Tag | Content |
UniProt Accession | |
Genbank Protein ID | |
Genbank Nucleotide ID | |
Protein Name | Formamidopyrimidine-DNA glycosylase |
Protein Synonyms/Alias | Fapy-DNA glycosylase |
Gene Name | mutM |
Gene Synonyms/Alias | fpg; OrderedLocusNames=SYNPCC7002_A1816 |
Created Date | 3-June-2014 |
Organism | Synechococcus sp. (strain ATCC 27264 / PCC 7002 / PR-6) (Agmenellum quadruplicatum) |
NCBI Taxa ID | 32049 |
Phosphorylation | Position | Peptide | Code | Type | References | 61 | DWQRRGKYLLGKLSD | Y | HTP | [1] | |
Reference | [1]Global phosphoproteomic analysis reveals diverse functions of serine/threonine/tyrosine phosphorylation in the model cyanobacterium Synechococcus sp. strain PCC 7002. Yang MK,Qiao ZX,Zhang WY,Xiong Q,Zhang J,Li T,Ge F,Zhao JD J. Proteome Res. 2013, Apr, 5;12(4):1909-23. [ PMID:23461524] |
Functional Description From UniProt | 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 (By similarity) |
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| Completeproteome; DNAdamage; DNArepair; DNA-binding; Glycosidase; Hydrolase; Lyase; Metal-binding; Multifunctionalenzyme; Zinc; Zinc-finger |
Protein Sequence | MPELPEVETV RRGLMQISLN QQFTGAEILL RKTLAYPTDP DHFLGMIQGL FIQDWQRRGK 60 YLLGKLSDGS TLGIHLRMTG KFLWTTPDVP VQKHTRIRFF IEGDRELRFV DLRTFGQIWW 120 VPAGTIVKSV ITGLTRLGVE PLSPDFTADL LANFCEKRQR PMKTFLLDQS IITGLGNIYA 180 DEALFKSGIH PTRKASSLKM SEIEKLHKAI VEVLETSIAQ GGTTFSDFVS TTGTNGNYGG 240 MALTYGRTGE PCRVCSHPIE RIKLGGRSTH FCPQCQS 277 |
| GO:0003684 F:damaged DNA binding IEA:InterPro GO:0008534 F:oxidized purine nucleobase lesion DNA N-glycosylase activity IEA:UniProtKB-HAMAP GO:0008270 F:zinc ion binding IEA:UniProtKB-HAMAP GO:0006284 P:base-excision repair IEA:InterPro GO:0006289 P:nucleotide-excision repair IEA:InterPro |
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