Tag | Content |
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CPLM ID | CPLM-003280 |
UniProt Accession | |
Genbank Protein ID | |
Genbank Nucleotide ID | |
Protein Name | Endonuclease III |
Protein Synonyms/Alias | DNA-(apurinic or apyrimidinic site) lyase |
Gene Name | nth |
Gene Synonyms/Alias | b1633; JW1625 |
Created Date | July 27, 2013 |
Organism | Escherichia coli (strain K12) |
NCBI Taxa ID | 83333 |
Lysine Modification | Position | Peptide | Type | References |
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77 | EGVKTYIKTIGLYNS | acetylation | [1] | 154 | RTQFAPGKNVEQVEE | acetylation | [1] | 162 | NVEQVEEKLLKVVPA | acetylation | [1] | 165 | QVEEKLLKVVPAEFK | acetylation | [1] |
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Reference | [1] Acetyl-Phosphate Is a Critical Determinant of Lysine Acetylation in E. coli. Weinert BT, Iesmantavicius V, Wagner SA, Schölz C, Gummesson B, Beli P, Nyström T, Choudhary C. Mol Cell. 2013 Jul 25;51(2):265-72. [ PMID: 23830618] |
Functional Description | DNA repair enzyme that has both DNA N-glycosylase activity and AP-lyase activity. The DNA N-glycosylase activity releases various damaged pyrimidines from DNA by cleaving the N- glycosidic bond, leaving an AP (apurinic/apyrimidinic) site. The AP-lyase activity cleaves the phosphodiester bond 3' to the AP site by a beta-elimination, leaving a 3'-terminal unsaturated sugar and a product with a terminal 5'-phosphate. |
Sequence Annotation | DOMAIN 108 127 HhH. METAL 187 187 Iron-sulfur (4Fe-4S). METAL 194 194 Iron-sulfur (4Fe-4S). METAL 197 197 Iron-sulfur (4Fe-4S). METAL 203 203 Iron-sulfur (4Fe-4S). |
Keyword | 3D-structure; 4Fe-4S; Complete proteome; Direct protein sequencing; DNA damage; DNA repair; DNA-binding; Glycosidase; Hydrolase; Iron; Iron-sulfur; Lyase; Metal-binding; Reference proteome. |
Sequence Source | UniProt (SWISSPROT/TrEMBL); GenBank; EMBL |
Protein Length | 211 AA |
Protein Sequence | MNKAKRLEIL TRLRENNPHP TTELNFSSPF ELLIAVLLSA QATDVSVNKA TAKLYPVANT 60 PAAMLELGVE GVKTYIKTIG LYNSKAENII KTCRILLEQH NGEVPEDRAA LEALPGVGRK 120 TANVVLNTAF GWPTIAVDTH IFRVCNRTQF APGKNVEQVE EKLLKVVPAE FKVDCHHWLI 180 LHGRYTCIAR KPRCGSCIIE DLCEYKEKVD I 211 |
Gene Ontology | GO:0051539; F:4 iron, 4 sulfur cluster binding; IEA:UniProtKB-KW. GO:0003677; F:DNA binding; IEA:UniProtKB-KW. GO:0003906; F:DNA-(apurinic or apyrimidinic site) lyase activity; IEA:EC. GO:0004519; F:endonuclease activity; IEA:InterPro. GO:0016798; F:hydrolase activity, acting on glycosyl bonds; IEA:UniProtKB-KW. GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. GO:0006284; P:base-excision repair; IEA:InterPro. |
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