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Database: UniProt
Entry: G7QD15_9DELT
LinkDB: G7QD15_9DELT
Original site: G7QD15_9DELT 
ID   G7QD15_9DELT            Unreviewed;       484 AA.
AC   G7QD15;
DT   25-JAN-2012, integrated into UniProtKB/TrEMBL.
DT   25-JAN-2012, sequence version 1.
DT   22-NOV-2017, entry version 28.
DE   RecName: Full=M18 family aminopeptidase {ECO:0000256|RuleBase:RU004387};
DE            EC=3.4.11.- {ECO:0000256|RuleBase:RU004387};
GN   ORFNames=DFW101_0304 {ECO:0000313|EMBL:EHJ46321.1};
OS   Desulfovibrio sp. FW1012B.
OC   Bacteria; Proteobacteria; Deltaproteobacteria; Desulfovibrionales;
OC   Desulfovibrionaceae; Desulfovibrio.
OX   NCBI_TaxID=644968 {ECO:0000313|EMBL:EHJ46321.1, ECO:0000313|Proteomes:UP000004662};
RN   [1] {ECO:0000313|Proteomes:UP000004662}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=FW1012B {ECO:0000313|Proteomes:UP000004662};
RX   PubMed=25767232;
RA   Ramsay B.D., Hwang C., Woo H.L., Carroll S.L., Lucas S., Han J.,
RA   Lapidus A.L., Cheng J.F., Goodwin L.A., Pitluck S., Peters L.,
RA   Chertkov O., Held B., Detter J.C., Han C.S., Tapia R., Land M.L.,
RA   Hauser L.J., Kyrpides N.C., Ivanova N.N., Mikhailova N., Pagani I.,
RA   Woyke T., Arkin A.P., Dehal P., Chivian D., Criddle C.S., Wu W.,
RA   Chakraborty R., Hazen T.C., Fields M.W.;
RT   "High-Quality Draft Genome Sequence of Desulfovibrio carbinoliphilus
RT   FW-101-2B, an Organic Acid-Oxidizing Sulfate-Reducing Bacterium
RT   Isolated from Uranium(VI)-Contaminated Groundwater.";
RL   Genome Announc. 3:0-0(2015).
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; CM001368; EHJ46321.1; -; Genomic_DNA.
DR   RefSeq; WP_009179768.1; NZ_CM001368.1.
DR   ProteinModelPortal; G7QD15; -.
DR   STRING; 644968.DFW101_0304; -.
DR   MEROPS; M18.004; -.
DR   EnsemblBacteria; EHJ46321; EHJ46321; DFW101_0304.
DR   eggNOG; ENOG4105DFM; Bacteria.
DR   eggNOG; COG1362; LUCA.
DR   OrthoDB; POG091H01QL; -.
DR   Proteomes; UP000004662; 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:EHJ46321.1};
KW   Complete proteome {ECO:0000313|Proteomes:UP000004662};
KW   Hydrolase {ECO:0000256|RuleBase:RU004386,
KW   ECO:0000313|EMBL:EHJ46321.1};
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:UP000004662};
KW   Zinc {ECO:0000256|RuleBase:RU004386}.
SQ   SEQUENCE   484 AA;  52687 MW;  E7587FDD5A26F20A CRC64;
     MTESQEKNTP PQAVPSLTIE AKCCFEAYAS AEERQAMRDL ADRYLKFLSA CKTERETVAY
     VREVLSKAGF TECPDGDFTA DAVFRVLKDK TVFVARKGKR PLSDGFRLLG AHCDTPRIDL
     KQHPLYQTCG VAQFKTHYYG GIRKHQWLAR PLALHGVVAK KDGSVVTVTI GEDPADPVFT
     IPDLLPHLAY KQVEQKLSDA FEAEKLNIIV GHCPVETVPP ADGGSQNAAP KDNGNDTIKA
     KVLALLNERY GIDEMDLYSA ELQAVPAGAA RLVGLDGSLV GGYGQDDRVC VFTGLEALLN
     APEPEHAQIV LFWDKEEIGS EGSTGAKSRF FEYSLEDLIE AWDPKARKSR VLAAAKAVSA
     DVHGAMDPDY QDLHEKLNAA ILGFGPCFCK FTGHRGKVGA NDAHPEYVAW LRNLLDTAGV
     PWQMAELGRV DLGGGGTVAK FLAVYGMDII DFGPAVLSMH SPFELTSVAD VYATMLAYKA
     FLSS
//
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