ID A0AAE4ZK69_RHOHA Unreviewed; 433 AA. AC A0AAE4ZK69; DT 29-MAY-2024, integrated into UniProtKB/TrEMBL. DT 29-MAY-2024, sequence version 1. DT 24-JUL-2024, entry version 2. DE RecName: Full=Probable M18 family aminopeptidase 2 {ECO:0000256|HAMAP-Rule:MF_00467}; DE EC=3.4.11.- {ECO:0000256|HAMAP-Rule:MF_00467}; GN Name=apeB {ECO:0000256|HAMAP-Rule:MF_00467}; GN ORFNames=GS505_19305 {ECO:0000313|EMBL:NKS27921.1}; OS Rhodococcus hoagii (Corynebacterium equii). OC Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Nocardiaceae; OC Prescottella. OX NCBI_TaxID=43767 {ECO:0000313|EMBL:NKS27921.1, ECO:0000313|Proteomes:UP000605618}; RN [1] {ECO:0000313|EMBL:NKS27921.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=Lh_141_1 {ECO:0000313|EMBL:NKS27921.1}; RX PubMed=32291839; RA Huber L., Giguere S., Slovis N.M., Alvarez-Narvaez S., Hart K.A., RA Greiter M., Morris E.R.A., Cohen N.D.; RT "The novel and transferable erm(51) gene confers Macrolides, Lincosamides, RT and Streptogramins B (MLSB) resistance to clonal Rhodococcus equi in the RT environment."; RL Environ. Microbiol. 0:0-0(2020). CC -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|ARBA:ARBA00001947, CC ECO:0000256|HAMAP-Rule:MF_00467, ECO:0000256|RuleBase:RU004387}; CC -!- SIMILARITY: Belongs to the peptidase M18 family. CC {ECO:0000256|ARBA:ARBA00008290, ECO:0000256|HAMAP-Rule:MF_00467, CC ECO:0000256|RuleBase:RU004386}. CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ CC whole genome shotgun (WGS) entry which is preliminary data. CC {ECO:0000313|EMBL:NKS27921.1}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; WUYZ01000007; NKS27921.1; -; Genomic_DNA. DR Proteomes; UP000605618; Unassembled WGS sequence. DR GO; GO:0004177; F:aminopeptidase activity; IEA:UniProtKB-KW. DR CDD; cd05658; M18_DAP; 1. DR Gene3D; 2.30.250.10; Aminopeptidase i, Domain 2; 1. DR Gene3D; 3.40.630.10; Zn peptidases; 1. DR HAMAP; MF_00467; Aminopeptidase_M18_2; 1. DR InterPro; IPR022984; M18_aminopeptidase_2. DR InterPro; IPR001948; Peptidase_M18. DR InterPro; IPR023358; Peptidase_M18_dom2. DR PANTHER; PTHR28570; ASPARTYL AMINOPEPTIDASE; 1. DR PANTHER; PTHR28570:SF3; ASPARTYL AMINOPEPTIDASE; 1. DR Pfam; PF02127; Peptidase_M18; 1. DR PRINTS; PR00932; AMINO1PTASE. DR SUPFAM; SSF101821; Aminopeptidase/glucanase lid domain; 1. DR SUPFAM; SSF53187; Zn-dependent exopeptidases; 1. PE 3: Inferred from homology; KW Aminopeptidase {ECO:0000256|ARBA:ARBA00022438, ECO:0000256|HAMAP- KW Rule:MF_00467}; KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|HAMAP-Rule:MF_00467}; KW Metal-binding {ECO:0000256|ARBA:ARBA00022723, ECO:0000256|HAMAP- KW Rule:MF_00467}; KW Metalloprotease {ECO:0000256|ARBA:ARBA00023049, ECO:0000256|HAMAP- KW Rule:MF_00467}; KW Protease {ECO:0000256|ARBA:ARBA00022670, ECO:0000256|HAMAP-Rule:MF_00467}; KW Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|HAMAP-Rule:MF_00467}. FT BINDING 88 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00467" FT BINDING 162 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00467" FT BINDING 407 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00467" SQ SEQUENCE 433 AA; 45744 MW; E7F6DE96F7325657 CRC64; MMVGMPSMTQ ADAQGLCSFV DASPSPFHVC ATVASELSAN GFTELQETDA WPSAPGRYYL VRGGSLIAWS TEGVSAGPAS PFRIVGGHTD SPNLRVKQHP DLVSAGWQLV GLEPYGGAWL NSWLDRDLGI SGRLSVRAGD AVQEVLVRVD RPILRVPQLA IHLSEERKGV QLDPQRHLNA VWGTGSEPRS FIGFLADEAG VAAEAVLGWE LMTHDLAPST VVGEDASLVS APRLDNQGTC YAGTQALLAA VAEPGDSTPV LALFDHEEVG SMSDRGAFSD LLNSVLERIV LLRGGGREDF LRAMSGSVCA SGDMAHATHP NYPDRHEPAH RIAINGGPVL KVNQNLRYAS DAAGAAEFAL ACDRAGVPLQ RYVHRADLPC GSTIGPITAS RTGLSTVDVG APQLAMHSAR ELMGARDVGM YADALAAFLT PVR //