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Database: UniProt
Entry: B0K8C5_THEP3
LinkDB: B0K8C5_THEP3
Original site: B0K8C5_THEP3 
ID   B0K8C5_THEP3            Unreviewed;       467 AA.
AC   B0K8C5;
DT   18-MAR-2008, integrated into UniProtKB/TrEMBL.
DT   18-MAR-2008, sequence version 1.
DT   28-MAR-2018, entry version 64.
DE   RecName: Full=M18 family aminopeptidase {ECO:0000256|RuleBase:RU004387};
DE            EC=3.4.11.- {ECO:0000256|RuleBase:RU004387};
GN   OrderedLocusNames=Teth39_0781 {ECO:0000313|EMBL:ABY94438.1};
OS   Thermoanaerobacter pseudethanolicus (strain ATCC 33223 / 39E)
OS   (Clostridium thermohydrosulfuricum).
OC   Bacteria; Firmicutes; Clostridia; Thermoanaerobacterales;
OC   Thermoanaerobacteraceae; Thermoanaerobacter.
OX   NCBI_TaxID=340099 {ECO:0000313|EMBL:ABY94438.1, ECO:0000313|Proteomes:UP000002156};
RN   [1] {ECO:0000313|Proteomes:UP000002156}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 33223 / 39E {ECO:0000313|Proteomes:UP000002156};
RA   Copeland A., Lucas S., Lapidus A., Barry K., Glavina del Rio T.,
RA   Dalin E., Tice H., Pitluck S., Bruce D., Goodwin L., Saunders E.,
RA   Brettin T., Detter J.C., Han C., Schmutz J., Larimer F., Land M.,
RA   Hauser L., Kyrpides N., Lykidis A., Hemme C., Fields M.W., He Z.,
RA   Zhou J., Richardson P.;
RT   "Complete sequence of Thermoanaerobacter pseudethanolicus 39E.";
RL   Submitted (JAN-2008) 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; CP000924; ABY94438.1; -; Genomic_DNA.
DR   RefSeq; WP_012269171.1; NC_010321.1.
DR   ProteinModelPortal; B0K8C5; -.
DR   STRING; 340099.Teth39_0781; -.
DR   MEROPS; M18.004; -.
DR   EnsemblBacteria; ABY94438; ABY94438; Teth39_0781.
DR   KEGG; tpd:Teth39_0781; -.
DR   eggNOG; ENOG4105DFM; Bacteria.
DR   eggNOG; COG1362; LUCA.
DR   HOGENOM; HOG000056589; -.
DR   OMA; CFDHEEI; -.
DR   Proteomes; UP000002156; 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   Gene3D; 2.30.250.10; -; 1.
DR   InterPro; IPR001948; Peptidase_M18.
DR   InterPro; IPR023358; Peptidase_M18_dom2.
DR   PANTHER; PTHR28570; PTHR28570; 1.
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:ABY94438.1}; Coiled coil {ECO:0000256|SAM:Coils};
KW   Complete proteome {ECO:0000313|Proteomes:UP000002156};
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:UP000002156};
KW   Zinc {ECO:0000256|RuleBase:RU004386}.
FT   COILED       43     63       {ECO:0000256|SAM:Coils}.
SQ   SEQUENCE   467 AA;  51806 MW;  BBD2249640416F39 CRC64;
     MEDKDLKEIE KRLGYKNVDA WTKISDEEKE KVYQFAEDYK DFMAQCKTER ETAEKIIEIA
     EKNGFINIEK VTNLKPGSKV YYNNKGKSVV LAVIGKESMQ KGIKAVASHI DSPRIDLKPN
     PMYEDGGLAL FKTHYYGGVK KYQWVTTPLA LHGVIVKANG EKINIVVGED ENDPVLYITD
     LLPHLGKDQM EKKAAEVVTG EALNAVIGSI PLSEEVSVKP NILKYLNEKF GIVEEDFLSA
     ELELVPAYKP RDIGFDRSMI GAYGQDDRVC AYTSLRAILE LEVPERTAVA IFADKEEIGS
     MGNTGFQSRF FENAIAEILE KYEGNTDIKL RRVLANSELL SADVNAAFDP TYPEVSEKQN
     TAYLGKGVCI TKYTGSRGKA GSNDANAEFV GKVRKLFNEN GVVWQTGELG KVDMGGGGTV
     AQFAANYGME VLDCGVALLS MHAPYELSSK VDVYMAYKAY KVFMEKD
//
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