | null | null | null | null | FUNCTION: Metallocarboxypeptidase that mediates protein deglutamylation of tubulin and non-tubulin target proteins. Catalyzes the removal of polyglutamate side chains present on the gamma-carboxyl group of glutamate residues within the C-terminal tail of alpha- and beta-tubulin. Specifically cleaves tubulin long-side-c... | Gallus gallus (Chicken) |
E1C3U7 | LOXL2_CHICK | MEGFLGFNHNHCFIVLFFVSLSLAQYEHWPYLPGYPEPPPQVYQPPRRPADVPKIQLRLAGQKRKHNEGRVEVFYNGEWGTVCDDDFSIHAAHVICRELGYVEAVSWLPSSKYGKGEGKIWMDNVHCNGKEATLAACTSNGWGVTDCKHTEDVGVVCSEKRIPGFKFDNSLLNQIENMNIQVEDIRIRPILATYRKRVPVTEGYVEVKDEGTWKQICDKHWTMKNSRVVCGMFGFPSERKYNTKVYKMFASRRKQHYWAYSMDCTGNEAHISSCKLGNHLNVDTEKNATCDNGMPAVASCVPGRAFAPSSHSGFRKAFRQ... | 1.4.3.13 | COFACTOR: Name=Cu cation; Xref=ChEBI:CHEBI:23378; Evidence={ECO:0000250|UniProtKB:Q9Y4K0}; COFACTOR: Name=lysine tyrosylquinone residue; Xref=ChEBI:CHEBI:20489; Evidence={ECO:0000250|UniProtKB:Q9Y4K0}; Note=Contains 1 lysine tyrosylquinone. {ECO:0000250|UniProtKB:P33072, ECO:0000250|UniProtKB:Q9Y4K0}; | collagen fibril organization [GO:0030199]; endothelial cell migration [GO:0043542]; endothelial cell proliferation [GO:0001935]; epithelial to mesenchymal transition [GO:0001837]; heterochromatin organization [GO:0070828]; negative regulation of DNA-templated transcription [GO:0045892]; negative regulation of stem cell... | basement membrane [GO:0005604]; chromatin [GO:0000785]; collagen-containing extracellular matrix [GO:0062023]; endoplasmic reticulum [GO:0005783]; extracellular space [GO:0005615]; membrane [GO:0016020]; nucleus [GO:0005634] | calcium ion binding [GO:0005509]; copper ion binding [GO:0005507]; protein-lysine 6-oxidase activity [GO:0004720] | PF01186;PF00530; | 3.10.250.10; | Lysyl oxidase family | PTM: The lysine tyrosylquinone cross-link (LTQ) is generated by condensation of the epsilon-amino group of a lysine with a topaquinone produced by oxidation of tyrosine. {ECO:0000250|UniProtKB:Q9Y4K0}. | SUBCELLULAR LOCATION: Secreted, extracellular space, extracellular matrix, basement membrane {ECO:0000250|UniProtKB:Q9Y4K0}. Nucleus {ECO:0000250|UniProtKB:Q9Y4K0}. Chromosome {ECO:0000250|UniProtKB:Q9Y4K0}. Endoplasmic reticulum {ECO:0000250|UniProtKB:Q9Y4K0}. Note=Associated with chromatin. It is unclear how LOXL2 is... | CATALYTIC ACTIVITY: Reaction=H2O + L-lysyl-[protein] + O2 = (S)-2-amino-6-oxohexanoyl-[protein] + H2O2 + NH4(+); Xref=Rhea:RHEA:24544, Rhea:RHEA-COMP:9752, Rhea:RHEA-COMP:12448, ChEBI:CHEBI:15377, ChEBI:CHEBI:15379, ChEBI:CHEBI:16240, ChEBI:CHEBI:28938, ChEBI:CHEBI:29969, ChEBI:CHEBI:131803; EC=1.4.3.13; Evidence={ECO:... | null | null | null | null | FUNCTION: Mediates the post-translational oxidative deamination of lysine residues on target proteins leading to the formation of deaminated lysine (allysine). Acts as a transcription corepressor and specifically mediates deamination of trimethylated 'Lys-4' of histone H3 (H3K4me3), a specific tag for epigenetic transc... | Gallus gallus (Chicken) |
E1C656 | HACE1_CHICK | MERAMEQLNRLTRSLRRARTVELPDDNETAVYTLMPMVMADQHRSVSELLSNSKFDVNYAFGRVKRSLLHIAANCGSVECLVLLLKKGANPNYQDISGCTPLHLAARNGQKKCMSKLLEYSADVNICNNEGLTAIHWLAVNGRTELLHDLVQHVSNVDVEDAMGQTALHVACQNGHKTTVQCLLDSGADINRPNVSGATPLYFACSHGQRDTAQILLMRGAKYLPDKNGITPLDLCVQGGYGETCEVLIQYHPRLFQTIIQMTQNEDLRENMLRQVLEHLSQQSESQYLKILTSLAEVATTNGHKLLSLSSNYEAQMKSL... | 2.3.2.26 | null | cell cycle [GO:0007049]; Golgi organization [GO:0007030]; membrane fusion [GO:0061025]; protein K48-linked ubiquitination [GO:0070936]; protein polyubiquitination [GO:0000209]; protein ubiquitination [GO:0016567]; regulation of cell migration [GO:0030334]; ubiquitin-dependent protein catabolic process [GO:0006511] | cytoplasm [GO:0005737]; endoplasmic reticulum [GO:0005783]; Golgi cisterna membrane [GO:0032580]; Golgi membrane [GO:0000139]; nucleus [GO:0005634] | small GTPase binding [GO:0031267]; ubiquitin protein ligase activity [GO:0061630]; ubiquitin-protein transferase activity [GO:0004842] | PF12796;PF13857;PF00632; | 1.25.40.20;3.30.2160.10;3.30.2410.10;3.90.1750.10; | null | null | SUBCELLULAR LOCATION: Golgi apparatus, Golgi stack membrane {ECO:0000250}. Cytoplasm {ECO:0000250}. Endoplasmic reticulum {ECO:0000250}. | CATALYTIC ACTIVITY: Reaction=S-ubiquitinyl-[E2 ubiquitin-conjugating enzyme]-L-cysteine + [acceptor protein]-L-lysine = [E2 ubiquitin-conjugating enzyme]-L-cysteine + N(6)-ubiquitinyl-[acceptor protein]-L-lysine.; EC=2.3.2.26; | null | PATHWAY: Protein modification; protein ubiquitination. | null | null | FUNCTION: E3 ubiquitin-protein ligase involved in Golgi membrane fusion and regulation of small GTPases. Acts as a regulator of Golgi membrane dynamics during the cell cycle: recruited to Golgi membrane by Rab proteins and regulates postmitotic Golgi membrane fusion. Acts by mediating ubiquitination during mitotic Golg... | Gallus gallus (Chicken) |
E1C7U0 | STING_CHICK | MPQDPSTRSSPARLLIPEPRAGRARHAACVLLAVCFVVLFLSGEPLAPIIRSVCTQLAALQLGVLLKGCCCLAEEIFHLHSRHHGSLWQVLCSCFPPRWYLALLLVGGSAYLDPPEDNGHSPRLALTLSCLCQLLVLALGLQKLSAVEVSELTESSKKNVAHGLAWSYYIGYLKVVLPRLKECMEELSRTNPMLRAHRDTWKLHILVPLGCDIWDDLEKADSNIQYLADLPETILTRAGIKRRVYKHSLYVIRDKDNKLRPCVLEFASPLQTLCAMSQDDCAAFSREQRLEQARLFYRSLRDILGSSKECAGLYRLIAYE... | null | null | activation of innate immune response [GO:0002218]; autophagosome assembly [GO:0000045]; cGAS/STING signaling pathway [GO:0140896]; defense response to virus [GO:0051607]; innate immune response [GO:0045087]; positive regulation of interferon-beta production [GO:0032728]; positive regulation of macroautophagy [GO:001623... | autophagosome [GO:0005776]; autophagosome membrane [GO:0000421]; cytoplasm [GO:0005737]; cytoplasmic vesicle [GO:0031410]; endoplasmic reticulum membrane [GO:0005789]; endoplasmic reticulum-Golgi intermediate compartment membrane [GO:0033116]; Golgi membrane [GO:0000139]; perinuclear region of cytoplasm [GO:0048471] | 2',3'-cyclic GMP-AMP binding [GO:0061507]; cyclic-di-GMP binding [GO:0035438]; protein homodimerization activity [GO:0042803]; proton channel activity [GO:0015252] | PF15009; | 1.20.5.5200;3.40.50.12100; | STING family | PTM: Phosphorylation by TBK1 leads to activation and production of IFN-beta (Probable). Following cyclic nucleotide (c-di-GMP or cGAMP)-binding, activation and translocation from the endoplasmic reticulum, STING1 is phosphorylated by TBK1 at Ser-366 in the pLxIS motif (Probable). The phosphorylated pLxIS motif constitu... | SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000250|UniProtKB:Q86WV6}; Multi-pass membrane protein {ECO:0000255}. Cytoplasm, perinuclear region {ECO:0000250|UniProtKB:Q86WV6}. Endoplasmic reticulum-Golgi intermediate compartment membrane {ECO:0000250|UniProtKB:Q86WV6}; Multi-pass membrane protein {ECO:000... | CATALYTIC ACTIVITY: Reaction=H(+)(in) = H(+)(out); Xref=Rhea:RHEA:34979, ChEBI:CHEBI:15378; Evidence={ECO:0000250|UniProtKB:Q86WV6}; | null | null | null | null | FUNCTION: Facilitator of innate immune signaling that acts as a sensor of cytosolic DNA from bacteria and viruses and promotes the production of type I interferon (IFN-alpha and IFN-beta) (By similarity). Innate immune response is triggered in response to non-CpG double-stranded DNA from viruses and bacteria delivered ... | Gallus gallus (Chicken) |
E1C8P7 | DSCL1_CHICK | MWLVTFFLLYSLRKAHTEDVGTSLYFVNDSIQQVTFSSTVGVVIPCPAAGSPSAVLRWYLATGDDIYDVPHIRHVHANGTLQLYPFSPSAFNSFIHDNDYFCTAENSAGKIRSPNIRVKAVFREPYTVRVEDQRSMRGNVAVFKCLIPSSVQEYVSVVSWEKDTVSIIPENRFFITSYGGLYISDVQKEDALSTYRCITKHKYSGETRQSNGARLSVSDADPAESIPTMLDSFQSREVRAGRLVELPCIASGYPNPAIRWLKDGRPLPADGRWAKRITGLSIADLRVEDSGTYICEVTNTFGSAEVTGTLTVIDPLRVTL... | null | null | axon guidance [GO:0007411]; camera-type eye photoreceptor cell differentiation [GO:0060219]; dendrite self-avoidance [GO:0070593]; homophilic cell adhesion via plasma membrane adhesion molecules [GO:0007156]; retina layer formation [GO:0010842]; synapse assembly [GO:0007416] | axon [GO:0030424]; plasma membrane [GO:0005886]; synapse [GO:0045202] | cell-cell adhesion mediator activity [GO:0098632] | PF00041;PF07679;PF13927; | 2.60.40.10; | null | null | SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:Q4VA61}; Single-pass type I membrane protein {ECO:0000250|UniProtKB:Q4VA61}. Synapse {ECO:0000269|PubMed:18216854}. | null | null | null | null | null | FUNCTION: Cell adhesion molecule that plays a role in neuronal self-avoidance. Promotes repulsion between specific neuronal processes of either the same cell or the same subtype of cells (By similarity). Adhesion molecule that promotes lamina-specific synaptic connections in the retina: expressed in specific subsets of... | Gallus gallus (Chicken) |
E1CG36 | CAP15_STRSQ | MNELEFHPHADRRTGSHTMEYQHLGVVPVVSAQANSTPLGGCTLSDGVIRAMGDAARFHVDMEQLWQAAGSFLAEATGSEDACPVTGAAAGMAIAVAACVAGTDGLRVQRLPDPGDQPNEIVLQKGHSISYGGAPLAQMIALGGGRAVEVGAVNETPRSHVASAVTRRTAALVYVTSRTHAVHRKGVPLDELVAIGREHGVPVIVDAAGEGGLRRWVASGADLVIYSGPKMLGAPTSGFICGRGDLVAACRAQYSGIARPMKVGKENLLGLLQAVREYTAVPEEQRAAEQLERMTKLAARLDKIPGLSARTAQDDSGRTI... | 1.-.-.- | COFACTOR: Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326; Evidence={ECO:0000269|PubMed:29343643, ECO:0000269|PubMed:37556254}; Note=Requires pyridoxal phosphate as an oxygenase cofactor. {ECO:0000269|PubMed:29343643}; | antibiotic biosynthetic process [GO:0017000] | null | L-seryl-tRNA(Sec) selenium transferase activity [GO:0004125]; monooxygenase activity [GO:0004497] | PF03841; | 3.40.640.10; | SelA family | null | null | CATALYTIC ACTIVITY: Reaction=(5'S,6'R)-C-glycyluridine + O2 = CO2 + H2O + uridine-5'-carboxamide; Xref=Rhea:RHEA:77179, ChEBI:CHEBI:15377, ChEBI:CHEBI:15379, ChEBI:CHEBI:16526, ChEBI:CHEBI:195553, ChEBI:CHEBI:195554; Evidence={ECO:0000269|PubMed:29343643}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:77180; Evi... | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=560 uM for (5'S,6'R)-C-glycyluridine {ECO:0000269|PubMed:29343643}; Note=kcat is 0.93 min(-1) with (5'S,6'R)-C-glycyluridine as substrate. {ECO:0000269|PubMed:29343643}; | PATHWAY: Antibiotic biosynthesis. {ECO:0000305|PubMed:29343643}. | BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 7.5. {ECO:0000269|PubMed:29343643}; | null | FUNCTION: Monooxygenase-decarboxylase involved in the biosynthesis of the capuramycin-type nucleoside antibiotic A-503083 (PubMed:29343643). Catalyzes the oxidative decarboxylation of 5'-C-glycyluridine (GlyU) to uridine-5'-carboxamide (CarU) (PubMed:29343643). Is stereospecific for the (5'S,6'R)-diastereomer of GlyU (... | Streptomyces sp |
