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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   25-APR-2018, entry version 74.
DE   RecName: Full=Ribonuclease PH {ECO:0000255|HAMAP-Rule:MF_00564};
DE            Short=RNase PH {ECO:0000255|HAMAP-Rule:MF_00564};
DE            EC=2.7.7.56 {ECO:0000255|HAMAP-Rule:MF_00564};
DE   AltName: Full=tRNA nucleotidyltransferase {ECO:0000255|HAMAP-Rule:MF_00564};
GN   Name=rph {ECO:0000255|HAMAP-Rule:MF_00564};
GN   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 3'-5' exoribonuclease that plays an
CC       important role in tRNA 3'-end maturation. Removes nucleotide
CC       residues following the 3'-CCA terminus of tRNAs; can also add
CC       nucleotides to the ends of RNA molecules by using nucleoside
CC       diphosphates as substrates, but this may not be physiologically
CC       important. Probably plays a role in initiation of 16S rRNA
CC       degradation (leading to ribosome degradation) during starvation.
CC       {ECO:0000255|HAMAP-Rule:MF_00564}.
CC   -!- CATALYTIC ACTIVITY: tRNA(n+1) + phosphate = tRNA(n) + a nucleoside
CC       diphosphate. {ECO:0000255|HAMAP-Rule:MF_00564}.
CC   -!- SUBUNIT: Homohexameric ring arranged as a trimer of dimers.
CC       {ECO:0000255|HAMAP-Rule:MF_00564}.
CC   -!- SIMILARITY: Belongs to the RNase PH family. {ECO:0000255|HAMAP-
CC       Rule:MF_00564}.
DR   EMBL; CP000362; ABG30141.1; -; Genomic_DNA.
DR   RefSeq; WP_011566763.1; NZ_FOOO01000001.1.
DR   ProteinModelPortal; Q16D02; -.
DR   SMR; Q16D02; -.
DR   STRING; 375451.RD1_0426; -.
DR   EnsemblBacteria; ABG30141; ABG30141; RD1_0426.
DR   KEGG; rde:RD1_0426; -.
DR   eggNOG; ENOG4105ED0; Bacteria.
DR   eggNOG; COG0689; LUCA.
DR   HOGENOM; HOG000229516; -.
DR   KO; K00989; -.
DR   OMA; KGKGQGW; -.
DR   OrthoDB; POG091H03ML; -.
DR   BioCyc; RDEN375451:G1G6J-398-MONOMER; -.
DR   Proteomes; UP000007029; Chromosome.
DR   GO; GO:0000049; F:tRNA binding; IEA:UniProtKB-KW.
DR   GO; GO:0009022; F:tRNA nucleotidyltransferase activity; IEA:UniProtKB-EC.
DR   GO; GO:0006364; P:rRNA processing; IEA:UniProtKB-KW.
DR   GO; GO:0008033; P:tRNA processing; IEA:UniProtKB-KW.
DR   CDD; cd11362; RNase_PH_bact; 1.
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; IPR036345; ExoRNase_PH_dom2_sf.
DR   InterPro; IPR027408; PNPase/RNase_PH_dom_sf.
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; Reference proteome;
KW   RNA-binding; rRNA processing; Transferase; tRNA processing;
KW   tRNA-binding.
FT   CHAIN         1    237       Ribonuclease PH.
FT                                /FTId=PRO_1000024873.
FT   REGION      124    126       Phosphate (substrate) binding.
FT                                {ECO:0000255|HAMAP-Rule:MF_00564}.
FT   BINDING      86     86       Phosphate (substrate) binding.
FT                                {ECO:0000255|HAMAP-Rule:MF_00564}.
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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