ID PNP_PSEPW Reviewed; 701 AA. AC B1J2B3; DT 14-APR-2009, integrated into UniProtKB/Swiss-Prot. DT 29-APR-2008, sequence version 1. DT 29-SEP-2021, entry version 75. 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=PputW619_0725; OS Pseudomonas putida (strain W619). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales; OC Pseudomonadaceae; Pseudomonas. OX NCBI_TaxID=390235; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=W619; RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., RA Glavina del Rio T., Dalin E., Tice H., Pitluck S., Chain P., Malfatti S., RA Shin M., Vergez L., Schmutz J., Larimer F., Land M., Hauser L., RA Kyrpides N., Kim E., Taghavi S., Vangronsveld D., van der Lelie D., RA Richardson P.; RT "Complete sequence of Pseudomonas putida W619."; RL Submitted (FEB-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; CC Evidence={ECO:0000255|HAMAP-Rule:MF_01595}; CC -!- SUBUNIT: Component of the RNA degradosome, which is a multiprotein CC complex involved in RNA processing and mRNA degradation. CC {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; CP000949; ACA71230.1; -; Genomic_DNA. DR RefSeq; WP_012312657.1; NC_010501.1. DR SMR; B1J2B3; -. DR STRING; 390235.PputW619_0725; -. DR EnsemblBacteria; ACA71230; ACA71230; PputW619_0725. DR KEGG; ppw:PputW619_0725; -. DR eggNOG; COG1185; Bacteria. DR HOGENOM; CLU_004217_2_2_6; -. DR OMA; LHILDVM; -. DR OrthoDB; 122725at2; -. DR BioCyc; PPUT390235:G1GBA-737-MONOMER; -. DR Proteomes; UP000000720; 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; 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; 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; 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; RNA-binding; KW Transferase. FT CHAIN 1..701 FT /note="Polyribonucleotide nucleotidyltransferase" FT /id="PRO_1000147947" 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 METAL 487 FT /note="Magnesium" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01595" FT METAL 493 FT /note="Magnesium" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01595" SQ SEQUENCE 701 AA; 75069 MW; BA473DB3CB45B969 CRC64; MNPVIKKFQF GQSTVTLETG RIARQATGAV LVTVDNDVTV LVTVVGAKQA DPGKGFFPLS VHYQEKTYAA GKIPGGFFKR EGRPSEKETL TSRLIDRPIR PLFPEGFMNE VQVVCTVVST SKKTDPDIAA MIGTSAALAI SGIPFEGPIG AARVAFHEST GYLLNPTYEQ LAASSLDMVV AGTSDAVLMV ESEAQELTED QMLGAVLFAH DEFQAVIQAV KELAAEAGKP TWDWKPAVAN TELFNAIRAE FGEAVSQGYT ITVKADRYAR LGELRDQAIA KFSGEEGQPS ASEVKEIFGE IEYRTVRENI VNGKPRIDGR DTKTVRPLNI EVGVLPKTHG SALFTRGETQ ALVVATLGTA RDAQLLDTLE GEKKDPFMLH YNFPPFSVGE CGRMGGAGRR EIGHGRLARR SVQAMLPAAD VFPYTIRVVS EITESNGSSS MASVCGASLA LMDAGVPMKA PVAGIAMGLV KEGEKFAVLT DILGDEDHLG DMDFKVAGTA KGVTALQMDI KINGITEEIM EIALGQALEA RLNILGQMNQ IIGQSRTELS ANAPTMIAMK IDTDKIRDVI GKGGATIRAI CEETKASIDI EDDGSIKIFG ETKEAAEAAR QRVLGITAEA EIGKIYVGKV ERIVDFGAFV NILPGKDGLV HISMLSDARV EKVTDILKEG QEVEVLVLDV DNRGRIKLSI KDVAAAKASG V //