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Database: UniProt
Entry: F2NJ69_DESAR
LinkDB: F2NJ69_DESAR
Original site: F2NJ69_DESAR 
ID   F2NJ69_DESAR            Unreviewed;       471 AA.
AC   F2NJ69;
DT   31-MAY-2011, integrated into UniProtKB/TrEMBL.
DT   31-MAY-2011, sequence version 1.
DT   25-OCT-2017, entry version 37.
DE   RecName: Full=M18 family aminopeptidase {ECO:0000256|RuleBase:RU004387};
DE            EC=3.4.11.- {ECO:0000256|RuleBase:RU004387};
GN   OrderedLocusNames=Desac_0130 {ECO:0000313|EMBL:AEB08027.1};
OS   Desulfobacca acetoxidans (strain ATCC 700848 / DSM 11109 / ASRB2).
OC   Bacteria; Proteobacteria; Deltaproteobacteria; Syntrophobacterales;
OC   Syntrophaceae; Desulfobacca.
OX   NCBI_TaxID=880072 {ECO:0000313|EMBL:AEB08027.1, ECO:0000313|Proteomes:UP000000483};
RN   [1] {ECO:0000313|Proteomes:UP000000483}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 700848 / DSM 11109 / ASRB2
RC   {ECO:0000313|Proteomes:UP000000483};
RG   US DOE Joint Genome Institute (JGI-PGF);
RA   Lucas S., Copeland A., Lapidus A., Bruce D., Goodwin L., Pitluck S.,
RA   Peters L., Kyrpides N., Mavromatis K., Ivanova N., Ovchinnikova G.,
RA   Teshima H., Detter J.C., Han C., Land M., Hauser L., Markowitz V.,
RA   Cheng J.-F., Hugenholtz P., Woyke T., Wu D., Spring S., Schueler E.,
RA   Brambilla E., Klenk H.-P., Eisen J.A.;
RT   "The complete genome of Desulfobacca acetoxidans DSM 11109.";
RL   Submitted (MAR-2011) 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; CP002629; AEB08027.1; -; Genomic_DNA.
DR   RefSeq; WP_013705140.1; NC_015388.1.
DR   STRING; 880072.Desac_0130; -.
DR   MEROPS; M18.004; -.
DR   EnsemblBacteria; AEB08027; AEB08027; Desac_0130.
DR   KEGG; dao:Desac_0130; -.
DR   eggNOG; ENOG4105DFM; Bacteria.
DR   eggNOG; COG1362; LUCA.
DR   OMA; CFDHEEI; -.
DR   OrthoDB; POG091H01QL; -.
DR   BioCyc; DACE880072:GHK9-131-MONOMER; -.
DR   Proteomes; UP000000483; 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   InterPro; IPR023367; Peptidase_M42_dom2.
DR   Pfam; PF02127; Peptidase_M18; 1.
DR   PRINTS; PR00932; AMINO1PTASE.
DR   SUPFAM; SSF101821; SSF101821; 1.
PE   3: Inferred from homology;
KW   Aminopeptidase {ECO:0000256|RuleBase:RU004386,
KW   ECO:0000313|EMBL:AEB08027.1};
KW   Complete proteome {ECO:0000313|Proteomes:UP000000483};
KW   Hydrolase {ECO:0000256|RuleBase:RU004386,
KW   ECO:0000313|EMBL:AEB08027.1};
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:UP000000483};
KW   Zinc {ECO:0000256|RuleBase:RU004386}.
SQ   SEQUENCE   471 AA;  52003 MW;  2D247BF5F4E6BD5F CRC64;
     MEIPDKDTLK QIQDRLSLTP RLVWDHVDEV ERQALMAYAE VYKGFLNQAK TEREAVLEVQ
     RQVQERGFIE LASGQAGSKF FLNYRGKTIA LAVLGERPVS QGLRIVAAHI DSPRLDLKQN
     PLYEETDLVY LKTHYYGGVK KYQWLARPLA LHGVILKENG ESVTLRLGED PDDPVFTVCD
     LLPHLARKVQ MDKKVDEAFI GEKLNLLVGS LPLGDKEIKE RTKLHLLHLL SQRYGLTEED
     LFSAELEVVP AGPARDIGWD RSLLGGYGQD DRACAFAAVA AALDLTAPSH ACLVLLVDKE
     EIGSAGNTSA QSILLEEIVA QLLARQGEST ALRRQALMQS QAISADVAAA FDPDWPEVYE
     KRNAARLGYG VCLTKYTGHG GKYQANDAHA EYLNRLRGIF RESGVIWQTG ELGKIDEGGG
     GTIAKFLAAY GMDIVDLGPA LLSMHSPFEV ASKADLYMTY KAIRSFFSCA A
//
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