E1JIB2 | IYD_DROME | MDVDELISSSKLLKHWPSLFITLALIWIVKRLFFKGNRVLKTYNLDEQVEEEVEHFADLGDELQPALEDKPHVPFVPGQNLNPNGAKRLYELMRGRRSIRSFNSHPKPDLSVIEDCIRAAGTAPSGAHTEPWTYCVVQEPELKRSIREIVEQEELVNYSQRMHPQWVTDLRPLQTNHVKEYLTEAPYLILIFKQTYGLSENGKRMRRHYYNEISTSIAAGILLCALQAAGLASLVTTPLNCGPALRNLLGRPVNEKLLILLPVGYPKDGCTVPDLARKNLSNIMVTF | 1.21.1.1 | COFACTOR: Name=FMN; Xref=ChEBI:CHEBI:58210; Evidence={ECO:0000269|PubMed:27643701}; | positive regulation of fertilization [GO:1905516]; thyroid hormone metabolic process [GO:0042403]; tyrosine metabolic process [GO:0006570] | plasma membrane [GO:0005886] | FMN binding [GO:0010181]; iodide peroxidase activity [GO:0004447]; iodotyrosine deiodinase activity [GO:0140616] | PF00881; | 3.40.109.10; | Nitroreductase family | null | SUBCELLULAR LOCATION: Cell membrane {ECO:0000255}; Single-pass membrane protein {ECO:0000255}. | CATALYTIC ACTIVITY: Reaction=2 iodide + L-tyrosine + 2 NADP(+) = 3,5-diiodo-L-tyrosine + H(+) + 2 NADPH; Xref=Rhea:RHEA:32479, ChEBI:CHEBI:15378, ChEBI:CHEBI:16382, ChEBI:CHEBI:57506, ChEBI:CHEBI:57783, ChEBI:CHEBI:58315, ChEBI:CHEBI:58349; EC=1.21.1.1; Evidence={ECO:0000269|PubMed:27643701}; PhysiologicalDirection=rig... | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=14 uM for 3-iodo-L-tyrosine (at pH 7.4 and 25 degrees Celsius) {ECO:0000269|PubMed:27643701}; KM=8 uM for 3-bromo-L-tyrosine (at pH 7.4 and 25 degrees Celsius) {ECO:0000269|PubMed:27643701}; KM=21 uM for 3-chloro-L-tyrosine (at pH 7.4 and 25 degrees Celsius) {ECO:0... | null | null | null | FUNCTION: Catalyzes the dehalogenation of halotyrosines such as 3-bromo-L-tyrosine, 3-chloro-L-tyrosine, 3-iodo-L-tyrosine and 3,5-diiodo-L-tyrosine (PubMed:27643701). Activity towards 3-fluoro-L-tyrosine is weak (PubMed:27643701). Important for male and female fertility (PubMed:29764939). May be involved in maintainin... | Drosophila melanogaster (Fruit fly) |
E1JIT7 | PSD_DROME | MSEELKVVLRRSEQHSGFGFSLLGTTGPPHVIYDIVENSPAADCGAVEAGDVILKVNGTDVHRYTTKEVLKCLRLSEQLVTLELKRDPKLKARIKEQLANTQSPHYVDIESPNIYDYHSSSTNSSPNHRPNAGGKGAATTPSQTGLRYKSPTHLPSLRQNSSPLLASGSTTTTTTATHTHSHSRNSSASSTKIKVVETSITTSTTNVVGLTSPTGSVGGGVGGEATSPTFRPSRIPQALTKCAVPKPVPVLHSPQNKRPRPSQIPTKAANGNGNGHTAHLPPQSLQHSNSYSGSPVTRQRFADREPEREPEPNSAPPQPA... | null | null | axoneme assembly [GO:0035082]; compound eye morphogenesis [GO:0001745]; negative regulation of microtubule polymerization [GO:0031115]; positive regulation of ARF protein signal transduction [GO:0032014]; response to alcohol [GO:0097305] | axon [GO:0030424]; cell body [GO:0044297]; cell cortex [GO:0005938]; Golgi membrane [GO:0000139]; plasma membrane [GO:0005886] | guanyl-nucleotide exchange factor activity [GO:0005085]; microtubule binding [GO:0008017]; phospholipid binding [GO:0005543] | PF17820;PF15410;PF01369; | 2.30.42.10;1.10.1000.11;2.30.29.30; | PSD family | null | SUBCELLULAR LOCATION: Cell projection, axon {ECO:0000269|PubMed:31718774}. Cytoplasm {ECO:0000269|PubMed:31718774}. Cell membrane {ECO:0000269|PubMed:31718774}; Peripheral membrane protein {ECO:0000269|PubMed:31718774}. Cytoplasm, cell cortex {ECO:0000269|PubMed:31718774}. | null | null | null | null | null | FUNCTION: Guanine nucleotide exchange factor for Arf6 (PubMed:28607459). Regulates axon growth and branching by inhibiting microtubule polymerisation at the cortex (PubMed:31718774). Together with shot, promotes axonal microtubule bundle integrity (PubMed:31718774). Required for normal ethanol-induced tolerance and pre... | Drosophila melanogaster (Fruit fly) |
E1U8D0 | MTCL2_MOUSE | METPAGESSARGYGPPPAPAPAAERKKSHRAPSPARPKDVAGWSLAKGRRGTGPGSATACGTASSARPDKKGRAVAPGTRGTGPRVAGVRTGVRAKGRPRPGTGPRPPPPPPSLTDSSSEVSDCASEEARQLGLELALSSDAESAAGGPAGTRTGQPPQPAQSGQQPPRPPASPDEPSVAASSVGSSRLPLSASLAFSDLTEEMLDCGPGGLVRELEELRSENDYLKDEIEELRAEMLEMRDVYMEEDVYQLQELRQQLDQASKTCRILQYRLRKAERRSLRAAQTGQVDGELIRGLEQDVKVSKDISMRLHKELEVVEK... | null | null | cell division [GO:0051301]; chromosome segregation [GO:0007059]; insulin receptor signaling pathway [GO:0008286]; negative regulation of gluconeogenesis [GO:0045721]; regulation of autophagy [GO:0010506] | extracellular space [GO:0005615]; Golgi membrane [GO:0000139]; microtubule [GO:0005874]; midbody [GO:0030496] | null | PF14818;PF11365; | null | MTCL family | PTM: Proteolytically cleaved into a C-terminal SOGA 25 kDa form that is detected in plasma (By similarity). Proteolytically cleaved in primary hepatocytes into a C-terminal SOGA 80 kDa form. {ECO:0000250|UniProtKB:O94964, ECO:0000269|PubMed:20813965}.; PTM: Phosphorylated during mitosis in a CDK1-dependent manner. {ECO... | SUBCELLULAR LOCATION: [C-terminal 80 kDa form]: Secreted {ECO:0000269|PubMed:20813965}. Note=Secreted in primary hepatocyte-conditioned media. {ECO:0000269|PubMed:20813965}.; SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton {ECO:0000269|PubMed:28550165, ECO:0000269|PubMed:35543016}. Golgi apparatus membrane {ECO:0000269|P... | null | null | null | null | null | FUNCTION: Microtubule-associated factor that enables integration of the centrosomal and Golgi-associated microtubules on the Golgi membrane, supporting directional migration. Preferentially acts on the perinuclear microtubules accumulated around the Golgi. Associates with the Golgi membrane through the N-terminal coile... | Mus musculus (Mouse) |
E1WAC8 | SCTB1_SALTS | MLISNVGINPAAYLNNHSVENSSQTASQSVSAKDILNSIGISSSKVSDLGLSPTLSAPAPGVLTQTPGTITSFLKASIQNTDMNQDLNALANNVTTKANEVVQTQLREQQAEVGKFFDISGMSSSAVALLAAANTLMLTLNQADSKLSGKLSLVSFDAAKTTASSMMREGMNALSGSISQSALQLGITGVGAKLEYKGLQNERGALKHNAAKIDKLTTESHSIKNVLNGQNSVKLGAEGVDSLKSLNMKKTGTDATKNLNDATLKSNAGTSATESLGIKDSNKQISPEHQAILSKRLESVESDIRLEQNTMDMTRIDARK... | null | null | actin filament organization [GO:0007015]; protein localization to Golgi apparatus [GO:0034067]; regulation of entry of bacterium into host cell [GO:2000535]; regulation of protein localization [GO:0032880] | extracellular region [GO:0005576]; host cell membrane [GO:0033644]; membrane [GO:0016020]; phagocytic vesicle [GO:0045335] | identical protein binding [GO:0042802]; syntaxin binding [GO:0019905] | PF09599; | null | SctB/SipC family | null | SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:7608068}. Host membrane {ECO:0000250|UniProtKB:P0CL47}; Single-pass membrane protein {ECO:0000255}. Note=Secreted via the type III secretion system 1 (SPI-1 T3SS). {ECO:0000269|PubMed:7608068}. | null | null | null | null | null | FUNCTION: Component of the type III secretion system 1 (SPI-1 T3SS), also called injectisome, which is used to inject bacterial effector proteins into eukaryotic host cells (By similarity). SipB/SctE1 and SipC/SctB1 are inserted into the host membrane where they form a pore and allow the translocation of effector prote... | Salmonella typhimurium (strain SL1344) |
E1WKT5 | SOTC_BACF6 | MKKFTCVQDIGDLKSALAESFEIKKDRFKYVELGRNKTLLMIFFNSSLRTRLSTQKAALNLGMNVIVLDINQGAWKLETERGVIMDGDKPEHLLEAIPVMGCYCDIIGVRSFARFENREYDYNEVIINQFIQHSGRPVFSMEAATRHPLQSFADLITIEEYKKTARPKVVMTWAPHPRPLPQAVPNSFAEWMNATDYEFVITHPEGYELDPKFVGNARVEYDQMKAFEGADFIYAKNWAAYTGDNYGQILSTDRNWTVGDRQMAVTNNAYFMHCLPVRRNMIVTDDVIESPQSIVIPEAANREISATVVLKRLLENLP | 2.1.3.11 | null | arginine biosynthetic process via ornithine [GO:0042450]; citrulline biosynthetic process [GO:0019240] | null | amino acid binding [GO:0016597]; ornithine carbamoyltransferase activity [GO:0004585] | PF00185;PF02729; | 3.40.50.1370; | Aspartate/ornithine carbamoyltransferase superfamily, SOTCase family | null | null | CATALYTIC ACTIVITY: Reaction=carbamoyl phosphate + N(2)-succinyl-L-ornithine = H(+) + N(2)-succinyl-L-citrulline + phosphate; Xref=Rhea:RHEA:25884, ChEBI:CHEBI:15378, ChEBI:CHEBI:43474, ChEBI:CHEBI:58228, ChEBI:CHEBI:58514, ChEBI:CHEBI:58862; EC=2.1.3.11; Evidence={ECO:0000269|PubMed:16704984}; PhysiologicalDirection=l... | null | PATHWAY: Amino-acid biosynthesis; L-arginine biosynthesis. {ECO:0000269|PubMed:12095263, ECO:0000269|PubMed:16704984}. | null | null | FUNCTION: Catalyzes the transfer of the carbamoyl group from carbamoyl phosphate to the delta-amino group of N(2)-succinyl-L-ornithine to produce N(2)-succinyl-L-citrulline (PubMed:16704984). Is essential for arginine biosynthesis (PubMed:12095263, PubMed:16704984). Has no activity with either L-ornithine or L-aspartat... | Bacteroides fragilis (strain 638R) |
E1XUJ2 | LDI_CASD6 | MRFTLKTTAIVSAAALLAGFGPPPRAAELPPGRLATTEDYFAQQAKQAVTPDVMAQLAYMNYIDFISPFYSRGCSFEAWELKHTPQRVIKYSIAFYAYGLASVALIDPKLRALAGHDLDIAVSKMKCKRVWGDWEEDGFGTDPIEKENIMYKGHLNLMYGLYQLVTGSRRYEAEHAHLTRIIHDEIAANPFAGIVCEPDNYFVQCNSVAYLSLWVYDRLHGTDYRAATRAWLDFIQKDLIDPERGAFYLSYHPESGAVKPWISAYTTAWTLAMVHGMDPAFSERYYPRFKQTFVEVYDEGRKARVRETAGTDDADGGVGL... | 4.2.1.127; 5.4.4.4 | null | cellular response to organic substance [GO:0071310]; monoterpene catabolic process [GO:0043694]; monoterpenoid metabolic process [GO:0016098]; protein tetramerization [GO:0051262] | periplasmic space [GO:0042597] | hydro-lyase activity [GO:0016836]; intramolecular hydroxytransferase activity [GO:0050486] | PF18566; | null | null | null | SUBCELLULAR LOCATION: Periplasm {ECO:0000305|PubMed:20663876}. | CATALYTIC ACTIVITY: Reaction=(S)-linalool = beta-myrcene + H2O; Xref=Rhea:RHEA:30711, ChEBI:CHEBI:98, ChEBI:CHEBI:15377, ChEBI:CHEBI:17221; EC=4.2.1.127; Evidence={ECO:0000269|PubMed:20663876, ECO:0000269|PubMed:21950166, ECO:0000269|PubMed:27062179, ECO:0000269|PubMed:28068311, ECO:0000269|Ref.8}; CATALYTIC ACTIVITY: ... | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=750 uM for linalool {ECO:0000269|PubMed:20663876}; KM=800 uM for linalool (for linalool dehydration) {ECO:0000269|Ref.8}; KM=500 uM for geraniol {ECO:0000269|PubMed:20663876, ECO:0000269|Ref.8}; KM=200 uM for beta-myrcene {ECO:0000269|Ref.8}; Vmax=140 nmol/sec/mg e... | PATHWAY: Terpene metabolism; monoterpene degradation. {ECO:0000269|PubMed:20663876, ECO:0000269|PubMed:22286981}. | BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 9.0 for the linalool dehydratase activity. {ECO:0000269|PubMed:20663876}; | BIOPHYSICOCHEMICAL PROPERTIES: Temperature dependence: Optimum temperature is 35 degrees Celsius for the linalool dehydratase activity. {ECO:0000269|PubMed:20663876}; | FUNCTION: Anaerobically catalyzes the stereospecific hydration of beta-myrcene to (3S)-linalool and the isomerization of (3S)-linalool to geraniol (PubMed:20663876, PubMed:28068311, Ref.8). Is thus involved in the initial steps of the anaerobic degradation of the monoterpene beta-myrcene (PubMed:20663876). Also catalyz... | Castellaniella defragrans (strain DSM 12143 / CCUG 39792 / 65Phen) (Alcaligenes defragrans) |
E2AXC7 | BRCC3_CAMFO | MDDSSLQKVELQTDVYMVCLQHALSTENFEVMGLLIGNFACGIAKISAVIILRRLDKKKDRVEISSEQLLKAAAEAERLTVELNRPMRVLGWYHSHPHITVCPSHVDVRTQATYQTMDHSFVGLIFSVFSEGKESKEHEIFLNCFQSDNGEATEIPLEIVHTPDISDRCLRTMTDLSKILVQEEEDMAEACKDHPDVLASIHNNAVRTRALIHITDIITKPLVQTFEKRIALNKLRATHLQRQLQELQKMCNG | 3.4.19.- | COFACTOR: Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000269|PubMed:26344097}; Note=Binds 1 zinc ion per subunit. {ECO:0000269|PubMed:26344097}; | cell cycle [GO:0007049]; cell division [GO:0051301]; double-strand break repair [GO:0006302]; positive regulation of NLRP3 inflammasome complex assembly [GO:1900227]; proteolysis [GO:0006508] | BRCA1-A complex [GO:0070531]; BRISC complex [GO:0070552]; cytoplasm [GO:0005737]; spindle pole [GO:0000922] | cysteine-type deubiquitinase activity [GO:0004843]; metal ion binding [GO:0046872]; metal-dependent deubiquitinase activity [GO:0140492]; polyubiquitin modification-dependent protein binding [GO:0031593] | PF18110;PF01398; | 3.40.140.10; | Peptidase M67A family, BRCC36 subfamily | null | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:P46736}. Nucleus {ECO:0000250|UniProtKB:P46736}. Cytoplasm, cytoskeleton, spindle pole {ECO:0000250|UniProtKB:Q15018}. Cytoplasm, cytoskeleton {ECO:0000250|UniProtKB:Q15018}. Note=A minor proportion is detected in the nucleus. Translocates into the nucleus in respo... | null | null | null | null | null | FUNCTION: Metalloprotease that specifically cleaves 'Lys-63'-linked polyubiquitin chains, leaving the last ubiquitin chain attached to its substrates. Catalytic subunit of the BRISC complex; does not have activity by itself, but needs to be associated into a heterotetramer with ABRAXAS2 for minimal in vitro activity (P... | Camponotus floridanus (Florida carpenter ant) |
