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Database: UniProt
Entry: K4KEL2_SIMAS
LinkDB: K4KEL2_SIMAS
Original site: K4KEL2_SIMAS 
ID   K4KEL2_SIMAS            Unreviewed;       428 AA.
AC   K4KEL2;
DT   09-JAN-2013, integrated into UniProtKB/TrEMBL.
DT   09-JAN-2013, sequence version 1.
DT   07-JUN-2017, entry version 30.
DE   RecName: Full=M18 family aminopeptidase {ECO:0000256|RuleBase:RU004387};
DE            EC=3.4.11.- {ECO:0000256|RuleBase:RU004387};
GN   OrderedLocusNames=M5M_01325 {ECO:0000313|EMBL:AFU97494.1};
OS   Simiduia agarivorans (strain DSM 21679 / JCM 13881 / BCRC 17597 /
OS   SA1).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Cellvibrionales;
OC   Cellvibrionaceae; Simiduia.
OX   NCBI_TaxID=1117647 {ECO:0000313|EMBL:AFU97494.1, ECO:0000313|Proteomes:UP000000466};
RN   [1] {ECO:0000313|EMBL:AFU97494.1, ECO:0000313|Proteomes:UP000000466}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 21679 / JCM 13881 / BCRC 17597 / SA1
RC   {ECO:0000313|Proteomes:UP000000466};
RX   PubMed=23405302; DOI=10.1128/genomeA.00039-12;
RA   Lin S.Y., Shieh W.Y., Chen J.S., Tang S.L.;
RT   "Complete genome sequence of Simiduia agarivorans SA1(T), a marine
RT   bacterium able to degrade a variety of polysaccharides.";
RL   Genome Announc. 1:E00039-E00039(2013).
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; CP003746; AFU97494.1; -; Genomic_DNA.
DR   RefSeq; WP_015045667.1; NZ_ATUQ01000005.1.
DR   MEROPS; M18.002; -.
DR   EnsemblBacteria; AFU97494; AFU97494; M5M_01325.
DR   KEGG; saga:M5M_01325; -.
DR   KO; K01267; -.
DR   OMA; CFDHEEI; -.
DR   OrthoDB; POG091H01I4; -.
DR   BioCyc; SAGA1117647:GLK7-269-MONOMER; -.
DR   Proteomes; UP000000466; 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:AFU97494.1};
KW   Complete proteome {ECO:0000313|Proteomes:UP000000466};
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:UP000000466};
KW   Zinc {ECO:0000256|RuleBase:RU004386}.
SQ   SEQUENCE   428 AA;  46341 MW;  2C2980618496427B CRC64;
     MDQTTLLNGL ADFIASSPTP FHAVDTMARR LRAEGYQALA EGERWQLQAG GRYYVVRNGA
     SLIAFKYGKD LDKGIQMVGA HTDSPCLKVK PNPVVNSQGY LQLGVEVYGG VLLAPWFDRD
     LSLAGRVSYL TKKGERAKAL VNFSRAIAFI PSLAIHLDRE VNKNRTINPQ TDIPPVLAQL
     PGPDAGADFG QILADQLAAE GVTDVASVLD YELCFYDTQR PAVLGLNNEF FVGARLDNLA
     SCYAGLEALL AAPEGQSQLL ICNDHEEVGS SSCCGAAGPM LRQFLERLVP DVERRNQIIH
     HSLLVSADNA HGIHPNYADK HEQNHGPLLN KGPVIKINAN QRYATTGETS AYFRHLCQQL
     NVPVQAFVVR TDMACGSTIG PITSAEIGVS TIDVGLPTWG MHSIRETAGT ADLGYLIAIL
     QKHFAEPA
//
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