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Database: UniProt
Entry: F3YTQ5_DESAF
LinkDB: F3YTQ5_DESAF
Original site: F3YTQ5_DESAF 
ID   F3YTQ5_DESAF            Unreviewed;       468 AA.
AC   F3YTQ5;
DT   28-JUN-2011, integrated into UniProtKB/TrEMBL.
DT   28-JUN-2011, sequence version 1.
DT   22-NOV-2017, entry version 42.
DE   RecName: Full=M18 family aminopeptidase {ECO:0000256|RuleBase:RU004387};
DE            EC=3.4.11.- {ECO:0000256|RuleBase:RU004387};
GN   ORFNames=Desaf_0073 {ECO:0000313|EMBL:EGJ48436.1};
OS   Desulfovibrio africanus str. Walvis Bay.
OC   Bacteria; Proteobacteria; Deltaproteobacteria; Desulfovibrionales;
OC   Desulfovibrionaceae; Desulfovibrio.
OX   NCBI_TaxID=690850 {ECO:0000313|EMBL:EGJ48436.1, ECO:0000313|Proteomes:UP000007844};
RN   [1] {ECO:0000313|EMBL:EGJ48436.1, ECO:0000313|Proteomes:UP000007844}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Walvis Bay {ECO:0000313|EMBL:EGJ48436.1};
RX   PubMed=21642452; DOI=10.1128/JB.05223-11;
RA   Brown S.D., Wall J.D., Kucken A.M., Gilmour C.C., Podar M.,
RA   Brandt C.C., Teshima H., Detter J.C., Han C.S., Land M.L., Lucas S.,
RA   Han J., Pennacchio L., Nolan M., Pitluck S., Woyke T., Goodwin L.,
RA   Palumbo A.V., Elias D.A.;
RT   "Genome sequence of the mercury-methylating and pleomorphic
RT   Desulfovibrio africanus Strain Walvis Bay.";
RL   J. Bacteriol. 193:4037-4038(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; CP003221; EGJ48436.1; -; Genomic_DNA.
DR   RefSeq; WP_014258312.1; NC_016629.1.
DR   STRING; 690850.Desaf_0073; -.
DR   MEROPS; M18.004; -.
DR   EnsemblBacteria; EGJ48436; EGJ48436; Desaf_0073.
DR   KEGG; daf:Desaf_0073; -.
DR   eggNOG; ENOG4105DFM; Bacteria.
DR   eggNOG; COG1362; LUCA.
DR   OrthoDB; POG091H01QL; -.
DR   BioCyc; DAFR690850:GHYW-73-MONOMER; -.
DR   Proteomes; UP000007844; 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   PANTHER; PTHR28570; PTHR28570; 1.
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:EGJ48436.1};
KW   Complete proteome {ECO:0000313|Proteomes:UP000007844};
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:UP000007844};
KW   Zinc {ECO:0000256|RuleBase:RU004386}.
SQ   SEQUENCE   468 AA;  52301 MW;  00E43318192A3085 CRC64;
     MTKKKNAVPA GLESEPKSCW EIYDTPAHEK AMEKLARSYV DFLSRCKTER ESVEYVVERL
     KQAGFKPDLS EAACYRVKRD KTIFIARKGK RPLSEGFRFL GAHADTPRLD LKQHPLYQEA
     EVGLAKTHYY GGIRKHQWLA RPLALHGVAV KKNGQAVTIV IGEDPNDPVL TIADLLPHLA
     YKQVEQKLSD AFEAEKLNVI FGHSPAENSD EENGNGTGKK RIKRRMLEIL DERYGLVEDD
     LYSAEMHIVP AGPARFVGLD RALIGGYGHD DRVCLFAALE AFLRADQPEY TQVVVFWDKE
     EIGSEGSTGA KSKFFEYCLM DVLEAWEPKT KLHHVMELSK AVSADVHGAL DPDFQELHDK
     LNAALLGYGP CFCKFTGHRG KVGANDAHPE YVAWLRNVLD EAGVPWQMAE LGRVDIGGGG
     TVAKYLAEYG MDIIDFGTPV LSMHSPFEII SKVDLYATTL AYEAFLKK
//
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