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 |
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B6ULW7 | BTDD_PAPAN | MRTFALLTAMLLLVALQAQAEARQARADEAAAQQQPGADDQGMAHSFTRPENAALPLSESAKGLRCFCRRGVCQLL | null | null | antibacterial humoral response [GO:0019731]; antimicrobial humoral immune response mediated by antimicrobial peptide [GO:0061844]; cellular response to lipopolysaccharide [GO:0071222]; defense response to fungus [GO:0050832]; defense response to Gram-negative bacterium [GO:0050829]; defense response to Gram-positive ba... | extracellular matrix [GO:0031012]; extracellular space [GO:0005615] | null | PF00879; | null | Alpha-defensin family, Theta subfamily | PTM: Forms a cyclic peptide with subunit A (BTD-7). An additional intersubunit disulfide bond is formed. {ECO:0000269|PubMed:18852242}. | null | null | null | null | null | null | FUNCTION: BTD-7 has antimicrobial activity against the Gram-negative bacterium E.coli ML35, the Gram-positive bacterium S.aureus 502a, and the fungus C.albicans 16820. {ECO:0000269|PubMed:18852242}. | Papio anubis (Olive baboon) |
B6V6V5 | KSHA4_RHORH | MTVPQERIEIRNIDPGTNPTRFARGWHCIGLAKDFRDGKPHQVKVFGTDLVVFADTAGKLHVLDAFCRHMGGNLARGEIKGDTIACPFHDWRWNGQGRCEAVPYARRTPKLGRTKAWTTMERNGVLFVWHCPQGSEPTPELAIPEIEGYEDGQWSDWTWTTIHVEGSHCREIVDNVVDMAHFFYVHFQMPEYFKNVFDGHIAGQHMRSYGRDDIKTGVQMDLPEAQTISDAFYYGPSFMLDTIYTVSEGTTIESKLINCHYPVTNNSFVLQFGTIVKKIEGMSEEQAAEMATMFTDGLEEQFAQDIEIWKHKSRIENPLL... | 1.14.15.30 | COFACTOR: Name=[2Fe-2S] cluster; Xref=ChEBI:CHEBI:190135; Evidence={ECO:0000255|PROSITE-ProRule:PRU00628, ECO:0000269|PubMed:19561185}; Note=Binds 1 [2Fe-2S] cluster per subunit. {ECO:0000255|PROSITE-ProRule:PRU00628, ECO:0000269|PubMed:19561185}; COFACTOR: Name=Fe cation; Xref=ChEBI:CHEBI:24875; Evidence={ECO:0000269|... | cholesterol metabolic process [GO:0008203]; lipid catabolic process [GO:0016042] | null | 2 iron, 2 sulfur cluster binding [GO:0051537]; 3-ketosteroid 9-alpha-monooxygenase activity [GO:0036200]; iron ion binding [GO:0005506] | PF19298;PF00355; | 2.102.10.10; | null | null | null | CATALYTIC ACTIVITY: Reaction=androsta-1,4-diene-3,17-dione + 2 H(+) + O2 + 2 reduced [2Fe-2S]-[ferredoxin] = 9alpha-hydroxyandrosta-1,4-diene-3,17-dione + H2O + 2 oxidized [2Fe-2S]-[ferredoxin]; Xref=Rhea:RHEA:32199, Rhea:RHEA-COMP:10000, Rhea:RHEA-COMP:10001, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, Ch... | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=10 uM for nordion {ECO:0000269|PubMed:19561185}; KM=23 uM for 5alpha-androstane-3,17-dione {ECO:0000269|PubMed:19561185}; KM=33 uM for 5beta-androstane-3,17-dione {ECO:0000269|PubMed:19561185}; | null | BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 7. {ECO:0000269|PubMed:19561185}; | BIOPHYSICOCHEMICAL PROPERTIES: Temperature dependence: Optimum temperature is 33 degrees Celsius. {ECO:0000269|PubMed:19561185}; | FUNCTION: In vitro, catalyzes the introduction of a 9alpha-hydroxyl moiety into the ring B of 3-ketosteroid substrates such as 1,4-androstadiene-3,17-dione (ADD), 4-androstene-3,17-dione (AD), 4-androstene-17beta-ol-3-one (testosterone), 4-pregnene-3,20-dione (progesterone), 19-nor-4-androstene-3,17-dione (nordion), 1-... | Rhodococcus rhodochrous |
B6V6V6 | KSHB_RHORH | MTTVEVPHGSRSVILTVSAVVEETADTRSIVFAVPDELRDKFAYRPGQFLTLRIPSDRTGSVARCYSLASSPFTDDAPKVTVKRTSDGYGSNWLCDNIATGQTLEVLPPAGVFTPKSLDHDFLLFGAGSGITPVISILKSALTQGGGKVVLVYANRDEKSVIFAEELRALAEKYPTRLTVVHWLESVQGLPTADQLAAIAAPYESYEAFMCGPGPFMDTVHQALNTVGMPRARVHAEVFNSLSGDPFADQAPVEVSDEDAADAATVEVELDGEVHKLSWPRKQTLVDIMLAKGIDVPYSCQEGECGSCACTVLEGKVEME... | 1.14.15.30 | COFACTOR: Name=FAD; Xref=ChEBI:CHEBI:57692; Evidence={ECO:0000269|PubMed:19561185}; Note=Binds 1 FAD per subunit. {ECO:0000269|PubMed:19561185}; COFACTOR: Name=[2Fe-2S] cluster; Xref=ChEBI:CHEBI:190135; Evidence={ECO:0000255|PROSITE-ProRule:PRU00465}; Note=Binds 1 2Fe-2S cluster. {ECO:0000255|PROSITE-ProRule:PRU00465}; | cholesterol catabolic process [GO:0006707] | null | 2 iron, 2 sulfur cluster binding [GO:0051537]; 3-ketosteroid 9-alpha-monooxygenase activity [GO:0036200]; FAD binding [GO:0071949]; metal ion binding [GO:0046872] | PF00970;PF00111;PF00175; | 3.10.20.30;3.40.50.80;2.40.30.10; | null | null | null | CATALYTIC ACTIVITY: Reaction=androsta-1,4-diene-3,17-dione + 2 H(+) + O2 + 2 reduced [2Fe-2S]-[ferredoxin] = 9alpha-hydroxyandrosta-1,4-diene-3,17-dione + H2O + 2 oxidized [2Fe-2S]-[ferredoxin]; Xref=Rhea:RHEA:32199, Rhea:RHEA-COMP:10000, Rhea:RHEA-COMP:10001, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, Ch... | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=10 uM for 19-nor-AD {ECO:0000269|PubMed:19561185}; KM=23 uM for 5alpha-androstane-3,17-dione {ECO:0000269|PubMed:19561185}; KM=33 uM for 5beta-androstane-3,17-dione {ECO:0000269|PubMed:19561185}; | PATHWAY: Steroid metabolism; cholesterol degradation. {ECO:0000305|PubMed:19561185}. | BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 7. {ECO:0000269|PubMed:19561185}; | BIOPHYSICOCHEMICAL PROPERTIES: Temperature dependence: Optimum temperature is 33 degrees Celsius. {ECO:0000269|PubMed:19561185}; | FUNCTION: Probably involved in the degradation of cholesterol. In vitro, catalyzes the introduction of a 9alpha-hydroxyl moiety into the ring B of 3-ketosteroid substrates such as 1,4-androstadiene-3,17-dione (ADD), 4-androstene-3,17-dione (AD), 4-androstene-17beta-ol-3-one (testosterone), 4-pregnene-3,20-dione (proges... | Rhodococcus rhodochrous |
B6V8E6 | CTNB1_CANLF | MATQADLMELDMAMEPDRKAAVSHWQQQSYLDSGIHSGATTTAPSLSGKGNPEEEDVDTTQVLYEWEQGFSQSFTQEQVADIDGQYAMTRAQRVRAAMFPETLDEGMQIPSTQFDAAHPTNVQRLAEPSQMLKHAVVNLINYQDDAELATRAIPELTKLLNDEDQVVVNKAAVMVHQLSKKEASRHAIMRSPQMVSAIVRTMQNTNDVETARCTAGTLHNLSHHREGLLAIFKSGGIPALVKMLGSPVDSVLFYAITTLHNLLLHQEGAKMAVRLAGGLQKMVALLNKTNVKFLAITTDCLQILAYGNQESKLIILASGG... | null | null | adherens junction assembly [GO:0034333]; bicellular tight junction assembly [GO:0070830]; canonical Wnt signaling pathway [GO:0060070]; cell adhesion [GO:0007155]; cell-cell adhesion [GO:0098609]; cellular response to growth factor stimulus [GO:0071363]; cellular response to indole-3-methanol [GO:0071681]; endothelial ... | adherens junction [GO:0005912]; beta-catenin destruction complex [GO:0030877]; beta-catenin-TCF7L2 complex [GO:0070369]; catenin complex [GO:0016342]; cell cortex [GO:0005938]; cell junction [GO:0030054]; cell periphery [GO:0071944]; cell projection [GO:0042995]; cell-cell junction [GO:0005911]; centrosome [GO:0005813]... | alpha-catenin binding [GO:0045294]; cadherin binding [GO:0045296]; DNA-binding transcription factor binding [GO:0140297]; protein phosphatase binding [GO:0019903]; RNA polymerase II-specific DNA-binding transcription factor binding [GO:0061629]; transcription coactivator activity [GO:0003713] | PF00514; | 1.25.10.10; | Beta-catenin family | PTM: Phosphorylation by GSK3B requires prior phosphorylation of Ser-45 by another kinase. Phosphorylation proceeds then from Thr-41 to Ser-33. Phosphorylated by NEK2. EGF stimulates tyrosine phosphorylation. Phosphorylated on Ser-33 and Ser-37 by HIPK2. This phosphorylation triggers proteasomal degradation. Phosphoryla... | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:P35222}. Nucleus {ECO:0000250|UniProtKB:P35222}. Cytoplasm, cytoskeleton {ECO:0000269|PubMed:10873669}. Cell junction, adherens junction {ECO:0000250|UniProtKB:Q02248}. Cell junction {ECO:0000269|PubMed:10873669}. Cell membrane {ECO:0000250|UniProtKB:P35222}. Cytop... | null | null | null | null | null | FUNCTION: Key downstream component of the canonical Wnt signaling pathway (By similarity). In the absence of Wnt, forms a complex with AXIN1, AXIN2, APC, CSNK1A1 and GSK3B that promotes phosphorylation on N-terminal Ser and Thr residues and ubiquitination of CTNNB1 via BTRC and its subsequent degradation by the proteas... | Canis lupus familiaris (Dog) (Canis familiaris) |
B6VQ60 | BRCA1_CAEEL | MADVALRITETVARLQKELKCGICCSTYKDPILSTCFHIFCRSCINACFERKRKVQCPICRSVLDKRSCRDTYQITMAVQNYLKLSEAFKKDIENMNTFKSLPPEKMFMESQMPLDITIIPENDGKRCAPDFAIPFLPVRRKRPSRPQPPSAFAEEPAEPVEPPEPATKQPVELQSRVFPLEKLKKDVETSTETYKISREELKNVDIEEYINTLRENSTEIDEIDALFQLMPTMRQFLRNNINQLMEKFHVAPPKKSEKPANRRVSFASSQDLENIKIMTASESLETPPEPIQKLAQKPEVFKSTQNLIDLNLNTAVKKP... | 2.3.2.27 | null | apoptotic process [GO:0006915]; cellular response to ionizing radiation [GO:0071479]; DNA damage response [GO:0006974]; DNA repair [GO:0006281]; double-strand break repair via homologous recombination [GO:0000724]; embryo development ending in birth or egg hatching [GO:0009792]; meiotic chromosome separation [GO:005130... | BRCA1-A complex [GO:0070531]; BRCA1-BARD1 complex [GO:0031436]; chromosome [GO:0005694]; cytoplasm [GO:0005737]; plasma membrane [GO:0005886] | metal ion binding [GO:0046872]; ubiquitin protein ligase activity [GO:0061630] | PF16589;PF13445; | 3.40.50.10190;3.30.40.10; | null | PTM: Phosphorylation of CeBCD complexes is required for E3 ubiquitin-protein ligase activity. {ECO:0000269|PubMed:16628214}. | SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:16628214, ECO:0000269|PubMed:30383754}. Chromosome {ECO:0000269|PubMed:16628214, ECO:0000269|PubMed:30383754}. Cytoplasm {ECO:0000269|PubMed:16628214}. Note=Mainly localizes to the nucleus and a small proportion is chromatin bound (PubMed:30383754). Co-localizes with br... | CATALYTIC ACTIVITY: Reaction=S-ubiquitinyl-[E2 ubiquitin-conjugating enzyme]-L-cysteine + [acceptor protein]-L-lysine = [E2 ubiquitin-conjugating enzyme]-L-cysteine + N(6)-ubiquitinyl-[acceptor protein]-L-lysine.; EC=2.3.2.27; Evidence={ECO:0000269|PubMed:16628214}; | null | PATHWAY: Protein modification; protein ubiquitination. {ECO:0000269|PubMed:16628214}. | null | null | FUNCTION: E3 ubiquitin-protein ligase that specifically mediates the formation of polyubiquitin chains and plays a central role in DNA repair (PubMed:16628214). Plays a role in triggering cellular responses at damage sites in response to DNA damage that may be induced by UV and ionizing radiation for example (PubMed:14... | Caenorhabditis elegans |
B6VQA1 | DIMM_DROME | MDATQLTELMGSHDFMQLQHQLHHNNNNYNTDGHNGLSSESAEGSSRPVRRATRRTSQLSNNTYDLEMTDSSSQSDDTSGGGGSSNGGGSTTNTGHPSGCSLGGQGPSGRGRVQQASSGACPSTIAPNSTSSNSSNANGNASRRRKGALNAKERNMRRLESNERERMRMHSLNDAFQSLREVIPHVEMERRLSKIETLTLAKNYIINLTHIILSKRNEEAAALELNSGAVGGVLLSNLSSESGGPVASGIPANSNAATICFEDTLASGGAFDCAILAATDGSLLNAATVTTSPAMQSIQSQAIHLQTPMEQQQQQASHLP... | null | null | axon development [GO:0061564]; neuroendocrine cell differentiation [GO:0061101]; neuron fate commitment [GO:0048663]; positive regulation of hormone secretion [GO:0046887]; positive regulation of peptide secretion [GO:0002793]; positive regulation of transcription by RNA polymerase II [GO:0045944]; regulation of DNA-te... | cytoplasm [GO:0005737]; nucleus [GO:0005634] | DNA-binding transcription factor activity [GO:0003700]; DNA-binding transcription factor activity, RNA polymerase II-specific [GO:0000981]; E-box binding [GO:0070888]; protein dimerization activity [GO:0046983] | PF00010; | 4.10.280.10; | null | null | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:16870731}. | null | null | null | null | null | FUNCTION: Transcription factor that regulates neurosecretory (NS) cell function and neuroendocrine cell fate. Acts as a master regulator of common NS functions such as Phm expression and neuropeptide production. Plays a role as a regulator of peptide-containing large dense-core vesicle (LDCV) production and peptidergic... | Drosophila melanogaster (Fruit fly) |
B6YWB8 | CAS10_THEON | MEIDELTALGGLLHDIGKPVQRAGLYSGDHSTQGARFLRDLAENTGRAEYELLSLFSEFHHKGHMKNDELMIRRIKELSPERFGLTMEDVLNALWIVYEADNLASGEREEGQPQASRPLYSVFNPGKAYPWAELDFEKELPVPGDVFSIRSQDYRELVKRLWEELSKAKLRSDRLLPVLEKYLTFVSSVTSEGNIISLYDHMRMTSAIALAMLRAGCTAEDVRSGRCRKEKRFLLIEGDFSGIQDFIYRVSGKGTLKYLRARSAYLELIGWDVVLEILSRLGLTRANVVFNAGGHFMIIAQNTPDAVKELEEIRAKAVEW... | 2.7.7.-; 3.1.-.- | COFACTOR: Name=a divalent metal cation; Xref=ChEBI:CHEBI:60240; Evidence={ECO:0000269|PubMed:25773141}; Note=Ni(2+) and Mn(2+), but not Mg(2+), Ca(2+), Zn(2+), Co(2+), or Cu(2+), is required for ssDNase activity. {ECO:0000269|PubMed:25773141}; | defense response to virus [GO:0051607] | null | ATP binding [GO:0005524]; endonuclease activity [GO:0004519]; exonuclease activity [GO:0004527]; identical protein binding [GO:0042802]; transferase activity [GO:0016740] | PF18211;PF01966; | 3.30.70.270; | CRISPR-associated Cas10/Csm1 family | null | null | null | null | null | null | null | FUNCTION: CRISPR (clustered regularly interspaced short palindromic repeat) is an adaptive immune system that provides protection against mobile genetic elements (viruses, transposable elements and conjugative plasmids). CRISPR clusters contain spacers, sequences complementary to antecedent mobile elements, and target ... | Thermococcus onnurineus (strain NA1) |
B6ZK72 | LSD19_STRLS | MPAETVRKEVALEYCRRVNAGELEGVLQLFAPDALLVDPLGTEPVVGRAALAARLAPALRGAVHEEPGRPYAAHDGTSVVLPATVTVGAPGAPPQRRGRTRVMGVIEVGEDGLIREMRVMWGVTDSSWTARPAPDEERRKELAREHCLRINDGDVDGLLKLYSPRIRFEDPVGSWTRTGLEALRAHATMAVGSNVRETAGLTVAGQDGRHAAVTVSATMDYLPSGPLLARHHLMTLPAPADPHRALIGIEYVMVIGVDADGLIDEMRAYWGATDVSLLDPAA | 5.5.1.- | null | antibiotic biosynthetic process [GO:0017000] | null | isomerase activity [GO:0016853] | PF12680; | 3.10.450.50; | null | null | null | null | null | null | null | null | FUNCTION: Epoxide hydrolase responsible for the double epoxide-opening cyclization of bisepoxyprelasalocid A to form lasalocid A, a polyether antibiotic. In vitro, accepts various substrate analogs differing in the left segment of lasalocid and epoxide stereochemistry to afford products with excellent regioselectivity.... | Streptomyces lasalocidi (Streptomyces lasaliensis) |
B6ZK77 | IRL1B_DANRE | MRSRVPLQILLYAAVIRSLKVVSKRGSVDGCTDWSVDYLRYRVLLGEPVRIKCALFYGYIRANYTHAQSAGLSLMWYRSATHTDHEEPITLDGTRTLKEEDALWFRPAQLQDSGHYSCVLRNSSYCMKVSMALTVAENSSGLCYNSKMRRLEKAELSKSKDILCPDIQDYTPAGSEPHVTWYKECRPKQWRSSIIRTADLLSIRDVREDDIGNYTCEIQFGRFLVRRTTELTVTAPLTDKPPKILQPPEHKLSVMELQLGGPVNLTCRAFFGYSGDVSPLIYWMKGEKFIEDLDETRIRESEIKMVREHLGEQEVSVSLT... | 3.2.2.6 | null | negative regulation of exocytosis [GO:0045920]; neuron remodeling [GO:0016322]; signal transduction [GO:0007165]; synapse organization [GO:0050808] | axon terminus [GO:0043679]; cytoplasm [GO:0005737]; neuronal cell body [GO:0043025]; plasma membrane [GO:0005886] | NAD+ nucleosidase activity [GO:0003953]; NAD+ nucleotidase, cyclic ADP-ribose generating [GO:0061809] | PF13927;PF18452;PF01582; | 2.60.40.10;3.40.50.10140; | Interleukin-1 receptor family | null | SUBCELLULAR LOCATION: Cell membrane {ECO:0000250}; Single-pass type I membrane protein {ECO:0000250}. Cytoplasm {ECO:0000250}. Note=May localize to the cell body and growth cones of dendrite-like processes. {ECO:0000269|PubMed:18657618}. | CATALYTIC ACTIVITY: Reaction=H2O + NAD(+) = ADP-D-ribose + H(+) + nicotinamide; Xref=Rhea:RHEA:16301, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:17154, ChEBI:CHEBI:57540, ChEBI:CHEBI:57967; EC=3.2.2.6; Evidence={ECO:0000255|PROSITE-ProRule:PRU00204}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:16302; Ev... | null | null | null | null | FUNCTION: May regulate secretion and presynaptic differentiation through inhibition of the activity of N-type voltage-gated calcium channel. During presynaptic differentiation may regulate both synaptic vesicle accumulation in axon terminals and subsequent axon terminal remodeling. {ECO:0000269|PubMed:18657618}. | Danio rerio (Zebrafish) (Brachydanio rerio) |
B6ZLK2 | CHD1_CHICK | MNGHSDEESVRNSSGESRSDDDSGSASGSGSGSSSGSSSDGSSSQSGSSDSESGSESGSQSESESDTSREKKQVQAKPPKADGSEFWKSSPSILAVQRSAVLKKQQQQQKAASSDSGSEEDSSSSEDSADDSSSETKKKKHKDEDWQMSGSGSVSGTGSDSESEEDGDKSSCEESESDYEPKNKVKSRKPPSRIKPKSGKKSTGQKKRQLDSSEEEEDDDEDYDKRGSRRQATVNVSYKEAEETKTDSDDLLEVCGEDVPQTEEDEFETIEKFMDSRIGRKGATGASTTIYAVEVDGDPNAGFEKSKELGEIQYLIKWKG... | 3.6.4.12 | null | nucleosome organization [GO:0034728]; regulation of transcription by RNA polymerase II [GO:0006357] | chromatin [GO:0000785]; chromosome, centromeric region [GO:0000775]; nucleus [GO:0005634] | ATP binding [GO:0005524]; ATP hydrolysis activity [GO:0016887]; ATP-dependent chromatin remodeler activity [GO:0140658]; chromatin binding [GO:0003682]; DNA binding [GO:0003677]; helicase activity [GO:0004386]; histone binding [GO:0042393] | PF18375;PF13907;PF00385;PF00271;PF00176; | 2.40.50.40;1.10.10.60;3.40.50.300;3.40.50.10810; | SNF2/RAD54 helicase family | null | SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:19625449}. Chromosome, centromere {ECO:0000269|PubMed:19625449}. | 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; | null | null | null | null | FUNCTION: ATP-dependent chromatin-remodeling factor which functions as substrate recognition component of the transcription regulatory histone acetylation (HAT) complex SAGA. Regulates polymerase II transcription. Also required for efficient transcription by RNA polymerase I, and more specifically the polymerase I tran... | Gallus gallus (Chicken) |
B7FAS6 | SAM10_CAEEL | MPPQVIQQQQQSLASEMTARDRLTSYIYEYLQQTGASKTAETFKEEVLSTNPAAGLAAANSTKLSDKSFLLEWWLLFWDLYSAAPERRDAGGDPFSAEAKYFHEAMIGMPPGMNGHFAPPPMGMEMMGGHPGAFGGRFAPGRMPPGAMAPGGMPPGAFPMFPPDPRLQRMAPNQGMRMPPPPVGQPFPGAVGMPRPVGPGAPMDMSGMQRFDFMGGPPPGGGAQPFPGASGSGGMMPNGAHPHMSLNSPSMGVPPADMPPFMGMPPMPPTSSSAMPFGMSSDHQPMSAGPAAAAPGATTAGGPGTPGMIGSVPGPGSVPQ... | null | null | branching morphogenesis of a nerve [GO:0048755]; negative regulation of gene expression [GO:0010629]; positive regulation of transcription by RNA polymerase II [GO:0045944]; regulation of protein localization to synapse [GO:1902473]; synapse assembly [GO:0007416] | cytoplasm [GO:0005737]; nucleus [GO:0005634] | null | null | null | null | null | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:21115607}. Nucleus {ECO:0000269|PubMed:21115607}. Note=In PLM neurons, translocates into the nucleus during the 3-fold embryonic stage and remains nuclear in the adult. Nuclear localization is idb-1-dependent. {ECO:0000269|PubMed:21115607}. | null | null | null | null | null | FUNCTION: Involved cell autonomously in PLM neuron pre-synaptic differentiation by negatively regulating prk-2 expression and in neurite branch positioning. {ECO:0000269|PubMed:21115607}. | Caenorhabditis elegans |
B7FDP2 | SCX39_CENSU | MNSLLMITACFFLIGTVWAKEGYLVNKSTGCKYGCLLLGKNEGCDKECKAKNQGGSYGYCYAFGCWCEGLPESTPTYPLPNKSCSKK | null | null | defense response [GO:0006952]; modulation of process of another organism [GO:0035821] | extracellular region [GO:0005576] | sodium channel inhibitor activity [GO:0019871]; toxin activity [GO:0090729] | PF00537; | 3.30.30.10; | Long (4 C-C) scorpion toxin superfamily, Sodium channel inhibitor family, Beta subfamily | null | SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:19631296}. | null | null | null | null | null | FUNCTION: Beta toxins bind voltage-independently at site-4 of sodium channels (Nav) and shift the voltage of activation toward more negative potentials thereby affecting sodium channel activation and promoting spontaneous and repetitive firing. This toxin is lethal to crustaceans (freshwater crayfish (Cambarellus monte... | Centruroides suffusus (Durango bark scorpion) |
