ID PNP_OLEA2 Reviewed; 750 AA. AC Q30WI5; DT 29-APR-2008, integrated into UniProtKB/Swiss-Prot. DT 06-DEC-2005, sequence version 1. DT 25-MAY-2022, entry version 94. 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}; OrderedLocusNames=Dde_3167; OS Oleidesulfovibrio alaskensis (strain ATCC BAA-1058 / DSM 17464 / G20) OS (Desulfovibrio alaskensis). OC Bacteria; Proteobacteria; Deltaproteobacteria; Desulfovibrionales; OC Desulfovibrionaceae; Oleidesulfovibrio. OX NCBI_TaxID=207559; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC BAA-1058 / DSM 17464 / G20; RX PubMed=21685289; DOI=10.1128/jb.05400-11; RA Hauser L.J., Land M.L., Brown S.D., Larimer F., Keller K.L., RA Rapp-Giles B.J., Price M.N., Lin M., Bruce D.C., Detter J.C., Tapia R., RA Han C.S., Goodwin L.A., Cheng J.F., Pitluck S., Copeland A., Lucas S., RA Nolan M., Lapidus A.L., Palumbo A.V., Wall J.D.; RT "Complete genome sequence and updated annotation of Desulfovibrio RT alaskensis G20."; RL J. Bacteriol. 193:4268-4269(2011). 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; CC Evidence={ECO:0000255|HAMAP-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; CP000112; ABB39961.1; -; Genomic_DNA. DR RefSeq; WP_011368916.1; NC_007519.1. DR AlphaFoldDB; Q30WI5; -. DR SMR; Q30WI5; -. DR STRING; 207559.Dde_3167; -. DR EnsemblBacteria; ABB39961; ABB39961; Dde_3167. DR KEGG; dde:Dde_3167; -. DR eggNOG; COG1185; Bacteria. DR HOGENOM; CLU_004217_2_2_7; -. DR OMA; LHILDVM; -. DR OrthoDB; 122725at2; -. DR Proteomes; UP000002710; Chromosome. 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 Gene3D; 2.40.50.140; -; 1. DR Gene3D; 3.30.1370.10; -; 1. DR Gene3D; 3.30.230.70; -; 2. 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_S5_D2-typ_fold. DR InterPro; IPR022967; S1_dom. DR InterPro; IPR003029; S1_domain. DR PANTHER; PTHR11252; PTHR11252; 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; SSF46915; SSF46915; 1. DR SUPFAM; SSF50249; SSF50249; 1. DR SUPFAM; SSF54211; SSF54211; 2. DR SUPFAM; SSF54791; SSF54791; 1. DR SUPFAM; SSF55666; SSF55666; 2. DR TIGRFAMs; TIGR03591; polynuc_phos; 1. DR PROSITE; PS50084; KH_TYPE_1; 1. DR PROSITE; PS50126; S1; 1. PE 3: Inferred from homology; KW Cytoplasm; Magnesium; Metal-binding; Nucleotidyltransferase; KW Reference proteome; RNA-binding; Transferase. FT CHAIN 1..750 FT /note="Polyribonucleotide nucleotidyltransferase" FT /id="PRO_0000329625" FT DOMAIN 559..618 FT /note="KH" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01595" FT DOMAIN 628..695 FT /note="S1 motif" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01595" FT REGION 705..750 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 710..750 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT METAL 492 FT /note="Magnesium" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01595" FT METAL 498 FT /note="Magnesium" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01595" SQ SEQUENCE 750 AA; 81752 MW; 05216917061BD92B CRC64; MENLFGAKRL TATVGGKEII METGRLANQA DGAVWIQCGG TVVLCTVCTQ PLEREISFFP LVVDYTEKMY AAGRIPGSFF RREIGRPSER ETLVSRLIDR PLRPLFPKGF TNEVQILANV ISADQENDSD VLALCGSSAA VMLSSVPFEA PVAGARVCRI DGEFVLNPTI TEAAKADLNL VVAANRDALV MVEGEADFVP EEVIAQALEW AHREVQPIID MQEKLRELAG KAKIEFVAPE EDTELKEKAE ALATADLAAA LQVREKMARK EAKKAVKEKV KAALLQDPAF AETPERLAAL GDILSSLEKR IVRQRILKEG LRIDGRDTKT VRPIIIEAGA LPRAHGSAIF SRGETKSLVV TTLGSTTDEQ RMDSLTGDVT KRFMLHYNFP PYSVGEVKPV RVSRREIGHG ALAERALRPV LPSPDSFPFT LRVVSETMES NGSSSMAAVC GGSLSLMDAG VPVKAPVAGI AMGLIKEDDQ FIVLTDILGD EDALGDMDFK IAGTAEGVTA VQMDIKIDGL PAEVMGRALA QAREARLHIL NEMAKVLPEP RQALSKYAPQ LSVVEVNPEI IRVIIGPGGK NIKAITSATG ASIDIEDSGR ISIFAPTKES MDMAREMVMY YDQRPELGKN YTAKVRKIME IGAIVEILPN CEALIHISQL DTSRVEKTED VVQLGQDVEV KVIEINDGRV RASRKAVMLE AQGVEWDPAD TARPPRKPRD RDDRGDRGGR GDRGDRGGRN GRGGDRRDRR //