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Database: UniProt
Entry: A0A177YGA4_9NOCA
LinkDB: A0A177YGA4_9NOCA
Original site: A0A177YGA4_9NOCA 
ID   A0A177YGA4_9NOCA        Unreviewed;       425 AA.
AC   A0A177YGA4;
DT   07-SEP-2016, integrated into UniProtKB/TrEMBL.
DT   07-SEP-2016, sequence version 1.
DT   27-SEP-2017, entry version 8.
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=A3K89_04110 {ECO:0000313|EMBL:OAK54547.1};
OS   Rhodococcus kyotonensis.
OC   Bacteria; Actinobacteria; Corynebacteriales; Nocardiaceae;
OC   Rhodococcus.
OX   NCBI_TaxID=398843 {ECO:0000313|EMBL:OAK54547.1, ECO:0000313|Proteomes:UP000077519};
RN   [1] {ECO:0000313|EMBL:OAK54547.1, ECO:0000313|Proteomes:UP000077519}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=KB10 {ECO:0000313|EMBL:OAK54547.1,
RC   ECO:0000313|Proteomes:UP000077519};
RA   Jeong H., Hong C.E., Jo S.H., Park J.M.;
RT   "Genome sequence of Rhodococcus kyotonensis KB10.";
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:OAK54547.1}.
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DR   EMBL; LVHI01000012; OAK54547.1; -; Genomic_DNA.
DR   RefSeq; WP_068424930.1; NZ_LVHI01000012.1.
DR   EnsemblBacteria; OAK54547; OAK54547; A3K89_04110.
DR   Proteomes; UP000077519; 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:OAK54547.1};
KW   Complete proteome {ECO:0000313|Proteomes:UP000077519};
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:UP000077519};
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;  45088 MW;  3608C4B2C25F631E CRC64;
     MVPMSSNATA AGLCNFVDVS PSPFHVCRTV SVQLEEVGFV RVEETEAWPT EPGKYYLIRG
     GSLVAWSTHA DGPFRIVGGH TDSPNLRVKQ NPDLESAGWQ MVGLEPYGGA WLNSWLDRDL
     GISGRLSVRD GNSLREVLVK VDEPILRVPQ LAIHLSEDRK GVTLDPQRHV NAIWGVGNSP
     RSFVDYVAAL EGVEPTDVLG WELMTHDLAP SAIVGVGSEL VSAPRLDNQG TCYAGTQALI
     AAVAAPTDVT PVLALFDHEE VGSMSDRGAF SDLLNTVLER IVLGRGGGRE EFLRTMAGSI
     CASGDMAHAT HPNYPDRHEP AHRIELGGGP VLKVNQNLRY ATDSAGAGAF ALACDQAGVP
     LQRYVHRADL PCGSTIGPIT ASRTGLSTVD VGAAQLAMHS SRELMGASDI TAYADALAAF
     LAPAA
//
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