CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-002895
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Endonuclease 4 
Protein Synonyms/Alias
 Endodeoxyribonuclease IV; Endonuclease IV 
Gene Name
 nfo 
Gene Synonyms/Alias
 b2159; JW2146 
Created Date
 July 27, 2013 
Organism
 Escherichia coli (strain K12) 
NCBI Taxa ID
 83333 
Lysine Modification
Position
Peptide
Type
References
86PVTEALEKSRDAFIDacetylation[1]
198RTPAECEKTFADFARacetylation[1]
210FARTVGFKYLRGMHLacetylation[1]
221GMHLNDAKSTFGSRVacetylation[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
 Endonuclease IV plays a role in DNA repair. It cleaves phosphodiester bonds at apurinic or apyrimidinic sites (AP sites) to produce new 5'-ends that are base-free deoxyribose 5-phosphate residues. It preferentially attacks modified AP sites created by bleomycin and neocarzinostatin. 
Sequence Annotation
 METAL 69 69 Zinc 1.
 METAL 109 109 Zinc 1.
 METAL 145 145 Zinc 1.
 METAL 145 145 Zinc 2.
 METAL 179 179 Zinc 2.
 METAL 182 182 Zinc 3.
 METAL 216 216 Zinc 2.
 METAL 229 229 Zinc 3.
 METAL 231 231 Zinc 3.
 METAL 261 261 Zinc 2.  
Keyword
 3D-structure; Complete proteome; DNA damage; DNA repair; Endonuclease; Hydrolase; Manganese; Metal-binding; Nuclease; Reference proteome; Zinc. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 285 AA 
Protein Sequence
MKYIGAHVSA AGGLANAAIR AAEIDATAFA LFTKNQRQWR AAPLTTQTID EFKAACEKYH 60
YTSAQILPHD SYLINLGHPV TEALEKSRDA FIDEMQRCEQ LGLSLLNFHP GSHLMQISEE 120
DCLARIAESI NIALDKTQGV TAVIENTAGQ GSNLGFKFEH LAAIIDGVED KSRVGVCIDT 180
CHAFAAGYDL RTPAECEKTF ADFARTVGFK YLRGMHLNDA KSTFGSRVDR HHSLGEGNIG 240
HDAFRWIMQD DRFDGIPLIL ETINPDIWAE EIAWLKAQQT EKAVA 285 
Gene Ontology
 GO:0005622; C:intracellular; IEA:InterPro.
 GO:0008833; F:deoxyribonuclease IV (phage-T4-induced) activity; IEA:HAMAP.
 GO:0003677; F:DNA binding; IEA:InterPro.
 GO:0004519; F:endonuclease activity; IDA:EcoCyc.
 GO:0008270; F:zinc ion binding; IEA:HAMAP.
 GO:0000726; P:non-recombinational repair; IDA:EcoCyc. 
Interpro
 IPR018246; AP_endonuc_F2_Zn_BS.
 IPR001719; Endodeoxyribonuclease_IV.
 IPR013022; Xyl_isomerase-like_TIM-brl. 
Pfam
 PF01261; AP_endonuc_2 
SMART
 SM00518; AP2Ec 
PROSITE
 PS00729; AP_NUCLEASE_F2_1
 PS00730; AP_NUCLEASE_F2_2
 PS00731; AP_NUCLEASE_F2_3
 PS51432; AP_NUCLEASE_F2_4 
PRINTS