CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-006942
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Protein Xni 
Protein Synonyms/Alias
 Exonuclease IX; ExoIX 
Gene Name
 ygdG 
Gene Synonyms/Alias
 exo; xni; b2798; JW5446 
Created Date
 July 27, 2013 
Organism
 Escherichia coli (strain K12) 
NCBI Taxa ID
 83333 
Lysine Modification
Position
Peptide
Type
References
128ATIVSTDKGYCQLLSacetylation[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
 May have a role in processing of nucleic acids. It does not seem to be an exonuclease, as it can only bind 1 divalent metal cation, not the 2 that are thought to be necessary for exonuclease activity. 
Sequence Annotation
 METAL 9 9 Divalent metal cation (Potential).
 METAL 50 50 Divalent metal cation (Potential).
 METAL 102 102 Divalent metal cation (Potential).
 METAL 105 105 Divalent metal cation (Potential).
 METAL 127 127 Divalent metal cation (Potential).  
Keyword
 Coiled coil; Complete proteome; Metal-binding; Reference proteome. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 251 AA 
Protein Sequence
MAVHLLIVDA LNLIRRIHAV QGSPCVETCQ HALDQLIMHS QPTHAVAVFD DENRSSGWRH 60
QRLPDYKAGR PPMPEELHDE MPALRAAFEQ RGVPCWSTSG NEADDLAATL AVKVTQAGHQ 120
ATIVSTDKGY CQLLSPTLRI RDYFQKRWLD APFIDKEFGV QPQQLPDYWG LAGISSSKVP 180
GVAGIGPKSA TQLLVEFQSL EGIYENLDAV AEKWRKKLET HKEMAFLCRD IARLQTDLHI 240
DGNLQQLRLV R 251 
Gene Ontology
 GO:0008409; F:5'-3' exonuclease activity; IEA:InterPro.
 GO:0003677; F:DNA binding; IEA:InterPro.
 GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
 GO:0008152; P:metabolic process; IEA:GOC. 
Interpro
 IPR020046; 5-3_exonucl_a-hlix_arch_N.
 IPR020045; 5-3_exonuclease_C.
 IPR002421; 5-3_exonuclease_N.
 IPR008918; HhH2.
 IPR022895; Uncharacterised_YgdG. 
Pfam
 PF01367; 5_3_exonuc
 PF02739; 5_3_exonuc_N 
SMART
 SM00475; 53EXOc
 SM00279; HhH2 
PROSITE
  
PRINTS