E2BJ30 | ORCO_HARSA | MMKMKQQGLVADLLPNIRVMKFFGHFVFNYYDDNSSKYLHKIFCCVNLFLLLLQFALCAVNLIIESADVDDLTANTITLLFFTHSIVKIIYFAVRSKYFYRTWAIWNNPNSHPLFAESNARYHAIALKKMRLLLFLVGATTVLSAIAWTVLTFFEHPIRKLVDPVTNETTIIELPQLLLRSYYPFDASKGIMHVIVLIYQFYWVLFMLIDANSLDVLFCSWLLFACEQLQHLKQIMKPLMELSATLDTVVPNSSELFKAGSAEHLRESENQPPPPVPPQGDSMLDLDLRNIYSNRQDFTATFRPTAGMTFNGGVGPNGLT... | null | null | antennal development [GO:0007469]; detection of chemical stimulus involved in sensory perception of smell [GO:0050911]; detection of pheromone [GO:0043695]; mating behavior [GO:0007617]; olfactory behavior [GO:0042048]; response to pheromone [GO:0019236]; signal transduction [GO:0007165]; social behavior [GO:0035176] | plasma membrane [GO:0005886] | odorant binding [GO:0005549]; olfactory receptor activity [GO:0004984] | PF02949; | null | Insect chemoreceptor superfamily, Heteromeric odorant receptor channel (TC 1.A.69) family, Orco subfamily | null | SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000255}. | null | null | null | null | null | FUNCTION: Odorant coreceptor which complexes with conventional odorant receptors (ORs) to form odorant-sensing units, providing sensitive and prolonged odorant signaling and calcium permeability (By similarity). Obligate coreceptor of all odorant receptors (By similarity). Orco is a universal and integral part of the f... | Harpegnathos saltator (Jerdon's jumping ant) |
E2DWQ7 | A3AKI_PHYIN | MRLAIMLSATAVAINFATCSAIDQTKVLVYGTPAHYIHDSAGRRLLRKNEENEETSEERAPNFNLANLNEEMFNVAALTKRADAKKLAKQLMGNDKLADAAYIWWQHNRVTLDQIDTFLKLASRKTQGAKYNQIYNSYMMHLGLTGY | null | null | null | extracellular region [GO:0005576]; host cell endosome [GO:0044174] | null | PF16810; | 1.10.10.2460; | RxLR effector family | PTM: Proteolytically cleaved. The cleavage site directly after the RxLR sequence and the high conservation among other effector proteins suggest that the RxLR motif might play a crucial role in the intracellular processing before secretion. {ECO:0000269|PubMed:28522546}.; PTM: glycosylated. {ECO:0000269|PubMed:28522546... | SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:15894622, ECO:0000269|PubMed:16965554, ECO:0000269|PubMed:17914356, ECO:0000269|PubMed:29312401}. Host cytoplasm {ECO:0000269|PubMed:15894622, ECO:0000269|PubMed:16965554, ECO:0000269|PubMed:17914356, ECO:0000269|PubMed:29312401}. Host endosome {ECO:0000269|PubMed:2324... | null | null | null | null | null | FUNCTION: Multifunctional effector that can suppress host BAK1/SERK3-mediated immunity through at least two different pathways (PubMed:19794118, PubMed:20457921, PubMed:21348873, PubMed:26348328). Manipulates plant immunity by targeting and stabilizing host E3 ligase CMPG1. Preventing the normal 26S proteasome-dependen... | Phytophthora infestans (Potato late blight agent) (Botrytis infestans) |
E2E2N7 | BCGS_ORIVU | MEIYSPVVPAVKDVKRLDEIRKSAKFHPSIWGDFFLSYNSDNTQISEAEEEEVAKQKEAVRELLAQVPEGSTYKMELIDLIQRLGVNYHFEKEIHDSLNYIHENSQHNDDEVRTTALRFRLLRQQGYRVPCDVFRKFTDGEGNFATALTNDVEGLLELYEASHLATRGEEILDRAMEFSSSHLQALLNQHLVGSVSLSKRVDEALKMPIRKTLTRLGARKFISLYQEDESRNELLLNFAKLDFNMVQKMHQRELSDATRWWKKLEVAKRMPYARDRVVECFFWIVGVYFEPCYATARRILSKAINMASIVDDTYEYATLD... | 3.1.7.11; 4.2.3.-; 4.2.3.100; 4.2.3.113; 4.2.3.20 | COFACTOR: Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000269|PubMed:20419468}; Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000269|PubMed:20419468}; Note=Binds 3 Mg(2+) or Mn(2+) ions per subunit. {ECO:0000250|UniProtKB:E2E2P0}; | diterpenoid biosynthetic process [GO:0016102] | null | (R)-limonene synthase activity [GO:0034002]; hydrolase activity [GO:0016787]; magnesium ion binding [GO:0000287]; protein homodimerization activity [GO:0042803]; sesquiterpene synthase activity [GO:0010334] | PF01397;PF03936; | 1.10.600.10;1.50.10.130; | Terpene synthase family | null | null | CATALYTIC ACTIVITY: Reaction=(2E,6E)-farnesyl diphosphate = bicyclogermacrene + diphosphate; Xref=Rhea:RHEA:31999, ChEBI:CHEBI:33019, ChEBI:CHEBI:63709, ChEBI:CHEBI:175763; EC=4.2.3.100; Evidence={ECO:0000269|PubMed:20419468}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:32000; Evidence={ECO:0000269|PubMed:2041... | null | PATHWAY: Secondary metabolite biosynthesis; terpenoid biosynthesis. {ECO:0000269|PubMed:20419468, ECO:0000269|Ref.2}. | null | null | FUNCTION: Involved in the biosynthesis of phenolic sesquiterpenes natural products (Ref.2). Sesquiterpene synthase converting (2E,6E)-farnesyl diphosphate (FPP) to alloaromadendrene and bicyclo-germacrene. The product formation is dependent on the metal ions present and in presence of manganese, bicyclo-germacrene is g... | Origanum vulgare (Wild marjoram) |
E2E2P0 | GTPS_ORIVU | MATLSMQVSILSKEVKNVNNIGMRASKPMVARRVSTTRLRPICSASLQVEEETRRSGNYQASIWNNDYVQSFNTNQYKDEKHLKKKEELIAQVKILLNTKMEAVKQLELIEDLRNLGLTYYFQDEVKKILTSIYNDHKCFKNEQVGDLYFTSLGFRLLRLHGFDVSEEVFDFFKNEDGSDFKASLGENIKDVLQLYEASFLIREGEVILEQARVFSTKHLEKKVDEGINDEKLLAWIRHSLALPLHWRIQRLEARWFLDAYRARKDMIPLIFELGKIDFHIIQETQLEELQEVSKWWTNSNLAEKLPFVRDRIVECYFWA... | 4.2.3.114; 4.2.3.115 | COFACTOR: Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000269|PubMed:20419468, ECO:0000269|Ref.2}; Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000269|PubMed:20419468, ECO:0000269|Ref.2}; Note=Manganese > magnesium. {ECO:0000269|PubMed:20419468, ECO:0000269|Ref.2}; | defense response to insect [GO:0002213]; diterpenoid biosynthetic process [GO:0016102]; geranyl diphosphate metabolic process [GO:0033383]; response to insect [GO:0009625]; response to water deprivation [GO:0009414] | chloroplast [GO:0009507] | gamma-terpinene synthase activity [GO:0102903]; magnesium ion binding [GO:0000287]; protein homodimerization activity [GO:0042803]; terpene synthase activity [GO:0010333] | PF01397;PF03936; | 1.10.600.10;1.50.10.130; | Terpene synthase family | null | SUBCELLULAR LOCATION: Plastid, chloroplast {ECO:0000305}. | CATALYTIC ACTIVITY: Reaction=(2E)-geranyl diphosphate = diphosphate + gamma-terpinene; Xref=Rhea:RHEA:32559, ChEBI:CHEBI:10577, ChEBI:CHEBI:33019, ChEBI:CHEBI:58057; EC=4.2.3.114; Evidence={ECO:0000269|PubMed:20419468, ECO:0000269|Ref.2}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:32560; Evidence={ECO:0000269... | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=8.71 uM for geranyl diphosphate (in the presence of 0.5 mM manganese) {ECO:0000269|PubMed:20419468, ECO:0000269|Ref.2}; KM=0.7 mM for manganese (in the presence of 10 uM geranyl diphosphate) {ECO:0000269|PubMed:20419468, ECO:0000269|Ref.2}; KM=3.41 mM for magnesium... | PATHWAY: Secondary metabolite biosynthesis; terpenoid biosynthesis. {ECO:0000269|PubMed:20419468, ECO:0000269|Ref.2}. | BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 6.8. {ECO:0000269|PubMed:20419468, ECO:0000269|Ref.2}; | BIOPHYSICOCHEMICAL PROPERTIES: Temperature dependence: Optimum temperature is 28 degrees Celsius. {ECO:0000269|PubMed:20419468, ECO:0000269|Ref.2}; | FUNCTION: Involved in the biosynthesis of phenolic monoterpenes natural products thymol and carvacrol which have a broad range of biological activities acting as antimicrobial compounds, insecticides, antioxidants and pharmaceutical agents (PubMed:20419468, PubMed:26156773, PubMed:30231481, Ref.2). Monoterpene synthase... | Origanum vulgare (Wild marjoram) |
E2JF22 | PIEZ1_MOUSE | MEPHVLGAGLYWLLLPCTLLAASLLRFNALSLVYLLFLLLLPWLPGPSRHSIPGHTGRLLRALLCLSLLFLVAHLAFQICLHTVPHLDQFLGQNGSLWVKVSQHIGVTRLDLKDIFNTTRLVAPDLGVLLASSLCLGLCGRLTRKAGQSRRTQELQDDDDDDDDDDEDIDAAPAVGLKGAPALATKRRLWLASRFRVTAHWLLMTSGRTLVIVLLALAGIAHPSAFSSIYLVVFLAICTWWSCHFPLSPLGFNTLCVMVSCFGAGHLICLYCYQTPFIQDMLPPGNIWARLFGLKNFVDLPNYSSPNALVLNTKHAWPIY... | null | null | cellular response to mechanical stimulus [GO:0071260]; detection of mechanical stimulus [GO:0050982]; monoatomic cation transport [GO:0006812]; positive regulation of cell-cell adhesion mediated by integrin [GO:0033634]; positive regulation of integrin activation [GO:0033625]; positive regulation of myotube differentia... | endoplasmic reticulum [GO:0005783]; endoplasmic reticulum membrane [GO:0005789]; endoplasmic reticulum-Golgi intermediate compartment membrane [GO:0033116]; lamellipodium membrane [GO:0031258]; plasma membrane [GO:0005886] | identical protein binding [GO:0042802]; mechanosensitive monoatomic cation channel activity [GO:0140135]; mechanosensitive monoatomic ion channel activity [GO:0008381]; monoatomic cation channel activity [GO:0005261] | PF15917;PF12166; | null | PIEZO (TC 1.A.75) family | null | SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000250|UniProtKB:Q92508}; Multi-pass membrane protein {ECO:0000269|PubMed:29261642, ECO:0007744|PDB:6BPZ}. Endoplasmic reticulum-Golgi intermediate compartment membrane {ECO:0000250|UniProtKB:Q0KL00}. Cell membrane {ECO:0000269|PubMed:20813920, ECO:0000269|PubM... | CATALYTIC ACTIVITY: Reaction=K(+)(in) = K(+)(out); Xref=Rhea:RHEA:29463, ChEBI:CHEBI:29103; Evidence={ECO:0000269|PubMed:20813920}; CATALYTIC ACTIVITY: Reaction=Na(+)(in) = Na(+)(out); Xref=Rhea:RHEA:34963, ChEBI:CHEBI:29101; Evidence={ECO:0000269|PubMed:20813920}; CATALYTIC ACTIVITY: Reaction=Ca(2+)(in) = Ca(2+)(out);... | null | null | null | null | FUNCTION: Pore-forming subunit of a mechanosensitive non-specific cation channel. Generates currents characterized by a linear current-voltage relationship that are sensitive to ruthenium red and gadolinium (PubMed:20813920, PubMed:22343900). Conductance to monovalent alkali ions is highest for K(+), intermediate for N... | Mus musculus (Mouse) |
E2QWQ2 | NLK_CANLF | MSLCGARANAKMMAAYNGGTSAAAAGHHHHHHHHLPHLPPPHLHHHHHPQHHLHPGSAAAVHPVQQHTSSAAAAAAAAAAAAAMLNPGQQQPYFPSPAPGQAPGPAAAAPAQVQAAAAATVKAHHHQHSHHPQQQLDIEPDRPIGYGAFGVVWSVTDPRDGKRVALKKMPNVFQNLVSCKRVFRELKMLCFFKHDNVLSALDILQPPHIDYFEEIYVVTELMQSDLHKIIVSPQPLSSDHVKVFLYQILRGLKYLHSAGILHRDIKPGNLLVNSNCVLKICDFGLARVEELDESRHMTQEVVTQYYRAPEILMGSRHYSN... | 2.7.11.24 | COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250|UniProtKB:O54949}; | cellular response to osmotic stress [GO:0071470]; intracellular signal transduction [GO:0035556]; negative regulation of TORC1 signaling [GO:1904262]; negative regulation of Wnt signaling pathway [GO:0030178]; phosphorylation [GO:0016310]; protein stabilization [GO:0050821]; regulation of DNA-templated transcription [G... | cytoplasm [GO:0005737]; nucleus [GO:0005634] | ATP binding [GO:0005524]; DNA-binding transcription factor binding [GO:0140297]; magnesium ion binding [GO:0000287]; MAP kinase activity [GO:0004707]; protein serine kinase activity [GO:0106310]; protein serine/threonine kinase activity [GO:0004674]; SH2 domain binding [GO:0042169]; ubiquitin protein ligase binding [GO... | PF00069; | 1.10.510.10; | Protein kinase superfamily, CMGC Ser/Thr protein kinase family, MAP kinase subfamily | PTM: Phosphorylated on Thr-298. Intermolecular autophosphorylation on Thr-298 activates the enzyme. {ECO:0000250|UniProtKB:O54949}. | SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:O54949}. Cytoplasm {ECO:0000250|UniProtKB:O54949}. Note=Predominantly nuclear. A smaller fraction is cytoplasmic. {ECO:0000250|UniProtKB:O54949}. | 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:0000250|UniProtKB:O54949}; CATALYT... | null | null | null | null | FUNCTION: Serine/threonine-protein kinase that regulates a number of transcription factors with key roles in cell fate determination. Positive effector of the non-canonical Wnt signaling pathway, acting downstream of WNT5A, MAP3K7/TAK1 and HIPK2. Negative regulator of the canonical Wnt/beta-catenin signaling pathway. B... | Canis lupus familiaris (Dog) (Canis familiaris) |
