ID PTH_ALHEH Reviewed; 197 AA. AC Q0ABZ7; DT 12-DEC-2006, integrated into UniProtKB/Swiss-Prot. DT 17-OCT-2006, sequence version 1. DT 16-JUN-2009, entry version 17. DE RecName: Full=Peptidyl-tRNA hydrolase; DE Short=PTH; DE EC=3.1.1.29; GN Name=pth; OrderedLocusNames=Mlg_0285; OS Alkalilimnicola ehrlichei (strain MLHE-1). OC Bacteria; Proteobacteria; Gammaproteobacteria; Chromatiales; OC Ectothiorhodospiraceae; Alkalilimnicola. OX NCBI_TaxID=187272; 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., Dalin E., Tice H., RA Pitluck S., Sims D., Brettin T., Bruce D., Han C., Tapia R., Gilna P., RA Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N., RA Mikhailova N., Oremland R.S., Hoeft S.E., Switzer-Blum J., Kulp T., RA King G., Tabita R., Witte B., Santini J.M., Basu P., Hollibaugh J.T., RA Xie G., Stolz J.F., Richardson P.; RT "Complete sequence of Alkalilimnicola ehrilichei MLHE-1."; 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; CP000453; ABI55640.1; -; Genomic_DNA. DR RefSeq; YP_741130.1; -. DR GeneID; 4269315; -. DR GenomeReviews; CP000453_GR; Mlg_0285. DR KEGG; aeh:Mlg_0285; -. DR NMPDR; fig|187272.6.peg.269; -. DR HOGENOM; Q0ABZ7; -. DR OMA; Q0ABZ7; 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 1 197 Peptidyl-tRNA hydrolase. FT /FTId=PRO_0000264001. SQ SEQUENCE 197 AA; 21844 MW; A6A83CC1A5CCFCAD CRC64; MTDSPQPIQL IVGLGNPGDR YAGTRHNAGF WLLDELLRRH GGALRPERRY HADLATLHLG PHQCRLMRPQ TYMNRSGQAV GPYAQFFRLP PESILVVHDE IDLPPGQVKL KQGGGHGGHN GLRDIIRALG NERGFCRARI GVGHPGHRDG VVPYVLSRPA PDERRAIADA VEELADCVEW LLAGDWGRAC QRLHSRS //