B7FXW1 | SQLE_PHATC | MLVDRVENNEKQQQQMASSSDAMSDSSLSDDEIIEHVVHGKEPKSTYELSWVSNAIAWSGALVWPLMLTVPLLLSSMYSPISYRQVFPESWYVYDTLSNCAPKPLGLVLGILAVAVGQVFVWIFFYLFKFGYLGTDPRSIQSKGAREYIFREGLLTHIGQPEGFVLLIGYLAITWMLKLMPQSYYSFEGTIQYKELFMCLVLQDGIQYTMHVLEHIVSPAFYQMSHKPHHRFTNPRLFDAFNGSLMDTFCMIIIPLFVTANLVRHCNVWTYMAFGSSYACWLTLIHSEYVFPWDGIFRKLGLGTPADHHVHHKFFKFNYG... | 1.14.19.- | COFACTOR: Name=Fe cation; Xref=ChEBI:CHEBI:24875; Evidence={ECO:0000305|PubMed:30478288}; | cholesterol biosynthetic process via lathosterol [GO:0033490]; ergosterol biosynthetic process [GO:0006696]; sphingolipid biosynthetic process [GO:0030148]; sterol biosynthetic process [GO:0016126] | endoplasmic reticulum membrane [GO:0005789] | C-4 methylsterol oxidase activity [GO:0000254]; C-5 sterol desaturase activity [GO:0000248]; iron ion binding [GO:0005506]; monooxygenase activity [GO:0004497]; sphingolipid delta-4 desaturase activity [GO:0042284]; sphingosine hydroxylase activity [GO:0000170] | PF04116; | null | Sterol desaturase family | null | SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000269|PubMed:30478288}; Multi-pass membrane protein {ECO:0000255}. Note=Detected in the outer envelope of chloroplasts, which is termed the chloroplast endoplasmic reticulum and is continuous with the nuclear envelope. {ECO:0000269|PubMed:30478288}. | CATALYTIC ACTIVITY: Reaction=2 Fe(II)-[cytochrome b5] + 2 H(+) + O2 + squalene = (S)-2,3-epoxysqualene + 2 Fe(III)-[cytochrome b5] + H2O; Xref=Rhea:RHEA:58916, Rhea:RHEA-COMP:10438, Rhea:RHEA-COMP:10439, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, ChEBI:CHEBI:15440, ChEBI:CHEBI:15441, ChEBI:CHEBI:29033, Ch... | null | PATHWAY: Terpene metabolism; lanosterol biosynthesis; lanosterol from farnesyl diphosphate. {ECO:0000305|PubMed:30478288}. | null | null | FUNCTION: Catalyzes the stereospecific epoxidation of squalene at the terminal double bond to form (S)-2,3-epoxysqualene, the first oxygenation step in sterol biosynthesis. {ECO:0000269|PubMed:30478288}. | Phaeodactylum tricornutum (strain CCAP 1055/1) |
B7G620 | IDH1_PHATC | MSSLSTLRILHSTAGRRWASYYGIYPKSAACSSSSVAIARFFSTAADRPPKHAMLSVENKVVAPPMVYIAGEEMTRYACDLVVKSWLEPYFDLSQWEYFDLSCVNRDNTNDQVLRDAVTAGQRIGAIFKEPTITPSAIQKKAFGLKNSLGSPNGAMRAGWNGITISRDTIHIDGIELGYKRPVFFERHAVGGEYGAGWSKVGRGTLLTTYLPSDGRDPFVVDKRDLTDQHNVVVTYHNPYDNVEPLAHLFFQRCLDANITPYVVTKKTVFKWQEGFWAVMKDVFDEHYKSRFEEKGLLQACGGDLQHLISDAATMQLIRW... | 1.1.1.41 | COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000269|PubMed:32824636}; Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000269|PubMed:32824636}; Note=Binds 1 Mg(2+) or Mn(2+) ion per subunit. {ECO:0000250|UniProtKB:A0A096P8D3}; | isocitrate metabolic process [GO:0006102]; NAD metabolic process [GO:0019674]; NADP metabolic process [GO:0006739]; tricarboxylic acid cycle [GO:0006099] | cytosol [GO:0005829]; mitochondrion [GO:0005739]; peroxisome [GO:0005777] | calcium ion binding [GO:0005509]; identical protein binding [GO:0042802]; isocitrate dehydrogenase (NAD+) activity [GO:0004449]; isocitrate dehydrogenase (NADP+) activity [GO:0004450]; magnesium ion binding [GO:0000287]; protein homodimerization activity [GO:0042803] | PF00036;PF00180; | 1.10.238.10;3.40.718.10; | Isocitrate and isopropylmalate dehydrogenases family | null | SUBCELLULAR LOCATION: Mitochondrion {ECO:0000255, ECO:0000305|PubMed:32824636}. | CATALYTIC ACTIVITY: Reaction=D-threo-isocitrate + NAD(+) = 2-oxoglutarate + CO2 + NADH; Xref=Rhea:RHEA:23632, ChEBI:CHEBI:15562, ChEBI:CHEBI:16526, ChEBI:CHEBI:16810, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945; EC=1.1.1.41; Evidence={ECO:0000269|PubMed:32824636}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:23633; Ev... | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=903 uM for NAD(+) with Mg(2+) as cofactor (at pH 8.0 and 25 degrees Celsius) {ECO:0000269|PubMed:32824636}; KM=1132.5 uM for NAD(+) with Mn(2+) as cofactor (at pH 8.0 and 25 degrees Celsius) {ECO:0000269|PubMed:32824636}; Vmax=87.13 umol/min/mg enzyme with Mn(2+) a... | null | BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 8.0 with Mn(2+) as cofactor and 8.8 with Mg(2+) as cofactor. {ECO:0000269|PubMed:32824636}; | BIOPHYSICOCHEMICAL PROPERTIES: Temperature dependence: Optimum temperature is around 30 degrees Celsius with Mn(2+) as cofactor and 35 degrees Celsius with Mg(2+) as cofactor. Stable below 28 degrees Celsius, but rapidly loses activity above 30 degrees Celsius. Has 60% of maximal activity after 20-minute incubation at... | FUNCTION: Performs an essential role in the oxidative function of the tricarboxylic acid cycle and respiration (By similarity). Catalyzes the decarboxylation of isocitrate to produce 2-oxoglutarate and generate NADH to provide electrons for energy production. No activity with NADP(+) (PubMed:32824636). {ECO:0000250|Uni... | Phaeodactylum tricornutum (strain CCAP 1055/1) |
B7G6D3 | MCA3C_PHATC | MGFLRRQLREQFEKKKPEALQADIRMISGCQDVQTSADVSNVSSFQLPDPAGNAGGACTSTLLNVLYKDHQTPEDTMSFVELLNKMRENLEAKGFSQVPQLTASHPIDVNDDFDLVPPAATGTRRALLIGINYVGHEQGVLRGCHNDVKNMVEYIKAVHGFEDENITILMDDGEHTAPTHANMIAAYKKIVALSKADDALFCHFSGHGAKIRDDDRGEEDDGYDETLVPIDYHENGMIRDDDLYDILIKPLVQGVHLVCLMDCCHSGTVLDLPYVYKADGNFTEMEIDENFDFKKLLGKFGIDDFDKFGGEALGKINGDA... | 3.4.22.- | null | proteolysis [GO:0006508] | null | cysteine-type endopeptidase activity [GO:0004197]; metal ion binding [GO:0046872] | PF00656; | 3.40.50.12660; | Peptidase C14B family | PTM: Auto-proteolytic cleavage into a large and a small subunit which probably remain associated by non-covalent bonds. {ECO:0000269|PubMed:34566902}.; PTM: Following oxidative stress, the oxidation of Cys-202 leads to the formation of a disulfide bond between Cys-202 and Cys-259 which enhances catalytic activity. {ECO... | null | null | null | null | null | null | FUNCTION: Cysteine protease that cleaves specifically after arginine residues. {ECO:0000269|PubMed:34566902}. | Phaeodactylum tricornutum (strain CCAP 1055/1) |
B7IE18 | MURJ_THEAB | MSILFSSILFSIATFFSRILGLFRDVLFAKYFGVSYELDAYFIAIMFPFFLRKVFGEGAMSSAFVPLYSEKSGEEKDKFLSSVINGFSLIILALVILSYFFPELIINLFGAGSSHETKILAKKLLLITSPSIYFIFLWAISYSILNTNNKFFWPALTPSISNITIIIGTFLSTKYGIISPTIGFLIGSILMFFSIIKSIIKHKYYFTIKHFPHFLKLFFPTFMTMVVSQINTVVDMNVVSFYDKGSISYLQYASRFYLLPYGLFAVSVSTVVLSKISNDRKNFNYHLNDALKTTLFFTIPSMVGLIFLSTPIIRFFYEHG... | null | null | cell wall organization [GO:0071555]; lipid translocation [GO:0034204]; peptidoglycan biosynthetic process [GO:0009252]; regulation of cell shape [GO:0008360] | plasma membrane [GO:0005886] | lipid-linked peptidoglycan transporter activity [GO:0015648] | PF03023; | null | MurJ/MviN family | null | SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000255|HAMAP-Rule:MF_02078, ECO:0000269|PubMed:28024149}; Multi-pass membrane protein {ECO:0000255|HAMAP-Rule:MF_02078, ECO:0000269|PubMed:28024149}. | null | null | PATHWAY: Cell wall biogenesis; peptidoglycan biosynthesis. {ECO:0000255|HAMAP-Rule:MF_02078}. | null | null | FUNCTION: Involved in peptidoglycan biosynthesis. Transports lipid-linked peptidoglycan precursors from the inner to the outer leaflet of the cytoplasmic membrane. {ECO:0000255|HAMAP-Rule:MF_02078, ECO:0000305|PubMed:28024149}. | Thermosipho africanus (strain TCF52B) |
B7JBP8 | SQRD_ACIF2 | MAHVVILGAGTGGMPAAYEMKEALGSGHEVTLISANDYFQFVPSNPWVGVGWKERDDIAFPIRHYVERKGIHFIAQSAEQIDAEAQNITLADGNTVHYDYLMIATGPKLAFENVPGSDPHEGPVQSICTVDHAERAFAEYQALLREPGPIVIGAMAGASCFGPAYEYAMIVASDLKKRGMRDKIPSFTFITSEPYIGHLGIQGVGDSKGILTKGLKEEGIEAYTNCKVTKVEDNKMYVTQVDEKGETIKEMVLPVKFGMMIPAFKGVPAVAGVEGLCNPGGFVLVDEHQRSKKYANIFAAGIAIAIPPVETTPVPTGAPK... | 1.8.5.4 | COFACTOR: Name=FAD; Xref=ChEBI:CHEBI:57692; Evidence={ECO:0000269|PubMed:20303979, ECO:0000269|PubMed:22542586}; Note=Binds 1 FAD per subunit. {ECO:0000269|PubMed:20303979, ECO:0000269|PubMed:22542586}; | null | membrane [GO:0016020] | nucleotide binding [GO:0000166]; quinone binding [GO:0048038]; sulfide:quinone oxidoreductase activity [GO:0070224] | PF07992; | 3.50.50.100; | SQRD family | null | SUBCELLULAR LOCATION: Membrane {ECO:0000303|PubMed:20303979}; Peripheral membrane protein {ECO:0000303|PubMed:20303979}. | CATALYTIC ACTIVITY: Reaction=n a quinone + n H(+) + n hydrogen sulfide = n a quinol + n sulfur; Xref=Rhea:RHEA:30239, ChEBI:CHEBI:15378, ChEBI:CHEBI:24646, ChEBI:CHEBI:26833, ChEBI:CHEBI:29919, ChEBI:CHEBI:132124; EC=1.8.5.4; Evidence={ECO:0000269|PubMed:20303979, ECO:0000269|PubMed:22542586}; | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=2.8 uM for sodium sulfide {ECO:0000269|PubMed:20303979}; KM=22 uM for decylubiquinone {ECO:0000269|PubMed:20303979}; | null | null | null | FUNCTION: Catalyzes the oxidation of hydrogen sulfide, with the help of a quinone. Consecutive reaction cycles lead to the accumulation of a polysulfide product on the active site Cys residues; these products are released when they exceed a critical length, typically as cyclooctasulfur. {ECO:0000269|PubMed:20303979, EC... | Acidithiobacillus ferrooxidans (strain ATCC 23270 / DSM 14882 / CIP 104768 / NCIMB 8455) (Ferrobacillus ferrooxidans (strain ATCC 23270)) |
B7L8Y4 | HCHA_ECO55 | MTVQTSKNPQVDIAEDNAFFPSEYSLSQYTSPVSDLDGVDYPKPYRGKHKILVIAADERYLPTDNGKLFSTGNHPIETLLPLYHLHAAGFEFEVATISGLMTKFEYWAMPHKDEKVMPFFEQHKSLFRNPKKLADVVASLNADSEYAAIFVPGGHGTLIGLPESQDVAAALQWAIKNDRFVISLCHGPAAFLALRHGDNPLNGYSICAFPDAADKQTPEIGYMPGHLTWYFGEELKKMGMNIINDDITGRVHKDRKLLTGDSPFAANALGKLAAQEMLAAYAG | 3.1.2.-; 3.5.1.-; 3.5.1.124 | null | DNA repair [GO:0006281]; methylglyoxal catabolic process to D-lactate via S-lactoyl-glutathione [GO:0019243]; protein repair [GO:0030091] | cytoplasm [GO:0005737] | glyoxalase III activity [GO:0019172]; protein deglycase activity [GO:0036524]; thiolester hydrolase activity [GO:0016790]; zinc ion binding [GO:0008270] | null | 3.40.50.880; | Peptidase C56 family, HchA subfamily | null | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_01046}. | CATALYTIC ACTIVITY: Reaction=H2O + N(omega)-(1-hydroxy-2-oxopropyl)-L-arginyl-[protein] = H(+) + L-arginyl-[protein] + lactate; Xref=Rhea:RHEA:49548, Rhea:RHEA-COMP:10532, Rhea:RHEA-COMP:12428, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:24996, ChEBI:CHEBI:29965, ChEBI:CHEBI:131708; EC=3.5.1.124; Evidence={ECO:00... | null | null | null | null | FUNCTION: Protein and nucleotide deglycase that catalyzes the deglycation of the Maillard adducts formed between amino groups of proteins or nucleotides and reactive carbonyl groups of glyoxals. Thus, functions as a protein deglycase that repairs methylglyoxal- and glyoxal-glycated proteins, and releases repaired prote... | Escherichia coli (strain 55989 / EAEC) |
B7M3A5 | HCHA_ECO8A | MTVQKSKNPQVDIAEDNAFFPSEYSLSQYTSPVSDLDGVDYPKPYRGKHKILVIAADERYLPTDNGKLFSTGNHPIETLLPLYHLHAAGFEFEVATISGLMTKFEYWAMPHKDEKVMPFFEQHKSLFRNPKKLADVVASLNADSEYAAIFVPGGHGALIGLPESQDVAAALQWAIKNDRFVISLCHGPAAFLALRHGDNPLNGYSICAFPDAADKQTPEIGYMPGHLTWYFGEELKKMGMNIINDDIAGRVHKDRKVLTGDSPFAANALGKLAAQEMLAAYAG | 3.1.2.-; 3.5.1.-; 3.5.1.124 | null | DNA repair [GO:0006281]; methylglyoxal catabolic process to D-lactate via S-lactoyl-glutathione [GO:0019243]; protein repair [GO:0030091] | cytoplasm [GO:0005737] | glyoxalase III activity [GO:0019172]; protein deglycase activity [GO:0036524]; thiolester hydrolase activity [GO:0016790]; zinc ion binding [GO:0008270] | null | 3.40.50.880; | Peptidase C56 family, HchA subfamily | null | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_01046}. | CATALYTIC ACTIVITY: Reaction=H2O + N(omega)-(1-hydroxy-2-oxopropyl)-L-arginyl-[protein] = H(+) + L-arginyl-[protein] + lactate; Xref=Rhea:RHEA:49548, Rhea:RHEA-COMP:10532, Rhea:RHEA-COMP:12428, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:24996, ChEBI:CHEBI:29965, ChEBI:CHEBI:131708; EC=3.5.1.124; Evidence={ECO:00... | null | null | null | null | FUNCTION: Protein and nucleotide deglycase that catalyzes the deglycation of the Maillard adducts formed between amino groups of proteins or nucleotides and reactive carbonyl groups of glyoxals. Thus, functions as a protein deglycase that repairs methylglyoxal- and glyoxal-glycated proteins, and releases repaired prote... | Escherichia coli O8 (strain IAI1) |
B7MCM0 | HCHA_ECO45 | MTVQKSKNPQVDIAEDNAFFPSEYSLSQYTSPVSDLDGVDYPKPYRGKHKILVIAADERYLPTDNGKLFSTGNHPIETLLPLYHLHAAGFEFEVATISGLMTKFEYWAMPHKDEKVMPFFEQHKSLFRNPKKLADVVASLNADSEYAAIFVPGGHGALIGLPESEDVAAALQWAIENDRFVISLCHGPAAFLALRHGDNPLNGYSICAFPDAADKQTPEIGYMPGHLTWYFGEELKKMGMNIINDDITGRVHKDRKVLTGDSPFAANALGKLAAQEMLAAYAG | 3.1.2.-; 3.5.1.-; 3.5.1.124 | null | DNA repair [GO:0006281]; methylglyoxal catabolic process to D-lactate via S-lactoyl-glutathione [GO:0019243]; protein repair [GO:0030091] | cytoplasm [GO:0005737] | glyoxalase III activity [GO:0019172]; protein deglycase activity [GO:0036524]; thiolester hydrolase activity [GO:0016790]; zinc ion binding [GO:0008270] | null | 3.40.50.880; | Peptidase C56 family, HchA subfamily | null | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_01046}. | CATALYTIC ACTIVITY: Reaction=H2O + N(omega)-(1-hydroxy-2-oxopropyl)-L-arginyl-[protein] = H(+) + L-arginyl-[protein] + lactate; Xref=Rhea:RHEA:49548, Rhea:RHEA-COMP:10532, Rhea:RHEA-COMP:12428, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:24996, ChEBI:CHEBI:29965, ChEBI:CHEBI:131708; EC=3.5.1.124; Evidence={ECO:00... | null | null | null | null | FUNCTION: Protein and nucleotide deglycase that catalyzes the deglycation of the Maillard adducts formed between amino groups of proteins or nucleotides and reactive carbonyl groups of glyoxals. Thus, functions as a protein deglycase that repairs methylglyoxal- and glyoxal-glycated proteins, and releases repaired prote... | Escherichia coli O45:K1 (strain S88 / ExPEC) |
B7MWF3 | HCHA_ECO81 | MTVQTSKNPQVDIAEDNAFFPSEYSLSQYTSPVSDLDGVDYPKPYRGKHKILVIAADERYLPTDNGKLFSTGNHPIETLLPLYHLHAAGFEFEVATISGLMTKFEYWAMPHKDEKVMPFFEQHKSLFRNPKKLADVVASLNADSEYAAIFVPGGHGALIGLPESQDVAAALQWAIKNDRFVISLCHGPAAFLALRHGDNPLNGYSICAFPDAADKQTPEIGYMPGHLTWYFGEELKKMGMNIINDDITGRVHKDRKVLTGDSPFAANALGKLAAQEMLAAYAG | 3.1.2.-; 3.5.1.-; 3.5.1.124 | null | DNA repair [GO:0006281]; methylglyoxal catabolic process to D-lactate via S-lactoyl-glutathione [GO:0019243]; protein repair [GO:0030091] | cytoplasm [GO:0005737] | glyoxalase III activity [GO:0019172]; protein deglycase activity [GO:0036524]; thiolester hydrolase activity [GO:0016790]; zinc ion binding [GO:0008270] | null | 3.40.50.880; | Peptidase C56 family, HchA subfamily | null | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_01046}. | CATALYTIC ACTIVITY: Reaction=H2O + N(omega)-(1-hydroxy-2-oxopropyl)-L-arginyl-[protein] = H(+) + L-arginyl-[protein] + lactate; Xref=Rhea:RHEA:49548, Rhea:RHEA-COMP:10532, Rhea:RHEA-COMP:12428, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:24996, ChEBI:CHEBI:29965, ChEBI:CHEBI:131708; EC=3.5.1.124; Evidence={ECO:00... | null | null | null | null | FUNCTION: Protein and nucleotide deglycase that catalyzes the deglycation of the Maillard adducts formed between amino groups of proteins or nucleotides and reactive carbonyl groups of glyoxals. Thus, functions as a protein deglycase that repairs methylglyoxal- and glyoxal-glycated proteins, and releases repaired prote... | Escherichia coli O81 (strain ED1a) |
B7NBV8 | HCHA_ECOLU | MTVQTSKNPQVDIAEDNAFFPSEYSLSQYTSPVSDLDGVDYPKPYRGKHKILVIAADERYLPTDNGKLFSTGNHPIETLLPLYHLHAAGFEFEVATISGLMTKFEYWAMPHKDEKVMPFFEQHKSLFRNPKKLADVVASLNADSEYAAIFVPGGHGALIGLPESQDVAAALQWAIKNDRFVISLCHGPAAFLALRHGDNPLNGYSICAFPDAADKQTPEIGYMPGHLTWYFGEELKKMGMNIINDDITGRVHKDRKVLTGDSPFAANALGKLAAQEMLAAYAG | 3.1.2.-; 3.5.1.-; 3.5.1.124 | null | DNA repair [GO:0006281]; methylglyoxal catabolic process to D-lactate via S-lactoyl-glutathione [GO:0019243]; protein repair [GO:0030091] | cytoplasm [GO:0005737] | glyoxalase III activity [GO:0019172]; protein deglycase activity [GO:0036524]; thiolester hydrolase activity [GO:0016790]; zinc ion binding [GO:0008270] | null | 3.40.50.880; | Peptidase C56 family, HchA subfamily | null | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_01046}. | CATALYTIC ACTIVITY: Reaction=H2O + N(omega)-(1-hydroxy-2-oxopropyl)-L-arginyl-[protein] = H(+) + L-arginyl-[protein] + lactate; Xref=Rhea:RHEA:49548, Rhea:RHEA-COMP:10532, Rhea:RHEA-COMP:12428, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:24996, ChEBI:CHEBI:29965, ChEBI:CHEBI:131708; EC=3.5.1.124; Evidence={ECO:00... | null | null | null | null | FUNCTION: Protein and nucleotide deglycase that catalyzes the deglycation of the Maillard adducts formed between amino groups of proteins or nucleotides and reactive carbonyl groups of glyoxals. Thus, functions as a protein deglycase that repairs methylglyoxal- and glyoxal-glycated proteins, and releases repaired prote... | Escherichia coli O17:K52:H18 (strain UMN026 / ExPEC) |
B7NRB5 | HCHA_ECO7I | MTVQTSKNPQVDIAEDNAFFPSEYSLSQYTSPVSDLDGVDYPKPYRGKHKILVIAADERYLPTDNGKLFSTGNHPIETLLPLYHLHAAGFEFEVATISGLMTKFEYWAMPHKDEKVMPFFEQHKSLFRNPKKLADVVASLNADSEYAAIFVPGGHGALIGLPESQDVAAALQWAIKNDRFVISLCHGPAAFLALRHSDNPLNGYSICAFPDAADKQTPDIGYMPGHLTWYFGEELKKMGMNIINDDITGRVHKDRKLLTGDSPFAANALGKLAAQEMLAAYAS | 3.1.2.-; 3.5.1.-; 3.5.1.124 | null | DNA repair [GO:0006281]; methylglyoxal catabolic process to D-lactate via S-lactoyl-glutathione [GO:0019243]; protein repair [GO:0030091] | cytoplasm [GO:0005737] | glyoxalase III activity [GO:0019172]; protein deglycase activity [GO:0036524]; thiolester hydrolase activity [GO:0016790]; zinc ion binding [GO:0008270] | null | 3.40.50.880; | Peptidase C56 family, HchA subfamily | null | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_01046}. | CATALYTIC ACTIVITY: Reaction=H2O + N(omega)-(1-hydroxy-2-oxopropyl)-L-arginyl-[protein] = H(+) + L-arginyl-[protein] + lactate; Xref=Rhea:RHEA:49548, Rhea:RHEA-COMP:10532, Rhea:RHEA-COMP:12428, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:24996, ChEBI:CHEBI:29965, ChEBI:CHEBI:131708; EC=3.5.1.124; Evidence={ECO:00... | null | null | null | null | FUNCTION: Protein and nucleotide deglycase that catalyzes the deglycation of the Maillard adducts formed between amino groups of proteins or nucleotides and reactive carbonyl groups of glyoxals. Thus, functions as a protein deglycase that repairs methylglyoxal- and glyoxal-glycated proteins, and releases repaired prote... | Escherichia coli O7:K1 (strain IAI39 / ExPEC) |
B7QK46 | QPCT_IXOSC | MLFPVLLLLKLVIGALIIDASALSWHDLKWPRDLRPLAHHDLLYMGQISEEDRGDFNATLRNFLVPRVVGSQKHREVREFIVRSLKDLDWDVEEDCFDGQTPHGIKPFCNVIATLNPSACHRLVLACHYDSLLHKEGTFIGATDSAVPCAQLLYLARSLNGKLQNQKTRGDGLTLQLVFFDGEEAFERWSSHDSLYGSRHLAQKWHEDRTSAERLESCLERSEIANQIDRMEVMVLLDLLGAENPRFYSYFGETQPVYRRLVNIESRLNDAGLMELPRRRRRTNYFSNSSTVGFIEDDHIPFLKRSVPIVHIIPSPFPDV... | 2.3.2.5 | null | peptidyl-pyroglutamic acid biosynthetic process, using glutaminyl-peptide cyclotransferase [GO:0017186] | extracellular region [GO:0005576] | glutaminyl-peptide cyclotransferase activity [GO:0016603]; zinc ion binding [GO:0008270] | PF04389; | 3.40.630.10; | Glutaminyl-peptide cyclotransferase family | null | SUBCELLULAR LOCATION: Secreted {ECO:0000305}. | CATALYTIC ACTIVITY: Reaction=N-terminal L-glutaminyl-[peptide] = N-terminal 5-oxo-L-prolyl-[peptide] + NH4(+); Xref=Rhea:RHEA:23652, Rhea:RHEA-COMP:11736, Rhea:RHEA-COMP:11846, ChEBI:CHEBI:28938, ChEBI:CHEBI:64722, ChEBI:CHEBI:87215; EC=2.3.2.5; Evidence={ECO:0000269|PubMed:23770496, ECO:0000269|PubMed:24598748}; | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=21.8 uM for L-glutaminyl 2-naphthylamide (Gln-beta-NA) (in the presence of Zn(2+), at 25 degrees Celsius) {ECO:0000269|PubMed:24598748}; KM=8.8 uM for L-glutaminyl 2-naphthylamide (Gln-beta-NA) (in the absence of Zn(2+), at 25 degrees Celsius) {ECO:0000269|PubMed:2... | null | null | null | FUNCTION: Responsible for the biosynthesis of pyroglutamyl peptides (PubMed:23770496, PubMed:24598748). Seems to have a preference for substrates with neutral or hydrophobic amino-acid residues at the second and third positions (PubMed:24598748). Shows activity towards the peptides [Gln-1]-corazonin, [Gln-1]-periviscer... | Ixodes scapularis (Black-legged tick) (Deer tick) |
B7S4N9 | VKT_OXYSC | MSSGGLLLLLGLLTLWEVLTPVSSKDRPKFCHLPPKPGPCRAAIPRFYYNPHSKQCEKFIYGGCHGNANSFKTPDECNYTCLGVSLPK | null | null | null | extracellular space [GO:0005615] | calcium channel regulator activity [GO:0005246]; potassium channel regulator activity [GO:0015459]; serine-type endopeptidase inhibitor activity [GO:0004867]; toxin activity [GO:0090729] | PF00014; | 4.10.410.10; | Venom Kunitz-type family | null | SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:1485334}. | null | null | null | null | null | FUNCTION: Heterotrimer: blocks the voltage-dependent L-type calcium channels (Cav) from the heart, and the small conductance calcium-activated potassium channels (KCa) in the chromaffin cells and in the brain. Is very toxic to mice.; FUNCTION: Monomer: serine protease inhibitor that inhibits plasma kallikrein (Ki=0.057... | Oxyuranus scutellatus scutellatus (Australian taipan) (Coastal taipan) |
