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Database: UniProt
Entry: Q6AL63_DESPS
LinkDB: Q6AL63_DESPS
Original site: Q6AL63_DESPS 
ID   Q6AL63_DESPS            Unreviewed;       437 AA.
AC   Q6AL63;
DT   13-SEP-2004, integrated into UniProtKB/TrEMBL.
DT   13-SEP-2004, 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=DP2183 {ECO:0000313|EMBL:CAG36912.1};
OS   Desulfotalea psychrophila (strain LSv54 / DSM 12343).
OC   Bacteria; Proteobacteria; Deltaproteobacteria; Desulfobacterales;
OC   Desulfobulbaceae; Desulfotalea.
OX   NCBI_TaxID=177439 {ECO:0000313|EMBL:CAG36912.1, ECO:0000313|Proteomes:UP000000602};
RN   [1] {ECO:0000313|Proteomes:UP000000602}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=LSv54 / DSM 12343 {ECO:0000313|Proteomes:UP000000602};
RX   PubMed=15305914; DOI=10.1111/j.1462-2920.2004.00665.x;
RA   Rabus R., Ruepp A., Frickey T., Rattei T., Fartmann B., Stark M.,
RA   Bauer M., Zibat A., Lombardot T., Becker I., Amann J., Gellner K.,
RA   Teeling H., Leuschner W.D., Gloeckner F.-O., Lupas A.N., Amann R.,
RA   Klenk H.-P.;
RT   "The genome of Desulfotalea psychrophila, a sulfate-reducing bacterium
RT   from permanently cold Arctic sediments.";
RL   Environ. Microbiol. 6:887-902(2004).
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; CR522870; CAG36912.1; -; Genomic_DNA.
DR   RefSeq; WP_011189424.1; NC_006138.1.
DR   ProteinModelPortal; Q6AL63; -.
DR   STRING; 177439.DP2183; -.
DR   MEROPS; M18.002; -.
DR   EnsemblBacteria; CAG36912; CAG36912; DP2183.
DR   KEGG; dps:DP2183; -.
DR   eggNOG; ENOG4105DFM; Bacteria.
DR   eggNOG; COG1362; LUCA.
DR   HOGENOM; HOG000253244; -.
DR   KO; K01267; -.
DR   OMA; CFDHEEI; -.
DR   OrthoDB; POG091H01I4; -.
DR   BioCyc; DPSY177439:GJW5-2246-MONOMER; -.
DR   Proteomes; UP000000602; 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:CAG36912.1};
KW   Complete proteome {ECO:0000313|Proteomes:UP000000602};
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:UP000000602};
KW   Zinc {ECO:0000256|RuleBase:RU004386}.
SQ   SEQUENCE   437 AA;  48720 MW;  1A50EEB91DC3E1BE CRC64;
     MNDFRQHAQN LIDFISSSPT AFHATATIRQ MLQANGFCQL FEGESWDLQQ GTGYFVVRDQ
     GALIAFTLGQ EERLEDGFRM LGAHTDSPSL QLKPHPLHHK KSYCKLAVEL YGGALLATWF
     DRDLSIAGRV LVRSGEGEYQ KILLDFARPL LCIPSLAIHL DREANKNRSI NSQKELEPLL
     SQKINAGLPD FNTILKKQIE REYPAISVEE ILSFDLFCYD QQKPSLLGLE EEFMVTSRLD
     NQLSCHAGAR AIIDAGFAKN TMLLCFNHEE NGSVSTSGGD SSFVNTVIER IIAEPEKRHI
     ALARSFLISM DNAHATHPNY PEKSEENHNI DLNYGPVIKI NANQRYATSA ISAGIYKAIA
     REAGVPCQEF VMKSDMPCGS TIGPMISARL GVRTIDVGAA SFAMHSIREM TGVKDPYLLY
     RVAAHFLQSD IHHKIHE
//
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