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Database: UniProt
Entry: A0A171B102_9ACTN
LinkDB: A0A171B102_9ACTN
Original site: A0A171B102_9ACTN 
ID   A0A171B102_9ACTN        Unreviewed;       437 AA.
AC   A0A171B102;
DT   06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT   06-JUL-2016, sequence version 1.
DT   28-MAR-2018, 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=STXM2123_4916 {ECO:0000313|EMBL:GAT84215.1};
OS   Streptomyces sp. F-3.
OC   Bacteria; Actinobacteria; Streptomycetales; Streptomycetaceae;
OC   Streptomyces.
OX   NCBI_TaxID=1840095 {ECO:0000313|EMBL:GAT84215.1, ECO:0000313|Proteomes:UP000078145};
RN   [1] {ECO:0000313|EMBL:GAT84215.1, ECO:0000313|Proteomes:UP000078145}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Wang L.S., Gao P.J., Liu L., Zhang H.Q., Cheng Z., Sun X.M.;
RT   "Streptomyces sp. F-3 geneom sequencing.";
RL   Submitted (MAY-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:GAT84215.1}.
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DR   EMBL; BDDR01000040; GAT84215.1; -; Genomic_DNA.
DR   EnsemblBacteria; GAT84215; GAT84215; STXM2123_4916.
DR   Proteomes; UP000078145; 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   Gene3D; 2.30.250.10; -; 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; PTHR28570; 1.
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:GAT84215.1};
KW   Complete proteome {ECO:0000313|Proteomes:UP000078145};
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:UP000078145};
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;  46499 MW;  75A209264EBD4C47 CRC64;
     MNPMSTSQRF DRGHTDDLMS FLAASPSPYH AAANAAARLE KAGFRRVAET DAWDGTSGGK
     YVLRGGAIVA WYVPEGAAPH TPFRIVGAHT DSPNLRVKPL PDTGAHGWRQ VAVEIYGGPL
     LNSWLDRDLG LAGRLTLRDG SSHLVNIDRP LLRVPQLAIH LDRSVTTEGL KLDKQRHLQP
     VWGLGDDVRD GDLIAFLEQE AGIPAGEVAG WDLMTHSVEP PAYLGRDREL VAGPRMDNLL
     SVHAGTAALA AVATGPGAAK LPYIPVLAAF DHEENGSQSD TGADGPLLGT VLERSVFARS
     GTYEDRARAF AGTVCLSSDT GHAVHPNYAE RHDPTHHPRA GGGPILKVNV NNRYATDGSG
     RAVWVAACEK AQVPFQSFVS NNSMPCGTTI GPITAARHGI RTVDIGVAIL SMHSARELCA
     ANDPFMLANA LVAFLEG
//
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