ACL_RS07185
  | Uniprot: A9NF43
Description: dephospho-CoA kinase EC number: 3.2.2.-; 3.2.2.23; 4.2.99.18 Annotation score: 3 out of 5 Miscellaneous [CC]: Protein existence: Inferred from homology Catalytic activity: CATALYTIC ACTIVITY: Hydrolysis of DNA containing ring-opened 7-methylguanine residues, releasing 2,6-diamino-4-hydroxy-5-(N-methyl)formamidopyrimidine. {ECO:0000256|SAAS:SAAS00020866}.; CATALYTIC ACTIVITY: The C-O-P bond 3' to the apurinic or apyrimidinic site in DNA is broken by a beta-elimination reaction, leaving a 3'-terminal unsaturated sugar and a product with a terminal 5'-phosphate. {ECO:0000256|SAAS:SAAS00557314}. Cofactor: COFACTOR: Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000256|SAAS:SAAS00610166}; Enzyme regulation: Function [CC]: FUNCTION: Involved in base excision repair of DNA damaged by oxidation or by mutagenic agents. Acts as DNA glycosylase that recognizes and removes damaged bases. Has a preference for oxidized purines, such as 7,8-dihydro-8-oxoguanine (8-oxoG). Has AP (apurinic/apyrimidinic) lyase activity and introduces nicks in the DNA strand. Cleaves the DNA backbone by beta-delta elimination to generate a single-strand break at the site of the removed base with both 3'- and 5'-phosphates. {ECO:0000256|SAAS:SAAS00348515}. Pathway: Active site: Binding site: Calcium binding: DNA binding: Metal binding: Nucleotide binding: Site: Gene names (primary): Gene names (synonym): Mass: 51,823 Subunit structure [CC]: SUBUNIT: Monomer. {ECO:0000256|SAAS:SAAS00020849}. Gene ontology (GO): ATP binding [GO:0005524]; damaged DNA binding [GO:0003684]; dephospho-CoA kinase activity [GO:0004140]; oxidized purine nucleobase lesion DNA N-glycosylase activity [GO:0008534]; zinc ion binding [GO:0008270]; base-excision repair [GO:0006284]; coenzyme A biosynthetic process [GO:0015937]; nucleotide-excision repair [GO:0006289] Gene ontology IDs: GO:0003684; GO:0004140; GO:0005524; GO:0006284; GO:0006289; GO:0008270; GO:0008534; GO:0015937 Chain: Signal peptide: Domain [CC]: Sequence similarities: SIMILARITY: Belongs to the CoaE family. {ECO:0000256|SAAS:SAAS00580898}.; SIMILARITY: Belongs to the FPG family. {ECO:0000256|SAAS:SAAS00557294}.; SIMILARITY: Contains DPCK (dephospho-CoA kinase) domain. {ECO:0000256|SAAS:SAAS00515713}.; SIMILARITY: Contains FPG-type zinc finger. {ECO:0000256|SAAS:SAAS00551694}. Protein families: CoaE family; FPG family Coiled coil: Domain [FT]: DOMAIN 2 109 FPG_CAT. {ECO:0000259|PROSITE:PS51068}.; DOMAIN 232 266 FPG-type. {ECO:0000259|PROSITE:PS51066}. Motif: Region: EMBL: CP000896 ProteinModelPortal: A9NF43 MEROPS: EnsemblBacteria KO: ABX80973 UniPathway: K10563 CDD: Gene3D: HAMAP: 3.40.50.300 InterPro: MF_00376 PANTHER: IPR001977;IPR015886;IPR015887;IPR020629;IPR012319;IPR027417;IPR010979;IPR000214;IPR010663 PIRSF: PRINTS: PROSITE: Pfam: PS51219;PS51068;PS01242;PS51066 ProDom: PF01121;PF01149;PF06831;PF06827 SMART: SUPFAM: SM00898;SM01232 TIGRFAMs: SSF46946;SSF52540;SSF81624 |
368411-369770(+) >nucleotide sequence GAAATCATACGTGAGGTTTTAGTATACTATCGACCTATTGTTTCAAATGATGCGTCATTT GAAACCAAATTAAAAGGTCAACGTATACATAAAGTAGAACGTGAAGCAAAGTATTTAAAG TTTATTTTAGATGACTATCTTTTAGTATCTCATTTACGTATGGAAGGCAAATACTTTATG GACGCGCCTTTAAATAAACATATACATGTAGTGTTTAATCTATCAAGCGGTCACACGTTA AGTTATGAAGATACACGTAAATTTGGCCGTTTTGAACTGGTAGATATTAAATATAAAGAC ACTTATTTAAAAGATATTAAAGGGCTTGCTAAAGACCCTGATACCCTAGATTTAAACACC TTTTATAGTAGTTTTAATCAAAGAAGTAAAACGATTAAAGAAATATTACTGGATCAATCC ATTATTGGTGGTATTGGTAATATTTATGCAAATGAAATACTTTACTTATCTAAAATACAT CCAGCCAAAAAAGGTTTTTTAATCAGTAAAGATGAAGCAAAAACCTTACTAAATAACTCT AATCTTGTTTTAAACAAGGCCATCGAAATGGGTGGAACGACAATTGACACCTTTGAATCA TTAGGGCATAAGGGTGAGTTTCAACAGGAGTTAAATGTTCATGGCAAAACTGGAGAGATT TGTAAGGTATGTGGCACTAAAATAATTAAATTTCAGTTAAAAGGACGAGGTACTTATATT TGTCCTAAATGCCAACCATCTTATGTAGTCGCAATCACAGGTGGTATTGCAACCGGTAAA TCTACTGCAACAAACTATTTAAGAAAAAAAGGATTTGTAGTTGTAGATTCTGATGAAATT GTAGGAAGTCTTTATCAAGATAGTGATGTACTAAATTTAATTGCAAAAACCTTTAAAATG GAAACACCAATTGATAAAGCAAAACTTGCAAACATCGTTTTCCATGATGAAAAACAAAGA AAAAAATTAGAACACATCTTACATCCACTCGTTTTTGATGAAATTAGCAAACAAAAACAA TTAAATAATGAACATATCTTATTTTTAGATATTCCTTTATTATTTGAATCGAATTACAAA GAGTTTGATGAATCCATCTTAATAGATACAACTGAAGCACTTCAACTGGATAGATTAATG AAGCGCAACAAATATACTCAAGAAGAAGCACTTGTTCGTATAAAAGCGCAGATACCTTTA AGTAAAAAGCGCAAACTAGCTACACACATTATAAAAAATAATGGATCTATAGATGCGTTA TATGAAAAAATAGATAAATTATTAGAAAGGTATGTATAA >protein sequence FILDDYLLVSHLRMEGKYFMDAPLNKHIHVVFNLSSGHTLSYEDTRKFGRFELVDIKYKD TYLKDIKGLAKDPDTLDLNTFYSSFNQRSKTIKEILLDQSIIGGIGNIYANEILYLSKIH PAKKGFLISKDEAKTLLNNSNLVLNKAIEMGGTTIDTFESLGHKGEFQQELNVHGKTGEI CKVCGTKIIKFQLKGRGTYICPKCQPSYVVAITGGIATGKSTATNYLRKKGFVVVDSDEI VGSLYQDSDVLNLIAKTFKMETPIDKAKLANIVFHDEKQRKKLEHILHPLVFDEISKQKQ LNNEHILFLDIPLLFESNYKEFDESILIDTTEALQLDRLMKRNKYTQEEALVRIKAQIPL SKKRKLATHIIKNNGSIDALYEKIDKLLERYV |
© Fisunov Lab of Proteomics, 2016.