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 28-JAN-2026, entry version 88. 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=CCNA_00151; OS Caulobacter vibrioides (strain NA1000 / CB15N) (Caulobacter crescentus). OC Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria; OC Caulobacterales; 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=tRNA(n+1) + phosphate = tRNA(n) + a ribonucleoside 5'- CC diphosphate; 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 GeneID; 7332405; -. DR KEGG; ccs:CCNA_00151; -. DR PATRIC; fig|565050.3.peg.150; -. DR HOGENOM; CLU_050858_0_0_5; -. DR OrthoDB; 9802265at2; -. DR PhylomeDB; B8GXP2; -. DR Proteomes; UP000001364; Chromosome. DR GO; GO:0000175; F:3'-5'-RNA exonuclease 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:0031125; P:rRNA 3'-end processing; IEA:UniProtKB-ARBA. DR GO; GO:0016075; P:rRNA catabolic process; IEA:UniProtKB-UniRule. DR GO; GO:0008033; P:tRNA processing; IEA:UniProtKB-UniRule. DR CDD; cd11362; RNase_PH_bact; 1. DR FunFam; 3.30.230.70:FF:000003; Ribonuclease PH; 1. DR Gene3D; 3.30.230.70; GHMP Kinase, N-terminal domain; 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_Su5_D2-typ_SF. DR InterPro; IPR050080; RNase_PH. DR InterPro; IPR002381; RNase_PH_bac-type. DR InterPro; IPR018336; RNase_PH_CS. DR NCBIfam; TIGR01966; RNasePH; 1. DR PANTHER; PTHR11953; EXOSOME COMPLEX COMPONENT; 1. DR PANTHER; PTHR11953:SF0; EXOSOME COMPLEX COMPONENT RRP41; 1. DR Pfam; PF01138; RNase_PH; 1. DR Pfam; PF03725; RNase_PH_C; 1. DR SUPFAM; SSF55666; Ribonuclease PH domain 2-like; 1. DR SUPFAM; SSF54211; Ribosomal protein S5 domain 2-like; 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 //