CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-002201
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Exodeoxyribonuclease 7 large subunit 
Protein Synonyms/Alias
 Exodeoxyribonuclease VII large subunit; Exonuclease VII large subunit 
Gene Name
 xseA 
Gene Synonyms/Alias
 b2509; JW2493 
Created Date
 July 27, 2013 
Organism
 Escherichia coli (strain K12) 
NCBI Taxa ID
 83333 
Lysine Modification
Position
Peptide
Type
References
113GEGLLQQKYEQLKAKacetylation[1]
161HDILHVLKRRDPSLPacetylation[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
 Bidirectionally degrades single-stranded DNA into large acid-insoluble oligonucleotides, which are then degraded further into small acid-soluble oligonucleotides. It can also degrade 3' or 5' ss regions extending from the termini of duplex DNA molecules and displaced ss regions. 
Sequence Annotation
  
Keyword
 Complete proteome; Cytoplasm; Direct protein sequencing; Exonuclease; Hydrolase; Nuclease; Reference proteome. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 456 AA 
Protein Sequence
MLPSQSPAIF TVSRLNQTVR LLLEHEMGQV WISGEISNFT QPASGHWYFT LKDDTAQVRC 60
AMFRNSNRRV TFRPQHGQQV LVRANITLYE PRGDYQIIVE SMQPAGEGLL QQKYEQLKAK 120
LQAEGLFDQQ YKKPLPSPAH CVGVITSKTG AALHDILHVL KRRDPSLPVI IYPAAVQGDD 180
APGQIVRAIE LANQRNECDV LIVGRGGGSL EDLWSFNDER VARAIFTSRI PVVSAVGHET 240
DVTIADFVAD LRAPTPSAAA EVVSRNQQEL LRQVQSTRQR LEMAMDYYLA NRTRRFTQIH 300
HRLQQQHPQL RLARQQTMLE RLQKRMSFAL ENQLKRTGQQ QQRLTQRLNQ QNPQPKIHRA 360
QTRIQQLEYR LAETLRAQLS ATRERFGNAV THLEAVSPLS TLARGYSVTT ATDGNVLKKV 420
KQVKAGEMLT TRLEDGWIES EVKNIQPVKK SRKKVH 456 
Gene Ontology
 GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
 GO:0009318; C:exodeoxyribonuclease VII complex; IEA:InterPro.
 GO:0008855; F:exodeoxyribonuclease VII activity; IEA:HAMAP.
 GO:0003676; F:nucleic acid binding; IEA:InterPro.
 GO:0006308; P:DNA catabolic process; IEA:HAMAP.
 GO:0090305; P:nucleic acid phosphodiester bond hydrolysis; IEA:GOC. 
Interpro
 IPR003753; Exonuc_VII_L.
 IPR020579; Exonuc_VII_lsu_C.
 IPR025824; OB-fold_nuc-bd_dom. 
Pfam
 PF02601; Exonuc_VII_L
 PF13742; tRNA_anti_2 
SMART
  
PROSITE
  
PRINTS