ID RNPH_DESRM Reviewed; 245 AA.
AC A4J7Y7;
DT 26-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2007, sequence version 1.
DT 29-MAY-2013, entry version 39.
DE RecName: Full=Ribonuclease PH;
DE Short=RNase PH;
DE EC=2.7.7.56;
DE AltName: Full=tRNA nucleotidyltransferase;
GN Name=rph; OrderedLocusNames=Dred_2684;
OS Desulfotomaculum reducens (strain MI-1).
OC Bacteria; Firmicutes; Clostridia; Clostridiales; Peptococcaceae;
OC Desulfotomaculum.
OX NCBI_TaxID=349161;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MI-1;
RG US DOE Joint Genome Institute;
RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H.,
RA Pitluck S., Sims D., Brettin T., Bruce D., Han C., Tapia R.,
RA Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N., Kim E.,
RA Tebo B.M., Richardson P.;
RT "Complete sequence of Desulfotomaculum reducens MI-1.";
RL Submitted (MAR-2007) 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; CP000612; ABO51190.1; -; Genomic_DNA.
DR RefSeq; YP_001114015.1; NC_009253.1.
DR ProteinModelPortal; A4J7Y7; -.
DR SMR; A4J7Y7; 3-239.
DR STRING; 349161.Dred_2684; -.
DR EnsemblBacteria; ABO51190; ABO51190; Dred_2684.
DR GeneID; 4955983; -.
DR KEGG; drm:Dred_2684; -.
DR PATRIC; 21731783; VBIDesRed82656_2937.
DR eggNOG; COG0689; -.
DR HOGENOM; HOG000229516; -.
DR KO; K00989; -.
DR OMA; MLPRATG; -.
DR ProtClustDB; PRK00173; -.
DR BioCyc; DRED349161:GHP6-2764-MONOMER; -.
DR GO; GO:0000049; F:tRNA binding; IEA:InterPro.
DR GO; GO:0009022; F:tRNA nucleotidyltransferase activity; IEA:EC.
DR GO; GO:0004549; F:tRNA-specific ribonuclease activity; IEA:InterPro.
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; 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 1 245 Ribonuclease PH.
FT /FTId=PRO_1000072565.
SQ SEQUENCE 245 AA; 26567 MW; D46F05D1E4FC2F77 CRC64;
MDRVDGRKQG QIRPVRMTPN YNKYAEGSVL IEVGDTRVIC TATVEERVPP FLKGLGKGWV
TAEYSMLPRA TGSRTIREAA RGKLGGRTME IQRLIGRALR SVVNLEALGE RSLTMDCDVI
QADGGTRTAS ITGAYVAMIF ALNRLVEQGM LEKIPVSDFI AATSVGIVKG RPVIDLCYAE
DSVAEVDMNV VMTGTGRFVE IQGTGEEATF SREEMNQLLD LAAAGIEELN KVQRQVLGDI
AAKIG
//
