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
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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 bacterium [GO:0050830]; disruption of plasma membrane integrity in another organism [GO:0051673]; innate immune response in mucosa [GO:0002227]; killing of cells of another organism [GO:0031640] | 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 | MTVPQERIEIRNIDPGTNPTRFARGWHCIGLAKDFRDGKPHQVKVFGTDLVVFADTAGKLHVLDAFCRHMGGNLARGEIKGDTIACPFHDWRWNGQGRCEAVPYARRTPKLGRTKAWTTMERNGVLFVWHCPQGSEPTPELAIPEIEGYEDGQWSDWTWTTIHVEGSHCREIVDNVVDMAHFFYVHFQMPEYFKNVFDGHIAGQHMRSYGRDDIKTGVQMDLPEAQTISDAFYYGPSFMLDTIYTVSEGTTIESKLINCHYPVTNNSFVLQFGTIVKKIEGMSEEQAAEMATMFTDGLEEQFAQDIEIWKHKSRIENPLLTEEDGPVYQLRRWYNQFYVDLEDVTPDMTQRFEFEVDTSRALESWHKEVEENLAGTAE | 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|PubMed:19561185}; Note=Binds 1 Fe cation. {ECO:0000269|PubMed:19561185}; | 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, ChEBI:CHEBI:33737, ChEBI:CHEBI:33738, ChEBI:CHEBI:40799, ChEBI:CHEBI:63641; EC=1.14.15.30; Evidence={ECO:0000269|PubMed:19561185, ECO:0000305|PubMed:21642460}; | 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-(5alpha)-androstene-3,17-dione, 5alpha-androstane-3,17-dione and 5beta-androstane-3,17-dione (PubMed:19561185, PubMed:21642460). KSH has the highest activity with 3-keto-delta4 steroid substrates (PubMed:19561185). {ECO:0000269|PubMed:19561185, ECO:0000269|PubMed:21642460}. | Rhodococcus rhodochrous |
B6V6V6 | KSHB_RHORH | MTTVEVPHGSRSVILTVSAVVEETADTRSIVFAVPDELRDKFAYRPGQFLTLRIPSDRTGSVARCYSLASSPFTDDAPKVTVKRTSDGYGSNWLCDNIATGQTLEVLPPAGVFTPKSLDHDFLLFGAGSGITPVISILKSALTQGGGKVVLVYANRDEKSVIFAEELRALAEKYPTRLTVVHWLESVQGLPTADQLAAIAAPYESYEAFMCGPGPFMDTVHQALNTVGMPRARVHAEVFNSLSGDPFADQAPVEVSDEDAADAATVEVELDGEVHKLSWPRKQTLVDIMLAKGIDVPYSCQEGECGSCACTVLEGKVEMENCDVLDPEDIEAGYILGCQARPVTDHLKIEF | 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, ChEBI:CHEBI:33737, ChEBI:CHEBI:33738, ChEBI:CHEBI:40799, ChEBI:CHEBI:63641; EC=1.14.15.30; Evidence={ECO:0000269|PubMed:19561185}; | 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 (progesterone), 19-nor-4-androstene-3,17-dione (nordion), 1-(5alpha)-androstene-3,17-dione, 5alpha-androstane-3,17-dione and 5beta-androstane-3,17-dione. KSH has the highest activity with 3-keto-Delta4 steroid substrates. {ECO:0000269|PubMed:19561185}. | Rhodococcus rhodochrous |
B6V8E6 | CTNB1_CANLF | MATQADLMELDMAMEPDRKAAVSHWQQQSYLDSGIHSGATTTAPSLSGKGNPEEEDVDTTQVLYEWEQGFSQSFTQEQVADIDGQYAMTRAQRVRAAMFPETLDEGMQIPSTQFDAAHPTNVQRLAEPSQMLKHAVVNLINYQDDAELATRAIPELTKLLNDEDQVVVNKAAVMVHQLSKKEASRHAIMRSPQMVSAIVRTMQNTNDVETARCTAGTLHNLSHHREGLLAIFKSGGIPALVKMLGSPVDSVLFYAITTLHNLLLHQEGAKMAVRLAGGLQKMVALLNKTNVKFLAITTDCLQILAYGNQESKLIILASGGPQALVNIMRTYTYEKLLWTTSRVLKVLSVCSSNKPAIVEAGGMQALGLHLTDPSQRLVQNCLWTLRNLSDAATKQEGMEGLLGTLVQLLGSDDINVVTCAAGILSNLTCNNYKNKMMVCQVGGIEALVRTVLRAGDREDITEPAICALRHLTSRHQEAEMAQNAVRLHYGLPVVVKLLHPPSHWPLIKATVGLIRNLALCPANHAPLREQGAIPRLVQLLVRAHQDTQRRTSMGGTQQQFVEGVRMEEIVEGCTGALHILARDVHNRIVIRGLNTIPLFVQLLYSPIENIQRVAAGVLCELAQDKEAAEAIEAEGATAPLTELLHSRNEGVATYAAAVLFRMSEDKPQDYKKRLSVELTSSLFRTEPMAWNETADLGLDIGAQGEPLGYRQDDPSYRSFHSGGYGQDALGMDPMMEHEMGGHHPGADYPVDGLPDLGHAQDLMDGLPPGDSNQLAWFDTDL | 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 tube morphogenesis [GO:0061154]; negative regulation of cell population proliferation [GO:0008285]; negative regulation of DNA-templated transcription [GO:0045892]; negative regulation of mitotic cell cycle, embryonic [GO:0045976]; neuron projection extension [GO:1990138]; positive regulation of apoptotic process [GO:0043065]; positive regulation of DNA-templated transcription [GO:0045893]; positive regulation of heparan sulfate proteoglycan biosynthetic process [GO:0010909]; positive regulation of neuroblast proliferation [GO:0002052]; positive regulation of transcription by RNA polymerase II [GO:0045944]; protein localization to cell surface [GO:0034394]; regulation of calcium ion import [GO:0090279]; regulation of centriole-centriole cohesion [GO:0030997]; regulation of centromeric sister chromatid cohesion [GO:0070602]; regulation of protein localization to cell surface [GO:2000008]; regulation of smooth muscle cell proliferation [GO:0048660]; response to estradiol [GO:0032355]; sympathetic ganglion development [GO:0061549] | 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]; cytoplasm [GO:0005737]; cytosol [GO:0005829]; exocytic vesicle [GO:0070382]; nucleus [GO:0005634]; perinuclear region of cytoplasm [GO:0048471]; plasma membrane [GO:0005886]; protein-DNA complex [GO:0032993]; spindle pole [GO:0000922]; synapse [GO:0045202]; transcription regulator complex [GO:0005667] | 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. Phosphorylation at Ser-552 by AMPK promotes stabilization of the protein, enhancing TCF/LEF-mediated transcription. Phosphorylation on Ser-191 and Ser-246 by CDK5. Phosphorylation by CDK2 regulates insulin internalization. Phosphorylation by PTK6 at Tyr-64, Tyr-142, Tyr-331 and/or Tyr-333 with the predominant site at Tyr-64 is not essential for inhibition of transcriptional activity. Phosphorylation by SRC at Tyr-333 promotes interaction with isoform M2 of PKM (PKM2); promoting transcription activation. {ECO:0000250|UniProtKB:P35222, ECO:0000250|UniProtKB:Q02248}.; PTM: Ubiquitinated by the SCF(BTRC) E3 ligase complex when phosphorylated by GSK3B, leading to its degradation. Ubiquitinated by a E3 ubiquitin ligase complex containing UBE2D1, SIAH1, CACYBP/SIP, SKP1, APC and TBL1X, leading to its subsequent proteasomal degradation (By similarity). Ubiquitinated and degraded following interaction with SOX9 (By similarity). {ECO:0000250|UniProtKB:P35222, ECO:0000250|UniProtKB:Q02248}.; PTM: S-nitrosylation at Cys-619 within adherens junctions promotes VEGF-induced, NO-dependent endothelial cell permeability by disrupting interaction with E-cadherin, thus mediating disassembly adherens junctions. {ECO:0000250}.; PTM: O-glycosylation at Ser-23 decreases nuclear localization and transcriptional activity, and increases localization to the plasma membrane and interaction with E-cadherin CDH1. {ECO:0000250|UniProtKB:Q96S06}.; PTM: Deacetylated at Lys-49 by SIRT1. {ECO:0000250|UniProtKB:P35222}. | 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}. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome {ECO:0000250|UniProtKB:P35222}. Cytoplasm, cytoskeleton, spindle pole {ECO:0000250|UniProtKB:P35222}. Synapse {ECO:0000250|UniProtKB:Q02248}. Cytoplasm, cytoskeleton, cilium basal body {ECO:0000250|UniProtKB:Q02248}. Note=Colocalized with RAPGEF2 and TJP1 at cell-cell contacts (PubMed:10873669). Cytoplasmic when it is un-stable (highly phosphorylated) or bound to CDH1 (By similarity). Translocates to the nucleus when it is stabilized (low level of phosphorylation) (By similarity). Interaction with GLIS2 and MUC1 promotes nuclear translocation (By similarity). Interaction with EMD inhibits nuclear localization (By similarity). The majority of beta-catenin is localized to the cell membrane (By similarity). In interphase, colocalizes with CROCC between CEP250 puncta at the proximal end of centrioles, and this localization is dependent on CROCC and CEP250 (By similarity). In mitosis, when NEK2 activity increases, it localizes to centrosomes at spindle poles independent of CROCC (By similarity). Colocalizes with CDK5 in the cell-cell contacts and plasma membrane of undifferentiated and differentiated neuroblastoma cells (By similarity). Interaction with FAM53B promotes translocation to the nucleus (By similarity). {ECO:0000250|UniProtKB:P35222, ECO:0000269|PubMed:10873669}. | 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 proteasome. In the presence of Wnt ligand, CTNNB1 is not ubiquitinated and accumulates in the nucleus, where it acts as a coactivator for transcription factors of the TCF/LEF family, leading to activate Wnt responsive genes (By similarity). Involved in the regulation of cell adhesion, as component of an E-cadherin:catenin adhesion complex (By similarity). Acts as a negative regulator of centrosome cohesion. Involved in the CDK2/PTPN6/CTNNB1/CEACAM1 pathway of insulin internalization. Blocks anoikis of malignant kidney and intestinal epithelial cells and promotes their anchorage-independent growth by down-regulating DAPK2. Disrupts PML function and PML-NB formation by inhibiting RANBP2-mediated sumoylation of PML (By similarity). Promotes neurogenesis by maintaining sympathetic neuroblasts within the cell cycle. Involved in chondrocyte differentiation via interaction with SOX9: SOX9-binding competes with the binding sites of TCF/LEF within CTNNB1, thereby inhibiting the Wnt signaling (By similarity). Acts as a positive regulator of odontoblast differentiation during mesenchymal tooth germ formation, via promoting the transcription of differentiation factors such as LEF1, BMP2 and BMP4 (By similarity). Activity is repressed in a MSX1-mediated manner at the bell stage of mesenchymal tooth germ formation which prevents premature differentiation of odontoblasts (By similarity). {ECO:0000250|UniProtKB:P35222, ECO:0000250|UniProtKB:Q02248}. | Canis lupus familiaris (Dog) (Canis familiaris) |
B6VQ60 | BRCA1_CAEEL | MADVALRITETVARLQKELKCGICCSTYKDPILSTCFHIFCRSCINACFERKRKVQCPICRSVLDKRSCRDTYQITMAVQNYLKLSEAFKKDIENMNTFKSLPPEKMFMESQMPLDITIIPENDGKRCAPDFAIPFLPVRRKRPSRPQPPSAFAEEPAEPVEPPEPATKQPVELQSRVFPLEKLKKDVETSTETYKISREELKNVDIEEYINTLRENSTEIDEIDALFQLMPTMRQFLRNNINQLMEKFHVAPPKKSEKPANRRVSFASSQDLENIKIMTASESLETPPEPIQKLAQKPEVFKSTQNLIDLNLNTAVKKPVVVASDDDEVVEDSEGELQIDEDDLANVTCATSSTTLDADRTPKAIQDDEDRIDDELSQVPKTIVCSRIHNDADEVVGLELLSDFYHKFLSNACRFAEDVNEHTTHLVMMNSEGRSISQKSTAYLYAIARKCVIVGRQWLVDCITTGLLLSEADYTITSCSSTIPVKIPPSIGSEMGWLRSRNDEHGKLFAGRRFMILRKFTMNPYFDYKQLIELVQQCGGEILSCYENLSPEKLYIIFSKHSKAIEESKNIENLYKCDVVTMEWVLDSISEYLILPTQPYKAVDSIGCLQD | 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:0051307]; mitotic sister chromatid segregation [GO:0000070]; negative regulation of fatty acid biosynthetic process [GO:0045717]; nucleotide-excision repair [GO:0006289]; positive regulation of double-strand break repair via homologous recombination [GO:1905168]; positive regulation of transcription by RNA polymerase II [GO:0045944]; protein ubiquitination [GO:0016567] | 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 brd-1 in germline nuclei at meiotic prophase I (PubMed:30383754). At the transition between mid- and late- pachytene, localization together with brd-1 is less diffuse and becomes a linear pattern along the chromosomes (PubMed:30383754). In late pachytene nuclei, co-localizes with brd-1 and syp-1 at crossover sites and the short arm of the bivalent (PubMed:30383754). Co-localizes with the pro-crossover factors cosa-1, zhp-3 and msh-5 at crossover sites in mid-late pachytene nuclei (PubMed:30383754). Co-localizes with plk-2 in pachytene nuclei (PubMed:30383754). Localizes to DNA damage sites on chromatin following DNA damage. {ECO:0000269|PubMed:16628214, ECO:0000269|PubMed:30383754}. | 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:14711411, PubMed:16628214, PubMed:24424777, PubMed:26903030, PubMed:30383754). Functions in double-strand break repair, and is required for homologous recombination between sister chromatids in meiotic and mitotic cells (PubMed:18219312, PubMed:19646877, PubMed:24424777, PubMed:26903030). In particular, protects against chromosome non-disjunction and nuclear fragmentation during meiotic double-strand break repair to ensure sister chromatid recombination and aid chromosome stability (PubMed:14711411, PubMed:18219312, PubMed:24424777). Required for normal cell cycle progression (PubMed:20207739). Along with brap-2 modulates the expression of cell cycle arrest protein cki-1 in response to increased levels of reactive oxygen species (PubMed:20207739). Constituent of the CeBCD complex that possesses E3 ubiquitin-protein ligase activity (PubMed:14711411). When bound to chromatin, the brc-1-brd-1 heterodimer within the CeBCD complex is inactive during normal conditions, but in response to DNA damage, the brc-1-brd-1 heterodimer associates with other proteins such as the recombinase rad-51 or the E2-ubiquitin-conjugating enzyme let-70, which activate the CeBCD complex as an E3-ubiquitin ligase (PubMed:16628214). Moreover, association between the brc-1-brd-1 heterodimer and rad-51 and let-70, probably requires DNA checkpoint proteins such as atl-1 and mre-11 in order to induce ubiquitination at DNA damage sites (PubMed:16628214). To this end, the brc-1-brd-1 heterodimer coordinates a diverse range of cellular pathways such as DNA damage repair, ubiquitination and transcriptional regulation to maintain genomic stability (PubMed:14711411). {ECO:0000269|PubMed:14711411, ECO:0000269|PubMed:16628214, ECO:0000269|PubMed:18219312, ECO:0000269|PubMed:19646877, ECO:0000269|PubMed:20207739, ECO:0000269|PubMed:24424777, ECO:0000269|PubMed:26903030, ECO:0000269|PubMed:30383754}. | Caenorhabditis elegans |
B6VQA1 | DIMM_DROME | MDATQLTELMGSHDFMQLQHQLHHNNNNYNTDGHNGLSSESAEGSSRPVRRATRRTSQLSNNTYDLEMTDSSSQSDDTSGGGGSSNGGGSTTNTGHPSGCSLGGQGPSGRGRVQQASSGACPSTIAPNSTSSNSSNANGNASRRRKGALNAKERNMRRLESNERERMRMHSLNDAFQSLREVIPHVEMERRLSKIETLTLAKNYIINLTHIILSKRNEEAAALELNSGAVGGVLLSNLSSESGGPVASGIPANSNAATICFEDTLASGGAFDCAILAATDGSLLNAATVTTSPAMQSIQSQAIHLQTPMEQQQQQASHLPHHQQAMHGHGHLGASIQSQQQPSLVLNGTTSVGLGIGIGVGVGVGVGVCNNAPSFADINDNFDEPFREFL | 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-templated transcription [GO:0006355]; sensory organ development [GO:0007423]; ventral cord development [GO:0007419] | 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 cell differentiation. Controls transcription of FMRFamide in Tv neuronal cells and Fur1 in Ap-let cells (Tvb and dorsal apterous cells). Also required for up-regulation of Phm in Tv and Ap-let cells, and expression of three neuropeptide genes, Ms, FMRFamide and Lk. Influences both regulated and constitutive secretory activity in neuroendocrine cells at embryonic and postembryonic level. Loss of function studies show reduced cellular levels of various neuropeptides and neuropeptide biosynthetic enzymes. {ECO:0000269|PubMed:12642483, ECO:0000269|PubMed:15081360, ECO:0000269|PubMed:15748845, ECO:0000269|PubMed:16651547, ECO:0000269|PubMed:16870731, ECO:0000269|PubMed:17967878, ECO:0000269|PubMed:20045330}. | Drosophila melanogaster (Fruit fly) |
B6YWB8 | CAS10_THEON | MEIDELTALGGLLHDIGKPVQRAGLYSGDHSTQGARFLRDLAENTGRAEYELLSLFSEFHHKGHMKNDELMIRRIKELSPERFGLTMEDVLNALWIVYEADNLASGEREEGQPQASRPLYSVFNPGKAYPWAELDFEKELPVPGDVFSIRSQDYRELVKRLWEELSKAKLRSDRLLPVLEKYLTFVSSVTSEGNIISLYDHMRMTSAIALAMLRAGCTAEDVRSGRCRKEKRFLLIEGDFSGIQDFIYRVSGKGTLKYLRARSAYLELIGWDVVLEILSRLGLTRANVVFNAGGHFMIIAQNTPDAVKELEEIRAKAVEWLYREFESDLYLAIEWEPVSGREFGREGGKNLFAEARKRLKHKLTVRKLKRFGEIKGLFEHGHTERLAECPVCGRELPEGKLEPSASDPETKVCPTCNRLVSLGGNLPKLLGFGRTAKNDAGVLVEGPFSGFVPYLQGGRPVGEQILVKNTLNPGEIPESAQFVPYFVADYFKKDPKGGVATFEELSMASTGTRRLGVMKGDVDRLGEFFSSMDSPSKLATASRFMDYFFKGYIGAIIEGKFGYIIGDVPSLRDWPEEPDIVVVYAGGDDFFIVGAWDQIFELAFRVRRAFNAYTGGKLTLSVGLGYFDERTPIYRMADVVSERLDTAKDEGRNRVFVVGRSRPLDGKHKLSYEWNHYEELWRTYAPRIYAGNGRLKGKLESKKGLLWKLLEIRELYVRDPNDVRWAYLTAYLLGRHGLSDLFPELVGIDTKAVERKEPQPVYWVDGVLKIVLMAVRR | 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 invading nucleic acids. CRISPR clusters are transcribed and processed into CRISPR RNA (crRNA). The type III-A Csm effector complex binds crRNA and acts as a crRNA-guided RNase, DNase and cyclic oligoadenylate synthase; binding of target RNA cognate to the crRNA is required for all activities. {ECO:0000250|UniProtKB:A0A0A7HFE1}.; FUNCTION: A single-strand deoxyribonuclease (ssDNase) which digests linear and circular ssDNA; has 5'-3' and 3'-5' exonuclease activity as well as a less efficient endonuclease activity. Has a minimal size requirement; 100 nucleotide ssDNA (nt) is more efficiently digested than 50 or 25 nt ssDNA, while 14 nt ssDNA is not cleaved at all. It has no activity on dsDNA or ssRNA. {ECO:0000269|PubMed:25773141}.; FUNCTION: ssDNase activity is stimulated in the ternary Csm effector complex; binding of cognate target RNA activates the ssDNase, as the target RNA is degraded ssDNA activity decreases. {ECO:0000250|UniProtKB:A0A0A7HFE1}.; FUNCTION: When associated with the ternary Csm effector complex (the crRNA, Cas proteins and a cognate target ssRNA) synthesizes cyclic oligoadenylates (cOA) from ATP. cOAs are second messengers that stimulate the ssRNase activity of Csm6, inducing an antiviral state important for defense against invading nucleic acids. {ECO:0000250|UniProtKB:A0A0A7HFE1}. | 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. {ECO:0000269|PubMed:18710235, ECO:0000269|PubMed:19025863, ECO:0000269|PubMed:20394359, ECO:0000269|PubMed:21375229}. | Streptomyces lasalocidi (Streptomyces lasaliensis) |
B6ZK77 | IRL1B_DANRE | MRSRVPLQILLYAAVIRSLKVVSKRGSVDGCTDWSVDYLRYRVLLGEPVRIKCALFYGYIRANYTHAQSAGLSLMWYRSATHTDHEEPITLDGTRTLKEEDALWFRPAQLQDSGHYSCVLRNSSYCMKVSMALTVAENSSGLCYNSKMRRLEKAELSKSKDILCPDIQDYTPAGSEPHVTWYKECRPKQWRSSIIRTADLLSIRDVREDDIGNYTCEIQFGRFLVRRTTELTVTAPLTDKPPKILQPPEHKLSVMELQLGGPVNLTCRAFFGYSGDVSPLIYWMKGEKFIEDLDETRIRESEIKMVREHLGEQEVSVSLTIDSLQEEDLGNYSCYVENGHGRRHAIIQLSRRELMYTVELAGGLGAILLMLIFLVSLYKCYRIELMLFYRNHFGSEDVDGENKDYDAYVSYTKVDPDQWSQETREEEHFALEILPDMLEKHYGYKLFIPDRDLIPTGTYIEDVARCVDQSKRLIIVMTPNYVVRRGWSIFELETRLRNMLVSGEIKVILIECSDLRGIMNYQEVEALKHTIKLLTVIRWPGPGSSKPNSRFWKQLQYEMPFRRPEPKLSHEQVLDASEQGPFGELQTVSALSMVSATSTAMATAHPDLRSGFHNTYNTQLRQKHYYRGYEYDIPSSGTLPPLATMGSQHTYCNIPMSLLNGQRPPGQPAHGQQQSLEEQQVNNALLPLLPRETSISSVIW | 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; Evidence={ECO:0000255|PROSITE-ProRule:PRU00204}; | 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 | MNGHSDEESVRNSSGESRSDDDSGSASGSGSGSSSGSSSDGSSSQSGSSDSESGSESGSQSESESDTSREKKQVQAKPPKADGSEFWKSSPSILAVQRSAVLKKQQQQQKAASSDSGSEEDSSSSEDSADDSSSETKKKKHKDEDWQMSGSGSVSGTGSDSESEEDGDKSSCEESESDYEPKNKVKSRKPPSRIKPKSGKKSTGQKKRQLDSSEEEEDDDEDYDKRGSRRQATVNVSYKEAEETKTDSDDLLEVCGEDVPQTEEDEFETIEKFMDSRIGRKGATGASTTIYAVEVDGDPNAGFEKSKELGEIQYLIKWKGWSHIHNTWETEETLKQQNVKGMKKLDNYKKKDQETKRWLKNASPEDVEYYNCQQELTDDLHKQYQIVERIIAHSNQKSAAGYPDYYCKWQGLPYSECSWEDGALIAKKFQARIDEYFSRNQSKTTPFKDCKVLKQRPRFVALKKQPSYIGGHESLELRDYQLNGLNWLAHSWCKGNSCILADEMGLGKTIQTISFLNYLFHEHQLYGPFLLVVPLSTLTSWQREIQTWAPQMNAVVYLGDITSRNMIRTHEWMHPQTKRLKFNILLTTYEILLKDKSFLGGLNWAFIGVDEAHRLKNDDSLLYKTLIDFKSNHRLLITGTPLQNSLKELWSLLHFIMPEKFSSWEDFEEEHGKGREYGYASLHKELEPFLLRRVKKDVEKSLPAKVEQILRMEMSALQKQYYKWILTRNYKALSKGSKGSTSGFLNIMMELKKCCNHCYLIKPPDDNEFYNKQEALQHLIRSSGKLILLDKLLIRLRERGNRVLIFSQMVRMLDILAEYLKYRQFPFQRLDGSIKGELRKQALDHFNAEGSEDFCFLLSTRAGGLGINLASADTVVIFDSDWNPQNDLQAQARAHRIGQKKQVNIYRLVTKGSVEEDILERAKKKMVLDHLVIQRMDTTGKTVLHTGSTPSSSTPFNKEELSAILKFGAEELFKEPEGEEQEPQEMDIDEILKRAETRENEPGPLTVGDELLSQFKVANFSNMDEDDIELEPERNSRNWEEIIPESQRRRIEEEERQKELEEIYMLPRMRNCAKQISFNGSEGRRSRSRRYSGSDSDSITERKRPKKRGRPRTIPRENIKGFSDAEIRRFIKSYKKFGGPLERLDAVARDAELVDKSETDLRRLGELVHNGCIKALKDNSSGQERAGGRLGKVKGPTFRISGVQVNAKLVISHEEELAPLHKSIPSDPEERKRYVIPCHTKAAHFDIDWGKEDDSNLLVGIYEYGYGSWEMIKMDPDLSLTQKILPDDPDKKPQAKQLQTRADYLIKLLNKDLARKEAQRLAGAGNSKRRKTRNKKNKMKASKIKEEIKSDSSPQPSEKSDEDDDEEDNKVNEIKSENKEKSKKIPLLDTPVHITATSEPVPISEESEELDQKTFSVCKERMRPVKAALKQLDRPEKGLSEREQLEHTRQCLIKIGDHITECLKEYTNPEQIKQWRKNLWIFVSKFTEFDARKLHKLYKHAIKKRQESQQHNDQNISSNVNTHVIRNPDVERLKETTNHDDSSRDSYSSDRHLSQYHDHHKDRHQGDAYKKSDSRKRPYSAFSNGKDHRDWDHYKQDSRYYSDSKHRKLDDHRSRDHRSNLEGNLKDSRGHSDHRSHSDHRIHSDHRSTSEYSHHKSSRDYRYHSDWQMDHRASGSGPRSPLDQRSPYGSRSPLGHRSPFEHSSDHKSTPEHTWSSRKT | 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 transcription termination step. Regulates negatively DNA replication. Not only involved in transcription-related chromatin remodeling, but also required to maintain a specific chromatin configuration across the genome. Required for maintaining open chromatin and pluripotency in embryonic stem cells (By similarity). Required for centromeric localization of CENPA (PubMed:19625449). {ECO:0000250|UniProtKB:P40201, ECO:0000269|PubMed:19625449}. | Gallus gallus (Chicken) |
B7FAS6 | SAM10_CAEEL | MPPQVIQQQQQSLASEMTARDRLTSYIYEYLQQTGASKTAETFKEEVLSTNPAAGLAAANSTKLSDKSFLLEWWLLFWDLYSAAPERRDAGGDPFSAEAKYFHEAMIGMPPGMNGHFAPPPMGMEMMGGHPGAFGGRFAPGRMPPGAMAPGGMPPGAFPMFPPDPRLQRMAPNQGMRMPPPPVGQPFPGAVGMPRPVGPGAPMDMSGMQRFDFMGGPPPGGGAQPFPGASGSGGMMPNGAHPHMSLNSPSMGVPPADMPPFMGMPPMPPTSSSAMPFGMSSDHQPMSAGPAAAAPGATTAGGPGTPGMIGSVPGPGSVPQVATTSVGSVGTPSSIGQQLHQPKQEITTNGEEIMKTEALTPTGGGGGGSVPPPPPAATAAVSMNGGGPGSAPGSAHSVNNNVNPGTPGSNPLSNPMSNPPLSSGPPPPGSNDAFGKDDNGEISKIREGLLDGFCA | 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 montezumae spp.)), it provokes a reversible paralysis to insects (crickets (Achaeta spp.)), but is not toxic to mice. At high concentrations, it does displace the (beta) mammal-specific toxin Cn2 from rat brain synaptosomes. {ECO:0000269|PubMed:19631296}. | Centruroides suffusus (Durango bark scorpion) |
B7FXW1 | SQLE_PHATC | MLVDRVENNEKQQQQMASSSDAMSDSSLSDDEIIEHVVHGKEPKSTYELSWVSNAIAWSGALVWPLMLTVPLLLSSMYSPISYRQVFPESWYVYDTLSNCAPKPLGLVLGILAVAVGQVFVWIFFYLFKFGYLGTDPRSIQSKGAREYIFREGLLTHIGQPEGFVLLIGYLAITWMLKLMPQSYYSFEGTIQYKELFMCLVLQDGIQYTMHVLEHIVSPAFYQMSHKPHHRFTNPRLFDAFNGSLMDTFCMIIIPLFVTANLVRHCNVWTYMAFGSSYACWLTLIHSEYVFPWDGIFRKLGLGTPADHHVHHKFFKFNYGHLFMWFDQLGGTYRDPSGFAPRVFRENV | 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, ChEBI:CHEBI:29034; Evidence={ECO:0000269|PubMed:30478288}; | 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 | MSSLSTLRILHSTAGRRWASYYGIYPKSAACSSSSVAIARFFSTAADRPPKHAMLSVENKVVAPPMVYIAGEEMTRYACDLVVKSWLEPYFDLSQWEYFDLSCVNRDNTNDQVLRDAVTAGQRIGAIFKEPTITPSAIQKKAFGLKNSLGSPNGAMRAGWNGITISRDTIHIDGIELGYKRPVFFERHAVGGEYGAGWSKVGRGTLLTTYLPSDGRDPFVVDKRDLTDQHNVVVTYHNPYDNVEPLAHLFFQRCLDANITPYVVTKKTVFKWQEGFWAVMKDVFDEHYKSRFEEKGLLQACGGDLQHLISDAATMQLIRWTDGGFGMAAHNYDGDMLTDQIAQVHRSPGFITSNLVGKAPDGSLIKEFEASHGTVSDLWNDHLAGKETSLNPLGLVEAIVGALQHAAVLDAEKNPDDEHKVKARDQIFNFTTTLRTAMHNTFRYGQGTRDMSGPSGYTTEDFVRKVAWRLQRYLDAQYDEAPPPQLGEPSRKLRRNYDIDEEAINGLFQKYDKNGDGFIDFEEFTRMLVKMNLAPLLTKKEKEKKPDV | 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; Evidence={ECO:0000269|PubMed:32824636}; | 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+) as cofactor (at pH 8.0 and 25 degrees Celsius) {ECO:0000269|PubMed:32824636}; Vmax=48.34 umol/min/mg enzyme with Mg(2+) as cofactor (at pH 8.0 and 25 degrees Celsius) {ECO:0000269|PubMed:32824636}; Note=kcat is 180.5 sec(-1) for NAD(+) with Mn(2+) as cofactor. kcat is 79.0 sec(-1) for NAD(+) with Mg(2+) as cofactor. {ECO:0000269|PubMed:32824636}; | 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 35 degrees Celsius. {ECO:0000269|PubMed:32824636}; | 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|UniProtKB:A0A096P8D3, ECO:0000269|PubMed:32824636}. | Phaeodactylum tricornutum (strain CCAP 1055/1) |