B7SBD2 | TOX3_RAT | MDVRFYPAAAGDPAGLDFAQCLGYYGYSKLGNNNYMNMAEANNAFFAASEQTFHTPSLGDEEFEIPPITPPPESDPTLGMPDVLLPFQTLSDPLPSQGNEFTPQFPPQSLDLPSITISRNLVEQDGVLHSNGLHMDQSHTQVSQYRQDPSLVMRSIVHMTDAARSGIMPPAQLTTINQSQLSAQLGLNLGGASVPHTSPSPPASKSATPSPSSSINEEDADETNRAVGEKRTAPDSGKKPKTPKKKKKKDPNEPQKPVSAYALFFRDTQAAIKGQNPNATFGEVSKIVASMWDSLGEEQKQVYKRKTEAAKKEYLKALAA... | null | null | apoptotic process [GO:0006915]; calcium-mediated signaling [GO:0019722]; negative regulation of neuron apoptotic process [GO:0043524]; positive regulation of DNA-templated transcription [GO:0045893]; positive regulation of transcription by RNA polymerase II [GO:0045944]; regulation of apoptotic process [GO:0042981]; re... | nucleus [GO:0005634] | chromatin binding [GO:0003682]; chromatin DNA binding [GO:0031490]; phosphoprotein binding [GO:0051219]; protein homodimerization activity [GO:0042803]; transcription coactivator activity [GO:0003713] | PF00505; | 1.10.30.10; | null | null | SUBCELLULAR LOCATION: Nucleus {ECO:0000305}. | null | null | null | null | null | FUNCTION: Transcriptional coactivator of the p300/CBP-mediated transcription complex. Activates transactivation through cAMP response element (CRE) sites. Protects against cell death by inducing antiapoptotic and repressing pro-apoptotic transcripts. Stimulates transcription from the estrogen-responsive or BCL-2 promot... | Rattus norvegicus (Rat) |
B7SXM5 | IER2_DANRE | MDVTAEAKQIMVQALGKMYSSRSQRGGLRLHRSLLLTLVMKSARDIYHSARLMSEKSGQSVTEECTSHTQEPMDTSSSTATPLRETSGQSSEDGQRSGLEGHPHPLNPAADKENCGPSRPDRHSRKRRSKTATDSDFIPCKKAKLECAEVRGVLQNSSANCGRALDSLSLVPMPRTIVTF | null | null | cilium assembly [GO:0060271]; convergent extension [GO:0060026]; determination of left/right symmetry [GO:0007368]; Kupffer's vesicle development [GO:0070121] | cytoplasm [GO:0005737]; nucleus [GO:0005634] | null | PF05760; | null | IER family | null | SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:19164561}. Cytoplasm {ECO:0000250|UniProtKB:Q9BTL4}. | null | null | null | null | null | FUNCTION: DNA-binding protein that seems to act as a transcription factor (By similarity). Mediates with FIBPB FGF-signaling in Kupffer's vesicle ciliogenesis and in the establishment of laterality in the embryo (PubMed:19164561). {ECO:0000250|UniProtKB:Q9BTL4, ECO:0000269|PubMed:19164561}. | Danio rerio (Zebrafish) (Brachydanio rerio) |
B7TB45 | SPZ2_DROME | MKAGRAFGCLFWALLYCVLYLDLVSGNSADDELMDFDFADSNDAAMEDWQLDDLEEAKKAEQAEKKLESNMLDFSVDLDEPEPEKQLPPFDWRERVLRNALAKALADEGLRQKFAEVLPILRMLSSQQRLALSALISAQMNAKKGHELKFEQVRMMFGNEKKLLLPIVFDIANLIKSSTRKYINLGSDLASSALYHTPINRREDDLTPEESQQDDQLGTIAVEVEPKKVSTEEVQLESLEDFFDEMGSEVLDPQMINEALTGDLHDNKTKTFKPENHGQRVRRSANEFVHKLTRSVPASVTEQQLLGGIAGRTIKLNTTA... | null | null | central nervous system formation [GO:0021556]; innate immune response [GO:0045087]; motor neuron axon guidance [GO:0008045]; negative regulation of neuron apoptotic process [GO:0043524]; regulation of neuronal synaptic plasticity in response to neurotrophin [GO:0031637]; Toll signaling pathway [GO:0008063] | extracellular region [GO:0005576]; extracellular space [GO:0005615] | growth factor activity [GO:0008083]; receptor ligand activity [GO:0048018]; Toll binding [GO:0005121] | PF16077; | 2.10.90.10; | null | null | null | null | null | null | null | null | FUNCTION: Neurotrophin which may function as a ligand for the Toll-related receptors Toll-7 and Tollo (PubMed:22022271, PubMed:23892553). Binds to Toll-7 and probably acts as its ligand in promoting motor axon targeting and neuronal survival in the central nervous system (CNS) (PubMed:23892553). Involved in synaptic ta... | Drosophila melanogaster (Fruit fly) |
B7U179 | ABAP1_ARATH | MIISKSFKAPLKFSVKSSTAPVISNHPPMENHPKRQRTTRLAARNLKRKLSHNTDGAPIVTQLIDIDDEPIDLVVAIRRHVEVLNSSFSDPDFDHEAVKEAAADIADLAKIDENVEIIVENGAIPALVRYLESPLVVCGNVPKSCEHKLEKDCALALGLIAAIQPGYQQLIVDAGAIVPTVKLLKRRGECGECMFANAVIRRAADIITNIAHDNPRIKTNIRVEGGIAPLVELLNFPDVKVQRAAAGALRTVSFRNDENKSQIVELNALPTLVLMLQSQDSTVHGEAIGAIGNLVHSSPDIKKEVIRAGALQPVIGLLSS... | null | null | DNA-templated DNA replication [GO:0006261]; negative regulation of cell population proliferation [GO:0008285]; negative regulation of DNA-templated DNA replication [GO:2000104]; protein ubiquitination [GO:0016567]; regulation of cell population proliferation [GO:0042127] | DNA replication preinitiation complex [GO:0031261]; nucleus [GO:0005634] | null | PF00514;PF00651; | 1.25.10.10; | null | null | SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:18818695}. | null | null | PATHWAY: Protein modification; protein ubiquitination. | null | null | FUNCTION: May act as a substrate-specific adapter of an E3 ubiquitin-protein ligase complex (CUL3-RBX1-BTB) which mediates the ubiquitination and subsequent proteasomal degradation of target proteins (By similarity). In association with TCP24, exerts a negative role in cell proliferation in leaves, possibly by inhibiti... | Arabidopsis thaliana (Mouse-ear cress) |
B7U540 | KCJ18_HUMAN | MTAASRANPYSIVSLEEDGLHLVTMSGANGFGNGKVHTRRRCRNRFVKKNGQCNIAFANMDEKSQRYLADMFTTCVDIRWRYMLLIFSLAFLASWLLFGVIFWVIAVAHGDLEPAEGHGRTPCVMQVHGFMAAFLFSIETQTTIGYGLRCVTEECLVAVFMVVAQSIVGCIIDSFMIGAIMAKMARPKKRAQTLLFSHNAVVALRDGKLCLMWRVGNLRKSHIVEAHVRAQLIKPRVTEEGEYIPLDQIDIDVGFDKGLDRIFLVSPITILHEIDEASPLFGISRQDLETDDFEIVVILEGMVEATAMTTQARSSYLANE... | 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] | inward rectifier potassium channel activity [GO:0005242] | PF01007;PF17655;PF08466; | 1.10.287.70;2.60.40.1400; | Inward rectifier-type potassium channel (TC 1.A.2.1) family, KCNJ12 subfamily | PTM: Probably phosphorylated by PKC; decreases single-channel open probability. {ECO:0000269|PubMed:20074522}. | SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:21665951}; Multi-pass membrane protein {ECO:0000255}. | null | null | null | null | null | FUNCTION: Inward rectifier potassium channels are characterized by a greater tendency to allow potassium to flow into the cell rather than out of it. Their voltage dependence is regulated by the concentration of extracellular potassium; as external potassium is raised, the voltage range of the channel opening shifts to... | Homo sapiens (Human) |
B7UI21 | NLEB1_ECO27 | MLSSLNVLQSSFRGKTALSNSTLLQKVSFAGKEYSLEPIDERTPILFQWFEARPERYEKGEVPILNTKEHPYLSNIINAAKIENERIIGVLVDGNFTYEQKKEFLNLENEHQNIKIIYRADVDFSMYDKKLSDIYLENIHKQESYPASERDNYLLGLLREELKNIPEGKDSLIESYAEKREHTWFDFFRNLAILKAGSLFTETGKTGCHNISPCSGCIYLDADMIITDKLGVLYAPDGIAVHVDCNDEIKSLENGAIVVNRSNHPALLAGLDIMKSKVDAHPYYDGLGKGIKRHFNYSSLHNYNAFCDFIEFKHENIIPN... | 2.4.1.- | COFACTOR: Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000269|PubMed:23955153, ECO:0000269|PubMed:24025841, ECO:0000269|PubMed:30979585}; | symbiont-mediated suppression of host defense-related programmed cell death [GO:0034054]; symbiont-mediated suppression of host NF-kappaB cascade [GO:0085034] | extracellular region [GO:0005576]; host cell cytoplasm [GO:0030430] | manganese ion binding [GO:0030145]; protein-arginine N-acetylglucosaminyltransferase activity [GO:0106362]; toxin activity [GO:0090729] | null | null | Glycosyltransferase NleB family | PTM: Auto-glycosylated: arginine GlcNAcylation is required for activity toward death domain-containing host target proteins. {ECO:0000269|PubMed:32432056}. | SUBCELLULAR LOCATION: Secreted {ECO:0000250|UniProtKB:A0A482PDI9}. Host cytoplasm {ECO:0000269|PubMed:32432056}. Note=Secreted via the type III secretion system (T3SS). {ECO:0000250|UniProtKB:A0A482PDI9}. | CATALYTIC ACTIVITY: Reaction=L-arginyl-[protein] + UDP-N-acetyl-alpha-D-glucosamine = H(+) + N(omega)-(N-acetyl-beta-D-glucosaminyl)-L-arginyl-[protein] + UDP; Xref=Rhea:RHEA:66632, Rhea:RHEA-COMP:10532, Rhea:RHEA-COMP:17079, ChEBI:CHEBI:15378, ChEBI:CHEBI:29965, ChEBI:CHEBI:57705, ChEBI:CHEBI:58223, ChEBI:CHEBI:167322... | null | null | null | null | FUNCTION: Protein-arginine N-acetylglucosaminyltransferase effector that disrupts TNF signaling in infected cells, including NF-kappa-B signaling, apoptosis and necroptosis (PubMed:20126447, PubMed:20485572, PubMed:22144899, PubMed:23955153, PubMed:24025841, PubMed:28138023, PubMed:28522607, PubMed:30979585). Acts by c... | Escherichia coli O127:H6 (strain E2348/69 / EPEC) |
B7UI22 | NLEE_ECO27 | MINPVTNTQGVSPINTKYAEHVVKNIYPKIKHDYFNESPNIYDKKYISGITRGVAELKQEEFVNEKARRFSYMKTMYSVCPEAFEPISRNEASTPEGSWLTVISGKRPMGQFSVDSLYNPDLHALCELPDICCKIFPKENNDFLYIVVVYRNDSPLGEQRANRFIELYNIKRDIMQELNYELPELKAVKSEMIIAREMGEIFSYMPGEIDSYMKYINNKLSKIE | 2.1.1.- | null | methylation [GO:0032259]; symbiont-mediated suppression of host NF-kappaB cascade [GO:0085034] | extracellular region [GO:0005576]; host cell nucleus [GO:0042025] | protein-cysteine methyltransferase activity [GO:0106363]; toxin activity [GO:0090729] | PF20798; | null | NleE/OspZ family | null | SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:17984206}. Host nucleus {ECO:0000269|PubMed:17984206}. Note=Secreted via the type III secretion system (T3SS) (PubMed:17984206). Localizes in the nucleus of the infected cells (PubMed:17984206). {ECO:0000269|PubMed:17984206}. | CATALYTIC ACTIVITY: Reaction=L-cysteinyl-[protein] + S-adenosyl-L-methionine = H(+) + S-adenosyl-L-homocysteine + S-methyl-L-cysteinyl-[protein]; Xref=Rhea:RHEA:66544, Rhea:RHEA-COMP:10131, Rhea:RHEA-COMP:10132, ChEBI:CHEBI:15378, ChEBI:CHEBI:29950, ChEBI:CHEBI:57856, ChEBI:CHEBI:59789, ChEBI:CHEBI:82612; Evidence={ECO... | null | null | null | null | FUNCTION: Cysteine methyltransferase effector that inhibits host cell NF-kappa-B activation by preventing nuclear translocation of host protein RELA/p65 (PubMed:20126447, PubMed:20485572, PubMed:22158122, PubMed:25412445, PubMed:27445336). Acts by mediating cysteine methylation of host proteins TAB2 and TAB3: methylati... | Escherichia coli O127:H6 (strain E2348/69 / EPEC) |
B7UM99 | TIR_ECO27 | MPIGNLGNNVNGNHLIPPAPPLPSQTDGAARGGTGHLISSTGALGSRSLFSPLRNSMADSVDSRDIPGLPTNPSRLAAATSETCLLGGFEVLHDKGPLDILNTQIGPSAFRVEVQADGTHAAIGEKNGLEVSVTLSPQEWSSLQSIDTEGKNRFVFTGGRGGSGHPMVTVASDIAEARTKILAKLDPDNHGGRQPKDVDTRSVGVGSASGIDDGVVSETHTSTTNSSVRSDPKFWVSVGAIAAGLAGLAATGIAQALALTPEPDDPTTTDPDQAANAAESATKDQLTQEAFKNPENQKVNIDANGNAIPSGELKDDIVEQ... | null | null | null | extracellular region [GO:0005576]; host cell plasma membrane [GO:0020002]; membrane [GO:0016020] | null | PF07489;PF03549;PF07490; | 4.10.820.10; | Tir receptor family | PTM: Phosphorylated on Tyr-474 by host kinases. Tyr-454 can also be phosphorylated, although at lower efficiency. Phosphorylation is stimulated by clustering of Tir by intimin. {ECO:0000269|PubMed:10096089, ECO:0000269|PubMed:11918809, ECO:0000269|PubMed:14757753, ECO:0000269|PubMed:15813734, ECO:0000269|PubMed:1663606... | SUBCELLULAR LOCATION: Secreted. Host cell membrane; Multi-pass membrane protein. Note=Secreted via the type III secretion system (T3SS). Released into the host cytoplasm via T3SS and then independently inserts into the plasma membrane from a cytoplasmic location. In host cells, localizes to the tip of the actin pedesta... | null | null | null | null | null | FUNCTION: Multifunctional protein that is required for efficient pedestal formation in host epithelial cells during infection. The extracellular region acts as a receptor for bacterial intimin, allowing the bacterium to attach tightly to the host-cell surface. Simultaneously, the intracellular region initiates a signal... | Escherichia coli O127:H6 (strain E2348/69 / EPEC) |
B7UX51 | HCHA_PSEA8 | MSNERDTSRTPTPDHAEHNAFFPSPYSLSQYTSAKTDFDGADYPTPYKGGKKVLMIGTDERYILMQNGSMFSTGNHPVEMLLPMYHLDKAGFEFDVATLSGNPVKLEMWAMPGEDEAVKSIYAKYLPKLKAPQKLADLLEQAVADDSPYAAVFVPGGHGVLAGIPHSREVKRLLNAFLAKDRYIITLCHGPACLLAPAVEEKPEDYPFKDYEICVFPDALDTGANLEIGYMPGPLPWLVGENLQKLGVKILNKGITGQVHRDRKLLTGDSPLASNNLGKLAAKTLLEAFAR | 3.1.2.-; 3.5.1.-; 3.5.1.124 | null | DNA repair [GO:0006281]; methylglyoxal catabolic process to D-lactate via S-lactoyl-glutathione [GO:0019243]; protein repair [GO:0030091] | cytoplasm [GO:0005737] | glyoxalase III activity [GO:0019172]; protein deglycase activity [GO:0036524]; thiolester hydrolase activity [GO:0016790] | PF01965; | 3.40.50.880; | Peptidase C56 family, HchA subfamily | null | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_01046}. | CATALYTIC ACTIVITY: Reaction=H2O + N(omega)-(1-hydroxy-2-oxopropyl)-L-arginyl-[protein] = H(+) + L-arginyl-[protein] + lactate; Xref=Rhea:RHEA:49548, Rhea:RHEA-COMP:10532, Rhea:RHEA-COMP:12428, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:24996, ChEBI:CHEBI:29965, ChEBI:CHEBI:131708; EC=3.5.1.124; Evidence={ECO:00... | null | null | null | null | FUNCTION: Protein and nucleotide deglycase that catalyzes the deglycation of the Maillard adducts formed between amino groups of proteins or nucleotides and reactive carbonyl groups of glyoxals. Thus, functions as a protein deglycase that repairs methylglyoxal- and glyoxal-glycated proteins, and releases repaired prote... | Pseudomonas aeruginosa (strain LESB58) |
B7WN72 | SHANK_CAEEL | MNQEEDTVNLQIFVPELNVRKFLAVTQNDFIWDVKRKLLATLPQALPQAFNYGLFLPPCDGRAGKFLLEDRTIRDYPFTDCVPYLELKYKKRVYKMLNLDEKQLKAMHTKGQLKKFMDYVQQKNNEKVEKMCSQGLDANFHDAQGETPLTLAAGIPNNRAVIVSLIGGGAHVDFRNSEGQTAMHKAAFLSSFENVKTLIELGASPNYRDPIGLTPLYYNMLTADSNDQVAEILLREAADIGVTDMHGNHEIHQACKNGLTKHVEHLLYFGGQIDAENVNGNSPLHVCAVNNRPECARVLLFRGADHLAVNKQGQTALHVS... | null | null | defecation [GO:0030421]; rhythmic behavior [GO:0007622] | cytoplasmic vesicle [GO:0031410]; dendritic spine [GO:0043197]; postsynaptic density [GO:0014069]; postsynaptic membrane [GO:0045211]; pseudopodium [GO:0031143] | ionotropic glutamate receptor binding [GO:0035255]; synaptic receptor adaptor activity [GO:0030160] | PF12796;PF00595;PF00536; | 2.30.42.10;1.25.40.20;1.10.150.50; | SHANK family | null | SUBCELLULAR LOCATION: Cell projection, pseudopodium {ECO:0000269|PubMed:15013747}. Cytoplasmic vesicle {ECO:0000269|PubMed:15013747}. Postsynaptic density {ECO:0000305|PubMed:28477407}. Note=Localizes to sperm pseudopodium. {ECO:0000269|PubMed:15013747}. | null | null | null | null | null | FUNCTION: Scaffold protein that most likely acts in the postsynaptic density (PSD) of excitatory synapses which orchestrates synapse formation and maintenance at neuromuscular junctions (PubMed:28477407). Associates with and trafficks the L-type calcium channel egl-19 to the cell surface of body wall muscles to ensure ... | Caenorhabditis elegans |
B7WN96 | ELT3_CAEEL | METANYYLPSPPYSSTSSSDSRESRMNTPIPTTYSEENVNSLFHLMPDNTDQWMTSQKNFWQEGSPSSSEYLHQQAVQPSQQARLPGISNFMKDSQLSVKPAAYYCSPTMNDYRVEKVANTLLDPYVQLDQPTYADFTNAQVLNHQQEMLQMNFPTPLSTSYMNTAQVTQTHQMPFNIFELNLSNFATFQPACDTPLPLLNSSPTHPYTTMSNFTPPPQDPLVAEPKPMKKRMAAVQCHQNSICSNCKTRETTLWRRNGEGGVECNACNLYFRKNNRKRPLSLRKDGIMKRNRRPRNESPNSAIRNTHQRHGHAAAC | null | null | cell fate commitment [GO:0045165]; determination of adult lifespan [GO:0008340]; lysosome organization [GO:0007040]; negative regulation of transcription by RNA polymerase II [GO:0000122]; positive regulation of transcription by RNA polymerase II [GO:0045944]; regulation of transcription by RNA polymerase II [GO:000635... | nucleus [GO:0005634] | DNA-binding transcription factor activity, RNA polymerase II-specific [GO:0000981]; RNA polymerase II cis-regulatory region sequence-specific DNA binding [GO:0000978]; RNA polymerase II transcription regulatory region sequence-specific DNA binding [GO:0000977]; RNA polymerase II-specific DNA-binding transcription facto... | PF00320; | 3.30.50.10; | null | null | SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:10191044}. | null | null | null | null | null | FUNCTION: Transcription factor (PubMed:18662544, PubMed:28600327). Required, in concert with signal transducer and transcription factor sta-2, for up-regulation of the vacuolar H(+)-ATPase and acceleration of lysosome maturation at molt (PubMed:31735670). Involved in regulating hypodermal development, perhaps acting do... | Caenorhabditis elegans |
B7XDF1 | DSCR6_XENLA | MDSSQYMLKATLTQMCLCSRGVRNVHSEHPQQQDSSLTLWRPWLLGAGDRELDGQQRRSGEADGVPTNTGPKGALGFQHPVRLYMPKSKTSEYLQHMGRKVLASFPVQATIHFYNDDSDSEEEDEEEEMEFYNYYQNCAANGVDSSRGSSDNYSVQGGPKRNIGSHAGSA | null | null | anterior/posterior axis specification [GO:0009948]; cellular response to retinoic acid [GO:0071300]; ectodermal placode formation [GO:0060788]; embryonic pattern specification [GO:0009880]; negative regulation of DNA-binding transcription factor activity [GO:0043433]; negative regulation of DNA-templated transcription ... | nucleus [GO:0005634] | transcription coregulator activity [GO:0003712] | PF14998; | null | Ripply family | null | SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:19247927}. | null | null | null | null | null | FUNCTION: Acts as a transcriptional corepressor. Negative regulator of the transcriptional activity of tbx1 that plays a key role in pharyngeal development. Plays a role in the formation of the anteroposterior (AP) axis during embryonic development; required to establish the posterolateral border of the pre-placodal ec... | Xenopus laevis (African clawed frog) |
B7YZU2 | LINT_DROME | MFKWVTPASTATLSRCTLPATTAATTTTTAMAATRTATTTTRTTRPQLLSIALTSLIIIVASFVPTTSGFRSIETNGGGRKLFGGYRITPKHCRATKTLPSSDPRANGPTICMFNHECAQRGGEVVGACMDGFLFGACCQIPPTHELASTLINEAQNAYFQQHQQQTKLQQSAAQSSFESYGEQQQSLSEEQVAQQPSQNIYDQQNLDKVYQQLDSSSSISPPNGAYGDEPQQQEYQSESEQPVRDENAYPTSSSSTEATQSQSSSASVEFEQEPSQPADASNDQTTQKINKQPVQPPNFHVHKHSVTINSPSSPPQNDD... | 3.4.21.- | null | lumen formation, open tracheal system [GO:0035149]; proteolysis [GO:0006508]; trachea morphogenesis [GO:0060439] | perivitelline space [GO:0098595]; plasma membrane [GO:0005886] | serine-type endopeptidase activity [GO:0004252] | PF00089; | 2.40.10.10; | Peptidase S1 family | null | SUBCELLULAR LOCATION: Cell membrane {ECO:0000305|PubMed:29309404}; Single-pass type II membrane protein {ECO:0000305}. | null | null | null | null | null | FUNCTION: Probable endopeptidase. In tracheal terminal cells, acts downstream of ich to regulate seamless tube growth and/or maintenance probably by processing lumenal matrix proteins. {ECO:0000305|PubMed:29309404}. | Drosophila melanogaster (Fruit fly) |
B7YZV4 | PDE1_DROME | MQPSSPNATNYLADNIQISSANLSQTEMVVGRDSADYTAMHSINVGVGNSFLRGDTDIPQESGHSFETPSNMSFTAGQWDTESLPPVDTPDALNKAAGRIRSLLRRMDHETVAYEDMQRNLHYAARVLEAVFIDESREGCNGNCKNLNCSRHSHGRDDQQQDNNNSNRSCSLQEASPGGAGAGVTPGADNQDSIESRTKGVSQAPQTHSGPTGPPSNTSSETIAQPAPKLQPALETVRESVMEESPSKDPGDKGPPPPASTSTLTSQTTTSSSATAEPSAKAAESQAGSAGSSGSCSNPAAVHRQRRLRTPTWARSMSTN... | 3.1.4.17 | COFACTOR: Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000250|UniProtKB:Q01064}; Note=Binds 2 divalent metal cations per subunit. Site 1 may preferentially bind zinc ions. {ECO:0000250|UniProtKB:Q01064}; COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250|UniProtKB:Q01064}; Note=Binds 2 divalent... | cAMP metabolic process [GO:0046058]; cAMP-mediated signaling [GO:0019933]; cGMP metabolic process [GO:0046068]; male mating behavior [GO:0060179]; sexual reproduction [GO:0019953] | extracellular space [GO:0005615]; neuronal cell body [GO:0043025] | 3',5'-cyclic-AMP phosphodiesterase activity [GO:0004115]; 3',5'-cyclic-GMP phosphodiesterase activity [GO:0047555]; calmodulin binding [GO:0005516]; calmodulin-activated 3',5'-cyclic-GMP phosphodiesterase activity [GO:0048101]; calmodulin-activated dual specificity 3',5'-cyclic-GMP, 3',5'-cyclic-AMP phosphodiesterase a... | PF00233;PF08499; | 1.10.1300.10; | Cyclic nucleotide phosphodiesterase family, PDE1 subfamily | null | null | CATALYTIC ACTIVITY: Reaction=a nucleoside 3',5'-cyclic phosphate + H2O = a nucleoside 5'-phosphate + H(+); Xref=Rhea:RHEA:14653, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:57867, ChEBI:CHEBI:58464; EC=3.1.4.17; Evidence={ECO:0000269|PubMed:15673286}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:14654; Ev... | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=15.3 uM for 3',5'-cyclic GMP {ECO:0000269|PubMed:15673286}; KM=20.5 uM for 3',5'-cyclic AMP {ECO:0000269|PubMed:15673286}; | null | null | null | FUNCTION: Cyclic nucleotide phosphodiesterase with a dual specificity for the second messengers cAMP and cGMP, which are key regulators of many important physiological processes (PubMed:15673286). Required for male fertility and male mating behavior (PubMed:20551439). {ECO:0000269|PubMed:15673286, ECO:0000269|PubMed:20... | Drosophila melanogaster (Fruit fly) |
