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 04-MAR-2015, entry version 50. 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., RA Malfatti S., Shin M., Vergez L., Schmutz J., Larimer F., Land M., RA Hauser L., Kyrpides N., Kim E., Taghavi S., Vangronsveld D., RA van der Lelie D., 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 CC phosphorolysis of single-stranded polyribonucleotides processively CC in the 3'- to 5'-direction. {ECO:0000255|HAMAP-Rule:MF_01595}. CC -!- CATALYTIC ACTIVITY: RNA(n+1) + phosphate = RNA(n) + a nucleoside CC diphosphate. {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 CC nucleotidyltransferase family. {ECO:0000255|HAMAP-Rule:MF_01595}. CC -!- SIMILARITY: Contains 1 KH domain. {ECO:0000255|HAMAP- CC Rule:MF_01595}. CC -!- SIMILARITY: Contains 1 S1 motif domain. {ECO:0000255|HAMAP- CC 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; YP_001747599.1; NC_010501.1. DR ProteinModelPortal; B1J2B3; -. DR SMR; B1J2B3; 618-692. DR STRING; 390235.PputW619_0725; -. DR EnsemblBacteria; ACA71230; ACA71230; PputW619_0725. DR GeneID; 6109637; -. DR KEGG; ppw:PputW619_0725; -. DR PATRIC; 19951183; VBIPsePut93764_0730. DR eggNOG; COG1185; -. DR HOGENOM; HOG000218326; -. DR KO; K00962; -. DR OMA; RFMFHYN; -. DR OrthoDB; EOG6WT8CC; -. DR BioCyc; PPUT390235:GHHJ-730-MONOMER; -. DR Proteomes; UP000000720; Chromosome. 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; S1_dom. 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 Complete proteome; Cytoplasm; Magnesium; Metal-binding; KW Nucleotidyltransferase; RNA-binding; Transferase. FT CHAIN 1 701 Polyribonucleotide FT nucleotidyltransferase. FT /FTId=PRO_1000147947. FT DOMAIN 554 613 KH. {ECO:0000255|HAMAP-Rule:MF_01595}. FT DOMAIN 623 691 S1 motif. {ECO:0000255|HAMAP- FT Rule:MF_01595}. FT METAL 487 487 Magnesium. {ECO:0000255|HAMAP- FT Rule:MF_01595}. FT METAL 493 493 Magnesium. {ECO:0000255|HAMAP- FT 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 //