B7G6D3 | MCA3C_PHATC | MGFLRRQLREQFEKKKPEALQADIRMISGCQDVQTSADVSNVSSFQLPDPAGNAGGACTSTLLNVLYKDHQTPEDTMSFVELLNKMRENLEAKGFSQVPQLTASHPIDVNDDFDLVPPAATGTRRALLIGINYVGHEQGVLRGCHNDVKNMVEYIKAVHGFEDENITILMDDGEHTAPTHANMIAAYKKIVALSKADDALFCHFSGHGAKIRDDDRGEEDDGYDETLVPIDYHENGMIRDDDLYDILIKPLVQGVHLVCLMDCCHSGTVLDLPYVYKADGNFTEMEIDENFDFKKLLGKFGIDDFDKFGGEALGKINGDALGKVGKDALGKLNKFFG | 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:0000269|PubMed:34566902}. | 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 | MSILFSSILFSIATFFSRILGLFRDVLFAKYFGVSYELDAYFIAIMFPFFLRKVFGEGAMSSAFVPLYSEKSGEEKDKFLSSVINGFSLIILALVILSYFFPELIINLFGAGSSHETKILAKKLLLITSPSIYFIFLWAISYSILNTNNKFFWPALTPSISNITIIIGTFLSTKYGIISPTIGFLIGSILMFFSIIKSIIKHKYYFTIKHFPHFLKLFFPTFMTMVVSQINTVVDMNVVSFYDKGSISYLQYASRFYLLPYGLFAVSVSTVVLSKISNDRKNFNYHLNDALKTTLFFTIPSMVGLIFLSTPIIRFFYEHGAFTSKDTLITSKILIAYTLGLPFYGIYSTISRSYHAIKNTKTPFIAATIVSLSNIILDIIFGLKYGPIGVALATSIAGIIGVLYLLFSVKTFPIKDFLKISLNSLIMLFVIYLTDFTDNEFWFLIQILIGILVYLIFSSIFYRDLIRRFLYARKK | 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 | MAHVVILGAGTGGMPAAYEMKEALGSGHEVTLISANDYFQFVPSNPWVGVGWKERDDIAFPIRHYVERKGIHFIAQSAEQIDAEAQNITLADGNTVHYDYLMIATGPKLAFENVPGSDPHEGPVQSICTVDHAERAFAEYQALLREPGPIVIGAMAGASCFGPAYEYAMIVASDLKKRGMRDKIPSFTFITSEPYIGHLGIQGVGDSKGILTKGLKEEGIEAYTNCKVTKVEDNKMYVTQVDEKGETIKEMVLPVKFGMMIPAFKGVPAVAGVEGLCNPGGFVLVDEHQRSKKYANIFAAGIAIAIPPVETTPVPTGAPKTGYMIESMVSAAVHNIKADLEGRKGEQTMGTWNAVCFADMGDRGAAFIALPQLKPRKVDVFAYGRWVHLAKVAFEKYFIRKMKMGVSEPFYEKVLFKMMGITRLKEEDTHRKAS | 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, ECO:0000269|PubMed:22542586}. | 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:0000255|HAMAP-Rule:MF_01046}; CATALYTIC ACTIVITY: Reaction=H2O + N(6)-(1-hydroxy-2-oxopropyl)-L-lysyl-[protein] = H(+) + L-lysyl-[protein] + lactate; Xref=Rhea:RHEA:49552, Rhea:RHEA-COMP:9752, Rhea:RHEA-COMP:12429, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:24996, ChEBI:CHEBI:29969, ChEBI:CHEBI:131709; EC=3.5.1.124; Evidence={ECO:0000255|HAMAP-Rule:MF_01046}; CATALYTIC ACTIVITY: Reaction=H2O + S-(1-hydroxy-2-oxopropyl)-L-cysteinyl-[protein] = H(+) + L-cysteinyl-[protein] + lactate; Xref=Rhea:RHEA:49556, Rhea:RHEA-COMP:10131, Rhea:RHEA-COMP:12430, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:24996, ChEBI:CHEBI:29950, ChEBI:CHEBI:131710; EC=3.5.1.124; Evidence={ECO:0000255|HAMAP-Rule:MF_01046}; CATALYTIC ACTIVITY: Reaction=H2O + N(omega)-(1-hydroxy-2-oxoethyl)-L-arginyl-[protein] = glycolate + H(+) + L-arginyl-[protein]; Xref=Rhea:RHEA:57188, Rhea:RHEA-COMP:10532, Rhea:RHEA-COMP:14844, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:29805, ChEBI:CHEBI:29965, ChEBI:CHEBI:141553; EC=3.5.1.124; Evidence={ECO:0000255|HAMAP-Rule:MF_01046}; CATALYTIC ACTIVITY: Reaction=H2O + N(6)-(1-hydroxy-2-oxoethyl)-L-lysyl-[protein] = glycolate + H(+) + L-lysyl-[protein]; Xref=Rhea:RHEA:57192, Rhea:RHEA-COMP:9752, Rhea:RHEA-COMP:14845, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:29805, ChEBI:CHEBI:29969, ChEBI:CHEBI:141554; EC=3.5.1.124; Evidence={ECO:0000255|HAMAP-Rule:MF_01046}; CATALYTIC ACTIVITY: Reaction=H2O + S-(1-hydroxy-2-oxoethyl)-L-cysteinyl-[protein] = glycolate + H(+) + L-cysteinyl-[protein]; Xref=Rhea:RHEA:57196, Rhea:RHEA-COMP:10131, Rhea:RHEA-COMP:14846, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:29805, ChEBI:CHEBI:29950, ChEBI:CHEBI:141555; EC=3.5.1.124; Evidence={ECO:0000255|HAMAP-Rule:MF_01046}; CATALYTIC ACTIVITY: Reaction=H2O + N(2)-(1-hydroxy-2-oxopropyl)-dGTP = dGTP + H(+) + lactate; Xref=Rhea:RHEA:57244, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:24996, ChEBI:CHEBI:61429, ChEBI:CHEBI:141569; Evidence={ECO:0000255|HAMAP-Rule:MF_01046}; CATALYTIC ACTIVITY: Reaction=H2O + N(2)-(1-hydroxy-2-oxopropyl)-GTP = GTP + H(+) + lactate; Xref=Rhea:RHEA:57256, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:24996, ChEBI:CHEBI:37565, ChEBI:CHEBI:141570; Evidence={ECO:0000255|HAMAP-Rule:MF_01046}; CATALYTIC ACTIVITY: Reaction=H2O + N(2)-(1-hydroxy-2-oxopropyl)-GDP = GDP + H(+) + lactate; Xref=Rhea:RHEA:57260, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:24996, ChEBI:CHEBI:58189, ChEBI:CHEBI:141573; Evidence={ECO:0000255|HAMAP-Rule:MF_01046}; CATALYTIC ACTIVITY: Reaction=H2O + N(2)-(1-hydroxy-2-oxopropyl)-GMP = GMP + H(+) + lactate; Xref=Rhea:RHEA:57268, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:24996, ChEBI:CHEBI:58115, ChEBI:CHEBI:141575; Evidence={ECO:0000255|HAMAP-Rule:MF_01046}; CATALYTIC ACTIVITY: Reaction=H2O + N(2)-(1-hydroxy-2-oxoethyl)-dGTP = dGTP + glycolate + H(+); Xref=Rhea:RHEA:57248, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:29805, ChEBI:CHEBI:61429, ChEBI:CHEBI:141572; Evidence={ECO:0000255|HAMAP-Rule:MF_01046}; CATALYTIC ACTIVITY: Reaction=H2O + N(2)-(1-hydroxy-2-oxoethyl)-GTP = glycolate + GTP + H(+); Xref=Rhea:RHEA:57252, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:29805, ChEBI:CHEBI:37565, ChEBI:CHEBI:141571; Evidence={ECO:0000255|HAMAP-Rule:MF_01046}; CATALYTIC ACTIVITY: Reaction=H2O + N(2)-(1-hydroxy-2-oxoethyl)-GDP = GDP + glycolate + H(+); Xref=Rhea:RHEA:57264, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:29805, ChEBI:CHEBI:58189, ChEBI:CHEBI:141574; Evidence={ECO:0000255|HAMAP-Rule:MF_01046}; CATALYTIC ACTIVITY: Reaction=H2O + N(2)-(1-hydroxy-2-oxoethyl)-GMP = glycolate + GMP + H(+); Xref=Rhea:RHEA:57304, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:29805, ChEBI:CHEBI:58115, ChEBI:CHEBI:141576; Evidence={ECO:0000255|HAMAP-Rule:MF_01046}; CATALYTIC ACTIVITY: Reaction=an N(2)-(1-hydroxy-2-oxopropyl)-guanosine in RNA + H2O = a guanosine in RNA + H(+) + lactate; Xref=Rhea:RHEA:57288, Rhea:RHEA-COMP:14855, Rhea:RHEA-COMP:14858, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:24996, ChEBI:CHEBI:74269, ChEBI:CHEBI:141580; Evidence={ECO:0000255|HAMAP-Rule:MF_01046}; CATALYTIC ACTIVITY: Reaction=an N(2)-(1-hydroxy-2-oxopropyl)-2'-deoxyguanosine in DNA + H2O = a 2'-deoxyguanosine in DNA + H(+) + lactate; Xref=Rhea:RHEA:57300, Rhea:RHEA-COMP:11367, Rhea:RHEA-COMP:14856, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:24996, ChEBI:CHEBI:85445, ChEBI:CHEBI:141578; Evidence={ECO:0000255|HAMAP-Rule:MF_01046}; CATALYTIC ACTIVITY: Reaction=an N(2)-(1-hydroxy-2-oxoethyl)-guanosine in RNA + H2O = a guanosine in RNA + glycolate + H(+); Xref=Rhea:RHEA:57292, Rhea:RHEA-COMP:14855, Rhea:RHEA-COMP:14859, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:29805, ChEBI:CHEBI:74269, ChEBI:CHEBI:141581; Evidence={ECO:0000255|HAMAP-Rule:MF_01046}; CATALYTIC ACTIVITY: Reaction=an N(2)-(1-hydroxy-2-oxoethyl)-2'-deoxyguanosine in DNA + H2O = a 2'-deoxyguanosine in DNA + glycolate + H(+); Xref=Rhea:RHEA:57296, Rhea:RHEA-COMP:11367, Rhea:RHEA-COMP:14857, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:29805, ChEBI:CHEBI:85445, ChEBI:CHEBI:141579; Evidence={ECO:0000255|HAMAP-Rule:MF_01046}; | 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 proteins and lactate or glycolate, respectively. Deglycates cysteine, arginine and lysine residues in proteins, and thus reactivates these proteins by reversing glycation by glyoxals. Acts on early glycation intermediates (hemithioacetals and aminocarbinols), preventing the formation of Schiff bases and advanced glycation endproducts (AGE). Also functions as a nucleotide deglycase able to repair glycated guanine in the free nucleotide pool (GTP, GDP, GMP, dGTP) and in DNA and RNA. Is thus involved in a major nucleotide repair system named guanine glycation repair (GG repair), dedicated to reversing methylglyoxal and glyoxal damage via nucleotide sanitization and direct nucleic acid repair. Plays an important role in protecting cells from carbonyl stress. {ECO:0000255|HAMAP-Rule:MF_01046}. | 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:0000255|HAMAP-Rule:MF_01046}; CATALYTIC ACTIVITY: Reaction=H2O + N(6)-(1-hydroxy-2-oxopropyl)-L-lysyl-[protein] = H(+) + L-lysyl-[protein] + lactate; Xref=Rhea:RHEA:49552, Rhea:RHEA-COMP:9752, Rhea:RHEA-COMP:12429, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:24996, ChEBI:CHEBI:29969, ChEBI:CHEBI:131709; EC=3.5.1.124; Evidence={ECO:0000255|HAMAP-Rule:MF_01046}; CATALYTIC ACTIVITY: Reaction=H2O + S-(1-hydroxy-2-oxopropyl)-L-cysteinyl-[protein] = H(+) + L-cysteinyl-[protein] + lactate; Xref=Rhea:RHEA:49556, Rhea:RHEA-COMP:10131, Rhea:RHEA-COMP:12430, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:24996, ChEBI:CHEBI:29950, ChEBI:CHEBI:131710; EC=3.5.1.124; Evidence={ECO:0000255|HAMAP-Rule:MF_01046}; CATALYTIC ACTIVITY: Reaction=H2O + N(omega)-(1-hydroxy-2-oxoethyl)-L-arginyl-[protein] = glycolate + H(+) + L-arginyl-[protein]; Xref=Rhea:RHEA:57188, Rhea:RHEA-COMP:10532, Rhea:RHEA-COMP:14844, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:29805, ChEBI:CHEBI:29965, ChEBI:CHEBI:141553; EC=3.5.1.124; Evidence={ECO:0000255|HAMAP-Rule:MF_01046}; CATALYTIC ACTIVITY: Reaction=H2O + N(6)-(1-hydroxy-2-oxoethyl)-L-lysyl-[protein] = glycolate + H(+) + L-lysyl-[protein]; Xref=Rhea:RHEA:57192, Rhea:RHEA-COMP:9752, Rhea:RHEA-COMP:14845, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:29805, ChEBI:CHEBI:29969, ChEBI:CHEBI:141554; EC=3.5.1.124; Evidence={ECO:0000255|HAMAP-Rule:MF_01046}; CATALYTIC ACTIVITY: Reaction=H2O + S-(1-hydroxy-2-oxoethyl)-L-cysteinyl-[protein] = glycolate + H(+) + L-cysteinyl-[protein]; Xref=Rhea:RHEA:57196, Rhea:RHEA-COMP:10131, Rhea:RHEA-COMP:14846, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:29805, ChEBI:CHEBI:29950, ChEBI:CHEBI:141555; EC=3.5.1.124; Evidence={ECO:0000255|HAMAP-Rule:MF_01046}; CATALYTIC ACTIVITY: Reaction=H2O + N(2)-(1-hydroxy-2-oxopropyl)-dGTP = dGTP + H(+) + lactate; Xref=Rhea:RHEA:57244, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:24996, ChEBI:CHEBI:61429, ChEBI:CHEBI:141569; Evidence={ECO:0000255|HAMAP-Rule:MF_01046}; CATALYTIC ACTIVITY: Reaction=H2O + N(2)-(1-hydroxy-2-oxopropyl)-GTP = GTP + H(+) + lactate; Xref=Rhea:RHEA:57256, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:24996, ChEBI:CHEBI:37565, ChEBI:CHEBI:141570; Evidence={ECO:0000255|HAMAP-Rule:MF_01046}; CATALYTIC ACTIVITY: Reaction=H2O + N(2)-(1-hydroxy-2-oxopropyl)-GDP = GDP + H(+) + lactate; Xref=Rhea:RHEA:57260, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:24996, ChEBI:CHEBI:58189, ChEBI:CHEBI:141573; Evidence={ECO:0000255|HAMAP-Rule:MF_01046}; CATALYTIC ACTIVITY: Reaction=H2O + N(2)-(1-hydroxy-2-oxopropyl)-GMP = GMP + H(+) + lactate; Xref=Rhea:RHEA:57268, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:24996, ChEBI:CHEBI:58115, ChEBI:CHEBI:141575; Evidence={ECO:0000255|HAMAP-Rule:MF_01046}; CATALYTIC ACTIVITY: Reaction=H2O + N(2)-(1-hydroxy-2-oxoethyl)-dGTP = dGTP + glycolate + H(+); Xref=Rhea:RHEA:57248, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:29805, ChEBI:CHEBI:61429, ChEBI:CHEBI:141572; Evidence={ECO:0000255|HAMAP-Rule:MF_01046}; CATALYTIC ACTIVITY: Reaction=H2O + N(2)-(1-hydroxy-2-oxoethyl)-GTP = glycolate + GTP + H(+); Xref=Rhea:RHEA:57252, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:29805, ChEBI:CHEBI:37565, ChEBI:CHEBI:141571; Evidence={ECO:0000255|HAMAP-Rule:MF_01046}; CATALYTIC ACTIVITY: Reaction=H2O + N(2)-(1-hydroxy-2-oxoethyl)-GDP = GDP + glycolate + H(+); Xref=Rhea:RHEA:57264, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:29805, ChEBI:CHEBI:58189, ChEBI:CHEBI:141574; Evidence={ECO:0000255|HAMAP-Rule:MF_01046}; CATALYTIC ACTIVITY: Reaction=H2O + N(2)-(1-hydroxy-2-oxoethyl)-GMP = glycolate + GMP + H(+); Xref=Rhea:RHEA:57304, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:29805, ChEBI:CHEBI:58115, ChEBI:CHEBI:141576; Evidence={ECO:0000255|HAMAP-Rule:MF_01046}; CATALYTIC ACTIVITY: Reaction=an N(2)-(1-hydroxy-2-oxopropyl)-guanosine in RNA + H2O = a guanosine in RNA + H(+) + lactate; Xref=Rhea:RHEA:57288, Rhea:RHEA-COMP:14855, Rhea:RHEA-COMP:14858, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:24996, ChEBI:CHEBI:74269, ChEBI:CHEBI:141580; Evidence={ECO:0000255|HAMAP-Rule:MF_01046}; CATALYTIC ACTIVITY: Reaction=an N(2)-(1-hydroxy-2-oxopropyl)-2'-deoxyguanosine in DNA + H2O = a 2'-deoxyguanosine in DNA + H(+) + lactate; Xref=Rhea:RHEA:57300, Rhea:RHEA-COMP:11367, Rhea:RHEA-COMP:14856, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:24996, ChEBI:CHEBI:85445, ChEBI:CHEBI:141578; Evidence={ECO:0000255|HAMAP-Rule:MF_01046}; CATALYTIC ACTIVITY: Reaction=an N(2)-(1-hydroxy-2-oxoethyl)-guanosine in RNA + H2O = a guanosine in RNA + glycolate + H(+); Xref=Rhea:RHEA:57292, Rhea:RHEA-COMP:14855, Rhea:RHEA-COMP:14859, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:29805, ChEBI:CHEBI:74269, ChEBI:CHEBI:141581; Evidence={ECO:0000255|HAMAP-Rule:MF_01046}; CATALYTIC ACTIVITY: Reaction=an N(2)-(1-hydroxy-2-oxoethyl)-2'-deoxyguanosine in DNA + H2O = a 2'-deoxyguanosine in DNA + glycolate + H(+); Xref=Rhea:RHEA:57296, Rhea:RHEA-COMP:11367, Rhea:RHEA-COMP:14857, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:29805, ChEBI:CHEBI:85445, ChEBI:CHEBI:141579; Evidence={ECO:0000255|HAMAP-Rule:MF_01046}; | 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 proteins and lactate or glycolate, respectively. Deglycates cysteine, arginine and lysine residues in proteins, and thus reactivates these proteins by reversing glycation by glyoxals. Acts on early glycation intermediates (hemithioacetals and aminocarbinols), preventing the formation of Schiff bases and advanced glycation endproducts (AGE). Also functions as a nucleotide deglycase able to repair glycated guanine in the free nucleotide pool (GTP, GDP, GMP, dGTP) and in DNA and RNA. Is thus involved in a major nucleotide repair system named guanine glycation repair (GG repair), dedicated to reversing methylglyoxal and glyoxal damage via nucleotide sanitization and direct nucleic acid repair. Plays an important role in protecting cells from carbonyl stress. {ECO:0000255|HAMAP-Rule:MF_01046}. | 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:0000255|HAMAP-Rule:MF_01046}; CATALYTIC ACTIVITY: Reaction=H2O + N(6)-(1-hydroxy-2-oxopropyl)-L-lysyl-[protein] = H(+) + L-lysyl-[protein] + lactate; Xref=Rhea:RHEA:49552, Rhea:RHEA-COMP:9752, Rhea:RHEA-COMP:12429, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:24996, ChEBI:CHEBI:29969, ChEBI:CHEBI:131709; EC=3.5.1.124; Evidence={ECO:0000255|HAMAP-Rule:MF_01046}; CATALYTIC ACTIVITY: Reaction=H2O + S-(1-hydroxy-2-oxopropyl)-L-cysteinyl-[protein] = H(+) + L-cysteinyl-[protein] + lactate; Xref=Rhea:RHEA:49556, Rhea:RHEA-COMP:10131, Rhea:RHEA-COMP:12430, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:24996, ChEBI:CHEBI:29950, ChEBI:CHEBI:131710; EC=3.5.1.124; Evidence={ECO:0000255|HAMAP-Rule:MF_01046}; CATALYTIC ACTIVITY: Reaction=H2O + N(omega)-(1-hydroxy-2-oxoethyl)-L-arginyl-[protein] = glycolate + H(+) + L-arginyl-[protein]; Xref=Rhea:RHEA:57188, Rhea:RHEA-COMP:10532, Rhea:RHEA-COMP:14844, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:29805, ChEBI:CHEBI:29965, ChEBI:CHEBI:141553; EC=3.5.1.124; Evidence={ECO:0000255|HAMAP-Rule:MF_01046}; CATALYTIC ACTIVITY: Reaction=H2O + N(6)-(1-hydroxy-2-oxoethyl)-L-lysyl-[protein] = glycolate + H(+) + L-lysyl-[protein]; Xref=Rhea:RHEA:57192, Rhea:RHEA-COMP:9752, Rhea:RHEA-COMP:14845, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:29805, ChEBI:CHEBI:29969, ChEBI:CHEBI:141554; EC=3.5.1.124; Evidence={ECO:0000255|HAMAP-Rule:MF_01046}; CATALYTIC ACTIVITY: Reaction=H2O + S-(1-hydroxy-2-oxoethyl)-L-cysteinyl-[protein] = glycolate + H(+) + L-cysteinyl-[protein]; Xref=Rhea:RHEA:57196, Rhea:RHEA-COMP:10131, Rhea:RHEA-COMP:14846, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:29805, ChEBI:CHEBI:29950, ChEBI:CHEBI:141555; EC=3.5.1.124; Evidence={ECO:0000255|HAMAP-Rule:MF_01046}; CATALYTIC ACTIVITY: Reaction=H2O + N(2)-(1-hydroxy-2-oxopropyl)-dGTP = dGTP + H(+) + lactate; Xref=Rhea:RHEA:57244, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:24996, ChEBI:CHEBI:61429, ChEBI:CHEBI:141569; Evidence={ECO:0000255|HAMAP-Rule:MF_01046}; CATALYTIC ACTIVITY: Reaction=H2O + N(2)-(1-hydroxy-2-oxopropyl)-GTP = GTP + H(+) + lactate; Xref=Rhea:RHEA:57256, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:24996, ChEBI:CHEBI:37565, ChEBI:CHEBI:141570; Evidence={ECO:0000255|HAMAP-Rule:MF_01046}; CATALYTIC ACTIVITY: Reaction=H2O + N(2)-(1-hydroxy-2-oxopropyl)-GDP = GDP + H(+) + lactate; Xref=Rhea:RHEA:57260, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:24996, ChEBI:CHEBI:58189, ChEBI:CHEBI:141573; Evidence={ECO:0000255|HAMAP-Rule:MF_01046}; CATALYTIC ACTIVITY: Reaction=H2O + N(2)-(1-hydroxy-2-oxopropyl)-GMP = GMP + H(+) + lactate; Xref=Rhea:RHEA:57268, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:24996, ChEBI:CHEBI:58115, ChEBI:CHEBI:141575; Evidence={ECO:0000255|HAMAP-Rule:MF_01046}; CATALYTIC ACTIVITY: Reaction=H2O + N(2)-(1-hydroxy-2-oxoethyl)-dGTP = dGTP + glycolate + H(+); Xref=Rhea:RHEA:57248, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:29805, ChEBI:CHEBI:61429, ChEBI:CHEBI:141572; Evidence={ECO:0000255|HAMAP-Rule:MF_01046}; CATALYTIC ACTIVITY: Reaction=H2O + N(2)-(1-hydroxy-2-oxoethyl)-GTP = glycolate + GTP + H(+); Xref=Rhea:RHEA:57252, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:29805, ChEBI:CHEBI:37565, ChEBI:CHEBI:141571; Evidence={ECO:0000255|HAMAP-Rule:MF_01046}; CATALYTIC ACTIVITY: Reaction=H2O + N(2)-(1-hydroxy-2-oxoethyl)-GDP = GDP + glycolate + H(+); Xref=Rhea:RHEA:57264, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:29805, ChEBI:CHEBI:58189, ChEBI:CHEBI:141574; Evidence={ECO:0000255|HAMAP-Rule:MF_01046}; CATALYTIC ACTIVITY: Reaction=H2O + N(2)-(1-hydroxy-2-oxoethyl)-GMP = glycolate + GMP + H(+); Xref=Rhea:RHEA:57304, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:29805, ChEBI:CHEBI:58115, ChEBI:CHEBI:141576; Evidence={ECO:0000255|HAMAP-Rule:MF_01046}; CATALYTIC ACTIVITY: Reaction=an N(2)-(1-hydroxy-2-oxopropyl)-guanosine in RNA + H2O = a guanosine in RNA + H(+) + lactate; Xref=Rhea:RHEA:57288, Rhea:RHEA-COMP:14855, Rhea:RHEA-COMP:14858, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:24996, ChEBI:CHEBI:74269, ChEBI:CHEBI:141580; Evidence={ECO:0000255|HAMAP-Rule:MF_01046}; CATALYTIC ACTIVITY: Reaction=an N(2)-(1-hydroxy-2-oxopropyl)-2'-deoxyguanosine in DNA + H2O = a 2'-deoxyguanosine in DNA + H(+) + lactate; Xref=Rhea:RHEA:57300, Rhea:RHEA-COMP:11367, Rhea:RHEA-COMP:14856, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:24996, ChEBI:CHEBI:85445, ChEBI:CHEBI:141578; Evidence={ECO:0000255|HAMAP-Rule:MF_01046}; CATALYTIC ACTIVITY: Reaction=an N(2)-(1-hydroxy-2-oxoethyl)-guanosine in RNA + H2O = a guanosine in RNA + glycolate + H(+); Xref=Rhea:RHEA:57292, Rhea:RHEA-COMP:14855, Rhea:RHEA-COMP:14859, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:29805, ChEBI:CHEBI:74269, ChEBI:CHEBI:141581; Evidence={ECO:0000255|HAMAP-Rule:MF_01046}; CATALYTIC ACTIVITY: Reaction=an N(2)-(1-hydroxy-2-oxoethyl)-2'-deoxyguanosine in DNA + H2O = a 2'-deoxyguanosine in DNA + glycolate + H(+); Xref=Rhea:RHEA:57296, Rhea:RHEA-COMP:11367, Rhea:RHEA-COMP:14857, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:29805, ChEBI:CHEBI:85445, ChEBI:CHEBI:141579; Evidence={ECO:0000255|HAMAP-Rule:MF_01046}; | 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 proteins and lactate or glycolate, respectively. Deglycates cysteine, arginine and lysine residues in proteins, and thus reactivates these proteins by reversing glycation by glyoxals. Acts on early glycation intermediates (hemithioacetals and aminocarbinols), preventing the formation of Schiff bases and advanced glycation endproducts (AGE). Also functions as a nucleotide deglycase able to repair glycated guanine in the free nucleotide pool (GTP, GDP, GMP, dGTP) and in DNA and RNA. Is thus involved in a major nucleotide repair system named guanine glycation repair (GG repair), dedicated to reversing methylglyoxal and glyoxal damage via nucleotide sanitization and direct nucleic acid repair. Plays an important role in protecting cells from carbonyl stress. {ECO:0000255|HAMAP-Rule:MF_01046}. | 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:0000255|HAMAP-Rule:MF_01046}; CATALYTIC ACTIVITY: Reaction=H2O + N(6)-(1-hydroxy-2-oxopropyl)-L-lysyl-[protein] = H(+) + L-lysyl-[protein] + lactate; Xref=Rhea:RHEA:49552, Rhea:RHEA-COMP:9752, Rhea:RHEA-COMP:12429, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:24996, ChEBI:CHEBI:29969, ChEBI:CHEBI:131709; EC=3.5.1.124; Evidence={ECO:0000255|HAMAP-Rule:MF_01046}; CATALYTIC ACTIVITY: Reaction=H2O + S-(1-hydroxy-2-oxopropyl)-L-cysteinyl-[protein] = H(+) + L-cysteinyl-[protein] + lactate; Xref=Rhea:RHEA:49556, Rhea:RHEA-COMP:10131, Rhea:RHEA-COMP:12430, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:24996, ChEBI:CHEBI:29950, ChEBI:CHEBI:131710; EC=3.5.1.124; Evidence={ECO:0000255|HAMAP-Rule:MF_01046}; CATALYTIC ACTIVITY: Reaction=H2O + N(omega)-(1-hydroxy-2-oxoethyl)-L-arginyl-[protein] = glycolate + H(+) + L-arginyl-[protein]; Xref=Rhea:RHEA:57188, Rhea:RHEA-COMP:10532, Rhea:RHEA-COMP:14844, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:29805, ChEBI:CHEBI:29965, ChEBI:CHEBI:141553; EC=3.5.1.124; Evidence={ECO:0000255|HAMAP-Rule:MF_01046}; CATALYTIC ACTIVITY: Reaction=H2O + N(6)-(1-hydroxy-2-oxoethyl)-L-lysyl-[protein] = glycolate + H(+) + L-lysyl-[protein]; Xref=Rhea:RHEA:57192, Rhea:RHEA-COMP:9752, Rhea:RHEA-COMP:14845, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:29805, ChEBI:CHEBI:29969, ChEBI:CHEBI:141554; EC=3.5.1.124; Evidence={ECO:0000255|HAMAP-Rule:MF_01046}; CATALYTIC ACTIVITY: Reaction=H2O + S-(1-hydroxy-2-oxoethyl)-L-cysteinyl-[protein] = glycolate + H(+) + L-cysteinyl-[protein]; Xref=Rhea:RHEA:57196, Rhea:RHEA-COMP:10131, Rhea:RHEA-COMP:14846, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:29805, ChEBI:CHEBI:29950, ChEBI:CHEBI:141555; EC=3.5.1.124; Evidence={ECO:0000255|HAMAP-Rule:MF_01046}; CATALYTIC ACTIVITY: Reaction=H2O + N(2)-(1-hydroxy-2-oxopropyl)-dGTP = dGTP + H(+) + lactate; Xref=Rhea:RHEA:57244, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:24996, ChEBI:CHEBI:61429, ChEBI:CHEBI:141569; Evidence={ECO:0000255|HAMAP-Rule:MF_01046}; CATALYTIC ACTIVITY: Reaction=H2O + N(2)-(1-hydroxy-2-oxopropyl)-GTP = GTP + H(+) + lactate; Xref=Rhea:RHEA:57256, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:24996, ChEBI:CHEBI:37565, ChEBI:CHEBI:141570; Evidence={ECO:0000255|HAMAP-Rule:MF_01046}; CATALYTIC ACTIVITY: Reaction=H2O + N(2)-(1-hydroxy-2-oxopropyl)-GDP = GDP + H(+) + lactate; Xref=Rhea:RHEA:57260, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:24996, ChEBI:CHEBI:58189, ChEBI:CHEBI:141573; Evidence={ECO:0000255|HAMAP-Rule:MF_01046}; CATALYTIC ACTIVITY: Reaction=H2O + N(2)-(1-hydroxy-2-oxopropyl)-GMP = GMP + H(+) + lactate; Xref=Rhea:RHEA:57268, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:24996, ChEBI:CHEBI:58115, ChEBI:CHEBI:141575; Evidence={ECO:0000255|HAMAP-Rule:MF_01046}; CATALYTIC ACTIVITY: Reaction=H2O + N(2)-(1-hydroxy-2-oxoethyl)-dGTP = dGTP + glycolate + H(+); Xref=Rhea:RHEA:57248, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:29805, ChEBI:CHEBI:61429, ChEBI:CHEBI:141572; Evidence={ECO:0000255|HAMAP-Rule:MF_01046}; CATALYTIC ACTIVITY: Reaction=H2O + N(2)-(1-hydroxy-2-oxoethyl)-GTP = glycolate + GTP + H(+); Xref=Rhea:RHEA:57252, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:29805, ChEBI:CHEBI:37565, ChEBI:CHEBI:141571; Evidence={ECO:0000255|HAMAP-Rule:MF_01046}; CATALYTIC ACTIVITY: Reaction=H2O + N(2)-(1-hydroxy-2-oxoethyl)-GDP = GDP + glycolate + H(+); Xref=Rhea:RHEA:57264, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:29805, ChEBI:CHEBI:58189, ChEBI:CHEBI:141574; Evidence={ECO:0000255|HAMAP-Rule:MF_01046}; CATALYTIC ACTIVITY: Reaction=H2O + N(2)-(1-hydroxy-2-oxoethyl)-GMP = glycolate + GMP + H(+); Xref=Rhea:RHEA:57304, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:29805, ChEBI:CHEBI:58115, ChEBI:CHEBI:141576; Evidence={ECO:0000255|HAMAP-Rule:MF_01046}; CATALYTIC ACTIVITY: Reaction=an N(2)-(1-hydroxy-2-oxopropyl)-guanosine in RNA + H2O = a guanosine in RNA + H(+) + lactate; Xref=Rhea:RHEA:57288, Rhea:RHEA-COMP:14855, Rhea:RHEA-COMP:14858, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:24996, ChEBI:CHEBI:74269, ChEBI:CHEBI:141580; Evidence={ECO:0000255|HAMAP-Rule:MF_01046}; CATALYTIC ACTIVITY: Reaction=an N(2)-(1-hydroxy-2-oxopropyl)-2'-deoxyguanosine in DNA + H2O = a 2'-deoxyguanosine in DNA + H(+) + lactate; Xref=Rhea:RHEA:57300, Rhea:RHEA-COMP:11367, Rhea:RHEA-COMP:14856, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:24996, ChEBI:CHEBI:85445, ChEBI:CHEBI:141578; Evidence={ECO:0000255|HAMAP-Rule:MF_01046}; CATALYTIC ACTIVITY: Reaction=an N(2)-(1-hydroxy-2-oxoethyl)-guanosine in RNA + H2O = a guanosine in RNA + glycolate + H(+); Xref=Rhea:RHEA:57292, Rhea:RHEA-COMP:14855, Rhea:RHEA-COMP:14859, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:29805, ChEBI:CHEBI:74269, ChEBI:CHEBI:141581; Evidence={ECO:0000255|HAMAP-Rule:MF_01046}; CATALYTIC ACTIVITY: Reaction=an N(2)-(1-hydroxy-2-oxoethyl)-2'-deoxyguanosine in DNA + H2O = a 2'-deoxyguanosine in DNA + glycolate + H(+); Xref=Rhea:RHEA:57296, Rhea:RHEA-COMP:11367, Rhea:RHEA-COMP:14857, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:29805, ChEBI:CHEBI:85445, ChEBI:CHEBI:141579; Evidence={ECO:0000255|HAMAP-Rule:MF_01046}; | 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 proteins and lactate or glycolate, respectively. Deglycates cysteine, arginine and lysine residues in proteins, and thus reactivates these proteins by reversing glycation by glyoxals. Acts on early glycation intermediates (hemithioacetals and aminocarbinols), preventing the formation of Schiff bases and advanced glycation endproducts (AGE). Also functions as a nucleotide deglycase able to repair glycated guanine in the free nucleotide pool (GTP, GDP, GMP, dGTP) and in DNA and RNA. Is thus involved in a major nucleotide repair system named guanine glycation repair (GG repair), dedicated to reversing methylglyoxal and glyoxal damage via nucleotide sanitization and direct nucleic acid repair. Plays an important role in protecting cells from carbonyl stress. {ECO:0000255|HAMAP-Rule:MF_01046}. | 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:0000255|HAMAP-Rule:MF_01046}; CATALYTIC ACTIVITY: Reaction=H2O + N(6)-(1-hydroxy-2-oxopropyl)-L-lysyl-[protein] = H(+) + L-lysyl-[protein] + lactate; Xref=Rhea:RHEA:49552, Rhea:RHEA-COMP:9752, Rhea:RHEA-COMP:12429, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:24996, ChEBI:CHEBI:29969, ChEBI:CHEBI:131709; EC=3.5.1.124; Evidence={ECO:0000255|HAMAP-Rule:MF_01046}; CATALYTIC ACTIVITY: Reaction=H2O + S-(1-hydroxy-2-oxopropyl)-L-cysteinyl-[protein] = H(+) + L-cysteinyl-[protein] + lactate; Xref=Rhea:RHEA:49556, Rhea:RHEA-COMP:10131, Rhea:RHEA-COMP:12430, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:24996, ChEBI:CHEBI:29950, ChEBI:CHEBI:131710; EC=3.5.1.124; Evidence={ECO:0000255|HAMAP-Rule:MF_01046}; CATALYTIC ACTIVITY: Reaction=H2O + N(omega)-(1-hydroxy-2-oxoethyl)-L-arginyl-[protein] = glycolate + H(+) + L-arginyl-[protein]; Xref=Rhea:RHEA:57188, Rhea:RHEA-COMP:10532, Rhea:RHEA-COMP:14844, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:29805, ChEBI:CHEBI:29965, ChEBI:CHEBI:141553; EC=3.5.1.124; Evidence={ECO:0000255|HAMAP-Rule:MF_01046}; CATALYTIC ACTIVITY: Reaction=H2O + N(6)-(1-hydroxy-2-oxoethyl)-L-lysyl-[protein] = glycolate + H(+) + L-lysyl-[protein]; Xref=Rhea:RHEA:57192, Rhea:RHEA-COMP:9752, Rhea:RHEA-COMP:14845, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:29805, ChEBI:CHEBI:29969, ChEBI:CHEBI:141554; EC=3.5.1.124; Evidence={ECO:0000255|HAMAP-Rule:MF_01046}; CATALYTIC ACTIVITY: Reaction=H2O + S-(1-hydroxy-2-oxoethyl)-L-cysteinyl-[protein] = glycolate + H(+) + L-cysteinyl-[protein]; Xref=Rhea:RHEA:57196, Rhea:RHEA-COMP:10131, Rhea:RHEA-COMP:14846, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:29805, ChEBI:CHEBI:29950, ChEBI:CHEBI:141555; EC=3.5.1.124; Evidence={ECO:0000255|HAMAP-Rule:MF_01046}; CATALYTIC ACTIVITY: Reaction=H2O + N(2)-(1-hydroxy-2-oxopropyl)-dGTP = dGTP + H(+) + lactate; Xref=Rhea:RHEA:57244, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:24996, ChEBI:CHEBI:61429, ChEBI:CHEBI:141569; Evidence={ECO:0000255|HAMAP-Rule:MF_01046}; CATALYTIC ACTIVITY: Reaction=H2O + N(2)-(1-hydroxy-2-oxopropyl)-GTP = GTP + H(+) + lactate; Xref=Rhea:RHEA:57256, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:24996, ChEBI:CHEBI:37565, ChEBI:CHEBI:141570; Evidence={ECO:0000255|HAMAP-Rule:MF_01046}; CATALYTIC ACTIVITY: Reaction=H2O + N(2)-(1-hydroxy-2-oxopropyl)-GDP = GDP + H(+) + lactate; Xref=Rhea:RHEA:57260, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:24996, ChEBI:CHEBI:58189, ChEBI:CHEBI:141573; Evidence={ECO:0000255|HAMAP-Rule:MF_01046}; CATALYTIC ACTIVITY: Reaction=H2O + N(2)-(1-hydroxy-2-oxopropyl)-GMP = GMP + H(+) + lactate; Xref=Rhea:RHEA:57268, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:24996, ChEBI:CHEBI:58115, ChEBI:CHEBI:141575; Evidence={ECO:0000255|HAMAP-Rule:MF_01046}; CATALYTIC ACTIVITY: Reaction=H2O + N(2)-(1-hydroxy-2-oxoethyl)-dGTP = dGTP + glycolate + H(+); Xref=Rhea:RHEA:57248, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:29805, ChEBI:CHEBI:61429, ChEBI:CHEBI:141572; Evidence={ECO:0000255|HAMAP-Rule:MF_01046}; CATALYTIC ACTIVITY: Reaction=H2O + N(2)-(1-hydroxy-2-oxoethyl)-GTP = glycolate + GTP + H(+); Xref=Rhea:RHEA:57252, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:29805, ChEBI:CHEBI:37565, ChEBI:CHEBI:141571; Evidence={ECO:0000255|HAMAP-Rule:MF_01046}; CATALYTIC ACTIVITY: Reaction=H2O + N(2)-(1-hydroxy-2-oxoethyl)-GDP = GDP + glycolate + H(+); Xref=Rhea:RHEA:57264, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:29805, ChEBI:CHEBI:58189, ChEBI:CHEBI:141574; Evidence={ECO:0000255|HAMAP-Rule:MF_01046}; CATALYTIC ACTIVITY: Reaction=H2O + N(2)-(1-hydroxy-2-oxoethyl)-GMP = glycolate + GMP + H(+); Xref=Rhea:RHEA:57304, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:29805, ChEBI:CHEBI:58115, ChEBI:CHEBI:141576; Evidence={ECO:0000255|HAMAP-Rule:MF_01046}; CATALYTIC ACTIVITY: Reaction=an N(2)-(1-hydroxy-2-oxopropyl)-guanosine in RNA + H2O = a guanosine in RNA + H(+) + lactate; Xref=Rhea:RHEA:57288, Rhea:RHEA-COMP:14855, Rhea:RHEA-COMP:14858, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:24996, ChEBI:CHEBI:74269, ChEBI:CHEBI:141580; Evidence={ECO:0000255|HAMAP-Rule:MF_01046}; CATALYTIC ACTIVITY: Reaction=an N(2)-(1-hydroxy-2-oxopropyl)-2'-deoxyguanosine in DNA + H2O = a 2'-deoxyguanosine in DNA + H(+) + lactate; Xref=Rhea:RHEA:57300, Rhea:RHEA-COMP:11367, Rhea:RHEA-COMP:14856, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:24996, ChEBI:CHEBI:85445, ChEBI:CHEBI:141578; Evidence={ECO:0000255|HAMAP-Rule:MF_01046}; CATALYTIC ACTIVITY: Reaction=an N(2)-(1-hydroxy-2-oxoethyl)-guanosine in RNA + H2O = a guanosine in RNA + glycolate + H(+); Xref=Rhea:RHEA:57292, Rhea:RHEA-COMP:14855, Rhea:RHEA-COMP:14859, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:29805, ChEBI:CHEBI:74269, ChEBI:CHEBI:141581; Evidence={ECO:0000255|HAMAP-Rule:MF_01046}; CATALYTIC ACTIVITY: Reaction=an N(2)-(1-hydroxy-2-oxoethyl)-2'-deoxyguanosine in DNA + H2O = a 2'-deoxyguanosine in DNA + glycolate + H(+); Xref=Rhea:RHEA:57296, Rhea:RHEA-COMP:11367, Rhea:RHEA-COMP:14857, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:29805, ChEBI:CHEBI:85445, ChEBI:CHEBI:141579; Evidence={ECO:0000255|HAMAP-Rule:MF_01046}; | 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 proteins and lactate or glycolate, respectively. Deglycates cysteine, arginine and lysine residues in proteins, and thus reactivates these proteins by reversing glycation by glyoxals. Acts on early glycation intermediates (hemithioacetals and aminocarbinols), preventing the formation of Schiff bases and advanced glycation endproducts (AGE). Also functions as a nucleotide deglycase able to repair glycated guanine in the free nucleotide pool (GTP, GDP, GMP, dGTP) and in DNA and RNA. Is thus involved in a major nucleotide repair system named guanine glycation repair (GG repair), dedicated to reversing methylglyoxal and glyoxal damage via nucleotide sanitization and direct nucleic acid repair. Plays an important role in protecting cells from carbonyl stress. {ECO:0000255|HAMAP-Rule:MF_01046}. | 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:0000255|HAMAP-Rule:MF_01046}; CATALYTIC ACTIVITY: Reaction=H2O + N(6)-(1-hydroxy-2-oxopropyl)-L-lysyl-[protein] = H(+) + L-lysyl-[protein] + lactate; Xref=Rhea:RHEA:49552, Rhea:RHEA-COMP:9752, Rhea:RHEA-COMP:12429, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:24996, ChEBI:CHEBI:29969, ChEBI:CHEBI:131709; EC=3.5.1.124; Evidence={ECO:0000255|HAMAP-Rule:MF_01046}; CATALYTIC ACTIVITY: Reaction=H2O + S-(1-hydroxy-2-oxopropyl)-L-cysteinyl-[protein] = H(+) + L-cysteinyl-[protein] + lactate; Xref=Rhea:RHEA:49556, Rhea:RHEA-COMP:10131, Rhea:RHEA-COMP:12430, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:24996, ChEBI:CHEBI:29950, ChEBI:CHEBI:131710; EC=3.5.1.124; Evidence={ECO:0000255|HAMAP-Rule:MF_01046}; CATALYTIC ACTIVITY: Reaction=H2O + N(omega)-(1-hydroxy-2-oxoethyl)-L-arginyl-[protein] = glycolate + H(+) + L-arginyl-[protein]; Xref=Rhea:RHEA:57188, Rhea:RHEA-COMP:10532, Rhea:RHEA-COMP:14844, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:29805, ChEBI:CHEBI:29965, ChEBI:CHEBI:141553; EC=3.5.1.124; Evidence={ECO:0000255|HAMAP-Rule:MF_01046}; CATALYTIC ACTIVITY: Reaction=H2O + N(6)-(1-hydroxy-2-oxoethyl)-L-lysyl-[protein] = glycolate + H(+) + L-lysyl-[protein]; Xref=Rhea:RHEA:57192, Rhea:RHEA-COMP:9752, Rhea:RHEA-COMP:14845, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:29805, ChEBI:CHEBI:29969, ChEBI:CHEBI:141554; EC=3.5.1.124; Evidence={ECO:0000255|HAMAP-Rule:MF_01046}; CATALYTIC ACTIVITY: Reaction=H2O + S-(1-hydroxy-2-oxoethyl)-L-cysteinyl-[protein] = glycolate + H(+) + L-cysteinyl-[protein]; Xref=Rhea:RHEA:57196, Rhea:RHEA-COMP:10131, Rhea:RHEA-COMP:14846, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:29805, ChEBI:CHEBI:29950, ChEBI:CHEBI:141555; EC=3.5.1.124; Evidence={ECO:0000255|HAMAP-Rule:MF_01046}; CATALYTIC ACTIVITY: Reaction=H2O + N(2)-(1-hydroxy-2-oxopropyl)-dGTP = dGTP + H(+) + lactate; Xref=Rhea:RHEA:57244, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:24996, ChEBI:CHEBI:61429, ChEBI:CHEBI:141569; Evidence={ECO:0000255|HAMAP-Rule:MF_01046}; CATALYTIC ACTIVITY: Reaction=H2O + N(2)-(1-hydroxy-2-oxopropyl)-GTP = GTP + H(+) + lactate; Xref=Rhea:RHEA:57256, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:24996, ChEBI:CHEBI:37565, ChEBI:CHEBI:141570; Evidence={ECO:0000255|HAMAP-Rule:MF_01046}; CATALYTIC ACTIVITY: Reaction=H2O + N(2)-(1-hydroxy-2-oxopropyl)-GDP = GDP + H(+) + lactate; Xref=Rhea:RHEA:57260, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:24996, ChEBI:CHEBI:58189, ChEBI:CHEBI:141573; Evidence={ECO:0000255|HAMAP-Rule:MF_01046}; CATALYTIC ACTIVITY: Reaction=H2O + N(2)-(1-hydroxy-2-oxopropyl)-GMP = GMP + H(+) + lactate; Xref=Rhea:RHEA:57268, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:24996, ChEBI:CHEBI:58115, ChEBI:CHEBI:141575; Evidence={ECO:0000255|HAMAP-Rule:MF_01046}; CATALYTIC ACTIVITY: Reaction=H2O + N(2)-(1-hydroxy-2-oxoethyl)-dGTP = dGTP + glycolate + H(+); Xref=Rhea:RHEA:57248, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:29805, ChEBI:CHEBI:61429, ChEBI:CHEBI:141572; Evidence={ECO:0000255|HAMAP-Rule:MF_01046}; CATALYTIC ACTIVITY: Reaction=H2O + N(2)-(1-hydroxy-2-oxoethyl)-GTP = glycolate + GTP + H(+); Xref=Rhea:RHEA:57252, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:29805, ChEBI:CHEBI:37565, ChEBI:CHEBI:141571; Evidence={ECO:0000255|HAMAP-Rule:MF_01046}; CATALYTIC ACTIVITY: Reaction=H2O + N(2)-(1-hydroxy-2-oxoethyl)-GDP = GDP + glycolate + H(+); Xref=Rhea:RHEA:57264, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:29805, ChEBI:CHEBI:58189, ChEBI:CHEBI:141574; Evidence={ECO:0000255|HAMAP-Rule:MF_01046}; CATALYTIC ACTIVITY: Reaction=H2O + N(2)-(1-hydroxy-2-oxoethyl)-GMP = glycolate + GMP + H(+); Xref=Rhea:RHEA:57304, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:29805, ChEBI:CHEBI:58115, ChEBI:CHEBI:141576; Evidence={ECO:0000255|HAMAP-Rule:MF_01046}; CATALYTIC ACTIVITY: Reaction=an N(2)-(1-hydroxy-2-oxopropyl)-guanosine in RNA + H2O = a guanosine in RNA + H(+) + lactate; Xref=Rhea:RHEA:57288, Rhea:RHEA-COMP:14855, Rhea:RHEA-COMP:14858, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:24996, ChEBI:CHEBI:74269, ChEBI:CHEBI:141580; Evidence={ECO:0000255|HAMAP-Rule:MF_01046}; CATALYTIC ACTIVITY: Reaction=an N(2)-(1-hydroxy-2-oxopropyl)-2'-deoxyguanosine in DNA + H2O = a 2'-deoxyguanosine in DNA + H(+) + lactate; Xref=Rhea:RHEA:57300, Rhea:RHEA-COMP:11367, Rhea:RHEA-COMP:14856, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:24996, ChEBI:CHEBI:85445, ChEBI:CHEBI:141578; Evidence={ECO:0000255|HAMAP-Rule:MF_01046}; CATALYTIC ACTIVITY: Reaction=an N(2)-(1-hydroxy-2-oxoethyl)-guanosine in RNA + H2O = a guanosine in RNA + glycolate + H(+); Xref=Rhea:RHEA:57292, Rhea:RHEA-COMP:14855, Rhea:RHEA-COMP:14859, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:29805, ChEBI:CHEBI:74269, ChEBI:CHEBI:141581; Evidence={ECO:0000255|HAMAP-Rule:MF_01046}; CATALYTIC ACTIVITY: Reaction=an N(2)-(1-hydroxy-2-oxoethyl)-2'-deoxyguanosine in DNA + H2O = a 2'-deoxyguanosine in DNA + glycolate + H(+); Xref=Rhea:RHEA:57296, Rhea:RHEA-COMP:11367, Rhea:RHEA-COMP:14857, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:29805, ChEBI:CHEBI:85445, ChEBI:CHEBI:141579; Evidence={ECO:0000255|HAMAP-Rule:MF_01046}; | 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 proteins and lactate or glycolate, respectively. Deglycates cysteine, arginine and lysine residues in proteins, and thus reactivates these proteins by reversing glycation by glyoxals. Acts on early glycation intermediates (hemithioacetals and aminocarbinols), preventing the formation of Schiff bases and advanced glycation endproducts (AGE). Also functions as a nucleotide deglycase able to repair glycated guanine in the free nucleotide pool (GTP, GDP, GMP, dGTP) and in DNA and RNA. Is thus involved in a major nucleotide repair system named guanine glycation repair (GG repair), dedicated to reversing methylglyoxal and glyoxal damage via nucleotide sanitization and direct nucleic acid repair. Plays an important role in protecting cells from carbonyl stress. {ECO:0000255|HAMAP-Rule:MF_01046}. | Escherichia coli O7:K1 (strain IAI39 / ExPEC) |
B7QK46 | QPCT_IXOSC | MLFPVLLLLKLVIGALIIDASALSWHDLKWPRDLRPLAHHDLLYMGQISEEDRGDFNATLRNFLVPRVVGSQKHREVREFIVRSLKDLDWDVEEDCFDGQTPHGIKPFCNVIATLNPSACHRLVLACHYDSLLHKEGTFIGATDSAVPCAQLLYLARSLNGKLQNQKTRGDGLTLQLVFFDGEEAFERWSSHDSLYGSRHLAQKWHEDRTSAERLESCLERSEIANQIDRMEVMVLLDLLGAENPRFYSYFGETQPVYRRLVNIESRLNDAGLMELPRRRRRTNYFSNSSTVGFIEDDHIPFLKRSVPIVHIIPSPFPDVWHTLDDNEQNLHHPTISNLNKIFKAFVSEYLQL | 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:24598748}; Note=kcat is 8.8 sec(-1) for L-glutaminyl 2-naphthylamide (Gln-beta-NA) in the presence of Zn(2+). kcat is 6.9 sec(-1) for L-glutaminyl 2-naphthylamide (Gln-beta-NA) in the absence of Zn(2+). {ECO:0000269|PubMed:24598748}; | 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]-periviscerokinin and [Gln-1]-sulfakinin (PubMed:24598748). {ECO:0000269|PubMed:23770496, ECO:0000269|PubMed:24598748}. | 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 nM), tissue kallikrein (Ki=0.23 nM), trypsin (Ki=0.31 nM), plasmin (Ki=6.1 nM), elastase (Ki=201 nM), factor Xa (Ki=871 nM), alpha-factor XIIa (Ki=2380 nM). Does not inhibit APC, urokinase-type plasminogen activator (uPA/PLAU), tissue plasminogen activator (tPA/PLAT), thrombin and factor VIIa. In addition, the monomer inhibits fibrinolysis in whole blood and prolonged the intrinsec clotting time. | Oxyuranus scutellatus scutellatus (Australian taipan) (Coastal taipan) |
B7SBD2 | TOX3_RAT | MDVRFYPAAAGDPAGLDFAQCLGYYGYSKLGNNNYMNMAEANNAFFAASEQTFHTPSLGDEEFEIPPITPPPESDPTLGMPDVLLPFQTLSDPLPSQGNEFTPQFPPQSLDLPSITISRNLVEQDGVLHSNGLHMDQSHTQVSQYRQDPSLVMRSIVHMTDAARSGIMPPAQLTTINQSQLSAQLGLNLGGASVPHTSPSPPASKSATPSPSSSINEEDADETNRAVGEKRTAPDSGKKPKTPKKKKKKDPNEPQKPVSAYALFFRDTQAAIKGQNPNATFGEVSKIVASMWDSLGEEQKQVYKRKTEAAKKEYLKALAAYRASLVSKAAAESAEAQTIRSVQQTLASTNLTSSLLLNTSLSQHGTVPASPQTLPQSLPRSIAPKPLTMRLPMSQIVTSVTIAANMPSNIGAPLISSMGTTMVGSVSSTQVSPSVQTQQHQLQLQQQQQQQQQQMQQMQHQQLQQHQMHQQIQQQMQQQHFQHHMQQHLQQQQQQHLQQQISQQQLQQQLQQHLQLQQQLQHMQHQSQPSPRQHSPVTSQITSPIPAIGSPQPASQQHQPQIQSQTQTQVLPQVSIF | 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]; regulation of transcription by RNA polymerase II [GO:0006357] | 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 promoters. Required for depolarization-induced transcription activation of the C-FOS promoter in neurons. Associates with chromatin to the estrogen-responsive C3 promoter region. {ECO:0000269|PubMed:19196971}. | 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 | MKAGRAFGCLFWALLYCVLYLDLVSGNSADDELMDFDFADSNDAAMEDWQLDDLEEAKKAEQAEKKLESNMLDFSVDLDEPEPEKQLPPFDWRERVLRNALAKALADEGLRQKFAEVLPILRMLSSQQRLALSALISAQMNAKKGHELKFEQVRMMFGNEKKLLLPIVFDIANLIKSSTRKYINLGSDLASSALYHTPINRREDDLTPEESQQDDQLGTIAVEVEPKKVSTEEVQLESLEDFFDEMGSEVLDPQMINEALTGDLHDNKTKTFKPENHGQRVRRSANEFVHKLTRSVPASVTEQQLLGGIAGRTIKLNTTAFQQPSSQEEEKMASSNGGQSYSEVEDLAFAGLNGTEIPLSADERLDLQRNSAEETEEPLPSPEELIAGPRYRLGKRPLPGQKSGSPIKRKRVTSSLRGRPKTAASSHKPVVTPPNKKCERFTSNMCIRTDDYPLEQIMGSIRRHKNAMSALLAEFYDKPNNNLEFSDDFDDFSLSKKRREDEGSAGGMCQSVVRYARPQKAKSASGEWKYIVNTGQHTQTLRLEKCSNPVESCSYLAQTYRSHCSQVYNYHRLLSWDKVRGLHVDIFKVPTCCSCQVDGYRQQFPPLSSIQAKDYSPQSPVINHSHNGYSTINEEDLDYAEESEEDELGLRYPSFNNRETNELYSSSNKVRVKLPGISSSVGPYLSPPDDDEDRYGGYKSSSSSSKKYYSQVSRRRPQHSEARLDLDLAPSETHSDQEPPPPQHHQHHHLQYHRPQEELPSAYDFHRPQVYQPEREQLPLVRDPALSPVSAPVLASPAPPLPMPPMPIKQVPSHHQAHHQQPHHHLHQSTGKVAANRDPASMHHQPPRRPTQQWLPGQRRPFRPSAPLSGSGISRRHYHNRRQSIQ | 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 targeting of ISNb/d motorneurons and also some SNa motorneurons (PubMed:19018662). In larvae, involved in the negative regulation of the tracheal immune response to bacterial infection perhaps by acting as a ligand for the Toll-related receptor Tollo (PubMed:22022271). May be involved in the normal development of specific neurons at the neuromuscular junction (PubMed:24124519). {ECO:0000269|PubMed:19018662, ECO:0000269|PubMed:22022271, ECO:0000269|PubMed:23892553, ECO:0000269|PubMed:24124519}. | Drosophila melanogaster (Fruit fly) |
B7U179 | ABAP1_ARATH | MIISKSFKAPLKFSVKSSTAPVISNHPPMENHPKRQRTTRLAARNLKRKLSHNTDGAPIVTQLIDIDDEPIDLVVAIRRHVEVLNSSFSDPDFDHEAVKEAAADIADLAKIDENVEIIVENGAIPALVRYLESPLVVCGNVPKSCEHKLEKDCALALGLIAAIQPGYQQLIVDAGAIVPTVKLLKRRGECGECMFANAVIRRAADIITNIAHDNPRIKTNIRVEGGIAPLVELLNFPDVKVQRAAAGALRTVSFRNDENKSQIVELNALPTLVLMLQSQDSTVHGEAIGAIGNLVHSSPDIKKEVIRAGALQPVIGLLSSTCLETQREAALLIGQFAAPDSDCKVHIAQRGAITPLIKMLESSDEQVVEMSAFALGRLAQDAHNQAGIAHRGGIISLLNLLDVKTGSVQHNAAFALYGLADNEENVADFIKAGGIQKLQDDNFTVQPTRDCVVRTLKRLQNKIHGPVLNQLLYLMRTAEKTVQIRIALALAHLCDPKDGKLIFIDNNGVEFLLELLYFSSNKQQRYSSSALYELAKKATSFAPEDSAPCSPTQQVFLGEKFVNNPTMSDVTFLIDGKQFYAHKIGLVASSDIFRAMFDGLYKERNAQNVEIPNIRWEVFELMMKFIYSGRINIAKHLAKDLLVAADQYLLEGLKRQCEYTIAQEICLDNIPEMYELADTFNASALRRACTLFVLEHFTKLSSQLWFAKFVKQIIPEIRSYMTDILTRPVEASPPTVV | 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 inhibiting mitotic DNA replication. {ECO:0000250, ECO:0000269|PubMed:18818695}. | Arabidopsis thaliana (Mouse-ear cress) |
B7U540 | KCJ18_HUMAN | MTAASRANPYSIVSLEEDGLHLVTMSGANGFGNGKVHTRRRCRNRFVKKNGQCNIAFANMDEKSQRYLADMFTTCVDIRWRYMLLIFSLAFLASWLLFGVIFWVIAVAHGDLEPAEGHGRTPCVMQVHGFMAAFLFSIETQTTIGYGLRCVTEECLVAVFMVVAQSIVGCIIDSFMIGAIMAKMARPKKRAQTLLFSHNAVVALRDGKLCLMWRVGNLRKSHIVEAHVRAQLIKPRVTEEGEYIPLDQIDIDVGFDKGLDRIFLVSPITILHEIDEASPLFGISRQDLETDDFEIVVILEGMVEATAMTTQARSSYLANEILWGHRFEPVLFEEKNQYKIDYSHFHKTYEVPSTPRCSAKDLVENKFLLPSANSFCYENELAFLSRDEEDEADGDQDGRSRDGLSPQARHDFDRLQAGGGVLEQRPYRRGSEI | 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 more positive voltages. The inward rectification is mainly due to the blockage of outward current by internal magnesium. {ECO:0000269|PubMed:20074522, ECO:0000269|PubMed:27008341}. | Homo sapiens (Human) |
B7UI21 | NLEB1_ECO27 | MLSSLNVLQSSFRGKTALSNSTLLQKVSFAGKEYSLEPIDERTPILFQWFEARPERYEKGEVPILNTKEHPYLSNIINAAKIENERIIGVLVDGNFTYEQKKEFLNLENEHQNIKIIYRADVDFSMYDKKLSDIYLENIHKQESYPASERDNYLLGLLREELKNIPEGKDSLIESYAEKREHTWFDFFRNLAILKAGSLFTETGKTGCHNISPCSGCIYLDADMIITDKLGVLYAPDGIAVHVDCNDEIKSLENGAIVVNRSNHPALLAGLDIMKSKVDAHPYYDGLGKGIKRHFNYSSLHNYNAFCDFIEFKHENIIPNTSMYTSSSW | 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; Evidence={ECO:0000269|PubMed:23955153, ECO:0000269|PubMed:24025841, ECO:0000269|PubMed:26883593, ECO:0000269|PubMed:28860194, ECO:0000269|PubMed:30125331, ECO:0000269|PubMed:30979585, ECO:0000269|PubMed:32432056}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:66633; Evidence={ECO:0000269|PubMed:23955153, ECO:0000269|PubMed:24025841, ECO:0000269|PubMed:26883593, ECO:0000269|PubMed:28860194, ECO:0000269|PubMed:30125331, ECO:0000269|PubMed:30979585, ECO:0000269|PubMed:32432056}; | 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 catalyzing the transfer of a single N-acetylglucosamine (GlcNAc) to a conserved arginine residue in the death domain of host proteins FADD, TRADD, FAS, TNFRSF1A/TNFR1, TNFRSF25/DR3 and RIPK1: arginine GlcNAcylation prevents homotypic/heterotypic death domain interactions and assembly of the oligomeric TNF-alpha receptor complex, thereby disrupting TNF signaling (PubMed:23955153, PubMed:24025841, PubMed:26883593, PubMed:28522607, PubMed:28860194, PubMed:30979585). Has preference for host FADD as substrate compared to other death domain-containing proteins (PubMed:28860194). Also acts on host proteins without a death domain: catalyzes arginine GlcNAcylation of HIF1A, thereby regulating host glucose metabolism (PubMed:30125331). Also displays intra-bacterial activity by mediating GlcNAcylation of glutathione synthetase GshB (PubMed:31974499). Catalyzes auto-GlcNAcylation, which is required for activity toward death domain-containing host target proteins (PubMed:32432056). Shows a higher enzymatic activity than NleB2 (PubMed:23955153). {ECO:0000269|PubMed:20126447, ECO:0000269|PubMed:20485572, ECO:0000269|PubMed:22144899, ECO:0000269|PubMed:23955153, ECO:0000269|PubMed:24025841, ECO:0000269|PubMed:26883593, ECO:0000269|PubMed:28138023, ECO:0000269|PubMed:28522607, ECO:0000269|PubMed:28860194, ECO:0000269|PubMed:30125331, ECO:0000269|PubMed:30979585, ECO:0000269|PubMed:31974499, ECO:0000269|PubMed:32432056}. | 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:0000269|PubMed:22158122, ECO:0000269|PubMed:25412445, ECO:0000269|PubMed:27445336}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:66545; Evidence={ECO:0000269|PubMed:22158122, ECO:0000269|PubMed:25412445, ECO:0000269|PubMed:27445336}; | 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: methylation of a conserved cysteine residue of the RanBP2-type zinc finger (NZF) of TAB2 and TAB3 disrupts zinc-binding, thereby inactivating the ubiquitin chain-binding activity of TAB2 and TAB3, leading to NF-kappa-B inactivation (PubMed:22158122, PubMed:25412445, PubMed:27445336). Also mediates cysteine methylation of host protein ZRANB3, inactivating its ability to bind ubiquitin chains (PubMed:25412445). {ECO:0000269|PubMed:20126447, ECO:0000269|PubMed:20485572, ECO:0000269|PubMed:22158122, ECO:0000269|PubMed:25412445, ECO:0000269|PubMed:27445336}. | Escherichia coli O127:H6 (strain E2348/69 / EPEC) |
B7UM99 | TIR_ECO27 | MPIGNLGNNVNGNHLIPPAPPLPSQTDGAARGGTGHLISSTGALGSRSLFSPLRNSMADSVDSRDIPGLPTNPSRLAAATSETCLLGGFEVLHDKGPLDILNTQIGPSAFRVEVQADGTHAAIGEKNGLEVSVTLSPQEWSSLQSIDTEGKNRFVFTGGRGGSGHPMVTVASDIAEARTKILAKLDPDNHGGRQPKDVDTRSVGVGSASGIDDGVVSETHTSTTNSSVRSDPKFWVSVGAIAAGLAGLAATGIAQALALTPEPDDPTTTDPDQAANAAESATKDQLTQEAFKNPENQKVNIDANGNAIPSGELKDDIVEQIAQQAKEAGEVARQQAVESNAQAQQRYEDQHARRQEELQLSSGIGYGLSSALIVAGGIGAGVTTALHRRNQPAEQTTTTTTHTVVQQQTGGNTPAQGGTDATRAEDASLNRRDSQGSVASTHWSDSSSEVVNPYAEVGGARNSLSAHQPEEHIYDEVAADPGYSVIQNFSGSGPVTGRLIGTPGQGIQSTYALLANSGGLRLGMGGLTSGGESAVSSVNAAPTPGPVRFV | 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:16636066, ECO:0000269|PubMed:9390560}. | 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 pedestal. | 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 signaling cascade in the host cell, which leads to actin polymerization and formation of actin pedestals at the sites of bacterial adhesion. In strain E2348/69, acts mainly via the host adaptor proteins NCK1 and NCK2. Once clustered and phosphorylated at Tyr-474, Tir binds to NCK proteins, which in turn bind and activate host WASL/N-WASP, leading to actin polymerization. Can also trigger an inefficient, NCK-independent pedestal formation. This pathway involves phosphorylation of Tyr-454 and probably a putative host adaptor. Acts also via direct binding to the host cytoskeletal protein alpha-actinin in a NCK- and phosphotyrosine-independent manner. This interaction may stabilize the pedestal, but is not essential for its formation. {ECO:0000269|PubMed:10096089, ECO:0000269|PubMed:14757753, ECO:0000269|PubMed:14764108, ECO:0000269|PubMed:15813734, ECO:0000269|PubMed:17521329, ECO:0000269|PubMed:9390560}. | 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:0000255|HAMAP-Rule:MF_01046}; CATALYTIC ACTIVITY: Reaction=H2O + N(6)-(1-hydroxy-2-oxopropyl)-L-lysyl-[protein] = H(+) + L-lysyl-[protein] + lactate; Xref=Rhea:RHEA:49552, Rhea:RHEA-COMP:9752, Rhea:RHEA-COMP:12429, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:24996, ChEBI:CHEBI:29969, ChEBI:CHEBI:131709; EC=3.5.1.124; Evidence={ECO:0000255|HAMAP-Rule:MF_01046}; CATALYTIC ACTIVITY: Reaction=H2O + S-(1-hydroxy-2-oxopropyl)-L-cysteinyl-[protein] = H(+) + L-cysteinyl-[protein] + lactate; Xref=Rhea:RHEA:49556, Rhea:RHEA-COMP:10131, Rhea:RHEA-COMP:12430, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:24996, ChEBI:CHEBI:29950, ChEBI:CHEBI:131710; EC=3.5.1.124; Evidence={ECO:0000255|HAMAP-Rule:MF_01046}; CATALYTIC ACTIVITY: Reaction=H2O + N(omega)-(1-hydroxy-2-oxoethyl)-L-arginyl-[protein] = glycolate + H(+) + L-arginyl-[protein]; Xref=Rhea:RHEA:57188, Rhea:RHEA-COMP:10532, Rhea:RHEA-COMP:14844, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:29805, ChEBI:CHEBI:29965, ChEBI:CHEBI:141553; EC=3.5.1.124; Evidence={ECO:0000255|HAMAP-Rule:MF_01046}; CATALYTIC ACTIVITY: Reaction=H2O + N(6)-(1-hydroxy-2-oxoethyl)-L-lysyl-[protein] = glycolate + H(+) + L-lysyl-[protein]; Xref=Rhea:RHEA:57192, Rhea:RHEA-COMP:9752, Rhea:RHEA-COMP:14845, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:29805, ChEBI:CHEBI:29969, ChEBI:CHEBI:141554; EC=3.5.1.124; Evidence={ECO:0000255|HAMAP-Rule:MF_01046}; CATALYTIC ACTIVITY: Reaction=H2O + S-(1-hydroxy-2-oxoethyl)-L-cysteinyl-[protein] = glycolate + H(+) + L-cysteinyl-[protein]; Xref=Rhea:RHEA:57196, Rhea:RHEA-COMP:10131, Rhea:RHEA-COMP:14846, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:29805, ChEBI:CHEBI:29950, ChEBI:CHEBI:141555; EC=3.5.1.124; Evidence={ECO:0000255|HAMAP-Rule:MF_01046}; CATALYTIC ACTIVITY: Reaction=H2O + N(2)-(1-hydroxy-2-oxopropyl)-dGTP = dGTP + H(+) + lactate; Xref=Rhea:RHEA:57244, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:24996, ChEBI:CHEBI:61429, ChEBI:CHEBI:141569; Evidence={ECO:0000255|HAMAP-Rule:MF_01046}; CATALYTIC ACTIVITY: Reaction=H2O + N(2)-(1-hydroxy-2-oxopropyl)-GTP = GTP + H(+) + lactate; Xref=Rhea:RHEA:57256, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:24996, ChEBI:CHEBI:37565, ChEBI:CHEBI:141570; Evidence={ECO:0000255|HAMAP-Rule:MF_01046}; CATALYTIC ACTIVITY: Reaction=H2O + N(2)-(1-hydroxy-2-oxopropyl)-GDP = GDP + H(+) + lactate; Xref=Rhea:RHEA:57260, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:24996, ChEBI:CHEBI:58189, ChEBI:CHEBI:141573; Evidence={ECO:0000255|HAMAP-Rule:MF_01046}; CATALYTIC ACTIVITY: Reaction=H2O + N(2)-(1-hydroxy-2-oxopropyl)-GMP = GMP + H(+) + lactate; Xref=Rhea:RHEA:57268, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:24996, ChEBI:CHEBI:58115, ChEBI:CHEBI:141575; Evidence={ECO:0000255|HAMAP-Rule:MF_01046}; CATALYTIC ACTIVITY: Reaction=H2O + N(2)-(1-hydroxy-2-oxoethyl)-dGTP = dGTP + glycolate + H(+); Xref=Rhea:RHEA:57248, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:29805, ChEBI:CHEBI:61429, ChEBI:CHEBI:141572; Evidence={ECO:0000255|HAMAP-Rule:MF_01046}; CATALYTIC ACTIVITY: Reaction=H2O + N(2)-(1-hydroxy-2-oxoethyl)-GTP = glycolate + GTP + H(+); Xref=Rhea:RHEA:57252, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:29805, ChEBI:CHEBI:37565, ChEBI:CHEBI:141571; Evidence={ECO:0000255|HAMAP-Rule:MF_01046}; CATALYTIC ACTIVITY: Reaction=H2O + N(2)-(1-hydroxy-2-oxoethyl)-GDP = GDP + glycolate + H(+); Xref=Rhea:RHEA:57264, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:29805, ChEBI:CHEBI:58189, ChEBI:CHEBI:141574; Evidence={ECO:0000255|HAMAP-Rule:MF_01046}; CATALYTIC ACTIVITY: Reaction=H2O + N(2)-(1-hydroxy-2-oxoethyl)-GMP = glycolate + GMP + H(+); Xref=Rhea:RHEA:57304, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:29805, ChEBI:CHEBI:58115, ChEBI:CHEBI:141576; Evidence={ECO:0000255|HAMAP-Rule:MF_01046}; CATALYTIC ACTIVITY: Reaction=an N(2)-(1-hydroxy-2-oxopropyl)-guanosine in RNA + H2O = a guanosine in RNA + H(+) + lactate; Xref=Rhea:RHEA:57288, Rhea:RHEA-COMP:14855, Rhea:RHEA-COMP:14858, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:24996, ChEBI:CHEBI:74269, ChEBI:CHEBI:141580; Evidence={ECO:0000255|HAMAP-Rule:MF_01046}; CATALYTIC ACTIVITY: Reaction=an N(2)-(1-hydroxy-2-oxopropyl)-2'-deoxyguanosine in DNA + H2O = a 2'-deoxyguanosine in DNA + H(+) + lactate; Xref=Rhea:RHEA:57300, Rhea:RHEA-COMP:11367, Rhea:RHEA-COMP:14856, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:24996, ChEBI:CHEBI:85445, ChEBI:CHEBI:141578; Evidence={ECO:0000255|HAMAP-Rule:MF_01046}; CATALYTIC ACTIVITY: Reaction=an N(2)-(1-hydroxy-2-oxoethyl)-guanosine in RNA + H2O = a guanosine in RNA + glycolate + H(+); Xref=Rhea:RHEA:57292, Rhea:RHEA-COMP:14855, Rhea:RHEA-COMP:14859, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:29805, ChEBI:CHEBI:74269, ChEBI:CHEBI:141581; Evidence={ECO:0000255|HAMAP-Rule:MF_01046}; CATALYTIC ACTIVITY: Reaction=an N(2)-(1-hydroxy-2-oxoethyl)-2'-deoxyguanosine in DNA + H2O = a 2'-deoxyguanosine in DNA + glycolate + H(+); Xref=Rhea:RHEA:57296, Rhea:RHEA-COMP:11367, Rhea:RHEA-COMP:14857, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:29805, ChEBI:CHEBI:85445, ChEBI:CHEBI:141579; Evidence={ECO:0000255|HAMAP-Rule:MF_01046}; | 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 proteins and lactate or glycolate, respectively. Deglycates cysteine, arginine and lysine residues in proteins, and thus reactivates these proteins by reversing glycation by glyoxals. Acts on early glycation intermediates (hemithioacetals and aminocarbinols), preventing the formation of Schiff bases and advanced glycation endproducts (AGE). Also functions as a nucleotide deglycase able to repair glycated guanine in the free nucleotide pool (GTP, GDP, GMP, dGTP) and in DNA and RNA. Is thus involved in a major nucleotide repair system named guanine glycation repair (GG repair), dedicated to reversing methylglyoxal and glyoxal damage via nucleotide sanitization and direct nucleic acid repair. Plays an important role in protecting cells from carbonyl stress. {ECO:0000255|HAMAP-Rule:MF_01046}. | Pseudomonas aeruginosa (strain LESB58) |