E2QY99 | PALS1_CANLF | MTTSHMNGHVTEESDNEVKNVDLASPEEHQKHREMAVDCPGDLGTRMMPVRRSAQLERIRQQQEDMRRRREEEGKKQELDLNSSMRLKKLAQIPPKTGIDNPIFDTEEGIVLESPHYAVKILEVEDLFSSLKHIQHTLVDSQSQEDISLLLQLVQNKDFQNAFKIHNAVTVHMNKASPPFPLISNAQDLAQEVQTVLKPVHHKEGQELTALLSAPHVQALLLAHDKVAEQEMQLEPFTDERVYESIGQYGGETVKIVRIEKARDIPLGATVRNEMDSVIISRIVKGGAAEKSGLLHEGDEVLEINGIEIRGKDVNEVFDL... | null | null | central nervous system neuron development [GO:0021954]; cerebral cortex development [GO:0021987]; establishment or maintenance of epithelial cell apical/basal polarity [GO:0045197]; establishment or maintenance of polarity of embryonic epithelium [GO:0016332]; generation of neurons [GO:0048699]; morphogenesis of an epi... | adherens junction [GO:0005912]; apical plasma membrane [GO:0016324]; axon [GO:0030424]; bicellular tight junction [GO:0005923]; Golgi apparatus [GO:0005794]; perikaryon [GO:0043204]; plasma membrane [GO:0005886] | ATP binding [GO:0005524] | PF00625;PF02828;PF09060;PF00595;PF07653; | 2.30.42.10;1.10.287.650;3.40.50.300;2.30.30.40; | MAGUK family | null | SUBCELLULAR LOCATION: Golgi apparatus {ECO:0000250|UniProtKB:Q8N3R9}. Cell membrane {ECO:0000250|UniProtKB:Q9JLB2}; Peripheral membrane protein {ECO:0000250|UniProtKB:Q9JLB2}. Endomembrane system {ECO:0000250|UniProtKB:Q9JLB2}; Peripheral membrane protein {ECO:0000250|UniProtKB:Q9JLB2}. Cell junction, tight junction {E... | null | null | null | null | null | FUNCTION: Plays a role in tight junction biogenesis and in the establishment of cell polarity in epithelial cells (PubMed:17182851). Also involved in adherens junction biogenesis by ensuring correct localization of the exocyst complex protein EXOC4/SEC8 which allows trafficking of adherens junction structural component... | Canis lupus familiaris (Dog) (Canis familiaris) |
E2QYC9 | INADL_CANLF | MPENPAPDKLQVLQVLDRLKMKLQEKGDTSQNEKLSLFYETLQSPLFNQILTLQQSIKQLKGQLSHIPSDCSTNFDFSRKGLLVFTDSAITNGNAQRPSNNLTVSGLFPWTPKSGNEDFNSVIQQMAQGRQIEYIDIERPSTGGLGFSVVALRSQNLGEVDIFVKEVQPGSIADRDQRLRENDQILAINHTPLDQNISHQQAIALLQQTTGSLHLVVAREPVHTKSRTSINLTDTTMPETVHWGHIEDVELINDGSGLGFGIVGGKSSGVVVRTIVPGGLADRDGRLQTGDHILKIGDTDVQGMTSEQVAQVLRNCGNSV... | null | null | establishment of apical/basal cell polarity [GO:0035089]; microtubule organizing center organization [GO:0031023]; positive regulation of epithelial cell migration [GO:0010634]; regulation of microtubule cytoskeleton organization [GO:0070507]; regulation of protein localization [GO:0032880]; tight junction assembly [GO... | apical part of cell [GO:0045177]; apical plasma membrane [GO:0016324]; bicellular tight junction [GO:0005923]; cytoplasm [GO:0005737]; perinuclear region of cytoplasm [GO:0048471]; plasma membrane [GO:0005886]; tight junction [GO:0070160] | null | PF09045;PF00595; | 1.20.1440.360;2.30.42.10; | null | null | SUBCELLULAR LOCATION: Cell junction, tight junction {ECO:0000269|PubMed:12527193, ECO:0000269|PubMed:12771187, ECO:0000269|PubMed:15738264}. Apical cell membrane {ECO:0000269|PubMed:15738264}; Peripheral membrane protein {ECO:0000250|UniProtKB:Q8NI35}. Cytoplasm, perinuclear region {ECO:0000250|UniProtKB:Q63ZW7}. Note=... | null | null | null | null | null | FUNCTION: Scaffolding protein that facilitates the localization of proteins to the cell membrane (PubMed:17235357). Required for the correct formation of tight junctions and epithelial apico-basal polarity (PubMed:15738264). Positively regulates epithelial cell microtubule elongation and cell migration, possibly via fa... | Canis lupus familiaris (Dog) (Canis familiaris) |
E2RAK7 | APOA2_CANLF | MKLLAVTVLLLVICSLEGAFVRRQAEEPNLQSLVSQYFQTVTDYGKDLMEKAKGPELQAQAKAYFEKTQEQLTPLVKKAGTDLLNFLSNFMDLKTQPATQ | null | null | cholesterol homeostasis [GO:0042632]; cholesterol metabolic process [GO:0008203]; cholesterol transport [GO:0030301]; high-density lipoprotein particle assembly [GO:0034380]; high-density lipoprotein particle remodeling [GO:0034375]; lipoprotein metabolic process [GO:0042157]; low-density lipoprotein particle remodelin... | blood microparticle [GO:0072562]; chylomicron [GO:0042627]; spherical high-density lipoprotein particle [GO:0034366]; very-low-density lipoprotein particle [GO:0034361] | apolipoprotein receptor binding [GO:0034190]; cholesterol binding [GO:0015485]; cholesterol transfer activity [GO:0120020]; high-density lipoprotein particle binding [GO:0008035]; high-density lipoprotein particle receptor binding [GO:0070653]; lipase inhibitor activity [GO:0055102]; phosphatidylcholine binding [GO:003... | PF04711; | 6.10.250.100; | Apolipoprotein A2 family | null | SUBCELLULAR LOCATION: Secreted {ECO:0000250|UniProtKB:P02652}. | null | null | null | null | null | FUNCTION: May stabilize HDL (high density lipoprotein) structure by its association with lipids, and affect the HDL metabolism. | Canis lupus familiaris (Dog) (Canis familiaris) |
E2RD63 | PLD6_CANLF | MERFRWQVAAVAAVGLALALEALPSVLCWLRAGRRQQQRPPRRQVLFFPSQVTCTEALLQAPGEAPSGPPAGCRCSLPHGESSLSRLLRALLAARASLELCLFAFSSPQLGRAVQLLHQRGVRVRVITDCDYMALNGSQIGLLRKAGIQVRHDQDLGYMHHKFAIVDKKVLITGSLNWTTQAIQNNRENVLIMEDEEYVRLFLEEFERIWEEFNPTKYTFFPQKKTGTSLPPQVSCFGQLVSCHSKCSHHLSQV | 3.1.4.- | null | lipid catabolic process [GO:0016042]; meiotic cell cycle [GO:0051321]; mitochondrial fusion [GO:0008053]; P granule organization [GO:0030719]; piRNA processing [GO:0034587]; spermatid development [GO:0007286] | Golgi apparatus [GO:0005794]; mitochondrial outer membrane [GO:0005741]; mitochondrion [GO:0005739]; nuclear membrane [GO:0031965]; plasma membrane [GO:0005886] | cardiolipin hydrolase activity [GO:0035755]; metal ion binding [GO:0046872]; protein homodimerization activity [GO:0042803]; RNA endonuclease activity, producing 5'-phosphomonoesters [GO:0016891] | PF13091; | 3.30.870.10; | Phospholipase D family, MitoPLD/Zucchini subfamily | null | SUBCELLULAR LOCATION: Mitochondrion outer membrane {ECO:0000250|UniProtKB:Q5SWZ9}; Single-pass membrane protein {ECO:0000250|UniProtKB:Q5SWZ9}. Nucleus membrane {ECO:0000250|UniProtKB:Q5SWZ9}. Cell membrane {ECO:0000250|UniProtKB:Q5SWZ9}. Golgi apparatus {ECO:0000250|UniProtKB:Q5SWZ9}. Note=Localization in the mitochon... | CATALYTIC ACTIVITY: Reaction=a cardiolipin + H2O = 1,2-diacyl-sn-glycero-3-phospho-(1'-sn-glycerol) + a 1,2-diacyl-sn-glycero-3-phosphate + H(+); Xref=Rhea:RHEA:44884, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:58608, ChEBI:CHEBI:62237, ChEBI:CHEBI:64716; Evidence={ECO:0000250|UniProtKB:Q8N2A8}; PhysiologicalDir... | null | null | null | null | FUNCTION: Presents phospholipase and nuclease activities, depending on the different physiological conditions. Interaction with Mitoguardin (MIGA1 or MIGA2) affects the dimer conformation, facilitating the lipase activity over the nuclease activity. Plays a key role in mitochondrial fusion and fission via its phospholi... | Canis lupus familiaris (Dog) (Canis familiaris) |
E2RDM9 | TSPO2_CANLF | MQPQGAIFVALPHLGPILVSLLTRHRMIRWYDIPKKPPWCPPHKVLLAGWITIYFVMGYASYLVWKDLGGGFGRPLALPLGLYAVQLAVSWAVLIFFFAAHAHGLALLHMLLLYGLVVSTALIWHPINKLAAVLLLPYLAWLTVTASIAYHLWRDSLCPNHHQPLPMGEKRD | null | null | 5-aminolevulinic acid import across plasma membrane [GO:0140484]; enucleate erythrocyte differentiation [GO:0043353]; import across plasma membrane [GO:0098739]; intracellular cholesterol transport [GO:0032367]; lipid droplet organization [GO:0034389] | endoplasmic reticulum [GO:0005783]; endoplasmic reticulum membrane [GO:0005789]; mitochondrial outer membrane [GO:0005741]; plasma membrane [GO:0005886] | 5-aminolevulinic acid transmembrane transporter activity [GO:0140485]; cholesterol binding [GO:0015485] | PF03073; | 1.20.1260.100; | TspO/BZRP family | null | SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000250|UniProtKB:Q5TGU0}; Multi-pass membrane protein {ECO:0000255}. Cell membrane {ECO:0000269|PubMed:32358067}; Multi-pass membrane protein {ECO:0000255}. Note=Localizes to the plasma membrane and intracellular membranes in developing and mature erythrocytes.... | null | null | null | null | null | FUNCTION: Cholesterol-binding protein involved in the redistribution of cholesterol from lipid droplets to the endoplasmic reticulum (PubMed:32358067). Required to meet cholesterol demands during erythropoietic differentiation (PubMed:32358067). May play a role in transport processes at the plasma membrane of erythrocy... | Canis lupus familiaris (Dog) (Canis familiaris) |
E2RDP2 | ATG4D_CANLF | MNSVSPAAAQYRSGSPEDARRPEGRRPRGPRVPDPNGPRPSGASGPALGSPAAAPGEPDEVDKFKAKFLTAWNNVKYGWAVKSRTSFSKISSVHLCGRRYRFEGEGDIQRFQRDFVSRLWLTYRRDFPPLAGGCLTSDCGWGCMLRSGQMMLAQGLLLHFLPRDWTWAEGPGLGPSEPAGLASPNRYRGPARWMPPRWAQGTPELEQERRHRQIVSWFADHPQAPFGLHRLVELGQSSGKKAGDWYGPSLVAHILRKAVESCSEITRLVVYVSQDCTVYKADVARLVARPDPTAEWKSVVILVPVRLGGETLNPVYVPCV... | 3.4.22.- | null | aggrephagy [GO:0035973]; apoptotic process [GO:0006915]; autophagosome assembly [GO:0000045]; mitophagy [GO:0000423]; piecemeal microautophagy of the nucleus [GO:0034727]; protein processing [GO:0016485]; protein transport [GO:0015031] | cytoplasm [GO:0005737]; mitochondrial matrix [GO:0005759] | cysteine-type endopeptidase activity [GO:0004197]; protein-phosphatidylethanolamide deconjugating activity [GO:0019786] | PF03416; | null | Peptidase C54 family | PTM: Cleaved by CASP3 during apoptosis which leads to increased activity. The cleavage by CASP3 reveals a cryptic mitochondrial targeting sequence immediately downstream of their canonical caspase cleavage sites which leads to mitochondrial import of the protein. {ECO:0000250|UniProtKB:Q86TL0}. | SUBCELLULAR LOCATION: [Cysteine protease ATG4D]: Cytoplasm {ECO:0000250|UniProtKB:Q86TL0}.; SUBCELLULAR LOCATION: [Cysteine protease ATG4D, mitochondrial]: Cytoplasm {ECO:0000250|UniProtKB:Q86TL0}. Mitochondrion matrix {ECO:0000250|UniProtKB:Q86TL0}. Note=Imported into mitochondrial matrix after cleavage by CASP3 durin... | CATALYTIC ACTIVITY: Reaction=[protein]-C-terminal L-amino acid-glycyl-phosphatidylethanolamide + H2O = [protein]-C-terminal L-amino acid-glycine + a 1,2-diacyl-sn-glycero-3-phosphoethanolamine; Xref=Rhea:RHEA:67548, Rhea:RHEA-COMP:17323, Rhea:RHEA-COMP:17324, ChEBI:CHEBI:15377, ChEBI:CHEBI:64612, ChEBI:CHEBI:172940, Ch... | null | null | null | null | FUNCTION: [Cysteine protease ATG4D]: Cysteine protease that plays a key role in autophagy by mediating both proteolytic activation and delipidation of ATG8 family proteins. The protease activity is required for proteolytic activation of ATG8 family proteins: cleaves the C-terminal amino acid of ATG8 proteins MAP1LC3 an... | Canis lupus familiaris (Dog) (Canis familiaris) |
