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Database: UniProt
Entry: A4J7Y7
LinkDB: A4J7Y7
Original site: A4J7Y7 
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   01-OCT-2014, entry version 45.
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=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. {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   -!- SIMILARITY: Belongs to the RNase PH family. {ECO:0000255|HAMAP-
CC       Rule:MF_00564}.
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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; ICTAMVE; -.
DR   OrthoDB; EOG6CZQQP; -.
DR   BioCyc; DRED349161:GHP6-2764-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: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; Reference proteome;
KW   Transferase; 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
//
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