ID PTH2_BOVIN Reviewed; 179 AA. AC Q3ZBL5; Q05KI4; Q5BIN3; DT 27-JUN-2006, integrated into UniProtKB/Swiss-Prot. DT 27-SEP-2005, sequence version 1. DT 16-JUN-2009, entry version 28. DE RecName: Full=Peptidyl-tRNA hydrolase 2, mitochondrial; DE Short=PTH 2; DE EC=3.1.1.29; DE AltName: Full=Bcl-2 inhibitor of transcription; DE Flags: Precursor; GN Name=PTRH2; Synonyms=BIT1; OS Bos taurus (Bovine). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Laurasiatheria; Cetartiodactyla; Ruminantia; OC Pecora; Bovidae; Bovinae; Bos. OX NCBI_TaxID=9913; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA]. RC TISSUE=Placenta; RA Ushizawa K., Takahashi T., Hosoe M., Hashizume K.; RT "Expression of Bcl-2 family in bovine placenta."; RL Submitted (OCT-2005) to the EMBL/GenBank/DDBJ databases. RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RX PubMed=16305752; DOI=10.1186/1471-2164-6-166; RA Harhay G.P., Sonstegard T.S., Keele J.W., Heaton M.P., Clawson M.L., RA Snelling W.M., Wiedmann R.T., Van Tassell C.P., Smith T.P.L.; RT "Characterization of 954 bovine full-CDS cDNA sequences."; RL BMC Genomics 6:166-166(2005). RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC STRAIN=Hereford; TISSUE=Heart ventricle; RG NIH - Mammalian Gene Collection (MGC) project; RL Submitted (AUG-2005) 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: Mitochondrion (By similarity). CC -!- SIMILARITY: Belongs to the PTH2 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; AB238942; BAF35578.1; -; mRNA. DR EMBL; BT021191; AAX31373.1; -; mRNA. DR EMBL; BC103230; AAI03231.1; -; mRNA. DR IPI; IPI00694334; -. DR RefSeq; NP_001029691.1; -. DR UniGene; Bt.13767; -. DR SMR; Q3ZBL5; 63-179. DR Ensembl; ENSBTAG00000016710; Bos taurus. DR GeneID; 516595; -. DR KEGG; bta:516595; -. DR HOVERGEN; Q3ZBL5; -. DR OMA; Q3ZBL5; IQRRNPE. DR BRENDA; 3.1.1.29; 251. DR GO; GO:0005739; C:mitochondrion; IEA:UniProtKB-SubCell. DR GO; GO:0004045; F:aminoacyl-tRNA hydrolase activity; IEA:EC. DR GO; GO:0006412; P:translation; IEA:InterPro. DR InterPro; IPR002833; Pep_tRNA_hydro_PTH2. DR Pfam; PF01981; PTH2; 1. DR ProDom; PD010667; UPF0099; 1. DR TIGRFAMs; TIGR00283; Pep_tRNA_hydro_PTH2; 1. PE 2: Evidence at transcript level; KW Hydrolase; Mitochondrion; Phosphoprotein; Transit peptide. FT TRANSIT 1 62 Mitochondrion (Potential). FT CHAIN 63 179 Peptidyl-tRNA hydrolase 2, mitochondrial. FT /FTId=PRO_0000240443. FT MOD_RES 57 57 Phosphoserine (By similarity). FT CONFLICT 20 20 A -> V (in Ref. 2; AAX31373). SQ SEQUENCE 179 AA; 19291 MW; 8FC2E82B73B7BC02 CRC64; MISRSLVMEY LTNPGALSLA AGVACGVCLG WGLRMRFGML PKSSVRETNP DTETEASILG ESGEYKMILV VRNDLKMGKG KVAAQCSHAA VSAYKQIQRR NPELLKEWEY CGQPKVVVKA PDEETLVELL THAKVLGLTV SLIQDAGRTQ IAPGSRTVLG IGPGPADLID KVTGHLKLY //