B7Z0E2 | UNR_DROME | MNTQSKVYRTGEEIYDNLPCDSYFNMNAIRNLGIPTTFPTIGTFTLDSTTLGLQPQGQGPSPQQQQHQQQQQQQQQQHQQNMHHHQHQQQHMQQQQQQQQHQQQHQQQQHQQQQQHQQQQQQQQQHPTIGMFDANEVNDVIQNPPQIGVFQSNSVLTNGAGSGSSIFGSQSSNSSAAAADPSQTTRETGIIEKLLHSYGFIQCCERQARLFFHFSQFSGNIDHLKIGDPVEFEMTYDRRTGKPIASQVSKIAPEVVLSEERVTGTVTTELRTDSANNVLNSSETTGRISYENRGECFFLPYTKDDVEGNVNLRAGDKVSF... | null | null | dosage compensation complex assembly [GO:0042714]; negative regulation of translational initiation [GO:0045947] | cytosol [GO:0005829] | lncRNA binding [GO:0106222]; mRNA 3'-UTR binding [GO:0003730]; mRNA regulatory element binding translation repressor activity [GO:0000900]; protein-RNA adaptor activity [GO:0140517]; RISC complex binding [GO:1905172]; RNA binding [GO:0003723] | PF00313; | 2.40.50.140; | UNR family | null | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:16452509}. | null | null | null | null | null | FUNCTION: RNA-binding protein that acts as a regulator of dosage compensation in both males and females (PubMed:16452508, PubMed:16452509, PubMed:18203923, PubMed:19168682, PubMed:19941818, PubMed:25158899). In males, acts as positive regulator of dosage compensation by promoting assembly of the MSL complex, a multipro... | Drosophila melanogaster (Fruit fly) |
B7Z0L8 | MODI_DROME | MSLVPEASTSRAPKYCYFFKTLLVEELELETSYHNLHYGQCALIGRLAFKANQYRLENVRVKCLPKKYSLGEGTVSLLILGLTHDKVVENRVSTGRYCIVRGEVVLHNVQHPKGAKLTAGGVYDKINSLSNDPLAQKQYLSALLATYRPAIDLWYIQVIDRAEDLLTRRLEMRSLIEK | null | null | protection from non-homologous end joining at telomere [GO:0031848]; telomere capping [GO:0016233] | chromosome, telomeric region [GO:0000781]; polytene chromosome interband [GO:0005705]; telomere cap complex [GO:0000782] | null | null | null | null | null | SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:19181850, ECO:0000269|PubMed:19240120, ECO:0000269|PubMed:20679394, ECO:0000269|PubMed:26110638}. Chromosome {ECO:0000269|PubMed:19181850, ECO:0000269|PubMed:19240120, ECO:0000269|PubMed:20679394, ECO:0000269|PubMed:26110638}. Chromosome, telomere {ECO:0000269|PubMed:19... | null | null | null | null | null | FUNCTION: Part of the MTV complex that associates with the HipHop-HOAP complex to form the terminin telomere-capping complex involved in telomere maintenance and prevention of telomere fusion (PubMed:19240120, PubMed:27835648). Potentially functions downstream of mei-41/ATR (PubMed:19240120). As part of the MTV complex... | Drosophila melanogaster (Fruit fly) |
B7ZAQ6 | GPHRA_HUMAN | MSFLIDSSIMITSQILFFGFGWLFFMRQLFKDYEIRQYVVQVIFSVTFAFSCTMFELIIFEILGVLNSSSRYFHWKMNLCVILLILVFMVPFYIGYFIVSNIRLLHKQRLLFSCLLWLTFMYFFWKLGDPFPILSPKHGILSIEQLISRVGVIGVTLMALLSGFGAVNCPYTYMSYFLRNVTDTDILALERRLLQTMDMIISKKKRMAMARRTMFQKGEVHNKPSGFWGMIKSVTTSASGSENLTLIQQEVDALEELSRQLFLETADLYATKERIEYSKTFKGKYFNFLGYFFSIYCVWKIFMATINIVFDRVGKTDPVT... | null | null | intracellular pH reduction [GO:0051452]; positive regulation of canonical NF-kappaB signal transduction [GO:0043123]; protein transport [GO:0015031]; response to abscisic acid [GO:0009737]; T cell differentiation [GO:0030217] | Golgi cisterna membrane [GO:0032580]; Golgi membrane [GO:0000139]; Golgi-associated vesicle membrane [GO:0030660]; monoatomic ion channel complex [GO:0034702] | abscisic acid binding [GO:0010427]; voltage-gated monoatomic anion channel activity [GO:0008308] | PF12430;PF12537; | null | Golgi pH regulator (TC 1.A.38) family | null | SUBCELLULAR LOCATION: Golgi apparatus membrane {ECO:0000269|PubMed:18794847}; Multi-pass membrane protein {ECO:0000255}. | CATALYTIC ACTIVITY: Reaction=iodide(out) = iodide(in); Xref=Rhea:RHEA:66324, ChEBI:CHEBI:16382; Evidence={ECO:0000269|PubMed:18794847}; CATALYTIC ACTIVITY: Reaction=chloride(in) = chloride(out); Xref=Rhea:RHEA:29823, ChEBI:CHEBI:17996; Evidence={ECO:0000269|PubMed:18794847}; CATALYTIC ACTIVITY: Reaction=bromide(in) = b... | null | null | null | null | FUNCTION: Voltage-gated channel that enables the transfer of monoatomic anions such as iodide, chloride, bromide and fluoride which may function in counter-ion conductance and participates in Golgi acidification (PubMed:18794847). Plays a role in lymphocyte development, probably by acting as a RABL3 effector in hematop... | Homo sapiens (Human) |
B7ZC96 | KCMA1_DANRE | MSNNINFNKNPDSSVSISKMDVIIPFTPDVPCDNNGQRMWWAFLASSMVTFFGGLFIILLWRTLKYLWTVCCHCNIKNKEAQKVNNPITIQADGTTKTGNEKEEAPASEVGWMTSVKDWAGVMISAQTLTGRVLVVLVFALSIGALGIYFIDSSDPIESCQNFYKDFTLQIDMAFNVFFLLYFGLRFIAANDKLWFWLEVNSVVDFFTVPPVFVSVYLNRSWLGLRFLRALRLIQFSEILQFLNILKTSNSIKLVNLCSIFISTWLTAAGFIHLVENSGDPWENFQNSQPLSYWECVYLLMVTMSTVGYGDVYARTTLGR... | null | null | potassium ion transmembrane transport [GO:0071805]; response to auditory stimulus [GO:0010996] | membrane [GO:0016020]; monoatomic ion channel complex [GO:0034702]; postsynaptic membrane [GO:0045211] | calcium ion binding [GO:0005509]; calcium-activated potassium channel activity [GO:0015269]; large conductance calcium-activated potassium channel activity [GO:0060072] | PF03493;PF00520;PF21014; | 1.10.287.70;3.40.50.720; | Potassium channel family, Calcium-activated (TC 1.A.1.3) subfamily, KCa1.1/KCNMA1 sub-subfamily | PTM: Phosphorylated. {ECO:0000250|UniProtKB:Q12791}.; PTM: Palmitoylated. {ECO:0000250|UniProtKB:Q12791}. | SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:Q12791}; Multi-pass membrane protein {ECO:0000250|UniProtKB:Q12791}. | CATALYTIC ACTIVITY: Reaction=K(+)(in) = K(+)(out); Xref=Rhea:RHEA:29463, ChEBI:CHEBI:29103; Evidence={ECO:0000269|PubMed:22139424}; | null | null | null | null | FUNCTION: Potassium channel activated by both membrane depolarization or increase in cytosolic Ca(2+) that mediates export of K(+) (PubMed:22139424). It is also activated by the concentration of cytosolic Mg(2+) (By similarity). Its activation dampens the excitatory events that elevate the cytosolic Ca(2+) concentratio... | Danio rerio (Zebrafish) (Brachydanio rerio) |
B7ZNG0 | KIF7_MOUSE | MGLEAQRLPGAEEAPVRVALRVRPLLPKELLHGHQSCLRVEPERGRITLGRDRHFGFHVVLGEDTGQEAVYQACVQPLLEAFFEGFNATVFAYGQTGSGKTYTMGEASVASLHEDEQGIIPRAMAEAFKLIDENDLLDCLVHVSYLELYKEEFRDLLEVGTASRDIQLREDDRGNVVLCGVKEVDVEGLDEVLSLLEMGNAARHTGATHFNRLSSRSHTVFTVTLEQRGRTPSRLPRPAAGHLLVSKFHFVDLAGSERVLKTGSTGERLKESIQINSTLLALGNVISALGDPQRRGSHIPYRDSKITRILKDSLGGNAKT... | null | null | aorta development [GO:0035904]; cardiac septum development [GO:0003279]; coronary vasculature development [GO:0060976]; microtubule-based movement [GO:0007018]; mitotic spindle organization [GO:0007052]; negative regulation of smoothened signaling pathway [GO:0045879]; positive regulation of smoothened signaling pathwa... | ciliary basal body [GO:0036064]; ciliary tip [GO:0097542]; cilium [GO:0005929]; cytoplasm [GO:0005737]; kinesin complex [GO:0005871]; microtubule [GO:0005874] | ATP binding [GO:0005524]; ATP hydrolysis activity [GO:0016887]; identical protein binding [GO:0042802]; microtubule binding [GO:0008017]; microtubule motor activity [GO:0003777] | PF00225; | 3.40.850.10; | TRAFAC class myosin-kinesin ATPase superfamily, Kinesin family | PTM: Polyubiquitinated by UBR3. {ECO:0000269|PubMed:27195754}. | SUBCELLULAR LOCATION: Cell projection, cilium {ECO:0000269|PubMed:19666503, ECO:0000269|PubMed:24952464, ECO:0000269|PubMed:25644602}. Cytoplasm, cytoskeleton, cilium basal body {ECO:0000269|PubMed:25644602}. Note=Localizes to the cilium tip. | null | null | null | null | null | FUNCTION: Essential for hedgehog signaling regulation: acts both as a negative and a positive regulator of sonic hedgehog (Shh) and Indian hedgehog (Ihh) pathways, acting downstream of SMO, through both SUFU-dependent and -independent mechanisms. Involved in the regulation of microtubular dynamics. Required for proper ... | Mus musculus (Mouse) |
B7ZQJ9 | GT2D1_XENLA | MALAGKQYEGSLNNSRPNLWPSSIPGGKNEIITSLVTALDSMCTALSKLNTEVACIALHEESAFVVGTEKGRCFLNSRKELQADFQRFCIGAHKKDQENEVKRRNRDGIQNIQHVPLGPTSDIYLLRKMVEEIFEVLYSEALGKSNIVPVPYVKVMKEPGSVVVLGLPDGISFRKPAEYDLKSLMLILKHSHNIRFKLRIPTEESIREPKSCSELNSPPTSATKVIPETSQCHRLPIQEHPSSASNFPYSVSQPNQISLEPKQEVHSNMLGTNAVNQMLVQRPSAENNHDLSDCCGQQSPVAGSSLRQNVLASKHLLFSI... | null | null | negative regulation of DNA-templated transcription [GO:0045892]; negative regulation of transcription by RNA polymerase II [GO:0000122]; positive regulation of DNA-templated transcription [GO:0045893]; positive regulation of transcription by RNA polymerase II [GO:0045944]; regulation of activin receptor signaling pathw... | nucleus [GO:0005634]; transcription regulator complex [GO:0005667] | DNA-binding transcription factor activity [GO:0003700]; DNA-binding transcription factor binding [GO:0140297]; RNA polymerase II-specific DNA-binding transcription factor binding [GO:0061629]; SMAD binding [GO:0046332]; transcription cis-regulatory region binding [GO:0000976] | PF02946; | 3.90.1460.10; | TFII-I family | null | SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q9UHL9, ECO:0000255|PROSITE-ProRule:PRU00484}. | null | null | null | null | null | FUNCTION: Transcription factor that activates a subset of organizer-specific genes. Binds to the distal element (DE) of the gsc promoter to regulate its expression. In the presence of pou5f1.1/oct-25, forms a repression complex on the promoter of the gsc and mix2 genes to inhibit their transcription. {ECO:0000269|PubMe... | Xenopus laevis (African clawed frog) |
B7ZR30 | STK10_XENLA | MAFANFRRILRLPNFEKKRLREYEHVRRDVDPNQVWEIIGELGDGAFGKVYKAKNRETGILAAAKVIETKNEEELEDYMVEIEILATCNHHFIVKLLGAFYWEGKLWIMIEFCPGGAVDAVMLELDRGLKEPEIKTICRQMLEALAYLHSMKIIHRDLKAGNVLLTLDGDIKLADFGVSAKNVKTLQRRDSFIGTPYWMAPEVVMCETMKDAPYDYKADIWSLGITLIEMAQIEPPHHELNPMRVLLKIAKSEPPTLSSLSKWSPEFHSFLKTALDKNPETRPSAAQLLEHPFVKKASGNKPLRDLVAEAKAEVLDEIEE... | 2.7.11.1 | null | G2/M transition of mitotic cell cycle [GO:0000086]; oocyte maturation [GO:0001556]; protein autophosphorylation [GO:0046777]; regulation of lymphocyte migration [GO:2000401] | plasma membrane [GO:0005886] | ATP binding [GO:0005524]; protein homodimerization activity [GO:0042803]; protein serine kinase activity [GO:0106310]; protein serine/threonine kinase activity [GO:0004674] | PF00069;PF12474; | 1.10.510.10; | Protein kinase superfamily, STE Ser/Thr protein kinase family, STE20 subfamily | PTM: Autophosphorylates. Phosphorylated by plk1/plx1, suggesting the existence of a feedback loop with plk1/plx1. activation of the protein. {ECO:0000269|PubMed:15166215}. | SUBCELLULAR LOCATION: Cell membrane {ECO:0000250}; Peripheral membrane protein {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: May act as a polo kinase kinase by mediating phosphorylation of plk1/plx1 and subsequent activation of plk1/plx1 during oocyte maturation. {ECO:0000269|PubMed:12207013, ECO:0000269|PubMed:9831560}. | Xenopus laevis (African clawed frog) |
B7ZR65 | SOX9A_XENLA | MNLLDPFMKMTEEQDKCMSGAPSPTMSDDSAGSPCPSGSGSDTENTRPQENTFPKGDQELKKETEDEKFPVCIREAVSQVLKGYDWTLVPMPVRVNGSSKNKPHVKRPMNAFMVWAQAARRKLADQYPHLHNAELSKTLGKLWRLLNEGEKRPFVEEAERLRVQHKKDHPDYKYQPRRRKSVKNGQTEQEDGAEQTHISPNAIFKALQADSPHSSSSMSEVHSPGEHSGQSQGPPTPPTTPKTDIQPGKPDLKREGRPLQENGRQPPHIDFRDVDIGELSSEVISTIETFDVNEFDQYLPPNGHPGVGSTQASYTGSYGI... | null | null | cartilage development [GO:0051216]; chondrocyte differentiation [GO:0002062]; gonadal mesoderm development [GO:0007506]; growth plate cartilage chondrocyte growth [GO:0003430]; heart development [GO:0007507]; negative regulation of canonical Wnt signaling pathway [GO:0090090]; negative regulation of fatty acid oxidatio... | cytoplasm [GO:0005737]; nucleus [GO:0005634] | DNA binding [GO:0003677]; DNA-binding transcription factor activity, RNA polymerase II-specific [GO:0000981]; RNA polymerase II cis-regulatory region sequence-specific DNA binding [GO:0000978]; sequence-specific DNA binding [GO:0043565]; ubiquitin-like protein ligase binding [GO:0044389] | PF00505;PF12444; | 1.10.30.10; | null | PTM: Sumoylated. Lys-365 is the major site of sumoylation, although sumoylation at Lys-61 also occurs. Sumoylation plays a key role in regulating formation of the neural crest and otic placode. {ECO:0000269|PubMed:16256735}. | SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00267, ECO:0000269|PubMed:11807034}. Cytoplasm {ECO:0000250|UniProtKB:Q6F2E7}. Note=Restricted to the nucleus of Sertoli-like cells in the testis, but localizes to the cytoplasm of previtellogenic oocytes in the ovary before being translocated into the nucle... | null | null | null | null | null | FUNCTION: Transcription factor that plays a key role in chondrocytes differentiation and skeletal development (By similarity). Specifically binds the 5'-ACAAAG-3' DNA motif present in enhancers and super-enhancers and promotes expression of genes important for chondrogenesis, including COL2A1 (By similarity). Plays a c... | Xenopus laevis (African clawed frog) |
B7ZRU9 | EVI1A_XENLA | MKSEDYSYARMAPDIHEERQYRCEECDQLFESKTELSDHQKYPCVTPHSAFSLVENSFPPSLNDDSDLTEMQHTHECKECDQVFPDMQSLEKHLLSHTEEREYKCDQCPKAFNWKSNLIRHQMSHDTGKHYECENCSKQVFTDPSNLQRHIRSQHVGARAHACSDCGKTFATSSGLKQHKHIHSSVKPFVCEVCHKSYTQFSNLCRHKRMHADCRTQIKCKDCGQMFSTTSSLNKHRRFCEGKNHFAAGGLFGQGISLPGTPAMDKASMISMNHANAGLADYFGASRHTAGLTFPTAPGFPFSFPGLFPSSLYHRPPFIP... | null | null | negative regulation of DNA-templated transcription [GO:0045892]; negative regulation of transcription by RNA polymerase II [GO:0000122]; pronephric distal tubule morphogenesis [GO:0039013]; pronephric duct development [GO:0039022]; pronephros development [GO:0048793]; proximal/distal pattern formation involved in prone... | nuclear speck [GO:0016607] | DNA binding [GO:0003677]; metal ion binding [GO:0046872] | PF00096;PF13912; | 3.30.160.60; | null | null | SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q03112}. Nucleus speckle {ECO:0000250|UniProtKB:Q03112}. | null | null | null | null | null | FUNCTION: Transcriptional repressor during pronephros development. Plays a role in regionalization of the pronephros; may promote formation of the distal tubule and duct over formation of the glomus and proximal tubule. {ECO:0000269|PubMed:16574097}. | Xenopus laevis (African clawed frog) |
B7ZS96 | TTHY_XENLA | MASFKSFLLLALLAIVSEAAPPGHASHGEADSKCPLMVKVLDAVRGIPAANLLVNVFRQTESGKWEQITSGKTTELGEIHNLTTDEQFTEGVYKIEFATKAFWGKLGLSPFHEYVDVVFTANDAGHRHYTIAVLLTPYSFSSTAIVSEPHDDL | null | null | purine nucleobase metabolic process [GO:0006144]; response to estrogen [GO:0043627]; thyroid hormone transport [GO:0070327] | extracellular region [GO:0005576]; extracellular space [GO:0005615]; protein-containing complex [GO:0032991] | hormone activity [GO:0005179]; identical protein binding [GO:0042802]; thyroid hormone binding [GO:0070324] | PF00576; | 2.60.40.180; | Transthyretin family | PTM: Sulfonation of the reactive cysteine Cys-34 enhances the stability of the native conformation of TTR, avoiding misassembly of the protein leading to amyloid formation. {ECO:0000250|UniProtKB:P02766}. | SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:11080066}. | null | null | null | null | null | FUNCTION: Thyroid hormone-binding protein, with a much higher binding affinity for triiodothyronine (T3) than for thyroxine (T4). Probably transports triiodothyronine from the bloodstream to the brain. {ECO:0000250|UniProtKB:P02766, ECO:0000269|PubMed:11017780, ECO:0000269|PubMed:11080066, ECO:0000269|PubMed:12228058, ... | Xenopus laevis (African clawed frog) |
B7ZSG3 | WT1A_XENLA | MGSDVRDMNLLPPVSSLSGNSSCNMPVSSSAQWAPVLDFPPGAPYSSLTPHSFIKQEPTWNPDPHEDQCLSAFTVHFSGQFTGTAGACRYGPFGAPTPSQATTGQARMFSNAPYLSNCLDNQQGMRNQGYSAVAFDGTPSYGHTPSHHTSQFTNHSFKHEDPLSQQTSLGEQQYSVPPPVYGCHTPTDTCTGSQALLLRTPYNSDNLYPMTSQLDCMTWNQMNLGSSLKSHGTSYENDSHSSPMLYNCGGQYRIHTHGVFRGIQDVRRVPGVTPAIVRSTEANEKRPFMCAYPGCNKRYFKLSHLQMHSRKHTGEKPYQC... | null | null | glomus development [GO:0072013]; kidney vasculature development [GO:0061440]; negative regulation of pronephric nephron tubule development [GO:1900207]; negative regulation of transcription by RNA polymerase II [GO:0000122]; negative regulation of Wnt signaling pathway [GO:0030178]; pronephros development [GO:0048793];... | cytoplasm [GO:0005737]; nuclear speck [GO:0016607] | DNA-binding transcription factor activity, RNA polymerase II-specific [GO:0000981]; double-stranded methylated DNA binding [GO:0010385]; hemi-methylated DNA-binding [GO:0044729]; RNA binding [GO:0003723]; RNA polymerase II cis-regulatory region sequence-specific DNA binding [GO:0000978]; sequence-specific DNA binding [... | PF02165;PF00096; | 3.30.160.60; | EGR C2H2-type zinc-finger protein family | null | SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:P22561}. Cytoplasm {ECO:0000250|UniProtKB:P22561}. Nucleus speckle {ECO:0000250|UniProtKB:P22561}. Note=Shuttles between nucleus and cytoplasm. {ECO:0000250|UniProtKB:P22561}. | null | null | null | null | null | FUNCTION: Transcription factor required for development of the vascular component of the pronephric kidney, the glomus; may repress tubule-specific gene expression in the portion of the pronephros fated to form the glomus. Recognizes and binds to the DNA sequence 5'-GCG(T/G)GGGCG-3' (By similarity). Inhibits Wnt-signal... | Xenopus laevis (African clawed frog) |
B7ZSK1 | NMDE1_XENLA | MGMFVLLLYTFLYAGDLGHGAEKSFPVLNIAVILGRTRYITERDIRSLWTRDMSLDFDVNVVTLLVNQTDPKSIITHVCDLMSGTKIHGVVFGDDTDQEAIAQILDFVSSQTFIPILGIHGGSSMIMADKDEMSTFFQFGASIKQQATVMLNIMEEYDWHVFSVITSNFPGYRDFISFIKTTVDNSFVGWEVQNYITLDTSYTDAQTLTQLKKIHSSVILLYCSKDEATYIFEEARSLGLMGYGFVWIVPSLVTGNTDIIPYEFPSGLVSVSYDDWDYGIEARVRDGLGIITTAASAMLEKHSVIPEAKTSCYGQNERND... | null | null | calcium ion transmembrane import into cytosol [GO:0097553]; excitatory postsynaptic potential [GO:0060079]; long-term synaptic potentiation [GO:0060291]; protein heterotetramerization [GO:0051290]; regulation of synaptic plasticity [GO:0048167]; response to zinc ion [GO:0010043] | NMDA selective glutamate receptor complex [GO:0017146]; plasma membrane [GO:0005886]; postsynaptic membrane [GO:0045211] | glutamate-gated calcium ion channel activity [GO:0022849]; metal ion binding [GO:0046872]; NMDA glutamate receptor activity [GO:0004972] | PF01094;PF00060;PF10613;PF10565;PF00497; | 3.40.50.2300;3.40.190.10; | Glutamate-gated ion channel (TC 1.A.10.1) family | null | SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:28232581}; Multi-pass membrane protein {ECO:0000269|PubMed:28232581}. Postsynaptic cell membrane {ECO:0000250|UniProtKB:Q00959}; Multi-pass membrane protein {ECO:0000255}. | null | null | null | null | null | FUNCTION: Component of NMDA receptor complexes that function as heterotetrameric, ligand-gated ion channels with high calcium permeability and voltage-dependent sensitivity to magnesium. Channel activation requires binding of the neurotransmitter glutamate to the epsilon subunit, glycine binding to the zeta subunit, pl... | Xenopus laevis (African clawed frog) |
B7ZWR6 | OEP61_ARATH | MFNGLMDPEMIRLAQDQMSRMTPADFARIQQQMMSNPDLMNMATESMKNMRPEDLKQAAEQLKHTRPEDMAEISEKMAKASPEDIAAMRAHADAQFTYQINAAQMLKKQGNELHSRGNFSDAAEKYLRAKNNLKEIPSSKGGAILLACSLNLMSCYLKTNQHEECIKEGSEVLGYDARNVKALYRRGQAYRDLGLFEDAVSDLSKAHEVSPEDETIADVLRDVKERLAVEGPGKASRGVVIEDITEENNVTSGENKKPSKEANGHAQGVKTDVDGLQALRDNPEAIRTFQNFISKTDPDTLAALSGGKAGDMSPDMFKTA... | null | null | cytosol to endoplasmic reticulum transport [GO:0046967]; protein transport [GO:0015031] | chloroplast outer membrane [GO:0009707]; endoplasmic reticulum membrane [GO:0005789]; plastid [GO:0009536] | null | PF00515; | 1.25.40.10; | null | null | SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000305}; Single-pass membrane protein {ECO:0000305}. Plastid, chloroplast outer membrane {ECO:0000305}; Single-pass membrane protein {ECO:0000305}. Note=Resides most likely exclusively in the ER membrane. | null | null | null | null | null | FUNCTION: Plays a role in protein import into the endoplasmic reticulum (ER). May function as chaperone docking protein during post-translational protein translocation into the ER. Chaperone receptor mediating Hsp70-dependent protein targeting to chloroplasts. Interacts specifically with some chloroplast precursors, bu... | Arabidopsis thaliana (Mouse-ear cress) |
