ID   PNP_BAUCH               Reviewed;         697 AA.
AC   Q1LSL2;
DT   29-APR-2008, integrated into UniProtKB/Swiss-Prot.
DT   30-MAY-2006, sequence version 1.
DT   16-JUN-2009, entry version 24.
DE   RecName: Full=Polyribonucleotide nucleotidyltransferase;
DE            EC=2.7.7.8;
DE   AltName: Full=Polynucleotide phosphorylase;
DE            Short=PNPase;
GN   Name=pnp; OrderedLocusNames=BCI_0627;
OS   Baumannia cicadellinicola subsp. Homalodisca coagulata.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Candidatus Baumannia.
OX   NCBI_TaxID=374463;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=16729848; DOI=10.1371/journal.pbio.0040188;
RA   Wu D., Daugherty S.C., Van Aken S.E., Pai G.H., Watkins K.L.,
RA   Khouri H., Tallon L.J., Zaborsky J.M., Dunbar H.E., Tran P.L.,
RA   Moran N.A., Eisen J.A.;
RT   "Metabolic complementarity and genomics of the dual bacterial
RT   symbiosis of sharpshooters.";
RL   PLoS Biol. 4:1079-1092(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.
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DR   EMBL; CP000238; ABF13852.1; -; Genomic_DNA.
DR   RefSeq; YP_589052.1; -.
DR   SMR; Q1LSL2; 617-691.
DR   GeneID; 4056300; -.
DR   GenomeReviews; CP000238_GR; BCI_0627.
DR   KEGG; bci:BCI_0627; -.
DR   HOGENOM; Q1LSL2; -.
DR   OMA; Q1LSL2; 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    697       Polyribonucleotide
FT                                nucleotidyltransferase.
FT                                /FTId=PRO_0000329529.
FT   DOMAIN      553    612       KH.
FT   DOMAIN      622    690       S1 motif.
SQ   SEQUENCE   697 AA;  76711 MW;  7420BCBEF594D25F CRC64;
     MLNPIVHRFQ YGKHIVILET GIVARQATAA VMVNMADTIV LVTVVGVKQV KPGQKFFPLM
     VNYQERTYAA GRFPGGFFRR EGRPSEGEIL ISRMIDRPLR PLFPDGFLNE VQVIATVVSI
     NPQVSPDIVA MIGVSAALSI SGIPFNCPFG AARVGYINNQ YVLNPTIAEL VDSSLDLVVA
     STANAVLMVE SEAKQLSEEQ MLSAIIFGHE QQQLVIQNIN HMVTIVGKPK WSWQAQVIDT
     NLQLCVTELA ESRLNEAFCI SDKQERDVCI ETIKSDVLSA LQQKNETIEE ETISNIFANL
     EKQIARNRIL GGKLRIDGRN HKMIRSLDMR TSILPRTHGS ALFVRGETQA LVTVTLGTER
     NAQNIDELIG ERTDRFLLHY NFPPYCVGEI GLVGSPKRRE IGHGRLAKRG ILAVMPTANE
     FPYTVRVVSE ITESNGSSSM ASVCGTSLAL MDAGVPIKAA VAGVAMGLIK EDNNFVILSD
     ILSNEDYIGD MDFKVAGSKN GITALQMDIK TKGITNNIIQ LALNQAKDAR MHILNMMEQV
     ISMSRTDISP FAPRIHTIKI HPDKIKDVIG KCGSVIRALT EETKTIIDIE DDGTVTVAAT
     DSIKAQQAIC RIKDITAEIE VGSIYHGKVT RIVDFGAFIA ISSNKEGLVH ISQITNKRVE
     KVADYLSIDQ IVLVKVLEVD RQGRIRLSMK DTNLTNK
//