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Database: UniProt
Entry: Q04C43
LinkDB: Q04C43
Original site: Q04C43 
ID   PTH_LACDB               Reviewed;         185 AA.
AC   Q04C43;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   14-NOV-2006, sequence version 1.
DT   19-FEB-2014, entry version 48.
DE   RecName: Full=Peptidyl-tRNA hydrolase;
DE            Short=PTH;
DE            EC=3.1.1.29;
GN   Name=pth; OrderedLocusNames=LBUL_0317;
OS   Lactobacillus delbrueckii subsp. bulgaricus (strain ATCC BAA-365).
OC   Bacteria; Firmicutes; Bacilli; Lactobacillales; Lactobacillaceae;
OC   Lactobacillus.
OX   NCBI_TaxID=321956;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-365;
RX   PubMed=17030793; DOI=10.1073/pnas.0607117103;
RA   Makarova K.S., Slesarev A., Wolf Y.I., Sorokin A., Mirkin B.,
RA   Koonin E.V., Pavlov A., Pavlova N., Karamychev V., Polouchine N.,
RA   Shakhova V., Grigoriev I., Lou Y., Rohksar D., Lucas S., Huang K.,
RA   Goodstein D.M., Hawkins T., Plengvidhya V., Welker D., Hughes J.,
RA   Goh Y., Benson A., Baldwin K., Lee J.-H., Diaz-Muniz I., Dosti B.,
RA   Smeianov V., Wechter W., Barabote R., Lorca G., Altermann E.,
RA   Barrangou R., Ganesan B., Xie Y., Rawsthorne H., Tamir D., Parker C.,
RA   Breidt F., Broadbent J.R., Hutkins R., O'Sullivan D., Steele J.,
RA   Unlu G., Saier M.H. Jr., Klaenhammer T., Richardson P., Kozyavkin S.,
RA   Weimer B.C., Mills D.A.;
RT   "Comparative genomics of the lactic acid bacteria.";
RL   Proc. Natl. Acad. Sci. U.S.A. 103:15611-15616(2006).
CC   -!- FUNCTION: The natural substrate for this enzyme may be peptidyl-
CC       tRNAs which drop off the ribosome during protein synthesis (By
CC       similarity).
CC   -!- CATALYTIC ACTIVITY: N-substituted aminoacyl-tRNA + H(2)O = N-
CC       substituted amino acid + tRNA.
CC   -!- SUBUNIT: Monomer (By similarity).
CC   -!- SUBCELLULAR LOCATION: Cytoplasm (By similarity).
CC   -!- SIMILARITY: Belongs to the PTH family.
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DR   EMBL; CP000412; ABJ57979.1; -; Genomic_DNA.
DR   RefSeq; YP_812417.1; NC_008529.1.
DR   ProteinModelPortal; Q04C43; -.
DR   STRING; 321956.LBUL_0317; -.
DR   EnsemblBacteria; ABJ57979; ABJ57979; LBUL_0317.
DR   GeneID; 4436258; -.
DR   KEGG; lbu:LBUL_0317; -.
DR   PATRIC; 22220457; VBILacDel70259_0317.
DR   eggNOG; COG0193; -.
DR   HOGENOM; HOG000004797; -.
DR   KO; K01056; -.
DR   OMA; SEFINDF; -.
DR   OrthoDB; EOG6C5RTR; -.
DR   ProtClustDB; PRK05426; -.
DR   BioCyc; LDEL321956:GI15-315-MONOMER; -.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0004045; F:aminoacyl-tRNA hydrolase activity; IEA:UniProtKB-EC.
DR   GO; GO:0008152; P:metabolic process; IEA:GOC.
DR   Gene3D; 3.40.50.1470; -; 1.
DR   HAMAP; MF_00083; Pept_tRNA_hydro_bact; 1.
DR   InterPro; IPR001328; Pept_tRNA_hydro.
DR   InterPro; IPR018171; Pept_tRNA_hydro_CS.
DR   PANTHER; PTHR17224; PTHR17224; 1.
DR   Pfam; PF01195; Pept_tRNA_hydro; 1.
DR   SUPFAM; SSF53178; SSF53178; 1.
DR   TIGRFAMs; TIGR00447; pth; 1.
DR   PROSITE; PS01195; PEPT_TRNA_HYDROL_1; 1.
PE   3: Inferred from homology;
KW   Complete proteome; Cytoplasm; Hydrolase.
FT   CHAIN         1    185       Peptidyl-tRNA hydrolase.
FT                                /FTId=PRO_1000010600.
SQ   SEQUENCE   185 AA;  20761 MW;  1C1C91AF60939DFC CRC64;
     MKLIVALGNP GLKYEKTKHN TGFMALDHYL DEKGLRLDRD KFTALYAKEK VAGEDVIFME
     PQTYMNESGR AVGAAAKFFK IDPSDILVIH DDMDMPIAKL RIRAGGKSGG HNGIKSIIAC
     LGTEKFNRLK IGIRHPDKQS VVSWVLTPFN PDQQKELEAS FAKVDQIIDD FIAGKDAQYL
     MNRYN
//
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