B8A4F0 | ZD16A_DANRE | MHPCSSVLHLLLRCMRGCCRHTRSRVPRRLRRHVSYIRLIFKSLYFNSLTNSDVVTDSILEPVFWMVEVVTRWFGMVFVFLVVALTSSVVFIAYFCLLPLVLHTYSPGWMIWHICYGHWNLVMIVFHYYKATKTPPGYPPKMKTDVPFVSVCKKCIIPKPARSHHCGICKTCILKMDHHCPWLNNCVGHFNHRYFFSFCLFLTLGCMYCSVSGRHLFIDAYNTIDQLKHLEAEKQGVPVTGIGLLIGIVPSAGVAGKAVQVAQEVSQPPYTYKDRMFHKSVIYMWVLTSTVSVALGALTLWHALLITRGETSIERHINGK... | 2.3.1.225 | null | commitment of multipotent stem cells to neuronal lineage in forebrain [GO:0021898]; DNA damage response [GO:0006974]; eye development [GO:0001654]; fibroblast growth factor receptor signaling pathway involved in forebrain neuron fate commitment [GO:0021899]; heart development [GO:0007507]; protein palmitoylation [GO:00... | endoplasmic reticulum membrane [GO:0005789]; Golgi apparatus [GO:0005794] | palmitoyltransferase activity [GO:0016409]; protein-cysteine S-palmitoyltransferase activity [GO:0019706] | PF01529; | null | DHHC palmitoyltransferase family | null | SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000250|UniProtKB:Q969W1}; Multi-pass membrane protein {ECO:0000250|UniProtKB:Q9ESG8}. | CATALYTIC ACTIVITY: Reaction=hexadecanoyl-CoA + L-cysteinyl-[protein] = CoA + S-hexadecanoyl-L-cysteinyl-[protein]; Xref=Rhea:RHEA:36683, Rhea:RHEA-COMP:10131, Rhea:RHEA-COMP:11032, ChEBI:CHEBI:29950, ChEBI:CHEBI:57287, ChEBI:CHEBI:57379, ChEBI:CHEBI:74151; EC=2.3.1.225; Evidence={ECO:0000250|UniProtKB:Q969W1}; | null | null | null | null | FUNCTION: Palmitoyl acyltransferase that mediates palmitoylation of proteins and is required during embryonic heart development. Involved in the proliferation of neural stem cells by regulating the FGF/ERK pathway (By similarity). Involved in the proliferation of neural stem cells by regulating the FGF/ERK pathway (Pub... | Danio rerio (Zebrafish) (Brachydanio rerio) |
B8A4W9 | LOX3B_DANRE | MELHQWCRHIIVFLLNVWIPSCFAQTTPPARSSPTPTPQTADNPDSLKFRLSGFPRKHNEGRIEVFYKGEWGTICDDDFSLANAHVLCRQLGFVSATGWTHSAKYGKGAGKIWLDNVQCSGSERSVSVCKSRGWGNSDCTHDEDAGVICKDERLPGFVDSNVIEVQVDENRVEEVRLRPVFTTATKRMPVTEGVVEVKNKDGWAQICDIGWTPKNTHVVCGMMGFPHEKKVNKNFYKLYAERQKNFFLVHSVACLGTEVHLAACPLEFNYGNATESCPGGMPAVVSCVPGPLYTQSPTMKKKLKMPPTTRLKGGAKYGEG... | 1.4.3.-; 1.4.3.13 | COFACTOR: Name=Cu cation; Xref=ChEBI:CHEBI:23378; Evidence={ECO:0000250|UniProtKB:P16636}; COFACTOR: Name=lysine tyrosylquinone residue; Xref=ChEBI:CHEBI:20489; Evidence={ECO:0000250|UniProtKB:P33072}; Note=Contains 1 lysine tyrosylquinone. {ECO:0000250|UniProtKB:P33072}; | collagen fibril organization [GO:0030199]; embryonic viscerocranium morphogenesis [GO:0048703]; fibronectin fibril organization [GO:1905590]; inflammatory response [GO:0006954]; lung development [GO:0030324]; negative regulation of T-helper 17 cell lineage commitment [GO:2000329]; peptidyl-lysine oxidation [GO:0018057]... | collagen-containing extracellular matrix [GO:0062023]; cytoplasm [GO:0005737]; extracellular space [GO:0005615]; membrane [GO:0016020]; nucleus [GO:0005634] | copper ion binding [GO:0005507]; fibronectin binding [GO:0001968]; 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:P33072}. | SUBCELLULAR LOCATION: Secreted, extracellular space {ECO:0000250|UniProtKB:Q9Z175}. Cytoplasm {ECO:0000250|UniProtKB:P58215}. Nucleus {ECO:0000250|UniProtKB:P58215}. Note=It is unclear how loxl3b is both intracellular (cytoplasmic and nuclear) and extracellular: it contains a clear signal sequence and is predicted to l... | 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: Protein-lysine 6-oxidase that mediates the oxidation of peptidyl lysine residues to allysine in target proteins (By similarity). Catalyzes the post-translational oxidative deamination of peptidyl lysine residues in precursors of elastin and different types of collagens, a prerequisite in the formation of cros... | Danio rerio (Zebrafish) (Brachydanio rerio) |
B8AL97 | CUCIN_ORYSI | MAKKKTSSSMARSQLAALLISLCFLSLASNAVGWSRRGEREEEDERRRHGGEGGRPYHFGEESFRHWTRTRHGRFSVLERFPDEQVVGAAVGGYRVAVLEAAPRAFLQPSHYDADEVFYVKEGEGVIVLLREGRKESFCVREGDAMVIPAGAIVYSANTHSSKWFRVVMLLNPVSTPGHFEEYFPVGGDRPESFFSAFSDDVLQAAFNTRREELEKVFERQREGGEITTAPEEQIRELSKSCSRGGGGGSGSEWEIKPSSLTGKSPYFSNNHGKLFELTGDECRHLKKLDLQIGLANITRGSMIAPNYNTRATKLAVVLQ... | 3.4.-.- | COFACTOR: Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000269|PubMed:27064905}; | protein homotrimerization [GO:0070207]; proteolysis [GO:0006508] | extracellular space [GO:0005615] | IgE binding [GO:0019863]; metalloendopeptidase activity [GO:0004222]; nutrient reservoir activity [GO:0045735]; zinc ion binding [GO:0008270] | PF00190; | 2.60.120.10; | 7S seed storage protein family | null | SUBCELLULAR LOCATION: Secreted {ECO:0000305}. | null | null | null | BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 4.0. {ECO:0000269|PubMed:27064905}; | BIOPHYSICOCHEMICAL PROPERTIES: Temperature dependence: Optimum temperature is 55 degrees Celsius. {ECO:0000269|PubMed:27064905}; | FUNCTION: Seed storage protein (Probable). Globulin-like protein that acts as a zinc metalloprotease. Cleaves specifically between Leu-15 and Tyr-16 of insulin B chain, and Gln-1 and Leu-2 of neurotensin (NT) peptide in vitro. May play a role as an initiating endopeptidase in germinating seeds (PubMed:27064905). {ECO:0... | Oryza sativa subsp. indica (Rice) |
B8ANW0 | YUC8_ORYSI | MQGQQKQNAGGGGGDNASPCIVLDGPIIVGAGPSGLAVAATLRQHGAPFTVVERSGGVADLWTNRTYDRLRLHLPKVFCELPHVAFPPDFPTYPTKHDFLRYLHSYAARFAIAPLLRRTVTRAWYDHPASLWRVTTTTTSSSATSVITEYASPWLVVASGENAEVVVPKVKGRERFAGEALHSSEYRSGERFRGMRVLVVGCGNSGMEMCLDLCEHGAMPFMSVRSGVHVLPREMFGASTFGIAMKLLRWLPIKMVDRFLLLVARMVLGDTEKYGLKRPKLGPLEIKNITGKSPVLDVGAWSLIKSGNIKIVPEVESFSG... | 1.14.13.168 | COFACTOR: Name=FAD; Xref=ChEBI:CHEBI:57692; Evidence={ECO:0000250|UniProtKB:Q10RE2}; | auxin biosynthetic process [GO:0009851]; regulation of leaf development [GO:2000024]; regulation of root development [GO:2000280] | endoplasmic reticulum [GO:0005783] | flavin adenine dinucleotide binding [GO:0050660]; indole-3-pyruvate monooxygenase activity [GO:0103075]; N,N-dimethylaniline monooxygenase activity [GO:0004499]; NADP binding [GO:0050661] | PF00743; | 3.50.50.60; | FMO family | null | SUBCELLULAR LOCATION: Endoplasmic reticulum {ECO:0000250|UniProtKB:Q10RE2}. | CATALYTIC ACTIVITY: Reaction=H(+) + indole-3-pyruvate + NADPH + O2 = (indol-3-yl)acetate + CO2 + H2O + NADP(+); Xref=Rhea:RHEA:34331, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, ChEBI:CHEBI:16526, ChEBI:CHEBI:17640, ChEBI:CHEBI:30854, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349; EC=1.14.13.168; Evidence={ECO:0000... | null | null | null | null | FUNCTION: Involved in auxin biosynthesis (PubMed:24371168). Converts the indole-3-pyruvic acid (IPA) produced by the TAA family to indole-3-acetic acid (IAA) (By similarity). Seems not able to use tryptamine (TAM) as substrate (By similarity). Probably responsible for auxin biosynthesis in leaves and involved in the re... | Oryza sativa subsp. indica (Rice) |
B8AVJ9 | APL25_ORYSI | MWDLNDSPAAEAAPPPLSPSADDSGASSSSAAAVVEIPDDADDDSAAVVVVTRQFFPPAVPGGGGDPAPGNARAGWLRLAGAAPPVAATGPAASAAVSKKSRRGPRSRSSQYRGVTFYRRTGRWESHIWDCGKQVYLGGFDTAHAAARAYDRAAIKFRGVEADINFSLEDYEDDLKQMSNLTKEEFVHVLRRQSTGFPRGSSKYRGVTLHKCGRWEARMGQFLGKKYVYLGLFDTEEEAARAYDRAAIKCNGKDAVTNFDPSIYAGEFEPPAAATGDAAEHNLDLSLGSSAGSKRGNVDGGGDDEITGGGGGGTGSDQRV... | null | null | regulation of floral organ abscission [GO:0060860]; regulation of flower development [GO:0009909]; regulation of seed development [GO:0080050]; response to cold [GO:0009409]; seed abscission [GO:0097548] | nucleus [GO:0005634]; transcription regulator complex [GO:0005667] | DNA-binding transcription factor activity [GO:0003700]; transcription cis-regulatory region binding [GO:0000976] | PF00847; | 3.30.730.10; | AP2/ERF transcription factor family, AP2 subfamily | null | SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00366, ECO:0000269|PubMed:22408071}. | null | null | null | null | null | FUNCTION: Transcription factor (PubMed:22408071). Involved in spikelet transition and development (PubMed:22408071). Prevents lemma and palea elongation as well as grain growth (PubMed:22408071). Required for seed shattering through specifying abscission zone (AZ) development (PubMed:22408071). {ECO:0000269|PubMed:2240... | Oryza sativa subsp. indica (Rice) |
B8B183 | APO1_ORYSI | MMNPRRLPPLPSSTSSASAADDMDPRVWRRLPQPLVDRVLACLPTPSFLRLRAACRRFYHLLFSSPFLHSHLLLSPHLPFFAFVVPAAGHLLLLDPTATASWSRLPLPLPPVAGGPAAFSPAAASAGLLAFLSDASGHKTLLLANPITRLLAALPISPTPRLSPTVGLAAGPTSIIAVVAGDDLVSPFAVKNISADTFVADAASVPPSGFWAPSSLLPRLSSLDPGAGMAFASGRFYCMSSSPFAVLVFDVAENVWSKVQPPMRRFLRSPALVELGGGREGAARVALVSAVEKSRLSVPRSVRLWTLRGGGGGGGGGAWT... | null | null | cell differentiation [GO:0030154]; flower development [GO:0009908]; maintenance of meristem identity [GO:0010074]; protein ubiquitination [GO:0016567]; regulation of cell population proliferation [GO:0042127]; regulation of DNA-templated transcription [GO:0006355]; regulation of flower development [GO:0009909]; regulat... | membrane [GO:0016020] | null | PF00646; | null | null | null | SUBCELLULAR LOCATION: Membrane {ECO:0000255}; Multi-pass membrane protein {ECO:0000255}. | null | null | PATHWAY: Protein modification; protein ubiquitination. {ECO:0000305}. | null | null | FUNCTION: Component of SCF(ASK-cullin-F-box) E3 ubiquitin ligase complexes, which may mediate the ubiquitination and subsequent proteasomal degradation of target proteins (By similarity). Together with FL/APO2, involved in the temporal regulation of meristem identity during both vegetative and reproductive developments... | Oryza sativa subsp. indica (Rice) |
B8B2R4 | NAP1A_ORYSI | MGGDKENLDLSDLNASLPAAAAALSAEDRAGLVNALKDKLQSLAGQHTDVLEALSPNVRKRVEYLREIQGQHDEIELKFFEERAALEAKYQKLYEPLYTKRYNIVNGVVEVDGGNDEPASENAAEFKDADAKGVPDFWLTAMKTNEVLSEEIQERDEPALKYLKDIKWARIDDPKGFKLDFFFDTNPFFKNSVLTKTYHMVDEDEPILEKAIGTEIEWYPGKNLTQKILKKKPKKGSKNAKPITKTEVCESFFNFFSPPQVPDDDEDIDEDTADELQGQMEHDYDIGTTIRDKIIPHAVSWFTGEAVQAEDFDDMEDDEE... | null | null | double-strand break repair via homologous recombination [GO:0000724]; nucleosome assembly [GO:0006334] | chromatin [GO:0000785]; cytoplasm [GO:0005737]; nucleus [GO:0005634] | chromatin binding [GO:0003682]; histone binding [GO:0042393] | PF00956; | 1.20.5.1500;3.30.1120.90; | Nucleosome assembly protein (NAP) family | null | SUBCELLULAR LOCATION: Nucleus. Cytoplasm. Note=Shuttles between cytoplasm and nucleus. | null | null | null | null | null | FUNCTION: May modulate chromatin structure by regulation of nucleosome assembly/disassembly. {ECO:0000250, ECO:0000269|PubMed:12569397}. | Oryza sativa subsp. indica (Rice) |
B8BB68 | BAK1_ORYSI | MAAPRWAVWAVLLLRLLVPAARVLANMEGDALHSLRTNLVDPNNVLQSWDPTLVNPCTWFHVTCNNDNSVIRVDLGNAALSGTLVPQLGQLKNLQYLELYSNNISGTIPSELGNLTNLVSLDLYLNNFTGPIPDSLGNLLKLRFLRLNNNSLSGSIPKSLTAITALQVLDLSNNNLSGEVPSTGSFSLFTPISFANNPSLCGPGTTKPCPGAPPFSPPPPYNPPTPVQSPGSSSSTGAIAGGVAAGAALLFAIPAIGFAWYRRRKPQEHFFDVPAEEDPEVHLGQLKRFSLRELQVATDTFSNKNILGRGGFGKVYKGRL... | 2.7.11.1 | null | brassinosteroid mediated signaling pathway [GO:0009742]; phosphorylation [GO:0016310] | plasma membrane [GO:0005886] | ATP binding [GO:0005524]; protein homodimerization activity [GO:0042803]; protein serine kinase activity [GO:0106310]; protein serine/threonine kinase activity [GO:0004674] | PF00560;PF08263;PF07714; | 3.80.10.10;1.20.5.510;1.10.510.10; | Protein kinase superfamily, Ser/Thr protein kinase family | null | SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:Q6Z4U4}; Single-pass membrane protein {ECO:0000255}. | CATALYTIC ACTIVITY: Reaction=ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-[protein]; Xref=Rhea:RHEA:17989, Rhea:RHEA-COMP:9863, Rhea:RHEA-COMP:11604, ChEBI:CHEBI:15378, ChEBI:CHEBI:29999, ChEBI:CHEBI:30616, ChEBI:CHEBI:83421, ChEBI:CHEBI:456216; EC=2.7.11.1; Evidence={ECO:0000305}; CATALYTIC ACTIVITY: React... | null | null | null | null | FUNCTION: LRR receptor kinase involved in defense response. Does not seem to be required specifically for XA21-mediated immunity or basal resistance to Xanthomonas oryzae pv. oryzae (Xoo), or immunity to Magnaporthe oryzae. Involved in brassinosteroid (BR) signaling pathway. Acts as a coreceptor of BRI1. Forms at the p... | Oryza sativa subsp. indica (Rice) |
B8CH91 | FADB_SHEPW | MIYQSPTIEVELLEDNIAHLCFNAQGSVNKFDRETIDSLNAALDSIKQNNSIKGLMLTSAKPAFIVGADITEFLGLFAEEDAVLLSWLEEANVVFNKLEDLPFPTISAINGFALGAGCETILATDFRVADTTARIGLPETKLGIIPGFGGTVRLPRVVGTDNALEWITSGKDQRPEAALNVGAIDALVAPEQLQSAALKMLKDAIAEKLDWQTRRAKKLAPLTLPKLEAMMSFATAKGMVFKVAGKHYPAPMAVVSVIEKAAQLDRAGALKVEHQAFLKLAKTEVAQSLIGIFLNDQLVKGKAKKAGKLAKKVNSAAVLG... | 1.1.1.35; 4.2.1.17; 5.1.2.3; 5.3.3.8 | null | fatty acid beta-oxidation [GO:0006635] | fatty acid beta-oxidation multienzyme complex [GO:0036125] | 3-hydroxyacyl-CoA dehydrogenase activity [GO:0003857]; 3-hydroxybutyryl-CoA epimerase activity [GO:0008692]; delta(3)-delta(2)-enoyl-CoA isomerase activity [GO:0004165]; enoyl-CoA hydratase activity [GO:0004300]; NAD+ binding [GO:0070403] | PF00725;PF02737;PF00378; | 1.10.1040.50;3.40.50.720; | Enoyl-CoA hydratase/isomerase family; 3-hydroxyacyl-CoA dehydrogenase family | null | null | CATALYTIC ACTIVITY: Reaction=a (3S)-3-hydroxyacyl-CoA + NAD(+) = a 3-oxoacyl-CoA + H(+) + NADH; Xref=Rhea:RHEA:22432, ChEBI:CHEBI:15378, ChEBI:CHEBI:57318, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945, ChEBI:CHEBI:90726; EC=1.1.1.35; Evidence={ECO:0000255|HAMAP-Rule:MF_01621}; CATALYTIC ACTIVITY: Reaction=a (3S)-3-hydroxyacyl-... | null | PATHWAY: Lipid metabolism; fatty acid beta-oxidation. {ECO:0000255|HAMAP-Rule:MF_01621}. | null | null | FUNCTION: Involved in the aerobic and anaerobic degradation of long-chain fatty acids via beta-oxidation cycle. Catalyzes the formation of 3-oxoacyl-CoA from enoyl-CoA via L-3-hydroxyacyl-CoA. It can also use D-3-hydroxyacyl-CoA and cis-3-enoyl-CoA as substrate. {ECO:0000255|HAMAP-Rule:MF_01621}. | Shewanella piezotolerans (strain WP3 / JCM 13877) |
B8EIZ7 | TMM_METSB | MTRVAIIGAGPSGLAQLRAFQSAGKKGAAIPELVCFEKQSDWGGLWNYTWRTGVDEYGEPVHGSMYRYLWSNGPKECLEFADYSFEEHFGRPIPSYPPRAVLHDYIMGRVEKSDVRKFVRFSTVVRWIDFDETTQLFTVTVKDLKKDELYSETFDYVVVASGHFSTPNVPHFPGIEVFPGRVLHAHDFRDANEFVGKNLLVVGSSYSAEDIASQCYKYGAKSITFSYRSKPLNFDWPECFTVKPLLTKLTGKTAHFKDGSEAVVDAVLLCTGYLHHFPFLADNLRLKTNNRLYPAGLYKGIFWQDNPKLIYLGMQDQYFT... | 1.14.13.148 | COFACTOR: Name=FAD; Xref=ChEBI:CHEBI:57692; Evidence={ECO:0000250|UniProtKB:A3SLM3}; | null | null | flavin adenine dinucleotide binding [GO:0050660]; hypotaurine dehydrogenase activity [GO:0047822]; N,N-dimethylaniline monooxygenase activity [GO:0004499]; NADP binding [GO:0050661]; trimethylamine monooxygenase activity [GO:0034899] | PF00743; | 3.50.50.60; | FMO family | null | null | CATALYTIC ACTIVITY: Reaction=NADPH + O2 + trimethylamine = H2O + NADP(+) + trimethylamine N-oxide; Xref=Rhea:RHEA:31979, ChEBI:CHEBI:15377, ChEBI:CHEBI:15379, ChEBI:CHEBI:15724, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349, ChEBI:CHEBI:58389; EC=1.14.13.148; Evidence={ECO:0000269|PubMed:22006322}; PhysiologicalDirection=left-t... | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=9.4 uM for TMA {ECO:0000269|PubMed:22006322}; KM=89.7 uM for DMA {ECO:0000269|PubMed:22006322}; KM=10.3 uM for DMS {ECO:0000269|PubMed:22006322}; KM=3575 uM for DMSO {ECO:0000269|PubMed:22006322}; KM=3139 uM for cysteamine {ECO:0000269|PubMed:22006322}; KM=28.2 uM ... | null | null | null | FUNCTION: Catalyzes the oxidation of trimethylamine (TMA) to produce trimethylamine N-oxide (TMAO) (PubMed:22006322). In vitro, has a broad substrate specificity, oxidizing many nitrogen- and sulfur-containing compounds, including dimethylamine (DMA), dimethylsulfide (DMS), dimethylsulfoxide (DMSO), cysteamine, methima... | Methylocella silvestris (strain DSM 15510 / CIP 108128 / LMG 27833 / NCIMB 13906 / BL2) |
B8GYI7 | OBG_CAUVN | MKFLDQCKIYIRSGNGGGGSVSFRREKYIEYGGPDGGDGGRGGDVWIEAVEGLNTLIDYRYQQHFKAGTGVHGMGRARHGAAGEDVVLKVPVGTEVLEEDKETLIADLDHAGMRLLLAKGGNGGWGNLHFKGPVNQAPKYANPGQEGEERWIWLRLKLIADVGLVGLPNAGKSTFLAAASAAKPKIADYPFTTLTPNLGVVDLSSSERFVLADIPGLIEGASEGAGLGTRFLGHVERSATLIHLIDATQDDVAGAYETIRGELEAYGDELADKAEILALNKIDALDEETLAEKVAELEAVSGIKPRLVSGVSGQGVTELL... | 3.6.5.- | COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000255|HAMAP-Rule:MF_01454}; | ribosome biogenesis [GO:0042254] | cytoplasm [GO:0005737] | GTP binding [GO:0005525]; GTPase activity [GO:0003924]; magnesium ion binding [GO:0000287] | PF01018;PF01926; | 2.70.210.12;3.40.50.300; | TRAFAC class OBG-HflX-like GTPase superfamily, OBG GTPase family | null | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_01454, ECO:0000269|PubMed:14702318}. Note=Cosediments in sucrose gradients with the 50S ribosomal subunit. | null | null | null | null | null | FUNCTION: An essential GTPase which binds GTP, GDP and ppGpp with moderate affinity (with a twofold preference for GDP over GTP), shows high guanine nucleotide exchange rate constants for both nucleotides, and has a relatively low GTP hydrolysis rate. Deletion of the 159 N-terminal residues makes a protein that is non-... | Caulobacter vibrioides (strain NA1000 / CB15N) (Caulobacter crescentus) |
B8GZM2 | PLED_CAUVN | MSARILVVDDIEANVRLLEAKLTAEYYEVSTAMDGPTALAMAARDLPDIILLDVMMPGMDGFTVCRKLKDDPTTRHIPVVLITALDGRGDRIQGLESGASDFLTKPIDDVMLFARVRSLTRFKLVIDELRQREASGRRMGVIAGAAARLDGLGGRVLIVDDNERQAQRVAAELGVEHRPVIESDPEKAKISAGGPVDLVIVNAAAKNFDGLRFTAALRSEERTRQLPVLAMVDPDDRGRMVKALEIGVNDILSRPIDPQELSARVKTQIQRKRYTDYLRNNLDHSLELAVTDQLTGLHNRRYMTGQLDSLVKRATLGGDP... | 2.7.7.65 | COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000269|PubMed:17697997}; Note=Binds 2 Mg(2+) per monomer. {ECO:0000269|PubMed:17697997}; | cell adhesion involved in single-species biofilm formation [GO:0043709]; cell cycle [GO:0007049]; cell differentiation [GO:0030154]; negative regulation of bacterial-type flagellum-dependent cell motility [GO:1902201]; phosphorelay signal transduction system [GO:0000160] | cytoplasm [GO:0005737]; plasma membrane [GO:0005886] | diguanylate cyclase activity [GO:0052621]; GTP binding [GO:0005525]; metal ion binding [GO:0046872] | PF00990;PF00072; | 3.30.70.270;3.40.50.2300; | null | PTM: Phosphorylated by PleC and DivJ. Phosphorylation stimulates cyclase activity. {ECO:0000269|PubMed:12622822, ECO:0000269|PubMed:15075296}. | SUBCELLULAR LOCATION: Cytoplasm. Note=Phosphorylated PleD localizes to the differentiating pole. {ECO:0000269|PubMed:15075296}. | CATALYTIC ACTIVITY: Reaction=2 GTP = 3',3'-c-di-GMP + 2 diphosphate; Xref=Rhea:RHEA:24898, ChEBI:CHEBI:33019, ChEBI:CHEBI:37565, ChEBI:CHEBI:58805; EC=2.7.7.65; Evidence={ECO:0000269|PubMed:15075296}; | null | PATHWAY: Purine metabolism; 3',5'-cyclic di-GMP biosynthesis. | null | null | FUNCTION: Response regulator that is part of a signal transduction pathway controlling cell differentiation in the swarmer-to-stalked cell transition. {ECO:0000269|PubMed:12622822}.; FUNCTION: Catalyzes the condensation of two GTP molecules to the cyclic dinucleotide di-GMP (c-di-GMP), which acts as a secondary messeng... | Caulobacter vibrioides (strain NA1000 / CB15N) (Caulobacter crescentus) |
B8H444 | FTSH_CAUVN | MNFRNLAIWLVIVAVLGGVFVVSQNSRTKSSSEISYSQLLKDVDAGKIKSAEIAGQTVLAKTADNKTLTVNAPMNSEELVNRMVAKNADVKFKSGSISFLAILVQLLPILLVVGVWLFLMRQMQGGAKGAMGFGKSKARLLTENKNRITFEDVAGVDEAKEELQEVVDFLKDPAKFQRLGGKIPKGALLVGPPGTGKTLIARAVAGEAGVPFFTISGSDFVEMFVGVGASRVRDMFEQAKKNAPCIIFIDEIDAVGRHRGAGLGGGNDEREQTLNQLLVEMDGFEANEGIILIAATNRPDVLDPALLRPGRFDRQVVVPN... | 3.4.24.- | COFACTOR: Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000255|HAMAP-Rule:MF_01458}; Note=Binds 1 zinc ion per subunit. {ECO:0000255|HAMAP-Rule:MF_01458}; | cell cycle [GO:0007049]; cell division [GO:0051301]; protein catabolic process [GO:0030163]; proteolysis [GO:0006508] | plasma membrane [GO:0005886] | ATP binding [GO:0005524]; ATP hydrolysis activity [GO:0016887]; ATP-dependent peptidase activity [GO:0004176]; metalloendopeptidase activity [GO:0004222]; zinc ion binding [GO:0008270] | PF00004;PF17862;PF06480;PF01434; | 1.10.8.60;3.30.720.210;3.40.50.300;1.20.58.760; | AAA ATPase family; Peptidase M41 family | null | SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000255|HAMAP-Rule:MF_01458}; Multi-pass membrane protein {ECO:0000255|HAMAP-Rule:MF_01458}; Cytoplasmic side {ECO:0000255|HAMAP-Rule:MF_01458}. | null | null | null | null | null | FUNCTION: Acts as a processive, ATP-dependent zinc metallopeptidase for both cytoplasmic and membrane proteins. Plays a role in the quality control of integral membrane proteins. {ECO:0000255|HAMAP-Rule:MF_01458}.; FUNCTION: Absence of FtsH leads to increased sigma-32 levels, which suggests, in analogy to E.coli, that ... | Caulobacter vibrioides (strain NA1000 / CB15N) (Caulobacter crescentus) |
