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Database: UniProt
Entry: T0P9F3_9CLOT
LinkDB: T0P9F3_9CLOT
Original site: T0P9F3_9CLOT 
ID   T0P9F3_9CLOT            Unreviewed;       468 AA.
AC   T0P9F3;
DT   16-OCT-2013, integrated into UniProtKB/TrEMBL.
DT   16-OCT-2013, sequence version 1.
DT   07-JUN-2017, entry version 17.
DE   RecName: Full=M18 family aminopeptidase {ECO:0000256|RuleBase:RU004387};
DE            EC=3.4.11.- {ECO:0000256|RuleBase:RU004387};
GN   ORFNames=M918_13725 {ECO:0000313|EMBL:EQB86548.1};
OS   Clostridium sp. BL8.
OC   Bacteria; Firmicutes; Clostridia; Clostridiales; Clostridiaceae;
OC   Clostridium.
OX   NCBI_TaxID=1354301 {ECO:0000313|EMBL:EQB86548.1, ECO:0000313|Proteomes:UP000015873};
RN   [1] {ECO:0000313|EMBL:EQB86548.1, ECO:0000313|Proteomes:UP000015873}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=BL8 {ECO:0000313|EMBL:EQB86548.1,
RC   ECO:0000313|Proteomes:UP000015873};
RX   PubMed=25076986; DOI=10.1186/1757-4749-6-30;
RA   Marathe N.P., Shetty S.A., Lanjekar V.B., Rasane M.H., Ranade D.R.,
RA   Shouche Y.S.;
RT   "Genome sequencing of multidrug resistant novel Clostridium sp. BL8
RT   reveals its potential for pathogenicity.";
RL   Gut Pathog 6:30-30(2014).
CC   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC         Evidence={ECO:0000256|RuleBase:RU004387};
CC   -!- SIMILARITY: Belongs to the peptidase M18 family.
CC       {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:EQB86548.1}.
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DR   EMBL; AUPA01000220; EQB86548.1; -; Genomic_DNA.
DR   RefSeq; WP_021284982.1; NZ_AUPA01000220.1.
DR   EnsemblBacteria; EQB86548; EQB86548; M918_13725.
DR   PATRIC; fig|1354301.3.peg.3864; -.
DR   OrthoDB; POG091H01QL; -.
DR   Proteomes; UP000015873; Unassembled WGS sequence.
DR   GO; GO:0004177; F:aminopeptidase activity; IEA:UniProtKB-KW.
DR   GO; GO:0008237; F:metallopeptidase activity; IEA:UniProtKB-KW.
DR   GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR   InterPro; IPR001948; Peptidase_M18.
DR   Pfam; PF02127; Peptidase_M18; 1.
DR   PRINTS; PR00932; AMINO1PTASE.
PE   3: Inferred from homology;
KW   Aminopeptidase {ECO:0000256|RuleBase:RU004386,
KW   ECO:0000313|EMBL:EQB86548.1};
KW   Complete proteome {ECO:0000313|Proteomes:UP000015873};
KW   Hydrolase {ECO:0000256|RuleBase:RU004386};
KW   Metal-binding {ECO:0000256|RuleBase:RU004386};
KW   Metalloprotease {ECO:0000256|RuleBase:RU004386};
KW   Protease {ECO:0000256|RuleBase:RU004386};
KW   Reference proteome {ECO:0000313|Proteomes:UP000015873};
KW   Zinc {ECO:0000256|RuleBase:RU004386}.
SQ   SEQUENCE   468 AA;  51959 MW;  FBDE282517A3A214 CRC64;
     MGDYNKLVKK YELAWDKYTK EDLDKVFALS ERYIDFMSKC KTERECVNEF IVLAEKEGYR
     DINSYIAEGK KLQAGDKVYA NCMGKTLALF LIGSEPVEKG FKILGAHVDS PRLDLKQNPL
     YEDSDFAMLK THYYGGVKKY QWVTIPLAIH GVVIKKDGTT VNVVIGEDEK EPVVGISDLL
     IHLAGDQMAK TLAKGIEGES LNVCLGSMPI EDKEAKNRVK LNALRLLNEK YGIDEEDFVS
     AELEVVPAGR ARSYGLDSSM VMAYGHDDRI CAYTSFEAML NIKETDKTII TLLVDKEEVG
     SIGATGMQSR FFENTVAEIV NLMGDYSDLK VRRALANSKM LSSDVSAAFD PNYPSVSEKQ
     NNAFFGKGIV FNKYTGARGK GGCNDANPEF IAELRRIMEK HNVSWQTSEL GKVDQGGGGT
     IAYILAEYGM EVIDSGVALH NMHAPWEIAS KADIYEACRG YEAFLIEA
//
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