E2RE76 | APOA4_CANLF | MFLKAVVLTLSLVAITGARAEVSADQVATVVWDYFSQLSNNAKEAVEHLQQSELTQQLKSVTKGHISALRVIEKGRERNSWEHSRRVGPCEIMGRQVGIFGQPLRVATLPNCDLPVNSVPPNTHLSQAVGPYAEELRTQVNTHAEQLRNQLTSHAQRMQSALRQNVDDLHSSLTPFADELKAKIDQNVEELKGHLTPYTDELKVKIDQNVEELRRSLAPYAQDVQEKLNHQLEGLAFQMKKNAEELKAKISANAEELRQRLAPVAEDVRGKLKDNTAGLHKSLAELSSRLDQQVEEFRRNVGPYGETFNKALLQQVEELR... | null | null | acylglycerol homeostasis [GO:0055090]; cholesterol efflux [GO:0033344]; cholesterol homeostasis [GO:0042632]; cholesterol metabolic process [GO:0008203]; lipoprotein metabolic process [GO:0042157]; phosphatidylcholine metabolic process [GO:0046470]; phospholipid efflux [GO:0033700]; positive regulation of fatty acid bi... | blood microparticle [GO:0072562]; chylomicron [GO:0042627]; extracellular vesicle [GO:1903561]; high-density lipoprotein particle [GO:0034364]; low-density lipoprotein particle [GO:0034362]; very-low-density lipoprotein particle [GO:0034361] | cholesterol transfer activity [GO:0120020]; phosphatidylcholine binding [GO:0031210]; phosphatidylcholine-sterol O-acyltransferase activator activity [GO:0060228]; phospholipid binding [GO:0005543] | PF01442; | 6.10.250.2890;1.20.120.20; | Apolipoprotein A1/A4/E family | null | SUBCELLULAR LOCATION: Secreted {ECO:0000250|UniProtKB:P06727}. | null | null | null | null | null | FUNCTION: May have a role in chylomicrons and VLDL secretion and catabolism. Required for efficient activation of lipoprotein lipase by ApoC-II; potent activator of LCAT. Apoa-IV is a major component of HDL and chylomicrons. {ECO:0000250|UniProtKB:P06727}. | Canis lupus familiaris (Dog) (Canis familiaris) |
E2RG47 | STT3B_CANLF | MAEPSAPESKHKSSLNSSPWSGLMALGNSRHGHHGPGAQCAHKAAGGVAPPKPAPAGLSGGLSQPAGWQSLLSFTILFLAWLAGFSSRLFAVIRFESIIHEFDPWFNYRSTHHLASHGFYEFLNWFDERAWYPLGRIVGGTVYPGLMITAGLIHWILNTLNITVHIRDVCVFLAPTFSGLTSISTFLLTRELWNQGAGLLAACFIAIVPGYISRSVAGSFDNEGIAIFALQFTYYLWVKSVKTGSVFWTMCCCLSYFYMVSAWGGYVFIINLIPLHVFVLLLMQRYSKRVYIAYSTFYIVGLILSMQIPFVGFQPIRTSE... | 2.4.99.18 | COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250|UniProtKB:Q8TCJ2}; Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000250|UniProtKB:B9KDD4}; | post-translational protein modification [GO:0043687]; protein N-linked glycosylation via asparagine [GO:0018279] | oligosaccharyltransferase I complex [GO:0034998]; oligosaccharyltransferase II complex [GO:0034999] | dolichyl-diphosphooligosaccharide-protein glycotransferase activity [GO:0004579]; metal ion binding [GO:0046872] | PF02516;PF21436; | 3.40.50.12610; | STT3 family | null | SUBCELLULAR LOCATION: Endoplasmic reticulum {ECO:0000269|PubMed:12887896}. Endoplasmic reticulum membrane; Multi-pass membrane protein {ECO:0000250|UniProtKB:P39007}. | CATALYTIC ACTIVITY: Reaction=a dolichyl diphosphooligosaccharide + L-asparaginyl-[protein] = a dolichyl diphosphate + H(+) + N(4)-(oligosaccharide-(1->4)-N-acetyl-beta-D-glucosaminyl-(1->4)-N-acetyl-beta-D-glucosaminyl)-L-asparaginy-[protein]; Xref=Rhea:RHEA:22980, Rhea:RHEA-COMP:9529, Rhea:RHEA-COMP:12635, Rhea:RHEA-C... | null | PATHWAY: Protein modification; protein glycosylation. {ECO:0000250|UniProtKB:Q8TCJ2}. | null | null | FUNCTION: Catalytic subunit of the oligosaccharyl transferase (OST) complex that catalyzes the initial transfer of a defined glycan (Glc(3)Man(9)GlcNAc(2) in eukaryotes) from the lipid carrier dolichol-pyrophosphate to an asparagine residue within an Asn-X-Ser/Thr consensus motif in nascent polypeptide chains, the firs... | Canis lupus familiaris (Dog) (Canis familiaris) |
E2RH47 | RS3_CANLF | MAVQISKKRKFVADGIFKAELNEFLTRELAEDGYSGVEVRVTPTRTEIIILATRTQNVLGEKGRRIRELTAVVQKRFGFPEGSVELYAEKVATRGLCAIAQAESLRYKLLGGLAVRRACYGVLRFIMESGAKGCEVVVSGKLRGQRAKSMKFVDGLMIHSGDPVNYYVDTAVRHVLLRQGVLGIKVKIMLPWDPSGKIGPKKPLPDHVSIVEPKDEILPTTPISEQKGGKPEPPAMPQPVPTA | 4.2.99.18 | null | apoptotic process [GO:0006915]; cell cycle [GO:0007049]; cell division [GO:0051301]; DNA repair [GO:0006281]; positive regulation of apoptotic signaling pathway [GO:2001235]; regulation of translation [GO:0006417]; translation [GO:0006412] | cytosolic small ribosomal subunit [GO:0022627]; mitochondrial inner membrane [GO:0005743]; nucleolus [GO:0005730]; nucleus [GO:0005634]; spindle [GO:0005819] | class I DNA-(apurinic or apyrimidinic site) endonuclease activity [GO:0140078]; DNA binding [GO:0003677]; RNA binding [GO:0003723]; structural constituent of ribosome [GO:0003735] | PF07650;PF00189; | 3.30.300.20;3.30.1140.32; | Universal ribosomal protein uS3 family | PTM: Methylation by PRMT1 is required for import into the nucleolus and for ribosome assembly. {ECO:0000250|UniProtKB:P23396}.; PTM: Sumoylation by SUMO1 enhances protein stability through increased resistance to proteolysis. Sumoylation occurs at one or more of the three consensus sites, Lys-18, Lys-214 and Lys-230. {... | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:P23396}. Nucleus {ECO:0000250|UniProtKB:P23396}. Nucleus, nucleolus {ECO:0000250|UniProtKB:P23396}. Mitochondrion inner membrane {ECO:0000250|UniProtKB:P23396}; Peripheral membrane protein {ECO:0000250|UniProtKB:P23396}. Cytoplasm, cytoskeleton, spindle {ECO:000025... | CATALYTIC ACTIVITY: Reaction=2'-deoxyribonucleotide-(2'-deoxyribose 5'-phosphate)-2'-deoxyribonucleotide-DNA = a 3'-end 2'-deoxyribonucleotide-(2,3-dehydro-2,3-deoxyribose 5'-phosphate)-DNA + a 5'-end 5'-phospho-2'-deoxyribonucleoside-DNA + H(+); Xref=Rhea:RHEA:66592, Rhea:RHEA-COMP:13180, Rhea:RHEA-COMP:16897, Rhea:RH... | null | null | null | null | FUNCTION: Component of the small ribosomal subunit. The ribosome is a large ribonucleoprotein complex responsible for the synthesis of proteins in the cell. Has endonuclease activity and plays a role in repair of damaged DNA. Cleaves phosphodiester bonds of DNAs containing altered bases with broad specificity and cleav... | Canis lupus familiaris (Dog) (Canis familiaris) |
E2RK30 | PKHD1_CANLF | MIVWLISLMSIEILLLAGPALSFHIEPKEGSLAGGTWITVIFDGLELEQLYPTNGSQLEIHLVNVAVPALPSIPCDVSPVFLDLPVVMCRTRSLLPEVHEGLYYLEAHAGGQVVGSPSPGLQDCCTFKFSREQTPIVYQVTPPSGVPGKMIHVYGWIITGRSETFDFDAEYIDSPLILEAQGDKWVTACSLINRQTGSCYPLQENHGLGTLQCRVEGNYIGSQNVSFSVFNKGKSMVHKNAWLVSAKLDLFLYQTYSEILSVFPETGSLGGKTDIIITGDFFDNPALVTIAGVPCDIRHMSPRKIECTTRAPGKRARLTA... | null | null | branching morphogenesis of an epithelial tube [GO:0048754]; cell-cell junction organization [GO:0045216]; epithelial cell morphogenesis [GO:0003382]; establishment of centrosome localization [GO:0051660]; establishment of mitotic spindle orientation [GO:0000132]; negative regulation of epithelial cell apoptotic process... | apical plasma membrane [GO:0016324]; chromosome, centromeric region [GO:0000775]; cilium [GO:0005929]; endoplasmic reticulum [GO:0005783]; extracellular exosome [GO:0070062]; Golgi apparatus [GO:0005794]; nucleus [GO:0005634]; spindle [GO:0005819] | null | PF10162;PF01833; | 2.60.40.10;2.160.20.10; | null | PTM: Palmitoylated. Palmitoylation facilitates the trafficking to the cilia and membrane targeting. {ECO:0000250|UniProtKB:E9PZ36}.; PTM: N-glycosylated. {ECO:0000250|UniProtKB:E9PZ36}.; PTM: Several proteolytic cleavages occur within the extracellular domain, whereas at least one cleavage occurs within the cytoplasmic... | SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:P08F94}; Single-pass membrane protein {ECO:0000255}. Cytoplasm {ECO:0000250|UniProtKB:P08F94}. Apical cell membrane {ECO:0000250|UniProtKB:E9PZ36}. Cytoplasm, cytoskeleton, cilium basal body {ECO:0000250|UniProtKB:P08F94}. Cell projection, cilium {ECO:0000250|U... | null | null | null | null | null | FUNCTION: Promotes ciliogenesis in renal epithelial cells and therefore participates in the tubules formation and/ or ensures the maintenance of the architecture of the lumen of the kidney (By similarity). Has an impact on cellular symmetry by ensuring correct bipolar cell division through the regulation of centrosome ... | Canis lupus familiaris (Dog) (Canis familiaris) |
E2RQ08 | RPN1_CANLF | MEVPTARLLLLLLLGAWAPAPESASPEAPLLVNEDVKRTVDLSSHLAKVTAEVVLAHPGGGSTARAASFLLALEPELEARLAHLGVQVKGEDEEENNLEVRETKIKGKSGRFFTVKLPVALDPGAKVSVVVETVYTHVLQPYPTQITQSEKQFVVFEGNHYFYSPYPTKTQTMRVKLASRNVESYTKLGNPTRSEDLLDYGPFRDIPAYSQDTFKVHYENNSPFLTITSMTRVIEVSHWGNIAVEENVDLKHTGAVLKGPFSRYDYQRQPDSGIASIRSFKTILPAAAQDVYYRDEIGNVSTSHLLILDDSVEMEIRPRF... | null | null | protein glycosylation [GO:0006486]; protein N-linked glycosylation via asparagine [GO:0018279] | cytosol [GO:0005829]; oligosaccharyltransferase complex [GO:0008250]; rough endoplasmic reticulum [GO:0005791] | null | PF04597; | null | OST1 family | PTM: Ufmylated by UFL1 in response to endoplasmic reticulum stress, promoting reticulophagy of endoplasmic reticulum sheets. {ECO:0000250|UniProtKB:P04843}. | SUBCELLULAR LOCATION: Endoplasmic reticulum {ECO:0000269|PubMed:12887896}. Endoplasmic reticulum membrane; Single-pass type I membrane protein {ECO:0000269|PubMed:29519914}. | null | null | PATHWAY: Protein modification; protein glycosylation. {ECO:0000250|UniProtKB:P04843}. | null | null | FUNCTION: Subunit of the oligosaccharyl transferase (OST) complex that catalyzes the initial transfer of a defined glycan (Glc(3)Man(9)GlcNAc(2) in eukaryotes) from the lipid carrier dolichol-pyrophosphate to an asparagine residue within an Asn-X-Ser/Thr consensus motif in nascent polypeptide chains, the first step in ... | Canis lupus familiaris (Dog) (Canis familiaris) |
E2RSS3 | WEE2_CANLF | MDDSSINKELKQKLNVSYCEEESESEGQKEAPESRETQSQTPDWAEGQESEAKFTPPRTPSSSIHGVGTFEEKDKMSPDQALRTPGPGFHKCPGTPAQPDSRSEVVHCESPYTPKSLLSQSVISSTEKLPSRGSKHLRFTPVPFVDEMTSSALVNINPFTPESYRKQFLRSNGKRKTRGDLEEADPGEGKVEQGLPAKRCVLRETNMASRYEKEFLEVEKIGVGEFGTVYKCIKRLDGCVYAIKRSMKPVAGLSNENLALHEVYAHAVLGHHPHVVRYYSAWAEDDHMIIQNEYCNGGSLQTAISENTKSGNHFPELKLK... | 2.7.10.2 | null | female meiotic nuclear division [GO:0007143]; female pronucleus assembly [GO:0035038]; mitotic cell cycle [GO:0000278]; negative regulation of G2/MI transition of meiotic cell cycle [GO:0110031]; negative regulation of oocyte maturation [GO:1900194]; phosphorylation [GO:0016310]; positive regulation of phosphorylation ... | cytoplasm [GO:0005737]; nucleus [GO:0005634] | ATP binding [GO:0005524]; magnesium ion binding [GO:0000287]; non-membrane spanning protein tyrosine kinase activity [GO:0004715]; protein tyrosine kinase activity [GO:0004713] | PF00069; | 1.10.510.10; | Protein kinase superfamily, Ser/Thr protein kinase family, WEE1 subfamily | PTM: Phosphorylation leads to increase its activity. {ECO:0000250}. | SUBCELLULAR LOCATION: Nucleus {ECO:0000250}. | CATALYTIC ACTIVITY: Reaction=ATP + L-tyrosyl-[protein] = ADP + H(+) + O-phospho-L-tyrosyl-[protein]; Xref=Rhea:RHEA:10596, Rhea:RHEA-COMP:10136, Rhea:RHEA-COMP:10137, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:46858, ChEBI:CHEBI:82620, ChEBI:CHEBI:456216; EC=2.7.10.2; Evidence={ECO:0000255|PROSITE-ProRule:PRU100... | null | null | null | null | FUNCTION: Oocyte-specific protein tyrosine kinase that phosphorylates and inhibits CDK1 and acts as a key regulator of meiosis during both prophase I and metaphase II. Required to maintain meiotic arrest in oocytes during the germinal vesicle (GV) stage, a long period of quiescence at dictyate prophase I, by phosphoryl... | Canis lupus familiaris (Dog) (Canis familiaris) |
