RNPH_PSEMY
ID RNPH_PSEMY Reviewed; 239 AA.
AC A4Y0L7;
DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT 29-MAY-2007, sequence version 1.
DT 03-AUG-2022, entry version 78.
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}; OrderedLocusNames=Pmen_4386;
OS Pseudomonas mendocina (strain ymp).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC Pseudomonadaceae; Pseudomonas.
OX NCBI_TaxID=399739;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ymp;
RG US DOE Joint Genome Institute;
RA Copeland A., Lucas S., Lapidus A., Barry K., Glavina del Rio T., Dalin E.,
RA Tice H., Pitluck S., Kiss H., Brettin T., Detter J.C., Bruce D., Han C.,
RA Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N., Mikhailova N.,
RA Hersman L., Dubois J., Maurice P., Richardson P.;
RT "Complete sequence of Pseudomonas mendocina ymp.";
RL Submitted (APR-2007) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Phosphorolytic 3'-5' exoribonuclease that plays an important
CC role in tRNA 3'-end maturation. Removes nucleotide residues following
CC the 3'-CCA terminus of tRNAs; can also add nucleotides to the ends of
CC RNA molecules by using nucleoside diphosphates as substrates, but this
CC may not be physiologically important. Probably plays a role in
CC initiation of 16S rRNA degradation (leading to ribosome degradation)
CC during starvation. {ECO:0000255|HAMAP-Rule:MF_00564}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=phosphate + tRNA(n+1) = a ribonucleoside 5'-diphosphate +
CC tRNA(n); Xref=Rhea:RHEA:10628, Rhea:RHEA-COMP:17343, Rhea:RHEA-
CC COMP:17344, ChEBI:CHEBI:43474, ChEBI:CHEBI:57930, ChEBI:CHEBI:173114;
CC EC=2.7.7.56; Evidence={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}.
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DR EMBL; CP000680; ABP87133.1; -; Genomic_DNA.
DR RefSeq; WP_012020147.1; NC_009439.1.
DR AlphaFoldDB; A4Y0L7; -.
DR SMR; A4Y0L7; -.
DR STRING; 399739.Pmen_4386; -.
DR EnsemblBacteria; ABP87133; ABP87133; Pmen_4386.
DR KEGG; pmy:Pmen_4386; -.
DR PATRIC; fig|399739.8.peg.4445; -.
DR eggNOG; COG0689; Bacteria.
DR HOGENOM; CLU_050858_0_0_6; -.
DR OMA; KGKGQGW; -.
DR OrthoDB; 1824064at2; -.
DR GO; GO:0000175; F:3'-5'-exoribonuclease activity; IEA:UniProtKB-UniRule.
DR GO; GO:0000049; F:tRNA binding; IEA:UniProtKB-UniRule.
DR GO; GO:0009022; F:tRNA nucleotidyltransferase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0016075; P:rRNA catabolic process; IEA:UniProtKB-UniRule.
DR GO; GO:0006364; P:rRNA processing; IEA:UniProtKB-KW.
DR GO; GO:0008033; P:tRNA processing; IEA:UniProtKB-UniRule.
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 Nucleotidyltransferase; RNA-binding; rRNA processing; Transferase;
KW tRNA processing; tRNA-binding.
FT CHAIN 1..239
FT /note="Ribonuclease PH"
FT /id="PRO_1000024851"
FT BINDING 87
FT /ligand="phosphate"
FT /ligand_id="ChEBI:CHEBI:43474"
FT /ligand_note="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00564"
FT BINDING 125..127
FT /ligand="phosphate"
FT /ligand_id="ChEBI:CHEBI:43474"
FT /ligand_note="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00564"
SQ SEQUENCE 239 AA; 25790 MW; 48F791E2632CCF7B CRC64;
MKRPSGRAAD QLRSIRITRN YTKHAEGSVL VEFGDTKVIC TVSVESGVPR FLKGQGQGWL
TAEYGMLPRA TGERNQREAS RGKQGGRTLE IQRLIGRSLR AALDMSKLGE NTLYVDCDVI
QADGGTRTAS ITGAMVALID ALKVLKKRGS LKGEPLKQMI AAVSVGIYQG EPVLDLDYLE
DSAAETDLNV VMTNAGGFIE VQGTAEGAPF QPEEFNAMLA LAQKGMNEIF ELQKAALVD
