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Database: UniProt
Entry: Q30WU1_DESAG
LinkDB: Q30WU1_DESAG
Original site: Q30WU1_DESAG 
ID   Q30WU1_DESAG            Unreviewed;       464 AA.
AC   Q30WU1;
DT   06-DEC-2005, integrated into UniProtKB/TrEMBL.
DT   06-DEC-2005, sequence version 1.
DT   22-NOV-2017, entry version 79.
DE   RecName: Full=M18 family aminopeptidase {ECO:0000256|RuleBase:RU004387};
DE            EC=3.4.11.- {ECO:0000256|RuleBase:RU004387};
GN   OrderedLocusNames=Dde_3061 {ECO:0000313|EMBL:ABB39855.1};
OS   Desulfovibrio alaskensis (strain G20) (Desulfovibrio desulfuricans
OS   (strain G20)).
OC   Bacteria; Proteobacteria; Deltaproteobacteria; Desulfovibrionales;
OC   Desulfovibrionaceae; Desulfovibrio.
OX   NCBI_TaxID=207559 {ECO:0000313|EMBL:ABB39855.1, ECO:0000313|Proteomes:UP000002710};
RN   [1] {ECO:0000313|EMBL:ABB39855.1, ECO:0000313|Proteomes:UP000002710}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=G20 {ECO:0000313|EMBL:ABB39855.1,
RC   ECO:0000313|Proteomes:UP000002710};
RX   PubMed=21685289; DOI=10.1128/JB.05400-11;
RA   Hauser L.J., Land M.L., Brown S.D., Larimer F., Keller K.L.,
RA   Rapp-Giles B.J., Price M.N., Lin M., Bruce D.C., Detter J.C.,
RA   Tapia R., Han C.S., Goodwin L.A., Cheng J.F., Pitluck S., Copeland A.,
RA   Lucas S., Nolan M., Lapidus A.L., Palumbo A.V., Wall J.D.;
RT   "Complete genome sequence and updated annotation of Desulfovibrio
RT   alaskensis G20.";
RL   J. Bacteriol. 193:4268-4269(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; CP000112; ABB39855.1; -; Genomic_DNA.
DR   RefSeq; WP_011368821.1; NC_007519.1.
DR   ProteinModelPortal; Q30WU1; -.
DR   STRING; 207559.Dde_3061; -.
DR   MEROPS; M18.004; -.
DR   EnsemblBacteria; ABB39855; ABB39855; Dde_3061.
DR   KEGG; dde:Dde_3061; -.
DR   eggNOG; ENOG4105DFM; Bacteria.
DR   eggNOG; COG1362; LUCA.
DR   HOGENOM; HOG000056589; -.
DR   OMA; CFDHEEI; -.
DR   OrthoDB; POG091H01QL; -.
DR   BioCyc; DALA207559:GH1L-2715-MONOMER; -.
DR   Proteomes; UP000002710; 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:ABB39855.1};
KW   Complete proteome {ECO:0000313|Proteomes:UP000002710};
KW   Hydrolase {ECO:0000256|RuleBase:RU004386,
KW   ECO:0000313|EMBL:ABB39855.1};
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:UP000002710};
KW   Zinc {ECO:0000256|RuleBase:RU004386}.
SQ   SEQUENCE   464 AA;  51407 MW;  041C59F1AFEC1206 CRC64;
     MNAKLEHTPK SCWEIYGTEE HAQPMDELAE RYIDFISRCK TERETMEYVV ERLRSAGYTQ
     NFAHDRVYRV FKDKTIFIAA KGRNSISQGL RLIGAHADTP RIDLKQHPLY EACGVGQAKT
     HYYGGIRKYQ WLSRPLALHG VVVKEDGTVV QVNVGDDAGD PVFAISDLLP HLAQKQSGQT
     LSEAFEAEKM NIILAHRPVE NAADSKDADT QQPPKEKIKA RILEILHAKY GIVEEDLYSA
     ELQAVPAGPA RYVGLDSALI GGYGQDDRIC VFAALEALLQ DGTPEYTRCV LFWDKEEIGS
     EGSTGAKSRF FEYCIADLIA AWQPAARFSD VMLNTRAISA DVHGAMDPDW QDLHEKLNAA
     IIGYGPCFCK FTGHRGKYEA NDAHPEYVGW LRGVLNEQGI PWQMAELGRV DLGGGGTVAM
     YLAAYGMDII DFGPAILGMH SPFELASKAD LYATVKAYGA FLMC
//
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