CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-009877
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Endonuclease V 
Protein Synonyms/Alias
 Deoxyinosine 3'endonuclease; Deoxyribonuclease V; DNase V 
Gene Name
 nfi 
Gene Synonyms/Alias
 yjaF; b3998; JW5547 
Created Date
 July 27, 2013 
Organism
 Escherichia coli (strain K12) 
NCBI Taxa ID
 83333 
Lysine Modification
Position
Peptide
Type
References
53RAAMVLLKYPSLELVacetylation[1]
63SLELVEYKVARIATTacetylation[1]
138AKKRLCGKFEPLSSEacetylation[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
 Selectively cleaves double-stranded DNA at the second phosphodiester bond 3' to a deoxyinosine leaving behind the intact lesion on the nicked DNA. Has a wide substrate spectrum. In addition to deoxyinosine-containing DNA, the enzyme cleaves DNA containing urea residues, AP sites, base mismatches, insertion/deletion mismatches, flaps, and pseudo-Y structures. Participates in the excision repair of hypoxanthine and xanthine (deaminated adenine and guanine) in DNA. It thereby reduces the mutagenic effects of nitrous acid by attacking lesions caused by nitrosative deamination. 
Sequence Annotation
 METAL 35 35 Magnesium (By similarity).
 METAL 103 103 Magnesium (By similarity).  
Keyword
 Complete proteome; Cytoplasm; Direct protein sequencing; DNA damage; DNA repair; Endonuclease; Hydrolase; Magnesium; Metal-binding; Nuclease; Reference proteome. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 223 AA 
Protein Sequence
MDLASLRAQQ IELASSVIRE DRLDKDPPDL IAGADVGFEQ GGEVTRAAMV LLKYPSLELV 60
EYKVARIATT MPYIPGFLSF REYPALLAAW EMLSQKPDLV FVDGHGISHP RRLGVASHFG 120
LLVDVPTIGV AKKRLCGKFE PLSSEPGALA PLMDKGEQLA WVWRSKARCN PLFIATGHRV 180
SVDSALAWVQ RCMKGYRLPE PTRWADAVAS ERPAFVRYTA NQP 223 
Gene Ontology
 GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
 GO:0043737; F:deoxyribonuclease V activity; IDA:EcoCyc.
 GO:0000287; F:magnesium ion binding; IEA:HAMAP.
 GO:0006281; P:DNA repair; IEA:HAMAP. 
Interpro
 IPR007581; Endonuclease-V. 
Pfam
 PF04493; Endonuclease_5 
SMART
  
PROSITE
  
PRINTS