ID PNP_CLOBA Reviewed; 704 AA. AC B2V4H5; DT 14-APR-2009, integrated into UniProtKB/Swiss-Prot. DT 01-JUL-2008, sequence version 1. DT 27-MAR-2024, entry version 79. 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=CLH_1230; OS Clostridium botulinum (strain Alaska E43 / Type E3). OC Bacteria; Bacillota; Clostridia; Eubacteriales; Clostridiaceae; OC Clostridium. OX NCBI_TaxID=508767; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Alaska E43 / Type E3; RA Brinkac L.M., Brown J.L., Bruce D., Detter C., Munk C., Smith L.A., RA Smith T.J., Sutton G., Brettin T.S.; RT "Complete genome sequence of Clostridium botulinum E3 str. Alaska E43."; RL Submitted (MAY-2008) 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; CP001078; ACD52528.1; -; Genomic_DNA. DR RefSeq; WP_003374359.1; NC_010723.1. DR AlphaFoldDB; B2V4H5; -. DR SMR; B2V4H5; -. DR KEGG; cbt:CLH_1230; -. DR HOGENOM; CLU_004217_2_2_9; -. 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; IPR036456; PNPase_PH_RNA-bd_sf. 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; 1. 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; SSF46915; Polynucleotide phosphorylase/guanosine pentaphosphate synthase (PNPase/GPSI), domain 3; 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..704 FT /note="Polyribonucleotide nucleotidyltransferase" FT /id="PRO_1000192470" FT DOMAIN 552..611 FT /note="KH" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01595" FT DOMAIN 621..689 FT /note="S1 motif" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01595" FT BINDING 485 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01595" FT BINDING 491 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01595" SQ SEQUENCE 704 AA; 77547 MW; 4C3BD0CE43E9D131 CRC64; MNNVLSTNIA GKEMKVEFGK IGMLSNAATF MSYGDTVILT NVNASSEPRV GIDFFPLSVE YEERLYAVGK IPGGFIKREG RPSEKAILNG RAVDRTLRPL FPKGYRNDVQ VVCTVVSVEK DNLPEILAIN AASMALCLSS IPFAMPVAAV QVGLIDNNFI VNPNATEREE STLHLTVCAT KERVMMIEAG GNEIPEDIMI AAIKFGFDEC QNIINFQEEA VKKFGKEKDI PTLFTVDEEV EKDIKEFASD MIKEAMYITD KDERNAAIDA VNQKVKEEFG EKYEDKFGDI KEVLYNMQKK VVRHMLLKDK RRPDGRAFDQ VRPLGCEVGL LPRTHGTGLF TRGLTQVMTV ATLGAVGDIQ ILDGIDEAQS KRYMHHYNFP GYSVGEVKPL RGPGRREIGH GALAERALEP LIPSEEEFPY TIRLVSEVLS SNGSTSQASV CGSTLALLDA GVPLKRPAAG IAMGLITSED LSEEQVLTDI QGIEDFFGDM DFKVAGTTEG ITSIQVDTKL KGFSFNVVEN AIRDARKARM TILEKINECI SSPREDVSLY APKTETIQID PDKIRSVIGA GGKVINKIIQ DTGVKIDIKE DGSVFVSSSD HEGVKEAIKI IEGLTKDVKA GEIYLGKVTK ITTFGAFVEI LPNKEGLVHI SKLDKERVNK VEDVVSVGDE ILVKVTEIDS QGRINLSRKD VLLDQENKEN KEEK //