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Database: UniProt
Entry: Q21II8_SACD2
LinkDB: Q21II8_SACD2
Original site: Q21II8_SACD2 
ID   Q21II8_SACD2            Unreviewed;       432 AA.
AC   Q21II8;
DT   18-APR-2006, integrated into UniProtKB/TrEMBL.
DT   18-APR-2006, sequence version 1.
DT   07-JUN-2017, entry version 71.
DE   RecName: Full=M18 family aminopeptidase {ECO:0000256|RuleBase:RU004387};
DE            EC=3.4.11.- {ECO:0000256|RuleBase:RU004387};
GN   OrderedLocusNames=Sde_2231 {ECO:0000313|EMBL:ABD81491.1};
OS   Saccharophagus degradans (strain 2-40 / ATCC 43961 / DSM 17024).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Cellvibrionales;
OC   Cellvibrionaceae; Saccharophagus.
OX   NCBI_TaxID=203122 {ECO:0000313|EMBL:ABD81491.1, ECO:0000313|Proteomes:UP000001947};
RN   [1] {ECO:0000313|EMBL:ABD81491.1, ECO:0000313|Proteomes:UP000001947}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=2-40 / ATCC 43961 / DSM 17024
RC   {ECO:0000313|Proteomes:UP000001947};
RX   PubMed=18516288; DOI=10.1371/journal.pgen.1000087;
RA   Weiner R.M., Taylor L.E.II., Henrissat B., Hauser L., Land M.,
RA   Coutinho P.M., Rancurel C., Saunders E.H., Longmire A.G., Zhang H.,
RA   Bayer E.A., Gilbert H.J., Larimer F., Zhulin I.B., Ekborg N.A.,
RA   Lamed R., Richardson P.M., Borovok I., Hutcheson S.;
RT   "Complete genome sequence of the complex carbohydrate-degrading marine
RT   bacterium, Saccharophagus degradans strain 2-40 T.";
RL   PLoS Genet. 4:E1000087-E1000087(2008).
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; CP000282; ABD81491.1; -; Genomic_DNA.
DR   RefSeq; WP_011468709.1; NC_007912.1.
DR   ProteinModelPortal; Q21II8; -.
DR   STRING; 203122.Sde_2231; -.
DR   MEROPS; M18.002; -.
DR   EnsemblBacteria; ABD81491; ABD81491; Sde_2231.
DR   KEGG; sde:Sde_2231; -.
DR   eggNOG; ENOG4105DFM; Bacteria.
DR   eggNOG; COG1362; LUCA.
DR   HOGENOM; HOG000253244; -.
DR   KO; K01267; -.
DR   OMA; CFDHEEI; -.
DR   OrthoDB; POG091H01I4; -.
DR   Proteomes; UP000001947; 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:ABD81491.1};
KW   Complete proteome {ECO:0000313|Proteomes:UP000001947};
KW   Hydrolase {ECO:0000256|RuleBase:RU004386,
KW   ECO:0000313|EMBL:ABD81491.1};
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:UP000001947};
KW   Zinc {ECO:0000256|RuleBase:RU004386}.
SQ   SEQUENCE   432 AA;  47131 MW;  D0FE83CD16330346 CRC64;
     MTGNTFNNQD LIQFLQDSPT PFHAVLSMSQ RMQAAGFVEL NENEDWSLQP GGKYFVVRSG
     TAIAAFIHGV ESSVDHGIRV VGAHTDSPCL KVKPMPSKLS NGYQQLSIEV YGGVLLAPWF
     DRDLSLAGRV VYRDTSGALK SALINFKRAI GSVPSLAIHL DRAANEGRKI NPHVEMDVVL
     GQSAQKLDFK LLLQEQMQLE GYDNIAEILD FNLSFYDVQP PAVLGLNNEF LASARLDNLL
     SCYIGINSLI QADTTYTSVV ICNDHEEVGS RSEVGAQGPM LKDVLSRINP DPQANQKAIR
     RSLMLSVDNA HGIHPNYASK HDENHGPIIN AGPVIKFDAC QGYATNSDSA AFVRWLATKG
     EPIALQSFVM RADMRCGSTI GPITATELGI QTVDIGLATF GMHSVRELGG VKDGEQLNNL
     LMRFMSTETL KL
//
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