ID PNP_GEOSW Reviewed; 712 AA. AC C5D9D5; DT 22-SEP-2009, integrated into UniProtKB/Swiss-Prot. DT 28-JUL-2009, sequence version 1. DT 27-MAR-2024, entry version 78. DE RecName: Full=Polyribonucleotide nucleotidyltransferase {ECO:0000255|HAMAP-Rule:MF_01595}; DE EC=2.7.7.8 {ECO:0000255|HAMAP-Rule:MF_01595}; DE AltName: Full=Polynucleotide phosphorylase {ECO:0000255|HAMAP-Rule:MF_01595}; DE Short=PNPase {ECO:0000255|HAMAP-Rule:MF_01595}; GN Name=pnp {ECO:0000255|HAMAP-Rule:MF_01595}; GN OrderedLocusNames=GWCH70_1161; OS Geobacillus sp. (strain WCH70). OC Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Geobacillus. OX NCBI_TaxID=471223; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=WCH70; RG US DOE Joint Genome Institute; RA Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E., Tice H., RA Bruce D., Goodwin L., Pitluck S., Chertkov O., Brettin T., Detter J.C., RA Han C., Larimer F., Land M., Hauser L., Kyrpides N., Mikhailova N., RA Brumm P., Mead D.A., Richardson P.; RT "Complete sequence of chromosome of Geopacillus sp. WCH70."; RL Submitted (JUN-2009) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Involved in mRNA degradation. Catalyzes the phosphorolysis of CC single-stranded polyribonucleotides processively in the 3'- to 5'- CC direction. {ECO:0000255|HAMAP-Rule:MF_01595}. CC -!- CATALYTIC ACTIVITY: CC Reaction=phosphate + RNA(n+1) = a ribonucleoside 5'-diphosphate + CC RNA(n); Xref=Rhea:RHEA:22096, Rhea:RHEA-COMP:14527, Rhea:RHEA- CC COMP:17342, ChEBI:CHEBI:43474, ChEBI:CHEBI:57930, ChEBI:CHEBI:140395; CC EC=2.7.7.8; Evidence={ECO:0000255|HAMAP-Rule:MF_01595}; CC -!- COFACTOR: CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000255|HAMAP- CC Rule:MF_01595}; CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_01595}. CC -!- SIMILARITY: Belongs to the polyribonucleotide nucleotidyltransferase CC family. {ECO:0000255|HAMAP-Rule:MF_01595}. 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; CP001638; ACS24021.1; -; Genomic_DNA. DR AlphaFoldDB; C5D9D5; -. DR SMR; C5D9D5; -. DR STRING; 471223.GWCH70_1161; -. DR KEGG; gwc:GWCH70_1161; -. DR eggNOG; COG1185; Bacteria. DR HOGENOM; CLU_004217_2_2_9; -. DR OrthoDB; 9804305at2; -. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-UniRule. DR GO; GO:0004654; F:polyribonucleotide nucleotidyltransferase activity; IEA:UniProtKB-UniRule. DR GO; GO:0003723; F:RNA binding; IEA:UniProtKB-UniRule. DR GO; GO:0006402; P:mRNA catabolic process; IEA:UniProtKB-UniRule. DR GO; GO:0006396; P:RNA processing; IEA:InterPro. DR CDD; cd02393; KH-I_PNPase; 1. DR CDD; cd11363; RNase_PH_PNPase_1; 1. DR CDD; cd11364; RNase_PH_PNPase_2; 1. DR CDD; cd04472; S1_PNPase; 1. DR Gene3D; 3.30.230.70; GHMP Kinase, N-terminal domain; 2. DR Gene3D; 3.30.1370.10; K