E2RTQ2 | KIN13_GIAIC | MSDLVYQWLESANLQQYYPAFEQQGITPQRFITITIQDYGALGIQALPDKQKLFRLITTLKSRENILEQQPSAPNTGATPQSVPSSHVSPHVAQGDRFVGDKQKQNDIQQAQDMSLYESYDGGYEPPYVSAQGSGPANGDDYVIPTIPYHPNAPNPPNPRGIPTVNRTVVPPVDLFLNQIQSRIRVVIRKRPINPKELSQNQRDVVTADGWNQVSIHEPKVKVDLTKYTDLHTFKFDHVFNEQSDNQEIYQYAAKPLIRSVFEGKNCTVFAYGQTGSGKSFTMMHKDNGIYVLACFDILEYLRVYNGSQGNNSKFLVPVV... | null | null | axonemal microtubule depolymerization [GO:0060404]; cell morphogenesis [GO:0000902]; microtubule depolymerization [GO:0007019]; microtubule-based movement [GO:0007018]; mitotic cell cycle [GO:0000278]; mitotic cytokinesis [GO:0000281]; mitotic spindle microtubule depolymerization [GO:1990755]; plus-end specific microtu... | 9+2 motile cilium [GO:0097729]; axoneme [GO:0005930]; ciliary basal body [GO:0036064]; kinetochore [GO:0000776]; median body [GO:0097568]; microtubule [GO:0005874]; spindle [GO:0005819]; ventral disc [GO:0097597] | ATP binding [GO:0005524]; microtubule binding [GO:0008017]; microtubule motor activity [GO:0003777] | PF00225;PF00536; | 3.40.850.10;1.10.150.50; | TRAFAC class myosin-kinesin ATPase superfamily, Kinesin family, KIN-13 subfamily | PTM: Phosphorylated by PLK. {ECO:0000250|UniProtKB:Q969B0}. | SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton {ECO:0000269|PubMed:17766466, ECO:0000269|PubMed:31855176}. Cell projection, cilium, flagellum {ECO:0000269|PubMed:17766466, ECO:0000269|PubMed:31855176}. Cytoplasm, cytoskeleton, flagellum basal body {ECO:0000250|UniProtKB:Q969B0}. Cytoplasm, cytoskeleton, flagellum axonem... | null | null | null | null | null | FUNCTION: Involved in cell cycle (PubMed:17766466). Involved in formation of flagella, regulation of flagellar length, and formation of median bodies during interphase (By similarity). Regulates flagellar length in all eight distal flagellar tips by promoting disassembly of the microtubules (PubMed:17766466, PubMed:318... | Giardia intestinalis (strain ATCC 50803 / WB clone C6) (Giardia lamblia) |
E2RTQ7 | AURK_GIAIC | MPQHLVPHTGTGKRTTIEDFEIGRFLGRGKYGLVYLAREQSSKLVVALKVLYKSYIKSERVEGQVRRELDIHLNVRHINIIRLYTWFQDETRVFLVLEVAPYGELYQRLQQFGKFPLPVVSKIIRDVAQAIQYLHRKNIFHRDLKAENILICKGKETKEHTDAHNSDDSISVHEHELVRMAHYTYKIADFGWSVHHPTHGGRRRTQCGTLDYLPPEVMLGQSYDKACDIWSLGALCYELICGTAPFYHDEIKITRQNIANVEYSFTKDFSPASKDFIQRMLIRSPEARISIEDILRHPFLRQTDHRSKVPK | 2.7.11.1 | null | microtubule cytoskeleton organization involved in mitosis [GO:1902850]; mitotic cytokinesis [GO:0000281]; mitotic nuclear division [GO:0140014]; mitotic spindle organization [GO:0007052]; phosphorylation [GO:0016310]; regulation of cell cycle [GO:0051726]; regulation of cytokinesis [GO:0032465] | centrosome [GO:0005813]; chromosome passenger complex [GO:0032133]; cytoplasm [GO:0005737]; kinetochore [GO:0000776]; median body [GO:0097568]; motile cilium [GO:0031514]; nuclear membrane [GO:0031965]; nucleus [GO:0005634]; spindle [GO:0005819]; spindle microtubule [GO:0005876]; spindle midzone [GO:0051233]; spindle p... | ATP binding [GO:0005524]; cytoskeletal protein binding [GO:0008092]; protein serine/threonine kinase activity [GO:0004674] | PF00069; | 1.10.510.10; | Protein kinase superfamily, Ser/Thr protein kinase family, Aurora subfamily | PTM: Phosphorylated in mitosis and cytokinesis (PubMed:17964578). Activated by autophosphorylation at Thr-205 (PubMed:27859890). {ECO:0000269|PubMed:17964578, ECO:0000269|PubMed:27859890}. | SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:17964578}. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome {ECO:0000269|PubMed:17964578}. Cytoplasm, cytoskeleton, spindle {ECO:0000269|PubMed:17964578, ECO:0000269|PubMed:27859890}. Cytoplasm, cytoskeleton, spindle pole {ECO:0000269|PubMed:17964578}.... | 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:0000255|RuleBase:RU367134, ECO:0000... | null | null | null | null | FUNCTION: Involved in regulation of the cell cycle (PubMed:17964578, PubMed:27859890). Required for mitotic cell division and cytokinesis (PubMed:17964578, PubMed:27859890). Based on its localization to centrosomes and spindle microtubules, as well as to various cytoskeletal components such as the median body, parental... | Giardia intestinalis (strain ATCC 50803 / WB clone C6) (Giardia lamblia) |
E2RTZ4 | HMP_GIAIC | MTLSEDTLRAVEATAGLIAAQGIEFTRAFYERMLTKNEELKNIFNLAHQRTLRQPKALLDSLVAYALNIRRINELYELKGKGLPVPPEHWAELQGFFSAAERVANKHTSFGIQPAQYQIVGAHLLATIEDRITKDKDILAEWAKAYQFLADLFIKREEEIYAATEGCKGGWRQTRTFRVEEKTRVNEIICKFRLVPAEEGAGVVEHRPGQYLAIFVRSPEHFQHQQIRQYSIISAPNSAYYEIAVHRDEKGTVSRYLHDYVSTGDLLEVAPPYGDFFLRYLEADEQAPADTQASQEFQMLQSGAINFAAEKTMPIVLISG... | 1.14.12.17 | COFACTOR: Name=heme b; Xref=ChEBI:CHEBI:60344; Note=Binds 1 heme b group.; COFACTOR: Name=FAD; Xref=ChEBI:CHEBI:57692; Note=Binds 1 FAD.; | cellular response to nitrosative stress [GO:0071500]; nitric oxide catabolic process [GO:0046210]; response to toxic substance [GO:0009636] | null | FAD binding [GO:0071949]; heme binding [GO:0020037]; metal ion binding [GO:0046872]; nitric oxide dioxygenase NAD(P)H activity [GO:0008941]; oxygen binding [GO:0019825]; oxygen carrier activity [GO:0005344] | PF00970;PF00042;PF00175; | 1.10.490.10;3.40.50.80;2.40.30.10; | Globin family, Two-domain flavohemoproteins subfamily; Flavoprotein pyridine nucleotide cytochrome reductase family | null | null | CATALYTIC ACTIVITY: Reaction=NADPH + 2 nitric oxide + 2 O2 = H(+) + NADP(+) + 2 nitrate; Xref=Rhea:RHEA:19465, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, ChEBI:CHEBI:16480, ChEBI:CHEBI:17632, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349; EC=1.14.12.17; CATALYTIC ACTIVITY: Reaction=NADH + 2 nitric oxide + 2 O2 = H(+) + NAD(+) + 2 ni... | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=22 uM for O(2) {ECO:0000269|PubMed:20691663}; | null | null | null | FUNCTION: Flavohemoprotein involved in nitric oxide (NO) detoxification in an aerobic process, termed nitric oxide dioxygenase (NOD) reaction that utilizes O(2) and NAD(P)H to convert NO to nitrate, which protects the protozoan parasite from various noxious nitrogen compounds. Therefore, plays a central role in the ind... | Giardia intestinalis (strain ATCC 50803 / WB clone C6) (Giardia lamblia) |
E2RU10 | EB1_GIAIC | MPPVKAPGNVSDCYFVGRVSLLKWISELLNEPVKKVEDLASGHHYCMALNLVYPGQVNMHRVRMNAINEWERSENFKIIQDVLSRNNIDKGIDVNKLVTGKYMDNFEFFQWFKWFFDQNYKGSKSGATESGSANAVTKTSKPGNRSGSTAASMQNPKASSTSGPSIDSKELEDLRRQIAKGQLESQFYFDKLHEIEIYMDQMNELMTQVEIAEPEDSPFYIKSVVKKIEDILYAEYHQ | null | null | cell division [GO:0051301]; protein localization to microtubule [GO:0035372]; regulation of microtubule polymerization or depolymerization [GO:0031110]; spindle assembly [GO:0051225]; thigmotropism [GO:0009652] | cytoplasmic microtubule [GO:0005881]; microtubule organizing center [GO:0005815]; microtubule plus-end [GO:0035371]; motile cilium [GO:0031514]; nuclear membrane [GO:0031965]; spindle midzone [GO:0051233] | microtubule plus-end binding [GO:0051010] | PF00307;PF03271; | 1.20.5.1430;1.10.418.10; | MAPRE family | PTM: Phosphorylated in vitro by aurora kinase. Phosphorylation is important for cell division. {ECO:0000269|PubMed:27859890}. | SUBCELLULAR LOCATION: Nucleus membrane {ECO:0000269|PubMed:18590831, ECO:0000269|PubMed:19953272, ECO:0000269|PubMed:24828878, ECO:0000269|PubMed:27859890, ECO:0000269|PubMed:30318753}. Cytoplasm, cytoskeleton {ECO:0000269|PubMed:17766466, ECO:0000269|PubMed:18590831, ECO:0000269|PubMed:19953272, ECO:0000269|PubMed:248... | null | null | null | null | null | FUNCTION: Involved in cell division (PubMed:18590831, PubMed:24828878, PubMed:27859890). Involved in mitosis (PubMed:18590831, PubMed:24828878). Regulates dynamics of microtubules (MTs) during mitosis (PubMed:24828878). Required for cytokinesis (PubMed:27859890). Binds polymerized MTs in vitro (PubMed:18590831, PubMed:... | Giardia intestinalis (strain ATCC 50803 / WB clone C6) (Giardia lamblia) |
E2RU81 | PFP_GIAIC | MSAFEVYRRKFKPALPRAIQGASYHLHTEEKTHPVADEQDIAALFPKTTHLPLLDIQPDTGAPKLLEPKRVGVIFSGGQAPGGHNVLCGLYDKLQQIAPKSVLLGFQNGPKGLMTNKYVELTEKFLEPFRNMGGFHAIGSGRDKIAKPEDFDAAAKTAKDNNLDIICIIGGDDSNTNACLLAEDFLKRGLKTAVIGVPKTIDRDLYSTKGIECSFGFDSSTKVYAELIGNICYDCLSAKKYWHFIRLMGRSASHITLECGLQTHANICLVGEEILSKKMTSRQLFEYLADCVTKRADSGKNYGVCLVPEGLIEFIPENNE... | 2.7.1.90 | COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000255|HAMAP-Rule:MF_03185}; | fructose 6-phosphate metabolic process [GO:0006002]; photosynthesis [GO:0015979]; response to glucose [GO:0009749] | cytosol [GO:0005829] | 6-phosphofructokinase activity [GO:0003872]; ATP binding [GO:0005524]; diphosphate-fructose-6-phosphate 1-phosphotransferase activity [GO:0047334]; metal ion binding [GO:0046872] | PF00365; | 3.40.50.450;3.40.50.460; | Phosphofructokinase type A (PFKA) family, PPi-dependent PFK group II subfamily, Clade 'Long' sub-subfamily | null | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_03185}. | 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_03185, ECO:0000269|PubMed:76... | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=1.09 mM for phosphate {ECO:0000269|PubMed:7663168, ECO:0000269|PubMed:8577346}; KM=0.039 mM for diphosphate {ECO:0000269|PubMed:7663168, ECO:0000269|PubMed:8577346}; KM=0.25 mM for fructose 6-phosphate {ECO:0000269|PubMed:7663168, ECO:0000269|PubMed:8577346}; KM=0.... | PATHWAY: Carbohydrate degradation; glycolysis; D-glyceraldehyde 3-phosphate and glycerone phosphate from D-glucose: step 3/4. {ECO:0000255|HAMAP-Rule:MF_03185}. | BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 7.2 for the forward reaction and 7.0 for the reverse reaction. {ECO:0000269|PubMed:7663168, ECO:0000269|PubMed:8577346}; | 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... | Giardia intestinalis (strain ATCC 50803 / WB clone C6) (Giardia lamblia) |
E2RU97 | 1433_GIAIC | MAEAFTREDYVFMAQLNENAERYDEMVETMRKISGMEGELSDKERNLLSVAYKNVIGPRRAAWRIVSSIEAKEKGRQKPNAKRIEQIRVYRQKIEKELSDICNDILKLLQEQFVPRSTNADAKVFYYKMQGDYYRYLAEYSSGEDKEKIAGSALNAYNSAFEISQQLPPTHPIRLGLALNFSVFYYEILASPDRACELARKAFDAAITDLDKLTEESYKDSTLIMQLLRDNLNLWVTDSAGDDNAEEK | null | null | actin cytoskeleton organization [GO:0030036]; activation of protein kinase C activity [GO:1990051]; establishment of cell polarity [GO:0030010]; MAPK cascade [GO:0000165]; positive regulation of cytoskeleton organization [GO:0051495]; protein homotetramerization [GO:0051289]; protein homotrimerization [GO:0070207]; reg... | axoneme [GO:0005930]; cytoplasm [GO:0005737]; cytoskeleton [GO:0005856]; endoplasmic reticulum [GO:0005783]; motile cilium [GO:0031514]; nuclear envelope [GO:0005635]; nucleus [GO:0005634]; spindle [GO:0005819] | actin binding [GO:0003779]; identical protein binding [GO:0042802]; kinase binding [GO:0019900]; phosphoprotein binding [GO:0051219]; phosphoserine residue binding [GO:0050815]; protein homodimerization activity [GO:0042803] | PF00244; | 1.20.190.20; | 14-3-3 family | PTM: Phosphorylated constitutively throughout the life cycle. Phosphorylation is very high in trophozoites and encysting cells of 12 hours (PubMed:16368691). Phosphorylated during excystation (PubMed:19861170). Phosphorylation promotes its binding to various target proteins and is critical for encystation process. Phos... | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:16368691, ECO:0000269|PubMed:19733174, ECO:0000269|PubMed:19861170, ECO:0000269|PubMed:21135098, ECO:0000269|PubMed:24147113, ECO:0000269|PubMed:24728194, ECO:0000269|PubMed:28932813}. Cytoplasm, cytoskeleton {ECO:0000269|PubMed:28932813}. Nucleus {ECO:0000269|PubMed:... | null | null | null | null | null | FUNCTION: Adapter protein implicated in the regulation of a large spectrum of both general and specialized signaling pathways. Binds to a large number of partners, usually by recognition of a phosphoserine or phosphothreonine motif. Binding generally results in the modulation of the activity of the binding partner (By ... | Giardia intestinalis (strain ATCC 50803 / WB clone C6) (Giardia lamblia) |
