RNPH_CAUVN
ID RNPH_CAUVN Reviewed; 238 AA.
AC B8GXP2; P48196;
DT 16-JUN-2009, integrated into UniProtKB/Swiss-Prot.
DT 03-MAR-2009, sequence version 1.
DT 03-AUG-2022, entry version 74.
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=CCNA_00151;
OS Caulobacter vibrioides (strain NA1000 / CB15N) (Caulobacter crescentus).
OC Bacteria; Proteobacteria; Alphaproteobacteria; Caulobacterales;
OC Caulobacteraceae; Caulobacter.
OX NCBI_TaxID=565050;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=8606155; DOI=10.1128/jb.178.7.1829-1841.1996;
RA Roberts R.C., Toochinda C., Avedissian M., Baldini R.L., Gomes S.L.,
RA Shapiro L.;
RT "Identification of a Caulobacter crescentus operon encoding hrcA, involved
RT in negatively regulating heat-inducible transcription, and the chaperone
RT gene grpE.";
RL J. Bacteriol. 178:1829-1841(1996).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NA1000 / CB15N;
RX PubMed=20472802; DOI=10.1128/jb.00255-10;
RA Marks M.E., Castro-Rojas C.M., Teiling C., Du L., Kapatral V.,
RA Walunas T.L., Crosson S.;
RT "The genetic basis of laboratory adaptation in Caulobacter crescentus.";
RL J. Bacteriol. 192:3678-3688(2010).
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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; U33324; AAB01514.1; -; Genomic_DNA.
DR EMBL; CP001340; ACL93618.1; -; Genomic_DNA.
DR RefSeq; WP_010918041.1; NC_011916.1.
DR RefSeq; YP_002515526.1; NC_011916.1.
DR AlphaFoldDB; B8GXP2; -.
DR SMR; B8GXP2; -.
DR PRIDE; B8GXP2; -.
DR EnsemblBacteria; ACL93618; ACL93618; CCNA_00151.
DR GeneID; 7332405; -.
DR KEGG; ccs:CCNA_00151; -.
DR PATRIC; fig|565050.3.peg.150; -.
DR HOGENOM; CLU_050858_0_0_5; -.
DR OMA; KGKGQGW; -.
DR OrthoDB; 1824064at2; -.
DR PhylomeDB; B8GXP2; -.
DR Proteomes; UP000001364; Chromosome.
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; Reference proteome; RNA-binding; rRNA processing;
KW Transferase; tRNA processing; tRNA-binding.
FT CHAIN 1..238
FT /note="Ribonuclease PH"
FT /id="PRO_0000378308"
FT BINDING 86
FT /ligand="phosphate"
FT /ligand_id="ChEBI:CHEBI:43474"
FT /ligand_note="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00564"
FT BINDING 124..126
FT /ligand="phosphate"
FT /ligand_id="ChEBI:CHEBI:43474"
FT /ligand_note="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00564"
FT CONFLICT 25..28
FT /note="EGSC -> RAL (in Ref. 1; AAB01514)"
FT /evidence="ECO:0000305"
FT CONFLICT 206
FT /note="K -> T (in Ref. 1; AAB01514)"
FT /evidence="ECO:0000305"
FT CONFLICT 220..234
FT /note="LAEKGINELFALQRA -> AGREGVQRTVRLLARL (in Ref. 1;
FT AAB01514)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 238 AA; 25549 MW; 8DC29753AD7EFE58 CRC64;
MRPSERAPDQ LRAVTLETGV NRYAEGSCLI GFGHTKVLVT ATVEENVPGW MRNKGAGWVT
AEYGMLPRAT HTRGRREAAA GKQTGRTQEI QRLIGRSLRA VVDLKALGER QITLDCDVVQ
ADGGTRTAAI TGAWVALRLA TKYLLDEGVL KTDPILGQVA AVSCGVFNGV PVLDLDYEED
SNAEADSNFV LTGVGDIVEI QATGEKRGFT RAEFESLYGL AEKGINELFA LQRAAIGG
