ID PTH_BAUCH Reviewed; 193 AA. AC Q1LTH1; DT 12-DEC-2006, integrated into UniProtKB/Swiss-Prot. DT 30-MAY-2006, sequence version 1. DT 16-JUN-2009, entry version 20. DE RecName: Full=Peptidyl-tRNA hydrolase; DE Short=PTH; DE EC=3.1.1.29; GN Name=pth; OrderedLocusNames=BCI_0294; OS Baumannia cicadellinicola subsp. Homalodisca coagulata. OC Bacteria; Proteobacteria; Gammaproteobacteria; Candidatus Baumannia. OX NCBI_TaxID=374463; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=16729848; DOI=10.1371/journal.pbio.0040188; RA Wu D., Daugherty S.C., Van Aken S.E., Pai G.H., Watkins K.L., RA Khouri H., Tallon L.J., Zaborsky J.M., Dunbar H.E., Tran P.L., RA Moran N.A., Eisen J.A.; RT "Metabolic complementarity and genomics of the dual bacterial RT symbiosis of sharpshooters."; RL PLoS Biol. 4:1079-1092(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. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP000238; ABF13958.1; -; Genomic_DNA. DR RefSeq; YP_588743.1; -. DR GeneID; 4056704; -. DR GenomeReviews; CP000238_GR; BCI_0294. DR KEGG; bci:BCI_0294; -. DR HOGENOM; Q1LTH1; -. DR OMA; Q1LTH1; TEIDINN. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0004045; F:aminoacyl-tRNA hydrolase activity; IEA:HAMAP. DR GO; GO:0006412; P:translation; IEA:HAMAP. DR HAMAP; MF_00083; -; 1. DR InterPro; IPR001328; Pept_tRNA_hydro. DR InterPro; IPR018171; Pept_tRNA_hydro_CS. DR Gene3D; G3DSA:3.40.50.1470; Pept_tRNA_hydro; 1. DR PANTHER; PTHR17224; Pept_tRNA_hydro; 1. DR Pfam; PF01195; Pept_tRNA_hydro; 1. DR ProDom; PD005324; PeptRNAhydrolase; 1. DR TIGRFAMs; TIGR00447; pth; 1. DR PROSITE; PS01195; PEPT_TRNA_HYDROL_1; 1. DR PROSITE; PS01196; PEPT_TRNA_HYDROL_2; 1. PE 3: Inferred from homology; KW Complete proteome; Cytoplasm; Hydrolase. FT CHAIN 1 193 Peptidyl-tRNA hydrolase. FT /FTId=PRO_0000264007. SQ SEQUENCE 193 AA; 21892 MW; CCCF7A13DDE15397 CRC64; MTIKLIVGLA NPGNKYLLTR HNVGSWYVNQ LANNYHVSLI NKSSFLGYTG YLNIGKRRIF LLIPTIFMNY NGQAVAAIAK FYNIMPEEIL IAHDELNFLP GYARFKYSGG HGGHNGLKDV IYRLGDNNNF YRLRIGIGHP GDKNKVIKFV LDTPLDTEQQ LIQHAINESV LCTSLMFQQN IAYAIHQLHT ILK //