E3PJ86 | GSPD2_ECOH1 | MFWRDITLSVWRKKTTGLKTKKRLLPLVLAAALCSSPVWAEEATFTANFKDTDLKSFIETVGANLNKTIIMGPGVQGKVSIRTMTPLNERQYYQLFLNLLEAQGYAVVPMENDVLKVVKSSAAKVEPLPLVGEGSDNYAGDEMVTKVVPVRNVSVRELAPILRQMIDSAGSGNVVNYDPSNVIMLTGRASVVERLTEVIQRVDHAGNRTEEVIPLDNASASEIARVLESLTKNSGENQPATLKSQIVADERTNSVIVSGDPATRDKMRRLIRRLDSEMERSGNSQVFYLKYSKAEDLVDVLKQVSGTLTAAKEEAEGTVG... | null | null | protein secretion by the type II secretion system [GO:0015628] | cell outer membrane [GO:0009279]; type II protein secretion system complex [GO:0015627] | null | PF00263;PF03958;PF21305; | 3.30.1370.120; | Bacterial secretin family, GSP D subfamily | null | SUBCELLULAR LOCATION: Cell outer membrane {ECO:0000269|PubMed:22585966, ECO:0000305|PubMed:29632366}. Note=Some protein is also found in the cell inner membrane, the inner membrane protein does not form multimers and is unstable (PubMed:22585966). Most of the protein is in the periplasm which it traverses to contact pr... | null | null | null | null | null | FUNCTION: Part of a type II secretion system (T2SS, formerly general secretion pathway, GSP) for the export of folded proteins across the outer membrane (Probable). This subunit forms the outer membrane channel (Probable). {ECO:0000305|PubMed:22585966, ECO:0000305|PubMed:23820381, ECO:0000305|PubMed:29632366}. | Escherichia coli O78:H11 (strain H10407 / ETEC) |
E3PQQ8 | CCAP_CONVL | MVSLGHVLFVILLPVLLPVAADDPDDQMLSQISLPSSSRSEYDDNDVSKRVFCNGFTGCGGRHRDRSRRQERYGKRLIPVLAKRPFCNSFGCYNGKRSLSGAGPALSTPVDPSRNNKARTMARMLDAAASARHEQQQQLLQQREQRGLESRDPAASGDLSKRLFCNGYGGCRGGKRTLYSPWLERMNEVADDRSARNALCTRLGWRE | null | null | modulation of heart rate in another organism [GO:0044554]; negative regulation of heart rate in another organism [GO:0044555] | extracellular region [GO:0005576]; host extracellular space [GO:0043655] | toxin activity [GO:0090729] | null | null | null | null | SUBCELLULAR LOCATION: Secreted. | null | null | null | null | null | FUNCTION: [ConoCAP-a]: In contrast to other members of the CCAP family which are cardio-accelerators, conoCAP-a decreases the heart frequency in Drosophila larvae (26%), rats and zebrafish embryos. It also reduces the blood pressure in rats. It decreases systolic calcium in ventricular cardiac myocytes, indicating that... | Conus villepinii (Villepin's cone) |
E3PRJ4 | KAME_ACESD | MSSGLYSMEKKEFDKVLDLERVKPYGDTMNDGKVQLSFTLPLKNNERSAEAAKQIALKMGLEEPSVVMQQSLDEEFTFFVVYGNFVQSVNYNEIHVEAVNSEILSMEETDEYIKENIGRKIVVVGASTGTDAHTVGIDAIMNMKGYAGHYGLERYEMIDAYNLGSQVANEDFIKKAVELEADVLLVSQTVTQKNVHIQNMTHLIELLEAEGLRDRFVLLCGGPRINNEIAKELGYDAGFGPGRFADDVATFAVKTLNDRMNS | 5.4.3.3 | COFACTOR: Name=adenosylcob(III)alamin; Xref=ChEBI:CHEBI:18408; Evidence={ECO:0000269|PubMed:10617592, ECO:0000269|PubMed:11318641}; COFACTOR: Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326; Evidence={ECO:0000269|PubMed:11318641, ECO:0000269|PubMed:15514022}; | null | null | cobalamin binding [GO:0031419]; D-lysine 5,6-aminomutase activity [GO:0047826]; metal ion binding [GO:0046872]; protein dimerization activity [GO:0046983] | PF02310;PF16554; | 3.40.50.280;3.30.30.60; | KamE family | null | null | CATALYTIC ACTIVITY: Reaction=(3S)-3,6-diaminohexanoate = (3S,5S)-3,5-diaminohexanoate; Xref=Rhea:RHEA:21736, ChEBI:CHEBI:57434, ChEBI:CHEBI:57436; EC=5.4.3.3; Evidence={ECO:0000269|PubMed:11318641}; CATALYTIC ACTIVITY: Reaction=D-lysine = (2R,5S)-2,5-diaminohexanoate; Xref=Rhea:RHEA:18241, ChEBI:CHEBI:32557, ChEBI:CHEB... | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=6.6 uM for adenosylcobalamin (for recombinant alpha and beta subunits expressed together in E.coli to overcome presence of corrinoids in native system) {ECO:0000269|PubMed:10617592}; | PATHWAY: Amino-acid metabolism; lysine degradation. {ECO:0000269|PubMed:10617592}. | null | null | FUNCTION: Catalyzes the migration of the L-beta-lysine and D-lysine epsilon amino group to the delta carbon to produce 3,5-diaminohexanoate and 2,5-diaminohexanoate, respectively. {ECO:0000269|PubMed:10617592, ECO:0000269|PubMed:11318641}. | Acetoanaerobium sticklandii (strain ATCC 12662 / DSM 519 / JCM 1433 / CCUG 9281 / NCIMB 10654 / HF) (Clostridium sticklandii) |
E3PRJ5 | KAMD_ACESD | MISVESKLNLDFNLVEKARAKAKAIAIDTQEFIEKHTTVTVERAVCRLLGIDGVDTDEVPLPNIVVDHIKENNGLNLGAAMYIANAVLNTGKTPQEIAQAISAGELDLTKLPMKDLFEVKTKALSMAKETVEKIKNNRSIRESRFEEYGDKSGPLLYVIVATGNIYEDITQAVAAAKQGADVIAVIRTTGQSLLDYVPYGATTEGFGGTYATQENFRLMREALDKVGAEVGKYIRLCNYCSGLCMPEIAAMGAIERLDVMLNDALYGILFRDINMQRTMIDQNFSRIINGFAGVIINTGEDNYLTTADAFEEAHTVLASQ... | 5.4.3.3 | COFACTOR: Name=adenosylcob(III)alamin; Xref=ChEBI:CHEBI:18408; Evidence={ECO:0000269|PubMed:10617592, ECO:0000269|PubMed:11318641}; COFACTOR: Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326; Evidence={ECO:0000269|PubMed:11318641, ECO:0000269|PubMed:15514022}; | null | null | cobalamin binding [GO:0031419]; D-lysine 5,6-aminomutase activity [GO:0047826] | PF09043; | 3.20.20.440; | KamD family | null | null | CATALYTIC ACTIVITY: Reaction=(3S)-3,6-diaminohexanoate = (3S,5S)-3,5-diaminohexanoate; Xref=Rhea:RHEA:21736, ChEBI:CHEBI:57434, ChEBI:CHEBI:57436; EC=5.4.3.3; Evidence={ECO:0000269|PubMed:11318641}; CATALYTIC ACTIVITY: Reaction=D-lysine = (2R,5S)-2,5-diaminohexanoate; Xref=Rhea:RHEA:18241, ChEBI:CHEBI:32557, ChEBI:CHEB... | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=6.6 uM for adenosylcobalamin (for recombinant alpha and beta subunits expressed together in E.coli to overcome the presence of corrinoids in native system) {ECO:0000269|PubMed:10617592}; | PATHWAY: Amino-acid metabolism; lysine degradation. {ECO:0000269|PubMed:10617592}. | null | null | FUNCTION: Catalyzes the migration of the L-beta-lysine and D-lysine epsilon amino group to the delta carbon to produce 3,5-diaminohexanoate and 2,5-diaminohexanoate, respectively. {ECO:0000269|PubMed:10617592, ECO:0000269|PubMed:11318641}. | Acetoanaerobium sticklandii (strain ATCC 12662 / DSM 519 / JCM 1433 / CCUG 9281 / NCIMB 10654 / HF) (Clostridium sticklandii) |
E3PY95 | OAME_ACESD | MEKDLQLRVNEKLDVENILKDLDKYTPKRRGWTWRQPAENLQMGPFIYKDASTPLENSVALPSAKYFGDIDPQPLPVITTEIASGRFEDDIRRMRMAAWHGADHIMVIRTAGQSHYDGLIEGTPQGIGGVPITRKQVRAQRKALDLIEEEVGRPINYHSYVSGVAGPDIAVMFAEEGVNGAHQDPQYNVLYRNINMIRSFIDACESKTIMAWADMAQIDGAHNANATAREAWKVMPELMVQHALNSIFSLKVGMKKSNICLSTVPPTAPPAPSMYLDLPYAVALREMFEGYRMRAQMNTKYMEASTREATVTHVLNLLIS... | 5.4.3.5 | COFACTOR: Name=adenosylcob(III)alamin; Xref=ChEBI:CHEBI:18408; Evidence={ECO:0000269|PubMed:11577113, ECO:0000269|PubMed:20106986, ECO:0000269|PubMed:4711468, ECO:0000269|Ref.4}; COFACTOR: Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326; Evidence={ECO:0000269|PubMed:11577113, ECO:0000269|PubMed:20106986, ECO:00002... | null | null | cobalamin binding [GO:0031419]; D-ornithine 4,5-aminomutase activity [GO:0047831]; metal ion binding [GO:0046872]; protein dimerization activity [GO:0046983] | PF02310;PF09043;PF16554; | 3.40.50.280;3.20.20.440;3.30.30.60; | null | null | null | CATALYTIC ACTIVITY: Reaction=D-ornithine = (2R,4S)-2,4-diaminopentanoate; Xref=Rhea:RHEA:14893, ChEBI:CHEBI:57668, ChEBI:CHEBI:58697; EC=5.4.3.5; Evidence={ECO:0000269|PubMed:11577113, ECO:0000269|PubMed:4711468, ECO:0000269|Ref.4}; | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=44.5 uM for D-ornithine {ECO:0000269|PubMed:11577113, ECO:0000269|PubMed:4711468, ECO:0000269|Ref.4}; KM=0.43 uM for adenosylcobalamin {ECO:0000269|PubMed:11577113, ECO:0000269|PubMed:4711468, ECO:0000269|Ref.4}; KM=1.5 uM for pyridoxal phosphate {ECO:0000269|PubMe... | null | BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 9.0 or between 8.5-8.7 (with Tris-HCl buffer). Half-maximal activity is observed at pH 7.4 and 9.7. {ECO:0000269|PubMed:11577113, ECO:0000269|PubMed:4711468, ECO:0000269|Ref.4}; | BIOPHYSICOCHEMICAL PROPERTIES: Temperature dependence: Optimum temperature is 37 degrees Celsius for native enzyme. Displays half-maximal activity at 23 degrees Celsius and 49 degrees Celsius. Rapidly inactivated at temperatures above 45 degrees Celsius. Loses more than 35% and 30% of its activity when stored at -20 d... | FUNCTION: Component of a complex that catalyzes the reversible migration of the omega amino group of D-ornithine to C-4 to form (2R,4S)-2,4-diaminopentanoic acid. OraE may be the catalytic subunit. Active only on D-ornithine and 2,4-diaminopentanoic acid but not active on L-ornithine, L-beta-lysine, L-alpha-lysine or D... | Acetoanaerobium sticklandii (strain ATCC 12662 / DSM 519 / JCM 1433 / CCUG 9281 / NCIMB 10654 / HF) (Clostridium sticklandii) |
E3PZS2 | STAD2_OPHSP | MELHLALRASPLPAADPGRRPPPPRGNFATNCTAAINSTHISQEKFRSLDSWVEHNMLTFLKPVEKCWQPQDFLPDPSHLSAEELGDAVREIHERAAEIPDEVWVCMVGNMVTEEALPTYQSLISSVLGGTVAGSTPWDRWIRGWSAEENRHGDLLNKYLYLTGRLDMRQVEKTIQYLIGSGMDVGVGNSILCGFIYTCFQEKATFISHGNTARLAKHHGDTTLAKICGLVAADEKRHAVAYTNLMKKLFEVAPNESMLAFAHIMRAHVTMPASRMFDGRDPRLFTHFSAVTQKIGVYTVRDYGEMLDFFLKEWEISAVV... | 1.14.19.11; 1.14.19.2 | COFACTOR: Name=Fe(2+); Xref=ChEBI:CHEBI:29033; Evidence={ECO:0000250|UniProtKB:P22337}; Note=Binds 2 Fe(2+) ions per subunit. {ECO:0000250|UniProtKB:P22337}; | defense response [GO:0006952]; unsaturated fatty acid biosynthetic process [GO:0006636] | chloroplast stroma [GO:0009570]; cytosol [GO:0005829] | acyl-[acyl-carrier-protein] desaturase activity [GO:0045300]; metal ion binding [GO:0046872]; stearoyl-[acp] desaturase activity [GO:0102786]; stearoyl-CoA 9-desaturase activity [GO:0004768] | PF03405; | 1.10.620.20; | Fatty acid desaturase type 2 family | null | SUBCELLULAR LOCATION: Plastid, chloroplast stroma {ECO:0000250|UniProtKB:P22337}. | CATALYTIC ACTIVITY: Reaction=2 H(+) + hexadecanoyl-[ACP] + O2 + 2 reduced [2Fe-2S]-[ferredoxin] = (4Z)-hexadecenoyl-[ACP] + 2 H2O + 2 oxidized [2Fe-2S]-[ferredoxin]; Xref=Rhea:RHEA:38043, Rhea:RHEA-COMP:9652, Rhea:RHEA-COMP:10000, Rhea:RHEA-COMP:10001, Rhea:RHEA-COMP:11488, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:C... | null | PATHWAY: Lipid metabolism; fatty acid metabolism. | null | null | FUNCTION: Converts stearoyl-ACP to oleoyl-ACP by introduction of a cis double bond between carbons 9 and 10 of the acyl chain. Converts palmitoyl-ACP to (4Z)-hexadec-4-enoyl-ACP by introduction of a cis double bond between carbons 4 and 5 of the acyl chain. Catalyzes the desaturation of saturated fatty acid 18:0 and 16... | Ophrys sphegodes (Early spider orchid) (Arachnites aranifera) |
