ID   PNP_BUCCC               Reviewed;         693 AA.
AC   Q057K3;
DT   29-APR-2008, integrated into UniProtKB/Swiss-Prot.
DT   14-NOV-2006, sequence version 1.
DT   16-JUN-2009, entry version 17.
DE   RecName: Full=Polyribonucleotide nucleotidyltransferase;
DE            EC=2.7.7.8;
DE   AltName: Full=Polynucleotide phosphorylase;
DE            Short=PNPase;
GN   Name=pnp; OrderedLocusNames=BCc_227;
OS   Buchnera aphidicola subsp. Cinara cedri.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales;
OC   Enterobacteriaceae; Buchnera.
OX   NCBI_TaxID=372461;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=17038625; DOI=10.1126/science.1130441;
RA   Perez-Brocal V., Gil R., Ramos S., Lamelas A., Postigo M.,
RA   Michelena J.M., Silva F.J., Moya A., Latorre A.;
RT   "A small microbial genome: the end of a long symbiotic relationship?";
RL   Science 314:312-313(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; CP000263; ABJ90696.1; -; Genomic_DNA.
DR   RefSeq; YP_802789.1; -.
DR   GeneID; 4440802; -.
DR   GenomeReviews; CP000263_GR; BCc_227.
DR   KEGG; bcc:BCc_227; -.
DR   OMA; Q057K3; AFDEIRP.
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    693       Polyribonucleotide
FT                                nucleotidyltransferase.
FT                                /FTId=PRO_0000329550.
FT   DOMAIN      554    613       KH.
FT   DOMAIN      623    691       S1 motif.
SQ   SEQUENCE   693 AA;  77154 MW;  92B9BFD73C99FFC1 CRC64;
     MLKPIIHKFK YGKHNIILET GVIARQATAS VLASMDDTTV LITIVSDNTT IPGQKFFPLV
     VNYQERTYAA GRIPGGFFRR EGRPSENEIL ISRLIDRPIR PLFPKDFLYE VQIIATVISV
     NPQINPDIIS IIGSSAALCL SGLPFLGPIG AARIGFLNNK YILNPSIEKI KKSSLDLVVS
     GTKNTIFMVE AEASILSEDN ILNAILFGHE SQQSLIDNIY LFSDKANKIP NIYKNIYKPD
     KQIFNLISKK IKKDINKAYY ILKKKERLKK LNDIKQKVTS ELLNNDSQLT SSKIEESIYF
     LERNIVRKRI LKGKLRIDGR INNEVRKIDV RTGILPRVHG SALFTRGETQ ALVSATLGTS
     RDAQNLDDLL GDRTDNFLFH YNFPPYSVGE IGIVGSPKRR EIGHGKLAKR SFLAVMPNIE
     DFPYTIRLVS EITESNGSSS MASVCGASLA LMDAGVPIKS AIAGIAMGLI KENDSYIILS
     DILGDEDYLG DMDFKVSGSR LGITALQMDI KVSGITSDII RSALYQAKSA RLKILDIMEN
     TLQIPRSDIS KFAPRIYTIK INPEKIKDVI GKGGSIIRML TEETGTVIEI KDDGIVKISA
     INGEKAKYAI KRIQEITEDI QIGKIYSGKV TRILDFGAFV SIGFGKEGLI HISQISNKRI
     DKVINHLKIN QIIFVKVLEV DRQGRIRLSM KNI
//