CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
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
77EGVKTYIKTIGLYNSacetylation[1]
154RTQFAPGKNVEQVEEacetylation[1]
162NVEQVEEKLLKVVPAacetylation[1]
165QVEEKLLKVVPAEFKacetylation[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
 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. 
Interpro
 IPR011257; DNA_glycosylase.
 IPR004036; Endonuclease-III_CS2.
 IPR005759; Endonuclease-III_Nth.
 IPR004035; Endouclease-III_FeS-bd_BS.
 IPR003651; Endouclease3_FeS-loop_motif.
 IPR003265; HhH-GPD_domain.
 IPR000445; HhH_motif.
 IPR003583; Hlx-hairpin-Hlx_DNA-bd_motif.
 IPR023170; HTH_base_excis_C. 
Pfam
 PF10576; EndIII_4Fe-2S
 PF00633; HHH
 PF00730; HhH-GPD 
SMART
 SM00478; ENDO3c
 SM00525; FES
 SM00278; HhH1 
PROSITE
 PS00764; ENDONUCLEASE_III_1
 PS01155; ENDONUCLEASE_III_2 
PRINTS