ID   RNPH_CLOPS              Reviewed;         248 AA.
AC   Q0SQU1;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   19-SEP-2006, sequence version 1.
DT   16-JUN-2009, entry version 21.
DE   RecName: Full=Ribonuclease PH;
DE            Short=RNase PH;
DE            EC=2.7.7.56;
DE   AltName: Full=tRNA nucleotidyltransferase;
GN   Name=rph; OrderedLocusNames=CPR_2240;
OS   Clostridium perfringens (strain SM101 / Type A).
OC   Bacteria; Firmicutes; Clostridia; Clostridiales; Clostridiaceae;
OC   Clostridium.
OX   NCBI_TaxID=289380;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=16825665; DOI=10.1101/gr.5238106;
RA   Myers G.S.A., Rasko D.A., Cheung J.K., Ravel J., Seshadri R.,
RA   DeBoy R.T., Ren Q., Varga J., Awad M.M., Brinkac L.M., Daugherty S.C.,
RA   Haft D.H., Dodson R.J., Madupu R., Nelson W.C., Rosovitz M.J.,
RA   Sullivan S.A., Khouri H., Dimitrov G.I., Watkins K.L., Mulligan S.,
RA   Benton J., Radune D., Fisher D.J., Atkins H.S., Hiscox T., Jost B.H.,
RA   Billington S.J., Songer J.G., McClane B.A., Titball R.W., Rood J.I.,
RA   Melville S.B., Paulsen I.T.;
RT   "Skewed genomic variability in strains of the toxigenic bacterial
RT   pathogen, Clostridium perfringens.";
RL   Genome Res. 16:1031-1040(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; CP000312; ABG85418.1; -; Genomic_DNA.
DR   RefSeq; YP_699516.1; -.
DR   GeneID; 4204122; -.
DR   GenomeReviews; CP000312_GR; CPR_2240.
DR   KEGG; cpr:CPR_2240; -.
DR   TIGR; CPR_2240; -.
DR   HOGENOM; Q0SQU1; -.
DR   OMA; Q0SQU1; 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    248       Ribonuclease PH.
FT                                /FTId=PRO_1000024797.
SQ   SEQUENCE   248 AA;  27682 MW;  9F5BB6A32DA93CC1 CRC64;
     MRSSGRKKEQ IRPVKITRNF TKYAEGSVLI EVGDTKVLCT ASIEEKVPPF LKGSGEGWIT
     AEYNMIPRST QSRKQRDINK LKIDGRTMEI QRLIGRALRS AVDMKALGEK TIWIDCDVLQ
     ADGGTRTTSI TGSFVALVDA VNKLHQKKPF NVYPIRHFVS AVSIGIVGEE KVLDLCYEED
     HVAKVDMNVV MIEEGEFIEI QGTGEIGPFS RKELDELLNL AEKGAKQMIQ AQKNALKTDS
     LWIGTGRE
//