Homology domain, type 1; 1. DR Gene3D; 2.40.50.140; Nucleic acid-binding proteins; 1. DR HAMAP; MF_01595; PNPase; 1. DR InterPro; IPR001247; ExoRNase_PH_dom1. DR InterPro; IPR015847; ExoRNase_PH_dom2. DR InterPro; IPR036345; ExoRNase_PH_dom2_sf. DR InterPro; IPR004087; KH_dom. DR InterPro; IPR004088; KH_dom_type_1. DR InterPro; IPR036612; KH_dom_type_1_sf. DR InterPro; IPR012340; NA-bd_OB-fold. DR InterPro; IPR012162; PNPase. DR InterPro; IPR027408; PNPase/RNase_PH_dom_sf. DR InterPro; IPR015848; PNPase_PH_RNA-bd_bac/org-type. DR InterPro; IPR020568; Ribosomal_Su5_D2-typ_SF. DR InterPro; IPR003029; S1_domain. DR NCBIfam; TIGR03591; polynuc_phos; 1. DR PANTHER; PTHR11252; POLYRIBONUCLEOTIDE NUCLEOTIDYLTRANSFERASE; 1. DR PANTHER; PTHR11252:SF0; POLYRIBONUCLEOTIDE NUCLEOTIDYLTRANSFERASE 1, MITOCHONDRIAL; 1. DR Pfam; PF00013; KH_1; 1. DR Pfam; PF03726; PNPase; 1. DR Pfam; PF01138; RNase_PH; 2. DR Pfam; PF03725; RNase_PH_C; 2. DR Pfam; PF00575; S1; 1. DR PIRSF; PIRSF005499; PNPase; 1. DR SMART; SM00322; KH; 1. DR SMART; SM00316; S1; 1. DR SUPFAM; SSF54791; Eukaryotic type KH-domain (KH-domain type I); 1. DR SUPFAM; SSF50249; Nucleic acid-binding proteins; 1. DR SUPFAM; SSF55666; Ribonuclease PH domain 2-like; 2. DR SUPFAM; SSF54211; Ribosomal protein S5 domain 2-like; 2. DR PROSITE; PS50084; KH_TYPE_1; 1. DR PROSITE; PS50126; S1; 1. PE 3: Inferred from homology; KW Cytoplasm; Magnesium; Metal-binding; Nucleotidyltransferase; RNA-binding; KW Transferase. FT CHAIN 1..712 FT /note="Polyribonucleotide nucleotidyltransferase" FT /id="PRO_1000215661" FT DOMAIN 554..613 FT /note="KH" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01595" FT DOMAIN 623..691 FT /note="S1 motif" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01595" FT BINDING 487 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01595" FT BINDING 493 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01595" SQ SEQUENCE 712 AA; 78909 MW; FDAE9FE8F54103B7 CRC64; MEQEKRIFSI DWAGRPLVVE IGQLAKQANG AVLVRYGDTV VLNTATASKE AKNVDFFPLT VNYEERLYAV GKIPGGFIKR EGRPSEKAIL ASRLIDRPIR PLFAEGFRNE VQIVSMVMSV DQDCSPEMAA LFGASLALTI SDIPFEGPIA GVTVGRVDGE FVINPTVEQS EKSDIHLVVA GTKDAINMVE AGADEVPEEV ILEAIMFGHE EVKRLIAFQE EIAAQVGKEK MEVVLYELDP QLEAEIRQLA EEDIKRAVQV PEKLARDAAI EEVKASVIAK YEEQEADEET LKQVNEILHK LVKEEVRRLI TEEKIRPDGR KIDEIRPLSS EVGVLPRTHG SGLFTRGQTQ VLSVCTLGAL GDVQILDGLG IEETKRFMHH YNFPPFSVGE TGPMRGPGRR EIGHGALGER ALEPVVPSEK EFPYTIRLVS EVLESNGSTS QASICASTLA MMDAGVPIKA PVAGIAMGLV KNDDNYTILT DIQGIEDHLG DMDFKVAGTA KGVTALQMDI KIKGLSREIL EEALQQAKKG RMEILEHMMQ TIREPRKELS KYAPKILTMQ INPEKIREVI GPSGKQINKI IDETGVKIDI EQDGTIFISS VNEAMNQKAK QIIEDIVREV EVGQIYLGKV KRIEKFGAFV ELFNGKDGLV HISELAEERV GRVEDVVSIG DEILVKVMEI DKQGRVNLSR KAVLRDKKEK KGKRPERHRM KP //