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Database: UniProt
Entry: D5XDR7_THEPJ
LinkDB: D5XDR7_THEPJ
Original site: D5XDR7_THEPJ 
ID   D5XDR7_THEPJ            Unreviewed;       485 AA.
AC   D5XDR7;
DT   13-JUL-2010, integrated into UniProtKB/TrEMBL.
DT   13-JUL-2010, sequence version 1.
DT   07-JUN-2017, entry version 42.
DE   RecName: Full=M18 family aminopeptidase {ECO:0000256|RuleBase:RU004387};
DE            EC=3.4.11.- {ECO:0000256|RuleBase:RU004387};
GN   OrderedLocusNames=TherJR_2984 {ECO:0000313|EMBL:ADG83813.1};
OS   Thermincola potens (strain JR).
OC   Bacteria; Firmicutes; Clostridia; Clostridiales; Peptococcaceae;
OC   Thermincola.
OX   NCBI_TaxID=635013 {ECO:0000313|EMBL:ADG83813.1, ECO:0000313|Proteomes:UP000002377};
RN   [1] {ECO:0000313|EMBL:ADG83813.1, ECO:0000313|Proteomes:UP000002377}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=JR {ECO:0000313|EMBL:ADG83813.1,
RC   ECO:0000313|Proteomes:UP000002377};
RG   US DOE Joint Genome Institute;
RA   Lucas S., Copeland A., Lapidus A., Cheng J.-F., Bruce D., Goodwin L.,
RA   Pitluck S., Chertkov O., Detter J.C., Han C., Tapia R., Land M.,
RA   Hauser L., Kyrpides N., Mikhailova N., Hazen T.C., Woyke T.;
RT   "Complete sequence of Thermincola sp. JR.";
RL   Submitted (MAY-2010) to the EMBL/GenBank/DDBJ databases.
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; CP002028; ADG83813.1; -; Genomic_DNA.
DR   RefSeq; WP_013121801.1; NC_014152.1.
DR   ProteinModelPortal; D5XDR7; -.
DR   STRING; 635013.TherJR_2984; -.
DR   MEROPS; M18.004; -.
DR   EnsemblBacteria; ADG83813; ADG83813; TherJR_2984.
DR   KEGG; tjr:TherJR_2984; -.
DR   eggNOG; ENOG4105DFM; Bacteria.
DR   eggNOG; COG1362; LUCA.
DR   HOGENOM; HOG000056589; -.
DR   OMA; YQWVTIP; -.
DR   OrthoDB; POG091H01QL; -.
DR   BioCyc; TPOT635013:GHIM-2984-MONOMER; -.
DR   Proteomes; UP000002377; 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:ADG83813.1};
KW   Complete proteome {ECO:0000313|Proteomes:UP000002377};
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:UP000002377};
KW   Zinc {ECO:0000256|RuleBase:RU004386}.
SQ   SEQUENCE   485 AA;  54002 MW;  36BE90A5997674ED CRC64;
     MNKKEETKSP GEKLKEELCA ETQLVWDSID KKEKEEVMRF NEDYKTFLSN AKTEKQTVKE
     IIQQARDKGF VSLEEMFKGG KKLKPGNKIF INYKNKSAIL VVVGKEPLWE GLNIVGSHVD
     APRLDLKPQP LYEDQNLALM KTHYYGGIKK YQWPAIPLAL HGVVYTARGT VAELMVGEKA
     EEPVFTISDL LPHLAKEQMG KKMGEAIKGE DLNILVGSIP VEDKEVKERV KLTVLKLLNE
     RYGITEEDFI SAELELVPAG PARDVGLDRS MVGGYGQDDR VCAYASLRAI LDVQSPIYTS
     VAIFVDKEEI GSTGNTGMKS RFFENAVAEM LYLVAGDYNE LYCRRTLAHS RALSADVSAG
     MDPNYPNVLD KYNAARLGYG VVITKYTGSG GKYSTSDANP GFINQVRRIF KENKVIWQTG
     ELGKVDQGGG GTIAQYIARY GMEVLDCGVA LLGMHSPFEV AHKGDIYMGY KAYKAFFEQA
     GNEKY
//
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