ID   PNP_BORA1               Reviewed;         718 AA.
AC   Q2KWI6;
DT   29-APR-2008, integrated into UniProtKB/Swiss-Prot.
DT   07-MAR-2006, sequence version 1.
DT   16-JUN-2009, entry version 23.
DE   RecName: Full=Polyribonucleotide nucleotidyltransferase;
DE            EC=2.7.7.8;
DE   AltName: Full=Polynucleotide phosphorylase;
DE            Short=PNPase;
GN   Name=pnp; OrderedLocusNames=BAV2667;
OS   Bordetella avium (strain 197N).
OC   Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC   Alcaligenaceae; Bordetella.
OX   NCBI_TaxID=360910;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=16885469; DOI=10.1128/JB.01927-05;
RA   Sebaihia M., Preston A., Maskell D.J., Kuzmiak H., Connell T.D.,
RA   King N.D., Orndorff P.E., Miyamoto D.M., Thomson N.R., Harris D.,
RA   Goble A., Lord A., Murphy L., Quail M.A., Rutter S., Squares R.,
RA   Squares S., Woodward J., Parkhill J., Temple L.M.;
RT   "Comparison of the genome sequence of the poultry pathogen Bordetella
RT   avium with those of B. bronchiseptica, B. pertussis, and B.
RT   parapertussis reveals extensive diversity in surface structures
RT   associated with host interaction.";
RL   J. Bacteriol. 188:6002-6015(2006).
CC   -!- FUNCTION: Involved in mRNA degradation. Hydrolyzes single-stranded
CC       polyribonucleotides processively in the 3'- to 5'-direction (By
CC       similarity).
CC   -!- CATALYTIC ACTIVITY: RNA(n+1) + phosphate = RNA(n) + a nucleoside
CC       diphosphate.
CC   -!- SUBUNIT: Homotrimer. Organized into a structure (processome or RNA
CC       degradosome) containing a number of RNA-processing enzymes (By
CC       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 http://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; AM167904; CAJ50278.1; -; Genomic_DNA.
DR   RefSeq; YP_787166.1; -.
DR   GeneID; 6266139; -.
DR   GenomeReviews; AM167904_GR; BAV2667.
DR   KEGG; bav:BAV2667; -.
DR   NMPDR; fig|521.1.peg.291; -.
DR   HOGENOM; Q2KWI6; -.
DR   OMA; Q2KWI6; GHGNLAK.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0000175; F:3'-5'-exoribonuclease activity; IEA:InterPro.
DR   GO; GO:0004654; F:polyribonucleotide nucleotidyltransferase a...; IEA:HAMAP.
DR   GO; GO:0003723; F:RNA binding; IEA:UniProtKB-KW.
DR   GO; GO:0006402; P:mRNA catabolic process; IEA:HAMAP.
DR   GO; GO:0006396; P:RNA processing; IEA:InterPro.
DR   HAMAP; MF_01595; -; 1.
DR   InterPro; IPR001247; ExoRNase_PH_dom1.
DR   InterPro; IPR015847; ExoRNase_PH_dom2.
DR   InterPro; IPR004087; KH.
DR   InterPro; IPR004088; KH_type_1.
DR   InterPro; IPR018111; KH_type_1_subgr.
DR   InterPro; IPR012340; NA-bd_OB-fold.
DR   InterPro; IPR012162; PNPase.
DR   InterPro; IPR015848; PNPase_PH_RNA-bd_bac/org-type.
DR   InterPro; IPR003029; Rbsml_prot_S1_RNA-bd_dom.
DR   Gene3D; G3DSA:2.40.50.140; OB_NA_bd_sub; 1.
DR   Gene3D; G3DSA:1.10.10.400; PNPase_PH_RNA-bd_bac/org-type; 1.
DR   PANTHER; PTHR11252; PNPase; 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   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; Nucleotidyltransferase; RNA-binding;
KW   Transferase.
FT   CHAIN         1    718       Polyribonucleotide
FT                                nucleotidyltransferase.
FT                                /FTId=PRO_0000329535.
FT   DOMAIN      558    617       KH.
FT   DOMAIN      627    695       S1 motif.
SQ   SEQUENCE   718 AA;  77312 MW;  01E0C1EF0D565AC3 CRC64;
     MFNKVTKTFQ YGQHTVVLET GEIARQASGA VLVSVEDTVV LATVVAAKKA KPGQDFFPLT
     VDYIEKTYAA GRIPGGFFKR EGKPSEKETL TSRLIDRPLR PLFPEGFYNE VQVVIHTLSV
     NPEIDPDIPA MIGASAALAI SGIPFNGPIG AARVAYVEGQ YLLNPTASQL KSSKMDLVVA
     GTENAVLMVE SEAQQLSEEI MLGGVVFGHE QMQAAINAIH DLVRDAGKPE WTWSPAAKNE
     ALIAAVTAAA QEGLSAAYQI REKQARTTKL REVYAEVSAK LAEQAAAAGQ DAPDGVTVDN
     ILFDLEARLV RSQILNGEPR IDGRDTRTVR PISVRLGVLP RAHGSALFTR GETQALVVAT
     LGTKQDEQII DALMGEYRDR FMLHYNMPPF ATGETGRIGV PKRREIGHGR LAKRSLVPVL
     PKPEDFQYTI RIVSEITESN GSSSMASVCG GSLAMMDAGV PITDHVAGVA MGLILENGKF
     AVLTDILGDE DHLGDMDFKV AGTENGITAL QMDIKIQGIT KEIMQVALAQ AREGRLHILG
     KMRESLDGSR TELSAFAPRM LTIKINPEKI RDVIGKGGAT IRALTEETGT QIDISDDGTI
     VIASVDEGQA KEAQRRIVEL TADVEVGQVY DGSVLRLLDF GAIVQVLPGR DGLLHISEIA
     NYRIANINDV LKVGQQVRVK VIEADEKGRL RLSVKAIGGI EQQQAAADVP AQAETPAE
//