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LOCUS WP_000026744 179 aa linear BCT 26-JUL-2024 ACCESSION WP_000026744 VERSION WP_000026744.1 KEYWORDS RefSeq. SOURCE Shigella flexneri ORGANISM Shigella flexneri Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria; Enterobacterales; Enterobacteriaceae; Shigella. REFERENCE 1 (residues 1 to 179) AUTHORS Makarova,K.S. and Grishin,N.V. TITLE The Zn-peptidase superfamily: functional convergence after evolutionary divergence JOURNAL J Mol Biol 292 (1), 11-17 (1999) PUBMED 10493853 REFERENCE 2 (residues 1 to 179) AUTHORS Rawlings,N.D. and Barrett,A.J. TITLE Evolutionary families of metallopeptidases JOURNAL Methods Enzymol 248, 183-228 (1995) PUBMED 7674922 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 11574951 Evidence Source :: NCBI SPARCLE ##Evidence-For-Name-Assignment-END## COMPLETENESS: full length. FEATURES Location/Qualifiers source 1..179 /organism="Shigella flexneri" /db_xref="taxon:623" Protein 1..179 /product="M48 family metallopeptidase" /EC_number="3.4.24.-" /GO_function="GO:0008237 - metallopeptidase activity [Evidence IEA]" /GO_function="GO:0008270 - zinc ion binding [Evidence IEA]" /GO_function="GO:0016787 - hydrolase activity [Evidence IEA]" /GO_function="GO:0046872 - metal ion binding [Evidence IEA]" /GO_process="GO:0006508 - proteolysis [Evidence IEA]" /calculated_mol_wt=20755 Region <122..172 /region_name="M48_yhfN_like" /note="Peptidase M48 YhfN-like, a novel minigluzincin; cd07344" /db_xref="CDD:320703" Site order(133..134,137,143) /site_type="active" /db_xref="CDD:320703" Site order(133,137,143) /site_type="other" /note="Zn binding site [ion binding]" /db_xref="CDD:320703" ORIGIN 1 msipffsfsw avmsnltylq gypeqllsqv rtlineqrlg dvlakrypgt hdyatdkalw 61 qytqdlknqf lrnappinkv mydnkihvlk nalglhtavs rvqgsklkak aeirvatvfr 121 napepflrmi vvhelahlke kehnkafyql cchmepqyhq lefdtrlwlt qlslgqdki