ID   PNP_BORAP               Reviewed;         722 AA.
AC   Q0SM46;
DT   29-APR-2008, integrated into UniProtKB/Swiss-Prot.
DT   05-SEP-2006, sequence version 1.
DT   16-JUN-2009, entry version 22.
DE   RecName: Full=Polyribonucleotide nucleotidyltransferase;
DE            EC=2.7.7.8;
DE   AltName: Full=Polynucleotide phosphorylase;
DE            Short=PNPase;
GN   Name=pnp; OrderedLocusNames=BAPKO_0858;
OS   Borrelia afzelii (strain PKo).
OC   Bacteria; Spirochaetes; Spirochaetales; Spirochaetaceae; Borrelia;
OC   Borrelia burgdorferi group.
OX   NCBI_TaxID=390236;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=16914037; DOI=10.1186/1471-2164-7-211;
RA   Gloeckner G., Schulte-Spechtel U., Schilhabel M., Felder M.,
RA   Suehnel J., Wilske B., Platzer M.;
RT   "Comparative genome analysis: selection pressure on the Borrelia vls
RT   cassettes is essential for infectivity.";
RL   BMC Genomics 7:211-211(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; CP000395; ABH02082.1; -; Genomic_DNA.
DR   RefSeq; YP_710258.1; -.
DR   GeneID; 4227019; -.
DR   GenomeReviews; CP000395_GR; BAPKO_0858.
DR   KEGG; baf:BAPKO_0858; -.
DR   NMPDR; fig|390236.5.peg.860; -.
DR   HOGENOM; Q0SM46; -.
DR   OMA; Q0SM46; GHGNLAK.
DR   BioCyc; BAFZ390236:BAPKO_0858-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    722       Polyribonucleotide
FT                                nucleotidyltransferase.
FT                                /FTId=PRO_0000329539.
FT   DOMAIN      553    612       KH.
FT   DOMAIN      622    717       S1 motif.
SQ   SEQUENCE   722 AA;  80376 MW;  9BCAB9C88DC5E0FB CRC64;
     MRKILKLKIG RDELVFETGF MAKQANGSVL ATYGGSSVLA TVCCSNNVRE DLDFVPLSVE
     YNEKYYAAGK IPGGFIKREG KPKDKEILVS RLIDRPMRPL FDKRFGREIQ VIPTTLATDQ
     LNPPDIVGMN AAFTAVFLSD IPFNGPIAAV RMVYLNGKFI VNPSFEEIHD SDLDIVVAGS
     LNGITMVEGG ANEVSEDILL SAIDSAHEYI KQICNAQKEF LDIVGEKEKL PLAFEEKIFE
     FKEELRDFIY ADLKEACFVK GKLNRDKAIT LLRNKSYEHF SSLEKLDDSN ESLFYKAFDD
     FEKEIVRNSI LNDKIRTDGR TPNEIRDILA EVDILSRTHG SSLFTRGETQ ALAVTTLGTS
     IDEQIMDDID GDKRLNFMLH YNFPPFSVGE TGRLMTGRRE IGHGHLAQRA LESMIPGKND
     FPYTIRVVSE ILESNGSSSM ATVCAGSMSL MSAGVPVKRQ VAGIAMGLIS EGDKYVVLSD
     ILGEEDHLGD MDFKVAGTEN GITGFQMDIK IENVTKQLMR DALEQARVGR IHILSIMNSV
     ISNSRVGISK YAPKIIQLQI DIDKISLVIG STGKTVKAIT DEFEVKVQIE QNGKIILFGD
     DDFKMQKAKE KIESIVREPK VGEIYEGTVK KINSFGAFIE LTPTKEGFLS TRLKSRDSKY
     GSGRFGHGNR YSRFGSGGDN IRGNAGLVRP PKLEEGQRIK VRIVDIDKFG KIDLEIVRDK
     DY
//