ID PNP_DESDG Reviewed; 750 AA. AC Q30WI5; DT 29-APR-2008, integrated into UniProtKB/Swiss-Prot. DT 06-DEC-2005, sequence version 1. DT 14-MAY-2014, entry version 60. DE RecName: Full=Polyribonucleotide nucleotidyltransferase; DE EC=2.7.7.8; DE AltName: Full=Polynucleotide phosphorylase; DE Short=PNPase; GN Name=pnp; OrderedLocusNames=Dde_3167; OS Desulfovibrio desulfuricans (strain G20). OC Bacteria; Proteobacteria; Deltaproteobacteria; Desulfovibrionales; OC Desulfovibrionaceae; Desulfovibrio. OX NCBI_TaxID=207559; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=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., RA Tapia R., Han C.S., Goodwin L.A., Cheng J.F., Pitluck S., Copeland A., RA Lucas S., 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 CC phosphorolysis of single-stranded polyribonucleotides processively CC in the 3'- to 5'-direction (By similarity). CC -!- CATALYTIC ACTIVITY: RNA(n+1) + phosphate = RNA(n) + a nucleoside CC diphosphate. CC -!- COFACTOR: Magnesium (By similarity). CC -!- SUBCELLULAR LOCATION: Cytoplasm (By similarity). CC -!- SIMILARITY: Belongs to the polyribonucleotide CC nucleotidyltransferase family. CC -!- SIMILARITY: Contains 1 KH domain. CC -!- SIMILARITY: Contains 1 S1 motif domain. 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; YP_389656.1; NC_007519.1. DR ProteinModelPortal; Q30WI5; -. DR STRING; 207559.Dde_3167; -. DR PRIDE; Q30WI5; -. DR EnsemblBacteria; ABB39961; ABB39961; Dde_3167. DR GeneID; 3758142; -. DR KEGG; dde:Dde_3167; -. DR PATRIC; 21745229; VBIDesDes50040_3099. DR eggNOG; COG1185; -. DR HOGENOM; HOG000218326; -. DR KO; K00962; -. DR OMA; HGNFKSN; -. DR OrthoDB; EOG6WT8CC; -. DR BioCyc; DALA207559:GH1L-2826-MONOMER; -. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0000175; F:3'-5'-exoribonuclease activity; IEA:InterPro. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004654; F:polyribonucleotide nucleotidyltransferase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0003723; F:RNA binding; IEA:UniProtKB-HAMAP. DR GO; GO:0006402; P:mRNA catabolic process; IEA:UniProtKB-HAMAP. DR GO; GO:0006396; P:RNA processing; IEA:InterPro. DR Gene3D; 1.10.10.400; -; 1. 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; IPR004087; KH_dom. DR InterPro; IPR004088; KH_dom_type_1. DR InterPro; IPR012340; NA-bd_OB-fold. DR InterPro; IPR012162; PNPase. DR InterPro; IPR027408; PNPase/RNase_PH_dom. DR InterPro; IPR015848; PNPase_PH_RNA-bd_bac/org-type. DR InterPro; IPR003029; Rbsml_prot_S1_RNA-bd_dom. DR InterPro; IPR020568; Ribosomal_S5_D2-typ_fold. DR InterPro; IPR022967; RNA-binding_domain_S1. 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 Complete proteome; Cytoplasm; Magnesium; Metal-binding; KW Nucleotidyltransferase; RNA-binding; Transferase. FT CHAIN 1 750 Polyribonucleotide FT nucleotidyltransferase. FT /FTId=PRO_0000329625. FT DOMAIN 559 618 KH. FT DOMAIN 628 695 S1 motif. FT METAL 492 492 Magnesium (By similarity). FT METAL 498 498 Magnesium (By similarity). 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 //