B8JK39 | ITA9_MOUSE | MGGPAAARTGAGGLRALLLALVAAGVPAGAYNLDAQRPVRFQGPSGSFFGYAVLEHFHDNTRWVLVGAPKADSKYSTSVKSPGAVFKCRVHTNPDRRCTELDMARGRTRGAPCGKTCRGDRDDEWMGVSLARQPRADGRVLACAHRWKNIYYEADHILPHGFCYLIPSNLQAKGKVLIPCYEEYKKKYGEEHGSCQAGIAGFFTEELVVMGAPGSFYWAGTLKVLNLTDNTYFKLNDEAIMNRRYTYLGYAVTAGHFSHPSITDVVGGAPQDEGIGKVYIFRADRRSGTLIKIFQASGKKMGSYFGSSLCAVDLNMDGLS... | null | null | cell adhesion [GO:0007155]; cell adhesion mediated by integrin [GO:0033627]; cell-cell adhesion [GO:0098609]; cell-matrix adhesion [GO:0007160]; integrin-mediated signaling pathway [GO:0007229]; negative regulation of vasoconstriction [GO:0045906]; neutrophil chemotaxis [GO:0030593] | basal plasma membrane [GO:0009925]; external side of plasma membrane [GO:0009897]; integrin alpha9-beta1 complex [GO:0034679]; integrin complex [GO:0008305] | collagen binding [GO:0005518]; integrin binding [GO:0005178]; integrin binding involved in cell-matrix adhesion [GO:0098640]; laminin binding [GO:0043236]; metal ion binding [GO:0046872] | PF01839;PF08441;PF20805;PF20806; | 1.20.5.930;2.130.10.130;2.60.40.1460;2.60.40.1510;2.60.40.1530; | Integrin alpha chain family | null | SUBCELLULAR LOCATION: Membrane {ECO:0000255}; Single-pass type I membrane protein {ECO:0000255}. | null | null | null | null | null | FUNCTION: Integrin alpha-9/beta-1 (ITGA9:ITGB1) is a receptor for VCAM1, cytotactin and osteopontin. It recognizes the sequence A-E-I-D-G-I-E-L in cytotactin. ITGA9:ITGB1 may play a crucial role in SVEP1/polydom-mediated myoblast cell adhesion (PubMed:22654117). Integrin ITGA9:ITGB1 represses PRKCA-mediated L-type volt... | Mus musculus (Mouse) |
B8JLQ9 | CBPO_DANRE | MMQASITSILVVLTLVAQDRLAGGLEHKSYDYTKYHTMDEISAWMNQMQRENPDVVSTMTYGQTYEKRNITLLKIGFSSTTPKKAIWMDCGIHAREWIAPAFCQHFVKEVLGSYKTDSRVNMLFKNLDFYITPVLNMDGYIYSWLNNSTRLWRKSRSPCHENSTCSGTDLNRNFYANWGMVGISRNCCSEVYNGATALSEPEAEAVTDFLGAHQNHLLCYLTIHSYGQLILVPYGHPNISAPNYDELMEVGLAAAKAIKAVHGKSYKVGSSPDVLYPNSGSSRDFARLIGIPYSFTFELRDEGQHGFILPEDQIQPTCQE... | 3.4.17.- | COFACTOR: Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000250|UniProtKB:P00730}; | proteolysis [GO:0006508] | apical plasma membrane [GO:0016324]; extracellular space [GO:0005615]; plasma membrane [GO:0005886]; side of membrane [GO:0098552] | metallocarboxypeptidase activity [GO:0004181]; zinc ion binding [GO:0008270] | PF00246; | 3.40.630.10; | Peptidase M14 family | PTM: N-glycosylated. {ECO:0000269|PubMed:21921028}. | SUBCELLULAR LOCATION: Apical cell membrane {ECO:0000250|UniProtKB:Q8IVL8}; Lipid-anchor, GPI-anchor {ECO:0000250|UniProtKB:Q8IVL8}. | null | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=346 uM for 3-(2-furyl)acryloyl-Glu-Glu (at pH 7.5) {ECO:0000269|PubMed:21921028}; KM=324 uM for 3-(2-furyl)acryloyl-Phe-Phe (at pH 7.5) {ECO:0000269|PubMed:21921028}; KM=794 uM for 3-(2-furyl)acryloyl-Phe-Ala (at pH 7.5) {ECO:0000269|PubMed:21921028}; KM=743 uM for... | null | BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 6.5-7.5. {ECO:0000269|PubMed:21921028}; | null | FUNCTION: Carboxypeptidase which preferentially cleaves C-terminal acidic residues from peptides and proteins. Can also cleave C-terminal hydrophobic amino acids, with a preference for small residues over large residues. {ECO:0000269|PubMed:21921028}. | Danio rerio (Zebrafish) (Brachydanio rerio) |
B8K1W0 | VM3DK_DABRR | MMQVLLVTICLAVFPYHGSSIILESGNVNDYEVVYPQKVTAMPKEAVKQPEQKYEDAMQYKFEVNGEPVLLHLEKNKDLFSEDYSETHYSPDGREITTKPLVQDHCYYHGHIQNDAHSSASISACNGLKGHFKLRGEMYLIEPLKLSDSEAHAVYKYENVEKEDEALKMCGVTQTNWESDEPIKKASLLVATSERNRYFNPYSYVELIITVDHSMVTKYKNDLTAIRTWVFELVNTINEIFKYLYIRVPLVGLEIWKNRDLINVTSAANVTLDLFGEWRKSYLLPRKIHDNSQLLTAIDLNGLTIGMAYVSTMCQSKYSV... | 3.4.24.- | COFACTOR: Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000250}; Note=Binds 1 zinc ion per subunit. {ECO:0000250}; | proteolysis [GO:0006508] | extracellular region [GO:0005576]; plasma membrane [GO:0005886] | metal ion binding [GO:0046872]; metalloendopeptidase activity [GO:0004222]; toxin activity [GO:0090729] | PF08516;PF00200;PF01562;PF01421; | 3.40.390.10;4.10.70.10; | Venom metalloproteinase (M12B) family, P-III subfamily, P-IIIa sub-subfamily | null | SUBCELLULAR LOCATION: Secreted {ECO:0000250}. | null | null | null | null | null | FUNCTION: Snake venom zinc metalloprotease that possesses high hemorrhagic activity (minimum hemorrhagic dose (MHD)=0.82 ug) when subcutaneously injected into mice. May also potently degrade alpha chain of fibrinogen (FGA). | Daboia russelii (Russel's viper) (Vipera russelii) |
B8K1W2 | ABCBB_CANLF | MSDAVILRSVKKFGEDNYGFESSTFYNNDKNSGLQDERKGDSSQVGFFQLFRFSSTTDIWLMFVGSLCAFLHGLSHPGVLLIFGTMTDVFIAYDTELQELKIPGKACVNNTIVWINSSLNQNVTNGTQCGLLDIESEMIKFASYYAGIALLVLITGYIQICFWVIAAARQIQKMRKISFRKVMRMEIGWFDCNSVGELNTRFSDDINRVNDAIADQMPIFIQRMTTSICGFLLGFYQGWKLTLVIISVSPLIGIGAAIIGLSVSKFTDYELKAYAKAGSVADEVISSMRTVAAFGGEKKEVERYEKNLVFAQRWGIRKGI... | 7.6.2.- | null | bile acid and bile salt transport [GO:0015721]; bile acid metabolic process [GO:0008206]; canalicular bile acid transport [GO:0015722]; cholesterol homeostasis [GO:0042632]; fatty acid metabolic process [GO:0006631]; phospholipid homeostasis [GO:0055091]; positive regulation of bile acid secretion [GO:0120189]; protein... | apical plasma membrane [GO:0016324]; cell surface [GO:0009986]; endosome [GO:0005768]; intercellular canaliculus [GO:0046581]; intracellular canaliculus [GO:0046691]; plasma membrane [GO:0005886]; recycling endosome [GO:0055037]; recycling endosome membrane [GO:0055038] | ABC-type bile acid transporter activity [GO:0015432]; ABC-type oligopeptide transporter activity [GO:0015421]; ABC-type xenobiotic transporter activity [GO:0008559]; ATP binding [GO:0005524]; ATP hydrolysis activity [GO:0016887]; bile acid transmembrane transporter activity [GO:0015125]; canalicular bile acid transmemb... | PF00664;PF00005; | 1.20.1560.10;3.40.50.300; | ABC transporter superfamily, ABCB family, Multidrug resistance exporter (TC 3.A.1.201) subfamily | PTM: N-glycosylated. {ECO:0000250|UniProtKB:O95342}.; PTM: Ubiquitinated; short-chain ubiquitination regulates cell-Surface expression of ABCB11. {ECO:0000250|UniProtKB:O95342}. | SUBCELLULAR LOCATION: Apical cell membrane {ECO:0000250|UniProtKB:O70127}; Multi-pass membrane protein {ECO:0000250|UniProtKB:O70127}. Recycling endosome membrane {ECO:0000250|UniProtKB:O70127}; Multi-pass membrane protein {ECO:0000250|UniProtKB:O70127}. Endosome {ECO:0000250|UniProtKB:O70127}. Cell membrane {ECO:00002... | CATALYTIC ACTIVITY: Reaction=ATP + cholate(in) + H2O = ADP + cholate(out) + H(+) + phosphate; Xref=Rhea:RHEA:50048, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:29747, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:456216; Evidence={ECO:0000250|UniProtKB:O95342}; PhysiologicalDirection=left-to-right; Xref=Rhea:... | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=33.7 uM for taurocholate {ECO:0000269|PubMed:18985798}; Vmax=219 pmol/min/mg enzyme for taurocholate transport {ECO:0000269|PubMed:18985798}; | null | null | null | FUNCTION: Catalyzes the transport of the major hydrophobic bile salts, such as taurine and glycine-conjugated cholic acid across the canalicular membrane of hepatocytes in an ATP-dependent manner, therefore participates in hepatic bile acid homeostasis and consequently to lipid homeostasis through regulation of biliary... | Canis lupus familiaris (Dog) (Canis familiaris) |
B8LIX8 | IFT25_CHLRE | MKDYAREENGGLVVMASCSDERFPPENMLDGKDNTFWVTTGMFPQEFVLRLESCIRVSKITTLSLNVRKLAVEKCDQDKPDQFEKVFEVELANRGDRLQTEVHQVNIRAKYLKFILLQGHGEFATVNRVSVVGGDDDGGGYDEPGGGYGSMQRQPSMGYGGGGGSAATGFAADPGNAAAGGGGGFEDEF | null | null | intraciliary transport [GO:0042073] | cytoplasm [GO:0005737]; cytoskeleton [GO:0005856]; intraciliary transport particle B [GO:0030992]; motile cilium [GO:0031514] | metal ion binding [GO:0046872] | null | 2.60.120.260; | IFT25 family | PTM: Phosphorylated. {ECO:0000269|PubMed:19412537}. | SUBCELLULAR LOCATION: Cell projection, cilium, flagellum. Cytoplasm, cytoskeleton, flagellum basal body. Note=Colocalizes with IFT27 at the distal-most portion of basal bodies, probably the transition zones, and concentrates in the basal body region. | null | null | null | null | null | FUNCTION: Component of the intraflagellar transport (IFT) complex B. Forms a subcomplex within the IFT complex B with IFT27. {ECO:0000269|PubMed:19412537}. | Chlamydomonas reinhardtii (Chlamydomonas smithii) |
B8M0U4 | ARO1_TALSN | MSMKMADPTKISILGRESIVADYSIWGTYIVQDLLTNLSSTTYVLVTDTNLGSIYLEKFSKIFNEAAAALSPPPRLLTKEIPPGENSKSRQGKADIEDWMLQQTCGRDTVIIALGGGVIGDLLGFVASTYMRGIRFVQVPTTLLAMVDSSIGGKTAIDTPLGKNLIGAIWQPQRIYIDIDFIDTLPEREFINGMAEVIKTAAISDEKEFAALERHADAILNAARSKARKGRFDAVRQELKDHIVASARHKAYVVTADEREGGLRNLLNLGHSIGHAIEAILSPQVLHGECVAIGMVKELELARYLGILKPVAVSRMIKCL... | 1.1.1.25; 2.5.1.19; 2.7.1.71; 4.2.1.10; 4.2.3.4 | COFACTOR: Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Note=Binds 2 Zn(2+) ions per subunit.; | amino acid biosynthetic process [GO:0008652]; aromatic amino acid family biosynthetic process [GO:0009073]; chorismate biosynthetic process [GO:0009423]; phosphorylation [GO:0016310] | cytoplasm [GO:0005737] | 3-dehydroquinate dehydratase activity [GO:0003855]; 3-dehydroquinate synthase activity [GO:0003856]; 3-phosphoshikimate 1-carboxyvinyltransferase activity [GO:0003866]; ATP binding [GO:0005524]; metal ion binding [GO:0046872]; shikimate 3-dehydrogenase (NADP+) activity [GO:0004764]; shikimate kinase activity [GO:000476... | PF01761;PF01487;PF00275;PF18317;PF08501;PF01202; | 3.40.50.1970;3.20.20.70;1.20.1090.10;3.65.10.10;3.40.50.10860;3.40.50.720;3.40.50.300; | Sugar phosphate cyclases superfamily, Dehydroquinate synthase family; EPSP synthase family; Shikimate kinase family; Type-I 3-dehydroquinase family; Shikimate dehydrogenase family | null | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_03143}. | CATALYTIC ACTIVITY: Reaction=7-phospho-2-dehydro-3-deoxy-D-arabino-heptonate = 3-dehydroquinate + phosphate; Xref=Rhea:RHEA:21968, ChEBI:CHEBI:32364, ChEBI:CHEBI:43474, ChEBI:CHEBI:58394; EC=4.2.3.4; Evidence={ECO:0000255|HAMAP-Rule:MF_03143}; CATALYTIC ACTIVITY: Reaction=3-dehydroquinate = 3-dehydroshikimate + H2O; Xr... | null | PATHWAY: Metabolic intermediate biosynthesis; chorismate biosynthesis; chorismate from D-erythrose 4-phosphate and phosphoenolpyruvate: step 2/7. {ECO:0000255|HAMAP-Rule:MF_03143}.; PATHWAY: Metabolic intermediate biosynthesis; chorismate biosynthesis; chorismate from D-erythrose 4-phosphate and phosphoenolpyruvate: st... | null | null | FUNCTION: The AROM polypeptide catalyzes 5 consecutive enzymatic reactions in prechorismate polyaromatic amino acid biosynthesis. {ECO:0000255|HAMAP-Rule:MF_03143}. | Talaromyces stipitatus (strain ATCC 10500 / CBS 375.48 / QM 6759 / NRRL 1006) (Penicillium stipitatum) |
B8M9J8 | TROPB_TALSN | MPGSLIDTRQQPLSVGIVGGGIIGVILAAGLVRRGIDVKVFEQARGFREIGAGMAFTANAVRCMEMLDPAIVWALRSSGAVPISIGDHQAEARDYLRWVDGYHESSKRLYQLDAGIRGFEACRRDQFLEALVKVLPEGIVECQKRLQKIHEKNETEKVTLEFADGTFAHVDCVIGADGIRSRVRQHLFGEDSPYSHPHYSHKFAFRGLITMENAISALGEDKARTLNMHVGPNAHLIHYPVANETMVNIAAFVSDPEEWPDKLSLVGPATREEAMGYFANWNPGLRAVLGFMPENIDRWAMFDTYDYPAPFFSRGKICLV... | 1.-.-.- | COFACTOR: Name=FAD; Xref=ChEBI:CHEBI:57692; Evidence={ECO:0000269|PubMed:31346489}; | secondary metabolite biosynthetic process [GO:0044550] | membrane [GO:0016020] | FAD binding [GO:0071949]; monooxygenase activity [GO:0004497] | PF01494; | 3.50.50.60; | PaxM FAD-dependent monooxygenase family | null | SUBCELLULAR LOCATION: Membrane; Single-pass membrane protein {ECO:0000255}. | null | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=65.3 uM for NADH {ECO:0000269|PubMed:22508998}; KM=158.2 uM for NADPH {ECO:0000269|PubMed:22508998}; | PATHWAY: Secondary metabolite biosynthesis. {ECO:0000269|PubMed:22508998, ECO:0000269|PubMed:31346489}. | null | null | FUNCTION: FAD-dependent monooxygenase; part of the gene cluster that mediates the biosynthesis of the tropolone class of fungal maleic anhydrides (PubMed:22508998, PubMed:24863423, PubMed:31346489). Within the pathway, tropB catalyzes a synthetically challenging asymmetric oxidative dearomatization reaction to convert ... | Talaromyces stipitatus (strain ATCC 10500 / CBS 375.48 / QM 6759 / NRRL 1006) (Penicillium stipitatum) |
B8N2C8 | CP51A_ASPFN | MIFSRSMASFTLVSAYAAAGLLAIIVLNLLRQLLFRNKTDPPLVFHWIPFLGSTVTYGMDPYAFFFSCRQKYGDIFTFILLGRKITVYLGIQGNEFILNGKLKDVNAEEIYSPLTTPVFGSDIVYDCPNSKLMEQKKFIKFGLTQAALESHVPLIEKEVLDYLKTSPNFKGTSGRVEITDAMAEITIFTAGRALQGEEVRKKLTAEFADLYHDLDRGFTPINFMLPWAPLPRNRKRDAAHARMREIYMDIINERRKNPDRETSDMIWNLMHCTYKNGQPLPDKEIAHMMITLLMAGQHSSSSISSWIMLRLASEPAVMEE... | 1.14.14.154 | COFACTOR: Name=heme; Xref=ChEBI:CHEBI:30413; Evidence={ECO:0000250|UniProtKB:Q4WNT5}; | bile acid biosynthetic process [GO:0006699]; cholesterol homeostasis [GO:0042632]; methylation [GO:0032259]; sterol biosynthetic process [GO:0016126] | endoplasmic reticulum membrane [GO:0005789] | heme binding [GO:0020037]; iron ion binding [GO:0005506]; methyltransferase activity [GO:0008168]; oxysterol 7-alpha-hydroxylase activity [GO:0008396]; steroid 7-alpha-hydroxylase activity [GO:0008387]; sterol 14-demethylase activity [GO:0008398] | PF00067; | 1.10.630.10; | Cytochrome P450 family | null | SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000305}; Single-pass membrane protein {ECO:0000255}. | CATALYTIC ACTIVITY: Reaction=a 14alpha-methyl steroid + 3 O2 + 3 reduced [NADPH--hemoprotein reductase] = a Delta(14) steroid + formate + 4 H(+) + 4 H2O + 3 oxidized [NADPH--hemoprotein reductase]; Xref=Rhea:RHEA:54028, Rhea:RHEA-COMP:11964, Rhea:RHEA-COMP:11965, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379,... | null | PATHWAY: Steroid biosynthesis; sterol biosynthesis. {ECO:0000250|UniProtKB:Q4WNT5}. | null | null | FUNCTION: Sterol 14alpha-demethylase, encoded by cyp51A, cyp51B and cyp51C, that plays a critical role in the third module of ergosterol biosynthesis pathway, being ergosterol the major sterol component in fungal membranes that participates in a variety of functions (By similarity). The third module or late pathway inv... | Aspergillus flavus (strain ATCC 200026 / FGSC A1120 / IAM 13836 / NRRL 3357 / JCM 12722 / SRRC 167) |
B8N4Q9 | ARO1_ASPFN | MAEPTKIKILGQESIIADFGLWRNYVAKDLISGCPSTTYVLITDTNIGSIYTPGFQKTFEDAATAVSPAPRLLVYHCPPGEVSKSRQTKADIEDWMLSQSPPCGRDTVVIALGGGVIGDLTGFVASTYMRGVRYVQVPTTLLAMVDSSIGGKTAIDTPLGKNLIGAIWQPTRIYIDLEFLETLPVREFVNGMAEVIKTAAISSEEEFTALEDNAEAILTAVRSERKPGQRWFEGIEDILKARILASARHKAYVVSADEREGGLRNLLNWGHSIGHAIEAILTPQVLHGECVAIGMVKEAELARHLGILKGVAVARIVKCI... | 1.1.1.25; 2.5.1.19; 2.7.1.71; 4.2.1.10; 4.2.3.4 | COFACTOR: Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Note=Binds 2 Zn(2+) ions per subunit.; | amino acid biosynthetic process [GO:0008652]; aromatic amino acid family biosynthetic process [GO:0009073]; chorismate biosynthetic process [GO:0009423]; phosphorylation [GO:0016310] | cytoplasm [GO:0005737] | 3-dehydroquinate dehydratase activity [GO:0003855]; 3-dehydroquinate synthase activity [GO:0003856]; 3-phosphoshikimate 1-carboxyvinyltransferase activity [GO:0003866]; ATP binding [GO:0005524]; metal ion binding [GO:0046872]; shikimate 3-dehydrogenase (NADP+) activity [GO:0004764]; shikimate kinase activity [GO:000476... | PF01761;PF01487;PF00275;PF18317;PF08501;PF01202; | 3.40.50.1970;3.20.20.70;1.20.1090.10;3.65.10.10;3.40.50.10860;3.40.50.720;3.40.50.300; | Sugar phosphate cyclases superfamily, Dehydroquinate synthase family; EPSP synthase family; Shikimate kinase family; Type-I 3-dehydroquinase family; Shikimate dehydrogenase family | null | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_03143}. | CATALYTIC ACTIVITY: Reaction=7-phospho-2-dehydro-3-deoxy-D-arabino-heptonate = 3-dehydroquinate + phosphate; Xref=Rhea:RHEA:21968, ChEBI:CHEBI:32364, ChEBI:CHEBI:43474, ChEBI:CHEBI:58394; EC=4.2.3.4; Evidence={ECO:0000255|HAMAP-Rule:MF_03143}; CATALYTIC ACTIVITY: Reaction=3-dehydroquinate = 3-dehydroshikimate + H2O; Xr... | null | PATHWAY: Metabolic intermediate biosynthesis; chorismate biosynthesis; chorismate from D-erythrose 4-phosphate and phosphoenolpyruvate: step 2/7. {ECO:0000255|HAMAP-Rule:MF_03143}.; PATHWAY: Metabolic intermediate biosynthesis; chorismate biosynthesis; chorismate from D-erythrose 4-phosphate and phosphoenolpyruvate: st... | null | null | FUNCTION: The AROM polypeptide catalyzes 5 consecutive enzymatic reactions in prechorismate polyaromatic amino acid biosynthesis. {ECO:0000255|HAMAP-Rule:MF_03143}. | Aspergillus flavus (strain ATCC 200026 / FGSC A1120 / IAM 13836 / NRRL 3357 / JCM 12722 / SRRC 167) |
B8N7E5 | RSP5_ASPFN | MTCSQPNLRVTIIAADGLYKRDVFRFPDPFAVATVGGEQTHTTSVIKKTLNPYWNEMFDLRVNEDSILAIQIFDQKKFKKKDQGFLGVINVRIGDVIDLQMGGDEMLTRDLKKSNDNLVVHGKLIINLSTNLSTPNTNQANGLHRSHMQPSTSSGLVPQVSASTPQPSPGPSQADPTASNPSLHPQRVPSTTRPSSTIVPANGPPAPPNGQQGSRTNLSSFEDSQGRLPAGWERREDNLGRTYYVDHNTRTTTWTRPSNNYNEQTSRTQREASMQLERRAHQSRMLPEDRTGASSPNLQENQQQAQTPPAGGSASAVSMM... | 2.3.2.26 | null | chromatin organization [GO:0006325]; late endosome to vacuole transport via multivesicular body sorting pathway [GO:0032511]; mitochondria-associated ubiquitin-dependent protein catabolic process [GO:0072671]; mitochondrion organization [GO:0007005]; nonfunctional rRNA decay [GO:0070651]; poly(A)+ mRNA export from nucl... | cellular bud tip [GO:0005934]; cytosolic ribosome [GO:0022626]; endosome membrane [GO:0010008]; Golgi apparatus [GO:0005794]; nucleus [GO:0005634]; RSP5-BUL ubiquitin ligase complex [GO:1990306]; ubiquitin ligase complex [GO:0000151] | phosphatidylinositol binding [GO:0035091]; ubiquitin binding [GO:0043130]; ubiquitin protein ligase activity [GO:0061630] | PF00168;PF00632;PF00397; | 2.20.70.10;2.60.40.150;3.30.2160.10;3.30.2410.10;3.90.1750.10; | RSP5/NEDD4 family | null | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:P39940}. | CATALYTIC ACTIVITY: Reaction=S-ubiquitinyl-[E2 ubiquitin-conjugating enzyme]-L-cysteine + [acceptor protein]-L-lysine = [E2 ubiquitin-conjugating enzyme]-L-cysteine + N(6)-ubiquitinyl-[acceptor protein]-L-lysine.; EC=2.3.2.26; | null | PATHWAY: Protein modification; protein ubiquitination. | null | null | FUNCTION: E3 ubiquitin-protein ligase which accepts ubiquitin from an E2 ubiquitin-conjugating enzyme in the form of a thioester and then directly transfers the ubiquitin to targeted substrates. Probably involved in the regulatory network controlling carbon source utilization. {ECO:0000250|UniProtKB:Q5BDP1}. | Aspergillus flavus (strain ATCC 200026 / FGSC A1120 / IAM 13836 / NRRL 3357 / JCM 12722 / SRRC 167) |
B8NFL5 | CP51B_ASPFN | MGILAVILDSVCERCSGSSLWMLSTVALLSILVVSVVINVLRQLLFKNYKEPPLVFHWFPFIGSTISYGMDPYRFFFNCREKYGDIFTFVLLGKKTTVYLGTKGNDFILNGKLRDVCAEEVYSPLTTPVFGRHVVYDCPNAKLMEQKKGPNGVFDVCKTIAEITIYTASRSLQGKEVRSRFDSTFAELYHDLDMGFAPINFMLPWAPLPHNRKRDAAQKRMTETYMEIIKERRKAGSKKDSEDMVWNLMSCMYKDGTPVPDEEIAHMMIALLMAGQHSSSSTAAWIVLHLAASPEITEELYQEQLRILGHDMPPLTYENL... | 1.14.14.154 | COFACTOR: Name=heme; Xref=ChEBI:CHEBI:30413; Evidence={ECO:0000250|UniProtKB:E9QY26}; | ergosterol biosynthetic process [GO:0006696]; methylation [GO:0032259] | endoplasmic reticulum membrane [GO:0005789] | heme binding [GO:0020037]; iron ion binding [GO:0005506]; methyltransferase activity [GO:0008168]; sterol 14-demethylase activity [GO:0008398] | PF00067; | 1.10.630.10; | Cytochrome P450 family | null | SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000305}; Single-pass membrane protein {ECO:0000255}. | CATALYTIC ACTIVITY: Reaction=a 14alpha-methyl steroid + 3 O2 + 3 reduced [NADPH--hemoprotein reductase] = a Delta(14) steroid + formate + 4 H(+) + 4 H2O + 3 oxidized [NADPH--hemoprotein reductase]; Xref=Rhea:RHEA:54028, Rhea:RHEA-COMP:11964, Rhea:RHEA-COMP:11965, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379,... | null | PATHWAY: Steroid biosynthesis; sterol biosynthesis. {ECO:0000250|UniProtKB:E9QY26}. | null | null | FUNCTION: Sterol 14alpha-demethylase, encoded by cyp51A, cyp51B and cyp51C, that plays a critical role in the third module of ergosterol biosynthesis pathway, being ergosterol the major sterol component in fungal membranes that participates in a variety of functions (By similarity). The third module or late pathway inv... | Aspergillus flavus (strain ATCC 200026 / FGSC A1120 / IAM 13836 / NRRL 3357 / JCM 12722 / SRRC 167) |