B7WN72 | SHANK_CAEEL | MNQEEDTVNLQIFVPELNVRKFLAVTQNDFIWDVKRKLLATLPQALPQAFNYGLFLPPCDGRAGKFLLEDRTIRDYPFTDCVPYLELKYKKRVYKMLNLDEKQLKAMHTKGQLKKFMDYVQQKNNEKVEKMCSQGLDANFHDAQGETPLTLAAGIPNNRAVIVSLIGGGAHVDFRNSEGQTAMHKAAFLSSFENVKTLIELGASPNYRDPIGLTPLYYNMLTADSNDQVAEILLREAADIGVTDMHGNHEIHQACKNGLTKHVEHLLYFGGQIDAENVNGNSPLHVCAVNNRPECARVLLFRGADHLAVNKQGQTALHVSHIVGNPGVADVVQAHNPKSSVPYRGTPQYSTRRRLSSTITRRRSMSQSSICSQDVYRTPQSVRKGPMSAAPSPSPSRSSRTTITPSEYGTMRRSGMDSMRGGGMIAAGHETNIARILVIPRGVKGFGFILRGAKHVAMPLNFEPTAQVPALQFFEGVDMSGMAVRAGLRPGDYLLEIDGIDVRRCSHDEVVEFIQQAGDTITLKVITVDVADMSRGGTIVHRPPTASSRHSLVFTPTPSAIYSSTKASSVYRMRFDTHDAHGVDYYAPNEIRNAYSESRHASVRQRPGSGRRISAAELENLMVRQRVPSVQGSPYQMQYDQESLNGGYSSKKYNSVSDMKRRKGQRNVVASSAGLNRSTFEQAAPTTSTFEYNCSSRSTPQLSRMDSFDSFDDEDEMPAPPPASYISPDLQRDSSMQRSEYSRPFRPTSRPKTPPPPPPMQHQNHQNHQYQQQHPSLPRSASTPQPIQQQQSSIPPPPPPPPPPHCEPTMVHVEFTPPSTSSVPPPPPPLPPISSGAPPPPPPPPPGGLMHVAASAPVLMSNSKGISADALKSVQLKKAEPRETSAASVSNNNNNNNNSTTDFQMDLKNALAKRRSKVAHDVDEDEERESRFEGLSLRETVRENVVERGKGIQNIGIVNKKDSGYTSSRTSLEPSESEEKDHRPHFSLDHSPNVQRVTLISQHLEDNYGQKDNMSVASSSTASSSSTVDLTKPGCFVVPSHVIPPVDYDDDPDSGTGDSDGEIRCSEISFEHKKVDVWSVDDVIGWLSSLHLSEYTPAFRSQRINGRCLRQCDRSRFTQLGVTRIAHRQIIESALRGLLQ | 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 the function of the calcium channel and therefore maintain the Ca(2+) current density (PubMed:28477407). The maintenance of Ca(2+) also allows for the downstream regulation of Ca(2+)-induced expression of genes such as gem-4 (PubMed:28477407). Plays a role in the regulation of the defecation cycle, and this may be in association with the inositol trisphosphate (IP3) receptor itr-1, which in turn mediates periodic calcium release and muscle contractions (PubMed:15013747, PubMed:21191812). Required for normal fertility and pharyngeal pumping (PubMed:21191812). {ECO:0000269|PubMed:15013747, ECO:0000269|PubMed:21191812, ECO:0000269|PubMed:28477407}. | 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:0006357]; response to osmotic stress [GO:0006970]; response to oxidative stress [GO:0006979] | 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 factor binding [GO:0061629]; zinc ion binding [GO:0008270] | 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 downstream of transcription factor elt-1 (PubMed:11259601). Modulates environmentally induced changes in collagen gene expression, including rol-6, sqt-1, lon-3, and dpy-13 (PubMed:32229533). Involved in regulating expression of various genes, including gst-4, sod-3, ugt-9, and col-144 (PubMed:18662544, PubMed:28600327). In response to oxidative stress, required to up-regulate expression of gst-4 mRNA (PubMed:28600327). Regulated by the Insulin/IGF-1-like signaling (IIS) mediated pathway (PubMed:18662544). Plays a role in longevity (PubMed:18662544, PubMed:23262285). May regulate the expression of genes that control sensitivity to osmotic stress, in conjunction with the GATA region-binding transcription factor elt-2 (PubMed:20126308). May form a transcriptional circuit with GATA factors egl-18 and elt-6 (PubMed:18662544). {ECO:0000269|PubMed:11259601, ECO:0000269|PubMed:18662544, ECO:0000269|PubMed:23262285, ECO:0000269|PubMed:28600327, ECO:0000269|PubMed:32229533}. | 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 [GO:0045892]; negative regulation of transcription by RNA polymerase II [GO:0000122] | 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 ectoderm (PPE) acting downstream of the retinoic acid receptor (RAR) signaling. {ECO:0000269|PubMed:19247927, ECO:0000269|PubMed:22354841}. | Xenopus laevis (African clawed frog) |
B7YZU2 | LINT_DROME | MFKWVTPASTATLSRCTLPATTAATTTTTAMAATRTATTTTRTTRPQLLSIALTSLIIIVASFVPTTSGFRSIETNGGGRKLFGGYRITPKHCRATKTLPSSDPRANGPTICMFNHECAQRGGEVVGACMDGFLFGACCQIPPTHELASTLINEAQNAYFQQHQQQTKLQQSAAQSSFESYGEQQQSLSEEQVAQQPSQNIYDQQNLDKVYQQLDSSSSISPPNGAYGDEPQQQEYQSESEQPVRDENAYPTSSSSTEATQSQSSSASVEFEQEPSQPADASNDQTTQKINKQPVQPPNFHVHKHSVTINSPSSPPQNDDFVMQVLSTLPPEHADDHHIVFTTEVPTKITSGLQDQTSSESNSFEEVSSTPAATQKPKPKPTQMPTQKTTQKATQKPTPKPTQKAKPKPVPQLAESMKRPIQQKPQQVAKPKPSPKPAQSTNNHHHNHLILDGGEFTHSDITHPGADADLVEDLQFSTGYGPQPVYAEPPKQQQQQQPAEQSYISSSTSAKRPTTGHNSPTTVSSITTHVDSIESIILQLNNTSHGPSYNVVSQQTPSYGYPGAAVVQTEPAAQNPTFYQENESEKVQESDSQSDYGYTTTVNYESFYDKVSDEQDASAAVSQSAEMPTARPGYGEDVSAVLEDHTMPANGYHDAEAPVAPQTSEFNKMPVMGIAYPVDMSYMEEEGNLPATAAGYGQMSSDSYEASTESTYQKLSTVQTEEPQPTYVRPTTNANKQNRPVASYIGMVTMQHYNPQPGNGDYQAQVPPEVSVSSHTTKVQEQMDETSNGYQQSETTSGYVSPPTAVPAPAQRPQYDAVQGDASSERPVLVTASPRPRPKPSTKRPAVKRPISGESTKKKPQPQPSAGAYNQEKISEHSTRKPVSNGYDKVPESPITHIQIKKPSATQHKEQEQTGYPRPASPAGYEQTTAAAPAPAAPSLNYDKPDAPPSQYDQPSAPSASYDQLAPMPSLNYNEQHASSPGRKPSTAKPISTSYVTGPSTPRPPATVDYHYDNVPPLFMADDKLDAFIQSTAENIVGSTPGNYQPPLVATASTPAYAHRPTSSGSYGHKKPGFVQINGTPKPPRPTVLITPKPTAINLVTYSSLSDDSNKLASSTSSYVTGRPGVQGVSSNDFKDPGYFGSSPVHVAFTQSTTEAVYAVPSDDKPAFPGYFGPTPSYPAFSVPGEKVGQNVMEETYTSPNDFVNFPPVRNPNLNMSAASSAVTSDLDLSTPAFVEDVVLKDKMHTLVHKLVASLQGNFEALADMIEEPGSNKTVATYQAGAGGTAKPVRVVTTRKPVRTATTTRPKVTTKKPVTRVTTKAPNKKTSAVSTTTRKPATRRTTVAAKVTTTTRRPATKKPTRRVSSTVKTTTVSSARPADDEIVDEEDEEDVNPNPSDNEIDQGATLSSYGGANGRKIHSTSRTLPTPNLAFHSPSTECGVRPHVKSGRIVGGKGSTFGAYPWQVLVRESTWLGLFTKNKCGGVLITSRYVITAAHCQPGFLASLVAVMGEFDISGDLESKRSVTKNVKRVIVHRQYDPATFENDLALLELDSPVQFDTHIVPICMPNDVADFTGRMATVTGWGRLKYGGGVPSVLQEVQVPIIENSVCQEMFHTAGHNKKILTSFLCAGYANGQKDSCEGDSGGPLVLQRPDGRYELAGTVSHGIKCAAPYLPGVYMRTTFYKPWLRSITGVK | 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 | MQPSSPNATNYLADNIQISSANLSQTEMVVGRDSADYTAMHSINVGVGNSFLRGDTDIPQESGHSFETPSNMSFTAGQWDTESLPPVDTPDALNKAAGRIRSLLRRMDHETVAYEDMQRNLHYAARVLEAVFIDESREGCNGNCKNLNCSRHSHGRDDQQQDNNNSNRSCSLQEASPGGAGAGVTPGADNQDSIESRTKGVSQAPQTHSGPTGPPSNTSSETIAQPAPKLQPALETVRESVMEESPSKDPGDKGPPPPASTSTLTSQTTTSSSATAEPSAKAAESQAGSAGSSGSCSNPAAVHRQRRLRTPTWARSMSTNKTRLADEDDELSEVQPDAVPPEVREWLASTFTRQMATSRRKSDEKPKFRSVAHAIRAGIFVDRMYRRVSSSALTAFPPDVVRLLKNLDDWTFDVFALTEAASGQVVKYVAYELFNRYGSIHKFKIAPGILEAFLHRVEEGYCRYRNPYHNNLHAVDVMQTIHYCLCNTGLMNWLTDLEIFASLLAALLHDYEHTGTTNNFHVMSGSETALLYNDRAVLENHHASASFRLLREDEYNILSHLSREEFRELRGLVIEMVLGTDMTNHFQQMKAMRQLLTLQEATIDKQKVLSLVLHCCDISHPAKQWGVHHRWTMLLLEEFFRQGDLEKELGLPFSPLCDRNNTLVAESQICFIDFIVEPSMGVMSDMLELILAPIAPMNKSKPATLVEHETTANSTTNSAIVIPNSGITPSMDKPRDHRTEAKTTAAECLARKSVTGTTASKFNIPKPWLTCLVENKRIWKEQAVKDAEARALATAAEEAAAAAAAEAEESKPETETADGEQSEPAAEPADGAAA | 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 metal cations per subunit. Site 2 has a preference for magnesium ions. {ECO:0000250|UniProtKB:Q01064}; | 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 activity [GO:0004117]; metal ion binding [GO:0046872] | 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; Evidence={ECO:0000305|PubMed:15673286}; CATALYTIC ACTIVITY: Reaction=3',5'-cyclic GMP + H2O = GMP + H(+); Xref=Rhea:RHEA:16957, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:57746, ChEBI:CHEBI:58115; Evidence={ECO:0000269|PubMed:15673286}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:16958; Evidence={ECO:0000305|PubMed:15673286}; CATALYTIC ACTIVITY: Reaction=3',5'-cyclic AMP + H2O = AMP + H(+); Xref=Rhea:RHEA:25277, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:58165, ChEBI:CHEBI:456215; Evidence={ECO:0000269|PubMed:15673286}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:25278; Evidence={ECO:0000305|PubMed:15673286}; | 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:20551439}. | Drosophila melanogaster (Fruit fly) |
B7Z0E2 | UNR_DROME | MNTQSKVYRTGEEIYDNLPCDSYFNMNAIRNLGIPTTFPTIGTFTLDSTTLGLQPQGQGPSPQQQQHQQQQQQQQQQHQQNMHHHQHQQQHMQQQQQQQQHQQQHQQQQHQQQQQHQQQQQQQQQHPTIGMFDANEVNDVIQNPPQIGVFQSNSVLTNGAGSGSSIFGSQSSNSSAAAADPSQTTRETGIIEKLLHSYGFIQCCERQARLFFHFSQFSGNIDHLKIGDPVEFEMTYDRRTGKPIASQVSKIAPEVVLSEERVTGTVTTELRTDSANNVLNSSETTGRISYENRGECFFLPYTKDDVEGNVNLRAGDKVSFQIATNQRGNLGACHIRLENPAQPVKYRGVVCSMKESFGFIERADVVKEIFFHFSEAEGNVELRPGDDVEFTIQTRSSASVPPQGREFACNITRLAPGSVIFEDVDSTVYKGQVLKSLDRNNPVRQNNDPLPGRIRYRALDYSEVEVPFGDKDQKGDFTLRHGDWVQFLLATDRRDQLQRATSIALLDETFKVSGEKREQGTIASLKEGFGFLRCVERQARLFFHFTEVLDTSREIDINDEVEFTVIQEPGLAYNNSRLQAIRIKHLPPNSVQFETLVASNIEGCVTREAPKSPIKSQDRVEGGVITYEHADVKKTIMYFLKDCEKPPRIGERVRFDIYMVKRNKECIAVNVQQVSLHQQQQQQQQQLHLNQSNAGANINQNDQLGGLSNGISSSSSNASLQNGYVMHGSPGGSTSSVGSNNPVHLDEFKMENNNHAGSDAGQVYRGFIAVMKENFGFIETLSHDEEVFFHFSNYMGNPNWLELGQEVEYTLARNGNTSVSGNCLPAENVRMLPKNSIPQPAVLETTHNGVVARPLRCINPDQQEYAGLIEILDELRTTVISQHEFGITSLVNKRDLLQKGDLVSFRIDESGRAACVNAVRQKKRATVDSIKGQFGFLNFEVEDGKKLFFHMSEVQGNTVALHPGDTVEFSVVTNQRNGKSSACNVLKINDRPDRLISRLKLNGDDTVPRLILIRAPKGPQGKGFSVLARHPRIPGNLVE | 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 multiprotein complex that mediates X-chromosome dosage compensation (PubMed:19168682, PubMed:25158899). Promotes MSL complex assembly via association with roX1 and roX2 non-coding RNA components of the MSL complex, facilitating the interaction between non-coding RNAs and mle (PubMed:19168682, PubMed:25158899). In females, acts as an inhibitor of dosage compensation together with Sxl by preventing production of msl-2 protein, an essential component of the MSL complex (PubMed:16452508, PubMed:16452509, PubMed:18203923, PubMed:19941818). Specifically binds to the 3'-UTR of msl-2 transcripts, and cooperates with Sxl to prevent translation initiation of msl-2 transcripts (PubMed:16452508, PubMed:16452509, PubMed:18203923, PubMed:19941818). Mechanistically, Sxl and Unr inhibit translation initiation by preventing ribosome recruitment after pAbp-mediated recruitment of the eIF4F complex (PubMed:19941818). {ECO:0000269|PubMed:16452508, ECO:0000269|PubMed:16452509, ECO:0000269|PubMed:18203923, ECO:0000269|PubMed:19168682, ECO:0000269|PubMed:19941818, ECO:0000269|PubMed:25158899}. | 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:19181850, ECO:0000269|PubMed:19240120, ECO:0000269|PubMed:20679394, ECO:0000269|PubMed:26110638}. Note=Localizes to euchromatic telomeres of polytene chromosomes (PubMed:26110638). Telomere localization is not dependent on peo/pendolino (PubMed:26110638). localizes to specific interband regions on chromosomes (PubMed:19240120). Localization to telomeres is dependent on ver/verrocchio and telomere associated cav/HOAP (PubMed:19181850). {ECO:0000269|PubMed:19181850, ECO:0000269|PubMed:19240120, ECO:0000269|PubMed:26110638}. | 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 binds single stranded DNA in a sequence-independent manner, protecting it from degradation (PubMed:27835648). {ECO:0000269|PubMed:19240120, ECO:0000269|PubMed:27835648}. | Drosophila melanogaster (Fruit fly) |
B7ZAQ6 | GPHRA_HUMAN | MSFLIDSSIMITSQILFFGFGWLFFMRQLFKDYEIRQYVVQVIFSVTFAFSCTMFELIIFEILGVLNSSSRYFHWKMNLCVILLILVFMVPFYIGYFIVSNIRLLHKQRLLFSCLLWLTFMYFFWKLGDPFPILSPKHGILSIEQLISRVGVIGVTLMALLSGFGAVNCPYTYMSYFLRNVTDTDILALERRLLQTMDMIISKKKRMAMARRTMFQKGEVHNKPSGFWGMIKSVTTSASGSENLTLIQQEVDALEELSRQLFLETADLYATKERIEYSKTFKGKYFNFLGYFFSIYCVWKIFMATINIVFDRVGKTDPVTRGIEITVNYLGIQFDVKFWSQHISFILVGIIIVTSIRGLLITLTKFFYAISSSKSSNVIVLLLAQIMGMYFVSSVLLIRMSMPLEYRTIITEVLGELQFNFYHRWFDVIFLVSALSSILFLYLAHKQAPEKQMAP | 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) = bromide(out); Xref=Rhea:RHEA:75383, ChEBI:CHEBI:15858; Evidence={ECO:0000269|PubMed:18794847}; CATALYTIC ACTIVITY: Reaction=fluoride(in) = fluoride(out); Xref=Rhea:RHEA:76159, ChEBI:CHEBI:17051; Evidence={ECO:0000269|PubMed:18794847}; | 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 hematopoietic cells (By similarity). {ECO:0000250|UniProtKB:Q8BS95, ECO:0000269|PubMed:18794847}. | Homo sapiens (Human) |
B7ZC96 | KCMA1_DANRE | MSNNINFNKNPDSSVSISKMDVIIPFTPDVPCDNNGQRMWWAFLASSMVTFFGGLFIILLWRTLKYLWTVCCHCNIKNKEAQKVNNPITIQADGTTKTGNEKEEAPASEVGWMTSVKDWAGVMISAQTLTGRVLVVLVFALSIGALGIYFIDSSDPIESCQNFYKDFTLQIDMAFNVFFLLYFGLRFIAANDKLWFWLEVNSVVDFFTVPPVFVSVYLNRSWLGLRFLRALRLIQFSEILQFLNILKTSNSIKLVNLCSIFISTWLTAAGFIHLVENSGDPWENFQNSQPLSYWECVYLLMVTMSTVGYGDVYARTTLGRLFMVFFILGGLAMFASYVPEIIELIGNRKKYGGSYSAVNGRKHIVVCGHITLESVSNFLKDFLHKDRDDVNVEIVFLHNISPNLELEALFKRHFTQVEFYQGSVLNPHDLARVKIESADACLILANKYCADPDAEDASNIMRVISIKNYHPKIRIITQMLQYHNKAHLLNIPSWNWKEGDDAICLAELKAGFIAQSCLAQGLSTMLANLFSMRSYIKIEEDTWQKYYLEGVANEMYTEYLSSAFVGLSFPTVCELCYVKLKLLLIAIEYKSEQRESSILINPGNHVKMQEGTLGFFIASDAKEVKRAFFYCKACHDDITDPKRIKKCGCKRIEDEHPSTLSPKKKQRNGGMRNSPNCSPKMMRHDPLLIPGNEQIESMDANVKRYDSTGMFHWCPSKEIEKVILTRSEASMTVLSGHVVVCIFGDVTSALVGLRNLVMPLRASNFHYHELKPIVFVGSLDYLRREWETLHNFPKVFILPGTPLSRADLRAVNINLCDMCVILSANQNNIDDASLQDKECILASLNIKSMQFDDSIGVLQANSQGFTPPGMDRSSPDNSPVHGLVRQASVTTGSNIPIITELVNDSNVQFLDQDDDDDPDTELYLTQPFACGTAFAVSVLDSLMSATYFNDNILTLIRTLVTGGATPELEALLAEENALRGGYSTPQTLANRDRCRVAQLALYDGPFADLGDGGCYGDLFCKALKTYNMLCFGIYRLRDAHLGAPSQCTKRYVITNPPYEFEMVPTDLIFCLMQFDHNAGQSRASLSHSSHSSHSSSKKSSSVHSIPATNRQNRSSKAREARDKQNATRMNRMGPEKRWFTDEAENAYPRNIQIKPMSTHMANQVNQYKSTSSLIPPIREVEDEC | 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+) concentration and/or depolarize the cell membrane (By similarity). It therefore contributes to repolarization of the membrane potential (By similarity). Involved in determining peripheral auditory sensitivity (PubMed:24803460). {ECO:0000250|UniProtKB:Q12791, ECO:0000269|PubMed:24803460, ECO:0000303|PubMed:22139424}. | Danio rerio (Zebrafish) (Brachydanio rerio) |
B7ZNG0 | KIF7_MOUSE | MGLEAQRLPGAEEAPVRVALRVRPLLPKELLHGHQSCLRVEPERGRITLGRDRHFGFHVVLGEDTGQEAVYQACVQPLLEAFFEGFNATVFAYGQTGSGKTYTMGEASVASLHEDEQGIIPRAMAEAFKLIDENDLLDCLVHVSYLELYKEEFRDLLEVGTASRDIQLREDDRGNVVLCGVKEVDVEGLDEVLSLLEMGNAARHTGATHFNRLSSRSHTVFTVTLEQRGRTPSRLPRPAAGHLLVSKFHFVDLAGSERVLKTGSTGERLKESIQINSTLLALGNVISALGDPQRRGSHIPYRDSKITRILKDSLGGNAKTVMIACVSPSSSDFDETLNTLNYASRAQNIRNRATVNWHPEAERVPEEQAAGARGPPRHRSETRIIHRGRRVPCPAVGSAAVAAGLGAECARCRARTSAAYSLLRELQAEPGLPGAAARKVRDWLCAVEGERSTLSSASGPDSGIESAPAEDQAAQGTSGRKGDEGTQQLLTLQSQVARLEEENRDFLAALEDAMEQYKLQSDRLREQQEEMVELRLRLELAQPGWGAPGLLQGLPPGSFVPRPHTAPLGGAHTHMLGMMPSTCLPGEEVSSEQQVVSGKEVKAEVLAQADKLRSASSTTSEEEGEEEEEEEEEEEEPPRRTLYLRRNGISNWSQRAGLSPGSPPDRKGPEVCPEEPAAAIPAPQAVGSGKVPVQTRQAPAAMASEWRLAQAQQKIRELAINIRMKEELIGELVRTGKAAQALNRQHSQRIRELEQEAERVRAELCEGQRQLRELEGREPQDASERSRLQEFRKRVAAAQSQVQVLKEKKQATERLVSLSAQSETRLQELERNVQLMRRQQGQLQRRLREETEQKRRLETEMNKRQHRVKELELKHEQQQKILKIKTEEIAAFQRKRRSGSNGSVVSLEQQQKIEEQKKWLDQEMEKVLQQRRALEELGEELRKREVILAKKEALMQEKTGLESKRLRSSQALNEDIVRVSSRLEHLEKELSEKSGQLRQGSAQNQQQIRGEIDTLRQEKDSLLKQRLEIDSKLRQGSLLSPEEERTLFQLDEAIEALDAAIEYKNEAITCRQRVLRASASLLSQCEMNLMAKLSYLSSSETRALLCKYFDKVVTLREEQHQQQIAFSELEMQLEEQQRLVYWLEVALERQRLEMDRQLTLQQKEHEQNVQLLLQQGRDHLGEGLADSKRQYEARIHALEKELGRHMWINQELKQKLSAGSTAGQSQGCERRSLCLENRQCLGNEDGLHPAAPEPLWQSSLLEGVSRVWDESRDLVHAPLPLTWKRSSLCSEQGSSEESRVRETTEPPVGRVLPMGEVGLSWNFGPLPKPRWEPRRTSPGMIDVRKNPL | 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 pathway [GO:0045880]; spindle elongation [GO:0051231] | 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 organization of the ciliary tip and control of ciliary localization of SUFU-GLI2 complexes. Required for localization of GLI3 to cilia in response to Shh. Negatively regulates Shh signaling by preventing inappropriate activation of the transcriptional activator GLI2 in the absence of ligand. Positively regulates Shh signaling by preventing the processing of the transcription factor GLI3 into its repressor form. In keratinocytes, promotes the dissociation of SUFU-GLI2 complexes, GLI2 nuclear translocation and Shh signaling activation. Involved in the regulation of epidermal differentiation and chondrocyte development. {ECO:0000269|PubMed:19549984, ECO:0000269|PubMed:19592253, ECO:0000269|PubMed:19666503, ECO:0000269|PubMed:21795282, ECO:0000269|PubMed:23034632, ECO:0000269|PubMed:24952464}. | Mus musculus (Mouse) |
B7ZQJ9 | GT2D1_XENLA | MALAGKQYEGSLNNSRPNLWPSSIPGGKNEIITSLVTALDSMCTALSKLNTEVACIALHEESAFVVGTEKGRCFLNSRKELQADFQRFCIGAHKKDQENEVKRRNRDGIQNIQHVPLGPTSDIYLLRKMVEEIFEVLYSEALGKSNIVPVPYVKVMKEPGSVVVLGLPDGISFRKPAEYDLKSLMLILKHSHNIRFKLRIPTEESIREPKSCSELNSPPTSATKVIPETSQCHRLPIQEHPSSASNFPYSVSQPNQISLEPKQEVHSNMLGTNAVNQMLVQRPSAENNHDLSDCCGQQSPVAGSSLRQNVLASKHLLFSIVHDKTDKWDSFLRETEDINILRECVQILFNSRYAGALGLDHMVPVPYRKIACHPEAVEINGFPDKIPFKRPCTYGVPKLKRILEERHNIHFTIKSMFDQRIFDGTTFTKETTKSDSSSLGEEACSENQKAAALDMLGFPTGSRSEKSSISDECEPGTSSETTGVKLIKLEAEDPDIMQIAVPGTSSETSGVKIIKLESEDPDLIQITVPGTSNETSGVKPKLESEDPDLIQIAVPDRLAECVKNHLAPEDPSYVLDTGKVCDDRPCGVLRNENKHLDGIGDIIRQLRKHVENLFNRKYAKAIGASGPVKVPYAKFLMYPEDLFVLGLPEGVAFRRPNCFGITKLRRILEYSDGIQFVVKRPELISEGLEDCVVGSPGTLGFNDKSNEVILDETNTRPSFQESFDARLSRIDIANTLREQVQVLFNKKYGEALGIKYPVQVPYKRIKNNPGSVIIEGLPPGIPFRKPCTFGSQNLERILAVADKIRFTVTRPFQGLIPRPDDEDANRLGEKVILREQVKELFNEKYGKALGLDQPALIPYKLIRDNPDAVEVRGMPNDIPFRNPNSYDLHRLENILKAQDQIQMVVIKQLEPFPEICSEPPKIKNGNTGPKRKRKRVSEGNSISSASSNCSSSSSSSSNMDPISSAHHVSLVQWPMYMLDYGGLNMQLPGPINY | 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 pathway [GO:0032925]; transcription by RNA polymerase II [GO:0006366] | 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|PubMed:11937490, ECO:0000269|PubMed:16055724, ECO:0000269|PubMed:18922797}. | Xenopus laevis (African clawed frog) |
B7ZR30 | STK10_XENLA | MAFANFRRILRLPNFEKKRLREYEHVRRDVDPNQVWEIIGELGDGAFGKVYKAKNRETGILAAAKVIETKNEEELEDYMVEIEILATCNHHFIVKLLGAFYWEGKLWIMIEFCPGGAVDAVMLELDRGLKEPEIKTICRQMLEALAYLHSMKIIHRDLKAGNVLLTLDGDIKLADFGVSAKNVKTLQRRDSFIGTPYWMAPEVVMCETMKDAPYDYKADIWSLGITLIEMAQIEPPHHELNPMRVLLKIAKSEPPTLSSLSKWSPEFHSFLKTALDKNPETRPSAAQLLEHPFVKKASGNKPLRDLVAEAKAEVLDEIEEQGEAEEEEDSDMLSPKTKGVSQSTHVEIGKDIEREQVGNGIKPHSATSPQKTDSQADNYSQRRNNEVKNCPENGRPDAVNGKPDIIILNPLSSNLEPKRNSTAESYRGEEHSSASSQRQRSAQSAELVPNGSFDSPTRYFTNWSKRDSDSGSNSASESMDISMNLSADLSMNKETGFLSHRENRLHKKTLKRTRRFVVDGVEVSITTSKIIGDDEKKDEEMRFLRRQELRELRLLQKEEHRHQAQLTSKHSFQLEQMSRRFEQEMNSKRKFYDTELETLERHQKQQIVWMEQEHAFRRRDEAKHIKTEQERDHIKFLEQLKLRKKELKAHVEKLPRQQRRETMKVQMDGFAHKKQTEEQQFVNRQKEDLNLAMRVIVLENRKEIYNKEREFLNKKQQLLRDRESVIWELEERHLQERHQLVKQQLKDQYFLQRHELLRKHEKEQEQMQRYNQRMMEQLRLRQQQEKVRLPKNQKAEAKTRMTMFKKSLHISPSGSAAEQRDKIKQFSLQEEKRQKAERLQQQQKHEHQLMEMLAECDCNVRDLLQMQNEKCHLLVEHETQKLKSLDEHHIQLIREWRENIRPRKKAFEDELELKKEAQEMFFRLNEEVAGDPFLSNKPTRFYSFSSPEAS | 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-[protein] = ADP + H(+) + O-phospho-L-threonyl-[protein]; Xref=Rhea:RHEA:46608, Rhea:RHEA-COMP:11060, Rhea:RHEA-COMP:11605, ChEBI:CHEBI:15378, ChEBI:CHEBI:30013, ChEBI:CHEBI:30616, ChEBI:CHEBI:61977, ChEBI:CHEBI:456216; EC=2.7.11.1; | 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 | MNLLDPFMKMTEEQDKCMSGAPSPTMSDDSAGSPCPSGSGSDTENTRPQENTFPKGDQELKKETEDEKFPVCIREAVSQVLKGYDWTLVPMPVRVNGSSKNKPHVKRPMNAFMVWAQAARRKLADQYPHLHNAELSKTLGKLWRLLNEGEKRPFVEEAERLRVQHKKDHPDYKYQPRRRKSVKNGQTEQEDGAEQTHISPNAIFKALQADSPHSSSSMSEVHSPGEHSGQSQGPPTPPTTPKTDIQPGKPDLKREGRPLQENGRQPPHIDFRDVDIGELSSEVISTIETFDVNEFDQYLPPNGHPGVGSTQASYTGSYGISSTPSATTGAGPAWMSKQQQQQPQQHSLSTLNSEQSQSQQRTHIKTEQLSPSHYSDQQQQHSPQQLNYSSFNLQHYSSSYPTITRAQYDYTEHQGSSTYYSHASGQNSGLYSTFSYMNPSQRPLYTPIADTTGVPSIPQTHSPQHWEQPVYTQLTRP | 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 oxidation [GO:0046322]; negative regulation of osteoblast differentiation [GO:0045668]; negative regulation of transcription by RNA polymerase II [GO:0000122]; neural crest formation [GO:0014029]; oligodendrocyte differentiation [GO:0048709]; otic placode formation [GO:0043049]; positive regulation of chondrocyte differentiation [GO:0032332]; positive regulation of DNA-templated transcription [GO:0045893]; positive regulation of transcription by RNA polymerase II [GO:0045944]; response to fatty acid [GO:0070542] | 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 nucleus of vitellogenic oocytes. {ECO:0000250|UniProtKB:Q6F2E7, ECO:0000269|PubMed:11807034}. | 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 central role in successive steps of chondrocyte differentiation (By similarity). Absolutely required for precartilaginous condensation, the first step in chondrogenesis during which skeletal progenitors differentiate into prechondrocytes (By similarity). Together with SOX5 and SOX6, required for overt chondrogenesis when condensed prechondrocytes differentiate into early stage chondrocytes, the second step in chondrogenesis (By similarity). Later, required to direct hypertrophic maturation and block osteoblast differentiation of growth plate chondrocytes: maintains chondrocyte columnar proliferation, delays prehypertrophy and then prevents osteoblastic differentiation of chondrocytes (By similarity). Also required for chondrocyte hypertrophy, both indirectly, by keeping the lineage fate of chondrocytes, and directly, by remaining present in upper hypertrophic cells (By similarity). Low lipid levels are the main nutritional determinant for chondrogenic commitment of skeletal progenitor cells: when lipids levels are low, FOXO transcription factors promote expression of SOX9, which induces chondrogenic commitment and suppresses fatty acid oxidation (By similarity). In addition to cartilage development, also acts as a regulator of proliferation and differentiation in epithelial stem/progenitor cells (By similarity). Involved in development of the cranial neural crest, which is fated to form skeletal elements (PubMed:11807034, PubMed:12812785, PubMed:15464575, PubMed:16256735, PubMed:16943273). Also required for otic placode specification during inner ear development (PubMed:15084460). {ECO:0000250|UniProtKB:Q04887, ECO:0000269|PubMed:11807034, ECO:0000269|PubMed:12812785, ECO:0000269|PubMed:15084460, ECO:0000269|PubMed:15464575, ECO:0000269|PubMed:16256735, ECO:0000269|PubMed:16943273}. | Xenopus laevis (African clawed frog) |
B7ZRU9 | EVI1A_XENLA | MKSEDYSYARMAPDIHEERQYRCEECDQLFESKTELSDHQKYPCVTPHSAFSLVENSFPPSLNDDSDLTEMQHTHECKECDQVFPDMQSLEKHLLSHTEEREYKCDQCPKAFNWKSNLIRHQMSHDTGKHYECENCSKQVFTDPSNLQRHIRSQHVGARAHACSDCGKTFATSSGLKQHKHIHSSVKPFVCEVCHKSYTQFSNLCRHKRMHADCRTQIKCKDCGQMFSTTSSLNKHRRFCEGKNHFAAGGLFGQGISLPGTPAMDKASMISMNHANAGLADYFGASRHTAGLTFPTAPGFPFSFPGLFPSSLYHRPPFIPPASPVKGLPGVEQSSKSQSPHVNQPQVLPATQDILKALSKHPSVDENKALEFITESNLNQRPHEKISDHSESSDLDDVSTPSGSDLETTSGSDLESDIESDKDKLKENGKLYKDKMSPLQSLAALNSKREYNNHSVFSPCLEEQTAVTGAVNDSIKAIASIAEKYFGSTGLVGLPDKKGTTLPYPSMFPLPFFPAFSQSMYTFPDRDVRPVPLKIEPESPKETKKVQKGKTESPFDLTTKRKEEKASPNVPSKSGAPTSSNHDQPLDLSMGSRSRAATTKQTEPRKNHIFNEKKDMDPELPKTSEHCLQHARPAPFFMDPIYRVEKRKPMDPLEILKEKYLRPSPGFLFHPQFPMPDQRTWMSAIENMAEKLESFNALKPEANNLIQSVPSMFNFRASSSALPENLLRKGKERYTCRYCGKIFPRSANLTRHLRTHTGEQPYRCKYCDRSFSISSNLQRHVRNIHNKEKPFKCHLCDRCFGQQTNLDRHLKKHENGNLSGTAASSPHSEIEGTGPILDEKEDSYFNEIRNFIGNSSHNKQSPLNSDERINGSHDKIMLAGQNSDILDDDEDEAILDEDDEESDIAVKVMKEPNTSVMLEKCSVDEYEEGGKSEVNSKVSPSRYDDEDDDDDEEEDFKKSLSALDHIRHFTDSLKMRKMDDGQFNDAELSAFTASHLTDDLKHPLYRKSKSQAYAMMLSLSDQESLHPTTHTSSSMWHNLARAAAESTALHSVSHV | 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 pronephric nephron development [GO:0072196] | 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, ECO:0000269|PubMed:12553426, ECO:0000269|PubMed:15590892, ECO:0000269|PubMed:16627555}. | Xenopus laevis (African clawed frog) |
B7ZSG3 | WT1A_XENLA | MGSDVRDMNLLPPVSSLSGNSSCNMPVSSSAQWAPVLDFPPGAPYSSLTPHSFIKQEPTWNPDPHEDQCLSAFTVHFSGQFTGTAGACRYGPFGAPTPSQATTGQARMFSNAPYLSNCLDNQQGMRNQGYSAVAFDGTPSYGHTPSHHTSQFTNHSFKHEDPLSQQTSLGEQQYSVPPPVYGCHTPTDTCTGSQALLLRTPYNSDNLYPMTSQLDCMTWNQMNLGSSLKSHGTSYENDSHSSPMLYNCGGQYRIHTHGVFRGIQDVRRVPGVTPAIVRSTEANEKRPFMCAYPGCNKRYFKLSHLQMHSRKHTGEKPYQCDFKDCERRFSRSDQLKRHQRRHTGIKPFQCKTCQRKFSRSDHLKTHTRTHTGKTSEKPFSCRWPSCQKKFARSDELVRHHNMHQRNMTKLQLAL | 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]; regulation of transcription by RNA polymerase II [GO:0006357]; specification of pronephric proximal tubule identity [GO:0039004]; Wnt signaling pathway [GO:0016055] | 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 [GO:0043565]; zinc ion binding [GO:0008270] | 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-signaling during embryonic development. Function may be isoform-specific: the isoform containing the KTS motif is less effective in inhibiting wnt signaling. {ECO:0000250|UniProtKB:P19544, ECO:0000269|PubMed:16574097, ECO:0000269|PubMed:16818449, ECO:0000269|PubMed:19549856, ECO:0000269|PubMed:9758706}. | Xenopus laevis (African clawed frog) |
B7ZSK1 | NMDE1_XENLA | MGMFVLLLYTFLYAGDLGHGAEKSFPVLNIAVILGRTRYITERDIRSLWTRDMSLDFDVNVVTLLVNQTDPKSIITHVCDLMSGTKIHGVVFGDDTDQEAIAQILDFVSSQTFIPILGIHGGSSMIMADKDEMSTFFQFGASIKQQATVMLNIMEEYDWHVFSVITSNFPGYRDFISFIKTTVDNSFVGWEVQNYITLDTSYTDAQTLTQLKKIHSSVILLYCSKDEATYIFEEARSLGLMGYGFVWIVPSLVTGNTDIIPYEFPSGLVSVSYDDWDYGIEARVRDGLGIITTAASAMLEKHSVIPEAKTSCYGQNERNDPPLHTLHNFMINVTWDGKDLSFTEDGYQANPKLVVLLLNMEREWEKVGKWENKSLNMKYPVWPRITASLDSDHDDNHLSIVTLEEAPFVIVENIDYLTGTCVRNTVPCRKYFRLNNSTTEGTSVKKCCKGFCIDILKKLSKTVKFTYDLYLVTNGKHGKKIKNVWNGMIGEVVYKRAVMAVGSLTINEERSVAVDFSVPFVETGISVMVSRSNGTVSPSAFLEPFSASVWVMMFVMLLLVSAMAVFIFEYFSPVGYNRNLAQGKDPHGPSFTIGKAVWLLWGLVFNNSVPVQNPKGTTSKIIVSIWAFFAVIFLASYTANLAAFMIQEEFVDQVTGLSDNKFQRPHDYSPPFRFGTVPNGSTERNIRNNYPDMHQYMVKFHQKGVQDALVSLKTGKLDAFIYDAAVLNYMAGRDEGCKLVTIGSGYIFATTGYGIALQKGSRWKRPIDLALLQFVGDGEMEELEKLWLTGICHTEKNEVMSSQLDIDNMAGVFYMLAAAMALSLITFVWEHLFYWKLRFCFTGVCTGTPGLLFSISRGIYSCIHGVHIEEKKKSPDFSFTASQTNMLKLLRASKNIANLSNLNQSQCNSPKRTSDYIQRNSLLTDMVLDKGNLTYSDNRPFQQKDIYSENTYDLAMLSANCPKDNLNNYVFQGQHPLTLNESNPNTVEVAVSAEAKVNTRPRQLWKKSVETLRQTQGSVNENGTEESKSSIKNQRFLPEDGHFSDVSEASSRATCHIDSENNNKHRKSKDNLKKRPVSAKYARECSEVELSYLKIKHGPNRDKVYTIDGDKEPSFIMDQPKYSENSPDQDDEDYPDVYQDHNDNYRKTEPLQSDRTPLHSEGRLPNNDIQYKLFSKHYNLKEKNTSMSDANDRHRQNSTHCRSCLSNMPNYTGHYTARSPYKCDDCLHTGKLYDIDEDQMLHEAANSMHSEDFYEHNWLENNALHFQKKNKLRINRQHSCDNINKPREHDLGRPPRSLSLKEKERYIQENPFAKFVIVPPEKLLGNNASLFTDSLKDSKRSKSLYPDNSSDNPFLHSYQETQKLSHGRSSSDIYKQSSLPKARNDNYLRSSIKSTTSYSSRDGRVPDDMCVSEYALPYVTSNNSVYSAPRVVNSCSNRRVFKKMPSLESDV | 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, plus membrane depolarization to eliminate channel inhibition by Mg(2+) (PubMed:28232581). Sensitivity to glutamate and channel kinetics depend on the subunit composition (Probable). Plays a role in dendritic branching in brain neurons and in synaptic plasticity (PubMed:18216193). Participates in the synaptic plasticity regulation through activation by the L-glutamate releaseed by BEST1, into the synaptic cleft, upon F2R/PAR-1 activation in astrocyte (By similarity). {ECO:0000250|UniProtKB:P35436, ECO:0000269|PubMed:18216193, ECO:0000269|PubMed:28232581, ECO:0000305}. | Xenopus laevis (African clawed frog) |
