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Database: UniProt
Entry: A0A164R5R4_9NOCA
LinkDB: A0A164R5R4_9NOCA
Original site: A0A164R5R4_9NOCA 
ID   A0A164R5R4_9NOCA        Unreviewed;       425 AA.
AC   A0A164R5R4;
DT   06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT   06-JUL-2016, sequence version 1.
DT   27-SEP-2017, entry version 9.
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=A2J03_20390 {ECO:0000313|EMBL:KZF10936.1};
OS   Rhodococcus sp. EPR-157.
OC   Bacteria; Actinobacteria; Corynebacteriales; Nocardiaceae;
OC   Rhodococcus.
OX   NCBI_TaxID=1813677 {ECO:0000313|EMBL:KZF10936.1, ECO:0000313|Proteomes:UP000077673};
RN   [1] {ECO:0000313|EMBL:KZF10936.1, ECO:0000313|Proteomes:UP000077673}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=EPR-157 {ECO:0000313|EMBL:KZF10936.1,
RC   ECO:0000313|Proteomes:UP000077673};
RA   Ploux O.;
RL   Submitted (MAR-2016) to the EMBL/GenBank/DDBJ databases.
CC   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000256|HAMAP-
CC         Rule:MF_00467, ECO:0000256|RuleBase:RU004387};
CC   -!- SIMILARITY: Belongs to the peptidase M18 family.
CC       {ECO:0000256|HAMAP-Rule:MF_00467, ECO:0000256|RuleBase:RU004386}.
CC   -!- CAUTION: The sequence shown here is derived from an
CC       EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is
CC       preliminary data. {ECO:0000313|EMBL:KZF10936.1}.
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DR   EMBL; LVCV01000141; KZF10936.1; -; Genomic_DNA.
DR   RefSeq; WP_068370583.1; NZ_LVCV01000141.1.
DR   EnsemblBacteria; KZF10936; KZF10936; A2J03_20390.
DR   Proteomes; UP000077673; Unassembled WGS sequence.
DR   GO; GO:0004177; F:aminopeptidase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0008237; F:metallopeptidase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0008270; F:zinc ion binding; IEA:UniProtKB-UniRule.
DR   HAMAP; MF_00467; Aminopeptidase_M18_2; 1.
DR   InterPro; IPR022984; M18_aminopeptidase_2.
DR   InterPro; IPR001948; Peptidase_M18.
DR   Pfam; PF02127; Peptidase_M18; 1.
DR   PRINTS; PR00932; AMINO1PTASE.
PE   3: Inferred from homology;
KW   Aminopeptidase {ECO:0000256|HAMAP-Rule:MF_00467,
KW   ECO:0000256|RuleBase:RU004386, ECO:0000313|EMBL:KZF10936.1};
KW   Complete proteome {ECO:0000313|Proteomes:UP000077673};
KW   Hydrolase {ECO:0000256|HAMAP-Rule:MF_00467,
KW   ECO:0000256|RuleBase:RU004386};
KW   Metal-binding {ECO:0000256|HAMAP-Rule:MF_00467,
KW   ECO:0000256|RuleBase:RU004386};
KW   Metalloprotease {ECO:0000256|HAMAP-Rule:MF_00467,
KW   ECO:0000256|RuleBase:RU004386};
KW   Protease {ECO:0000256|HAMAP-Rule:MF_00467,
KW   ECO:0000256|RuleBase:RU004386};
KW   Reference proteome {ECO:0000313|Proteomes:UP000077673};
KW   Zinc {ECO:0000256|HAMAP-Rule:MF_00467, ECO:0000256|RuleBase:RU004386}.
FT   METAL        80     80       Zinc. {ECO:0000256|HAMAP-Rule:MF_00467}.
FT   METAL       154    154       Zinc. {ECO:0000256|HAMAP-Rule:MF_00467}.
FT   METAL       399    399       Zinc. {ECO:0000256|HAMAP-Rule:MF_00467}.
SQ   SEQUENCE   425 AA;  45064 MW;  AA42EF043F9E397E CRC64;
     MVPMSSNASA AGLCNFVDVS PSPFHVCRTV SVQLEEVGFV RVDETETWPA EAGRYYLIRG
     GSLVAWSTES SGPFRIVGGH TDSPNLRVKQ HPDLESAGWQ MVGLEPYGGA WLNSWLDRDL
     GISGRLSVRD GNGLREVLVK VDEPILRVPQ LAIHLSEDRK GVTLDPQRHV NAVWGVGNSP
     RSFLGYVAER EGVDPAAVLG WELMTHDLAP SAVVGVESEL VSAPRLDNQG TCYAGTQALI
     AAVENPTAAT PVLALFDHEE VGSMSDRGAF SDLLNTVLER IVLGRGGGRE EFLRTMAGSV
     CASGDMAHAT HPNYPDRHEP SHRIELGGGP VLKVNQNLRY ATDSAGAGAF ALACDQANVP
     LQRYVHRADL PCGSTIGPIT ASRTGLSTVD VGAAQLAMHS SRELMGASDV AAYADALGAF
     LAPAG
//
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