ID   PNP_BURCM               Reviewed;         714 AA.
AC   Q0BDC6;
DT   29-APR-2008, integrated into UniProtKB/Swiss-Prot.
DT   17-OCT-2006, sequence version 1.
DT   16-JUN-2009, entry version 18.
DE   RecName: Full=Polyribonucleotide nucleotidyltransferase;
DE            EC=2.7.7.8;
DE   AltName: Full=Polynucleotide phosphorylase;
DE            Short=PNPase;
GN   Name=pnp; OrderedLocusNames=Bamb_2291;
OS   Burkholderia ambifaria (strain ATCC BAA-244 / AMMD) (Burkholderia
OS   cepacia (strain AMMD)).
OC   Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC   Burkholderiaceae; Burkholderia; Burkholderia cepacia complex.
OX   NCBI_TaxID=339670;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA   Glavina del Rio T., Hammon N., Israni S., Pitluck S., Bruce D.,
RA   Chain P., Malfatti S., Shin M., Vergez L., Schmutz J., Larimer F.,
RA   Land M., Hauser L., Kyrpides N., Kim E., Parke J., Coenye T.,
RA   Konstantinidis K., Ramette A., Tiedje J., Richardson P.;
RT   "Complete sequence of chromosome 1 of Burkholderia cepacia AMMD.";
RL   Submitted (AUG-2006) to the EMBL/GenBank/DDBJ databases.
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.
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DR   EMBL; CP000440; ABI87847.1; -; Genomic_DNA.
DR   RefSeq; YP_774181.1; -.
DR   GeneID; 4309088; -.
DR   GenomeReviews; CP000440_GR; Bamb_2291.
DR   KEGG; bam:Bamb_2291; -.
DR   NMPDR; fig|339670.3.peg.5589; -.
DR   OMA; Q0BDC6; 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    714       Polyribonucleotide
FT                                nucleotidyltransferase.
FT                                /FTId=PRO_0000329553.
FT   DOMAIN      560    619       KH.
FT   DOMAIN      629    697       S1 motif.
SQ   SEQUENCE   714 AA;  77008 MW;  113B5BE21B149D57 CRC64;
     MSMFNKVVKE FQWGQHKVRL ETGEVARQAS GAVIVDVEDT VVLATVVGAK SAKPGQDFFP
     LTVDYLEKTY SAGKIPGGFF RREGRPSEHE TLTSRLIDRP LRPLFPEGFY NEVQVVIHVL
     SVNPEIPADI PALIGASAAL AVSGLPFNGP VGAARVAYID NAYVLNPTRD QLKASSLDLV
     VAGTERAVLM VESEADQLPE DVMLGAVVFG HEQMQTAIDA IHELVREGGK PEWDWQPAPK
     NEALIARVTE LAHGDLLAAY QLRDKQARST KLKEVYAATS AKLEEDAQAA GTVAADKATV
     GNVLFDIEAK IVRSQILNGE PRIDGRDTRT VRPIEIRTGV LPRTHGSALF TRGETQALVV
     ATLGTKGDEQ IIDALEGEYR ERFMLHYNMP PFATGETGRV GSPKRREIGH GRLAKRALVK
     CLPSADEFGY SIRVVSEITE SNGSSSMASV CGGCLALMDA GVPMKAHVAG IAMGLILEGN
     KFAVLTDILG DEDHLGDMDF KVAGTEQGVT ALQMDIKIQG ITKEIMQVAL AQAKEGRMHI
     LGKMTSAVSG ANTQLSEFAP RMITIKINPE KIRDVIGKGG SVIRALTEET GTTIDISDDG
     VVTIASTSSE GMAEAKKRIE NITVEIEVGQ VYEGTVLKLL DFGAIVNLLP GKDGLLHISE
     IVNERVKDIN DYLKEGQQVK VKVIQTDEKG RVRLSAKALL NEAAASQSDT PPQQ
//