ID F9ZRB8_ACICS Unreviewed; 241 AA. AC F9ZRB8; DT 19-OCT-2011, integrated into UniProtKB/TrEMBL. DT 19-OCT-2011, sequence version 1. DT 02-DEC-2020, entry version 45. 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=Atc_2268 {ECO:0000313|EMBL:AEK58916.1}; OS Acidithiobacillus caldus (strain SM-1). OC Bacteria; Proteobacteria; Acidithiobacillia; Acidithiobacillales; OC Acidithiobacillaceae; Acidithiobacillus. OX NCBI_TaxID=990288 {ECO:0000313|EMBL:AEK58916.1, ECO:0000313|Proteomes:UP000006135}; RN [1] {ECO:0000313|EMBL:AEK58916.1, ECO:0000313|Proteomes:UP000006135} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=SM-1 {ECO:0000313|EMBL:AEK58916.1, RC ECO:0000313|Proteomes:UP000006135}; RX PubMed=21703548; DOI=10.1016/j.jgg.2011.04.006; RA You X.Y., Guo X., Zheng H.J., Zhang M.J., Liu L.J., Zhu Y.Q., Zhu B., RA Wang S.Y., Zhao G.P., Poetsch A., Jiang C.Y., Liu S.J.; RT "Unraveling the Acidithiobacillus caldus complete genome and its central RT metabolisms for carbon assimilation."; RL J. Genet. Genomics 38:243-252(2011). 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:11132, Rhea:RHEA- CC COMP:11133, ChEBI:CHEBI:43474, ChEBI:CHEBI:57930, ChEBI:CHEBI:83401; 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. {ECO:0000256|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; CP002573; AEK58916.1; -; Genomic_DNA. DR RefSeq; WP_014003343.1; NC_015850.1. DR EnsemblBacteria; AEK58916; AEK58916; Atc_2268. DR KEGG; acu:Atc_2268; -. DR HOGENOM; CLU_050858_0_0_6; -. DR OMA; KGKGQGW; -. DR OrthoDB; 1824064at2; -. DR BioCyc; ACAL990288:G1GZF-2312-MONOMER; -. DR Proteomes; UP000006135; Chromosome. DR GO; GO:0000175; F:3'-5'-exoribonuclease 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; -; 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_S5_D2-typ_fold. DR InterPro; IPR002381; RNase_PH_bac-type. DR InterPro; IPR018336; RNase_PH_CS. DR Pfam; PF01138; RNase_PH; 1. DR Pfam; PF03725; RNase_PH_C; 1. DR SUPFAM; SSF54211; SSF54211; 1. DR SUPFAM; SSF55666; SSF55666; 1. DR TIGRFAMs; TIGR01966; RNasePH; 1. DR PROSITE; PS01277; RIBONUCLEASE_PH; 1. PE 3: Inferred from homology; KW Nucleotidyltransferase {ECO:0000256|HAMAP-Rule:MF_00564}; KW Reference proteome {ECO:0000313|Proteomes:UP000006135}; KW RNA-binding {ECO:0000256|ARBA:ARBA00022884}; KW rRNA processing {ECO:0000256|ARBA:ARBA00022552, ECO:0000256|HAMAP- KW Rule:MF_00564}; Transferase {ECO:0000256|HAMAP-Rule:MF_00564}; 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 12..141 FT /note="RNase_PH" FT /evidence="ECO:0000259|Pfam:PF01138" FT DOMAIN 159..224 FT /note="RNase_PH_C" FT /evidence="ECO:0000259|Pfam:PF03725" FT REGION 125..127 FT /note="Phosphate (substrate) binding" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00564" FT BINDING 87 FT /note="Phosphate (substrate) binding" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00564" SQ SEQUENCE 241 AA; 26365 MW; A760F803B365FB90 CRC64; MPRPSGRDAQ TLRPVEIIRP FTKYAEGSVL IACGDTRVLC TASIEDKVPP FLKGQGRGWV TAEYGMLPRS TQERMPREAA KGKIGGRTHE IQRLIGRSLR AAVDLEALGE RTVWIDCDVL QADGGTRTAS ITGACIALAD ALQGLLQRGV LTHNPWRHWV AAVSVGIRED EAILDLDYAE DSTAEVDMNV VMTDDGRFVE VQGTAEGAAF SAAQMADMLL LARRGIDRLI ARQKSEFPHW P //