ID RNPH_ALHEH Reviewed; 238 AA. AC Q0A5V1; DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot. DT 17-OCT-2006, sequence version 1. DT 16-JUN-2009, entry version 23. DE RecName: Full=Ribonuclease PH; DE Short=RNase PH; DE EC=2.7.7.56; DE AltName: Full=tRNA nucleotidyltransferase; GN Name=rph; OrderedLocusNames=Mlg_2446; 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: Phosphorolytic exoribonuclease that removes nucleotide CC residues following the -CCA terminus of tRNA and adds nucleotides CC to the ends of RNA molecules by using nucleoside diphosphates as CC substrates (By similarity). CC -!- CATALYTIC ACTIVITY: tRNA(n+1) + phosphate = tRNA(n) + a nucleoside CC diphosphate. CC -!- SIMILARITY: Belongs to the RNase PH 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; ABI57786.1; -; Genomic_DNA. DR RefSeq; YP_743276.1; -. DR SMR; Q0A5V1; 2-236. DR GeneID; 4268752; -. DR GenomeReviews; CP000453_GR; Mlg_2446. DR KEGG; aeh:Mlg_2446; -. DR NMPDR; fig|187272.6.peg.2330; -. DR HOGENOM; Q0A5V1; -. DR OMA; Q0A5V1; YAMLPRA. DR GO; GO:0000175; F:3'-5'-exoribonuclease activity; IEA:InterPro. DR GO; GO:0000049; F:tRNA binding; IEA:HAMAP. DR GO; GO:0009022; F:tRNA nucleotidyltransferase activity; IEA:HAMAP. DR GO; GO:0004549; F:tRNA-specific ribonuclease activity; IEA:InterPro. DR GO; GO:0008033; P:tRNA processing; IEA:HAMAP. DR HAMAP; MF_00564; -; 1. DR InterPro; IPR001247; ExoRNase_PH_dom1. DR InterPro; IPR015847; ExoRNase_PH_dom2. DR InterPro; IPR018336; Ribonuclease-PH_CS. DR InterPro; IPR002381; RNase_PH_bac-type. DR Pfam; PF01138; RNase_PH; 1. DR Pfam; PF03725; RNase_PH_C; 1. DR TIGRFAMs; TIGR01966; RNasePH; 1. DR PROSITE; PS01277; RIBONUCLEASE_PH; 1. PE 3: Inferred from homology; KW Complete proteome; Nucleotidyltransferase; Transferase; KW tRNA processing. FT CHAIN 1 238 Ribonuclease PH. FT /FTId=PRO_1000024770. SQ SEQUENCE 238 AA; 26200 MW; 6AEFAFCEA8BF9C90 CRC64; MRPSGRKPDE LRPVRLTRHY TRHAEGSVLV EFGDTRVLCT ASVEERVPPW LRNQGRGWVT AEYGMLPRST GTRNDREAAR GKQQGRTIEI QRLIGRALRA AVDLEALGER RVVLDCDVLQ ADGGTRTAAI TGAYVALVDA CNLLRKEGRI RRSPIFGQVA AVSVGIYQGT PVLDLDYAED SEAETDMNVV MNEAGGFIEL QGTAEGHAFR RDELNAMTEL AELGVAQLIE TQRQALEA //