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   08-MAY-2019, entry version 70.
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:
CC       Reaction=phosphate + RNA(n+1) = a ribonucleoside 5'-diphosphate +
CC         RNA(n); Xref=Rhea:RHEA:22096, Rhea:RHEA-COMP:11128, Rhea:RHEA-
CC         COMP:11129, ChEBI:CHEBI:43474, ChEBI:CHEBI:57930,
CC         ChEBI:CHEBI:83400; EC=2.7.7.8; Evidence={ECO:0000255|HAMAP-
CC         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}.
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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; ENOG4105C62; Bacteria.
DR   eggNOG; COG1185; LUCA.
DR   HOGENOM; HOG000218326; -.
DR   KO; K00962; -.
DR   OMA; RYMHNYN; -.
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   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
//