B8NSJ0 | SKP1_ASPFN | MATPTLTFTSSDGVDIPVERDVAERSQLIKNMLEDLGETGEPIPIPNVNEAVLKKVIEWCTHHKNDPPSTGDDDDSRRKTTDIDEWDQKFMQVDQEMLFEIILAANYLDIKGLLDVGCKTVANMIKGKSPEEIRKTFNIQNDFTPEEEDQIRRENEWAEDR | null | null | exit from mitosis [GO:0010458]; G1/S transition of mitotic cell cycle [GO:0000082]; G2/M transition of mitotic cell cycle [GO:0000086]; kinetochore assembly [GO:0051382]; mitotic nuclear membrane biogenesis [GO:0101026]; negative regulation of cytoplasmic translation [GO:2000766]; negative regulation of mitotic metapha... | CBF3 complex [GO:0031518]; kinetochore [GO:0000776]; nuclear SCF ubiquitin ligase complex [GO:0043224]; RAVE complex [GO:0043291]; single-stranded DNA-dependent ATP-dependent DNA helicase complex [GO:0017117] | cullin family protein binding [GO:0097602]; DNA replication origin binding [GO:0003688]; ubiquitin protein ligase activity [GO:0061630] | PF01466;PF03931; | null | SKP1 family | null | null | null | null | PATHWAY: Protein modification; protein ubiquitination. | null | null | FUNCTION: Essential component of the SCF (SKP1-CUL1-F-box protein) E3 ubiquitin ligase complexes, which mediate the ubiquitination and subsequent proteasomal degradation of target proteins. Controls sulfur metabolite repression, probably by mediating the inactivation or degradation of the metR transcription factor (By ... | Aspergillus flavus (strain ATCC 200026 / FGSC A1120 / IAM 13836 / NRRL 3357 / JCM 12722 / SRRC 167) |
B8NUK6 | CP51C_ASPFN | MSWPRIGAYALLAFVAIMALNVTYQFLFRMLNKTRPPLVFHWIPFIGSTIHYGMDPYGFFFSCREKYGDIFTFILLGRPTTVYLGTQGNEFILNGKLKDVNAEEVYSPLTTPVFGSDVVYDCPNSKLIEQKKFIKFGLSQAALEAHVPLIEKEVEDYLAMSPNFHGTSGEVDIPAAMAEITIFTAGSALQGEEVRSKLTTEFAVLYHDLDKGFTPINFMLPWAPLPHNKKRDAAHARMRSIYIDIINKRRNAGDNVPEKLDMIGNLMQCTYKNGQPLPDKEIAHIMITLLMAGQHSSSSISSWIMLRLASQPAVVEELYQ... | 1.14.14.154 | COFACTOR: Name=heme; Xref=ChEBI:CHEBI:30413; | bile acid biosynthetic process [GO:0006699]; cholesterol homeostasis [GO:0042632]; sterol biosynthetic process [GO:0016126] | endoplasmic reticulum membrane [GO:0005789] | heme binding [GO:0020037]; iron ion binding [GO:0005506]; oxysterol 7-alpha-hydroxylase activity [GO:0008396]; steroid 7-alpha-hydroxylase activity [GO:0008387]; sterol 14-demethylase activity [GO:0008398] | PF00067; | 1.10.630.10; | Cytochrome P450 family | null | SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000305}; Single-pass membrane protein {ECO:0000255}. | CATALYTIC ACTIVITY: Reaction=a 14alpha-methyl steroid + 3 O2 + 3 reduced [NADPH--hemoprotein reductase] = a Delta(14) steroid + formate + 4 H(+) + 4 H2O + 3 oxidized [NADPH--hemoprotein reductase]; Xref=Rhea:RHEA:54028, Rhea:RHEA-COMP:11964, Rhea:RHEA-COMP:11965, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379,... | null | PATHWAY: Steroid biosynthesis; sterol biosynthesis. {ECO:0000250|UniProtKB:Q4WNT5}. | null | null | FUNCTION: Sterol 14alpha-demethylase, encoded by cyp51A, cyp51B and cyp51C, that plays a critical role in the third module of ergosterol biosynthesis pathway, being ergosterol the major sterol component in fungal membranes that participates in a variety of functions (By similarity). The third module or late pathway inv... | Aspergillus flavus (strain ATCC 200026 / FGSC A1120 / IAM 13836 / NRRL 3357 / JCM 12722 / SRRC 167) |
B8PYG1 | NSMF_DANRE | MGTVVSKKENLRNDAISSVAAKVRAARAFGEYLSHTRPENRNRSDHLLSDTFIGQETDSPDISRLNNNNSLQPYSQHTLIVKPSQEELQQGSQSAPLPTSSKRRLSVERSLSSEDQQNQRRTESSVKPARVYTITRERDMLGGQGSEESLELEVLKRTSEPSQINPPTGLRGSHHRGSQHRGNNGPTHQHHYGHAPMAQPLQSSGSTHNIRDWGSRRSRSREDCTPDCVACIRPHCQSQRSLDLDTSPHGGGKQHKKLERMYSEDRVSSEDREDHTNSWFPKENMFSFQTATTTMQAISNFRKHLRMVGSRRVKAQTFVD... | null | null | positive regulation of axon extension [GO:0045773]; positive regulation of neuron migration [GO:2001224]; regulation of neuronal synaptic plasticity [GO:0048168] | cell cortex [GO:0005938]; cytoplasm [GO:0005737]; cytoskeleton [GO:0005856]; dendrite [GO:0030425]; nuclear matrix [GO:0016363]; nuclear membrane [GO:0031965]; nucleus [GO:0005634]; plasma membrane [GO:0005886]; postsynaptic density [GO:0014069] | null | null | null | NSMF family | null | SUBCELLULAR LOCATION: Nucleus {ECO:0000250}. Nucleus envelope {ECO:0000250}. Nucleus membrane {ECO:0000250}. Nucleus matrix {ECO:0000250}. Cytoplasm {ECO:0000250}. Cytoplasm, cell cortex {ECO:0000250}. Cytoplasm, cytoskeleton {ECO:0000250}. Cell membrane {ECO:0000250}; Peripheral membrane protein {ECO:0000250}. Cell pr... | null | null | null | null | null | FUNCTION: Stimulates outgrowth of olfactory axons and migration of hypophysiotropic gonadotropin-releasing hormone 3 (GnRH3) neurons. May couple NMDA-sensitive glutamate receptor signaling to the nucleus and trigger long-lasting changes in the cytoarchitecture of dendrites and spine synapse processes. {ECO:0000269|PubM... | Danio rerio (Zebrafish) (Brachydanio rerio) |
B8Q0B2 | POPD1_PIG | MNYTESSPLAESTAIGFTPELGSITPVPSNETTCENWREIHHLVFHVANVFFAIGLVLPTTLHLHMILLRGMLTIGCTLYIVWATLYRCALDIMIWNSVFLGINVLHLSYLLYKKRPVKIEKELKGIYQRLFEPLRVPPDLFKRLTGQFCMIQTLKKGQAYAAEDKTSVDDRLSILLKGKMKVSYRGHFLHNIYPCAFIDSPEFRSTQMHKGEKFQVTIIADDNCRFLCWSRERLTYFLESEPFLYEVFRYLIGKDITNKLYSLNDPTLNDKTIKKLDHQLSLCTQLSMLEMRNSIVSTSDSEDGLHQFLRGTSSVSSLY... | null | null | epithelial cell-cell adhesion [GO:0090136]; heart development [GO:0007507]; positive regulation of locomotion [GO:0040017]; positive regulation of receptor recycling [GO:0001921]; regulation of cell shape [GO:0008360]; regulation of GTPase activity [GO:0043087]; regulation of membrane potential [GO:0042391]; response t... | bicellular tight junction [GO:0005923]; caveola [GO:0005901]; lateral plasma membrane [GO:0016328]; membrane [GO:0016020]; plasma membrane [GO:0005886]; sarcolemma [GO:0042383] | cAMP binding [GO:0030552]; structural molecule activity [GO:0005198] | PF04831; | null | Popeye family | null | SUBCELLULAR LOCATION: Lateral cell membrane {ECO:0000250}. Cell junction, tight junction {ECO:0000250}. Membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}. Cell membrane, sarcolemma {ECO:0000250|UniProtKB:Q9ES83}. Membrane, caveola {ECO:0000250|UniProtKB:Q9ES83}. Note=Its movement from the cytoplasm to m... | null | null | null | null | null | FUNCTION: Cell adhesion molecule involved in the establishment and/or maintenance of cell integrity. Involved in the formation and regulation of the tight junction (TJ) paracellular permeability barrier in epithelial cells. Plays a role in VAMP3-mediated vesicular transport and recycling of different receptor molecules... | Sus scrofa (Pig) |
B8QCG6 | NGFV_AGKCO | FLIGIWAAPKSEDNVPLGSPATSDLSDTSCAKTHEALKTSRNIDQHYPAPKKAEDQEFGSAANIIVDPKLFQKRRFQSPRVLFSTQPPPLSRDEQNVDNANSLNRNIRAKREDHPVHNRGEYSVCDSVNVWVANKTTATDIRGNVVTVMVDVNINNNVYKQYFFETKCRNPNPVPTGCRGIDARHWNSYC | null | null | memory [GO:0007613]; modulation of chemical synaptic transmission [GO:0050804]; negative regulation of neuron apoptotic process [GO:0043524]; nerve development [GO:0021675]; nerve growth factor signaling pathway [GO:0038180]; neuron projection morphogenesis [GO:0048812]; peripheral nervous system development [GO:000742... | axon [GO:0030424]; dendrite [GO:0030425]; extracellular space [GO:0005615]; synaptic vesicle [GO:0008021] | growth factor activity [GO:0008083]; lipid binding [GO:0008289]; nerve growth factor receptor binding [GO:0005163]; peptidase inhibitor activity [GO:0030414]; toxin activity [GO:0090729] | PF00243; | 2.10.90.10; | NGF-beta family | PTM: Glycosylated. {ECO:0000269|PubMed:21801740}. | SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:21801740}. | null | null | null | null | null | FUNCTION: Nerve growth factor is important for the development and maintenance of the sympathetic and sensory nervous systems. It stimulates division and differentiation of sympathetic and embryonic sensory neurons as well as basal forebrain cholinergic neurons in the brain. Its relevance in the snake venom is not clea... | Agkistrodon contortrix contortrix (Southern copperhead) |
B8QHP1 | CP52M_STABO | MLIKDIILTPMSLSAVAGLLPLLFVAFLVLHEPIWLLWYRYAARRHKCSMPRFIEKSFPLGIQRTMDMIKTAKSYTLLEVQYDRVFNKFKARTYLRQAPLQYQIFTIEPENIKTILATKFNDFGLGARFHTVGKVFGQGIFTLSGNGWKQSRSMLRPQFTKDQVCRIDQISSHAAELIKEMNRAMKVDQFIDVQHYFHKLTLDTATEFLFGESCESLNPENQSCIVARDGSEITAEQFVESYNFLLNYAFKRTLSSKVYWLFNSKEFRDHKKRAQSYIDYYVDKALYATSFAAENSIAEKDAAAESSGIYVFSLEMAKVT... | 1.14.14.80 | COFACTOR: Name=heme; Xref=ChEBI:CHEBI:30413; Evidence={ECO:0000250|UniProtKB:P04798}; | null | membrane [GO:0016020] | heme binding [GO:0020037]; iron ion binding [GO:0005506]; long-chain fatty acid omega-1 hydroxylase activity [GO:0120319]; long-chain fatty acid omega-hydroxylase activity [GO:0102033] | PF00067; | 1.10.630.10; | Cytochrome P450 family | null | SUBCELLULAR LOCATION: Membrane {ECO:0000255}; Single-pass membrane protein {ECO:0000255}. | CATALYTIC ACTIVITY: Reaction=an omega-methyl-long-chain fatty acid + O2 + reduced [NADPH--hemoprotein reductase] = an omega-hydroxy-long-chain fatty acid + H(+) + H2O + oxidized [NADPH--hemoprotein reductase]; Xref=Rhea:RHEA:56748, Rhea:RHEA-COMP:11964, Rhea:RHEA-COMP:11965, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:... | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=40 uM for oleic acid {ECO:0000269|PubMed:24242247}; KM=68 uM for linoleic acid {ECO:0000269|PubMed:24242247}; KM=54 uM for arachidonic acid {ECO:0000269|PubMed:24242247}; Vmax=535 pmol/min/mg enzyme for oleic acid {ECO:0000269|PubMed:24242247}; Vmax=451 pmol/min/mg... | null | BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 7. {ECO:0000269|PubMed:24242247}; | BIOPHYSICOCHEMICAL PROPERTIES: Temperature dependence: Optimum temperature is 25-30 degrees Celsius. {ECO:0000269|PubMed:24242247}; | FUNCTION: Catalyzes the first step of sophorolipid biosynthesis. Catalyzes the terminal (at the omega-position) or subterminal (at the omega(-1)-position) hydroxylation of a fatty acid. This converts the fatty acid to a substrate for the subsequent glycosyltransferase reactions (PubMed:23516968, PubMed:24242247). Oleic... | Starmerella bombicola (Yeast) (Candida bombicola) |
B8QSK0 | GNACT_ECOLX | MKIAYVVSSKKKCGPNIVILNIVKELANKHEMEIFFLDESDDDVFECVNVKSTQIKKASDLKEHLKRFDIIHSSGIRPDALVVLCKVIYRVKCKIITTIHNYVFQDLYYSYGLVKSLIWGLLWCSIWLFFDKLVILSKNADNYYWFLPSAKKNIIYNGIDDNDCLQNKKCNYRKEFNIPDDGILAGSCANLTKCKGIDLVIQTLTKEHKIYYIVAGDGIEKHNLINLVKARKLHERVYFIDFLDEPESFMSQLDVFLMPSRSEGFGLTVLESTKLGIPVITSNIPIFMELFDQMCLTFDIKNPSTLIDVITYAKKNRLHL... | 2.4.1.- | null | glycolipid biosynthetic process [GO:0009247]; Gram-negative-bacterium-type cell outer membrane assembly [GO:0043165]; lipopolysaccharide biosynthetic process [GO:0009103]; O antigen biosynthetic process [GO:0009243]; sulfolipid biosynthetic process [GO:0046506] | Gram-negative-bacterium-type cell wall [GO:0009276]; membrane [GO:0016020] | glycosyltransferase activity [GO:0016757]; UDP-sulfoquinovose:DAG sulfoquinovosyltransferase activity [GO:0046510] | PF13439;PF00534; | 3.40.50.2000; | Glycosyltransferase group 1 family, Glycosyltransferase 4 subfamily | null | SUBCELLULAR LOCATION: Membrane {ECO:0000255}; Single-pass membrane protein {ECO:0000255}. | null | null | PATHWAY: Bacterial outer membrane biogenesis; LPS O-antigen biosynthesis. {ECO:0000269|PubMed:21968437, ECO:0000269|PubMed:32421169}. | null | null | FUNCTION: Involved in the assembly of the O-repeating unit during O-antigen biosynthesis (PubMed:21968437, PubMed:32421169). N-acetylglucosamine transferase accountable for the alpha-D-GlcNAc-1,4-beta-D-Gal linkage within the O-antigen (PubMed:32421169). {ECO:0000269|PubMed:21968437, ECO:0000269|PubMed:32421169}. | Escherichia coli |
B8X8Z0 | TOXN_PECAT | MKFYTISSKYIEYLKEFDDKVPNSEDPTYQNPKAFIGIVLEIQGHKYLAPLTSPKKWHNNVKESSLSCFKLHENGVPENQLGLINLKFMIPIIEAEVSLLDLGNMPNTPYKRMLYKQLQFIRANSDKIASKSDTLRNLVLQGKMQGTCNFSLLEEKYRDFGKEAEDTEEGE | 3.1.-.- | null | defense response to virus [GO:0051607]; negative regulation of DNA-templated transcription [GO:0045892]; plasmid maintenance [GO:0006276] | null | identical protein binding [GO:0042802]; RNA binding [GO:0003723]; RNA endonuclease activity [GO:0004521] | PF13958; | 3.10.129.130; | ToxN/AbiQ toxin family | null | null | null | null | null | null | null | FUNCTION: Toxic component of a type III toxin-antitoxin (TA) system. An endoribonuclease which is active independently of the ribosome, cleaving between the second and third A of AAA(U/G) sequences, although not all occurrences of this tetranucleotide are cleaved (PubMed:23267117). Digests many mRNA species, including ... | Pectobacterium atrosepticum (Erwinia carotovora subsp. atroseptica) |
B8XCH5 | QKY_ARATH | MNTTPFHSDPPPSRIQRKLVVEVVEARNILPKDGQGSSSAYVVVDFDAQKKRTSTKFRDLNPIWNEMLDFAVSDPKNMDYDELDIEVYNDKRFGNGGGRKNHFLGRVKIYGSQFSRRGEEGLVYFPLEKKSVFSWIRGEIGLKIYYYDEAADEDTAGGGGGQQQQQQQQQFHPPQQEADEQQHQQQFHPPPQQMMNIPPEKPNVVVVEEGRVFESAQSQRYTETHQQPPVVIVEESPPQHVMQGPNDNHPHRNDNHPQRPPSPPPPPSAGEVHYYPPEVRKMQVGRPPGGDRIRVTKRPPNGDYSPRVINSKTGGGETTM... | null | COFACTOR: Name=Ca(2+); Xref=ChEBI:CHEBI:29108; Evidence={ECO:0000250|UniProtKB:Q6DN14}; Note=Binds Ca(2+) via the C2 domains in absence of phospholipids. {ECO:0000250|UniProtKB:Q6DN14}; | anisotropic cell growth [GO:0051211]; gynoecium development [GO:0048467]; plant organ development [GO:0099402]; plasmodesmata-mediated intercellular transport [GO:0010497]; positive regulation of flower development [GO:0009911]; tissue morphogenesis [GO:0048729] | cytosol [GO:0005829]; Golgi membrane [GO:0000139]; plasma membrane [GO:0005886]; plasmodesma [GO:0009506] | metal ion binding [GO:0046872] | PF00168;PF08372; | 2.60.40.150; | MCTP family | null | SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:24173806, ECO:0000269|PubMed:29259105}; Multi-pass membrane protein {ECO:0000255}. Cytoplasm {ECO:0000269|PubMed:29259105}. Golgi apparatus membrane {ECO:0000269|PubMed:29259105}; Multi-pass membrane protein {ECO:0000255}. Cell junction, plasmodesma {ECO:0000269|P... | null | null | null | null | null | FUNCTION: May be involved in Ca 2(+)-dependent signaling and membrane trafficking. Plays a role in fruit dehiscence (Probable). Components of the machinery involved in organ development mediated by the receptor-like kinase STRUBBELIG (SUB) (PubMed:19180193, PubMed:20298225). Collaboratively with SUB and POQ, regulates ... | Arabidopsis thaliana (Mouse-ear cress) |
B8XIA5 | MYC_MACMU | MDFFPVVENQQPPATMPLNVSFTNRNYDLDYDSVQPYFYCDEEENFYQQQQQSELQPPAPSEDIWKKFELLPTPPLSPSRRSGLCSPSYVAVTPFSPRGDNDGGGGSFSTADQLEMVTELLGGDMVNQSFICDPDDETFIKNIIIQDCMWSGFSAAAKLVSEKLASYQAARKDSGSPNPARGHSVCSTSSLYLQDLSAAASECIDPSVVFPYPLNDSSSPKSCASPDSSAFSPSSDSLLSSTESSPQASPEPLVLHEETPPTTSSDSEEEQEEEEEIDVVSVEKRQAPGKRSESGSPSAGGHSKPPHSPLVLKRCHVSTH... | null | null | chromatin remodeling [GO:0006338]; chromosome organization [GO:0051276]; DNA damage response [GO:0006974]; G1/S transition of mitotic cell cycle [GO:0000082]; intracellular iron ion homeostasis [GO:0006879]; MAPK cascade [GO:0000165]; negative regulation of apoptotic process [GO:0043066]; negative regulation of cell di... | cytoplasm [GO:0005737]; nucleolus [GO:0005730]; nucleoplasm [GO:0005654]; nucleus [GO:0005634] | DNA binding [GO:0003677]; DNA-binding transcription factor activity, RNA polymerase II-specific [GO:0000981]; E-box binding [GO:0070888]; protein dimerization activity [GO:0046983]; protein-containing complex binding [GO:0044877]; RNA polymerase II cis-regulatory region sequence-specific DNA binding [GO:0000978] | PF00010;PF02344;PF01056; | 4.10.280.10; | null | PTM: Phosphorylated by PRKDC (By similarity). Phosphorylation at Ser-344 by PIM2 leads to the stabilization of MYC (By similarity). Phosphorylation at Ser-77 by CDK2 prevents Ras-induced senescence. Phosphorylated at Ser-77 by DYRK2; this primes the protein for subsequent phosphorylation by GSK3B at Thr-73. Phosphoryla... | SUBCELLULAR LOCATION: Nucleus, nucleoplasm {ECO:0000250|UniProtKB:P01106}. Nucleus, nucleolus {ECO:0000250|UniProtKB:P01106}. Nucleus {ECO:0000250|UniProtKB:P01106}. Cytoplasm {ECO:0000250|UniProtKB:P01106}. | null | null | null | null | null | FUNCTION: Transcription factor that binds DNA in a non-specific manner, yet also specifically recognizes the core sequence 5'-CAC[GA]TG-3'. Activates the transcription of growth-related genes. Binds to the VEGFA promoter, promoting VEGFA production and subsequent sprouting angiogenesis. Regulator of somatic reprogrammi... | Macaca mulatta (Rhesus macaque) |
B8XTP8 | POLG_COSAA | MGANNSKESVSSNGNEGTIVNNFYSNQYYASIDASAQGVGTSTTPENGNVSGFLGLAGSAFNALSLLASPRTETGMMMEDRVLSRTAGNTSVNSQAAEGVLQAYGTETDSNSPTSCGDDPSKGTHATDRAFVIQLLPWKQTTNSYFAQWVRLTQKLSNNLHGNVMAKNIKSHAFAKMGFEVMLQANTSPFHNGILGLFLVPEFVRKGEITDEWIDLTPTSSLVSNTELYNPQTYANFPFDAKHSFDYSDITPEQFMIFPHQLINPKDTNVATVRVPYINIAPTNDTTVHTVWTAVVMVLVPLNFSSGASPTVSLTLTITP... | 2.7.7.48; 3.4.22.28; 3.6.4.13 | null | DNA-templated transcription [GO:0006351]; protein complex oligomerization [GO:0051259]; proteolysis [GO:0006508]; symbiont entry into host cell [GO:0046718]; viral RNA genome replication [GO:0039694]; virion attachment to host cell [GO:0019062] | host cell cytoplasmic vesicle membrane [GO:0044162]; host cell nucleolus [GO:0044196]; membrane [GO:0016020]; T=pseudo3 icosahedral viral capsid [GO:0039618] | ATP binding [GO:0005524]; ATP hydrolysis activity [GO:0016887]; cysteine-type endopeptidase activity [GO:0004197]; monoatomic ion channel activity [GO:0005216]; RNA binding [GO:0003723]; RNA helicase activity [GO:0003724]; RNA-dependent RNA polymerase activity [GO:0003968]; structural molecule activity [GO:0005198] | PF00548;PF00680;PF00073;PF00910; | 1.20.960.20;2.60.120.20;3.30.70.270;4.10.90.10;2.40.10.10; | Picornaviruses polyprotein family | PTM: [Genome polyprotein]: Specific enzymatic cleavages by the viral protease in vivo yield a variety of precursors and mature proteins (By similarity). The polyprotein seems to be cotranslationally cleaved at the 2A/2B junction by a ribosomal skip from one codon to the next without formation of a peptide bond (By simi... | SUBCELLULAR LOCATION: [Capsid protein VP2]: Virion {ECO:0000250|UniProtKB:P12296}. Host cytoplasm {ECO:0000305}.; SUBCELLULAR LOCATION: [Capsid protein VP3]: Virion {ECO:0000250|UniProtKB:P12296}. Host cytoplasm {ECO:0000305}.; SUBCELLULAR LOCATION: [Capsid protein VP1]: Virion {ECO:0000250|UniProtKB:P12296}. Host cyto... | CATALYTIC ACTIVITY: Reaction=a ribonucleoside 5'-triphosphate + RNA(n) = diphosphate + RNA(n+1); Xref=Rhea:RHEA:21248, Rhea:RHEA-COMP:14527, Rhea:RHEA-COMP:17342, ChEBI:CHEBI:33019, ChEBI:CHEBI:61557, ChEBI:CHEBI:140395; EC=2.7.7.48; Evidence={ECO:0000255|PROSITE-ProRule:PRU00539}; CATALYTIC ACTIVITY: Reaction=ATP + H2... | null | null | null | null | FUNCTION: [Capsid protein VP1]: Forms an icosahedral capsid of pseudo T=3 symmetry with capsid proteins VP2 and VP3. Together they form an icosahedral capsid composed of 60 copies of each VP1, VP2, and VP3, with a diameter of approximately 300 Angstroms.VP4 lies on the inner surface of the protein shell formed by VP1, ... | Cosavirus A (isolate Human/Pakistan/0553/-) (HCoSV-A) |
