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 01-MAY-2013, entry version 46.
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.
CC -----------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution-NoDerivs License
CC -----------------------------------------------------------------------
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; MLPRATG; -.
DR ProtClustDB; PRK00173; -.
DR BioCyc; RDEN375451:GJIZ-401-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 1 237 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
//
