ID PTH_BURCM Reviewed; 199 AA. AC Q0BBQ3; DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot. DT 17-OCT-2006, sequence version 1. DT 16-JUN-2009, entry version 19. DE RecName: Full=Peptidyl-tRNA hydrolase; DE Short=PTH; DE EC=3.1.1.29; GN Name=pth; OrderedLocusNames=Bamb_2864; OS Burkholderia ambifaria (strain ATCC BAA-244 / AMMD) (Burkholderia OS cepacia (strain AMMD)). OC Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales; OC Burkholderiaceae; Burkholderia; Burkholderia cepacia complex. OX NCBI_TaxID=339670; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., RA Glavina del Rio T., Hammon N., Israni S., Pitluck S., Bruce D., RA Chain P., Malfatti S., Shin M., Vergez L., Schmutz J., Larimer F., RA Land M., Hauser L., Kyrpides N., Kim E., Parke J., Coenye T., RA Konstantinidis K., Ramette A., Tiedje J., Richardson P.; RT "Complete sequence of chromosome 1 of Burkholderia cepacia AMMD."; RL Submitted (AUG-2006) to the EMBL/GenBank/DDBJ databases. 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; CP000440; ABI88420.1; -; Genomic_DNA. DR RefSeq; YP_774754.1; -. DR GeneID; 4310713; -. DR GenomeReviews; CP000440_GR; Bamb_2864. DR KEGG; bam:Bamb_2864; -. DR NMPDR; fig|339670.3.peg.300; -. DR OMA; Q0BBQ3; KIPLDNI. 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 1 199 Peptidyl-tRNA hydrolase. FT /FTId=PRO_1000010570. SQ SEQUENCE 199 AA; 21951 MW; C75B97BF3C0F22D3 CRC64; MIKLIVGLGN PGAEYTATRH NAGFWLVDQL AREAGATLRD ERRFHGFYAK ARLHGEEVHL LEPQTYMNRS GQSVVALASF FKILPDQILV AHDELDLPPG TVKLKLGGGS GGHNGLKDIS AHLSSQQYWR LRIGIGHPRD LIPEGARAGA KPDVANFVLK PPRREEQDVI DASIERALAV MPMVVKGELD RATMQLHRN //