ID RNPH_BACSU Reviewed; 245 AA. AC P28619; DT 01-DEC-1992, integrated into UniProtKB/Swiss-Prot. DT 01-DEC-1992, sequence version 1. DT 25-NOV-2008, entry version 63. DE RecName: Full=Ribonuclease PH; DE Short=RNase PH; DE EC=2.7.7.56; DE AltName: Full=tRNA nucleotidyltransferase; GN Name=rph; OrderedLocusNames=BSU28370; OS Bacillus subtilis. OC Bacteria; Firmicutes; Bacillales; Bacillaceae; Bacillus. OX NCBI_TaxID=1423; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RX MEDLINE=92325065; PubMed=1624460; RA Craven M.G., Henner D.J., Alessi D., Schauer A.T., Ost K.A., RA Deutscher M.P., Friedman D.I.; RT "Identification of the rph (RNase PH) gene of Bacillus subtilis: RT evidence for suppression of cold-sensitive mutations in Escherichia RT coli."; RL J. Bacteriol. 174:4727-4735(1992). RN [2] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RC STRAIN=168; RX MEDLINE=97124191; PubMed=8969504; RA Wipat A., Carter N., Brignell C.S., Guy J.B., Piper K., Sanders J., RA Emmerson P.T., Harwood C.R.; RT "The dnaB-pheA (256 degrees-240 degrees) region of the Bacillus RT subtilis chromosome containing genes responsible for stress responses, RT the utilization of plant cell walls and primary metabolism."; RL Microbiology 142:3067-3078(1996). RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=168; RX MEDLINE=98044033; PubMed=9384377; DOI=10.1038/36786; RA Kunst F., Ogasawara N., Moszer I., Albertini A.M., Alloni G., RA Azevedo V., Bertero M.G., Bessieres P., Bolotin A., Borchert S., RA Borriss R., Boursier L., Brans A., Braun M., Brignell S.C., Bron S., RA Brouillet S., Bruschi C.V., Caldwell B., Capuano V., Carter N.M., RA Choi S.-K., Codani J.-J., Connerton I.F., Cummings N.J., Daniel R.A., RA Denizot F., Devine K.M., Duesterhoeft A., Ehrlich S.D., Emmerson P.T., RA Entian K.-D., Errington J., Fabret C., Ferrari E., Foulger D., RA Fritz C., Fujita M., Fujita Y., Fuma S., Galizzi A., Galleron N., RA Ghim S.-Y., Glaser P., Goffeau A., Golightly E.J., Grandi G., RA Guiseppi G., Guy B.J., Haga K., Haiech J., Harwood C.R., Henaut A., RA Hilbert H., Holsappel S., Hosono S., Hullo M.-F., Itaya M., RA Jones L.-M., Joris B., Karamata D., Kasahara Y., Klaerr-Blanchard M., RA Klein C., Kobayashi Y., Koetter P., Koningstein G., Krogh S., RA Kumano M., Kurita K., Lapidus A., Lardinois S., Lauber J., RA Lazarevic V., Lee S.-M., Levine A., Liu H., Masuda S., Mauel C., RA Medigue C., Medina N., Mellado R.P., Mizuno M., Moestl D., Nakai S., RA Noback M., Noone D., O'Reilly M., Ogawa K., Ogiwara A., Oudega B., RA Park S.-H., Parro V., Pohl T.M., Portetelle D., Porwollik S., RA Prescott A.M., Presecan E., Pujic P., Purnelle B., Rapoport G., RA Rey M., Reynolds S., Rieger M., Rivolta C., Rocha E., Roche B., RA Rose M., Sadaie Y., Sato T., Scanlan E., Schleich S., Schroeter R., RA Scoffone F., Sekiguchi J., Sekowska A., Seror S.J., Serror P., RA Shin B.-S., Soldo B., Sorokin A., Tacconi E., Takagi T., Takahashi H., RA Takemaru K., Takeuchi M., Tamakoshi A., Tanaka T., Terpstra P., RA Tognoni A., Tosato V., Uchiyama S., Vandenbol M., Vannier F., RA Vassarotti A., Viari A., Wambutt R., Wedler E., Wedler H., RA Weitzenegger T., Winters P., Wipat A., Yamamoto H., Yamane K., RA Yasumoto K., Yata K., Yoshida K., Yoshikawa H.-F., Zumstein E., RA Yoshikawa H., Danchin A.; RT "The complete genome sequence of the Gram-positive bacterium Bacillus RT subtilis."; RL Nature 390:249-256(1997). 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. 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; M85163; AAA22705.1; -; Genomic_DNA. DR EMBL; Z75208; CAA99554.1; -; Genomic_DNA. DR EMBL; Z99118; CAB14797.1; -; Genomic_DNA. DR PIR; A44914; A44914. DR RefSeq; NP_390715.1; -. DR PDB; 1OYP; X-ray; 2.76 A; A/B/C/D/E/F=1-245. DR PDB; 1OYR; X-ray; 3.10 A; A/B/C/D/E/F=1-245. DR PDB; 1OYS; X-ray; 2.40 A; A=1-245. DR PDBsum; 1OYP; -. DR PDBsum; 1OYR; -. DR PDBsum; 1OYS; -. DR GeneID; 937463; -. DR GenomeReviews; AL009126_GR; BSU28370. DR KEGG; bsu:BSU28370; -. DR NMPDR; fig|224308.1.peg.2840; -. DR SubtiList; BG10357; rph. DR HOGENOM; P28619; -. DR BioCyc; BSUB224308:BSU2833-MON; -. 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; 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 1: Evidence at protein level; KW 3D-structure; Complete proteome; Nucleotidyltransferase; Transferase; KW tRNA processing. FT CHAIN 1 245 Ribonuclease PH. FT /FTId=PRO_0000139869. FT STRAND 14 17 FT STRAND 28 32 FT STRAND 35 45 FT HELIX 49 51 FT STRAND 58 64 FT HELIX 86 100 FT HELIX 104 107 FT STRAND 111 120 FT HELIX 125 146 FT STRAND 149 152 FT STRAND 159 167 FT TURN 168 170 FT STRAND 171 175 FT HELIX 178 183 FT STRAND 185 193 FT STRAND 198 207 FT HELIX 212 236 FT HELIX 238 240 SQ SEQUENCE 245 AA; 26681 MW; D180DB086A5316B8 CRC64; MRHDGRQHDE LRPITFDLDF ISHPEGSVLI TAGNTKVICN ASVEDRVPPF LRGGGKGWIT AEYSMLPRAT NQRTIRESSK GKISGRTMEI QRLIGRALRA VVDLEKLGER TIWIDCDVIQ ADGGTRTASI TGAFLAMAIA IGKLIKAGTI KTNPITDFLA AISVGIDKEQ GILLDLNYEE DSSAEVDMNV IMTGSGRFVE LQGTGEEATF SREDLNGLLG LAEKGIQELI DKQKEVLGDS LPELK //