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Database: UniProt
Entry: A0A0Q2U4I6_MYCGO
LinkDB: A0A0Q2U4I6_MYCGO
Original site: A0A0Q2U4I6_MYCGO 
ID   A0A0Q2U4I6_MYCGO        Unreviewed;       421 AA.
AC   A0A0Q2U4I6;
DT   20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT   20-JAN-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=AO501_25560 {ECO:0000313|EMBL:KQH75640.1};
OS   Mycobacterium gordonae.
OC   Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC   Mycobacterium.
OX   NCBI_TaxID=1778 {ECO:0000313|EMBL:KQH75640.1, ECO:0000313|Proteomes:UP000051677};
RN   [1] {ECO:0000313|EMBL:KQH75640.1, ECO:0000313|Proteomes:UP000051677}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CTRI 14-8773 {ECO:0000313|EMBL:KQH75640.1,
RC   ECO:0000313|Proteomes:UP000051677};
RA   Ustinova V., Smirnova T., Blagodatskikh K., Varlamov D., Larionova E.,
RA   Chernousova L.;
RT   "Mycobacterium gordonae draft genome assembly.";
RL   Submitted (OCT-2015) 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:KQH75640.1}.
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DR   EMBL; LKTM01000372; KQH75640.1; -; Genomic_DNA.
DR   RefSeq; WP_055581495.1; NZ_LKTM01000372.1.
DR   EnsemblBacteria; KQH75640; KQH75640; AO501_25560.
DR   Proteomes; UP000051677; 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:KQH75640.1};
KW   Complete proteome {ECO:0000313|Proteomes:UP000051677};
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:UP000051677};
KW   Zinc {ECO:0000256|HAMAP-Rule:MF_00467, ECO:0000256|RuleBase:RU004386}.
FT   METAL        76     76       Zinc. {ECO:0000256|HAMAP-Rule:MF_00467}.
FT   METAL       150    150       Zinc. {ECO:0000256|HAMAP-Rule:MF_00467}.
FT   METAL       395    395       Zinc. {ECO:0000256|HAMAP-Rule:MF_00467}.
SQ   SEQUENCE   421 AA;  44513 MW;  672E926E88079510 CRC64;
     MVATAPGLGE FIDASPSPFH ACATAAARLR DAGYTELSEF DRWPEQPGRH FILRAGSLVA
     WSGSAGLTPF RIVGAHTDSP NLRVKQHPDR CVAGWKVVAL EPYGGAWLNS WLDRDLGISG
     RLSVRDGSGV SHRLVRIDEP ILRVPQLAIH LAEDRKSLAL DPQRHLNAVW GVGSVAESFV
     GYVAEAAGVA GDDVLSADLM THDLTPSTVV GADGSLLSAP RLDNQASCYA GLEALLALDA
     EPTEFLPVLV LFDHEEVGST SDHGAQSNLL GTVLERIVLT AGGNREDFLR LLPASLLASA
     DMAHATHPNY PERHEPGHQI AVNGGPVLKV HPNLRYATDG RTAAAFALAC EQAGVPLQRY
     EHRADLPCGS TIGPMASART GIPTVDVGAP QLAMHSAREL MGAHDVGAYA AALQAFLAPQ
     A
//
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