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Database: UniProt
Entry: Q2SCH7_HAHCH
LinkDB: Q2SCH7_HAHCH
Original site: Q2SCH7_HAHCH 
ID   Q2SCH7_HAHCH            Unreviewed;       434 AA.
AC   Q2SCH7;
DT   24-JAN-2006, integrated into UniProtKB/TrEMBL.
DT   24-JAN-2006, sequence version 1.
DT   07-JUN-2017, entry version 78.
DE   RecName: Full=M18 family aminopeptidase {ECO:0000256|RuleBase:RU004387};
DE            EC=3.4.11.- {ECO:0000256|RuleBase:RU004387};
GN   OrderedLocusNames=HCH_04958 {ECO:0000313|EMBL:ABC31647.1};
OS   Hahella chejuensis (strain KCTC 2396).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Oceanospirillales;
OC   Hahellaceae; Hahella.
OX   NCBI_TaxID=349521 {ECO:0000313|EMBL:ABC31647.1, ECO:0000313|Proteomes:UP000000238};
RN   [1] {ECO:0000313|EMBL:ABC31647.1, ECO:0000313|Proteomes:UP000000238}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=KCTC 2396 {ECO:0000313|EMBL:ABC31647.1,
RC   ECO:0000313|Proteomes:UP000000238};
RX   PubMed=16352867; DOI=10.1093/nar/gki1016;
RA   Jeong H., Yim J.H., Lee C., Choi S.-H., Park Y.K., Yoon S.H.,
RA   Hur C.-G., Kang H.-Y., Kim D., Lee H.H., Park K.H., Park S.-H.,
RA   Park H.-S., Lee H.K., Oh T.K., Kim J.F.;
RT   "Genomic blueprint of Hahella chejuensis, a marine microbe producing
RT   an algicidal agent.";
RL   Nucleic Acids Res. 33:7066-7073(2005).
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; CP000155; ABC31647.1; -; Genomic_DNA.
DR   RefSeq; WP_011398712.1; NC_007645.1.
DR   ProteinModelPortal; Q2SCH7; -.
DR   STRING; 349521.HCH_04958; -.
DR   MEROPS; M18.002; -.
DR   EnsemblBacteria; ABC31647; ABC31647; HCH_04958.
DR   KEGG; hch:HCH_04958; -.
DR   eggNOG; ENOG4105DFM; Bacteria.
DR   eggNOG; COG1362; LUCA.
DR   HOGENOM; HOG000253244; -.
DR   KO; K01267; -.
DR   OMA; CFDHEEI; -.
DR   OrthoDB; POG091H01I4; -.
DR   Proteomes; UP000000238; 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:ABC31647.1};
KW   Complete proteome {ECO:0000313|Proteomes:UP000000238};
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:UP000000238};
KW   Zinc {ECO:0000256|RuleBase:RU004386}.
SQ   SEQUENCE   434 AA;  48181 MW;  081FAD705CA1C053 CRC64;
     MNKEEFNEGL LAFLDASPTP FHAVANMVEM LEKAGFKRLH EEYEWSLQAN ERYFITRNGS
     SLIAFGGAQG PLEVSGARMF GAHTDSPCLK IKPNPELLRK GYYQLGVEVY GGVLLNPWFD
     RELSLAGRVT YLSGAGEVKS TLINWERPIA MIPSLAIHLD REVNNSRSIN PQKDLPAVLM
     QCRADSPPEF RGLLLEQVKQ EHPELDAERV LDYELCLYDT QPANIHGLQK EFLSSARLDN
     LLSCYIGLQA LLDAGSSQPC FLVFNDHEEV GSVSAEGAQG PFLRSVLLRI AEDEARLSQM
     ISRSMMFSAD NAHGVHPNYA DRHDENHGPL LNSGPVIKVN SNQRYATNSI TSSFYRRLSE
     ELKLPYQVFV VRTDMACGST IGPLTAAELG VKTLDIGVPQ FAMHSIRETC GSADPLTLYE
     VSKLFFNTVT LPQA
//
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