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Database: UniProt
Entry: Q0AKA6
LinkDB: Q0AKA6
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   28-FEB-2018, entry version 68.
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=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 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; CP000449; ABI67287.1; -; Genomic_DNA.
DR   RefSeq; WP_011644931.1; NC_008347.1.
DR   ProteinModelPortal; Q0AKA6; -.
DR   SMR; Q0AKA6; -.
DR   STRING; 394221.Mmar10_3006; -.
DR   EnsemblBacteria; ABI67287; ABI67287; Mmar10_3006.
DR   KEGG; mmr:Mmar10_3006; -.
DR   eggNOG; ENOG4105ED0; Bacteria.
DR   eggNOG; COG0689; LUCA.
DR   HOGENOM; HOG000229516; -.
DR   KO; K00989; -.
DR   OMA; KGKGQGW; -.
DR   OrthoDB; POG091H03ML; -.
DR   BioCyc; MMAR394221:G1G79-3098-MONOMER; -.
DR   Proteomes; UP000001964; Chromosome.
DR   GO; GO:0000049; F:tRNA binding; IEA:InterPro.
DR   GO; GO:0009022; F:tRNA nucleotidyltransferase activity; IEA:UniProtKB-EC.
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    238       Ribonuclease PH.
FT                                /FTId=PRO_1000024824.
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   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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