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LOCUS WP_001189614 516 aa linear BCT 13-MAR-2021 ACCESSION WP_001189614 VERSION WP_001189614.1 KEYWORDS RefSeq. SOURCE Escherichia coli ORGANISM Escherichia coli Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria; Enterobacterales; Enterobacteriaceae; Escherichia. REFERENCE 1 (residues 1 to 516) AUTHORS Singh,S.K., Roberts,S.A., McDevitt,S.F., Weichsel,A., Wildner,G.F., Grass,G.B., Rensing,C. and Montfort,W.R. TITLE Crystal structures of multicopper oxidase CueO bound to copper(I) and silver(I): functional role of a methionine-rich sequence JOURNAL J Biol Chem 286 (43), 37849-37857 (2011) PUBMED 21903583 COMMENT REFSEQ: This record represents a single, non-redundant, protein sequence which may be annotated on many different RefSeq genomes from the same, or different, species. ##Evidence-For-Name-Assignment-START## Evidence Category :: HMM Evidence Accession :: NF008205.1 Evidence Source :: NCBI Protein Cluster (PRK) Source Identifier :: PRK10965 ##Evidence-For-Name-Assignment-END## COMPLETENESS: full length. FEATURES Location/Qualifiers source 1..516 /organism="Escherichia coli" /db_xref="taxon:562" gene 1..516 /gene="cueO" Protein 1..516 /product="multicopper oxidase CueO" /EC_number="1.16.3.1" /GO_function="GO:0005507 - copper ion binding [Evidence IEA]" /GO_function="GO:0016491 - oxidoreductase activity [Evidence IEA]" /calculated_mol_wt=56571 Region 1..516 /region_name="PRK10965" /note="multicopper oxidase; Provisional" /db_xref="CDD:236810" ORIGIN 1 mqrrdflkys valgvasalp lwsravfaae rptlpipdll ttdarnriql tigagqstfg 61 ektattwgyn gnllgpavkl qrgkavtvdi ynqlteettl hwhglevpge vdggpqgiip 121 pggkrsvtln vdqpaatcwf hphqhgktgr qvamglaglv vieddeilkl mlpkqwgidd 181 vpvivqdkkf sadgqidyql dvmtaavgwf gdtlltngai ypqhaaprgw lrlrllngcn 241 arslnfatsd nrplyviasd ggllpepvkv nelpvlmger fevlvevndn kpfdlvtlpv 301 sqmgmaiapf dkphpvmriq piaisasgal pdtlsslpal pslegltvrk lqlsmdpmld 361 mmgmqmlmek ygdqamvgmd hsqmmghmgh gnmnhmnhgg kfdfhhanki ngqafdmnkp 421 mfaaakgqye rwvisgvgdm mlhpfhihgt qfrilsengk ppaahragwk dtvkvegnvs 481 evlvkfnhda pkeraymahc hllehedtgm mlgftv