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Database: UniProt
Entry: Q479A2
LinkDB: Q479A2
Original site: Q479A2 
ID   RNPH_DECAR              Reviewed;         238 AA.
AC   Q479A2;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   13-SEP-2005, sequence version 1.
DT   01-MAY-2013, entry version 45.
DE   RecName: Full=Ribonuclease PH;
DE            Short=RNase PH;
DE            EC=2.7.7.56;
DE   AltName: Full=tRNA nucleotidyltransferase;
GN   Name=rph; OrderedLocusNames=Daro_3851;
OS   Dechloromonas aromatica (strain RCB).
OC   Bacteria; Proteobacteria; Betaproteobacteria; Rhodocyclales;
OC   Rhodocyclaceae; Dechloromonas.
OX   NCBI_TaxID=159087;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=RCB;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina T.,
RA   Hammon N., Israni S., Pitluck S., Di Bartolo G., Trong S., Kellar K.,
RA   Schmutz J., Larimer F., Land M., Ivanova N., Richardson P.;
RT   "Complete sequence of Dechloromonas aromatica RCB.";
RL   Submitted (AUG-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; CP000089; AAZ48579.1; -; Genomic_DNA.
DR   RefSeq; YP_287049.1; NC_007298.1.
DR   HSSP; O29756; 2BA1.
DR   ProteinModelPortal; Q479A2; -.
DR   SMR; Q479A2; 2-237.
DR   STRING; 159087.Daro_3851; -.
DR   EnsemblBacteria; AAZ48579; AAZ48579; Daro_3851.
DR   GeneID; 3568022; -.
DR   KEGG; dar:Daro_3851; -.
DR   PATRIC; 21606396; VBIDecAro89105_3838.
DR   eggNOG; COG0689; -.
DR   HOGENOM; HOG000229516; -.
DR   KO; K00989; -.
DR   OMA; MLPRATG; -.
DR   ProtClustDB; PRK00173; -.
DR   BioCyc; DARO159087:GI5B-3930-MONOMER; -.
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; RNase_PH; 1; -.
DR   InterPro; IPR001247; ExoRNase_PH_dom1.
DR   InterPro; IPR015847; ExoRNase_PH_dom2.
DR   InterPro; IPR020568; Ribosomal_S5_D2-typ_fold.
DR   InterPro; IPR002381; RNase_PH_bac-type.
DR   InterPro; IPR018336; RNase_PH_CS.
DR   Pfam; PF01138; RNase_PH; 1.
DR   Pfam; PF03725; RNase_PH_C; 1.
DR   SUPFAM; SSF55666; 3_ExoRNase; 1.
DR   SUPFAM; SSF54211; Ribosomal_S5_D2-typ_fold; 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_1000024800.
SQ   SEQUENCE   238 AA;  25696 MW;  7B447A21130B4C1E CRC64;
     MRPSQRQPDQ LRTVRITRNF TRHAEGSVLI EMGDTRVLCT ASVEENVPPF LRGKGQGWVT
     AEYGMLPRAT HTRSSREAAK GKQTGRTQEI QRLIGRALRS VIDLKALGER QITLDCDVLQ
     ADGGTRCASI TGAWVALYEA CDKLVQAGKL PANPVRDHVA AISVGIYKGA PVLDLDYPED
     SDCDTDMNVV MTGAGGIVEI QGTAEGEPFT REQMSVLVDL ATLGVRHLVA AQQSALAA
//
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