CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-008296
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Endonuclease 8 
Protein Synonyms/Alias
 DNA glycosylase/AP lyase Nei; DNA-(apurinic or apyrimidinic site) lyase Nei; Endonuclease VIII 
Gene Name
 nei 
Gene Synonyms/Alias
 b0714; JW0704 
Created Date
 July 27, 2013 
Organism
 Escherichia coli (strain K12) 
NCBI Taxa ID
 83333 
Lysine Modification
Position
Peptide
Type
References
220RGQVDENKHHGALFRacetylation[1]
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
 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 pyrimidines, such as thymine glycol, 5,6-dihydrouracil and 5,6-dihydrothymine. Acts on DNA bubble and 3'-fork structures, suggesting a role in replication-associated DNA repair. 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. 
Sequence Annotation
 ZN_FING 229 263 FPG-type.
 ACT_SITE 2 2 Schiff-base intermediate with DNA.
 ACT_SITE 3 3 Proton donor (Probable).
 ACT_SITE 53 53 Proton donor; for beta-elimination
 ACT_SITE 253 253 Proton donor; for delta-elimination
 BINDING 70 70 DNA.
 BINDING 125 125 DNA.
 BINDING 169 169 DNA.  
Keyword
 3D-structure; Complete proteome; Direct protein sequencing; DNA damage; DNA repair; DNA-binding; Glycosidase; Hydrolase; Lyase; Metal-binding; Multifunctional enzyme; Reference proteome; Zinc; Zinc-finger. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 263 AA 
Protein Sequence
MPEGPEIRRA ADNLEAAIKG KPLTDVWFAF PQLKPYQSQL IGQHVTHVET RGKALLTHFS 60
NDLTLYSHNQ LYGVWRVVDT GEEPQTTRVL RVKLQTADKT ILLYSASDIE MLTPEQLTTH 120
PFLQRVGPDV LDPNLTPEVV KERLLSPRFR NRQFAGLLLD QAFLAGLGNY LRVEILWQVG 180
LTGNHKAKDL NAAQLDALAH ALLEIPRFSY ATRGQVDENK HHGALFRFKV FHRDGEPCER 240
CGSIIEKTTL SSRPFYWCPG CQH 263 
Gene Ontology
 GO:0003684; F:damaged DNA binding; IDA:EcoliWiki.
 GO:0003906; F:DNA-(apurinic or apyrimidinic site) lyase activity; IDA:EcoliWiki.
 GO:0004519; F:endonuclease activity; IEA:InterPro.
 GO:0000703; F:oxidized pyrimidine nucleobase lesion DNA N-glycosylase activity; IEA:HAMAP.
 GO:0008270; F:zinc ion binding; IDA:EcoliWiki.
 GO:0006284; P:base-excision repair; IDA:EcoliWiki.
 GO:0006289; P:nucleotide-excision repair; IEA:InterPro. 
Interpro
 IPR015886; DNA_glyclase/AP_lyase_DNA-bd.
 IPR015887; DNA_glyclase_Znf_dom_DNA_BS.
 IPR012319; DNA_glycosylase/AP_lyase_cat.
 IPR023713; Endonuclease-VIII.
 IPR010979; Ribosomal_S13-like_H2TH.
 IPR000214; Znf_DNA_glyclase/AP_lyase.
 IPR010663; Znf_DNA_glyclase/IsotRNA_synth. 
Pfam
 PF01149; Fapy_DNA_glyco
 PF06831; H2TH
 PF06827; zf-FPG_IleRS 
SMART
 SM00898; Fapy_DNA_glyco 
PROSITE
 PS51068; FPG_CAT
 PS01242; ZF_FPG_1
 PS51066; ZF_FPG_2 
PRINTS