ID G2LE15_CHLTF Unreviewed; 240 AA. AC G2LE15; DT 16-NOV-2011, integrated into UniProtKB/TrEMBL. DT 16-NOV-2011, sequence version 1. DT 02-SEP-2026, entry version 74. 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 OrderedLocusNames=Cabther_A0311 {ECO:0000313|EMBL:AEP11077.1}; OS Chloracidobacterium thermophilum (strain B). OC Bacteria; Pseudomonadati; Acidobacteriota; Blastocatellia; OC Chloracidobacteriales; Chloracidobacteriaceae; Chloracidobacterium. OX NCBI_TaxID=981222 {ECO:0000313|EMBL:AEP11077.1, ECO:0000313|Proteomes:UP000006791}; RN [1] {ECO:0000313|EMBL:AEP11077.1, ECO:0000313|Proteomes:UP000006791} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=B {ECO:0000313|EMBL:AEP11077.1, RC ECO:0000313|Proteomes:UP000006791}; RX PubMed=21951563; DOI=10.1111/j.1462-2920.2011.02592.x; RA Garcia Costas A.M., Liu Z., Tomsho L.P., Schuster S.C., Ward D.M., RA Bryant D.A.; RT "Complete genome of Candidatus Chloracidobacterium thermophilum, a RT chlorophyll-based photoheterotroph belonging to the phylum Acidobacteria."; RL Environ. Microbiol. 14:177-190(2012). 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=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: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; CP002514; AEP11077.1; -; Genomic_DNA. DR RefSeq; WP_014098815.1; NC_016024.1. DR AlphaFoldDB; G2LE15; -. DR STRING; 981222.Cabther_A0311; -. DR KEGG; ctm:Cabther_A0311; -. DR HOGENOM; CLU_050858_0_0_0; -. DR OrthoDB; 9802265at2; -. DR Proteomes; UP000006791; Chromosome 1. 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 {ECO:0000256|HAMAP-Rule:MF_00564, KW ECO:0000313|EMBL:AEP11077.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000006791}; KW 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:AEP11077.1}; 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 11..140 FT /note="Exoribonuclease phosphorolytic" FT /evidence="ECO:0000259|Pfam:PF01138" FT DOMAIN 157..224 FT /note="Exoribonuclease phosphorolytic" FT /evidence="ECO:0000259|Pfam:PF03725" FT BINDING 86 FT /ligand="phosphate" FT /ligand_id="ChEBI:CHEBI:43474" FT /ligand_note="substrate" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00564" FT BINDING 124..126 FT /ligand="phosphate" FT /ligand_id="ChEBI:CHEBI:43474" FT /ligand_note="substrate" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00564" SQ SEQUENCE 240 AA; 26006 MW; 26A131F94DDEA922 CRC64; MRSGGRAPNA LRTVQLTPHV NKYAEGSVQV EFGDTRVICL ASVEEKVPPF LKGKGTGWVT AEYAMLPRAT DQRTPREVTR GNPSGRTHEI QRLIGRSLRA VVDFTKLGER TIYLDCDVIQ ADGGTRTAAI TGAFVALVLA ARKLQAAGVV TDMPVKDYLA AVSVGTVNGT PLLDLDYNED SKAEVDMNVV GTGDGRLVEV QGTAEQRPFS RENMNALLDL AMQGIRELIT LQRQLLGLLE //