ID   B1Y0J9_LEPCP            Unreviewed;       241 AA.
AC   B1Y0J9;
DT   20-MAY-2008, integrated into UniProtKB/TrEMBL.
DT   20-MAY-2008, sequence version 1.
DT   01-MAY-2013, entry version 32.
DE   RecName: Full=Ribonuclease PH;
DE            Short=RNase PH;
DE            EC=2.7.7.56;
DE   AltName: Full=tRNA nucleotidyltransferase;
GN   Name=rph; OrderedLocusNames=Lcho_0705;
OS   Leptothrix cholodnii (strain ATCC 51168 / LMG 8142 / SP-6) (Leptothrix
OS   discophora (strain SP-6)).
OC   Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC   Leptothrix.
OX   NCBI_TaxID=395495;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 51168 / LMG 8142 / SP-6;
RG   US DOE Joint Genome Institute;
RA   Copeland A., Lucas S., Lapidus A., Glavina del Rio T., Dalin E.,
RA   Tice H., Bruce D., Goodwin L., Pitluck S., Chertkov O., Brettin T.,
RA   Detter J.C., Han C., Kuske C.R., Schmutz J., Larimer F., Land M.,
RA   Hauser L., Kyrpides N., Lykidis A., Emerson D., Richardson P.;
RT   "Complete sequence of Leptothrix cholodnii SP-6.";
RL   Submitted (MAR-2008) 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; CP001013; ACB32980.1; -; Genomic_DNA.
DR   RefSeq; YP_001789745.1; NC_010524.1.
DR   ProteinModelPortal; B1Y0J9; -.
DR   SMR; B1Y0J9; 5-240.
DR   STRING; 395495.Lcho_0705; -.
DR   EnsemblBacteria; ACB32980; ACB32980; Lcho_0705.
DR   GeneID; 6163753; -.
DR   KEGG; lch:Lcho_0705; -.
DR   PATRIC; 22391689; VBILepCho83238_0706.
DR   eggNOG; COG0689; -.
DR   HOGENOM; HOG000229516; -.
DR   KO; K00989; -.
DR   OMA; MLPRATG; -.
DR   BioCyc; LCHO395495:GHYL-714-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.
SQ   SEQUENCE   241 AA;  25268 MW;  C060C982C26AA38A CRC64;
     MSSTRPLGRA ADALRPVRIT RSYTKHAEGS VLIEFGDTQV LCTASVEEKV PPHKKGSGEG
     WVTAEYGMLP RATHTRSARE AAKGKQSGRT QEIQRLIGRS LRCVFDLAAL GERSILIDCD
     VLQADGGTRT ASITGAFVAA HDAVQGLIAQ GKLKRSPIRD FVAAVSVGIL DGVALLDLEY
     VEDSACDTDM NIVMTGAGGF VEVQGTAEGV AFSRAEMDQL LALGSAGIAE LVAAQKAALG
     V
//