ID   PNP_AYWBP               Reviewed;         715 AA.
AC   Q2NJ06;
DT   29-APR-2008, integrated into UniProtKB/Swiss-Prot.
DT   07-FEB-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=AYWB_470;
OS   Aster yellows witches'-broom phytoplasma (strain AYWB).
OC   Bacteria; Tenericutes; Mollicutes; Acholeplasmatales;
OC   Acholeplasmataceae; Candidatus Phytoplasma;
OC   Candidatus Phytoplasma asteris.
OX   NCBI_TaxID=322098;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=16672622; DOI=10.1128/JB.188.10.3682-3696.2006;
RA   Bai X., Zhang J., Ewing A., Miller S.A., Jancso Radek A.,
RA   Shevchenko D.V., Tsukerman K., Walunas T., Lapidus A., Campbell J.W.,
RA   Hogenhout S.A.;
RT   "Living with genome instability: the adaptation of phytoplasmas to
RT   diverse environments of their insect and plant hosts.";
RL   J. Bacteriol. 188:3682-3696(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; CP000061; ABC65587.1; -; Genomic_DNA.
DR   RefSeq; YP_456666.1; -.
DR   GeneID; 3865843; -.
DR   GenomeReviews; CP000061_GR; AYWB_470.
DR   KEGG; ayw:AYWB_470; -.
DR   HOGENOM; Q2NJ06; -.
DR   OMA; Q2NJ06; 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   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   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    715       Polyribonucleotide
FT                                nucleotidyltransferase.
FT                                /FTId=PRO_0000329506.
FT   DOMAIN      565    625       KH.
FT   DOMAIN      635    709       S1 motif.
SQ   SEQUENCE   715 AA;  80440 MW;  462807B60999C430 CRC64;
     MLKKVFETTN LKDSFQVEIG TYARNVDSSI LVRYQDTVVL TTMVFSRKPN NLDFLPLTVI
     YQEKLYAAGK IPGSFLRREG RSNDHEILTS RLIDRSLRPL FPDYFQQEVQ VINTVLSLDP
     DFKSELASML GSSLSLLISE IPFFEAISGV YVGKINNEFI INPTLQQLAN STLHLIVAGT
     KHNVTMIEAH ANEVSEQDFL EAINFAHQYI KKLCLFQENI KQQFAPVKMT KTLHQTEQIQ
     QQSFFAKNHS QVKQAILSCN SKNDLQQLKE QILDQAKQTP FFKTIDAITV FDYEAHKKHL
     QITENLFQKL SKQEMRSLIL QEKIRPDKRE LEEIRTLESQ IDLLPRAHGS ALFTRGKTQS
     LAAVTLGCLS ESKIIDGLSD EQNKRFMLHY NFPPFSVGAV GRYTAPSRRE IGHGTLAEKA
     ISQVLPEEKD FPYTIRVVSE ILESNGSSSQ ATVCSSSLAL MASGVPLKKA VAGISVGLVF
     DQETNKYVIL SDIQGLEDHV GDMDLKIAGT NKGITALQMD LKIQGIPFKI LQEAFLQAKK
     GRLHILEQMN QTISQPRLEV SKYAPKVCMM QIKPEKIRDI IGSGGKIINQ IIESHDGVKI
     DIEQDGRVFV MHSNLETVKK TVAFIESLIQ EIQVGTCYQA SILRFLSDKQ GKMIGAVAQV
     CPGIEGLIHV NKMKFQKITD VLKIGETVLV KCTKINERGR IDFLLLPKKT QEKNS
//