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Database: UniProt
Entry: A4J9Q8_DESRM
LinkDB: A4J9Q8_DESRM
Original site: A4J9Q8_DESRM 
ID   A4J9Q8_DESRM            Unreviewed;       476 AA.
AC   A4J9Q8;
DT   01-MAY-2007, integrated into UniProtKB/TrEMBL.
DT   01-MAY-2007, sequence version 1.
DT   07-JUN-2017, entry version 57.
DE   RecName: Full=M18 family aminopeptidase {ECO:0000256|RuleBase:RU004387};
DE            EC=3.4.11.- {ECO:0000256|RuleBase:RU004387};
GN   OrderedLocusNames=Dred_3311 {ECO:0000313|EMBL:ABO51811.1};
OS   Desulfotomaculum reducens (strain MI-1).
OC   Bacteria; Firmicutes; Clostridia; Clostridiales; Peptococcaceae;
OC   Desulfotomaculum.
OX   NCBI_TaxID=349161 {ECO:0000313|EMBL:ABO51811.1, ECO:0000313|Proteomes:UP000001556};
RN   [1] {ECO:0000313|EMBL:ABO51811.1, ECO:0000313|Proteomes:UP000001556}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MI-1 {ECO:0000313|EMBL:ABO51811.1,
RC   ECO:0000313|Proteomes:UP000001556};
RG   US DOE Joint Genome Institute;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA   Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H.,
RA   Pitluck S., Sims D., Brettin T., Bruce D., Han C., Tapia R.,
RA   Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N., Kim E.,
RA   Tebo B.M., Richardson P.;
RT   "Complete sequence of Desulfotomaculum reducens MI-1.";
RL   Submitted (MAR-2007) to the EMBL/GenBank/DDBJ databases.
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}.
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DR   EMBL; CP000612; ABO51811.1; -; Genomic_DNA.
DR   ProteinModelPortal; A4J9Q8; -.
DR   STRING; 349161.Dred_3311; -.
DR   MEROPS; M18.004; -.
DR   PRIDE; A4J9Q8; -.
DR   EnsemblBacteria; ABO51811; ABO51811; Dred_3311.
DR   KEGG; drm:Dred_3311; -.
DR   eggNOG; ENOG4105DFM; Bacteria.
DR   eggNOG; COG1362; LUCA.
DR   HOGENOM; HOG000056589; -.
DR   OMA; YQWVTIP; -.
DR   OrthoDB; POG091H01QL; -.
DR   BioCyc; DRED349161:GHP6-3358-MONOMER; -.
DR   Proteomes; UP000001556; Chromosome.
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:ABO51811.1};
KW   Complete proteome {ECO:0000313|Proteomes:UP000001556};
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:UP000001556};
KW   Zinc {ECO:0000256|RuleBase:RU004386}.
SQ   SEQUENCE   476 AA;  52337 MW;  716E5B3C21040AA7 CRC64;
     MFRSKKLGGQ LMNTRPEDLT YKRKNVWQQV NEETTKQIFD FAEGYKYFLT KGKTERTCVR
     EIINTAQSKG FIPVQQCQNL KAGDKIIISS KGKVVALAII GQKGLDMGIS LVGSHIDAPR
     LDLKPHPLYQ DEGLGLFKTH YYGGIKKYQW LAIPLALHGV ICKSNGQLVD VTIGDNPGDP
     VFTVTDLLPH LAKDQMAKKL MEAFEGEQLN LLIGGIPLQN GEKDTAVKLN ILKLLHQKYG
     ITEEDFISAE LEAVPAGPAY DVGLDRSMVG AYGQDDRVCV YTSLQGILDA NQPTRTAVAL
     FIDKEEIGST GNTGMMGRFL QNAVSEIGVR LYNQFNALAL YNIFEKSIAL SADVTAAVDP
     NFEGVLEKQN AAHLCGGVVI TKYTGVKGKY ETNDANAEYI AFIRNMLNQN NITWQTGELG
     KVDQGGGGTI AHMISELGFE VVDCGVPLLS MHAPMEIASK ADIFESYRTY KNFFMA
//
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