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Database: UniProt
Entry: C0PZ50
LinkDB: C0PZ50
Original site: C0PZ50 
ID   PNP_SALPC               Reviewed;         711 AA.
AC   C0PZ50;
DT   01-SEP-2009, integrated into UniProtKB/Swiss-Prot.
DT   01-SEP-2009, sequence version 2.
DT   26-NOV-2014, entry version 42.
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=SPC_3353;
OS   Salmonella paratyphi C (strain RKS4594).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales;
OC   Enterobacteriaceae; Salmonella.
OX   NCBI_TaxID=476213;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=RKS4594;
RX   PubMed=19229335; DOI=10.1371/journal.pone.0004510;
RA   Liu W.-Q., Feng Y., Wang Y., Zou Q.-H., Chen F., Guo J.-T.,
RA   Peng Y.-H., Jin Y., Li Y.-G., Hu S.-N., Johnston R.N., Liu G.-R.,
RA   Liu S.-L.;
RT   "Salmonella paratyphi C: genetic divergence from Salmonella
RT   choleraesuis and pathogenic convergence with Salmonella typhi.";
RL   PLoS ONE 4:E4510-E4510(2009).
CC   -!- FUNCTION: Involved in mRNA degradation. Catalyzes the
CC       phosphorolysis of single-stranded polyribonucleotides processively
CC       in the 3'- to 5'-direction. {ECO:0000255|HAMAP-Rule:MF_01595}.
CC   -!- CATALYTIC ACTIVITY: RNA(n+1) + phosphate = RNA(n) + a nucleoside
CC       diphosphate. {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   -!- SUBUNIT: Component of the RNA degradosome, which is a multiprotein
CC       complex involved in RNA processing and mRNA degradation.
CC       {ECO:0000255|HAMAP-Rule:MF_01595}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_01595}.
CC   -!- SIMILARITY: Belongs to the polyribonucleotide
CC       nucleotidyltransferase family. {ECO:0000255|HAMAP-Rule:MF_01595}.
CC   -!- SIMILARITY: Contains 1 KH domain. {ECO:0000255|HAMAP-
CC       Rule:MF_01595}.
CC   -!- SIMILARITY: Contains 1 S1 motif domain. {ECO:0000255|HAMAP-
CC       Rule:MF_01595}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=ACN47438.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR   EMBL; CP000857; ACN47438.1; ALT_INIT; Genomic_DNA.
DR   RefSeq; YP_002638879.1; NC_012125.1.
DR   ProteinModelPortal; C0PZ50; -.
DR   SMR; C0PZ50; 617-692.
DR   STRING; 476213.SPC_3353; -.
DR   PRIDE; C0PZ50; -.
DR   EnsemblBacteria; ACN47438; ACN47438; SPC_3353.
DR   PATRIC; 32365640; VBISalEnt12305_3413.
DR   eggNOG; COG1185; -.
DR   HOGENOM; HOG000218326; -.
DR   OrthoDB; EOG6WT8CC; -.
DR   BioCyc; SENT476213:GH8J-3406-MONOMER; -.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-HAMAP.
DR   GO; GO:0000175; F:3'-5'-exoribonuclease activity; IEA:InterPro.
DR   GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP.
DR   GO; GO:0004654; F:polyribonucleotide nucleotidyltransferase activity; IEA:UniProtKB-HAMAP.
DR   GO; GO:0003723; F:RNA binding; IEA:UniProtKB-HAMAP.
DR   GO; GO:0006402; P:mRNA catabolic process; IEA:UniProtKB-HAMAP.
DR   GO; GO:0006396; P:RNA processing; IEA:InterPro.
DR   Gene3D; 1.10.10.400; -; 1.
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; IPR004087; KH_dom.
DR   InterPro; IPR004088; KH_dom_type_1.
DR   InterPro; IPR012340; NA-bd_OB-fold.
DR   InterPro; IPR012162; PNPase.
DR   InterPro; IPR027408; PNPase/RNase_PH_dom.
DR   InterPro; IPR015848; PNPase_PH_RNA-bd_bac/org-type.
DR   InterPro; IPR003029; Rbsml_prot_S1_RNA-bd_dom.
DR   InterPro; IPR020568; Ribosomal_S5_D2-typ_fold.
DR   InterPro; IPR022967; S1_dom.
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; 2.
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   Complete proteome; Cytoplasm; Magnesium; Metal-binding;
KW   Nucleotidyltransferase; RNA-binding; Transferase.
FT   CHAIN         1    711       Polyribonucleotide
FT                                nucleotidyltransferase.
FT                                /FTId=PRO_0000381917.
FT   DOMAIN      553    612       KH. {ECO:0000255|HAMAP-Rule:MF_01595}.
FT   DOMAIN      622    690       S1 motif. {ECO:0000255|HAMAP-
FT                                Rule:MF_01595}.
FT   METAL       486    486       Magnesium. {ECO:0000255|HAMAP-
FT                                Rule:MF_01595}.
FT   METAL       492    492       Magnesium. {ECO:0000255|HAMAP-
FT                                Rule:MF_01595}.
SQ   SEQUENCE   711 AA;  77039 MW;  BCF7F15FC536A017 CRC64;
     MLNPIVRKFQ YGQHTVTLET GMMARQATAA VMVSMDDTAV FVTVVGQKKA KPGQDFFPLT
     VNYQERTYAA GRIPGSFFRR EGRPSEGETL IARLIDRPVR PLFPEGFVNE VQVIATVVSV
     NPQVNPDIVA MIGASAALSL SGIPFNGPIG AARVGYINDQ YVLNPTQDEL KESKLDLVVA
     GTEAAVLMVE SEAELLSEDT MLGAVVFGHE QQQVVIQAIN DLVKEAGKPR WDWQPEAVND
     ALNARVAALA ESRLSDAYRI TDKQERYAQV DVIKSETIEQ LIAEDETLDA NELGEILHAI
     EKNVVRSRVL AGEPRIDGRE KDMIRGLDVR TGVLPRTHGS ALFTRGETQA LVTATLGTAR
     DAQVLDELMG ERTDSFLFHY NFPPYSVGET GMVGSPKRRE IGHGRLAKRG VLAVMPDMDK
     FPYTVRVVSE ITESNGSSSM ASVCGASLAL MDAGVPIKAA VAGIAMGLVK EGDNYVVLSD
     ILGDEDHLGD MDFKVAGSRD GISALQMDIK IEGITKEIMQ VALNQAKGAR LHILGVMEQA
     INAPRGDISE FAPRIHTIKI STDKIKDVIG KGGSVIRALT EETGTTIEIE DDGTVKIAAT
     DGEKAKYAIR RIEEITAEIE VGRIYNGKVT RIVDFGAFVA IGGGKEGLVH ISQIADKRVE
     KVTDYLQMGQ EVPVKVLEVD RQGRVRLSIK EATEQSQPAA APEAPASEQA E
//
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