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Database: UniProt
Entry: F8C329_THEGP
LinkDB: F8C329_THEGP
Original site: F8C329_THEGP 
ID   F8C329_THEGP            Unreviewed;       463 AA.
AC   F8C329;
DT   21-SEP-2011, integrated into UniProtKB/TrEMBL.
DT   21-SEP-2011, sequence version 1.
DT   22-NOV-2017, entry version 35.
DE   RecName: Full=M18 family aminopeptidase {ECO:0000256|RuleBase:RU004387};
DE            EC=3.4.11.- {ECO:0000256|RuleBase:RU004387};
GN   OrderedLocusNames=TOPB45_1440 {ECO:0000313|EMBL:AEH23520.1};
OS   Thermodesulfobacterium geofontis (strain OPF15).
OC   Bacteria; Thermodesulfobacteria; Thermodesulfobacteriales;
OC   Thermodesulfobacteriaceae; Thermodesulfobacterium.
OX   NCBI_TaxID=795359 {ECO:0000313|EMBL:AEH23520.1, ECO:0000313|Proteomes:UP000006583};
RN   [1] {ECO:0000313|Proteomes:UP000006583}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=OPB45 {ECO:0000313|Proteomes:UP000006583};
RA   Lucas S., Han J., Lapidus A., Cheng J.-F., Goodwin L., Pitluck S.,
RA   Peters L., Mikhailova N., Davenport K., Detter J.C., Han C., Tapia R.,
RA   Land M., Hauser L., Kyrpides N., Ivanova N., Pagani I.,
RA   Hamilton-Brehm S., Elkins J., Woyke T.;
RT   "Complete sequence of Thermodesulfobacterium sp. OPB45.";
RL   Submitted (JUN-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; CP002829; AEH23520.1; -; Genomic_DNA.
DR   RefSeq; WP_013910218.1; NC_015682.1.
DR   STRING; 795359.TOPB45_1440; -.
DR   MEROPS; M18.004; -.
DR   EnsemblBacteria; AEH23520; AEH23520; TOPB45_1440.
DR   KEGG; top:TOPB45_1440; -.
DR   PATRIC; fig|795359.3.peg.1463; -.
DR   eggNOG; ENOG4105DFM; Bacteria.
DR   eggNOG; COG1362; LUCA.
DR   OMA; YQWVTIP; -.
DR   OrthoDB; POG091H01QL; -.
DR   BioCyc; TGEO795359:G12Y3-1448-MONOMER; -.
DR   Proteomes; UP000006583; 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:AEH23520.1};
KW   Complete proteome {ECO:0000313|Proteomes:UP000006583};
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:UP000006583};
KW   Zinc {ECO:0000256|RuleBase:RU004386}.
SQ   SEQUENCE   463 AA;  52430 MW;  968DEAC67CF031B8 CRC64;
     MKIEELEKEL TYKAKHVYEE IDEEEKNLLE KIAKEYIEFL SIVKTERETV EFGKELLEKE
     GFKENDFKKG YFIYKNKFLA CWKLGKKPIT EGLRIIVSHI DTPRLDLKLH PLFEDTDLAF
     LKTHYYGGIK KYHWVAQPLA LHGVVAKKDG RIIKIVIGEN KEDPVFTICD LLPHLAKKIQ
     AEKKLSEAIV GEKLNVLVAG IPVEGKDEKV KEKVKLKFLE LIYKKYGIKE EDFVSAELYI
     VPAGSAREVG LDRSFVGGYG QDDRICAFTS LKAFLEVEDP EYTNLILFMD KEEIGSEGNT
     SAKSRIFEGI IYNLIKNSGL SSTADNFFNI MTKTKAISAD VTAGIDPNYM EVHDKLNDAK
     LGFGIAVSRY TGHGGKYMAN EAHVEFLAWL LKNWDENKVI YQVCSMGKVD EGGGGTVSKY
     FASYGMDIVD AGPPLLSMHS PFEIAHKGDL YMTYKAFKTF LKV
//
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