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PNP_CLOBH
ID   PNP_CLOBH               Reviewed;         702 AA.
AC   A5I4I7; A7G5N8;
DT   29-APR-2008, integrated into UniProtKB/Swiss-Prot.
DT   26-JUN-2007, sequence version 1.
DT   03-AUG-2022, entry version 88.
DE   RecName: Full=Polyribonucleotide nucleotidyltransferase {ECO:0000255|HAMAP-Rule:MF_01595};
DE            EC=2.7.7.8 {ECO:0000255|HAMAP-Rule:MF_01595};
DE   AltName: Full=Polynucleotide phosphorylase {ECO:0000255|HAMAP-Rule:MF_01595};
DE            Short=PNPase {ECO:0000255|HAMAP-Rule:MF_01595};
GN   Name=pnp {ECO:0000255|HAMAP-Rule:MF_01595};
GN   OrderedLocusNames=CBO2413, CLC_2259;
OS   Clostridium botulinum (strain Hall / ATCC 3502 / NCTC 13319 / Type A).
OC   Bacteria; Firmicutes; Clostridia; Eubacteriales; Clostridiaceae;
OC   Clostridium.
OX   NCBI_TaxID=441771;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Hall / ATCC 3502 / NCTC 13319 / Type A;
RX   PubMed=17519437; DOI=10.1101/gr.6282807;
RA   Sebaihia M., Peck M.W., Minton N.P., Thomson N.R., Holden M.T.G.,
RA   Mitchell W.J., Carter A.T., Bentley S.D., Mason D.R., Crossman L.,
RA   Paul C.J., Ivens A., Wells-Bennik M.H.J., Davis I.J., Cerdeno-Tarraga A.M.,
RA   Churcher C., Quail M.A., Chillingworth T., Feltwell T., Fraser A.,
RA   Goodhead I., Hance Z., Jagels K., Larke N., Maddison M., Moule S.,
RA   Mungall K., Norbertczak H., Rabbinowitsch E., Sanders M., Simmonds M.,
RA   White B., Whithead S., Parkhill J.;
RT   "Genome sequence of a proteolytic (Group I) Clostridium botulinum strain
RT   Hall A and comparative analysis of the clostridial genomes.";
RL   Genome Res. 17:1082-1092(2007).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Hall / ATCC 3502 / NCTC 13319 / Type A;
RX   PubMed=18060065; DOI=10.1371/journal.pone.0001271;
RA   Smith T.J., Hill K.K., Foley B.T., Detter J.C., Munk A.C., Bruce D.C.,
RA   Doggett N.A., Smith L.A., Marks J.D., Xie G., Brettin T.S.;
RT   "Analysis of the neurotoxin complex genes in Clostridium botulinum A1-A4
RT   and B1 strains: BoNT/A3, /Ba4 and /B1 clusters are located within
RT   plasmids.";
RL   PLoS ONE 2:E1271-E1271(2007).
CC   -!- FUNCTION: Involved in mRNA degradation. Catalyzes the phosphorolysis of
CC       single-stranded polyribonucleotides processively in the 3'- to 5'-
CC       direction. {ECO:0000255|HAMAP-Rule:MF_01595}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=phosphate + RNA(n+1) = a ribonucleoside 5'-diphosphate +
CC         RNA(n); Xref=Rhea:RHEA:22096, Rhea:RHEA-COMP:14527, Rhea:RHEA-
CC         COMP:17342, ChEBI:CHEBI:43474, ChEBI:CHEBI:57930, ChEBI:CHEBI:140395;
CC         EC=2.7.7.8; Evidence={ECO:0000255|HAMAP-Rule:MF_01595};
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_01595};
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_01595}.
CC   -!- SIMILARITY: Belongs to the polyribonucleotide nucleotidyltransferase
CC       family. {ECO:0000255|HAMAP-Rule:MF_01595}.
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DR   EMBL; CP000727; ABS36368.1; -; Genomic_DNA.
DR   EMBL; AM412317; CAL83959.1; -; Genomic_DNA.
DR   RefSeq; WP_011986787.1; NC_009698.1.
DR   RefSeq; YP_001254908.1; NC_009495.1.
DR   RefSeq; YP_001388103.1; NC_009698.1.
DR   AlphaFoldDB; A5I4I7; -.
DR   SMR; A5I4I7; -.
DR   GeneID; 5186668; -.
DR   KEGG; cbh:CLC_2259; -.
DR   KEGG; cbo:CBO2413; -.
DR   PATRIC; fig|413999.7.peg.2389; -.
DR   HOGENOM; CLU_004217_2_2_9; -.
DR   OMA; LHILDVM; -.
DR   PRO; PR:A5I4I7; -.
DR   Proteomes; UP000001986; Chromosome.
DR   GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR   GO; GO:0000175; F:3'-5'-exoribonuclease activity; IBA:GO_Central.
DR   GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0004654; F:polyribonucleotide nucleotidyltransferase activity; IBA:GO_Central.