B8XX90 | STING_PIG | MPYSSLHPSIPQPRGLRAQVAALVLLGACLVALWGLGELPEYTLRWLVLHLASQQIGLLVKGLCSLAEELCHVHSRYQSSYWRAARACLGCPIRCGALLLLSCYFYFSIRDKAGLPLPWMLALLGLSQALNILLGLQHLAPAEVSAICEKRNFNVAHGLAWSYYIGYLRLILPGLRARIQAYNQRHKNVLGGIGNHRLHILFPLDCGVPDDLSVADPNIRFLHELPQQSADRAGIKGRVYTNSIYELLENGQPAGVCVLGYATPLQTLFAMSQDGRAGFSREDRLEQAKLFCRTLEDILADAPEAQNNCRLIVYQEPTEG... | 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]; mitochondrial outer membrane [GO:0005741]; peri... | 2',3'-cyclic GMP-AMP binding [GO:0061507]; cyclic-di-GMP binding [GO:0035438]; protein homodimerization activity [GO:0042803]; proton channel activity [GO:0015252]; signaling adaptor activity [GO:0035591] | PF15009; | 1.20.5.5200;3.40.50.12100; | STING family | PTM: Phosphorylation by TBK1 leads to activation and production of IFN-beta. Following cyclic nucleotide (c-di-GMP or cGAMP)-binding, activation and translocation from the endoplasmic reticulum, STING1 is phosphorylated by TBK1 at Ser-365 in the pLxIS motif. The phosphorylated pLxIS motif constitutes an IRF3-binding mo... | SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000269|PubMed:20346968, ECO:0000269|PubMed:35584187}; Multi-pass membrane protein {ECO:0000250|UniProtKB:Q86WV6, ECO:0000255}. Cytoplasm, perinuclear region {ECO:0000250|UniProtKB:Q86WV6}. Endoplasmic reticulum-Golgi intermediate compartment membrane {ECO:00002... | 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) (PubMed:35584187). Innate immune response is triggered in response to non-CpG double-stranded DNA from viruses and bacteria delivere... | Sus scrofa (Pig) |
B8XY56 | RNT2_DANRE | MRFIAFAVIFSAVYLCSSAFTHPRGEWTKLILTQHWPQTFCKMEHCKTDFSYWTLHGLWPNTGVRCNTSWHFNASLIEDILPEMEKFWPDLLEPSSPKFWNYEWTKHGTCAAKSESLNSEHKYFGKALELYHKFDLNSVLLKNQIVPSEKHYTLEDVEEAITSAYGVKPKIQCVHPGQGGQVQILGQIEICVDRDFQLMGCEKSSEDTWSNDLPTVPVSGQSGLSVCDHSMPVYYPPVQA | 4.6.1.19 | null | RNA catabolic process [GO:0006401]; rRNA catabolic process [GO:0016075] | endoplasmic reticulum lumen [GO:0005788]; extracellular region [GO:0005576]; lysosomal lumen [GO:0043202] | ribonuclease T2 activity [GO:0033897]; RNA binding [GO:0003723]; RNA endonuclease activity [GO:0004521] | PF00445; | 3.90.730.10; | RNase T2 family | null | SUBCELLULAR LOCATION: Lysosome lumen {ECO:0000250}. Endoplasmic reticulum lumen {ECO:0000250}. Secreted {ECO:0000250}. | CATALYTIC ACTIVITY: Reaction=a ribonucleotidyl-ribonucleotide-RNA + H2O = a 3'-end 3'-phospho-ribonucleotide-RNA + a 5'-end dephospho-ribonucleoside-RNA + H(+); Xref=Rhea:RHEA:68052, Rhea:RHEA-COMP:10463, Rhea:RHEA-COMP:13936, Rhea:RHEA-COMP:17355, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:83062, ChEBI:CHEBI:13... | null | null | null | null | FUNCTION: Has ribonuclease activity, with higher activity at acidic pH. Probably is involved in lysosomal degradation of ribosomal RNA. {ECO:0000269|PubMed:21199949}. | Danio rerio (Zebrafish) (Brachydanio rerio) |
B8YG19 | XS20E_NEOPA | MRLGVALSTIAVLLTATSARNLDKRQWGWPNFGGGNGGNGGNGGKTINDYKREQGAGRDIHVYAPSNLAPNSPLLLSLHGMDQDPNYQQSNTHWETLADSEGFVVVYPRGGTGMSTWDIQGTKDTQWVSQIIDQMKKEYNIDTKRVYLSGFSMGGMFTYHAMSQIANKIAAFAPCSGPNVFGASKAQRPVPIFHVHGTNDDVLNYQQVEGFLKNYRDQFHCPSQADTKTNYPNRENPNATLYTWGPCDKGVYIKHLKLQGRGHSPSSADIQDIWDFVSQWTVDGPVSASGNGGGNTTPTNPSTGGNGNGNGGGNTTPTNP... | 3.1.1.72; 3.2.1.8 | null | xylan catabolic process [GO:0045493] | extracellular region [GO:0005576] | acetylxylan esterase activity [GO:0046555]; endo-1,4-beta-xylanase activity [GO:0031176] | PF02230;PF02013;PF00457; | 2.60.120.180;3.40.50.1820;3.90.1220.10; | AxeA family; Glycosyl hydrolase 11 (cellulase G) family | null | SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:19690850}. | CATALYTIC ACTIVITY: Reaction=Deacetylation of xylans and xylo-oligosaccharides.; EC=3.1.1.72; Evidence={ECO:0000269|PubMed:19690850}; CATALYTIC ACTIVITY: Reaction=Endohydrolysis of (1->4)-beta-D-xylosidic linkages in xylans.; EC=3.2.1.8; Evidence={ECO:0000269|PubMed:19690850}; | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=1.48 mg/ml for birchwood xylan for endo-1,4-beta-xylanase activity; KM=16.72 mg/ml for birchwood xylan for acetylxylan esterase activity; Vmax=5.15 umol/min/mg enzyme toward birchwood xylan for acetylxylan esterase activity; Vmax=153.27 umol/min/mg enzyme toward bi... | PATHWAY: Glycan degradation; xylan degradation. | BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 5.8 for acetylxylan esterase activity, and 5.8 for endo-1,4-beta-xylanase activity.; | BIOPHYSICOCHEMICAL PROPERTIES: Temperature dependence: Optimum temperature is 58 degrees Celsius for acetylxylan esterase activity, and 49 degrees Celsius for endo-1,4-beta-xylanase activity.; | FUNCTION: Bifunctional acetylxylan esterase/xylanase involved in the hydrolysis of xylan, a major structural heterogeneous polysaccharide found in plant biomass representing the second most abundant polysaccharide in the biosphere, after cellulose. Degrades xylan from acetylxylan, beechwood, birchwood, and oat spelt, a... | Neocallimastix patriciarum (Rumen fungus) |
B8ZXI1 | QTRT2_MOUSE | MKLSLIKVVNGCRLGKIQNLGKAGDCTVDIPGCLLYTRTGSAPHLTHQTLRNIHGVPGIAQLTLSSLAEHHEVLAEYKKGVGSFIGMPESLFYCSLHDPVTPGPAGYVTSKSVSVWGFGGRVEMTVSKFMAIQEALQPDWFQCLSDGEASCAETTSIKRARKSVDRSLLFLDSCLRLQEESEVLQKSVIIGVIEGGDVMEERLRSARETAKRPVGGFLLDGFQGDPAVTETRLHLLSSVTAELPEDKPRLICGVSRPDEVLECIERGVDLFESFFPYQVTERGCALTFTFDCQLNPEETLLQQNGIQEKIKGLDQAKKIE... | null | COFACTOR: Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000255|HAMAP-Rule:MF_03043, ECO:0000269|PubMed:29862811, ECO:0000269|PubMed:35815944}; Note=Binds 1 zinc ion per subunit. {ECO:0000255|HAMAP-Rule:MF_03043, ECO:0000269|PubMed:29862811, ECO:0000269|PubMed:35815944}; | tRNA-guanine transglycosylation [GO:0101030] | cytoplasm [GO:0005737]; mitochondrial outer membrane [GO:0005741]; mitochondrion [GO:0005739]; protein-containing complex [GO:0032991] | protein heterodimerization activity [GO:0046982]; protein homodimerization activity [GO:0042803]; tRNA binding [GO:0000049]; tRNA-guanosine(34) queuine transglycosylase activity [GO:0008479]; zinc ion binding [GO:0008270] | PF01702; | 3.20.20.105; | Queuine tRNA-ribosyltransferase family, QTRT2 subfamily | null | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_03043, ECO:0000269|PubMed:19414587}. Mitochondrion outer membrane {ECO:0000255|HAMAP-Rule:MF_03043, ECO:0000269|PubMed:19414587}; Peripheral membrane protein {ECO:0000255|HAMAP-Rule:MF_03043, ECO:0000269|PubMed:19414587}; Cytoplasmic side {ECO:0000255|HAMAP-Rul... | null | null | null | null | null | FUNCTION: Non-catalytic subunit of the queuine tRNA-ribosyltransferase (TGT) that catalyzes the base-exchange of a guanine (G) residue with queuine (Q) at position 34 (anticodon wobble position) in tRNAs with GU(N) anticodons (tRNA-Asp, -Asn, -His and -Tyr), resulting in the hypermodified nucleoside queuosine (7-(((4,5... | Mus musculus (Mouse) |
B9DFA8 | INVC_ARATH | MNSRSCICVSAMKPCCRFLISFRSSSLFGFSPPNSGKFINSSKLHCTKIDSRSIRSGIHCRRIVLDRNAFCDSDSISWGGGGSRVLRARGSSRGRGRGVLVIPHVASDFRNYSTSSLDSHVNDKSFESMFVKPLVFKEVEKTEGIPKRERGNVGGGKDANFGNVGVRKETERCLSQTEVEKEAWKLLRGAVVNYCGFPVGTVAANDPGDTQTLNYDQVFIRDFVPSAYAFMLDGEGEIVRNFLLHTLQLQSWEKTVDCHSPGPGLMPASFKVKSAPLEGNDGSFEEFLDPDFGGSAIGRVSPVDSGLWWIILLRAYGKLT... | 3.2.1.26 | null | circadian rhythm [GO:0007623]; regulation of seed germination [GO:0010029]; regulation of timing of transition from vegetative to reproductive phase [GO:0048510]; sucrose catabolic process [GO:0005987] | mitochondrion [GO:0005739] | glycopeptide alpha-N-acetylgalactosaminidase activity [GO:0033926]; sucrose alpha-glucosidase activity [GO:0004575] | PF12899; | 1.50.10.10; | Glycosyl hydrolase 100 family | null | SUBCELLULAR LOCATION: Mitochondrion {ECO:0000269|PubMed:23135328}. | CATALYTIC ACTIVITY: Reaction=Hydrolysis of terminal non-reducing beta-D-fructofuranoside residues in beta-D-fructofuranosides.; EC=3.2.1.26; Evidence={ECO:0000269|PubMed:23135328}; | null | null | BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 6.0. {ECO:0000269|PubMed:23135328}; | null | FUNCTION: Mitochondrial invertase that cleaves sucrose into glucose and fructose and is involved in the regulation of aerial tissue development and floral transition. May be modulating hormone balance in relation to the radicle emergence. {ECO:0000269|PubMed:23135328}. | Arabidopsis thaliana (Mouse-ear cress) |
B9DFG3 | ISE2_ARATH | MNTLPVVSLTASSSFKFFHFPSLHRSLSHSPNFSFTKSLILNPNHLSFKSTLNSLSPSQSQLYEEEDDEEEEEEDEDDDDEAADEYDNISDEIRNSDDDDDDEETEFSVDLPTESARERVEFRWQRVEKLRSLVRDFGVEMIDIDELISIYDFRIDKFQRLAIEAFLRGSSVVVSAPTSSGKTLIAEAAAVSTVAKGRRLFYTTPLKALSNQKFREFRETFGDDNVGLLTGDSAINKDAQIVIMTTEILRNMLYQSVGMASSGTGLFHVDAIVLDEVHYLSDISRGTVWEEIVIYCPKEVQLICLSATVANPDELAGWIG... | 3.6.4.13 | null | chloroplast rRNA processing [GO:1901259]; cytidine to uridine editing [GO:0016554]; embryo development ending in seed dormancy [GO:0009793]; Group II intron splicing [GO:0000373]; mRNA processing [GO:0006397]; nuclear-transcribed mRNA catabolic process, 3'-5' exonucleolytic nonsense-mediated decay [GO:0070478]; plasmod... | chloroplast [GO:0009507]; chloroplast stroma [GO:0009570]; cytoplasmic stress granule [GO:0010494]; Ski complex [GO:0055087] | ATP binding [GO:0005524]; ATP hydrolysis activity [GO:0016887]; mRNA binding [GO:0003729]; RNA binding [GO:0003723]; RNA helicase activity [GO:0003724] | PF00270;PF08148;PF00271; | 1.10.3380.30;3.40.50.300; | DExH box helicase family | null | SUBCELLULAR LOCATION: Plastid, chloroplast {ECO:0000269|PubMed:18431481, ECO:0000269|PubMed:22106293, ECO:0000269|PubMed:26147377}. Cytoplasmic granule {ECO:0000269|PubMed:17601829}. Note=Localizes to granule-like structures, probably stress granules (SGs), which number increases upon stress. {ECO:0000269|PubMed:176018... | CATALYTIC ACTIVITY: Reaction=ATP + H2O = ADP + H(+) + phosphate; Xref=Rhea:RHEA:13065, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:456216; EC=3.6.4.13; | null | null | null | null | FUNCTION: RNA helicase involved in group II intron splicing (PubMed:26147377). Essential protein required during embryogenesis. Involved in post-transcriptional gene silencing. Modulates the determination of cell fate. Necessary for normal plasmodesmata (PD) development and aperture regulation. {ECO:0000269|PubMed:1177... | Arabidopsis thaliana (Mouse-ear cress) |
B9DFG5 | PTI13_ARATH | MYPMDSDYHRRGLVANDRSPAQFVRLDKPRAVDDLYIGKREKMRRWLCCACHVEEPYHSSENEHLRSPKHHNDFGHHTRKPQAAVKPDALKEPPSIDVPALSLDELKEKTDNFGSKSLIGEGSYGRAYYATLKDGKAVAVKKLDNAAEPESNVEFLTQVSRVSKLKHDNFVELFGYCVEGNFRILAYEFATMGSLHDILHGRKGVQGAQPGPTLDWIQRVRIAVDAARGLEYLHEKVQPAVIHRDIRSSNVLLFEDFKAKIADFNLSNQSPDMAARLHSTRVLGTFGYHAPEYAMTGQLTQKSDVYSFGVVLLELLTGRK... | 2.7.10.2 | null | phosphorylation [GO:0016310]; stomatal complex patterning [GO:0010375] | cytosol [GO:0005829]; plasma membrane [GO:0005886] | ATP binding [GO:0005524]; non-membrane spanning protein tyrosine kinase activity [GO:0004715]; protein kinase binding [GO:0019901] | PF07714; | 1.10.510.10; | Protein kinase superfamily, Tyr protein kinase family | PTM: Phosphorylated by OXI1. {ECO:0000269|PubMed:17040918}. | SUBCELLULAR LOCATION: Cell membrane {ECO:0000305|PubMed:17644812}; Peripheral membrane protein {ECO:0000305|PubMed:17644812}. | 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 | null | Arabidopsis thaliana (Mouse-ear cress) |
B9DFK5 | RETIC_ARATH | MAGCAMNLQFSSVVKVRNEISSFGICNRDFVFRDLAKAMKVPVLRIRGGSGRQRSRLFVVNMSQSPIEPQSGGFAATEQIKGEGDNSILGKDNVRNLGTDQLENLDIDGNVGDGFNGSDGNGGGGGGGNGGEGDGEGEDYEEKEFGPILKFEEVMKETEARGATLPSDMLEAAKNYGIRKVLLLRYLDLQSSAGLLGFAIRSWAMLRNRMLADPSFLFKIGAEIVIDSCCATVAEVQKRGKDFWAEFELYVADLLVGTVVNIALVGMLAPYVRFGQPSASPGFLGRMVFAYNALPSSVFEAERPGCRFSAQQRLATYFYK... | null | null | chloroplast organization [GO:0009658]; leaf development [GO:0048366]; photoperiodism [GO:0009648]; response to reactive oxygen species [GO:0000302] | chloroplast [GO:0009507]; chloroplast envelope [GO:0009941]; chloroplast inner membrane [GO:0009706]; endoplasmic reticulum [GO:0005783]; plastid [GO:0009536] | null | PF11891; | null | RETICULATA family | null | SUBCELLULAR LOCATION: Plastid, chloroplast membrane {ECO:0000250|UniProtKB:Q9C9Z2}; Multi-pass membrane protein {ECO:0000255}. | null | null | null | null | null | FUNCTION: May play a role in leaf development. Required for leaf mesophyll cell division in the early stages of leaf organogenesis (PubMed:12848826, PubMed:16873448). Acts in a developmental pathway that involves PPT1/CUE1 but does not include ASE2/DOV1 (PubMed:16873448). {ECO:0000269|PubMed:12848826, ECO:0000269|PubMe... | Arabidopsis thaliana (Mouse-ear cress) |
B9DFS6 | SNX2B_ARATH | MMGSENDEESHLHSSKEEMEKLFLREDGDPLTKSNVNGDKSNSNYRSAMSTLFDSRHPSIVVTPADSDPLFAPPSYYSESRSPRSKPNGGDRVSSYLEPPSYADVIFSPFDDISEINGSEDGHSQSSDSLSRSPSSLSSDYIKITVSNPQKEQEATNSMIPGGSTYITYQITTRTNLSDYGGSEFSVRRRFRDIVTLADRLAESYRGFCIPPRPDKSIVESQVMQKQEFVEQRRVALEKYLRRLVAHPVIRNSDELKVFLQAQGKLPLATSTDVASRMLDGAVKLPKQLFGEGGGASSVEVVQPGRGGRDFLRMFKELRQ... | null | null | developmental process [GO:0032502]; late endosome to vacuole transport [GO:0045324]; protein maturation [GO:0051604]; protein transport [GO:0015031]; seedling development [GO:0090351]; vesicle-mediated transport [GO:0016192] | cytosol [GO:0005829]; Golgi apparatus [GO:0005794]; membrane [GO:0016020]; multivesicular body membrane [GO:0032585]; retromer complex [GO:0030904] | phosphatidylinositol binding [GO:0035091]; phospholipid binding [GO:0005543]; protein heterodimerization activity [GO:0046982] | PF00787;PF09325; | 1.20.1270.60;3.30.1520.10; | Sorting nexin family | null | SUBCELLULAR LOCATION: Cytoplasm. Endosome membrane; Peripheral membrane protein; Cytoplasmic side. Prevacuolar compartment membrane; Peripheral membrane protein; Cytoplasmic side. Golgi apparatus, trans-Golgi network membrane; Peripheral membrane protein; Cytoplasmic side. | null | null | null | null | null | FUNCTION: Plays a role in vesicular protein sorting. Acts at the crossroads between the secretory and endocytic pathways. Is involved in the endosome to vacuole protein transport and, as component of the membrane-associated retromer complex, is also involved in endosome-to-Golgi retrograde transport. {ECO:0000269|PubMe... | Arabidopsis thaliana (Mouse-ear cress) |
B9DFU2 | MAX1_ARATH | MKTQHQWWEVLDPFLTQHEALIAFLTFAAVVIVIYLYRPSWSVCNVPGPTAMPLVGHLPLMAKYGPDVFSVLAKQYGPIFRFQMGRQPLIIIAEAELCREVGIKKFKDLPNRSIPSPISASPLHKKGLFFTRDKRWSKMRNTILSLYQPSHLTSLIPTMHSFITSATHNLDSKPRDIVFSNLFLKLTTDIIGQAAFGVDFGLSGKKPIKDVEVTDFINQHVYSTTQLKMDLSGSLSIILGLLIPILQEPFRQVLKRIPGTMDWRVEKTNARLSGQLNEIVSKRAKEAETDSKDFLSLILKARESDPFAKNIFTSDYISAV... | 1.14.-.- | COFACTOR: Name=heme; Xref=ChEBI:CHEBI:30413; Evidence={ECO:0000250|UniProtKB:P04798}; | auxin polar transport [GO:0009926]; carotenoid biosynthetic process [GO:0016117]; positive regulation of flavonoid biosynthetic process [GO:0009963]; regulation of meristem structural organization [GO:0009934]; secondary shoot formation [GO:0010223] | membrane [GO:0016020] | heme binding [GO:0020037]; iron ion binding [GO:0005506]; monooxygenase activity [GO:0004497]; oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen [GO:0016705]; thromboxane-A synthase activity [GO:0004796] | PF00067; | 1.10.630.10; | Cytochrome P450 family | null | SUBCELLULAR LOCATION: Membrane {ECO:0000255}; Single-pass membrane protein {ECO:0000255}. | CATALYTIC ACTIVITY: Reaction=(11R)-carlactone + O2 + reduced [NADPH--hemoprotein reductase] = (11R)-19-hydroxycarlactone + H(+) + H2O + oxidized [NADPH--hemoprotein reductase]; Xref=Rhea:RHEA:76083, Rhea:RHEA-COMP:11964, Rhea:RHEA-COMP:11965, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, ChEBI:CHEBI:57618, C... | null | null | null | null | FUNCTION: Involved in the biosynthesis of strigolactone natural products, bioactive compounds promoting plant fitness and soil microbe interactions, but preventing shoot branching (PubMed:25425668, PubMed:32399509). Converts carlactone to carlactonoic acid by catalyzing consecutive oxidations at C-19 to convert the C-1... | Arabidopsis thaliana (Mouse-ear cress) |
B9DFX7 | HMA8_ARATH | MASNLLRFPLPPPSSLHIRPSKFLVNRCFPRLRRSRIRRHCSRPFFLVSNSVEISTQSFESTESSIESVKSITSDTPILLDVSGMMCGGCVARVKSVLMSDDRVASAVVNMLTETAAVKFKPEVEVTADTAESLAKRLTESGFEAKRRVSGMGVAENVKKWKEMVSKKEDLLVKSRNRVAFAWTLVALCCGSHTSHILHSLGIHIAHGGIWDLLHNSYVKGGLAVGALLGPGRELLFDGIKAFGKRSPNMNSLVGLGSMAAFSISLISLVNPELEWDASFFDEPVMLLGFVLLGRSLEERAKLQASTDMNELLSLISTQS... | 7.2.2.9 | null | copper ion homeostasis [GO:0055070]; copper ion transport [GO:0006825]; photosynthetic electron transport chain [GO:0009767] | chloroplast thylakoid membrane [GO:0009535] | ATP binding [GO:0005524]; ATP hydrolysis activity [GO:0016887]; copper ion binding [GO:0005507]; copper ion transmembrane transporter activity [GO:0005375]; P-type divalent copper transporter activity [GO:0043682] | PF00122;PF00403;PF00702; | 3.30.70.100;3.40.1110.10;2.70.150.10;3.40.50.1000; | Cation transport ATPase (P-type) (TC 3.A.3) family, Type IB subfamily | null | SUBCELLULAR LOCATION: Plastid, chloroplast thylakoid membrane {ECO:0000269|PubMed:15772282}; Multi-pass membrane protein {ECO:0000269|PubMed:15772282}. | CATALYTIC ACTIVITY: Reaction=ATP + Cu(2+)(in) + H2O = ADP + Cu(2+)(out) + H(+) + phosphate; Xref=Rhea:RHEA:10376, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:29036, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:456216; EC=7.2.2.9; | null | null | null | null | FUNCTION: Mediates copper transfer across the chloroplast thylakoid membrane. Required for copper delivery into the thylakoids lumen, which is essential for the function of copper proteins. {ECO:0000269|PubMed:15772282}. | Arabidopsis thaliana (Mouse-ear cress) |
B9DFZ0 | NTH2_ARATH | MILTGAASTFPIVARVLNAMNRRMYAATTLSSAKSISAESLNLRSDSNSEAAHGASESETRVSLRKKRIKQDDLEPVKKCSARETKARKDMCGLPDIEDSPYKKTNGTASSRTRKLNSYIKSTEASPSASSIKTAGLGIPPENWEKVLEGIRKMKPSEEAPVNAVECDRTGSFLPPKERRFYVLIGTLLSSQTKEHITGAAVERLHQNGLLTPEAIDKADESTIKELIYPVGFYTRKATNVKKVAKICLMEYDGDIPRTLEELLSLPGVGPKIAHLVLHVAWNDVQGICVDTHVHRICNRLGWVSKPGTKQKTSSPEETR... | 3.2.2.-; 4.2.99.18 | COFACTOR: Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883; Evidence={ECO:0000255|HAMAP-Rule:MF_03183}; Note=Binds 1 [4Fe-4S] cluster. The cluster does not appear to play a role in catalysis, but is probably involved in the proper positioning of the enzyme along the DNA strand. {ECO:0000255|HAMAP-Rule:MF_03183}; | base-excision repair [GO:0006284]; base-excision repair, AP site formation [GO:0006285] | chloroplast nucleoid [GO:0042644]; nucleus [GO:0005634] | 4 iron, 4 sulfur cluster binding [GO:0051539]; class I DNA-(apurinic or apyrimidinic site) endonuclease activity [GO:0140078]; DNA binding [GO:0003677]; DNA N-glycosylase activity [GO:0019104]; DNA-(apurinic or apyrimidinic site) endonuclease activity [GO:0003906]; metal ion binding [GO:0046872]; oxidized pyrimidine nu... | PF00633;PF00730; | 1.10.1670.10; | Nth/MutY family | null | SUBCELLULAR LOCATION: Plastid, chloroplast stroma, chloroplast nucleoid {ECO:0000269|PubMed:19372224}. | 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: Bifunctional DNA N-glycosylase with associated apurinic/apyrimidinic (AP) lyase function that catalyzes the first step in base excision repair (BER), the primary repair pathway for the repair of oxidative DNA damage. The DNA N-glycosylase activity releases the damaged DNA base from DNA by cleaving the N-glyco... | Arabidopsis thaliana (Mouse-ear cress) |
B9DGD6 | ACS_ARATH | MKIGSPSSPILSVVSSSGSLDPKISGSLGSRILPATQRSSPSENLLLHRKMSSNSLRHVESMSQLPSGAGKISQLNAVVLGESLASEENDLVFPSKEFSGQALVSSPQQYMEMHKRSMDDPAAFWSDIASEFYWKQKWGDQVFSENLDVRKGPISIEWFKGGITNICYNCLDKNVEAGLGDKTAIHWEGNELGVDASLTYSELLQRVCQLANYLKDNGVKKGDAVVIYLPMLMELPIAMLACARIGAVHSVVFAGFSADSLAQRIVDCKPNVILTCNAVKRGPKTINLKAIVDAALDQSSKDGVSVGICLTYDNSLATTR... | 6.2.1.1 | null | acetate metabolic process [GO:0006083]; acetyl-CoA biosynthetic process from acetate [GO:0019427]; fatty acid metabolic process [GO:0006631] | chloroplast [GO:0009507]; chloroplast stroma [GO:0009570]; cytosol [GO:0005829]; glyoxysome [GO:0009514]; mitochondrion [GO:0005739]; plastid [GO:0009536] | acetate-CoA ligase activity [GO:0003987]; AMP binding [GO:0016208]; ATP binding [GO:0005524] | PF16177;PF00501;PF13193; | 3.30.300.30;3.40.50.12780; | ATP-dependent AMP-binding enzyme family | null | SUBCELLULAR LOCATION: Plastid, chloroplast. Glyoxysome. | CATALYTIC ACTIVITY: Reaction=acetate + ATP + CoA = acetyl-CoA + AMP + diphosphate; Xref=Rhea:RHEA:23176, ChEBI:CHEBI:30089, ChEBI:CHEBI:30616, ChEBI:CHEBI:33019, ChEBI:CHEBI:57287, ChEBI:CHEBI:57288, ChEBI:CHEBI:456215; EC=6.2.1.1; Evidence={ECO:0000269|PubMed:10859180}; | null | null | null | null | FUNCTION: Catalyzes the production of acetyl-CoA, an activated form of acetate that can be used for lipid synthesis or for energy generation. May play a limited role in the biosynthesis of lipids. {ECO:0000269|PubMed:10859180, ECO:0000269|PubMed:12051672}. | Arabidopsis thaliana (Mouse-ear cress) |
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