ID PTH1_CORJK Reviewed; 193 AA. AC Q4JU39; DT 12-DEC-2006, integrated into UniProtKB/Swiss-Prot. DT 12-DEC-2006, sequence version 2. DT 16-JUN-2009, entry version 28. DE RecName: Full=Peptidyl-tRNA hydrolase 1; DE Short=PTH 1; DE EC=3.1.1.29; GN Name=pth1; OrderedLocusNames=jk1495; OS Corynebacterium jeikeium (strain K411). OC Bacteria; Actinobacteria; Actinobacteridae; Actinomycetales; OC Corynebacterineae; Corynebacteriaceae; Corynebacterium. OX NCBI_TaxID=306537; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=15968079; DOI=10.1128/JB.187.13.4671-4682.2005; RA Tauch A., Kaiser O., Hain T., Goesmann A., Weisshaar B., RA Albersmeier A., Bekel T., Bischoff N., Brune I., Chakraborty T., RA Kalinowski J., Meyer F., Rupp O., Schneiker S., Viehoever P., RA Puehler A.; RT "Complete genome sequence and analysis of the multiresistant RT nosocomial pathogen Corynebacterium jeikeium K411, a lipid-requiring RT bacterium of the human skin flora."; RL J. Bacteriol. 187:4671-4682(2005). 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; CR931997; CAI37668.1; ALT_INIT; Genomic_DNA. DR RefSeq; YP_251286.1; -. DR GeneID; 3432994; -. DR GenomeReviews; CR931997_GR; jk1495. DR KEGG; cjk:jk1495; -. DR NMPDR; fig|306537.3.peg.748; -. DR HOGENOM; Q4JU39; -. DR BioCyc; CJEI306537:JK1495-MON; -. 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 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; FALSE_NEG. 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 1. FT /FTId=PRO_0000264025. SQ SEQUENCE 193 AA; 20691 MW; 8DC188BFC3D5E8B9 CRC64; MASPNKKQHT NSDTWLIVGL GNPGDKYANT RHNVGRMVIG ELLDRQVPAA SLNTHKKTNT DIAEVKIAGR KVVLAQPRTF MNVSGGPVQQ LAAFFKIPAE NIIVAYDDLE GDPGAVKLRQ SGGDKGHNGL KSITKSLGTK DYWRLSCGIG RPPGRMDPAA YVLKPFPKSE AAEVAIMCAD AADEVERTLG VGN //