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Database: UniProt
Entry: A0A0F4JKS7_9ACTN
LinkDB: A0A0F4JKS7_9ACTN
Original site: A0A0F4JKS7_9ACTN 
ID   A0A0F4JKS7_9ACTN        Unreviewed;       437 AA.
AC   A0A0F4JKS7;
DT   24-JUN-2015, integrated into UniProtKB/TrEMBL.
DT   24-JUN-2015, sequence version 1.
DT   27-SEP-2017, entry version 11.
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=VR45_19315 {ECO:0000313|EMBL:KJY33561.1};
OS   Streptomyces sp. NRRL S-495.
OC   Bacteria; Actinobacteria; Streptomycetales; Streptomycetaceae;
OC   Streptomyces.
OX   NCBI_TaxID=1609133 {ECO:0000313|EMBL:KJY33561.1, ECO:0000313|Proteomes:UP000033484};
RN   [1] {ECO:0000313|EMBL:KJY33561.1, ECO:0000313|Proteomes:UP000033484}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NRRL S-495 {ECO:0000313|EMBL:KJY33561.1,
RC   ECO:0000313|Proteomes:UP000033484};
RA   Ju K.-S., Doroghazi J.R., Metcalf W.;
RL   Submitted (FEB-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:KJY33561.1}.
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DR   EMBL; JZWY01000367; KJY33561.1; -; Genomic_DNA.
DR   RefSeq; WP_045941042.1; NZ_JZWY01000367.1.
DR   EnsemblBacteria; KJY33561; KJY33561; VR45_19315.
DR   Proteomes; UP000033484; 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:KJY33561.1};
KW   Complete proteome {ECO:0000313|Proteomes:UP000033484};
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:UP000033484};
KW   Zinc {ECO:0000256|HAMAP-Rule:MF_00467, ECO:0000256|RuleBase:RU004386}.
FT   METAL        89     89       Zinc. {ECO:0000256|HAMAP-Rule:MF_00467}.
FT   METAL       160    160       Zinc. {ECO:0000256|HAMAP-Rule:MF_00467}.
FT   METAL       413    413       Zinc. {ECO:0000256|HAMAP-Rule:MF_00467}.
SQ   SEQUENCE   437 AA;  46462 MW;  2347E4754EED334C CRC64;
     MSTAARQAFF DRTHTDDLIA FLGTSPSPYH AVASAAERLE KAGFRQVLET DAWDGVAGGR
     YVVRGGALIA WYVPAGAGPE TPFRVVGTHT DSPNLRVKPI PDTGTAGWRQ VAVEIYGGVP
     LNTWLDRDLG LSGRITLRDG SRRLVQLDEP LLRVPQLAIH LDRQVNEGMK LDKQRHLTPI
     WGLGPVDEGA LIEYVAERAG VDPAEVSGWD LMTHDVQPAS YLGRDRELLA GPRLDNLLSV
     HAATAALAAV ATAAETEGAA LPYIPVLAAF DHEETGSESD TGAQSPLLGN VLERSVYARG
     GGLEDRARAL AGTVCLSSDM GHAVHPNYSE RHEPGHHPMP NAGPILKVNV NNRYATDGVG
     RAVFTAACEK AGVPWQTFVS NNAMPCGTTI GPITAARLGI QTVDCGIAAL SMHSARELCG
     AEDPYLLASA IKAFLEG
//
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