ID A9ILQ1_BORPD Unreviewed; 246 AA. AC A9ILQ1; DT 05-FEB-2008, integrated into UniProtKB/TrEMBL. DT 05-FEB-2008, sequence version 1. DT 27-MAR-2024, entry version 92. DE RecName: Full=Ribonuclease PH {ECO:0000256|HAMAP-Rule:MF_00564}; DE Short=RNase PH {ECO:0000256|HAMAP-Rule:MF_00564}; DE EC=2.7.7.56 {ECO:0000256|HAMAP-Rule:MF_00564}; DE AltName: Full=tRNA nucleotidyltransferase {ECO:0000256|HAMAP-Rule:MF_00564}; GN Name=rph {ECO:0000256|HAMAP-Rule:MF_00564, GN ECO:0000313|EMBL:CAP42611.1}; GN OrderedLocusNames=Bpet2268 {ECO:0000313|EMBL:CAP42611.1}; OS Bordetella petrii (strain ATCC BAA-461 / DSM 12804 / CCUG 43448). OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales; OC Alcaligenaceae; Bordetella. OX NCBI_TaxID=340100 {ECO:0000313|EMBL:CAP42611.1, ECO:0000313|Proteomes:UP000001225}; RN [1] {ECO:0000313|EMBL:CAP42611.1, ECO:0000313|Proteomes:UP000001225} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC BAA-461 / DSM 12804 / CCUG 43448 RC {ECO:0000313|Proteomes:UP000001225}; RX PubMed=18826580; DOI=10.1186/1471-2164-9-449; RA Gross R., Guzman C.A., Sebaihia M., Martins Dos Santos V.A., Pieper D.H., RA Koebnik R., Lechner M., Bartels D., Buhrmester J., Choudhuri J.V., RA Ebensen T., Gaigalat L., Herrmann S., Khachane A.N., Larisch C., Link S., RA Linke B., Meyer F., Mormann S., Nakunst D., Rueckert C., RA Schneiker-Bekel S., Schulze K., Vorhoelter F.J., Yevsa T., Engle J.T., RA Goldman W.E., Puehler A., Goebel U.B., Goesmann A., Bloecker H., Kaiser O., RA Martinez-Arias R.; RT "The missing link: Bordetella petrii is endowed with both the metabolic RT versatility of environmental bacteria and virulence traits of pathogenic RT Bordetellae."; RL BMC Genomics 9:449-449(2008). 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:0000256|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:0000256|HAMAP-Rule:MF_00564}; CC -!- SUBUNIT: Homohexameric ring arranged as a trimer of dimers. CC {ECO:0000256|HAMAP-Rule:MF_00564}. CC -!- SIMILARITY: Belongs to the RNase PH family. CC {ECO:0000256|ARBA:ARBA00006678, ECO:0000256|HAMAP-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; AM902716; CAP42611.1; -; Genomic_DNA. DR AlphaFoldDB; A9ILQ1; -. DR STRING; 94624.Bpet2268; -. DR KEGG; bpt:Bpet2268; -. DR eggNOG; COG0689; Bacteria. DR Proteomes; UP000001225; 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: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; 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; 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:SF2; EXOSOME COMPLEX COMPONENT MTR3; 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 {ECO:0000256|HAMAP-Rule:MF_00564, KW ECO:0000313|EMBL:CAP42611.1}; RNA-binding {ECO:0000256|ARBA:ARBA00022884}; KW rRNA processing {ECO:0000256|ARBA:ARBA00022552, ECO:0000256|HAMAP- KW Rule:MF_00564}; KW Transferase {ECO:0000256|HAMAP-Rule:MF_00564, ECO:0000313|EMBL:CAP42611.1}; KW tRNA processing {ECO:0000256|ARBA:ARBA00022694, ECO:0000256|HAMAP- KW Rule:MF_00564}; KW tRNA-binding {ECO:0000256|ARBA:ARBA00022555, ECO:0000256|HAMAP- KW Rule:MF_00564}. FT DOMAIN 19..149 FT /note="Exoribonuclease phosphorolytic" FT /evidence="ECO:0000259|Pfam:PF01138" FT DOMAIN 166..232 FT /note="Exoribonuclease phosphorolytic" FT /evidence="ECO:0000259|Pfam:PF03725" FT BINDING 95 FT /ligand="phosphate" FT /ligand_id="ChEBI:CHEBI:43474" FT /ligand_note="substrate" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00564" FT BINDING 133..135 FT /ligand="phosphate" FT /ligand_id="ChEBI:CHEBI:43474" FT /ligand_note="substrate" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00564" SQ SEQUENCE 246 AA; 25915 MW; 53ACB1E08D17C0A9 CRC64; MSSSTASAVA RPSGRAVDQL RPFSLQRGYT RYAEGSVLVR AGNTHVLCTA SVLDKVPPFL KGRGEGWVTA EYGMLPRATH TRGDREAARG KQSGRTQEIQ RLIGRSLRAV FDMKALGERT LHLDCDVLQA DGGTRCASIT GAWVAAADAV ALLMQRGDLA ANPIRDAVAA VSVGMVAGRP VLDLDYQEDS ACDADVNVVM TGAGAFVEVQ GTGEGATFAR SELDAMLGLA EQGIAQLVRA QREALA //