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Database: UniProt
Entry: F0JIB4_DESDE
LinkDB: F0JIB4_DESDE
Original site: F0JIB4_DESDE 
ID   F0JIB4_DESDE            Unreviewed;       461 AA.
AC   F0JIB4;
DT   03-MAY-2011, integrated into UniProtKB/TrEMBL.
DT   03-MAY-2011, sequence version 1.
DT   07-JUN-2017, entry version 38.
DE   RecName: Full=M18 family aminopeptidase {ECO:0000256|RuleBase:RU004387};
DE            EC=3.4.11.- {ECO:0000256|RuleBase:RU004387};
GN   ORFNames=DND132_0951 {ECO:0000313|EMBL:EGB14166.1};
OS   Desulfovibrio desulfuricans ND132.
OC   Bacteria; Proteobacteria; Deltaproteobacteria; Desulfovibrionales;
OC   Desulfovibrionaceae; Desulfovibrio.
OX   NCBI_TaxID=641491 {ECO:0000313|EMBL:EGB14166.1, ECO:0000313|Proteomes:UP000007845};
RN   [1] {ECO:0000313|EMBL:EGB14166.1, ECO:0000313|Proteomes:UP000007845}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ND132 {ECO:0000313|EMBL:EGB14166.1};
RX   PubMed=21357488; DOI=10.1128/JB.00170-11;
RA   Brown S.D., Gilmour C.C., Kucken A.M., Wall J.D., Elias D.A.,
RA   Brandt C.C., Podar M., Chertkov O., Held B., Bruce D.C., Detter J.C.,
RA   Tapia R., Han C.S., Goodwin L.A., Cheng J.F., Pitluck S., Woyke T.,
RA   Mikhailova N., Ivanova N.N., Han J., Lucas S., Lapidus A.L.,
RA   Land M.L., Hauser L.J., Palumbo A.V.;
RT   "Genome sequence of the mercury-methylating strain Desulfovibrio
RT   desulfuricans ND132.";
RL   J. Bacteriol. 193:2078-2079(2011).
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; CP003220; EGB14166.1; -; Genomic_DNA.
DR   RefSeq; WP_014321594.1; NC_016803.1.
DR   STRING; 641491.DND132_0951; -.
DR   MEROPS; M18.004; -.
DR   EnsemblBacteria; EGB14166; EGB14166; DND132_0951.
DR   KEGG; ddn:DND132_0951; -.
DR   eggNOG; ENOG4105DFM; Bacteria.
DR   eggNOG; COG1362; LUCA.
DR   OrthoDB; POG091H01QL; -.
DR   BioCyc; DDES641491:GH21-977-MONOMER; -.
DR   Proteomes; UP000007845; 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:EGB14166.1};
KW   Complete proteome {ECO:0000313|Proteomes:UP000007845};
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:UP000007845};
KW   Zinc {ECO:0000256|RuleBase:RU004386}.
SQ   SEQUENCE   461 AA;  51176 MW;  D95B34506C0ADDA8 CRC64;
     MSKQQLEYEP RSAWEAYASD EHRAAMDAMA IDYVRFLSEC KTERLVMDYV RERIEAAGFV
     EDFAGPQVFR FNRNKTCFLA RKGKRPLSEG YRLVGAHADC PRLDLKQRPL YEDLDICLAK
     THYYGGIRKY QWLTIPLALH GTVVKRSGET VTVCIGESQS DPVFTITDLL PHLAYKEVTK
     KVEEAFEAEK LNLVLGQSPV AAPSGNDEDK VKEPVKRKVL ELLNARYGIE EADFLSAEMQ
     AVPAGPARFV GLDESLIGGY GQDDRSSVFC ALEAFLAEPE PEYCQVVLFW DKEEIGSEGA
     TGAKSYFFEY CMEELVDAWE PGARLSRVLM NGSALSADVS AAMDPDYKDV YEPLNAARLG
     YGPCFNKFTG HRGKVGANDA HPDFIGWLRA IFDGAGVPWH MSELGKVDAG GGGTVAKFLA
     VYGMDVIDVG VPVLSMHSPF ELSAKADIYA CVLAFREFLK R
//
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