CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-004612
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 A/G-specific adenine glycosylase 
Protein Synonyms/Alias
  
Gene Name
 mutY 
Gene Synonyms/Alias
 micA; b2961; JW2928 
Created Date
 July 27, 2013 
Organism
 Escherichia coli (strain K12) 
NCBI Taxa ID
 83333 
Lysine Modification
Position
Peptide
Type
References
103VATLHGGKFPETFEEacetylation[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
 Adenine glycosylase active on G-A mispairs. MutY also corrects error-prone DNA synthesis past GO lesions which are due to the oxidatively damaged form of guanine: 7,8-dihydro-8- oxoguanine (8-oxo-dGTP). 
Sequence Annotation
 METAL 192 192 Iron-sulfur (4Fe-4S).
 METAL 199 199 Iron-sulfur (4Fe-4S).
 METAL 202 202 Iron-sulfur (4Fe-4S).
 METAL 208 208 Iron-sulfur (4Fe-4S).  
Keyword
 3D-structure; 4Fe-4S; Complete proteome; DNA damage; DNA repair; Glycosidase; Hydrolase; Iron; Iron-sulfur; Metal-binding; Reference proteome. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 350 AA 
Protein Sequence
MQASQFSAQV LDWYDKYGRK TLPWQIDKTP YKVWLSEVML QQTQVATVIP YFERFMARFP 60
TVTDLANAPL DEVLHLWTGL GYYARARNLH KAAQQVATLH GGKFPETFEE VAALPGVGRS 120
TAGAILSLSL GKHFPILDGN VKRVLARCYA VSGWPGKKEV ENKLWSLSEQ VTPAVGVERF 180
NQAMMDLGAM ICTRSKPKCS LCPLQNGCIA AANNSWALYP GKKPKQTLPE RTGYFLLLQH 240
EDEVLLAQRP PSGLWGGLYC FPQFADEESL RQWLAQRQIA ADNLTQLTAF RHTFSHFHLD 300
IVPMWLPVSS FTGCMDEGNA LWYNLAQPPS VGLAAPVERL LQQLRTGAPV 350 
Gene Ontology
 GO:0005622; C:intracellular; IEA:InterPro.
 GO:0051539; F:4 iron, 4 sulfur cluster binding; IEA:UniProtKB-KW.
 GO:0003677; F:DNA binding; IEA:InterPro.
 GO:0019104; F:DNA N-glycosylase activity; IEA:InterPro.
 GO:0004519; F:endonuclease activity; IEA:InterPro.
 GO:0016787; F:hydrolase activity; IDA:EcoCyc.
 GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
 GO:0006284; P:base-excision repair; IDA:EcoCyc. 
Interpro
 IPR011257; DNA_glycosylase.
 IPR004036; Endonuclease-III_CS2.
 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.
 IPR005760; MutY_bac.
 IPR015797; NUDIX_hydrolase_dom-like. 
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