E3Q1H1 | GNA1_TRYBB | MTDIVDLELRVLEESDLSSHLELLGHLTEAPPLSGVELANIADMRRRAGIVTKVFCHQPTGRIVGSASLMIQPKFTRGGRAVGHIEDVVVDPSYRGAGLGKALIMDLCEISRSKGCYKVILDSSEKSLPFYEKLGFRAHERQMRLDL | 2.3.1.4 | null | poly-N-acetyllactosamine biosynthetic process [GO:0030311]; UDP-N-acetylglucosamine biosynthetic process [GO:0006048] | endoplasmic reticulum [GO:0005783]; endoplasmic reticulum-Golgi intermediate compartment [GO:0005793]; glycosome [GO:0020015]; Golgi apparatus [GO:0005794] | glucosamine 6-phosphate N-acetyltransferase activity [GO:0004343]; identical protein binding [GO:0042802]; monosaccharide binding [GO:0048029]; protein homodimerization activity [GO:0042803] | PF00583; | 3.40.630.30; | Acetyltransferase family, GNA1 subfamily | PTM: Contains poly-N-acetyllactosamines. {ECO:0000269|PubMed:21531872}. | SUBCELLULAR LOCATION: Glycosome {ECO:0000269|PubMed:21531872}. Note=Predominantly located in glycosome microbodies in the bloodstream form of T.brucei. {ECO:0000269|PubMed:21531872}. | CATALYTIC ACTIVITY: Reaction=acetyl-CoA + D-glucosamine 6-phosphate = CoA + H(+) + N-acetyl-D-glucosamine 6-phosphate; Xref=Rhea:RHEA:10292, ChEBI:CHEBI:15378, ChEBI:CHEBI:57287, ChEBI:CHEBI:57288, ChEBI:CHEBI:57513, ChEBI:CHEBI:58725; EC=2.3.1.4; Evidence={ECO:0000255|RuleBase:RU365086, ECO:0000269|PubMed:21531872}; | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=144 uM for glucosamine 6-phosphate (at pH 7.2 and room temperature) {ECO:0000269|PubMed:21531872}; KM=234 uM for acetyl-CoA (at pH 7.2 and room temperature) {ECO:0000269|PubMed:21531872}; | PATHWAY: Nucleotide-sugar biosynthesis; UDP-N-acetyl-alpha-D-glucosamine biosynthesis; N-acetyl-alpha-D-glucosamine 1-phosphate from alpha-D-glucosamine 6-phosphate (route I): step 1/2. {ECO:0000255|RuleBase:RU365086, ECO:0000269|PubMed:21531872}. | null | null | FUNCTION: Involved in the biosynthesis of UDP-N-acetyl-alpha-D-glucosamine. Catalyzes the formation of N-acetyl-D-glucosamine 6-phosphate from acetyl-coenzyme A (acetyl-CoA) and D-glucosamine 6-phosphate. {ECO:0000269|PubMed:21531872}. | Trypanosoma brucei brucei |
E3SCZ8 | BIRC5_CAVPO | MGAPSLPRAWQLYLKEHRVSTFKNWPFVNGCSCTPERMAEAGFIHCPTENEPDLAQCFFCFKELEGWEPDDNPIEEHKKHSSGCAFLSVKKQFEELTLSEFLKLDKERAKNKIAKETNSKQKEFEETAAKVRQAMEQLAALE | null | null | apoptotic process [GO:0006915]; cell division [GO:0051301]; chromosome segregation [GO:0007059]; meiosis I [GO:0007127]; microtubule cytoskeleton organization [GO:0000226]; negative regulation of apoptotic process [GO:0043066]; negative regulation of neuron apoptotic process [GO:0043524]; regulation of insulin secretio... | chromosome, centromeric region [GO:0000775]; cytoplasm [GO:0005737]; kinetochore [GO:0000776]; microtubule [GO:0005874]; midbody [GO:0030496]; nucleus [GO:0005634]; spindle midzone [GO:0051233] | cysteine-type endopeptidase inhibitor activity [GO:0004869]; metal ion binding [GO:0046872] | PF00653; | null | IAP family | PTM: Ubiquitinated by the Cul9-RING ubiquitin-protein ligase complex, leading to its degradation. Ubiquitination is required for centrosomal targeting. Deubiquitinated by USP35 or USP38; leading to stabilization. {ECO:0000250|UniProtKB:O15392}.; PTM: In vitro phosphorylation at Thr-117 by AURKB prevents interaction wit... | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:20627126, ECO:0000269|PubMed:20727954, ECO:0000269|PubMed:21364656}. Nucleus {ECO:0000269|PubMed:20627126, ECO:0000269|PubMed:20727954, ECO:0000269|PubMed:21364656}. Chromosome {ECO:0000250|UniProtKB:O15392}. Chromosome, centromere {ECO:0000269|PubMed:20727954}. Cytop... | null | null | null | null | null | FUNCTION: Multitasking protein that has dual roles in promoting cell proliferation and preventing apoptosis (PubMed:20627126, PubMed:20727954, PubMed:21364656). Component of a chromosome passage protein complex (CPC) which is essential for chromosome alignment and segregation during mitosis and cytokinesis (PubMed:2072... | Cavia porcellus (Guinea pig) |
E3VNM4 | TGA10_ARATH | MQGHHQNHHQHLSSSSATSSHGNFMNKDGYDIGEIDPSLFLYLDGQGHHDPPSTAPSPLHHHHTTQNLAMRPPTSTLNIFPSQPMHIEPPPSSTHNTDNTRLVPAAQPSGSTRPASDPSMDLTNHSQFHQPPQGSKSIKKEGNRKGLASSDHDIPKSSDPKTLRRLAQNREAARKSRLRKKAYVQQLESCRIKLTQLEQEIQRARSQGVFFGGSLIGGDQQQGGLPIGPGNISSEAAVFDMEYARWLEEQQRLLNELRVATQEHLSENELRMFVDTCLAHYDHLINLKAMVAKTDVFHLISGAWKTPAERCFLWMGGFRP... | null | null | anther development [GO:0048653]; DNA-templated transcription [GO:0006351]; hydrogen peroxide mediated signaling pathway [GO:0071588]; response to molecule of bacterial origin [GO:0002237] | nucleus [GO:0005634] | DNA-binding transcription factor activity [GO:0003700]; protein homodimerization activity [GO:0042803]; transcription cis-regulatory region binding [GO:0000976] | PF00170;PF14144; | 1.20.5.170; | BZIP family | null | SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00768, ECO:0000255|PROSITE-ProRule:PRU00978, ECO:0000269|PubMed:20805327}. | null | null | null | null | null | FUNCTION: Together with TGA9, basic leucine-zipper transcription factor required for anther development, probably via the activation of SPL expression in anthers and via the regulation of genes with functions in early and middle tapetal development (PubMed:20805327). Required for signaling responses to pathogen-associa... | Arabidopsis thaliana (Mouse-ear cress) |
E3VWI2 | G3P2_STRAE | MTVRIGINGFGRIGRNVFRAAAARSSELEIVAVNDLGDVPTMAHLLAYDSILGRFPEEVTAEPGAIRVGDRTIKVLAERDPGALPWGDLGVDIVIESTGIFTDAAKARSHVDGGAKKVIIAAPASGEDFTVVLGVNDGDYDPERHTIISNASCTTNCLGVLAKVLHDAVGIDSGMMTTVHAYTQDQNLQDAPHKDLRRARAAALNIVPTSSGAAKAIGLVLPELAGRLDAFALRVPVPTGSVTDLTVTTRRGTSVEEVKEAYAAAASGPYKGLLSYVDAPLVSTDIVGDPASCVFDAGLTRVSGPQVKVVGWYDNEWGYS... | 1.2.1.12 | null | glucose metabolic process [GO:0006006]; glycolytic process [GO:0006096] | cytosol [GO:0005829] | glyceraldehyde-3-phosphate dehydrogenase (NAD+) (phosphorylating) activity [GO:0004365]; NAD binding [GO:0051287]; NADP binding [GO:0050661] | PF02800;PF00044; | 3.40.50.720; | Glyceraldehyde-3-phosphate dehydrogenase family | null | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305}. | CATALYTIC ACTIVITY: Reaction=D-glyceraldehyde 3-phosphate + NAD(+) + phosphate = (2R)-3-phospho-glyceroyl phosphate + H(+) + NADH; Xref=Rhea:RHEA:10300, ChEBI:CHEBI:15378, ChEBI:CHEBI:43474, ChEBI:CHEBI:57540, ChEBI:CHEBI:57604, ChEBI:CHEBI:57945, ChEBI:CHEBI:59776; EC=1.2.1.12; Evidence={ECO:0000269|PubMed:6822480}; | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=110 uM for NAD (at pH 8 and 26 degrees Celsius) {ECO:0000269|PubMed:6822480}; KM=250 uM for G3P (at pH 8 and 26 degrees Celsius) {ECO:0000269|PubMed:6822480}; | PATHWAY: Carbohydrate degradation; glycolysis; pyruvate from D-glyceraldehyde 3-phosphate: step 1/5. {ECO:0000305}. | null | null | FUNCTION: Catalyzes the oxidative phosphorylation of glyceraldehyde 3-phosphate (G3P) to 1,3-bisphosphoglycerate (BPG) using the cofactor NAD. The first reaction step involves the formation of a hemiacetal intermediate between G3P and a cysteine residue, and this hemiacetal intermediate is then oxidized to a thioester,... | Streptomyces arenae |
E3W9M2 | AA5GT_DIACA | MNMSCKFEIVLLVSWWLLLVLVFGVESSMFSEFDRLDFPKHFIFGASSCAYQVEGAAFEDGRTLSTFDIAAHSGHLPGNGDITSDEYHKYKEDVELMVETGLDAYRFSISWSRLIPNGRGPVNPKGLEYYNNLVNALLTKGTQPHVTLLHSDLPQALRDEYGGLFISPKFIDDFVAYADVCFREFGDRVLHWTTFNEANFLAFGDENTPASALYLSAHHLLLAHASATRLYRENYQASQRGFIGINVYAYDFIPETNTEVDVIAAKRARDFFIGWFVQPLMNGEYPLTMRKNGGPRLPKFTPNETELLTGSYDFIGLNYY... | 2.4.1.299 | null | anthocyanin-containing compound biosynthetic process [GO:0009718]; carbohydrate metabolic process [GO:0005975]; pigmentation [GO:0043473] | plant-type vacuole [GO:0000325] | beta-glucosidase activity [GO:0008422]; cyanidin 3-O-glucoside 5-O glucosyltransferase (vanilloyl-glucose dependent) activity [GO:0102458]; cyanidin 3-O-glucoside 5-O-glucosyltransferase (acyl-glucose dependent) activity [GO:0102506]; delphinidin 3-O-glucoside 5-O-glucosyltransferase (acyl-glucose dependent) activity [... | PF00232; | 3.20.20.80; | Glycosyl hydrolase 1 family | null | SUBCELLULAR LOCATION: Vacuole {ECO:0000269|PubMed:20971893}. | CATALYTIC ACTIVITY: Reaction=1-O-(trans-sinapoyl)-beta-D-glucose + cyanidin 3-O-beta-D-glucoside = (E)-sinapate + cyanidin 3,5-di-O-beta-D-glucoside; Xref=Rhea:RHEA:35427, ChEBI:CHEBI:16546, ChEBI:CHEBI:30023, ChEBI:CHEBI:71511, ChEBI:CHEBI:77857; EC=2.4.1.299; Evidence={ECO:0000269|PubMed:20971893}; | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=13 mM for cyanidin 3-glucopyranoside (with native enzyme at pH 5.0 and 30 degrees Celsius) {ECO:0000269|PubMed:20971893}; KM=46.5 mM for 1-O-beta-D-vanillyl-glucose (with native enzyme at pH 5.0 and 30 degrees Celsius) {ECO:0000269|PubMed:20971893}; KM=6.5 mM for c... | PATHWAY: Pigment biosynthesis; anthocyanin biosynthesis. {ECO:0000269|PubMed:20971893}. | BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 4.5-5.0. {ECO:0000269|PubMed:20971893}; | BIOPHYSICOCHEMICAL PROPERTIES: Temperature dependence: Optimum temperature is 48 degrees Celsius. {ECO:0000269|PubMed:20971893}; | FUNCTION: Beta-glycosidase that catalyzes the transfer of glucose moiety to anthocyanidin 3-glucoside at the 5 position. Anthocyanins are ubiquitous colored pigments that are responsible for variations in petal color. Uses acyl-glucoses, but not UDP-glucose, as the glucose donor. {ECO:0000269|PubMed:20971893}. | Dianthus caryophyllus (Carnation) (Clove pink) |
E3W9M3 | AA7GT_DELGR | MCPSFLVTLLLLQLSSLVVVLVVWAEQLPEFNVRRDDFPSNFVFGAGTSALQVEGAIAEDGKTPNIWDVDSHMGHMPDKSTTDIACDSYHRYKEDVKIMSDIGLEAYRFSIAWTRILPYGRGFINPKGVEYYNNLIDTLLEHGIQPHATIYHIDHPQILEDEYGGWLSPRMIEDFTTYADVCFREFGDRVSHWTTINEPNIISLGAYDSGQIPPHRCTPPGAYNCTAGNSSVEPYKAMHHFLLAHASAVQIYRTKYQAKQKGLIGLNVYGFWCAPQTNSRADIEATKRATAFYTGWAADPLVFGDYPIIMKENVGSRLPS... | 2.4.1.300 | null | anthocyanin-containing compound biosynthetic process [GO:0009718]; carbohydrate metabolic process [GO:0005975] | plant-type vacuole [GO:0000325] | beta-glucosidase activity [GO:0008422]; cyanidin 3-O-glucoside 7-O-glucosyltransferase (feruloyl-glucose dependent) activity [GO:0102514]; cyanidin 3-O-glucoside 7-O-glucosyltransferase (hydroxybenzoly-glucose dependent) activity [GO:0102507]; cyanidin 3-O-glucoside 7-O-glucosyltransferase (vanilloyl-glucose dependent)... | PF00232; | 3.20.20.80; | Glycosyl hydrolase 1 family | null | SUBCELLULAR LOCATION: Vacuole {ECO:0000269|PubMed:20971893}. | CATALYTIC ACTIVITY: Reaction=1-O-(4-hydroxy-3-methoxybenzoyl)-beta-D-glucose + cyanidin 3-O-beta-D-glucoside = cyanidin 3,7-di-O-beta-D-glucoside + vanillate; Xref=Rhea:RHEA:35431, ChEBI:CHEBI:16632, ChEBI:CHEBI:71512, ChEBI:CHEBI:71513, ChEBI:CHEBI:77857; EC=2.4.1.300; Evidence={ECO:0000269|PubMed:20971893}; | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=22.9 mM for cyanidin 3-glucopyranoside (at pH 5.0 and 30 degrees Celsius) {ECO:0000269|PubMed:20971893}; KM=260.8 mM for 1-O-beta-D-vanillyl-glucose (at pH 5.0 and 30 degrees Celsius) {ECO:0000269|PubMed:20971893}; Note=kcat is 0.17 sec(-1) with cyanidin 3-glucopyr... | PATHWAY: Pigment biosynthesis; anthocyanin biosynthesis. {ECO:0000269|PubMed:20971893}. | BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 6.0.; | BIOPHYSICOCHEMICAL PROPERTIES: Temperature dependence: Optimum temperature is 40 degrees Celsius. {ECO:0000269|PubMed:20971893}; | FUNCTION: Beta-glycosidase that catalyzes the transfer of glucose moiety to anthocyanidin 3-glucoside at the 7 position. Anthocyanins are ubiquitous colored pigments that are responsible for variations in petal color. {ECO:0000269|PubMed:20971893}. | Delphinium grandiflorum (Siberian larkspur) (Delphinium sinense) |
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