ID C1CZJ0_DEIDV Unreviewed; 249 AA. AC C1CZJ0; DT 26-MAY-2009, integrated into UniProtKB/TrEMBL. DT 26-MAY-2009, sequence version 1. DT 27-MAR-2024, entry version 79. 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:ACO47238.1}; GN OrderedLocusNames=Deide_22100 {ECO:0000313|EMBL:ACO47238.1}; OS Deinococcus deserti (strain DSM 17065 / CIP 109153 / LMG 22923 / VCD115). OC Bacteria; Deinococcota; Deinococci; Deinococcales; Deinococcaceae; OC Deinococcus. OX NCBI_TaxID=546414 {ECO:0000313|EMBL:ACO47238.1, ECO:0000313|Proteomes:UP000002208}; RN [1] {ECO:0000313|EMBL:ACO47238.1, ECO:0000313|Proteomes:UP000002208} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=DSM 17065 / CIP 109153 / LMG 22923 / VCD115 RC {ECO:0000313|Proteomes:UP000002208}; RX PubMed=19370165; DOI=10.1371/journal.pgen.1000434; RA de Groot A., Dulermo R., Ortet P., Blanchard L., Guerin P., Fernandez B., RA Vacherie B., Dossat C., Jolivet E., Siguier P., Chandler M., Barakat M., RA Dedieu A., Barbe V., Heulin T., Sommer S., Achouak W., Armengaud J.; RT "Alliance of proteomics and genomics to unravel the specificities of Sahara RT bacterium Deinococcus deserti."; RL PLoS Genet. 5:E1000434-E1000434(2009). 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; CP001114; ACO47238.1; -; Genomic_DNA. DR RefSeq; WP_012694359.1; NC_012526.1. DR AlphaFoldDB; C1CZJ0; -. DR STRING; 546414.Deide_22100; -. DR PaxDb; 546414-Deide_22100; -. DR KEGG; ddr:Deide_22100; -. DR eggNOG; COG0689; Bacteria. DR HOGENOM; CLU_050858_0_0_0; -. DR OrthoDB; 9802265at2; -. DR Proteomes; UP000002208; 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 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 Exonuclease {ECO:0000313|EMBL:ACO47238.1}; KW Hydrolase {ECO:0000313|EMBL:ACO47238.1}; KW Nuclease {ECO:0000313|EMBL:ACO47238.1}; KW Nucleotidyltransferase {ECO:0000256|HAMAP-Rule:MF_00564}; KW Reference proteome {ECO:0000313|Proteomes:UP000002208}; KW RNA-binding {ECO:0000256|ARBA:ARBA00022555, ECO:0000256|HAMAP- KW Rule:MF_00564}; 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:ACO47238.1}; 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 20..147 FT /note="Exoribonuclease phosphorolytic" FT /evidence="ECO:0000259|Pfam:PF01138" FT DOMAIN 166..230 FT /note="Exoribonuclease phosphorolytic" FT /evidence="ECO:0000259|Pfam:PF03725" FT REGION 1..36 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT BINDING 93 FT /ligand="phosphate" FT /ligand_id="ChEBI:CHEBI:43474" FT /ligand_note="substrate" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00564" FT BINDING 131..133 FT /ligand="phosphate" FT /ligand_id="ChEBI:CHEBI:43474" FT /ligand_note="substrate" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00564" SQ SEQUENCE 249 AA; 27199 MW; 973B2E5D06DF694E CRC64; MTSVQPNKFP PREGRGLLEP RPVSVKRGVN PHAPGSAHLI MGRTEILATV TLEDKPAPHM RGKKEGWLTA EYSMLPRATN DRQARERNLQ NGRRHEIQRL LGRALRASVD LKYFRNQTIY VDCDVLVADG GTRVASILAG HAALHDFCDR LINSGQLSEW PLTHKVGAIS VGLVGEEVRV DLDYAEDKVA RADLNVVATD TGLVIEVQGG AEEGPISLAE YSQLLHTGVQ AIHGVMDELG RELAVIQGV //