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Database: UniProt
Entry: Q16D02
LinkDB: Q16D02
Original site: Q16D02 
ID   RNPH_ROSDO              Reviewed;         237 AA.
AC   Q16D02;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   25-JUL-2006, sequence version 1.
DT   19-FEB-2014, entry version 50.
DE   RecName: Full=Ribonuclease PH;
DE            Short=RNase PH;
DE            EC=2.7.7.56;
DE   AltName: Full=tRNA nucleotidyltransferase;
GN   Name=rph; OrderedLocusNames=RD1_0426;
OS   Roseobacter denitrificans (strain ATCC 33942 / OCh 114) (Erythrobacter
OS   sp. (strain OCh 114)) (Roseobacter denitrificans).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Rhodobacterales;
OC   Rhodobacteraceae; Roseobacter.
OX   NCBI_TaxID=375451;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 33942 / OCh 114;
RX   PubMed=17098896; DOI=10.1128/JB.01390-06;
RA   Swingley W.D., Sadekar S., Mastrian S.D., Matthies H.J., Hao J.,
RA   Ramos H., Acharya C.R., Conrad A.L., Taylor H.L., Dejesa L.C.,
RA   Shah M.K., O'Huallachain M.E., Lince M.T., Blankenship R.E.,
RA   Beatty J.T., Touchman J.W.;
RT   "The complete genome sequence of Roseobacter denitrificans reveals a
RT   mixotrophic rather than photosynthetic metabolism.";
RL   J. Bacteriol. 189:683-690(2007).
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; CP000362; ABG30141.1; -; Genomic_DNA.
DR   RefSeq; YP_680827.1; NC_008209.1.
DR   ProteinModelPortal; Q16D02; -.
DR   STRING; 375451.RD1_0426; -.
DR   EnsemblBacteria; ABG30141; ABG30141; RD1_0426.
DR   GeneID; 4197993; -.
DR   KEGG; rde:RD1_0426; -.
DR   PATRIC; 23359035; VBIRosDen86677_0421.
DR   eggNOG; COG0689; -.
DR   HOGENOM; HOG000229516; -.
DR   KO; K00989; -.
DR   OMA; KGQGWVT; -.
DR   OrthoDB; EOG6CZQQP; -.
DR   ProtClustDB; PRK00173; -.
DR   BioCyc; RDEN375451:GJIZ-401-MONOMER; -.
DR   GO; GO:0000049; F:tRNA binding; IEA:InterPro.
DR   GO; GO:0009022; F:tRNA nucleotidyltransferase activity; IEA:UniProtKB-EC.
DR   GO; GO:0004549; F:tRNA-specific ribonuclease activity; IEA:InterPro.
DR   GO; GO:0090501; P:RNA phosphodiester bond hydrolysis; IEA:GOC.
DR   GO; GO:0008033; P:tRNA processing; IEA:UniProtKB-KW.
DR   Gene3D; 3.30.230.70; -; 1.
DR   HAMAP; MF_00564; RNase_PH; 1.
DR   InterPro; IPR001247; ExoRNase_PH_dom1.
DR   InterPro; IPR015847; ExoRNase_PH_dom2.
DR   InterPro; IPR027408; PNPase/RNase_PH_dom.
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; SSF54211; SSF54211; 1.
DR   SUPFAM; SSF55666; SSF55666; 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    237       Ribonuclease PH.
FT                                /FTId=PRO_1000024873.
SQ   SEQUENCE   237 AA;  25237 MW;  060943E509684F23 CRC64;
     MRPSGRELNE MRPVSIETGF TKHAEGSALI KIGDTHVLCT ATIEDRVPPF IKGSGLGWVT
     AEYGMLPRAT NTRMRRESTA GKQGGRTVEI QRLIGRSLRA GVDRVALGER QITVDCDVLQ
     ADGGTRCASI TGGWVALRLA VNKLMKAGDV ISDPLVDPVA AISCGIYAGQ PVMDLDYPED
     SEAGVDGNFI MTGSKQLIEV QMSAEGATFS RDQMNQLMDL AEKGVGELVA AQKAATA
//
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