ID   RNPH_ALCBS              Reviewed;         238 AA.
AC   Q0VT66;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   05-SEP-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=ABO_0206;
OS   Alcanivorax borkumensis (strain SK2 / ATCC 700651 / DSM 11573).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Oceanospirillales;
OC   Alcanivoracaceae; Alcanivorax.
OX   NCBI_TaxID=393595;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=16878126; DOI=10.1038/nbt1232;
RA   Schneiker S., Martins dos Santos V.A.P., Bartels D., Bekel T.,
RA   Brecht M., Buhrmester J., Chernikova T.N., Denaro R., Ferrer M.,
RA   Gertler C., Goesmann A., Golyshina O.V., Kaminski F., Khachane A.N.,
RA   Lang S., Linke B., McHardy A.C., Meyer F., Nechitaylo T., Puehler A.,
RA   Regenhardt D., Rupp O., Sabirova J.S., Selbitschka W., Yakimov M.M.,
RA   Timmis K.N., Vorhoelter F.-J., Weidner S., Kaiser O., Golyshin P.N.;
RT   "Genome sequence of the ubiquitous hydrocarbon-degrading marine
RT   bacterium Alcanivorax borkumensis.";
RL   Nat. Biotechnol. 24:997-1004(2006).
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; AM286690; CAL15654.1; -; Genomic_DNA.
DR   RefSeq; YP_691926.1; -.
DR   GeneID; 4212173; -.
DR   GenomeReviews; AM286690_GR; ABO_0206.
DR   KEGG; abo:ABO_0206; -.
DR   NMPDR; fig|393595.12.peg.205; -.
DR   HOGENOM; Q0VT66; -.
DR   OMA; Q0VT66; YAMLPRA.
DR   BioCyc; ABOR393595:ABO_0206-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    238       Ribonuclease PH.
FT                                /FTId=PRO_1000024769.
SQ   SEQUENCE   238 AA;  25617 MW;  A69CCB3802DA6C74 CRC64;
     MRPSGRAPDQ LRELSFTRNY TVHAEGSVLV AFGNTKVLCT ASVEDGVPRF LKGKGQGWLT
     AEYSMLPRST HTRSGREATR GKQGGRTLEI QRLIGRSLRA AVDMKALGER TIYLDCDVLQ
     ADGGTRTASI SGACVALVDA FTYLLETKKI KNDPLTGLVG AVSVGMYKDT PVLDLDYAED
     SNAGTDMNVV MTQQGGFIEI QGSAEGAPFT REQSDNLLEL AENGIGEIIK AQQVALGW
//