DR   GO; GO:0003723; F:RNA binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0006402; P:mRNA catabolic process; IEA:UniProtKB-UniRule.
DR   GO; GO:0006401; P:RNA catabolic process; IBA:GO_Central.
DR   GO; GO:0006396; P:RNA processing; IEA:InterPro.
DR   Gene3D; 2.40.50.140; -; 1.
DR   Gene3D; 3.30.1370.10; -; 1.
DR   Gene3D; 3.30.230.70; -; 2.
DR   HAMAP; MF_01595; PNPase; 1.
DR   InterPro; IPR001247; ExoRNase_PH_dom1.
DR   InterPro; IPR015847; ExoRNase_PH_dom2.
DR   InterPro; IPR036345; ExoRNase_PH_dom2_sf.
DR   InterPro; IPR004087; KH_dom.
DR   InterPro; IPR004088; KH_dom_type_1.
DR   InterPro; IPR036612; KH_dom_type_1_sf.
DR   InterPro; IPR012340; NA-bd_OB-fold.
DR   InterPro; IPR012162; PNPase.
DR   InterPro; IPR027408; PNPase/RNase_PH_dom_sf.
DR   InterPro; IPR015848; PNPase_PH_RNA-bd_bac/org-type.
DR   InterPro; IPR036456; PNPase_PH_RNA-bd_sf.
DR   InterPro; IPR020568; Ribosomal_S5_D2-typ_fold.
DR   InterPro; IPR022967; S1_dom.
DR   InterPro; IPR003029; S1_domain.
DR   PANTHER; PTHR11252; PTHR11252; 1.
DR   Pfam; PF00013; KH_1; 1.
DR   Pfam; PF03726; PNPase; 1.
DR   Pfam; PF01138; RNase_PH; 2.
DR   Pfam; PF03725; RNase_PH_C; 1.
DR   Pfam; PF00575; S1; 1.
DR   PIRSF; PIRSF005499; PNPase; 1.
DR   SMART; SM00322; KH; 1.
DR   SMART; SM00316; S1; 1.
DR   SUPFAM; SSF46915; SSF46915; 1.
DR   SUPFAM; SSF50249; SSF50249; 1.
DR   SUPFAM; SSF54211; SSF54211; 2.
DR   SUPFAM; SSF54791; SSF54791; 1.
DR   SUPFAM; SSF55666; SSF55666; 2.
DR   TIGRFAMs; TIGR03591; polynuc_phos; 1.
DR   PROSITE; PS50084; KH_TYPE_1; 1.
DR   PROSITE; PS50126; S1; 1.
PE   3: Inferred from homology;
KW   Cytoplasm; Magnesium; Metal-binding; Nucleotidyltransferase;
KW   Reference proteome; RNA-binding; Transferase.
FT   CHAIN           1..702
FT                   /note="Polyribonucleotide nucleotidyltransferase"
FT                   /id="PRO_0000329596"
FT   DOMAIN          552..612
FT                   /note="KH"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01595"
FT   DOMAIN          622..690
FT                   /note="S1 motif"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01595"
FT   BINDING         485
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01595"
FT   BINDING         491
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01595"
SQ   SEQUENCE   702 AA;  77454 MW;  70A40D92A1091252 CRC64;
     MIHTLETTVA GRKMKVDFGK TGMLSNAAIF MSYGDTVVMI NANASKEPRE GIDFFPLSVE
     YEERLYSVGK IPGGFIKREG KPSDKSILHA RSIDRPLRPL FPKGYRNDVQ IVNTVLSVEQ
     DNLPEILAIN GSSLALCLSS IPFTTPVAAV SVGLVDGEFI INPTVAQREN TILDLTVCAT
     KERVMMVEAG GQEIDEETMY SAIMFGFEEC KNIVAFQEEA VAKFGKTKNE PVLYKADEEV
     EKEVKSFAFD MIKEAMYIMD KDERNAQLDK VKEKISEEFS EKYEDKVADI AEVIYKTQKE
     IVRNMLLNED RRPDGRAFDE VRPISCEVGI LPRTHGTGLF TRGLTQVMTV ATLGALGDVQ
     ILDGIAEEES KRYMHHYNFP SYSVGEVRPL RGPGRREIGH GALAERALEP LIPSQSEFPY
     TIRLVSEVLS SNGSTSQASV CGSTLALLDA GVPIKRPAAG IAMGLITSED LEKEKVITDI
     QGIEDFFGDM DFKVAGTEKG ITSIQFDTKI KGLSNSCVKD ALEGAKKARL HILGKIKECI
     PEPRKELSKY APRTEIICID PEKIRDVIGA GGKVINKIIA DTNVKIEIKE DGKIFVTSNN
     EPEGVKKAIS IIEGLTKEVV QGEIYLGKVT KTTNFGAFVE ILPGKEGLVH ISKLDFARVE
     KVEDVVSVGD EILVKVTDID NQGRINLSRK DAIAKKEEEK DK
 
 
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