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Database: UniProt
Entry: Q0AKA6
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Original site: Q0AKA6 
ID   RNPH_MARMM              Reviewed;         238 AA.
AC   Q0AKA6;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   17-OCT-2006, sequence version 1.
DT   16-APR-2014, entry version 48.
DE   RecName: Full=Ribonuclease PH;
DE            Short=RNase PH;
DE            EC=2.7.7.56;
DE   AltName: Full=tRNA nucleotidyltransferase;
GN   Name=rph; OrderedLocusNames=Mmar10_3006;
OS   Maricaulis maris (strain MCS10).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Rhodobacterales;
OC   Hyphomonadaceae; Maricaulis.
OX   NCBI_TaxID=394221;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MCS10;
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., Saunders E., Brettin T., Bruce D., Han C., Tapia R.,
RA   Gilna P., Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N.,
RA   Mikhailova N., Viollier P., Stephens C., Richardson P.;
RT   "Complete sequence of Maricaulis maris MCS10.";
RL   Submitted (AUG-2006) 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; CP000449; ABI67287.1; -; Genomic_DNA.
DR   RefSeq; YP_758225.1; NC_008347.1.
DR   ProteinModelPortal; Q0AKA6; -.
DR   STRING; 394221.Mmar10_3006; -.
DR   EnsemblBacteria; ABI67287; ABI67287; Mmar10_3006.
DR   GeneID; 4283988; -.
DR   KEGG; mmr:Mmar10_3006; -.
DR   PATRIC; 22454244; VBIMarMar77530_3087.
DR   eggNOG; COG0689; -.
DR   HOGENOM; HOG000229516; -.
DR   KO; K00989; -.
DR   OMA; KGQGWVT; -.
DR   OrthoDB; EOG6CZQQP; -.
DR   ProtClustDB; PRK00173; -.
DR   BioCyc; MMAR394221:GHNB-3060-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; Transferase;
KW   tRNA processing.
FT   CHAIN         1    238       Ribonuclease PH.
FT                                /FTId=PRO_1000024824.
SQ   SEQUENCE   238 AA;  25507 MW;  830E948067F210D2 CRC64;
     MRPHGRARDA MREIKLEAGV SVYAEGSCLA RFGGTHVLCT ASIEESVPPW MRGGGKGWVT
     AEYGMLPRAT HTRSRREATA GKQSGRTQEI QRLIGRSLRA VVDLKALGER QITIDCDVLQ
     ADGGTRTAAI TGAWVALKQA TGYLIEEGLL TSDPVHGQLA AISCGVIDGE TRLDLEYEED
     RRAEADANFV LTDTGGIVEI QATAEDKPIP ETDFDLLFAL AKAGVVDLCE AQLAALKG
//
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