ID   RNPH_BURTA              Reviewed;         243 AA.
AC   Q2SY74;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   24-JAN-2006, sequence version 1.
DT   16-JUN-2009, entry version 24.
DE   RecName: Full=Ribonuclease PH;
DE            Short=RNase PH;
DE            EC=2.7.7.56;
DE   AltName: Full=tRNA nucleotidyltransferase;
GN   Name=rph; OrderedLocusNames=BTH_I1584;
OS   Burkholderia thailandensis (strain E264 / ATCC 700388 / DSM 13276 /
OS   CIP 106301).
OC   Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC   Burkholderiaceae; Burkholderia; pseudomallei group.
OX   NCBI_TaxID=271848;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Fraser C.M., Casjens S., Huang W.M., Sutton G.G., Clayton R.A.,
RA   Lathigra R., White O., Ketchum K.A., Palmer N., Dodson R.,
RA   Hickey E.K., Gwinn M.L., Dougherty B., Fleischmann R.D.,
RA   Richardson D.L., Peterson J.D., Kerlavage A.R., Quackenbush J.,
RA   Salzberg S.L., Hanson M., van-Vugt R., Adams M.D., Gocayne J.D.,
RA   Weidman J., Utterback T.R., Watthey L., McDonald L.A., Artiach P.,
RA   Bowman C., Garland S., Fujii C., Cotton M.D., Horst K., Tomb J.-F.,
RA   Roberts K., Hatch B., Smith H.O., Venter J.C.;
RL   Submitted (JUL-2005) 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.
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DR   EMBL; CP000086; ABC37325.1; -; Genomic_DNA.
DR   RefSeq; YP_442125.1; -.
DR   SMR; Q2SY74; 7-241.
DR   GeneID; 3848958; -.
DR   GenomeReviews; CP000086_GR; BTH_I1584.
DR   KEGG; bte:BTH_I1584; -.
DR   TIGR; BTH_I1584; -.
DR   HOGENOM; Q2SY74; -.
DR   OMA; Q2SY74; YAMLPRA.
DR   BioCyc; BTHA271848:BTH_I1584-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; 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    243       Ribonuclease PH.
FT                                /FTId=PRO_1000024791.
SQ   SEQUENCE   243 AA;  26034 MW;  0D77F5A3603C260A CRC64;
     MTNSSPRPSG RRADQLRDVR ITRHYTKHAE GSVLVEFGET KVICTASVVE RVPEFLRERG
     QGWLTAEYGM LPRATHTRSD REAARGKQTG RTQEIQRLIG RALRAVFDLN ALGPRTLHLD
     CDVIQADGGT RTASITGAFV AAHDAVTKLV AAGKIARSPI TDYVAAISVG VFGGAPVLDL
     DYDEDSACDT DMNVVMTGAG GFVEVQGTAE GVPFSRAEMN ALLDLAQAGI GELVRLQRAA
     LEA
//