B7ZWR6 | OEP61_ARATH | MFNGLMDPEMIRLAQDQMSRMTPADFARIQQQMMSNPDLMNMATESMKNMRPEDLKQAAEQLKHTRPEDMAEISEKMAKASPEDIAAMRAHADAQFTYQINAAQMLKKQGNELHSRGNFSDAAEKYLRAKNNLKEIPSSKGGAILLACSLNLMSCYLKTNQHEECIKEGSEVLGYDARNVKALYRRGQAYRDLGLFEDAVSDLSKAHEVSPEDETIADVLRDVKERLAVEGPGKASRGVVIEDITEENNVTSGENKKPSKEANGHAQGVKTDVDGLQALRDNPEAIRTFQNFISKTDPDTLAALSGGKAGDMSPDMFKTASSMIGKMSPEEIQKMVQTASSFKGDNPFAPTAPSTENGFTPTPDMLKLASDMMGKMSPEERERMFNMASSLKANAPASTSYGNAEASEPRESLGASGSSSGNSFVAPRSGFEPSIPSAPPADLQEQMRNQMKDPAMRQMFTSMIKNMNPEMMASMSEQFGMKLSQEDAAKAQQAMASLSPDALEKMMRWADRAQTGMEKAKKAKKWLFGKGGLIFAILMLVLAMVLHRLGYIGN | 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, but not with mitochondrial precursors. Able to select precursors for delivery to the chloroplast translocase independently of Hsp70. {ECO:0000269|PubMed:21612577, ECO:0000269|PubMed:22899711}. | Arabidopsis thaliana (Mouse-ear cress) |
B8A4F0 | ZD16A_DANRE | MHPCSSVLHLLLRCMRGCCRHTRSRVPRRLRRHVSYIRLIFKSLYFNSLTNSDVVTDSILEPVFWMVEVVTRWFGMVFVFLVVALTSSVVFIAYFCLLPLVLHTYSPGWMIWHICYGHWNLVMIVFHYYKATKTPPGYPPKMKTDVPFVSVCKKCIIPKPARSHHCGICKTCILKMDHHCPWLNNCVGHFNHRYFFSFCLFLTLGCMYCSVSGRHLFIDAYNTIDQLKHLEAEKQGVPVTGIGLLIGIVPSAGVAGKAVQVAQEVSQPPYTYKDRMFHKSVIYMWVLTSTVSVALGALTLWHALLITRGETSIERHINGKEAKRLAKRGRVYRNPFSYGKLNNWKVFFGVEKRSHWLTRVLLPSGHAPYGDGLTWDIYPLKKDMMPV | 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:0018345]; telencephalon development [GO:0021537] | 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 (PubMed:26663717). {ECO:0000250|UniProtKB:Q969W1, ECO:0000250|UniProtKB:Q9ESG8, ECO:0000269|PubMed:26663717}. | Danio rerio (Zebrafish) (Brachydanio rerio) |
B8A4W9 | LOX3B_DANRE | MELHQWCRHIIVFLLNVWIPSCFAQTTPPARSSPTPTPQTADNPDSLKFRLSGFPRKHNEGRIEVFYKGEWGTICDDDFSLANAHVLCRQLGFVSATGWTHSAKYGKGAGKIWLDNVQCSGSERSVSVCKSRGWGNSDCTHDEDAGVICKDERLPGFVDSNVIEVQVDENRVEEVRLRPVFTTATKRMPVTEGVVEVKNKDGWAQICDIGWTPKNTHVVCGMMGFPHEKKVNKNFYKLYAERQKNFFLVHSVACLGTEVHLAACPLEFNYGNATESCPGGMPAVVSCVPGPLYTQSPTMKKKLKMPPTTRLKGGAKYGEGRVEVLKGSEWGTVCDDRWNLVSASVVCREMGFGSAKEALTGASMGKGLGPIHMNEVQCTGNERSLWSCRYKNITAEDCKHTEDASVRCNVPYMGYEKTVRILGGRTRYEGRVEVLHREADGTLRWGLICGEGWGTQEAMVLCRQLGLGYANHGLQVRLSGGRSPYEGRVEVRVGQRWGSVCSEGWSTKEAMVLCRQLGLGFSMHAITETWYWDSSNVTDMVMSGVKCTGDEMSISQCQHHRTVNCQKAAARFAAGVICSETASDLVLNAPLVQQTTYIEDRPLHMLYCAAEEDCLSKSAASANWPYGHRRLLRFSSQIHNIGRADFRPKAGRHSWVWHACHGHYHSMDIFTHYDLMSANGTKVAEGHKASFCLEDTDCDEGVSKRYKCANFGEQGITVGCWDLYRHDIDCQWIDITDVKPGNYILQVVINPNYEVSESDFTNNAMKCNCKYDGHRIWVHNCHIGDAFSEEAEKKFEKYPGQLNNQIS | 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]; positive regulation of integrin-mediated signaling pathway [GO:2001046]; roof of mouth development [GO:0060021]; somite development [GO:0061053]; spinal cord development [GO:0021510] | 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 localize in the extracellular medium. However, the intracellular location is clearly reported and at least another protein of the family (loxl2) also has intracellular and extracellular localization despite the presence of a signal sequence. {ECO:0000250|UniProtKB:P58215}. | 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:0000250|UniProtKB:P58215}; CATALYTIC ACTIVITY: Reaction=H2O + N(6)-acetyl-L-lysyl-[protein] + O2 = (S)-2-amino-6-oxohexanoyl-[protein] + acetamide + H2O2; Xref=Rhea:RHEA:51648, Rhea:RHEA-COMP:10731, Rhea:RHEA-COMP:12448, ChEBI:CHEBI:15377, ChEBI:CHEBI:15379, ChEBI:CHEBI:16240, ChEBI:CHEBI:27856, ChEBI:CHEBI:61930, ChEBI:CHEBI:131803; Evidence={ECO:0000250|UniProtKB:P58215}; | 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 cross-links between collagens and elastin (By similarity). Can mediate oxidation of lysine residues that are acetylated (By similarity). Also able to catalyze deacetylation of lysine residues (By similarity). Required for maturation of neural crest derived cartilage elements (PubMed:21244857). {ECO:0000250|UniProtKB:P58215, ECO:0000250|UniProtKB:Q9Z175, ECO:0000269|PubMed:21244857}. | Danio rerio (Zebrafish) (Brachydanio rerio) |
B8AL97 | CUCIN_ORYSI | MAKKKTSSSMARSQLAALLISLCFLSLASNAVGWSRRGEREEEDERRRHGGEGGRPYHFGEESFRHWTRTRHGRFSVLERFPDEQVVGAAVGGYRVAVLEAAPRAFLQPSHYDADEVFYVKEGEGVIVLLREGRKESFCVREGDAMVIPAGAIVYSANTHSSKWFRVVMLLNPVSTPGHFEEYFPVGGDRPESFFSAFSDDVLQAAFNTRREELEKVFERQREGGEITTAPEEQIRELSKSCSRGGGGGSGSEWEIKPSSLTGKSPYFSNNHGKLFELTGDECRHLKKLDLQIGLANITRGSMIAPNYNTRATKLAVVLQGSGYFEMACPHVSGGGSSERREREREHGRRREEEQGEEEHGERGEKARRYHKVRAQVREGSVIVIPASHPATIVASEGESLAVVCFFVGANHDEKVFLAGRNSPLRQLDDPAKKLVFGGSAAREADRVLAAQPEQILLRGPHGRGSVSDM | 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:0000269|PubMed:27064905, ECO:0000305}. | Oryza sativa subsp. indica (Rice) |
B8ANW0 | YUC8_ORYSI | MQGQQKQNAGGGGGDNASPCIVLDGPIIVGAGPSGLAVAATLRQHGAPFTVVERSGGVADLWTNRTYDRLRLHLPKVFCELPHVAFPPDFPTYPTKHDFLRYLHSYAARFAIAPLLRRTVTRAWYDHPASLWRVTTTTTSSSATSVITEYASPWLVVASGENAEVVVPKVKGRERFAGEALHSSEYRSGERFRGMRVLVVGCGNSGMEMCLDLCEHGAMPFMSVRSGVHVLPREMFGASTFGIAMKLLRWLPIKMVDRFLLLVARMVLGDTEKYGLKRPKLGPLEIKNITGKSPVLDVGAWSLIKSGNIKIVPEVESFSGNGARFVDGNEMAFDAVIFATGYRSNVPSWLQEDGELFTEEGKLRSSGSSSEWRWRGPNGLYCVGFSGRGLLGAGADALRAAADIAGRWQETQQAAANISSV | 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:0000250|UniProtKB:Q10RE2}; | 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 regulation of lateral leaf growth (Ref.3). Required for maintaining water homeostasis and an appropriate root to shoot ratio (By similarity). Required for the inhibition of root growth by ethylene in etiolated seedlings (By similarity). Functions downstream of the ethylene-response transcription factor EIL1 (By similarity). {ECO:0000250|UniProtKB:Q10RE2, ECO:0000269|PubMed:24371168, ECO:0000269|Ref.3}. | Oryza sativa subsp. indica (Rice) |
B8AVJ9 | APL25_ORYSI | MWDLNDSPAAEAAPPPLSPSADDSGASSSSAAAVVEIPDDADDDSAAVVVVTRQFFPPAVPGGGGDPAPGNARAGWLRLAGAAPPVAATGPAASAAVSKKSRRGPRSRSSQYRGVTFYRRTGRWESHIWDCGKQVYLGGFDTAHAAARAYDRAAIKFRGVEADINFSLEDYEDDLKQMSNLTKEEFVHVLRRQSTGFPRGSSKYRGVTLHKCGRWEARMGQFLGKKYVYLGLFDTEEEAARAYDRAAIKCNGKDAVTNFDPSIYAGEFEPPAAATGDAAEHNLDLSLGSSAGSKRGNVDGGGDDEITGGGGGGTGSDQRVPMAFDLDWQTAAARSTKAKFDQNSNHPQMPPVLQVTHLPFSPRHHHQFLSNGDPGTAGGLSLTIGAGMAGHWPPQQQQGWGNAGGMSWPLPPHPPPPPTNAAAAATATAAAASSRFPPYIATQASTWLQKNGFHSLTRPT | 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:22408071}. | Oryza sativa subsp. indica (Rice) |
B8B183 | APO1_ORYSI | MMNPRRLPPLPSSTSSASAADDMDPRVWRRLPQPLVDRVLACLPTPSFLRLRAACRRFYHLLFSSPFLHSHLLLSPHLPFFAFVVPAAGHLLLLDPTATASWSRLPLPLPPVAGGPAAFSPAAASAGLLAFLSDASGHKTLLLANPITRLLAALPISPTPRLSPTVGLAAGPTSIIAVVAGDDLVSPFAVKNISADTFVADAASVPPSGFWAPSSLLPRLSSLDPGAGMAFASGRFYCMSSSPFAVLVFDVAENVWSKVQPPMRRFLRSPALVELGGGREGAARVALVSAVEKSRLSVPRSVRLWTLRGGGGGGGGGAWTEVARMPPEVHAQFAAAEGGRGFECAAHGDYVVLAPRGPVAQAPTSALVFDSRRDEWRWAPPCPYVVVAHHGGAGAAGFRVFAYEPRLATPAIGLLDATAPVALHGMHDG | 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]; regulation of vasculature development [GO:1901342]; response to ozone [GO:0010193] | 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 in an APO2-dependent manner (By similarity). Promotes spikelet formation by suppressing the precocious conversion of inflorescence meristems to spikelet meristems, probably via a positive regulation of class-C floral homeotic genes, but not of class-B genes, and through the control of cell proliferation in meristems (PubMed:21119645). Mediates culm development and strength/diameter enhancement at internodes (PubMed:21119645). Required for the regulation of the plastochron, floral organ identity, and floral determinacy (By similarity). Controls the number of primary rachis branches (PRBs) (PubMed:20151298). May trigger the formation of vascular bundle systems which, consequently, promote carbohydrate translocation to panicles (PubMed:20151298). Involved in ozone-induced grain yield regulation (PubMed:25923431). {ECO:0000250|UniProtKB:Q655Y0, ECO:0000250|UniProtKB:Q8LEA8, ECO:0000269|PubMed:20151298, ECO:0000269|PubMed:21119645, ECO:0000269|PubMed:25923431}. | Oryza sativa subsp. indica (Rice) |
B8B2R4 | NAP1A_ORYSI | MGGDKENLDLSDLNASLPAAAAALSAEDRAGLVNALKDKLQSLAGQHTDVLEALSPNVRKRVEYLREIQGQHDEIELKFFEERAALEAKYQKLYEPLYTKRYNIVNGVVEVDGGNDEPASENAAEFKDADAKGVPDFWLTAMKTNEVLSEEIQERDEPALKYLKDIKWARIDDPKGFKLDFFFDTNPFFKNSVLTKTYHMVDEDEPILEKAIGTEIEWYPGKNLTQKILKKKPKKGSKNAKPITKTEVCESFFNFFSPPQVPDDDEDIDEDTADELQGQMEHDYDIGTTIRDKIIPHAVSWFTGEAVQAEDFDDMEDDEEDDEDDDEDEEEEEDEDEDEDDEEEKSKPKKKSAGKPKLPSKGGAQGGADQPADCKQQ | 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 | MAAPRWAVWAVLLLRLLVPAARVLANMEGDALHSLRTNLVDPNNVLQSWDPTLVNPCTWFHVTCNNDNSVIRVDLGNAALSGTLVPQLGQLKNLQYLELYSNNISGTIPSELGNLTNLVSLDLYLNNFTGPIPDSLGNLLKLRFLRLNNNSLSGSIPKSLTAITALQVLDLSNNNLSGEVPSTGSFSLFTPISFANNPSLCGPGTTKPCPGAPPFSPPPPYNPPTPVQSPGSSSSTGAIAGGVAAGAALLFAIPAIGFAWYRRRKPQEHFFDVPAEEDPEVHLGQLKRFSLRELQVATDTFSNKNILGRGGFGKVYKGRLADGSLVAVKRLKEERTPGGELQFQTEVEMISMAVHRNLLRLRGFCMTPTERLLVYPYMANGSVASRLRERPPSEPPLDWRTRRRIALGSARGLSYLHDHCDPKIIHRDVKAANILLDEDFEAVVGDFGLAKLMDYKDTHVTTAVRGTIGHIAPEYLSTGKSSEKTDVFGYGIMLLELITGQRAFDLARLANDDDVMLLDWVKGLLKEKRLEMLVDPDLQSNYIDVEVESLIQVALLCTQGSPTERPKMAEVVRMLEGDGLAERWEEWQKIEVVRQEVELGPHRNSEWIVDSTDNLHAVELSGPR | 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: Reaction=ATP + L-threonyl-[protein] = ADP + H(+) + O-phospho-L-threonyl-[protein]; Xref=Rhea:RHEA:46608, Rhea:RHEA-COMP:11060, Rhea:RHEA-COMP:11605, ChEBI:CHEBI:15378, ChEBI:CHEBI:30013, ChEBI:CHEBI:30616, ChEBI:CHEBI:61977, ChEBI:CHEBI:456216; EC=2.7.11.1; Evidence={ECO:0000305}; | 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 plasma membrane a receptor complex with BRI1 which is activated in response to brassinolide. Phosphorylates BRI1. Required for normal plant growth and leaf development. Possesses kinase activity in vitro. {ECO:0000250|UniProtKB:Q6Z4U4}. | Oryza sativa subsp. indica (Rice) |
B8CH91 | FADB_SHEPW | MIYQSPTIEVELLEDNIAHLCFNAQGSVNKFDRETIDSLNAALDSIKQNNSIKGLMLTSAKPAFIVGADITEFLGLFAEEDAVLLSWLEEANVVFNKLEDLPFPTISAINGFALGAGCETILATDFRVADTTARIGLPETKLGIIPGFGGTVRLPRVVGTDNALEWITSGKDQRPEAALNVGAIDALVAPEQLQSAALKMLKDAIAEKLDWQTRRAKKLAPLTLPKLEAMMSFATAKGMVFKVAGKHYPAPMAVVSVIEKAAQLDRAGALKVEHQAFLKLAKTEVAQSLIGIFLNDQLVKGKAKKAGKLAKKVNSAAVLGAGIMGGGIAYQSASKGTPIVMKDIAQPALDLGLGEASKLLAAQVKRGRSNPAKMAAVLNNITPALDYAPVKAADVVVEAVVEHPKVKSMVLAEVEEHVSEDAIITSNTSTISINLLAKSLKKPERFCGMHFFNPVHKMPLVEVIRGEHSSDETVASVVAYASKMGKTPIVVNDCPGFFVNRVLFPYFAGFSGLLADGADFAAIDKVMEKQFGWPMGPAYLLDVVGLDTGHHAQAVMAEGFPERMGKTGKDAIDVMFEAERFGQKNNKGFYQYSVDRRGKPKKDLDPTSYELLQGEFGERKAFESDEIIARTMIPMIIETVRCLEEGIIASPAEADMGLVYGLGFPPFRGGVFRYLDTMGVANFVALADKYAHLGGLYQVTDAMRELAANNGSYYQQA | 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-CoA = a (2E)-enoyl-CoA + H2O; Xref=Rhea:RHEA:16105, ChEBI:CHEBI:15377, ChEBI:CHEBI:57318, ChEBI:CHEBI:58856; EC=4.2.1.17; Evidence={ECO:0000255|HAMAP-Rule:MF_01621}; CATALYTIC ACTIVITY: Reaction=a 4-saturated-(3S)-3-hydroxyacyl-CoA = a (3E)-enoyl-CoA + H2O; Xref=Rhea:RHEA:20724, ChEBI:CHEBI:15377, ChEBI:CHEBI:58521, ChEBI:CHEBI:137480; EC=4.2.1.17; Evidence={ECO:0000255|HAMAP-Rule:MF_01621}; CATALYTIC ACTIVITY: Reaction=(3S)-3-hydroxybutanoyl-CoA = (3R)-3-hydroxybutanoyl-CoA; Xref=Rhea:RHEA:21760, ChEBI:CHEBI:57315, ChEBI:CHEBI:57316; EC=5.1.2.3; Evidence={ECO:0000255|HAMAP-Rule:MF_01621}; CATALYTIC ACTIVITY: Reaction=a (3Z)-enoyl-CoA = a 4-saturated (2E)-enoyl-CoA; Xref=Rhea:RHEA:45900, ChEBI:CHEBI:85097, ChEBI:CHEBI:85489; EC=5.3.3.8; Evidence={ECO:0000255|HAMAP-Rule:MF_01621}; CATALYTIC ACTIVITY: Reaction=a (3E)-enoyl-CoA = a 4-saturated (2E)-enoyl-CoA; Xref=Rhea:RHEA:45228, ChEBI:CHEBI:58521, ChEBI:CHEBI:85097; EC=5.3.3.8; Evidence={ECO:0000255|HAMAP-Rule:MF_01621}; | 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 | MTRVAIIGAGPSGLAQLRAFQSAGKKGAAIPELVCFEKQSDWGGLWNYTWRTGVDEYGEPVHGSMYRYLWSNGPKECLEFADYSFEEHFGRPIPSYPPRAVLHDYIMGRVEKSDVRKFVRFSTVVRWIDFDETTQLFTVTVKDLKKDELYSETFDYVVVASGHFSTPNVPHFPGIEVFPGRVLHAHDFRDANEFVGKNLLVVGSSYSAEDIASQCYKYGAKSITFSYRSKPLNFDWPECFTVKPLLTKLTGKTAHFKDGSEAVVDAVLLCTGYLHHFPFLADNLRLKTNNRLYPAGLYKGIFWQDNPKLIYLGMQDQYFTFNMFDAQAWYARDVILGRIKLPAAEERQADIDHWRGLEEKLETAFDGIDFQTEYMRDLIPATDYPMFDLDKVAALFKEWEEDKVKSIMGYRDNSYVSIMTGNKAPPHHTKWMEALDDSFDAFQNRPEAAAE | 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-to-right; Xref=Rhea:RHEA:31980; Evidence={ECO:0000269|PubMed:22006322}; | 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 for methimazole {ECO:0000269|PubMed:22006322}; KM=35.7 uM for dimethylaniline {ECO:0000269|PubMed:22006322}; Vmax=29.4 nmol/min/mg enzyme with TMA as substrate {ECO:0000269|PubMed:22006322}; Vmax=6.9 nmol/min/mg enzyme with DMA as substrate {ECO:0000269|PubMed:22006322}; Vmax=34.6 nmol/min/mg enzyme with DMS as substrate {ECO:0000269|PubMed:22006322}; Vmax=4.8 nmol/min/mg enzyme with DMSO as substrate {ECO:0000269|PubMed:22006322}; Vmax=76.2 nmol/min/mg enzyme with cysteamine as substrate {ECO:0000269|PubMed:22006322}; Vmax=14.4 nmol/min/mg enzyme with methimazole as substrate {ECO:0000269|PubMed:22006322}; Vmax=29.2 nmol/min/mg enzyme with dimethylaniline as substrate {ECO:0000269|PubMed:22006322}; | 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, methimazole and dimethylaniline (PubMed:22006322). {ECO:0000269|PubMed:22006322}. | Methylocella silvestris (strain DSM 15510 / CIP 108128 / LMG 27833 / NCIMB 13906 / BL2) |
B8GYI7 | OBG_CAUVN | MKFLDQCKIYIRSGNGGGGSVSFRREKYIEYGGPDGGDGGRGGDVWIEAVEGLNTLIDYRYQQHFKAGTGVHGMGRARHGAAGEDVVLKVPVGTEVLEEDKETLIADLDHAGMRLLLAKGGNGGWGNLHFKGPVNQAPKYANPGQEGEERWIWLRLKLIADVGLVGLPNAGKSTFLAAASAAKPKIADYPFTTLTPNLGVVDLSSSERFVLADIPGLIEGASEGAGLGTRFLGHVERSATLIHLIDATQDDVAGAYETIRGELEAYGDELADKAEILALNKIDALDEETLAEKVAELEAVSGIKPRLVSGVSGQGVTELLRAAYKQVRIRRGDLEEEIDDDEDHVDETPGGWTP | 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-functional in vivo but which retains nucleotide binding and GTPase activity. Required for cell cycle progression from G1 to S phase and for DNA replication. {ECO:0000269|PubMed:15554976}. | Caulobacter vibrioides (strain NA1000 / CB15N) (Caulobacter crescentus) |
B8GZM2 | PLED_CAUVN | MSARILVVDDIEANVRLLEAKLTAEYYEVSTAMDGPTALAMAARDLPDIILLDVMMPGMDGFTVCRKLKDDPTTRHIPVVLITALDGRGDRIQGLESGASDFLTKPIDDVMLFARVRSLTRFKLVIDELRQREASGRRMGVIAGAAARLDGLGGRVLIVDDNERQAQRVAAELGVEHRPVIESDPEKAKISAGGPVDLVIVNAAAKNFDGLRFTAALRSEERTRQLPVLAMVDPDDRGRMVKALEIGVNDILSRPIDPQELSARVKTQIQRKRYTDYLRNNLDHSLELAVTDQLTGLHNRRYMTGQLDSLVKRATLGGDPVSALLIDIDFFKKINDTFGHDIGDEVLREFALRLASNVRAIDLPCRYGGEEFVVIMPDTALADALRIAERIRMHVSGSPFTVAHGREMLNVTISIGVSATAGEGDTPEALLKRADEGVYQAKASGRNAVVGKAA | 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 messenger. {ECO:0000269|PubMed:15075296}. | Caulobacter vibrioides (strain NA1000 / CB15N) (Caulobacter crescentus) |
B8H444 | FTSH_CAUVN | MNFRNLAIWLVIVAVLGGVFVVSQNSRTKSSSEISYSQLLKDVDAGKIKSAEIAGQTVLAKTADNKTLTVNAPMNSEELVNRMVAKNADVKFKSGSISFLAILVQLLPILLVVGVWLFLMRQMQGGAKGAMGFGKSKARLLTENKNRITFEDVAGVDEAKEELQEVVDFLKDPAKFQRLGGKIPKGALLVGPPGTGKTLIARAVAGEAGVPFFTISGSDFVEMFVGVGASRVRDMFEQAKKNAPCIIFIDEIDAVGRHRGAGLGGGNDEREQTLNQLLVEMDGFEANEGIILIAATNRPDVLDPALLRPGRFDRQVVVPNPDVAGREKIIRVHMKNVPLAADVDVKTLARGTPGFSGADLANLVNEAALMAARKNRRMVTMQDFEQAKDKVMMGAERRSMAMNEEEKKLTAYHEGGHAIVALNVPLADPVHKATIVPRGRALGMVMQLPEGDRYSMKYQQMTSRLAIMMGGRVAEEIIFGKENITSGASSDIKAATDLARNMVTRWGYSDILGTVAYGDNQDEVFLGHSVARTQNVSEETARLIDSEVKRLVQYGLDEARRILTDKIDDLHTLGKALLEYETLSGEEIADILKGIPPKREEEEAATAVIAPSLVPLSPGAGASVTA | 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 sigma-32 is a substrate for FtsH. May play a role in the general stress response, as overexpression leads to improved resistance to salt stress. | Caulobacter vibrioides (strain NA1000 / CB15N) (Caulobacter crescentus) |
B8JK39 | ITA9_MOUSE | MGGPAAARTGAGGLRALLLALVAAGVPAGAYNLDAQRPVRFQGPSGSFFGYAVLEHFHDNTRWVLVGAPKADSKYSTSVKSPGAVFKCRVHTNPDRRCTELDMARGRTRGAPCGKTCRGDRDDEWMGVSLARQPRADGRVLACAHRWKNIYYEADHILPHGFCYLIPSNLQAKGKVLIPCYEEYKKKYGEEHGSCQAGIAGFFTEELVVMGAPGSFYWAGTLKVLNLTDNTYFKLNDEAIMNRRYTYLGYAVTAGHFSHPSITDVVGGAPQDEGIGKVYIFRADRRSGTLIKIFQASGKKMGSYFGSSLCAVDLNMDGLSDLLVGAPMFSEIRDEGQVTVYLNQGHGALEEQLTLTGDAAYNAHFGESIANLGDIDDDGFPDVAVGAPKEEDFAGAVYIYHGDANGIVPKYSMKLSGRRLNPTLRMFGQSISGGIDMDGNGYPDVTIGAFLSDSVVLLRARPVITVDVSIFLPGSINITAPQCHDGQQPVNCLNVTVCFRFHGKNVPGEIGLNYNLTADVAQKEKGQLPRVYFVLFGETAGQVSERLQLSHMDEVCHHYVAHVKRRVQDVISPIVFEAAYSLDEHVMGEEDRELPDLTPVLRWKKGQRISQKNQTVFERNCQSEDCAADLQLRGKLLLSSVDEKTPHLALGAVKNISLNISISNLGDDAYDANVSFNVSRELFFINMWQKEEMGISCELLESDFLKCSVGFPFMRSKSKYEFSVIFDTSHLSGEEEILSFIVTAQSGNLERSEALHDNTLTLTVPLVHEVDTSITGIVSPTSFVYGESVDASNFIQLDDQECHFQPVNITLQVYNMGPSTLPGSSVSISFPSRLSPGGAEMFQVQDMVVSQEKGNCSLQRNPTPCIIPQEQENIFHTIFAFFSKSGRKVLDCEKPGSFCLTLHCNLSALPKEESRTINLYMLLNTEILKKDSSSVIQFMARAKVKVEPALRVVEIANGNPEETLVVFEALHNLEPRGYVVGWIIAISLLVGILIFLLLAVLLWKMGFFRRRYKEIIEAEKNRKENEDGWDWVQKNQ | 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 voltage-gated channel Ca(2+) influx and ROCK-mediated calcium sensitivity in vascular smooth muscle cells via its interaction with SVEP1, thereby inhibiting vasocontraction (PubMed:35802072). {ECO:0000250, ECO:0000269|PubMed:22654117, ECO:0000269|PubMed:35802072}. | Mus musculus (Mouse) |
B8JLQ9 | CBPO_DANRE | MMQASITSILVVLTLVAQDRLAGGLEHKSYDYTKYHTMDEISAWMNQMQRENPDVVSTMTYGQTYEKRNITLLKIGFSSTTPKKAIWMDCGIHAREWIAPAFCQHFVKEVLGSYKTDSRVNMLFKNLDFYITPVLNMDGYIYSWLNNSTRLWRKSRSPCHENSTCSGTDLNRNFYANWGMVGISRNCCSEVYNGATALSEPEAEAVTDFLGAHQNHLLCYLTIHSYGQLILVPYGHPNISAPNYDELMEVGLAAAKAIKAVHGKSYKVGSSPDVLYPNSGSSRDFARLIGIPYSFTFELRDEGQHGFILPEDQIQPTCQEAYEGAMSIINYVHDKNFKNTAITVTATLWTTLMALWISTSHVF | 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 3-(2-furyl)acryloyl-Lys-Ala (at pH 7.5) {ECO:0000269|PubMed:21921028}; | 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 | MMQVLLVTICLAVFPYHGSSIILESGNVNDYEVVYPQKVTAMPKEAVKQPEQKYEDAMQYKFEVNGEPVLLHLEKNKDLFSEDYSETHYSPDGREITTKPLVQDHCYYHGHIQNDAHSSASISACNGLKGHFKLRGEMYLIEPLKLSDSEAHAVYKYENVEKEDEALKMCGVTQTNWESDEPIKKASLLVATSERNRYFNPYSYVELIITVDHSMVTKYKNDLTAIRTWVFELVNTINEIFKYLYIRVPLVGLEIWKNRDLINVTSAANVTLDLFGEWRKSYLLPRKIHDNSQLLTAIDLNGLTIGMAYVSTMCQSKYSVGVVQDHSKINLRVAVTMAHEIGHNLGLTHDGVYCTCGGYSCIMSAVLGDQPSKYFSNCSYNQYRRFLTEHNPECIINPPLRTDIVSPPACGNELLERGEECDCGSPENCRDPCCDAASCKLHSWVECESGKCCNQCRFKRAGTECRPARDECDKAEQCTGRSANCPVDEFHENGRPCLHNFGYCYNGKCPIMYHQCHALFGQNVTGVQDSCFQYNRLGVYYAYCRKENGRKIPCAPKDEKCGRLYCSYKSPGNQIPCLPYYIPSDENKGMVDHGTKCGDGKVCSNGQCVDLNIAY | 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 | MSDAVILRSVKKFGEDNYGFESSTFYNNDKNSGLQDERKGDSSQVGFFQLFRFSSTTDIWLMFVGSLCAFLHGLSHPGVLLIFGTMTDVFIAYDTELQELKIPGKACVNNTIVWINSSLNQNVTNGTQCGLLDIESEMIKFASYYAGIALLVLITGYIQICFWVIAAARQIQKMRKISFRKVMRMEIGWFDCNSVGELNTRFSDDINRVNDAIADQMPIFIQRMTTSICGFLLGFYQGWKLTLVIISVSPLIGIGAAIIGLSVSKFTDYELKAYAKAGSVADEVISSMRTVAAFGGEKKEVERYEKNLVFAQRWGIRKGIVMGFFTGFMWCLIFLCYALAFWYGSKLVLEDGEYTAGTLVQIFLSILLGALNLGNASSCLEAFATGRAAATSIFHTIDRKPIIDCMSEDGYKLDRIKGEIEFHNVTFHYPSRPEVKILNNLSMVIKSGEMTAVVGSSGSGKSTALQLIQRFYDPSEGMVTLDGHDIRSLNIQWLRTQIGIVEQEPVLFSTTIAENIRYGREDATMEDIVRAAKAANAYNFIMDLPEQFDTLVGEGGGQMSGGQKQRVAIARALVRNPKILLLDMATSALDNESEAMVQEALSKIQQGHTIISVAHRLSTVRAADVIIGFEHGTAVERGSHEELLERKGVYFTLVTLQSQGEPTANAEGIRGEEETDGVSLDNEQTFCRGSYQSSLRASLRQRSKSQLSYLAHEPPLAVVDHKSTYEEDRKDKDIPVEEEIEPAPVRRILKFNAPEWPYMLFGAVGAAVNGSVTPLYAFLFSQILGTFSLPDKEEQRSQINGVCLLFVAVGCVSLCTQFLQGYAFAKSGELLTKRLRKYGFRAMLGQDIGWFDDLRNSPGALTTRLATDASQVQGAAGSQIGMMVNSFTNVTVAMIIAFFFSWKLSLVIMCFFPFLALSGALQTRMLTGFATQDKEALEIAGQITNEALSNIRTVAGIGKERQFIEAFEAELEKPFKTAFRKANVYGFCFGFSQCIVFVANSASYRYGGYLIPNEGLHFSYVFRVISSVVLSATALGRASSYTPSYAKAKISAARFFQLLDRQPPIKVYSSAGEKWDNFQGQVDFVDCKFTYPSRPDTQVLNGLSVSVRPGQTLAFVGSSGCGKSTSIQLLERFYDPDQGKVMIDGHDSRKVNVQFLRSNIGIVSQEPVLFACSIMDNIKYGDNTREIPMEKVIEAAKQAQLHDFVMSLPEKYETNVGSQGSQLSRGEKQRIAIARAIVRNPKILLLDEATSALDTESEKTVQVALDKAREGRTCIVIAHRLSTIQNSDIIAVMSQGIVIEKGTHEELMAQKGAYYKLVTTGAPIS | 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 ubiquitination [GO:0016567]; regulation of bile acid metabolic process [GO:1904251]; regulation of fatty acid beta-oxidation [GO:0031998]; transmembrane transport [GO:0055085]; xenobiotic export from cell [GO:0046618]; xenobiotic metabolic process [GO:0006805]; xenobiotic transmembrane transport [GO:0006855] | 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 transmembrane transporter activity [GO:0015126] | 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:0000250|UniProtKB:O70127}; Multi-pass membrane protein {ECO:0000250|UniProtKB:O70127}. Note=Internalized at the canalicular membrane through interaction with the adapter protein complex 2 (AP-2). At steady state, localizes in the canalicular membrane but is also present in recycling endosomes. ABCB11 constantly and rapidly exchanges between the two sites through tubulo-vesicles carriers that move along microtubules. Microtubule-dependent trafficking of ABCB11 is enhanced by taurocholate and cAMP and regulated by STK11 through a PKA-mediated pathway. Trafficking of newly synthesized ABCB11 through endosomal compartment to the bile canalicular membrane is accelerated by cAMP but not by taurocholate (By similarity). Cell membrane expression is up-regulated by short- and medium-chain fatty acids (By similarity). {ECO:0000250|UniProtKB:O70127, ECO:0000250|UniProtKB:O95342}. | 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:RHEA:50049; Evidence={ECO:0000250|UniProtKB:O95342}; CATALYTIC ACTIVITY: Reaction=ATP + H2O + taurocholate(in) = ADP + H(+) + phosphate + taurocholate(out); Xref=Rhea:RHEA:50052, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:36257, ChEBI:CHEBI:43474, ChEBI:CHEBI:456216; Evidence={ECO:0000269|PubMed:18985798}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:50053; Evidence={ECO:0000305|PubMed:18985798}; CATALYTIC ACTIVITY: Reaction=ATP + glycocholate(in) + H2O = ADP + glycocholate(out) + H(+) + phosphate; Xref=Rhea:RHEA:50056, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:29746, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:456216; Evidence={ECO:0000250|UniProtKB:O95342}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:50057; Evidence={ECO:0000250|UniProtKB:O95342}; CATALYTIC ACTIVITY: Reaction=ATP + glycochenodeoxycholate(in) + H2O = ADP + glycochenodeoxycholate(out) + H(+) + phosphate; Xref=Rhea:RHEA:50060, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:36252, ChEBI:CHEBI:43474, ChEBI:CHEBI:456216; Evidence={ECO:0000250|UniProtKB:O95342}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:50061; Evidence={ECO:0000250|UniProtKB:O95342}; CATALYTIC ACTIVITY: Reaction=ATP + H2O + taurochenodeoxycholate(in) = ADP + H(+) + phosphate + taurochenodeoxycholate(out); Xref=Rhea:RHEA:50064, ChEBI:CHEBI:9407, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:456216; Evidence={ECO:0000250|UniProtKB:O95342}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:50065; Evidence={ECO:0000250|UniProtKB:O95342}; CATALYTIC ACTIVITY: Reaction=ATP + glycoursodeoxycholate(in) + H2O = ADP + glycoursodeoxycholate(out) + H(+) + phosphate; Xref=Rhea:RHEA:50068, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:132030, ChEBI:CHEBI:456216; Evidence={ECO:0000250|UniProtKB:O95342}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:50069; Evidence={ECO:0000250|UniProtKB:O95342}; CATALYTIC ACTIVITY: Reaction=ATP + H2O + tauroursodeoxycholate(in) = ADP + H(+) + phosphate + tauroursodeoxycholate(out); Xref=Rhea:RHEA:50072, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:132028, ChEBI:CHEBI:456216; Evidence={ECO:0000250|UniProtKB:O95342}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:50073; Evidence={ECO:0000250|UniProtKB:O95342}; CATALYTIC ACTIVITY: Reaction=ATP + H2O + taurodeoxycholate(in) = ADP + H(+) + phosphate + taurodeoxycholate(out); Xref=Rhea:RHEA:50080, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:36261, ChEBI:CHEBI:43474, ChEBI:CHEBI:456216; Evidence={ECO:0000250|UniProtKB:O95342}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:50081; Evidence={ECO:0000250|UniProtKB:O95342}; CATALYTIC ACTIVITY: Reaction=ATP + H2O + taurolithocholate 3-sulfate(in) = ADP + H(+) + phosphate + taurolithocholate 3-sulfate(out); Xref=Rhea:RHEA:50084, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:58301, ChEBI:CHEBI:456216; Evidence={ECO:0000250|UniProtKB:O95342}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:50085; Evidence={ECO:0000250|UniProtKB:O95342}; CATALYTIC ACTIVITY: Reaction=ATP + H2O + pravastatin(in) = ADP + H(+) + phosphate + pravastatin(out); Xref=Rhea:RHEA:63908, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:63660, ChEBI:CHEBI:456216; Evidence={ECO:0000250|UniProtKB:O95342}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:63909; Evidence={ECO:0000250|UniProtKB:O95342}; | 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 lipid secretion in a bile salts dependent manner (PubMed:18985798). Transports taurine-conjugated bile salts more rapidly than glycine-conjugated bile salts. Also transports non-bile acid compounds, such as pravastatin and fexofenadine in an ATP-dependent manner and may be involved in their biliary excretion (By similarity). {ECO:0000250|UniProtKB:O95342, ECO:0000269|PubMed:18985798}. | 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 | MSMKMADPTKISILGRESIVADYSIWGTYIVQDLLTNLSSTTYVLVTDTNLGSIYLEKFSKIFNEAAAALSPPPRLLTKEIPPGENSKSRQGKADIEDWMLQQTCGRDTVIIALGGGVIGDLLGFVASTYMRGIRFVQVPTTLLAMVDSSIGGKTAIDTPLGKNLIGAIWQPQRIYIDIDFIDTLPEREFINGMAEVIKTAAISDEKEFAALERHADAILNAARSKARKGRFDAVRQELKDHIVASARHKAYVVTADEREGGLRNLLNLGHSIGHAIEAILSPQVLHGECVAIGMVKELELARYLGILKPVAVSRMIKCLSKYGLPTSLKDQRVRKHTAGKHCPLDQLMANMALDKKNDGPKKKVVLLSAIGQTYEPKASVVSNEDIRAVLAPSIEVIPGVPKSLNVVCAPPGSKSISNRALVLAALGSGTVRIKNLLHSDDTEVMLNALEHLGAATFAWEEEGEVLVVNGNGGKMQASPTELYLGNAGTASRFLTSVATLSGKGSVDFNILTGNNRMKQRPIGDLVDALTVNGAEIEYLEKAGSLPLKIAASGGFKGGRINLAAKVSSQYVSSLLMCAPYAKEPVVLKLVGGRPISLSYIEMTTAMMRSFGIDVQQSTTEEWTYHIPQGSYTNPAEYVIESDASSATYPLAIAAVTGTTCTVPNIGSASLQGDARFAVDVLRPMGCKVEQTATSTTVTGPADGVLRPLPNVDMEPMTDAFLGASVLAAIAQGEGSNHTTRIYGIANQRVKECNRIEAMRVELAKFGVVCREHPDGLEIDGIDRSTLRHPAGGVFCYDDHRVAFSFSILALVAPMPTLILEKECVGKTWPTYWDALKQKFGVRLEGKELDESVTTHHAPADRSNASVIIIGMRGAGKTTTGRWAAKVLNRKFIDLDVELEQTEGKSIPEIIKERGWQGFRDAELALFKRVLAERPTGHVLACGGGIVEIGEARKILTDYHKNKGNVLLVMRDIKRVMEFLNVDKTRPAYIEDMMSVWLRRKPWYHECSNVQYYSRHSSAPELALAVEDFGRFIQVVSGKIDYLAAIRKKRLSFFVSLTLPDLRDTGDLLRTVASGSDAVELRVDLLKDPSSDSAIPSAEYVAEQISFYRSKVALPIVFTVRTVSQGGKFPDDAHDAALELITLAIRSGCEFIDLEITFPEELLRKVTESKAHAKIIASHHDPQGKLNWANGSWIQYYNKALQYGDIIKLVGVAESLKDNTALKEFKDWAEQAHDVPVIAINMGDKGQLSRMLNGFLTPVSHPALPFKAAPGQLSAAEIRKGLSIMGEIPAKKFAIFGKPILASRSPAMHNTLFEQNGLPHVYTRLETDQTQDVKEFIRSPDFGGASVTIPLKLDIIPLIDEVLNEAEIIGAVNTIIPVEGKDGTTRLIGRNTDWSGIVRCLREAGAHSNEGKSSALVIGGGGTARAAIYALHHMGFSTVYVLGRSPEKIQNMASTFPTGFDIRVLENADDIETIPRVAVGTVPGDQPIEPNMREILCTIFKRSGQDPSADGASSVLLEMAYKPSVTPLMRLASDAGWKTIPGLEALVGQGVYQFEYWTGITPVYEVARNAVLGTNEK | 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:0004765] | 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; Xref=Rhea:RHEA:21096, ChEBI:CHEBI:15377, ChEBI:CHEBI:16630, ChEBI:CHEBI:32364; EC=4.2.1.10; Evidence={ECO:0000255|HAMAP-Rule:MF_03143}; CATALYTIC ACTIVITY: Reaction=NADP(+) + shikimate = 3-dehydroshikimate + H(+) + NADPH; Xref=Rhea:RHEA:17737, ChEBI:CHEBI:15378, ChEBI:CHEBI:16630, ChEBI:CHEBI:36208, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349; EC=1.1.1.25; Evidence={ECO:0000255|HAMAP-Rule:MF_03143}; CATALYTIC ACTIVITY: Reaction=ATP + shikimate = 3-phosphoshikimate + ADP + H(+); Xref=Rhea:RHEA:13121, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:36208, ChEBI:CHEBI:145989, ChEBI:CHEBI:456216; EC=2.7.1.71; Evidence={ECO:0000255|HAMAP-Rule:MF_03143}; CATALYTIC ACTIVITY: Reaction=3-phosphoshikimate + phosphoenolpyruvate = 5-O-(1-carboxyvinyl)-3-phosphoshikimate + phosphate; Xref=Rhea:RHEA:21256, ChEBI:CHEBI:43474, ChEBI:CHEBI:57701, ChEBI:CHEBI:58702, ChEBI:CHEBI:145989; EC=2.5.1.19; Evidence={ECO:0000255|HAMAP-Rule:MF_03143}; | 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: step 3/7. {ECO:0000255|HAMAP-Rule:MF_03143}.; PATHWAY: Metabolic intermediate biosynthesis; chorismate biosynthesis; chorismate from D-erythrose 4-phosphate and phosphoenolpyruvate: step 4/7. {ECO:0000255|HAMAP-Rule:MF_03143}.; PATHWAY: Metabolic intermediate biosynthesis; chorismate biosynthesis; chorismate from D-erythrose 4-phosphate and phosphoenolpyruvate: step 5/7. {ECO:0000255|HAMAP-Rule:MF_03143}.; PATHWAY: Metabolic intermediate biosynthesis; chorismate biosynthesis; chorismate from D-erythrose 4-phosphate and phosphoenolpyruvate: step 6/7. {ECO:0000255|HAMAP-Rule:MF_03143}. | 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 | MPGSLIDTRQQPLSVGIVGGGIIGVILAAGLVRRGIDVKVFEQARGFREIGAGMAFTANAVRCMEMLDPAIVWALRSSGAVPISIGDHQAEARDYLRWVDGYHESSKRLYQLDAGIRGFEACRRDQFLEALVKVLPEGIVECQKRLQKIHEKNETEKVTLEFADGTFAHVDCVIGADGIRSRVRQHLFGEDSPYSHPHYSHKFAFRGLITMENAISALGEDKARTLNMHVGPNAHLIHYPVANETMVNIAAFVSDPEEWPDKLSLVGPATREEAMGYFANWNPGLRAVLGFMPENIDRWAMFDTYDYPAPFFSRGKICLVGDAAHAAVPHHGAGACIGIEDALCATVLLAEVFVSTRGKSSIVRNRAIAAAFGSFNAVRRVRAQWFVDSSRRVCDLYQQPEWADPQKRIKAENCFEEIKDRSHKIWHFDYNSMLQEAIEKYRHNMGS | 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 3-methylorcinaldehyde into a hydroxycyclohexadione (PubMed:22508998, PubMed:24863423, PubMed:31346489). The pathway begins with the synthesis of 3-methylorcinaldehyde by the non-reducing polyketide synthase (PKS) tropA. 3-methylorcinaldehyde is the substrate for the FAD-dependent monooxygenase tropB to yield a dearomatized hydroxycyclohexadione. The 2-oxoglutarate-dependent dioxygenase tropC then performs the oxidative ring expansion to provide the first tropolone metabolite stipitaldehyde. Trop D converts stipitaldehyde into stipitacetal which is in turn converted to stipitalide by the short-chain dehydrogenase/reductase tropE. The next steps involve tropF, tropG, tropH, tropI and tropJ to form successive tropolone maleic anhydrides including stipitaldehydic, stipitatonic and stipitatic acids (Probable). {ECO:0000269|PubMed:22508998, ECO:0000269|PubMed:24863423, ECO:0000269|PubMed:31346489, ECO:0000305|PubMed:24863423}. | Talaromyces stipitatus (strain ATCC 10500 / CBS 375.48 / QM 6759 / NRRL 1006) (Penicillium stipitatum) |
