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Database: UniProt
Entry: M1E544_9FIRM
LinkDB: M1E544_9FIRM
Original site: M1E544_9FIRM 
ID   M1E544_9FIRM            Unreviewed;       449 AA.
AC   M1E544;
DT   01-MAY-2013, integrated into UniProtKB/TrEMBL.
DT   01-MAY-2013, sequence version 1.
DT   07-JUN-2017, entry version 28.
DE   RecName: Full=M18 family aminopeptidase {ECO:0000256|RuleBase:RU004387};
DE            EC=3.4.11.- {ECO:0000256|RuleBase:RU004387};
GN   ORFNames=Thena_1177 {ECO:0000313|EMBL:AEE14797.1};
OS   Thermodesulfobium narugense DSM 14796.
OC   Bacteria; Firmicutes; Clostridia; Thermoanaerobacterales;
OC   Thermodesulfobiaceae; Thermodesulfobium.
OX   NCBI_TaxID=747365 {ECO:0000313|EMBL:AEE14797.1, ECO:0000313|Proteomes:UP000011765};
RN   [1] {ECO:0000313|EMBL:AEE14797.1, ECO:0000313|Proteomes:UP000011765}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 14796 {ECO:0000313|EMBL:AEE14797.1,
RC   ECO:0000313|Proteomes:UP000011765};
RG   US DOE Joint Genome Institute (JGI-PGF);
RA   Lucas S., Han J., Lapidus A., Bruce D., Goodwin L., Pitluck S.,
RA   Peters L., Kyrpides N., Mavromatis K., Pagani I., Ivanova N.,
RA   Ovchinnikova G., Zhang X., Saunders L., Detter J.C., Tapia R., Han C.,
RA   Land M., Hauser L., Markowitz V., Cheng J.-F., Hugenholtz P.,
RA   Woyke T., Wu D., Spring S., Schroeder M., Brambilla E., Klenk H.-P.,
RA   Eisen J.A.;
RT   "The complete genome of Thermodesulfobium narugense DSM 14796.";
RL   Submitted (APR-2011) 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; CP002690; AEE14797.1; -; Genomic_DNA.
DR   RefSeq; WP_013756518.1; NC_015499.1.
DR   STRING; 747365.Thena_1177; -.
DR   MEROPS; M18.004; -.
DR   EnsemblBacteria; AEE14797; AEE14797; Thena_1177.
DR   KEGG; tnr:Thena_1177; -.
DR   eggNOG; ENOG4105DFM; Bacteria.
DR   eggNOG; COG1362; LUCA.
DR   OrthoDB; POG091H01QL; -.
DR   BioCyc; TNAR747365:GH4R-1190-MONOMER; -.
DR   Proteomes; UP000011765; 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:AEE14797.1};
KW   Complete proteome {ECO:0000313|Proteomes:UP000011765};
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:UP000011765};
KW   Zinc {ECO:0000256|RuleBase:RU004386}.
SQ   SEQUENCE   449 AA;  50878 MW;  086C08D116EC32C9 CRC64;
     MPDLKNILFM KRKNAWFKTD RESIFNFAQG YKNFLKKCKT ERETVKFVNE YFLNNKKDRE
     FIIINRNKSV ALIRLSEGFG MRMIASHIDA PRIDLKQNPL FEDSGLGLFH THYYGGIKKY
     QWLNIPISLH VFLVKSDKEI LEINIGEEPD DPIFVIPDLL PHLSKKVIDE KVTKEAFDAN
     KLNIICGSIP FSEEEKDQIK LNVLNYLYEK YKIVEEDFVS AEIQAVPAFE PRDIGFDKSL
     IGAYGQDDRI CAYASLMAFF DVGISDKTQV LLMVDKEEIG SEGNTSAQSS FVYDIAIEIL
     KRKGIEPTFA NILNFFKSSQ CLSADVSAAV NPMYKDVHEA DNAAYINNGV VITKFTGHGG
     KYYSNDANTE FVAEVREAFN KDGVIWQIAE LGKVDEGGGG TIAKYISKHN IETLDCGPAL
     ISMHSPLEIA SKADLYETYK AYKSFLIMK
//
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