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LOCUS WP_000186740 225 aa linear BCT 19-FEB-2025 ACCESSION WP_000186740 VERSION WP_000186740.1 KEYWORDS RefSeq. SOURCE Escherichia ORGANISM Escherichia Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria; Enterobacterales; Enterobacteriaceae. REFERENCE 1 (residues 1 to 225) AUTHORS Steczkiewicz,K., Muszewska,A., Knizewski,L., Rychlewski,L. and Ginalski,K. TITLE Sequence, structure and functional diversity of PD-(D/E)XK phosphodiesterase superfamily JOURNAL Nucleic Acids Res 40 (15), 7016-7045 (2012) PUBMED 22638584 REFERENCE 2 (residues 1 to 225) AUTHORS Zhang,J., McCabe,K.A. and Bell,C.E. TITLE Crystal structures of lambda exonuclease in complex with DNA suggest an electrostatic ratchet mechanism for processivity JOURNAL Proc Natl Acad Sci U S A 108 (29), 11872-11877 (2011) PUBMED 21730170 REFERENCE 3 (residues 1 to 225) AUTHORS Kovall,R. and Matthews,B.W. TITLE Toroidal structure of lambda-exonuclease JOURNAL Science 277 (5333), 1824-1827 (1997) PUBMED 9295273 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 :: Conserved Domain (CDD) Evidence Accession :: Domain architecture ID 16909715 Evidence Source :: NCBI SPARCLE ##Evidence-For-Name-Assignment-END## COMPLETENESS: full length. FEATURES Location/Qualifiers source 1..225 /organism="Escherichia" /db_xref="taxon:561" Protein 1..225 /product="lambda exonuclease family protein" /EC_number="3.1.11.3" /GO_function="GO:0004527 - exonuclease activity [Evidence IEA]" /GO_function="GO:0046872 - metal ion binding [Evidence IEA]" /calculated_mol_wt=25669 Region 18..207 /region_name="PDDEXK_lambda_exonuclease-like" /note="Uncharacterized nucleases similar to lambda phage exonuclease; cd22343" /db_xref="CDD:411747" Site order(85,119,129,131) /site_type="active" /db_xref="CDD:411747" ORIGIN 1 mtpdiilqrt gidvraveqg ddawhklrlg vitaseihnv iakprsgkkw pdmkmsyfht 61 llaevctgva pevnakalaw gkqyendart lfeftsgvnv tespiiyrde smrtacspdg 121 lcsdgnglel kcpftsrdfm kfrlggfeai ksaymaqvqy smwvtrkdaw yfanydprmk 181 reglhyvvie rnekymasfd emvpefiekm dealaeigfv ygeqw