B8N2C8 | CP51A_ASPFN | MIFSRSMASFTLVSAYAAAGLLAIIVLNLLRQLLFRNKTDPPLVFHWIPFLGSTVTYGMDPYAFFFSCRQKYGDIFTFILLGRKITVYLGIQGNEFILNGKLKDVNAEEIYSPLTTPVFGSDIVYDCPNSKLMEQKKFIKFGLTQAALESHVPLIEKEVLDYLKTSPNFKGTSGRVEITDAMAEITIFTAGRALQGEEVRKKLTAEFADLYHDLDRGFTPINFMLPWAPLPRNRKRDAAHARMREIYMDIINERRKNPDRETSDMIWNLMHCTYKNGQPLPDKEIAHMMITLLMAGQHSSSSISSWIMLRLASEPAVMEELYQEQITKLSPDGRTLPPLQYRDLDLLPLHQNLIKETLRLHLSIHSLMRKVKNPMPVPGTPYVVPADHVLLASPGVTALSDEYFPNASRWDPHRWENRVEKEDEEDIVDYGYGTVSKGTSSPYLPFGAGRHRCIGEKFAYVNLGVIVATMARHMKLFNVDGKKGVPATDYSSMFSGPSKPAIIGWERRFPEKS | 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, ChEBI:CHEBI:15740, ChEBI:CHEBI:57618, ChEBI:CHEBI:58210, ChEBI:CHEBI:138029, ChEBI:CHEBI:138031; EC=1.14.14.154; Evidence={ECO:0000250|UniProtKB:Q4WNT5}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:54029; Evidence={ECO:0000250|UniProtKB:Q4WNT5}; CATALYTIC ACTIVITY: Reaction=a 14alpha-methyl steroid + O2 + reduced [NADPH--hemoprotein reductase] = a 14alpha-hydroxymethyl steroid + H(+) + H2O + oxidized [NADPH--hemoprotein reductase]; Xref=Rhea:RHEA:68060, Rhea:RHEA-COMP:11964, Rhea:RHEA-COMP:11965, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, ChEBI:CHEBI:57618, ChEBI:CHEBI:58210, ChEBI:CHEBI:138029, ChEBI:CHEBI:176901; Evidence={ECO:0000250|UniProtKB:P10614}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:68061; Evidence={ECO:0000250|UniProtKB:P10614}; CATALYTIC ACTIVITY: Reaction=a 14alpha-hydroxymethyl steroid + O2 + reduced [NADPH--hemoprotein reductase] = a 14alpha-formyl steroid + H(+) + 2 H2O + oxidized [NADPH--hemoprotein reductase]; Xref=Rhea:RHEA:68064, Rhea:RHEA-COMP:11964, Rhea:RHEA-COMP:11965, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, ChEBI:CHEBI:57618, ChEBI:CHEBI:58210, ChEBI:CHEBI:176901, ChEBI:CHEBI:176902; Evidence={ECO:0000250|UniProtKB:P10614}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:68065; Evidence={ECO:0000250|UniProtKB:P10614}; CATALYTIC ACTIVITY: Reaction=a 14alpha-formyl steroid + O2 + reduced [NADPH--hemoprotein reductase] = a Delta(14) steroid + formate + 2 H(+) + H2O + oxidized [NADPH--hemoprotein reductase]; Xref=Rhea:RHEA:68068, Rhea:RHEA-COMP:11964, Rhea:RHEA-COMP:11965, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, ChEBI:CHEBI:15740, ChEBI:CHEBI:57618, ChEBI:CHEBI:58210, ChEBI:CHEBI:138031, ChEBI:CHEBI:176902; Evidence={ECO:0000250|UniProtKB:P10614}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:68069; Evidence={ECO:0000250|UniProtKB:P10614}; CATALYTIC ACTIVITY: Reaction=lanosterol + 3 O2 + 3 reduced [NADPH--hemoprotein reductase] = 4,4-dimethyl-5alpha-cholesta-8,14,24-trien-3beta-ol + formate + 4 H(+) + 4 H2O + 3 oxidized [NADPH--hemoprotein reductase]; Xref=Rhea:RHEA:25286, Rhea:RHEA-COMP:11964, Rhea:RHEA-COMP:11965, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, ChEBI:CHEBI:15740, ChEBI:CHEBI:16521, ChEBI:CHEBI:17813, ChEBI:CHEBI:57618, ChEBI:CHEBI:58210; EC=1.14.14.154; Evidence={ECO:0000250|UniProtKB:Q4WNT5}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:25287; Evidence={ECO:0000250|UniProtKB:Q4WNT5}; CATALYTIC ACTIVITY: Reaction=lanosterol + O2 + reduced [NADPH--hemoprotein reductase] = 32-hydroxylanosterol + H(+) + H2O + oxidized [NADPH--hemoprotein reductase]; Xref=Rhea:RHEA:75103, Rhea:RHEA-COMP:11964, Rhea:RHEA-COMP:11965, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, ChEBI:CHEBI:16521, ChEBI:CHEBI:57618, ChEBI:CHEBI:58210, ChEBI:CHEBI:166806; Evidence={ECO:0000250|UniProtKB:P10614}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:75104; Evidence={ECO:0000250|UniProtKB:P10614}; CATALYTIC ACTIVITY: Reaction=32-hydroxylanosterol + O2 + reduced [NADPH--hemoprotein reductase] = 32-oxolanosterol + H(+) + 2 H2O + oxidized [NADPH--hemoprotein reductase]; Xref=Rhea:RHEA:75107, Rhea:RHEA-COMP:11964, Rhea:RHEA-COMP:11965, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, ChEBI:CHEBI:57618, ChEBI:CHEBI:58210, ChEBI:CHEBI:166681, ChEBI:CHEBI:166806; Evidence={ECO:0000250|UniProtKB:P10614}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:75108; Evidence={ECO:0000250|UniProtKB:P10614}; CATALYTIC ACTIVITY: Reaction=32-oxolanosterol + O2 + reduced [NADPH--hemoprotein reductase] = 4,4-dimethyl-5alpha-cholesta-8,14,24-trien-3beta-ol + formate + 2 H(+) + H2O + oxidized [NADPH--hemoprotein reductase]; Xref=Rhea:RHEA:75111, Rhea:RHEA-COMP:11964, Rhea:RHEA-COMP:11965, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, ChEBI:CHEBI:15740, ChEBI:CHEBI:17813, ChEBI:CHEBI:57618, ChEBI:CHEBI:58210, ChEBI:CHEBI:166681; Evidence={ECO:0000250|UniProtKB:P10614}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:75112; Evidence={ECO:0000250|UniProtKB:P10614}; CATALYTIC ACTIVITY: Reaction=eburicol + 3 O2 + 3 reduced [NADPH--hemoprotein reductase] = 14-demethyleburicol + formate + 4 H(+) + 4 H2O + 3 oxidized [NADPH--hemoprotein reductase]; Xref=Rhea:RHEA:75439, Rhea:RHEA-COMP:11964, Rhea:RHEA-COMP:11965, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, ChEBI:CHEBI:15740, ChEBI:CHEBI:57618, ChEBI:CHEBI:58210, ChEBI:CHEBI:70315, ChEBI:CHEBI:194330; Evidence={ECO:0000250|UniProtKB:Q4WNT5}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:75440; Evidence={ECO:0000250|UniProtKB:Q4WNT5}; CATALYTIC ACTIVITY: Reaction=eburicol + O2 + reduced [NADPH--hemoprotein reductase] = 32-hydroxyeburicol + H(+) + H2O + oxidized [NADPH--hemoprotein reductase]; Xref=Rhea:RHEA:75427, Rhea:RHEA-COMP:11964, Rhea:RHEA-COMP:11965, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, ChEBI:CHEBI:57618, ChEBI:CHEBI:58210, ChEBI:CHEBI:70315, ChEBI:CHEBI:194328; Evidence={ECO:0000250|UniProtKB:P10614}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:75428; Evidence={ECO:0000250|UniProtKB:P10614}; CATALYTIC ACTIVITY: Reaction=32-hydroxyeburicol + O2 + reduced [NADPH--hemoprotein reductase] = 32-oxoeburicol + H(+) + 2 H2O + oxidized [NADPH--hemoprotein reductase]; Xref=Rhea:RHEA:75431, Rhea:RHEA-COMP:11964, Rhea:RHEA-COMP:11965, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, ChEBI:CHEBI:57618, ChEBI:CHEBI:58210, ChEBI:CHEBI:194328, ChEBI:CHEBI:194329; Evidence={ECO:0000250|UniProtKB:P10614}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:75432; Evidence={ECO:0000250|UniProtKB:P10614}; CATALYTIC ACTIVITY: Reaction=32-oxoeburicol + O2 + reduced [NADPH--hemoprotein reductase] = 14-demethyleburicol + formate + 2 H(+) + H2O + oxidized [NADPH--hemoprotein reductase]; Xref=Rhea:RHEA:75435, Rhea:RHEA-COMP:11964, Rhea:RHEA-COMP:11965, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, ChEBI:CHEBI:15740, ChEBI:CHEBI:57618, ChEBI:CHEBI:58210, ChEBI:CHEBI:194329, ChEBI:CHEBI:194330; Evidence={ECO:0000250|UniProtKB:P10614}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:75436; Evidence={ECO:0000250|UniProtKB:P10614}; | 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 involves the ergosterol synthesis itself through consecutive reactions that mainly occur in the endoplasmic reticulum (ER) membrane (By similarity). In filamentous fungi, during the initial step of this module, lanosterol (lanosta-8,24-dien-3beta-ol) can be metabolized to eburicol (By similarity). Sterol 14alpha-demethylase catalyzes the three-step oxidative removal of the 14alpha-methyl group (C-32) of both these sterols in the form of formate, and converts eburicol and lanosterol to 14-demethyleburicol (4,4,24-trimethylergosta-8,14,24(28)-trienol) and 4,4-dimethyl-5alpha-cholesta-8,14,24-trien-3beta-ol, respectively, which are further metabolized by other enzymes in the pathway to ergosterol (By similarity). Can also use substrates not intrinsic to fungi, such as 24,25-dihydrolanosterol (DHL), producing 4,4'-dimethyl-8,14-cholestadien-3-beta-ol, but at lower rates than the endogenous substrates (By similarity). {ECO:0000250|UniProtKB:P10613, ECO:0000250|UniProtKB:P10614, ECO:0000250|UniProtKB:Q4WNT5}.; FUNCTION: As a target of azole drugs, plays a crucial role in azole susceptibility (PubMed:18775650, PubMed:29311090). {ECO:0000269|PubMed:18775650, ECO:0000269|PubMed:29311090}. | Aspergillus flavus (strain ATCC 200026 / FGSC A1120 / IAM 13836 / NRRL 3357 / JCM 12722 / SRRC 167) |
B8N4Q9 | ARO1_ASPFN | MAEPTKIKILGQESIIADFGLWRNYVAKDLISGCPSTTYVLITDTNIGSIYTPGFQKTFEDAATAVSPAPRLLVYHCPPGEVSKSRQTKADIEDWMLSQSPPCGRDTVVIALGGGVIGDLTGFVASTYMRGVRYVQVPTTLLAMVDSSIGGKTAIDTPLGKNLIGAIWQPTRIYIDLEFLETLPVREFVNGMAEVIKTAAISSEEEFTALEDNAEAILTAVRSERKPGQRWFEGIEDILKARILASARHKAYVVSADEREGGLRNLLNWGHSIGHAIEAILTPQVLHGECVAIGMVKEAELARHLGILKGVAVARIVKCIAAYGLPTSLKDSRIRKLTAGKHCSVDQLLFNMALDKKNDGPKKKIVLLSAIGRTYEPKASVVPNEDIGVVLAPSIEVHPGVEPASNIICIPPGSKSISNRALVLAALGSGTCRVKNLLHSDDTEVMLNALERLGAATFSWEEEGEVLVVNGKGGNLQASPSELYLGNAGTASRFLTTVATLANASSVDSSILTGNNRMKQRPIGDLVDALTANGASVEYVERKGSLPLKVAASGGFAGGRINLAAKVSSQYVSSLLMCAPYAKEPVTLKLVGGKPISQPYIDMTTAMMRSFGIDVQKSTTEEHTYHIPQGRYVNPAEYVIESDASSATYPLAIAAITGTTCTVPNIGSKSLQGDARFAVEVLGPMGCTVKQTDTSTTVVGPSDGILRPLPNVDMEPMTDAFLTASVLAAVARGDGASHTTRIYGIANQRVKECNRIKAMKDELAKFGVVCREHDDGLEIDGIDRSTLRQPAGGVYCYDDHRVAFSFSVLSLVAPQPTLILEKECVGKTWPGWWDTLRQKFSAKLEGKELKEEESSPLAGAGRATASVFIIGMRGAGKTTTGRWVAKTLNRPFVDLDTELENVEGQTIPDIVKQRGWQGFRDAELSLLQRTLKERSSGYVLACGGGIVEIPEARKLLIDYHKNKGNVMLIMRDIKQVMDFLNIDKTRPAYVEDMMGVWLRRKPWFQECSNIQYYSQHATGKLAKASEDFTRFFNVVTGEADSLSIIKRKKHSFFVSLTLPDLRTAGDILEKVCVGSDAVELRVDLLKDPASDSDIPSVDYVAEQMAFLRSYVSLPLIFTIRTKSQGGRFPDDAHDAAMELYRLAFRSGSEFVDLEIAFPDEMLRAVTEMKGYSKIIASHHDPKGELSWANMSWMKYYNRALEYGDIIKLVGVAKNLDDNTALRKFKSWAEEAHETPLIAINMGDNGQLSRILNGFMTPVSHPSLPFKAAPGQLSATEIRKGLSLMGEIKQKKFAVFGTPVSGSRSPVLHNTLFSQAGLPHEYGRLETANVEDVKDFIRSPDFGGASVTIPLKLDIMPLLDHITPEAEIIGAVNTIIPVADGDKPARLVGSNTDWQGMTLSLHNAGVETANKDASALVIGGGGTARAAIYALHSMGFSPIYVIGRSAPKLQSMVSTFPSSYNIQVIDSPETLKTIPTVAIGTIPADKPIDPVMRETLCHMFERAQEADADVVKTGEKAHRVLLEMAYKPSVTALMQLASDSNWHTIPGLEVLVGQGWYQFKHWTGISPLYEDARAAVLSS | 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:0004765] | 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; Xref=Rhea:RHEA:21096, ChEBI:CHEBI:15377, ChEBI:CHEBI:16630, ChEBI:CHEBI:32364; EC=4.2.1.10; Evidence={ECO:0000255|HAMAP-Rule:MF_03143}; CATALYTIC ACTIVITY: Reaction=NADP(+) + shikimate = 3-dehydroshikimate + H(+) + NADPH; Xref=Rhea:RHEA:17737, ChEBI:CHEBI:15378, ChEBI:CHEBI:16630, ChEBI:CHEBI:36208, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349; EC=1.1.1.25; Evidence={ECO:0000255|HAMAP-Rule:MF_03143}; CATALYTIC ACTIVITY: Reaction=ATP + shikimate = 3-phosphoshikimate + ADP + H(+); Xref=Rhea:RHEA:13121, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:36208, ChEBI:CHEBI:145989, ChEBI:CHEBI:456216; EC=2.7.1.71; Evidence={ECO:0000255|HAMAP-Rule:MF_03143}; CATALYTIC ACTIVITY: Reaction=3-phosphoshikimate + phosphoenolpyruvate = 5-O-(1-carboxyvinyl)-3-phosphoshikimate + phosphate; Xref=Rhea:RHEA:21256, ChEBI:CHEBI:43474, ChEBI:CHEBI:57701, ChEBI:CHEBI:58702, ChEBI:CHEBI:145989; EC=2.5.1.19; Evidence={ECO:0000255|HAMAP-Rule:MF_03143}; | 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: step 3/7. {ECO:0000255|HAMAP-Rule:MF_03143}.; PATHWAY: Metabolic intermediate biosynthesis; chorismate biosynthesis; chorismate from D-erythrose 4-phosphate and phosphoenolpyruvate: step 4/7. {ECO:0000255|HAMAP-Rule:MF_03143}.; PATHWAY: Metabolic intermediate biosynthesis; chorismate biosynthesis; chorismate from D-erythrose 4-phosphate and phosphoenolpyruvate: step 5/7. {ECO:0000255|HAMAP-Rule:MF_03143}.; PATHWAY: Metabolic intermediate biosynthesis; chorismate biosynthesis; chorismate from D-erythrose 4-phosphate and phosphoenolpyruvate: step 6/7. {ECO:0000255|HAMAP-Rule:MF_03143}. | 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 | MTCSQPNLRVTIIAADGLYKRDVFRFPDPFAVATVGGEQTHTTSVIKKTLNPYWNEMFDLRVNEDSILAIQIFDQKKFKKKDQGFLGVINVRIGDVIDLQMGGDEMLTRDLKKSNDNLVVHGKLIINLSTNLSTPNTNQANGLHRSHMQPSTSSGLVPQVSASTPQPSPGPSQADPTASNPSLHPQRVPSTTRPSSTIVPANGPPAPPNGQQGSRTNLSSFEDSQGRLPAGWERREDNLGRTYYVDHNTRTTTWTRPSNNYNEQTSRTQREASMQLERRAHQSRMLPEDRTGASSPNLQENQQQAQTPPAGGSASAVSMMATGATTAGTGELPPGWEQRTTPEGRPYFVDHNTRTTTWVDPRRQQYIRMYGQNANGTNTTIQQQPVSQLGPLPSGWEMRLTNTARVYFVDHNTKTTTWDDPRLPSSLDQGVPQYKRDFRRKLIYFRSQPALRIMSGQCHVKVRRNNIFEDSYAEIMRQSASDLKKRLMIKFDGEDGLDYGGLSREFFFLLSHEMFNPFYCLFEYSAHDNYTLQINPHSGVNPEHLNYFKFIGRVVGLAIFHRRFLDSFFIGAFYKMMLRKKVSLQDMEGVDEDLHRNLTWTLDNDIEGIIELTFAVDDEKFGERRTIDLKPGGRDIPVTNENKGEYVELVTEWKIVKRVEEQFNAFMSGFNELIPADLVNVFDERELELLIGGIADIDVDDWKKHTDYRGYQESDEVIQNFWKIVRTWDAEQKSRLLQFTTGTSRIPVNGFKDLQGSDGPRRFTIEKSGDPGALPKSHTCFNRLDLPPYKTNDVLEHKLSIAVEETLGFGQE | 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 nucleus [GO:0016973]; positive regulation of fatty acid biosynthetic process [GO:0045723]; positive regulation of proteasomal ubiquitin-dependent protein catabolic process [GO:0032436]; positive regulation of receptor-mediated endocytosis [GO:0048260]; positive regulation of transcription by RNA polymerase II [GO:0045944]; protein K63-linked ubiquitination [GO:0070534]; regulation of actin cytoskeleton organization [GO:0032956]; regulation of dolichol biosynthetic process [GO:0010794]; regulation of ergosterol biosynthetic process [GO:0032443]; regulation of mRNA export from nucleus [GO:0010793]; regulation of multivesicular body size [GO:0010796]; regulation of nitrogen utilization [GO:0006808]; regulation of phosphate metabolic process [GO:0019220]; regulation of protein localization [GO:0032880]; regulation of ribosomal large subunit export from nucleus [GO:2000203]; regulation of rRNA processing [GO:2000232]; regulation of tRNA export from nucleus [GO:2000238]; regulation of tRNA processing [GO:2000235]; regulation of ubiquinone biosynthetic process [GO:0010795]; ribophagy [GO:0034517]; ubiquitin-dependent endocytosis [GO:0070086]; ubiquitin-dependent protein catabolic process via the multivesicular body sorting pathway [GO:0043162] | 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 | MGILAVILDSVCERCSGSSLWMLSTVALLSILVVSVVINVLRQLLFKNYKEPPLVFHWFPFIGSTISYGMDPYRFFFNCREKYGDIFTFVLLGKKTTVYLGTKGNDFILNGKLRDVCAEEVYSPLTTPVFGRHVVYDCPNAKLMEQKKGPNGVFDVCKTIAEITIYTASRSLQGKEVRSRFDSTFAELYHDLDMGFAPINFMLPWAPLPHNRKRDAAQKRMTETYMEIIKERRKAGSKKDSEDMVWNLMSCMYKDGTPVPDEEIAHMMIALLMAGQHSSSSTAAWIVLHLAASPEITEELYQEQLRILGHDMPPLTYENLQKLDLHAKVIKETLRIHAPIHSIIRAVKNPMPVEGTPYVIPTSHNVLSSPGVTARSEEHFPDPLEWKPHRWDEAIAVSSEDEEKVDYGYGLVTKGTNSPYLPFGAGRHRCIGEQFAYVQLGAITAALVRLFKFSNLPGVQTLPDTDYSSLFSKPLGNSKIQFEKREPVTKA | 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, ChEBI:CHEBI:15740, ChEBI:CHEBI:57618, ChEBI:CHEBI:58210, ChEBI:CHEBI:138029, ChEBI:CHEBI:138031; EC=1.14.14.154; Evidence={ECO:0000250|UniProtKB:Q4WNT5}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:54029; Evidence={ECO:0000250|UniProtKB:Q4WNT5}; CATALYTIC ACTIVITY: Reaction=a 14alpha-methyl steroid + O2 + reduced [NADPH--hemoprotein reductase] = a 14alpha-hydroxymethyl steroid + H(+) + H2O + oxidized [NADPH--hemoprotein reductase]; Xref=Rhea:RHEA:68060, Rhea:RHEA-COMP:11964, Rhea:RHEA-COMP:11965, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, ChEBI:CHEBI:57618, ChEBI:CHEBI:58210, ChEBI:CHEBI:138029, ChEBI:CHEBI:176901; Evidence={ECO:0000250|UniProtKB:P10614}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:68061; Evidence={ECO:0000250|UniProtKB:P10614}; CATALYTIC ACTIVITY: Reaction=a 14alpha-hydroxymethyl steroid + O2 + reduced [NADPH--hemoprotein reductase] = a 14alpha-formyl steroid + H(+) + 2 H2O + oxidized [NADPH--hemoprotein reductase]; Xref=Rhea:RHEA:68064, Rhea:RHEA-COMP:11964, Rhea:RHEA-COMP:11965, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, ChEBI:CHEBI:57618, ChEBI:CHEBI:58210, ChEBI:CHEBI:176901, ChEBI:CHEBI:176902; Evidence={ECO:0000250|UniProtKB:P10614}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:68065; Evidence={ECO:0000250|UniProtKB:P10614}; CATALYTIC ACTIVITY: Reaction=a 14alpha-formyl steroid + O2 + reduced [NADPH--hemoprotein reductase] = a Delta(14) steroid + formate + 2 H(+) + H2O + oxidized [NADPH--hemoprotein reductase]; Xref=Rhea:RHEA:68068, Rhea:RHEA-COMP:11964, Rhea:RHEA-COMP:11965, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, ChEBI:CHEBI:15740, ChEBI:CHEBI:57618, ChEBI:CHEBI:58210, ChEBI:CHEBI:138031, ChEBI:CHEBI:176902; Evidence={ECO:0000250|UniProtKB:P10614}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:68069; Evidence={ECO:0000250|UniProtKB:P10614}; CATALYTIC ACTIVITY: Reaction=lanosterol + 3 O2 + 3 reduced [NADPH--hemoprotein reductase] = 4,4-dimethyl-5alpha-cholesta-8,14,24-trien-3beta-ol + formate + 4 H(+) + 4 H2O + 3 oxidized [NADPH--hemoprotein reductase]; Xref=Rhea:RHEA:25286, Rhea:RHEA-COMP:11964, Rhea:RHEA-COMP:11965, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, ChEBI:CHEBI:15740, ChEBI:CHEBI:16521, ChEBI:CHEBI:17813, ChEBI:CHEBI:57618, ChEBI:CHEBI:58210; EC=1.14.14.154; Evidence={ECO:0000250|UniProtKB:Q4WNT5}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:25287; Evidence={ECO:0000250|UniProtKB:Q4WNT5}; CATALYTIC ACTIVITY: Reaction=lanosterol + O2 + reduced [NADPH--hemoprotein reductase] = 32-hydroxylanosterol + H(+) + H2O + oxidized [NADPH--hemoprotein reductase]; Xref=Rhea:RHEA:75103, Rhea:RHEA-COMP:11964, Rhea:RHEA-COMP:11965, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, ChEBI:CHEBI:16521, ChEBI:CHEBI:57618, ChEBI:CHEBI:58210, ChEBI:CHEBI:166806; Evidence={ECO:0000250|UniProtKB:P10614}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:75104; Evidence={ECO:0000250|UniProtKB:P10614}; CATALYTIC ACTIVITY: Reaction=32-hydroxylanosterol + O2 + reduced [NADPH--hemoprotein reductase] = 32-oxolanosterol + H(+) + 2 H2O + oxidized [NADPH--hemoprotein reductase]; Xref=Rhea:RHEA:75107, Rhea:RHEA-COMP:11964, Rhea:RHEA-COMP:11965, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, ChEBI:CHEBI:57618, ChEBI:CHEBI:58210, ChEBI:CHEBI:166681, ChEBI:CHEBI:166806; Evidence={ECO:0000250|UniProtKB:P10614}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:75108; Evidence={ECO:0000250|UniProtKB:P10614}; CATALYTIC ACTIVITY: Reaction=32-oxolanosterol + O2 + reduced [NADPH--hemoprotein reductase] = 4,4-dimethyl-5alpha-cholesta-8,14,24-trien-3beta-ol + formate + 2 H(+) + H2O + oxidized [NADPH--hemoprotein reductase]; Xref=Rhea:RHEA:75111, Rhea:RHEA-COMP:11964, Rhea:RHEA-COMP:11965, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, ChEBI:CHEBI:15740, ChEBI:CHEBI:17813, ChEBI:CHEBI:57618, ChEBI:CHEBI:58210, ChEBI:CHEBI:166681; Evidence={ECO:0000250|UniProtKB:P10614}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:75112; Evidence={ECO:0000250|UniProtKB:P10614}; CATALYTIC ACTIVITY: Reaction=eburicol + 3 O2 + 3 reduced [NADPH--hemoprotein reductase] = 14-demethyleburicol + formate + 4 H(+) + 4 H2O + 3 oxidized [NADPH--hemoprotein reductase]; Xref=Rhea:RHEA:75439, Rhea:RHEA-COMP:11964, Rhea:RHEA-COMP:11965, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, ChEBI:CHEBI:15740, ChEBI:CHEBI:57618, ChEBI:CHEBI:58210, ChEBI:CHEBI:70315, ChEBI:CHEBI:194330; Evidence={ECO:0000250|UniProtKB:Q4WNT5}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:75440; Evidence={ECO:0000250|UniProtKB:Q4WNT5}; CATALYTIC ACTIVITY: Reaction=eburicol + O2 + reduced [NADPH--hemoprotein reductase] = 32-hydroxyeburicol + H(+) + H2O + oxidized [NADPH--hemoprotein reductase]; Xref=Rhea:RHEA:75427, Rhea:RHEA-COMP:11964, Rhea:RHEA-COMP:11965, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, ChEBI:CHEBI:57618, ChEBI:CHEBI:58210, ChEBI:CHEBI:70315, ChEBI:CHEBI:194328; Evidence={ECO:0000250|UniProtKB:P10614}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:75428; Evidence={ECO:0000250|UniProtKB:P10614}; CATALYTIC ACTIVITY: Reaction=32-hydroxyeburicol + O2 + reduced [NADPH--hemoprotein reductase] = 32-oxoeburicol + H(+) + 2 H2O + oxidized [NADPH--hemoprotein reductase]; Xref=Rhea:RHEA:75431, Rhea:RHEA-COMP:11964, Rhea:RHEA-COMP:11965, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, ChEBI:CHEBI:57618, ChEBI:CHEBI:58210, ChEBI:CHEBI:194328, ChEBI:CHEBI:194329; Evidence={ECO:0000250|UniProtKB:P10614}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:75432; Evidence={ECO:0000250|UniProtKB:P10614}; CATALYTIC ACTIVITY: Reaction=32-oxoeburicol + O2 + reduced [NADPH--hemoprotein reductase] = 14-demethyleburicol + formate + 2 H(+) + H2O + oxidized [NADPH--hemoprotein reductase]; Xref=Rhea:RHEA:75435, Rhea:RHEA-COMP:11964, Rhea:RHEA-COMP:11965, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, ChEBI:CHEBI:15740, ChEBI:CHEBI:57618, ChEBI:CHEBI:58210, ChEBI:CHEBI:194329, ChEBI:CHEBI:194330; Evidence={ECO:0000250|UniProtKB:P10614}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:75436; Evidence={ECO:0000250|UniProtKB:P10614}; | 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 involves the ergosterol synthesis itself through consecutive reactions that mainly occur in the endoplasmic reticulum (ER) membrane (By similarity). In filamentous fungi, during the initial step of this module, lanosterol (lanosta-8,24-dien-3beta-ol) can be metabolized to eburicol (By similarity). Sterol 14alpha-demethylase catalyzes the three-step oxidative removal of the 14alpha-methyl group (C-32) of both these sterols in the form of formate, and converts eburicol and lanosterol to 14-demethyleburicol (4,4,24-trimethylergosta-8,14,24(28)-trienol) and 4,4-dimethyl-5alpha-cholesta-8,14,24-trien-3beta-ol, respectively, which are further metabolized by other enzymes in the pathway to ergosterol (By similarity). Can also use substrates not intrinsic to fungi, such as 24,25-dihydrolanosterol (DHL), producing 4,4'-dimethyl-8,14-cholestadien-3-beta-ol, but at lower rates than the endogenous substrates (By similarity). {ECO:0000250|UniProtKB:P10613, ECO:0000250|UniProtKB:P10614, ECO:0000250|UniProtKB:Q4WNT5}.; FUNCTION: As a target of azole drugs, plays a crucial role in azole susceptibility (PubMed:18775650, PubMed:29311090). {ECO:0000269|PubMed:18775650, ECO:0000269|PubMed:29311090}. | 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 metaphase/anaphase transition [GO:0045841]; positive regulation of glucose transmembrane transport [GO:0010828]; protein neddylation [GO:0045116]; protein ubiquitination [GO:0016567]; regulation of DNA recombination [GO:0000018]; regulation of exit from mitosis [GO:0007096]; regulation of protein-containing complex assembly [GO:0043254]; resolution of meiotic recombination intermediates [GO:0000712]; SCF-dependent proteasomal ubiquitin-dependent protein catabolic process [GO:0031146]; septin ring assembly [GO:0000921]; silent mating-type cassette heterochromatin formation [GO:0030466]; vacuolar acidification [GO:0007035]; vacuolar proton-transporting V-type ATPase complex assembly [GO:0070072] | 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 similarity). {ECO:0000250}. | Aspergillus flavus (strain ATCC 200026 / FGSC A1120 / IAM 13836 / NRRL 3357 / JCM 12722 / SRRC 167) |
