ID   PNP_BLOPB               Reviewed;         699 AA.
AC   Q493T3;
DT   29-APR-2008, integrated into UniProtKB/Swiss-Prot.
DT   13-SEP-2005, sequence version 1.
DT   16-JUN-2009, entry version 25.
DE   RecName: Full=Polyribonucleotide nucleotidyltransferase;
DE            EC=2.7.7.8;
DE   AltName: Full=Polynucleotide phosphorylase;
DE            Short=PNPase;
GN   Name=pnp; OrderedLocusNames=BPEN_112;
OS   Blochmannia pennsylvanicus (strain BPEN).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales;
OC   Enterobacteriaceae; ant endosymbionts; Candidatus Blochmannia.
OX   NCBI_TaxID=291272;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=16077009; DOI=10.1101/gr.3771305;
RA   Degnan P.H., Lazarus A.B., Wernegreen J.J.;
RT   "Genome sequence of Blochmannia pennsylvanicus indicates parallel
RT   evolutionary trends among bacterial mutualists of insects.";
RL   Genome Res. 15:1023-1033(2005).
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; CP000016; AAZ40752.1; -; Genomic_DNA.
DR   RefSeq; YP_277625.1; -.
DR   SMR; Q493T3; 619-692.
DR   GeneID; 3563170; -.
DR   GenomeReviews; CP000016_GR; BPEN_112.
DR   KEGG; bpn:BPEN_112; -.
DR   HOGENOM; Q493T3; -.
DR   OMA; Q493T3; GHGNLAK.
DR   BioCyc; CBLO291272:BPEN_112-MON; -.
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    699       Polyribonucleotide
FT                                nucleotidyltransferase.
FT                                /FTId=PRO_0000329534.
FT   DOMAIN      555    614       KH.
FT   DOMAIN      624    692       S1 motif.
SQ   SEQUENCE   699 AA;  77476 MW;  4914F2EB0F17C4B9 CRC64;
     MLDPIIHKFK YGQHTVILDI GTIARQANAA VMVSMSDTTV LVTVVSSNQV RLEQDFFPLV
     VNYQERTYAA GKFPGGFFRR EGRPSENETL TSRLIDRPIR PLFPKGFIND VQVVATVVSV
     NPQVNPDIVA IIGVSAALSL SDIPFFGPIG AARVGYIKNQ YVLNPTTTEL SNSKLDLVIS
     GTESNILMVE SESCLLSEKE ILDAIIFGHE QQQIVIHNIN KLVKKVGKTK YSWNEKEVNI
     SLKTYLSELY ESRAQDIYCF FDKKERHAQV DSIKKDIVKT VLNSYQHAAV DEKEIMYLLN
     YLEAQSIRYR ILTNKLRIDG RSQDTIRKID IKTGILPRTH GSALFTRGDT QALVAVTLGT
     ERDAQNIDGL TGIRVDRFLL HYNFPPYCVG EIGVIGAPKR REIGHGRLAK RGMLAVMPNA
     NEFPYTIRVV SEITESNGSS SMASICGTSL ALMDAGVPIK AAVAGVAMGL IKEGNDFVVL
     SDIVSDEDHI GDMDFKVSGS RQGITALQMD IKTDGITYDI INIALKKAKN ARLQILDVME
     QIIKFPNQEI SKFAPRIYSI KVNPDKIKDV IGKGGSVIRS LTEETNTIID IEDNGIIKIV
     ALDYDKAKQA IRRINDITAN VEIGAVYTGK VSHIVEFGAF VTILSGKEGL VHISQISERR
     INKVTDYLKL GQKVLVKVLE IDRQGRIRLS MKGVHQVSA
//