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Database: UniProt
Entry: J9RXU7_9ACTN
LinkDB: J9RXU7_9ACTN
Original site: J9RXU7_9ACTN 
ID   J9RXU7_9ACTN            Unreviewed;       430 AA.
AC   J9RXU7;
DT   28-NOV-2012, integrated into UniProtKB/TrEMBL.
DT   28-NOV-2012, sequence version 1.
DT   22-NOV-2017, entry version 27.
DE   RecName: Full=M18 family aminopeptidase {ECO:0000256|RuleBase:RU004387};
DE            EC=3.4.11.- {ECO:0000256|RuleBase:RU004387};
GN   ORFNames=KTR9_0762 {ECO:0000313|EMBL:AFR47426.1};
OS   Gordonia sp. KTR9.
OC   Bacteria; Actinobacteria; Corynebacteriales; Gordoniaceae; Gordonia.
OX   NCBI_TaxID=337191 {ECO:0000313|EMBL:AFR47426.1, ECO:0000313|Proteomes:UP000003281};
RN   [1] {ECO:0000313|EMBL:AFR47426.1, ECO:0000313|Proteomes:UP000003281}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=KTR9 {ECO:0000313|EMBL:AFR47426.1,
RC   ECO:0000313|Proteomes:UP000003281};
RX   PubMed=22923396; DOI=10.1128/AEM.02120-12;
RA   Chen H.P., Zhu S.H., Casabon I., Hallam S.J., Crocker F.H., Mohn W.W.,
RA   Indest K.J., Eltis L.D.;
RT   "Genomic and transcriptomic studies of an RDX (hexahydro-1,3,5-
RT   trinitro-1,3,5-triazine)-degrading actinobacterium.";
RL   Appl. Environ. Microbiol. 78:7798-7800(2012).
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; CP002907; AFR47426.1; -; Genomic_DNA.
DR   RefSeq; WP_014925433.1; NC_018581.1.
DR   MEROPS; M18.002; -.
DR   EnsemblBacteria; AFR47426; AFR47426; KTR9_0762.
DR   KEGG; gor:KTR9_0762; -.
DR   PATRIC; fig|337191.3.peg.968; -.
DR   KO; K01267; -.
DR   OrthoDB; POG091H01I4; -.
DR   BioCyc; GSP337191:G136T-770-MONOMER; -.
DR   Proteomes; UP000003281; 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:AFR47426.1};
KW   Complete proteome {ECO:0000313|Proteomes:UP000003281};
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   Zinc {ECO:0000256|RuleBase:RU004386}.
SQ   SEQUENCE   430 AA;  45476 MW;  ADF2EFF2D5064692 CRC64;
     MSASARIPTS ATARGLGEFV DASPSPFHVC ATVARELENA GYTRLFEDQE WPGGDLDAPS
     ARHYVIRGGS IIAWETGPSG AFRIVGGHTD SPNLRLKQHP DRSSAGVAMV ALEPYGGAWL
     NSWLDRDLGL SGRLAYRSGN SVAHTLVHVT EPVVRVPQLA IHLSEDRKGV SLDPQRHVNA
     VWGIGDEVPD VLGWVSEYAG IDPDAVLGWE LMTHDVAPSA IIGADGNLLS APRLDNQGTC
     YTGLRALLDA GSSNHTKMLV LFDHEEVGSG SERGAASDFL GSVCERIVLA RGGSRADFLR
     AMAASVCLSG DMAHATHPNY PERHEPGHRI SIGGGPVLKV NQNLRYASDA VGEAVFALAC
     DAAGVPMQRY VHRADLPCGS TIGPITASRT GLTTIDVGAP QLAMHSAREL MGADDVPMYS
     AALQAFLTQG
//
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