B8NUK6 | CP51C_ASPFN | MSWPRIGAYALLAFVAIMALNVTYQFLFRMLNKTRPPLVFHWIPFIGSTIHYGMDPYGFFFSCREKYGDIFTFILLGRPTTVYLGTQGNEFILNGKLKDVNAEEVYSPLTTPVFGSDVVYDCPNSKLIEQKKFIKFGLSQAALEAHVPLIEKEVEDYLAMSPNFHGTSGEVDIPAAMAEITIFTAGSALQGEEVRSKLTTEFAVLYHDLDKGFTPINFMLPWAPLPHNKKRDAAHARMRSIYIDIINKRRNAGDNVPEKLDMIGNLMQCTYKNGQPLPDKEIAHIMITLLMAGQHSSSSISSWIMLRLASQPAVVEELYQEQLANLERTGPNGSLAPLQYKDFDNLPLHQNVIRETLRLHSSIHSLLRKVKNPLPVPGTPYVIPTSHVLLAAPGVTALSDEYFPNAMAWDPHRWETQAPQENNKDDIVDYGYGAMSKGTSSPYLPFGAGRHRCIGEKFAYLNLAVIVATMVRHLRFSNLDGQTGVPDTDYSSLFSGPMKPARIRWERRAAKSG | 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, ChEBI:CHEBI:15740, ChEBI:CHEBI:57618, ChEBI:CHEBI:58210, ChEBI:CHEBI:138029, ChEBI:CHEBI:138031; EC=1.14.14.154; Evidence={ECO:0000250|UniProtKB:Q4WNT5}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:54029; Evidence={ECO:0000250|UniProtKB:Q4WNT5}; CATALYTIC ACTIVITY: Reaction=a 14alpha-methyl steroid + O2 + reduced [NADPH--hemoprotein reductase] = a 14alpha-hydroxymethyl steroid + H(+) + H2O + oxidized [NADPH--hemoprotein reductase]; Xref=Rhea:RHEA:68060, Rhea:RHEA-COMP:11964, Rhea:RHEA-COMP:11965, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, ChEBI:CHEBI:57618, ChEBI:CHEBI:58210, ChEBI:CHEBI:138029, ChEBI:CHEBI:176901; Evidence={ECO:0000250|UniProtKB:P10614}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:68061; Evidence={ECO:0000250|UniProtKB:P10614}; CATALYTIC ACTIVITY: Reaction=a 14alpha-hydroxymethyl steroid + O2 + reduced [NADPH--hemoprotein reductase] = a 14alpha-formyl steroid + H(+) + 2 H2O + oxidized [NADPH--hemoprotein reductase]; Xref=Rhea:RHEA:68064, Rhea:RHEA-COMP:11964, Rhea:RHEA-COMP:11965, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, ChEBI:CHEBI:57618, ChEBI:CHEBI:58210, ChEBI:CHEBI:176901, ChEBI:CHEBI:176902; Evidence={ECO:0000250|UniProtKB:P10614}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:68065; Evidence={ECO:0000250|UniProtKB:P10614}; CATALYTIC ACTIVITY: Reaction=a 14alpha-formyl steroid + O2 + reduced [NADPH--hemoprotein reductase] = a Delta(14) steroid + formate + 2 H(+) + H2O + oxidized [NADPH--hemoprotein reductase]; Xref=Rhea:RHEA:68068, Rhea:RHEA-COMP:11964, Rhea:RHEA-COMP:11965, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, ChEBI:CHEBI:15740, ChEBI:CHEBI:57618, ChEBI:CHEBI:58210, ChEBI:CHEBI:138031, ChEBI:CHEBI:176902; Evidence={ECO:0000250|UniProtKB:P10614}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:68069; Evidence={ECO:0000250|UniProtKB:P10614}; CATALYTIC ACTIVITY: Reaction=lanosterol + 3 O2 + 3 reduced [NADPH--hemoprotein reductase] = 4,4-dimethyl-5alpha-cholesta-8,14,24-trien-3beta-ol + formate + 4 H(+) + 4 H2O + 3 oxidized [NADPH--hemoprotein reductase]; Xref=Rhea:RHEA:25286, Rhea:RHEA-COMP:11964, Rhea:RHEA-COMP:11965, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, ChEBI:CHEBI:15740, ChEBI:CHEBI:16521, ChEBI:CHEBI:17813, ChEBI:CHEBI:57618, ChEBI:CHEBI:58210; EC=1.14.14.154; Evidence={ECO:0000250|UniProtKB:Q4WNT5}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:25287; Evidence={ECO:0000250|UniProtKB:Q4WNT5}; CATALYTIC ACTIVITY: Reaction=lanosterol + O2 + reduced [NADPH--hemoprotein reductase] = 32-hydroxylanosterol + H(+) + H2O + oxidized [NADPH--hemoprotein reductase]; Xref=Rhea:RHEA:75103, Rhea:RHEA-COMP:11964, Rhea:RHEA-COMP:11965, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, ChEBI:CHEBI:16521, ChEBI:CHEBI:57618, ChEBI:CHEBI:58210, ChEBI:CHEBI:166806; Evidence={ECO:0000250|UniProtKB:P10614}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:75104; Evidence={ECO:0000250|UniProtKB:P10614}; CATALYTIC ACTIVITY: Reaction=32-hydroxylanosterol + O2 + reduced [NADPH--hemoprotein reductase] = 32-oxolanosterol + H(+) + 2 H2O + oxidized [NADPH--hemoprotein reductase]; Xref=Rhea:RHEA:75107, Rhea:RHEA-COMP:11964, Rhea:RHEA-COMP:11965, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, ChEBI:CHEBI:57618, ChEBI:CHEBI:58210, ChEBI:CHEBI:166681, ChEBI:CHEBI:166806; Evidence={ECO:0000250|UniProtKB:P10614}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:75108; Evidence={ECO:0000250|UniProtKB:P10614}; CATALYTIC ACTIVITY: Reaction=32-oxolanosterol + O2 + reduced [NADPH--hemoprotein reductase] = 4,4-dimethyl-5alpha-cholesta-8,14,24-trien-3beta-ol + formate + 2 H(+) + H2O + oxidized [NADPH--hemoprotein reductase]; Xref=Rhea:RHEA:75111, Rhea:RHEA-COMP:11964, Rhea:RHEA-COMP:11965, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, ChEBI:CHEBI:15740, ChEBI:CHEBI:17813, ChEBI:CHEBI:57618, ChEBI:CHEBI:58210, ChEBI:CHEBI:166681; Evidence={ECO:0000250|UniProtKB:P10614}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:75112; Evidence={ECO:0000250|UniProtKB:P10614}; CATALYTIC ACTIVITY: Reaction=eburicol + 3 O2 + 3 reduced [NADPH--hemoprotein reductase] = 14-demethyleburicol + formate + 4 H(+) + 4 H2O + 3 oxidized [NADPH--hemoprotein reductase]; Xref=Rhea:RHEA:75439, Rhea:RHEA-COMP:11964, Rhea:RHEA-COMP:11965, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, ChEBI:CHEBI:15740, ChEBI:CHEBI:57618, ChEBI:CHEBI:58210, ChEBI:CHEBI:70315, ChEBI:CHEBI:194330; Evidence={ECO:0000250|UniProtKB:Q4WNT5}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:75440; Evidence={ECO:0000250|UniProtKB:Q4WNT5}; CATALYTIC ACTIVITY: Reaction=eburicol + O2 + reduced [NADPH--hemoprotein reductase] = 32-hydroxyeburicol + H(+) + H2O + oxidized [NADPH--hemoprotein reductase]; Xref=Rhea:RHEA:75427, Rhea:RHEA-COMP:11964, Rhea:RHEA-COMP:11965, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, ChEBI:CHEBI:57618, ChEBI:CHEBI:58210, ChEBI:CHEBI:70315, ChEBI:CHEBI:194328; Evidence={ECO:0000250|UniProtKB:P10614}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:75428; Evidence={ECO:0000250|UniProtKB:P10614}; CATALYTIC ACTIVITY: Reaction=32-hydroxyeburicol + O2 + reduced [NADPH--hemoprotein reductase] = 32-oxoeburicol + H(+) + 2 H2O + oxidized [NADPH--hemoprotein reductase]; Xref=Rhea:RHEA:75431, Rhea:RHEA-COMP:11964, Rhea:RHEA-COMP:11965, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, ChEBI:CHEBI:57618, ChEBI:CHEBI:58210, ChEBI:CHEBI:194328, ChEBI:CHEBI:194329; Evidence={ECO:0000250|UniProtKB:P10614}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:75432; Evidence={ECO:0000250|UniProtKB:P10614}; CATALYTIC ACTIVITY: Reaction=32-oxoeburicol + O2 + reduced [NADPH--hemoprotein reductase] = 14-demethyleburicol + formate + 2 H(+) + H2O + oxidized [NADPH--hemoprotein reductase]; Xref=Rhea:RHEA:75435, Rhea:RHEA-COMP:11964, Rhea:RHEA-COMP:11965, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, ChEBI:CHEBI:15740, ChEBI:CHEBI:57618, ChEBI:CHEBI:58210, ChEBI:CHEBI:194329, ChEBI:CHEBI:194330; Evidence={ECO:0000250|UniProtKB:P10614}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:75436; Evidence={ECO:0000250|UniProtKB:P10614}; | 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 involves the ergosterol synthesis itself through consecutive reactions that mainly occur in the endoplasmic reticulum (ER) membrane (By similarity). In filamentous fungi, during the initial step of this module, lanosterol (lanosta-8,24-dien-3beta-ol) can be metabolized to eburicol (By similarity). Sterol 14alpha-demethylase catalyzes the three-step oxidative removal of the 14alpha-methyl group (C-32) of both these sterols in the form of formate, and converts eburicol and lanosterol to 14-demethyleburicol (4,4,24-trimethylergosta-8,14,24(28)-trienol) and 4,4-dimethyl-5alpha-cholesta-8,14,24-trien-3beta-ol, respectively, which are further metabolized by other enzymes in the pathway to ergosterol (By similarity). Can also use substrates not intrinsic to fungi, such as 24,25-dihydrolanosterol (DHL), producing 4,4'-dimethyl-8,14-cholestadien-3-beta-ol, but at lower rates than the endogenous substrates (By similarity). {ECO:0000250|UniProtKB:P10613, ECO:0000250|UniProtKB:P10614, ECO:0000250|UniProtKB:Q4WNT5}.; FUNCTION: As a target of azole drugs, plays a crucial role in azole drug susceptibility. {ECO:0000269|PubMed:26248359, ECO:0000269|PubMed:29311090}. | Aspergillus flavus (strain ATCC 200026 / FGSC A1120 / IAM 13836 / NRRL 3357 / JCM 12722 / SRRC 167) |
B8PYG1 | NSMF_DANRE | MGTVVSKKENLRNDAISSVAAKVRAARAFGEYLSHTRPENRNRSDHLLSDTFIGQETDSPDISRLNNNNSLQPYSQHTLIVKPSQEELQQGSQSAPLPTSSKRRLSVERSLSSEDQQNQRRTESSVKPARVYTITRERDMLGGQGSEESLELEVLKRTSEPSQINPPTGLRGSHHRGSQHRGNNGPTHQHHYGHAPMAQPLQSSGSTHNIRDWGSRRSRSREDCTPDCVACIRPHCQSQRSLDLDTSPHGGGKQHKKLERMYSEDRVSSEDREDHTNSWFPKENMFSFQTATTTMQAISNFRKHLRMVGSRRVKAQTFVDRKAKSFSRSWSDPTPVKPDSLHDSRDSGDLQASSGNLDEEDCDDVDWEEERELERVACEGDDFIPPKLMLISSKVPKAEYVPNIIRRDDPSIIPILYDHEHATFDDILEEIEKKLTAYRKGCKIWNMLIFCQGGPGHLYLLKNKVATFAKVEKEEGMMQFWKKLGRFMSLLNPEPNLIHIMGCYVLGNANGEKLFQNLKRLMKPHGIEFKSPLELSAQGKEMIEMYFDFRLYRLWKTRQHSKLHDYDDLL | 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 projection, dendrite {ECO:0000250}. Synapse {ECO:0000250}. Synapse, synaptosome {ECO:0000250}. Postsynaptic density {ECO:0000250}. Membrane {ECO:0000250}. | 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|PubMed:19097186}. | Danio rerio (Zebrafish) (Brachydanio rerio) |
B8Q0B2 | POPD1_PIG | MNYTESSPLAESTAIGFTPELGSITPVPSNETTCENWREIHHLVFHVANVFFAIGLVLPTTLHLHMILLRGMLTIGCTLYIVWATLYRCALDIMIWNSVFLGINVLHLSYLLYKKRPVKIEKELKGIYQRLFEPLRVPPDLFKRLTGQFCMIQTLKKGQAYAAEDKTSVDDRLSILLKGKMKVSYRGHFLHNIYPCAFIDSPEFRSTQMHKGEKFQVTIIADDNCRFLCWSRERLTYFLESEPFLYEVFRYLIGKDITNKLYSLNDPTLNDKTIKKLDHQLSLCTQLSMLEMRNSIVSTSDSEDGLHQFLRGTSSVSSLYVPSPHQRASAKMKPIEEGVEDDDEVFEPETPNTFKVRQLP | 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 to ischemia [GO:0002931]; skeletal muscle tissue development [GO:0007519]; striated muscle cell differentiation [GO:0051146]; substrate adhesion-dependent cell spreading [GO:0034446]; vesicle-mediated transport [GO:0016192] | 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 membrane is an early event occurring concurrently with cell-cell contact. Detected at cell-cell contact but never observed at the free surface of epithelial cells. Colocalizes in epithelial cells with OCLN and TJP1 in an apical-lateral position within the z axis. Colocalizes with VAMP3 at the cell-cell contact in cardiac and skeletal muscle (By similarity). {ECO:0000250|UniProtKB:Q9ES83}. | 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 through its interaction with VAMP3. Plays a role in the regulation of cell shape and movement by modulating the Rho-family GTPase activity through its interaction with ARHGEF25/GEFT. Induces primordial adhesive contact and aggregation of epithelial cells in a Ca(2+)-independent manner. Important for skeletal muscle and heart development. Also involved in striated muscle regeneration and repair and in the regulation of cell spreading (By similarity). Important for the maintenance of cardiac function. Plays a regulatory function in heart rate dynamics mediated, at least in part, through cAMP-binding and, probably, by increasing cell surface expression of the potassium channel KCNK2 and enhancing current density. Is a caveolae-associated protein important for the preservation of caveolae structural and functional integrity as well as for heart protection against ischemia injury (By similarity). {ECO:0000250|UniProtKB:Q5PQZ7, ECO:0000250|UniProtKB:Q8NE79, ECO:0000250|UniProtKB:Q9ES83}. | 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:0007422]; positive regulation of collateral sprouting [GO:0048672]; positive regulation of peptidyl-serine phosphorylation [GO:0033138]; regulation of neuron differentiation [GO:0045664]; transmembrane receptor protein tyrosine kinase signaling pathway [GO:0007169] | 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 clear. However, it has been shown to inhibit metalloproteinase-dependent proteolysis of platelet glycoprotein Ib alpha, suggesting a metalloproteinase inhibition to prevent metalloprotease autodigestion and/or protection against prey proteases (By similarity). Binds a lipid between the two protein chains in the homodimer. The lipid-bound form promotes histamine relase from mouse mast cells, contrary to the lipid-free form (By similarity). {ECO:0000250|UniProtKB:P61898, ECO:0000250|UniProtKB:P61899}. | Agkistrodon contortrix contortrix (Southern copperhead) |
B8QHP1 | CP52M_STABO | MLIKDIILTPMSLSAVAGLLPLLFVAFLVLHEPIWLLWYRYAARRHKCSMPRFIEKSFPLGIQRTMDMIKTAKSYTLLEVQYDRVFNKFKARTYLRQAPLQYQIFTIEPENIKTILATKFNDFGLGARFHTVGKVFGQGIFTLSGNGWKQSRSMLRPQFTKDQVCRIDQISSHAAELIKEMNRAMKVDQFIDVQHYFHKLTLDTATEFLFGESCESLNPENQSCIVARDGSEITAEQFVESYNFLLNYAFKRTLSSKVYWLFNSKEFRDHKKRAQSYIDYYVDKALYATSFAAENSIAEKDAAAESSGIYVFSLEMAKVTRDPVTIRDQIFNILIAGRDTTAATLSFAIHFLARNPDVFNKLREEVLDHFGTKEEQRPLSFELLKQAPYLKQVINEVLRLAPVLPLNFRTAVRDTTLPIGGGPEQKDPIFVPKGTAVYYSIYMVHRDIKYWGPDAHEFNPNRWENLKLDNVWAFLPFNGGPRICLGQQFALTELSLTLVRLLQEYSKIEMGPDFPESPRFSTTLTAQHAPPGVVVRFS | 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:CHEBI:15379, ChEBI:CHEBI:57618, ChEBI:CHEBI:58210, ChEBI:CHEBI:140991, ChEBI:CHEBI:140992; EC=1.14.14.80; Evidence={ECO:0000269|PubMed:23516968, ECO:0000269|PubMed:24242247}; CATALYTIC ACTIVITY: Reaction=an (omega-1)-ethyl fatty acid + O2 + reduced [NADPH--hemoprotein reductase] = an (omega-1)-hydroxy-long-chain fatty acid + H(+) + H2O + oxidized [NADPH--hemoprotein reductase]; Xref=Rhea:RHEA:60936, Rhea:RHEA-COMP:11964, Rhea:RHEA-COMP:11965, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, ChEBI:CHEBI:57618, ChEBI:CHEBI:58210, ChEBI:CHEBI:84493, ChEBI:CHEBI:144045; Evidence={ECO:0000269|PubMed:23516968, ECO:0000269|PubMed:24242247}; CATALYTIC ACTIVITY: Reaction=(9Z)-octadecenoate + O2 + reduced [NADPH--hemoprotein reductase] = 18-hydroxy-(9Z)-octadecenoate + H(+) + H2O + oxidized [NADPH--hemoprotein reductase]; Xref=Rhea:RHEA:41728, Rhea:RHEA-COMP:11964, Rhea:RHEA-COMP:11965, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, ChEBI:CHEBI:30823, ChEBI:CHEBI:57618, ChEBI:CHEBI:58210, ChEBI:CHEBI:78424; EC=1.14.14.80; Evidence={ECO:0000269|PubMed:24242247}; CATALYTIC ACTIVITY: Reaction=(9Z)-octadecenoate + O2 + reduced [NADPH--hemoprotein reductase] = 17-hydroxy-(9Z)-octadecenoate + H(+) + H2O + oxidized [NADPH--hemoprotein reductase]; Xref=Rhea:RHEA:60928, Rhea:RHEA-COMP:11964, Rhea:RHEA-COMP:11965, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, ChEBI:CHEBI:30823, ChEBI:CHEBI:57618, ChEBI:CHEBI:58210, ChEBI:CHEBI:144040; Evidence={ECO:0000269|PubMed:24242247}; CATALYTIC ACTIVITY: Reaction=(9Z,12Z)-octadecadienoate + O2 + reduced [NADPH--hemoprotein reductase] = 18-hydroxy-(9Z,12Z)-octadecadienoate + H(+) + H2O + oxidized [NADPH--hemoprotein reductase]; Xref=Rhea:RHEA:60580, Rhea:RHEA-COMP:11964, Rhea:RHEA-COMP:11965, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, ChEBI:CHEBI:30245, ChEBI:CHEBI:57618, ChEBI:CHEBI:58210, ChEBI:CHEBI:132029; Evidence={ECO:0000269|PubMed:24242247}; CATALYTIC ACTIVITY: Reaction=(9Z,12Z)-octadecadienoate + O2 + reduced [NADPH--hemoprotein reductase] = 17-hydroxy-(9Z,12Z)-octadecadienoate + H(+) + H2O + oxidized [NADPH--hemoprotein reductase]; Xref=Rhea:RHEA:60932, Rhea:RHEA-COMP:11964, Rhea:RHEA-COMP:11965, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, ChEBI:CHEBI:30245, ChEBI:CHEBI:57618, ChEBI:CHEBI:58210, ChEBI:CHEBI:144041; Evidence={ECO:0000269|PubMed:24242247}; CATALYTIC ACTIVITY: Reaction=hexadecanoate + O2 + reduced [NADPH--hemoprotein reductase] = 16-hydroxyhexadecanoate + H(+) + H2O + oxidized [NADPH--hemoprotein reductase]; Xref=Rhea:RHEA:40199, Rhea:RHEA-COMP:11964, Rhea:RHEA-COMP:11965, ChEBI:CHEBI:7896, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, ChEBI:CHEBI:55329, ChEBI:CHEBI:57618, ChEBI:CHEBI:58210; EC=1.14.14.80; Evidence={ECO:0000269|PubMed:24242247}; CATALYTIC ACTIVITY: Reaction=(9Z)-hexadecenoate + O2 + reduced [NADPH--hemoprotein reductase] = (9Z)-16-hydroxyhexadec-9-enoate + H(+) + H2O + oxidized [NADPH--hemoprotein reductase]; Xref=Rhea:RHEA:60940, Rhea:RHEA-COMP:11964, Rhea:RHEA-COMP:11965, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, ChEBI:CHEBI:32372, ChEBI:CHEBI:57618, ChEBI:CHEBI:58210, ChEBI:CHEBI:144048; Evidence={ECO:0000269|PubMed:24242247}; CATALYTIC ACTIVITY: Reaction=O2 + octadecanoate + reduced [NADPH--hemoprotein reductase] = 18-hydroxyoctadecanoate + H(+) + H2O + oxidized [NADPH--hemoprotein reductase]; Xref=Rhea:RHEA:46356, Rhea:RHEA-COMP:11964, Rhea:RHEA-COMP:11965, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, ChEBI:CHEBI:25629, ChEBI:CHEBI:57618, ChEBI:CHEBI:58210, ChEBI:CHEBI:86046; EC=1.14.14.80; Evidence={ECO:0000269|PubMed:24242247}; | 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 enzyme for linoleic acid {ECO:0000269|PubMed:24242247}; Vmax=306 pmol/min/mg enzyme for arachidonic acid {ECO:0000269|PubMed:24242247}; | 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 acid is the preferred substrate, but it acts on various other C-16, C-18 and C-20 saturated and unsaturated fatty acids, namely palmitic, palmitoleic, stearic, linoleic, cis-9,10-epoxystearic, trans-9,10-epoxystearic and arachidonic acid (PubMed:24242247). {ECO:0000269|PubMed:23516968, ECO:0000269|PubMed:24242247}. | Starmerella bombicola (Yeast) (Candida bombicola) |
B8QSK0 | GNACT_ECOLX | MKIAYVVSSKKKCGPNIVILNIVKELANKHEMEIFFLDESDDDVFECVNVKSTQIKKASDLKEHLKRFDIIHSSGIRPDALVVLCKVIYRVKCKIITTIHNYVFQDLYYSYGLVKSLIWGLLWCSIWLFFDKLVILSKNADNYYWFLPSAKKNIIYNGIDDNDCLQNKKCNYRKEFNIPDDGILAGSCANLTKCKGIDLVIQTLTKEHKIYYIVAGDGIEKHNLINLVKARKLHERVYFIDFLDEPESFMSQLDVFLMPSRSEGFGLTVLESTKLGIPVITSNIPIFMELFDQMCLTFDIKNPSTLIDVITYAKKNRLHLSQKFHAIFQDRFTSSKMATKYENVYNNLFREVL | 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 its own transcript and its cognate antitoxin RNA ToxI. ToxI has 5.5 nearly identical 36 nucleotide-long repeats (a single repeat neutralizes the toxin in vivo); a single repeat folds into a pseudoknot which binds the toxin (PubMed:21240270). The ToxI precursor RNA is a preferential target in vivo and is progressively degraded to single repeat lengths as ToxN-ToxI complex self-assembly occurs (PubMed:23267117). In vivo expression of ToxI antitoxin inhibits endonuclease activity of ToxN (PubMed:23267117). The toxin alone inhibits growth when expressed in E.coli without causing cell lysis; this bacteriostatic effect is neutralized by cognate RNA antitoxin ToxI (PubMed:19124776, PubMed:23267117). Non-cognate antitoxin RNA from B.thuringiensis does not inhibit this toxin (PubMed:23267117). The RNA antitoxin is less stable than the proteinaceous toxin; synthesis of ToxI in the absence of new ToxN synthesis restores growth and also detectable accumulation of the ToxN protein (PubMed:19124776). Negatively regulates its own operon in complex with ToxI (PubMed:19633081). The toxin-antitoxin system functions in plasmid maintenance (a plasmid addiction system) (PubMed:23267117). {ECO:0000269|PubMed:19124776, ECO:0000269|PubMed:19633081, ECO:0000269|PubMed:21240270, ECO:0000269|PubMed:23267117}.; FUNCTION: The TA system protects P.atrosepticum strain 1043 against phage phiM1 and phiA2, E.coli against some but not all coliphages and S.marcescens against some bacteriophages, causing an abortive infection (Abi phenotype) (PubMed:19124776). Also protects P.atrosepticum strain 1043 against phage phiTE; phage that escape Abi and grow in this bacterium have evolved a pseudo-ToxI RNA by expanding a pre-existing sequence similar to the bona fide ToxI repeats (PubMed:23109916). {ECO:0000269|PubMed:19124776, ECO:0000269|PubMed:23109916}. | Pectobacterium atrosepticum (Erwinia carotovora subsp. atroseptica) |
B8XCH5 | QKY_ARATH | MNTTPFHSDPPPSRIQRKLVVEVVEARNILPKDGQGSSSAYVVVDFDAQKKRTSTKFRDLNPIWNEMLDFAVSDPKNMDYDELDIEVYNDKRFGNGGGRKNHFLGRVKIYGSQFSRRGEEGLVYFPLEKKSVFSWIRGEIGLKIYYYDEAADEDTAGGGGGQQQQQQQQQFHPPQQEADEQQHQQQFHPPPQQMMNIPPEKPNVVVVEEGRVFESAQSQRYTETHQQPPVVIVEESPPQHVMQGPNDNHPHRNDNHPQRPPSPPPPPSAGEVHYYPPEVRKMQVGRPPGGDRIRVTKRPPNGDYSPRVINSKTGGGETTMEKKTHHPYNLVEPMQYLFVRIVKARGLPPNESAYVKVRTSNHFVRSKPAVNRPGESVDSPEWNQVFALGHNRSDSAVTGATLEISAWDASSESFLGGVCFDLSEVPVRDPPDSPLAPQWYRLEGSGADQNSGRISGDIQLSVWIGTQVDEAFPEAWSSDAPHVAHTRSKVYQSPKLWYLRVTVLEAQDLHIAPNLPPLTAPEIRVKAQLGFQSARTRRGSMNNHSGSFHWHEDMIFVAGEPLEDCLVLMVEDRTTKEATLLGHAMIPVSSIEQRIDERFVPSKWHTLEGEGGGGGGGGGPGGGGGGGPYCGRISLRLCLEGGYHVLEEAAHVCSDFRPTAKQLWKPPIGILELGILGARGLLPMKAKNGGKGSTDAYCVAKYGKKWVRTRTITDSFDPRWHEQYTWQVYDPCTVLTVGVFDNWRMFSDASDDRPDTRIGKIRIRVSTLESNKVYTNSYPLLVLLPSGMKKMGEIEVAVRFACPSLLPDVCAAYGQPLLPRMHYIRPLGVAQQDALRGAATKMVAAWLARAEPPLGPEVVRYMLDADSHAWSMRKSKANWYRIVGVLAWAVGLAKWLDNIRRWRNPVTTVLVHILYLVLVWYPDLVVPTAFLYVVMIGVWYYRFRPKIPAGMDIRLSQAETVDPDELDEEFDTIPSSRRPEVIRARYDRLRILAVRVQTILGDFAAQGERIQALVSWRDPRATKLFIAICLVITIVLYAVPAKMVAVALGFYYLRHPMFRDTMPTASLNFFRRLPSLSDRLI | 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|PubMed:25256344}. | 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 cell growth anisotropy during gynoecium development, thus linking together cell-cell communication and cellular growth (PubMed:24173806). Together with SUB/SCM, links RLK-dependent signal transduction and intercellular communication mediated by plasmodesmata (PD) to regulate tissue morphogenesis (PubMed:25256344). May function as a signaling molecule by regulating the trafficking of other regulators (PubMed:29259105). {ECO:0000269|PubMed:19180193, ECO:0000269|PubMed:24173806, ECO:0000269|PubMed:25256344, ECO:0000303|PubMed:20298225, ECO:0000303|PubMed:29259105}. | Arabidopsis thaliana (Mouse-ear cress) |
B8XIA5 | MYC_MACMU | MDFFPVVENQQPPATMPLNVSFTNRNYDLDYDSVQPYFYCDEEENFYQQQQQSELQPPAPSEDIWKKFELLPTPPLSPSRRSGLCSPSYVAVTPFSPRGDNDGGGGSFSTADQLEMVTELLGGDMVNQSFICDPDDETFIKNIIIQDCMWSGFSAAAKLVSEKLASYQAARKDSGSPNPARGHSVCSTSSLYLQDLSAAASECIDPSVVFPYPLNDSSSPKSCASPDSSAFSPSSDSLLSSTESSPQASPEPLVLHEETPPTTSSDSEEEQEEEEEIDVVSVEKRQAPGKRSESGSPSAGGHSKPPHSPLVLKRCHVSTHQHNYAAPPSTRKDYPAAKRVKLDSVRVLRQISNNRKCTSPRSSDTEENDKRRTHNVLERQRRNELKRSFFALRDQIPELENNEKAPKVVILKKATAYILSVQAEEQKLISEKDLLRKRREQLKHKLEQLRNSCA | 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 division [GO:0051782]; negative regulation of monocyte differentiation [GO:0045656]; negative regulation of stress-activated MAPK cascade [GO:0032873]; positive regulation of cell population proliferation [GO:0008284]; positive regulation of cysteine-type endopeptidase activity involved in apoptotic process [GO:0043280]; positive regulation of DNA-templated transcription [GO:0045893]; positive regulation of epithelial cell proliferation [GO:0050679]; positive regulation of fibroblast proliferation [GO:0048146]; positive regulation of transcription by RNA polymerase II [GO:0045944]; regulation of DNA-templated transcription [GO:0006355]; regulation of somatic stem cell population maintenance [GO:1904672]; regulation of telomere maintenance [GO:0032204]; regulation of transcription by RNA polymerase II [GO:0006357]; response to gamma radiation [GO:0010332]; response to xenobiotic stimulus [GO:0009410] | 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. Phosphorylation at Thr-73 and Ser-77 by GSK3 is required for ubiquitination and degradation by the proteasome. Dephosphorylation at Ser-77 by protein phosphatase 2A (PPP2CA) promotes its degradation; interaction with PPP2CA is enhanced by AMBRA1 (By similarity). {ECO:0000250|UniProtKB:P01106, ECO:0000250|UniProtKB:P01108}.; PTM: Ubiquitinated by the SCF(FBXW7) complex when phosphorylated at Thr-73 and Ser-77, leading to its degradation by the proteasome. Ubiquitination is counteracted by USP28 in the nucleoplasm and USP36 in the nucleolus, both interacting with of FBXW7, leading to its deubiquitination and preventing degradation. Also polyubiquitinated by the DCX(TRPC4AP) complex. Ubiquitinated by TRIM6 in a phosphorylation-independent manner. {ECO:0000250|UniProtKB:P01106, ECO:0000250|UniProtKB:P01108}. | 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 reprogramming, controls self-renewal of embryonic stem cells. Functions with TAF6L to activate target gene expression through RNA polymerase II pause release (By similarity). Positively regulates transcription of HNRNPA1, HNRNPA2 and PTBP1 which in turn regulate splicing of pyruvate kinase PKM by binding repressively to sequences flanking PKM exon 9, inhibiting exon 9 inclusion and resulting in exon 10 inclusion and production of the PKM M2 isoform (By similarity). {ECO:0000250|UniProtKB:P01106, ECO:0000250|UniProtKB:P01108}. | Macaca mulatta (Rhesus macaque) |
