LOCUS CAQ43701.1 270 aa PRT BCT 06-FEB-2015 DEFINITION Stenotrophomonas maltophilia K279a putative formamidopyrimidine- dna glycosylase (fapy-dna glycosylase) (dna-(apurinic or apyrimidinic site) lyase mutm) protein. ACCESSION AM743169-83 PROTEIN_ID CAQ43701.1 SOURCE Stenotrophomonas maltophilia K279a ORGANISM Stenotrophomonas maltophilia K279a Bacteria; Proteobacteria; Gammaproteobacteria; Xanthomonadales; Xanthomonadaceae; Stenotrophomonas; Stenotrophomonas maltophilia group. REFERENCE 1 (bases 1 to 4851126) AUTHORS Crossman L.C. JOURNAL Submitted (24-MAY-2007) to the INSDC. Crossman L.C., Pathogen Sequencing Unit, The Wellcome Trust Sanger Institute, Hinxton, Cambridge, Cambridgeshire, CB10 1SA, UNITED KINGDOM. REFERENCE 2 AUTHORS Crossman L.C., Gould V.C., Dow J.M., Vernikos G.S., Okazaki A., Sebaihia M., Saunders D., Arrowsmith C., Carver T., Peters N., Adlem E., Kerhornou A., Lord A., Murphy L., Seeger K., Squares R., Rutter S., Quail M.A., Rajandream M.A., Harris D., Churcher C., Bentley S.D., Parkhill J., Thomson N.R., Avison M.B. TITLE The complete genome, comparative and functional analysis of Stenotrophomonas maltophilia reveals an organism heavily shielded by drug resistance determinants JOURNAL Genome Biol. 9(4), R74-R74(2008). PUBMED 18419807 FEATURES Qualifiers source /organism="Stenotrophomonas maltophilia K279a" /strain="K279a" /mol_type="genomic DNA" /country="United Kingdom" /db_xref="taxon:522373" protein /transl_table=11 /gene="fpg" /gene_synonym="mutM" /locus_tag="Smlt0090" /EC_number="4.2.99.18" /note="similarity:fasta; with=UniProt:Q9L7T2 (EMBL:AE004473;); Pseudomonas aeruginosa.; mutM; Formamidopyrimidine-DNA glycosylase (EC 3.2.2.23) (Fapy-DNA glycosylase) (DNA-(apurinic or apyrimidinic site) lyase mutM) (EC 4.2.99.18) (AP lyase mutM).; length=269; id 60.967%; ungapped id 60.967%; E()=7.7e-57; 269 aa overlap; query 2-270; subject 1-269" /note="similarity:fasta; with=UniProt:Q8P3C4 (EMBL:AE012540;); Xanthomonas campestris pv. campestris.; mutM; Formamidopyrimidine-DNA glycosylase (EC 3.2.2.23) (Fapy-DNA glycosylase) (DNA-(apurinic or apyrimidinic site) lyase mutM) (EC 4.2.99.18) (AP lyase mutM).; length=270; id 79.630%; ungapped id 79.926%; E()=2.5e-76; 270 aa overlap; query 2-270; subject 1-270" /db_xref="EnsemblGenomes-Gn:Smlt0090" /db_xref="EnsemblGenomes-Tr:CAQ43701" /db_xref="GOA:B2FU49" /db_xref="InterPro:IPR000214" /db_xref="InterPro:IPR010663" /db_xref="InterPro:IPR010979" /db_xref="InterPro:IPR012319" /db_xref="InterPro:IPR015886" /db_xref="InterPro:IPR015887" /db_xref="InterPro:IPR020629" /db_xref="InterPro:IPR035937" /db_xref="UniProtKB/Swiss-Prot:B2FU49" BEGIN 1 MPELPEVETT RRGLAPHLQG RRVHGVILRR ADLRWPIPPE VAELLPGQRI EDIRRRAKYL 61 LLDTAIGSAV LHLGMSGSLR VLPGDTPLRA HDHVDISLDN GRLLRFNDPR RFGSLLWQPA 121 GEVHPLLQGL GPEPLDDAFD GDYLFARSRG RSAPVKTFLM DQAVVVGVGN IYAAESLFKA 181 GISPLREAGK ISRERYQRLA DAVKEILGYA ITRGGTTLRD FISPDGAPGY FEQELLVYGR 241 DGLPCPNCGR ALKHATIGQR ASVWCSHCQR //