ID C7QB87_CATAD Unreviewed; 243 AA. AC C7QB87; DT 13-OCT-2009, integrated into UniProtKB/TrEMBL. DT 13-OCT-2009, sequence version 1. DT 27-MAR-2024, entry version 78. 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=Caci_7553 {ECO:0000313|EMBL:ACU76378.1}; OS Catenulispora acidiphila (strain DSM 44928 / JCM 14897 / NBRC 102108 / NRRL OS B-24433 / ID139908). OC Bacteria; Actinomycetota; Actinomycetes; Catenulisporales; OC Catenulisporaceae; Catenulispora. OX NCBI_TaxID=479433 {ECO:0000313|EMBL:ACU76378.1, ECO:0000313|Proteomes:UP000000851}; RN [1] {ECO:0000313|EMBL:ACU76378.1, ECO:0000313|Proteomes:UP000000851} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=DSM 44928 / JCM 14897 / NBRC 102108 / NRRL B-24433 / ID139908 RC {ECO:0000313|Proteomes:UP000000851}; RX PubMed=21304647; DOI=10.4056/sigs.17259; RA Copeland A., Lapidus A., Glavina Del Rio T., Nolan M., Lucas S., Chen F., RA Tice H., Cheng J.F., Bruce D., Goodwin L., Pitluck S., Mikhailova N., RA Pati A., Ivanova N., Mavromatis K., Chen A., Palaniappan K., Chain P., RA Land M., Hauser L., Chang Y.J., Jeffries C.D., Chertkov O., Brettin T., RA Detter J.C., Han C., Ali Z., Tindall B.J., Goker M., Bristow J., RA Eisen J.A., Markowitz V., Hugenholtz P., Kyrpides N.C., Klenk H.P.; RT "Complete genome sequence of Catenulispora acidiphila type strain (ID RT 139908)."; RL Stand. Genomic Sci. 1:119-125(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; CP001700; ACU76378.1; -; Genomic_DNA. DR RefSeq; WP_015796103.1; NC_013131.1. DR AlphaFoldDB; C7QB87; -. DR STRING; 479433.Caci_7553; -. DR KEGG; cai:Caci_7553; -. DR eggNOG; COG0689; Bacteria. DR HOGENOM; CLU_050858_0_0_11; -. DR InParanoid; C7QB87; -. DR OrthoDB; 9802265at2; -. DR Proteomes; UP000000851; 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:ACU76378.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000000851}; 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:ACU76378.1}; 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 13..143 FT /note="Exoribonuclease phosphorolytic" FT /evidence="ECO:0000259|Pfam:PF01138" FT DOMAIN 163..228 FT /note="Exoribonuclease phosphorolytic" FT /evidence="ECO:0000259|Pfam:PF03725" FT BINDING 89 FT /ligand="phosphate" FT /ligand_id="ChEBI:CHEBI:43474" FT /ligand_note="substrate" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00564" FT BINDING 127..129 FT /ligand="phosphate" FT /ligand_id="ChEBI:CHEBI:43474" FT /ligand_note="substrate" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00564" SQ SEQUENCE 243 AA; 25928 MW; A26A632488200C36 CRC64; MSAARVDGRK VGQLRPVTLT RKWSIHPEGS VLVEFGQTKV LCTASVTEGV PRWLRGSGKG WVTAEYAMLP RATNTRGDRE SVKGKVGGRT QEISRLIGRA LRAVVDTKAL GENTIIVDCD VLQADGGTRT AAITGAYVAL QDAVTWMRDK KMIKASREPL AGSVSAVSVG IIDGVPMLDL CYEEDVRAET DMNVVCTADG KFVEVQGTAE GAPFDRAELD ALLDLAAAGC RELASHQVKA LLS //