B8XTP8 | POLG_COSAA | MGANNSKESVSSNGNEGTIVNNFYSNQYYASIDASAQGVGTSTTPENGNVSGFLGLAGSAFNALSLLASPRTETGMMMEDRVLSRTAGNTSVNSQAAEGVLQAYGTETDSNSPTSCGDDPSKGTHATDRAFVIQLLPWKQTTNSYFAQWVRLTQKLSNNLHGNVMAKNIKSHAFAKMGFEVMLQANTSPFHNGILGLFLVPEFVRKGEITDEWIDLTPTSSLVSNTELYNPQTYANFPFDAKHSFDYSDITPEQFMIFPHQLINPKDTNVATVRVPYINIAPTNDTTVHTVWTAVVMVLVPLNFSSGASPTVSLTLTITPINSVFNGLHHTAQGPIPVRPFHNFQQFSTTVPLRTEPCYGMTVTPPVDYMPLPITDLVELAKVPSFVTVANSDTTSERSFPYFSVSNTEQGRNLFKSSVVLSDLHYQHTLVANLARYFCNYRGSLQFDFIAATTAMTRGKLLISYTPPGAGEPQSIDQAMMGTYAIWDLGLQSTFNFVVPFISASDFRFNTSSVSNALNSDGWITVWLMNPLTYPPSTPPTQQILMLMSAGSDFSYRLPISPGFAEGETSEHPMDNAECGKIDDKDAGMFSGHSVGLPTPHTSTSFFYDRYRFVGIVKSVVNNTPKPVNIYDDTGKVKNLQQVFPTSDTLLPHSLMSLSPCASVCGQPISSFLFAQRANPKKTLKLRSGDEFLYRCCPFSYIKCDLEFTVVPPANSTRDYIVHWYPPGATLDAGEVAVGNTSGSNGFDDNGMNAGSSLFSYNPTFHARAPSKVSAVIPFCLPVSLLPLYFDGFPDYSTTKGMYGCSPSFSFGTIYIESGLQETYSVYIRYKDFKGYAPRPLIRTPHIRLSERARYIMADSVLPRPLTRAERDVARDLLLIAGDIESNPGPAFNPEYTAHGPVTELIQLARKPETVDNVNRLLTTLNTLMAKWNNLKDTVTDAVFLRDMVCLLVKLTSLMYLVHGQGPGAYFAAASILLADGITFFDWYEKIKIFMARKLRVSPPFFPAAQGPDLRDFVTFFNAARGAQWMIDSLKSLITCIKQWLELEEENEAVQLEKMLIDSPRHCKAINDYNRGDSFQRPTNSFEFMDRLVECATKLGKVQIATYFRNFTTADSDTSRPEPVVVVLRGKPGVGKSAAATVMAAAVSKLLVGSQSVYTLSPDTEHMDGYHGQFVTLMDDLGQNPDGEDFRCFCQMVSCAQYRPAMADLKDKGILFTSRLLIATTNLPDFNPVTISDPRALDRRITFDILVTPGSAATKNGKLDLAAALKPDGPGEHPYTSDCPILHTTGLLLKNLRNNQTMNLKDLVDMIVKRIKHKKEVGNMLDSLVAQGPTMIVGYTKDDDGIAIVDCLEEWNKIKDKKKKQLALEMVAQELKDKHEEHKGTIKLLKMFVTGLGVVAAVAGAYATMKYFTKDKPKEEEEEPEEKKEKKTEESKEAAGPYNGPTKKEIKTLKLKAQSPLMDMEKKIAQNVMPFQIFYNGKRYTQSCLAIGKRVILVNKHAFESVEHKFVVDQKEYTLDQVTAISLDCGSGVTDVCAVCLPPGPDFKSIKKHFLPFNTTMFPGTRLTILSNDHYPMSREGSFLRFEDEVPTNVGNMPFVMLYKSTSYFGMCGSVVCSRFVDGGGIIGMHCAGGGGVSVGTRLTARMIESVFDYFYPPVAQGIIENTETGPRVHVPRTSKLKRTNATYPATEKYGPAALSRYDPRLNEGVNLDEVIFSKHTQNTLVEKGSTFRSALDMAAEIYGEKFRGNDFSPLSVEDAILGIPGLDRLDPNTASGLPYTKTRRQMIDFNTGQILDDTLKCRLGQWLAGRPPQEVHYQTFLKDEIRPIEKVKAGKTRIIDVPPLDHVIAFRMLFGRFIAHYHLNFGFKTGSAIGCDPDVAWASFGFELSGFPYLYDFDYSNFDASHSTSIFEILEQKFFSPELGFDPRCSLLLKSLAVSTHCYENKRLQIAGGLPSGTAGTSVLNTVINNIIFHGALYHTYTNFERDDISMLAYGDDIVVASKFELDLVMVKAFMNRIGYKITPADKSDEFRPKCMDDICFLKRRFVKVAGVWAPVMETENLEAMLSWYKPGTLNEKLQSVSRLAHFSGRDVYDHLFKPFIRDGFDVTPWKQLHLEWLNKLSA | 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 similarity). This process would release the P1-2A peptide from the translational complex (By similarity). {ECO:0000250|UniProtKB:P03304}.; PTM: [Capsid protein VP0]: During virion maturation, immature virions are rendered infectious following cleavage of VP0 into VP4 and VP2. This maturation seems to be an autocatalytic event triggered by the presence of RNA in the capsid and is followed by a conformational change of the particle. {ECO:0000250|UniProtKB:P03300}.; PTM: [Capsid protein VP4]: Myristoylation is required during RNA encapsidation and formation of the mature virus particle. {ECO:0000250|UniProtKB:Q66282}.; PTM: [VPg]: Uridylylated by the polymerase and is covalently linked to the 5'-end of genomic RNA. This uridylylated form acts as a nucleotide-peptide primer for the polymerase. {ECO:0000250|UniProtKB:P12296}. | 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 cytoplasm {ECO:0000305}.; SUBCELLULAR LOCATION: [Protein 2A]: Host nucleus, host nucleolus {ECO:0000250|UniProtKB:Q66765}.; SUBCELLULAR LOCATION: [Protein 2B]: Host cytoplasmic vesicle membrane {ECO:0000250|UniProtKB:Q66765}; Peripheral membrane protein {ECO:0000250|UniProtKB:Q66765}; Cytoplasmic side {ECO:0000250|UniProtKB:Q66765}. Note=Probably localizes to the surface of intracellular membrane vesicles that are induced after virus infection as the site for viral RNA replication. These vesicles are probably autophagosome-like vesicles. {ECO:0000305}.; SUBCELLULAR LOCATION: [Protein 2C]: Host cytoplasmic vesicle membrane {ECO:0000250|UniProtKB:Q66765}; Peripheral membrane protein {ECO:0000250|UniProtKB:Q66765}; Cytoplasmic side {ECO:0000250|UniProtKB:Q66765}. Note=Probably localizes to the surface of intracellular membrane vesicles that are induced after virus infection as the site for viral RNA replication. These vesicles are probably autophagosome-like vesicles. {ECO:0000305}.; SUBCELLULAR LOCATION: [Protein 3A]: Host cytoplasmic vesicle membrane {ECO:0000250|UniProtKB:P03304}; Peripheral membrane protein {ECO:0000305}; Cytoplasmic side {ECO:0000305}. Note=Probably localizes to the surface of intracellular membrane vesicles that are induced after virus infection as the site for viral RNA replication. These vesicles are probably autophagosome-like vesicles. {ECO:0000250|UniProtKB:P03304}.; SUBCELLULAR LOCATION: [VPg]: Virion {ECO:0000305}.; SUBCELLULAR LOCATION: [Protease 3C]: Host cytoplasm {ECO:0000305}.; SUBCELLULAR LOCATION: [RNA-directed RNA polymerase]: Host cytoplasmic vesicle membrane {ECO:0000250|UniProtKB:Q66765}; Peripheral membrane protein {ECO:0000250|UniProtKB:Q66765}; Cytoplasmic side {ECO:0000250|UniProtKB:Q66765}. Note=Probably localizes to the surface of intracellular membrane vesicles that are induced after virus infection as the site for viral RNA replication. These vesicles are probably autophagosome-like vesicles. {ECO:0000305}. | 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 + H2O = ADP + H(+) + phosphate; Xref=Rhea:RHEA:13065, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:456216; EC=3.6.4.13; Evidence={ECO:0000305}; CATALYTIC ACTIVITY: Reaction=Selective cleavage of Gln-|-Gly bond in the poliovirus polyprotein. In other picornavirus reactions Glu may be substituted for Gln, and Ser or Thr for Gly.; EC=3.4.22.28; Evidence={ECO:0000255|PROSITE-ProRule:PRU01222}; | 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, VP2 and VP3. All the three latter proteins contain a beta-sheet structure called beta-barrel jelly roll. VP1 is situated at the 12 fivefold axes, whereas VP2 and VP3 are located at the quasi-sixfold axes. {ECO:0000250|UniProtKB:P12296}.; FUNCTION: [Capsid protein VP2]: 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, VP2 and VP3. All the three latter proteins contain a beta-sheet structure called beta-barrel jelly roll. VP1 is situated at the 12 fivefold axes, whereas VP2 and VP3 are located at the quasi-sixfold axes. {ECO:0000250|UniProtKB:P12296}.; FUNCTION: [Capsid protein VP3]: 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, VP2 and VP3. All the three latter proteins contain a beta-sheet structure called beta-barrel jelly roll. VP1 is situated at the 12 fivefold axes, whereas VP2 and VP3 are located at the quasi-sixfold axes. {ECO:0000250|UniProtKB:P12296}.; FUNCTION: [Capsid protein VP4]: Lies on the inner surface of the capsid shell (By similarity). After binding to the host receptor, the capsid undergoes conformational changes (By similarity). Capsid protein VP4 is released, capsid protein VP1 N-terminus is externalized, and together, they shape a pore in the host membrane through which the viral genome is translocated into the host cell cytoplasm (By similarity). After genome has been released, the channel shrinks (By similarity). {ECO:0000250|UniProtKB:P03300, ECO:0000250|UniProtKB:P12296}.; FUNCTION: [Capsid protein VP0]: VP0 precursor is a component of immature procapsids. {ECO:0000250|UniProtKB:P08617}.; FUNCTION: [Protein 2A]: Involved in host translation shutoff by inhibiting cap-dependent mRNA translation (By similarity). Nuclear localization is required for this function (By similarity). The resulting inhibition of cellular protein synthesis serves to ensure maximal viral gene expression and to evade host immune response (By similarity). {ECO:0000250|UniProtKB:Q66765}.; FUNCTION: [Protein 2B]: Affects membrane integrity and causes an increase in membrane permeability. {ECO:0000250}.; FUNCTION: [Protein 2C]: Associates with and induces structural rearrangements of intracellular membranes (By similarity). It displays RNA-binding, nucleotide binding and NTPase activities (By similarity). Interacts with IFIH1/MDA5 to inhibit the induction of the IFN-beta signal pathway (By similarity). {ECO:0000250|UniProtKB:P03304, ECO:0000250|UniProtKB:P03305, ECO:0000250|UniProtKB:P08545}.; FUNCTION: [Protein 3A]: Serves as membrane anchor via its hydrophobic domain. {ECO:0000250}.; FUNCTION: [VPg]: Forms a primer, VPg-pU, which is utilized by the polymerase for the initiation of RNA chains. {ECO:0000250|UniProtKB:P03304}.; FUNCTION: [Protease 3C]: Cysteine protease that generates mature viral proteins from the precursor polyprotein (By similarity). In addition to its proteolytic activity, it binds to viral RNA, and thus influences viral genome replication. RNA and substrate cooperatively bind to the protease. Cleaves host PABP1, this cleavage is important for viral replication (By similarity). Cleaves host TANK and disrupts the TANK-TBK1-IKKepsilon-IRF3 complex, thereby inhibiting the induction of the IFN-beta signal pathway (By similarity). {ECO:0000250|UniProtKB:P03304, ECO:0000250|UniProtKB:P12296}.; FUNCTION: [RNA-directed RNA polymerase]: Replicates the genomic and antigenomic RNAs by recognizing replications specific signals (By similarity). Performs VPg uridylylation (By similarity). {ECO:0000250|UniProtKB:P12296}. | Cosavirus A (isolate Human/Pakistan/0553/-) (HCoSV-A) |
B8XX90 | STING_PIG | MPYSSLHPSIPQPRGLRAQVAALVLLGACLVALWGLGELPEYTLRWLVLHLASQQIGLLVKGLCSLAEELCHVHSRYQSSYWRAARACLGCPIRCGALLLLSCYFYFSIRDKAGLPLPWMLALLGLSQALNILLGLQHLAPAEVSAICEKRNFNVAHGLAWSYYIGYLRLILPGLRARIQAYNQRHKNVLGGIGNHRLHILFPLDCGVPDDLSVADPNIRFLHELPQQSADRAGIKGRVYTNSIYELLENGQPAGVCVLGYATPLQTLFAMSQDGRAGFSREDRLEQAKLFCRTLEDILADAPEAQNNCRLIVYQEPTEGGSFSLSQEILRHLRQEEREVTMGSAETSVVPTSSTLSQEPELLISGMEQPLPLRSDIF | 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:0016239]; positive regulation of type I interferon production [GO:0032481]; reticulophagy [GO:0061709] | 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]; perinuclear region of cytoplasm [GO:0048471]; plasma membrane [GO:0005886] | 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 motif, leading to recruitment of the transcription factor IRF3 to induce type-I interferons and other cytokines (By similarity). Phosphorylated on tyrosine residues upon MHC-II aggregation (By similarity). Dephosphorylation by PPP6C leads to inactivation and decreased production of IFN-beta (By similarity). Phosphorylation at Ser-357 is also required to activate IRF3 (By similarity). Phosphorylation at Ser-354 by MAP3K7/TAK1 facilitates its interaction with STEEP1, promoting STING1 translocation to COPII vesicles (By similarity). {ECO:0000250|UniProtKB:Q3TBT3, ECO:0000250|UniProtKB:Q86WV6}.; PTM: Ubiquitinated (By similarity). Ubiquitinated via 'Lys-63'-linked ubiquitin chains in response to double-stranded DNA treatment, leading to relocalization to autophagosomes and subsequent degradation; this process is dependent on SQSTM1 (By similarity). 'Lys-63'-linked ubiquitination mediated by TRIM56 at Lys-150 promotes homodimerization and recruitment of the antiviral kinase TBK1 and subsequent production of IFN-beta. 'Lys-48'-linked polyubiquitination at Lys-150 occurring after viral infection is mediated by RNF5 and leads to proteasomal degradation. 'Lys-11'-linked polyubiquitination at Lys-150 by RNF26 leads to stabilize STING1: it protects STING1 from RNF5-mediated 'Lys-48'-linked polyubiquitination (By similarity). 'Lys-33'-linked and 'Lys-48'-linked deubiquitinated by USP20; leading to its stabilization and promotion of innate antiviral response (By similarity). 'Lys-48'-linked deubiquitinated by USP44; leading to its stabilization and promotion of innate antiviral response (By similarity). Deubiquitinated by USP13; leading to inhibition of innate antiviral response (By similarity). 'Lys-63'-linked deubiquitinated by USP49; leading to inhibition of the subsequent recruitment of TBK1 to the signaling complex (By similarity). {ECO:0000250|UniProtKB:Q3TBT3, ECO:0000250|UniProtKB:Q86WV6}.; PTM: Palmitoylation takes place in the Golgi apparatus and creates a platform for the recruitment of TBK1. {ECO:0000250|UniProtKB:Q3TBT3}. | 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:0000250|UniProtKB:Q86WV6}; Multi-pass membrane protein {ECO:0000255}. Golgi apparatus membrane {ECO:0000250|UniProtKB:Q86WV6}; Multi-pass membrane protein {ECO:0000255}. Cytoplasmic vesicle, autophagosome membrane {ECO:0000250|UniProtKB:Q86WV6}; Multi-pass membrane protein {ECO:0000255}. Mitochondrion outer membrane {ECO:0000269|PubMed:20346968}; Multi-pass membrane protein {ECO:0000255}. Cell membrane {ECO:0000250|UniProtKB:Q3TBT3}; Multi-pass membrane protein {ECO:0000255}. Note=In response to double-stranded DNA stimulation, translocates from the endoplasmic reticulum through the endoplasmic reticulum-Golgi intermediate compartment and Golgi to post-Golgi vesicles, where the kinase TBK1 is recruited. Upon cGAMP-binding, translocates to the endoplasmic reticulum-Golgi intermediate compartment (ERGIC) in a process that is dependent on COPII vesicles; STING1-containing ERGIC serves as a membrane source for LC3 lipidation, which is a key step in autophagosome biogenesis. Localizes in the lysosome membrane in a TMEM203-dependent manner. {ECO:0000250|UniProtKB:Q3TBT3, ECO:0000250|UniProtKB:Q86WV6}. | 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 delivered to the cytoplasm (By similarity). Acts by binding cyclic dinucleotides: recognizes and binds cyclic di-GMP (c-di-GMP), a second messenger produced by bacteria, cyclic UMP-AMP (2',3'-cUAMP), and cyclic GMP-AMP (cGAMP), a messenger produced by CGAS in response to DNA virus in the cytosol (By similarity). Upon binding to c-di-GMP, cUAMP or cGAMP, STING1 oligomerizes, translocates from the endoplasmic reticulum and is phosphorylated by TBK1 on the pLxIS motif, leading to recruitment and subsequent activation of the transcription factor IRF3 to induce expression of type I interferon and exert a potent anti-viral state (By similarity). Exhibits 2',3' phosphodiester linkage-specific ligand recognition: can bind both 2'-3' linked cGAMP (2'-3'-cGAMP) and 3'-3' linked cGAMP but is preferentially activated by 2'-3' linked cGAMP (PubMed:31167783). The preference for 2'-3'-cGAMP, compared to other linkage isomers is probably due to the ligand itself, whichs adopts an organized free-ligand conformation that resembles the STING1-bound conformation and pays low energy costs in changing into the active conformation (By similarity). In addition to promote the production of type I interferons, plays a direct role in autophagy (By similarity). Following cGAMP-binding, STING1 buds from the endoplasmic reticulum into COPII vesicles, which then form the endoplasmic reticulum-Golgi intermediate compartment (ERGIC) (By similarity). The ERGIC serves as the membrane source for WIPI2 recruitment and LC3 lipidation, leading to formation of autophagosomes that target cytosolic DNA or DNA viruses for degradation by the lysosome (By similarity). Promotes autophagy by acting as a proton channel that directs proton efflux from the Golgi to facilitate MAP1LC3B/LC3B lipidation (By similarity). The autophagy- and interferon-inducing activities can be uncoupled and autophagy induction is independent of TBK1 phosphorylation (By similarity). Autophagy is also triggered upon infection by bacteria: following c-di-GMP-binding, which is produced by live Gram-positive bacteria, promotes reticulophagy (By similarity). May be involved in translocon function, the translocon possibly being able to influence the induction of type I interferons (By similarity). May be involved in transduction of apoptotic signals via its association with the major histocompatibility complex class II (MHC-II) (By similarity). {ECO:0000250|UniProtKB:Q3TBT3, ECO:0000250|UniProtKB:Q86WV6, ECO:0000269|PubMed:31167783, ECO:0000269|PubMed:35584187}. | 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:138284, ChEBI:CHEBI:173118; EC=4.6.1.19; Evidence={ECO:0000255|PROSITE-ProRule:PRU10045}; | 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 | MRLGVALSTIAVLLTATSARNLDKRQWGWPNFGGGNGGNGGNGGKTINDYKREQGAGRDIHVYAPSNLAPNSPLLLSLHGMDQDPNYQQSNTHWETLADSEGFVVVYPRGGTGMSTWDIQGTKDTQWVSQIIDQMKKEYNIDTKRVYLSGFSMGGMFTYHAMSQIANKIAAFAPCSGPNVFGASKAQRPVPIFHVHGTNDDVLNYQQVEGFLKNYRDQFHCPSQADTKTNYPNRENPNATLYTWGPCDKGVYIKHLKLQGRGHSPSSADIQDIWDFVSQWTVDGPVSASGNGGGNTTPTNPSTGGNGNGNGGGNTTPTNPSTGGNGNGNGGSTDKCSSNITKQGYKCCASNCEVVYTDSDGDWGVENDQWCGCGNRVTVGSGTCSAKILQQGYKCCPSGCIIYYTDEDGTWGVNGEEWCGCGSGSSSTGGGNDAPSSGSGYQGANGTNFCNNAKHSGESVTVTSNKVGDINGIGYELWADSGNNSATFYDDGSFSCSFQRAKDYLCRSGLSFDSTKTHKQIGHIYAEFKLVKQNIQNVDYSYVGIYGWTRNPLVEFYVVDNWLSQWRPGDWVGNKKHGDFTIGGAQYTVYENTRYGPSIDGDTNFKQYFSIRQQPRDCGTIDITAHFEQWEKLGMTMGKMHEAKVLGEAGSNNGGTSGTADFPFAKVYVKN | 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 birchwood xylan for Endo-1,4-beta-xylanase activity; | 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, and releases acetate from 4-methylumbelliferyl acetate and beta-D-xylose tetraacetate. No activity is observed against carboxy methyl cellulose, beta-glucan, p-nitrophenol acetate, p-nitrophenol laurate, p-nitrophenol myristate, p-nitrophenol, palmitate, or beta-naphthol acetate. {ECO:0000269|PubMed:19690850}. | Neocallimastix patriciarum (Rumen fungus) |
B8ZXI1 | QTRT2_MOUSE | MKLSLIKVVNGCRLGKIQNLGKAGDCTVDIPGCLLYTRTGSAPHLTHQTLRNIHGVPGIAQLTLSSLAEHHEVLAEYKKGVGSFIGMPESLFYCSLHDPVTPGPAGYVTSKSVSVWGFGGRVEMTVSKFMAIQEALQPDWFQCLSDGEASCAETTSIKRARKSVDRSLLFLDSCLRLQEESEVLQKSVIIGVIEGGDVMEERLRSARETAKRPVGGFLLDGFQGDPAVTETRLHLLSSVTAELPEDKPRLICGVSRPDEVLECIERGVDLFESFFPYQVTERGCALTFTFDCQLNPEETLLQQNGIQEKIKGLDQAKKIEATGCNQEMTSFEINLKEKKYQEDFDPLVRGCSCYCCKNHTRAYIHHLLMTNELLAGVLLMMHNFEHYFGFFCSIREALKNDTLAQLKELICRQMF | 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-Rule:MF_03043, ECO:0000269|PubMed:19414587}. Note=May associate with the mitochondrion outer membrane. {ECO:0000255|HAMAP-Rule:MF_03043, ECO:0000269|PubMed:19414587}. | 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-cis-dihydroxy-2-cyclopenten-1-yl)amino)methyl)-7-deazaguanosine). {ECO:0000255|HAMAP-Rule:MF_03043, ECO:0000269|PubMed:19414587, ECO:0000269|PubMed:35815944}. | Mus musculus (Mouse) |
B9DFA8 | INVC_ARATH | MNSRSCICVSAMKPCCRFLISFRSSSLFGFSPPNSGKFINSSKLHCTKIDSRSIRSGIHCRRIVLDRNAFCDSDSISWGGGGSRVLRARGSSRGRGRGVLVIPHVASDFRNYSTSSLDSHVNDKSFESMFVKPLVFKEVEKTEGIPKRERGNVGGGKDANFGNVGVRKETERCLSQTEVEKEAWKLLRGAVVNYCGFPVGTVAANDPGDTQTLNYDQVFIRDFVPSAYAFMLDGEGEIVRNFLLHTLQLQSWEKTVDCHSPGPGLMPASFKVKSAPLEGNDGSFEEFLDPDFGGSAIGRVSPVDSGLWWIILLRAYGKLTGDYTLQERIDVQTGIKLILKLCLADGFDMFPTLLVTDGSCMVDRRMGIHGHPLEIQALFYSALRCAREMLIVNDGTKSLVTAVNNRLSALSFHIREYYWVDIKKINEIYRYNTEEYSADATNKFNIYPEQIPTWLVDWIPDKGGYFIGNLQPAHMDFRFFTLGNLWAVISSLGNQEQNEGVMTLIEEKWDDLVANMPLKICFPALEKDEWRIITGSDPKNTPWSYHNGGSWPTLLWQFTLACIKMGKLELAKKAVAVAEKRLKEDEWPEYYDTKSGRFVGKQSRLYQTWTIAGFLAAKKLIEQPEKASLLFWEEDYQLLETCVCGLSKSSGRKNKCSRFTPPRS | 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 | MNTLPVVSLTASSSFKFFHFPSLHRSLSHSPNFSFTKSLILNPNHLSFKSTLNSLSPSQSQLYEEEDDEEEEEEDEDDDDEAADEYDNISDEIRNSDDDDDDEETEFSVDLPTESARERVEFRWQRVEKLRSLVRDFGVEMIDIDELISIYDFRIDKFQRLAIEAFLRGSSVVVSAPTSSGKTLIAEAAAVSTVAKGRRLFYTTPLKALSNQKFREFRETFGDDNVGLLTGDSAINKDAQIVIMTTEILRNMLYQSVGMASSGTGLFHVDAIVLDEVHYLSDISRGTVWEEIVIYCPKEVQLICLSATVANPDELAGWIGEIHGKTELVTSTRRPVPLTWYFSTKHSLLPLLDEKGINVNRKLSLNYLQLSASEARFRDDDDGYRKRRSKKRGGDTSYNNLVNVTDYPLSKNEINKIRRSQVPQISDTLWHLQGKNMLPAIWFIFNRRGCDAAVQYVENFQLLDDCEKSEVELALKKFRVLYPDAVRESAEKGLLRGIAAHHAGCLPLWKSFIEELFQRGLVKVVFATETLAAGINMPARTAVISSLSKKAGNERIELGPNELYQMAGRAGRRGIDEKGYTVLVQTAFEGAEECCKLVFAGVKPLVSQFTASYGMVLNLVAGSKVTRKSSGTEAGKVLQAGRSLEEAKKLVEKSFGNYVSSNVTVAAKQELAEIDNKIEILSSEISDEAIDKKSRKLLSARDYKEITVLKEELREEKRKRAEQRRRMELERFLALKPLLKGMEEGNLPFICLEFKDSEGREQSVPAVYLGHIDSFQGSKLQKMMSLDESFALNLIEDELAADEPGKPNVKPSYYVALGSDNSWYLFTEKWVRTVYRTGFPNIALALGDALPREIMKNLLDKADMQWDKLAESELGSLWRLEGSLETWSWSLNVPVLSSLSDEDEVLHMSEEYDNAAQKYKEQRSKISRLKKKMSRSEGFREYKKILENANLTVEKMKRLKARSRRLINRLEQIEPSGWKDFMRISNVIHESRALDINTHLIFPLGETAAAIRGENELWLAMVLRNKALVDLKPPQLAGVCASLVSEGIKVRPWRDNNYIYEPSDTVVDMVNFLEDQRSSLIKLQEKHEVMIPCCLDVQFSGMVEAWASGLSWKEMMMECAMDEGDLARLLRRTIDLLAQIPKLPDIDPVLQRSAAAAADIMDRPPISELAG | 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]; plasmodesmata-mediated intercellular transport [GO:0010497]; post-transcriptional gene silencing [GO:0016441]; regulatory ncRNA-mediated gene silencing [GO:0031047] | 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:17601829}. | 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:11779812, ECO:0000269|PubMed:11874921, ECO:0000269|PubMed:17601829, ECO:0000269|PubMed:20434343, ECO:0000269|PubMed:26147377}. | Arabidopsis thaliana (Mouse-ear cress) |
B9DFG5 | PTI13_ARATH | MYPMDSDYHRRGLVANDRSPAQFVRLDKPRAVDDLYIGKREKMRRWLCCACHVEEPYHSSENEHLRSPKHHNDFGHHTRKPQAAVKPDALKEPPSIDVPALSLDELKEKTDNFGSKSLIGEGSYGRAYYATLKDGKAVAVKKLDNAAEPESNVEFLTQVSRVSKLKHDNFVELFGYCVEGNFRILAYEFATMGSLHDILHGRKGVQGAQPGPTLDWIQRVRIAVDAARGLEYLHEKVQPAVIHRDIRSSNVLLFEDFKAKIADFNLSNQSPDMAARLHSTRVLGTFGYHAPEYAMTGQLTQKSDVYSFGVVLLELLTGRKPVDHTMPRGQQSLVTWATPRLSEDKVKQCVDPKLKGEYPPKAVAKLAAVAALCVQYESEFRPNMSIVVKALQPLLRSSTAAAVPVQEA | 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:PRU10028}; | null | null | null | null | null | Arabidopsis thaliana (Mouse-ear cress) |
B9DFK5 | RETIC_ARATH | MAGCAMNLQFSSVVKVRNEISSFGICNRDFVFRDLAKAMKVPVLRIRGGSGRQRSRLFVVNMSQSPIEPQSGGFAATEQIKGEGDNSILGKDNVRNLGTDQLENLDIDGNVGDGFNGSDGNGGGGGGGNGGEGDGEGEDYEEKEFGPILKFEEVMKETEARGATLPSDMLEAAKNYGIRKVLLLRYLDLQSSAGLLGFAIRSWAMLRNRMLADPSFLFKIGAEIVIDSCCATVAEVQKRGKDFWAEFELYVADLLVGTVVNIALVGMLAPYVRFGQPSASPGFLGRMVFAYNALPSSVFEAERPGCRFSAQQRLATYFYKGIMYGAVGFGCGIVGQGIANLIMTAKRNINKSEENIPVPPLIKSAALWGVFLSVSSNTRYQIINGLERVVEASPFAKKFPPAAMAFTVGVRLANNIYGGMQFVDWARLSGCQ | 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|PubMed:16873448}. | Arabidopsis thaliana (Mouse-ear cress) |
B9DFS6 | SNX2B_ARATH | MMGSENDEESHLHSSKEEMEKLFLREDGDPLTKSNVNGDKSNSNYRSAMSTLFDSRHPSIVVTPADSDPLFAPPSYYSESRSPRSKPNGGDRVSSYLEPPSYADVIFSPFDDISEINGSEDGHSQSSDSLSRSPSSLSSDYIKITVSNPQKEQEATNSMIPGGSTYITYQITTRTNLSDYGGSEFSVRRRFRDIVTLADRLAESYRGFCIPPRPDKSIVESQVMQKQEFVEQRRVALEKYLRRLVAHPVIRNSDELKVFLQAQGKLPLATSTDVASRMLDGAVKLPKQLFGEGGGASSVEVVQPGRGGRDFLRMFKELRQSVSNDWGGSKPPVVEEDKEFLEKKEKMYDLEQQIINASQQAESLVKAQQDMGETMGELGLAFIKLTKFENEEAVFNSQRARANDMKNLATSAVKASRFYRELNSQTVKHLDTLHDYLGLMMAVQGAFADRSSALLTVQTLLSELSSLEARAEKLEVASSKVFGGDKSRIKKIEELKETIKVTEDSKNVAIREYEQIKENNWSEVERLDRERRADFLNMMKGFVANQVGYAEKIANVWTKVAEETRQYDRESS | 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|PubMed:19825596}. | Arabidopsis thaliana (Mouse-ear cress) |
B9DFU2 | MAX1_ARATH | MKTQHQWWEVLDPFLTQHEALIAFLTFAAVVIVIYLYRPSWSVCNVPGPTAMPLVGHLPLMAKYGPDVFSVLAKQYGPIFRFQMGRQPLIIIAEAELCREVGIKKFKDLPNRSIPSPISASPLHKKGLFFTRDKRWSKMRNTILSLYQPSHLTSLIPTMHSFITSATHNLDSKPRDIVFSNLFLKLTTDIIGQAAFGVDFGLSGKKPIKDVEVTDFINQHVYSTTQLKMDLSGSLSIILGLLIPILQEPFRQVLKRIPGTMDWRVEKTNARLSGQLNEIVSKRAKEAETDSKDFLSLILKARESDPFAKNIFTSDYISAVTYEHLLAGSATTAFTLSSVLYLVSGHLDVEKRLLQEIDGFGNRDLIPTAHDLQHKFPYLDQVIKEAMRFYMVSPLVARETAKEVEIGGYLLPKGTWVWLALGVLAKDPKNFPEPEKFKPERFDPNGEEEKHRHPYAFIPFGIGPRACVGQRFALQEIKLTLLHLYRNYIFRHSLEMEIPLQLDYGIILSFKNGVKLRTIKRF | 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, ChEBI:CHEBI:58210, ChEBI:CHEBI:194508, ChEBI:CHEBI:194510; Evidence={ECO:0000269|PubMed:25425668}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:76084; Evidence={ECO:0000269|PubMed:25425668}; CATALYTIC ACTIVITY: Reaction=(11R)-19-hydroxycarlactone + O2 + reduced [NADPH--hemoprotein reductase] = (11R)-19-oxocarlactone + H(+) + 2 H2O + oxidized [NADPH--hemoprotein reductase]; Xref=Rhea:RHEA:76091, Rhea:RHEA-COMP:11964, Rhea:RHEA-COMP:11965, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, ChEBI:CHEBI:57618, ChEBI:CHEBI:58210, ChEBI:CHEBI:194510, ChEBI:CHEBI:194511; Evidence={ECO:0000269|PubMed:25425668}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:76092; Evidence={ECO:0000269|PubMed:25425668}; CATALYTIC ACTIVITY: Reaction=(11R)-19-oxocarlactone + O2 + reduced [NADPH--hemoprotein reductase] = (11R)-carlactonoate + 2 H(+) + H2O + oxidized [NADPH--hemoprotein reductase]; Xref=Rhea:RHEA:76095, Rhea:RHEA-COMP:11964, Rhea:RHEA-COMP:11965, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, ChEBI:CHEBI:57618, ChEBI:CHEBI:58210, ChEBI:CHEBI:194504, ChEBI:CHEBI:194511; Evidence={ECO:0000269|PubMed:25425668}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:76096; Evidence={ECO:0000269|PubMed:25425668}; | 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-19 methyl group into carboxylic acid (PubMed:25425668). Prefers 11R-carlactone to 11S-carlactone as substrate (PubMed:25425668). Acts downstream of CCD7/MAX3 and CCD8/MAX4 in strigolactone signaling pathway and may be implicated in synthesis of carotenoid-derived branch regulators. Acts as a positive regulator of the flavonoid pathway in the late vegetative stage plant. Strigolactones are hormones that inhibit tillering and shoot branching through the MAX-dependent pathway, contribute to the regulation of shoot architectural response to phosphate-limiting conditions and function as rhizosphere signal that stimulates hyphal branching of arbuscular mycorrhizal fungi and trigger seed germination of root parasitic weeds (PubMed:15737939, PubMed:16387852). {ECO:0000269|PubMed:15737939, ECO:0000269|PubMed:16387852, ECO:0000269|PubMed:25425668, ECO:0000269|PubMed:32399509}. | Arabidopsis thaliana (Mouse-ear cress) |
B9DFX7 | HMA8_ARATH | MASNLLRFPLPPPSSLHIRPSKFLVNRCFPRLRRSRIRRHCSRPFFLVSNSVEISTQSFESTESSIESVKSITSDTPILLDVSGMMCGGCVARVKSVLMSDDRVASAVVNMLTETAAVKFKPEVEVTADTAESLAKRLTESGFEAKRRVSGMGVAENVKKWKEMVSKKEDLLVKSRNRVAFAWTLVALCCGSHTSHILHSLGIHIAHGGIWDLLHNSYVKGGLAVGALLGPGRELLFDGIKAFGKRSPNMNSLVGLGSMAAFSISLISLVNPELEWDASFFDEPVMLLGFVLLGRSLEERAKLQASTDMNELLSLISTQSRLVITSSDNNTPVDSVLSSDSICINVSVDDIRVGDSLLVLPGETFPVDGSVLAGRSVVDESMLTGESLPVFKEEGCSVSAGTINWDGPLRIKASSTGSNSTISKIVRMVEDAQGNAAPVQRLADAIAGPFVYTIMSLSAMTFAFWYYVGSHIFPDVLLNDIAGPDGDALALSLKLAVDVLVVSCPCALGLATPTAILIGTSLGAKRGYLIRGGDVLERLASIDCVALDKTGTLTEGRPVVSGVASLGYEEQEVLKMAAAVEKTATHPIAKAIVNEAESLNLKTPETRGQLTEPGFGTLAEIDGRFVAVGSLEWVSDRFLKKNDSSDMVKLESLLDHKLSNTSSTSRYSKTVVYVGREGEGIIGAIAISDCLRQDAEFTVARLQEKGIKTVLLSGDREGAVATVAKNVGIKSESTNYSLSPEKKFEFISNLQSSGHRVAMVGDGINDAPSLAQADVGIALKIEAQENAASNAASVILVRNKLSHVVDALSLAQATMSKVYQNLAWAIAYNVISIPIAAGVLLPQYDFAMTPSLSGGLMALSSIFVVSNSLLLQLHKSETSKNSL | 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 | MILTGAASTFPIVARVLNAMNRRMYAATTLSSAKSISAESLNLRSDSNSEAAHGASESETRVSLRKKRIKQDDLEPVKKCSARETKARKDMCGLPDIEDSPYKKTNGTASSRTRKLNSYIKSTEASPSASSIKTAGLGIPPENWEKVLEGIRKMKPSEEAPVNAVECDRTGSFLPPKERRFYVLIGTLLSSQTKEHITGAAVERLHQNGLLTPEAIDKADESTIKELIYPVGFYTRKATNVKKVAKICLMEYDGDIPRTLEELLSLPGVGPKIAHLVLHVAWNDVQGICVDTHVHRICNRLGWVSKPGTKQKTSSPEETRVALQQWLPKGEWVAINFLLVGFGQTICTPLRPHCGTCSITEICPSAFKETPSTSSKLKKSIKSKKL | 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 nucleobase lesion DNA N-glycosylase activity [GO:0000703] | 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:RHEA-COMP:17067, ChEBI:CHEBI:15378, ChEBI:CHEBI:136412, ChEBI:CHEBI:157695, ChEBI:CHEBI:167181; EC=4.2.99.18; Evidence={ECO:0000255|HAMAP-Rule:MF_03183}; | 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-glycosidic bond, leaving an AP site. The AP lyase activity cleaves the phosphodiester bond 3' to the AP site by a beta-elimination. Primarily recognizes and repairs oxidative base damage of pyrimidines. {ECO:0000255|HAMAP-Rule:MF_03183, ECO:0000269|PubMed:19372224}. | Arabidopsis thaliana (Mouse-ear cress) |
B9DGD6 | ACS_ARATH | MKIGSPSSPILSVVSSSGSLDPKISGSLGSRILPATQRSSPSENLLLHRKMSSNSLRHVESMSQLPSGAGKISQLNAVVLGESLASEENDLVFPSKEFSGQALVSSPQQYMEMHKRSMDDPAAFWSDIASEFYWKQKWGDQVFSENLDVRKGPISIEWFKGGITNICYNCLDKNVEAGLGDKTAIHWEGNELGVDASLTYSELLQRVCQLANYLKDNGVKKGDAVVIYLPMLMELPIAMLACARIGAVHSVVFAGFSADSLAQRIVDCKPNVILTCNAVKRGPKTINLKAIVDAALDQSSKDGVSVGICLTYDNSLATTRENTKWQNGRDVWWQDVISQYPTSCEVEWVDAEDPLFLLYTSGSTGKPKGVLHTTGGYMIYTATTFKYAFDYKSTDVYWCTADCGWITGHSYVTYGPMLNGATVVVFEGAPNYPDPGRCWDIVDKYKVSIFYTAPTLVRSLMRDDDKFVTRHSRKSLRVLGSVGEPINPSAWRWFFNVVGDSRCPISDTWWQTETGGFMITPLPGAWPQKPGSATFPFFGVQPVIVDEKGNEIEGECSGYLCVKGSWPGAFRTLFGDHERYETTYFKPFAGYYFSGDGCSRDKDGYYWLTGRVDDVINVSGHRIGTAEVESALVLHPQCAEAAVVGIEHEVKGQGIYAFVTLLEGVPYSEELRKSLVLMVRNQIGAFAAPDRIHWAPGLPKTRSGKIMRRILRKIASRQLEELGDTSTLADPSVVDQLIALADV | 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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