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Database: UniProt
Entry: B2FN86
LinkDB: B2FN86
Original site: B2FN86 
ID   PNP_STRMK               Reviewed;         702 AA.
AC   B2FN86;
DT   14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT   10-JUN-2008, sequence version 1.
DT   14-MAY-2014, entry version 46.
DE   RecName: Full=Polyribonucleotide nucleotidyltransferase;
DE            EC=2.7.7.8;
DE   AltName: Full=Polynucleotide phosphorylase;
DE            Short=PNPase;
GN   Name=pnp; OrderedLocusNames=Smlt3385;
OS   Stenotrophomonas maltophilia (strain K279a).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Xanthomonadales;
OC   Xanthomonadaceae; Stenotrophomonas;
OC   Stenotrophomonas maltophilia group.
OX   NCBI_TaxID=522373;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=K279a;
RX   PubMed=18419807; DOI=10.1186/gb-2008-9-4-r74;
RA   Crossman L.C., Gould V.C., Dow J.M., Vernikos G.S., Okazaki A.,
RA   Sebaihia M., Saunders D., Arrowsmith C., Carver T., Peters N.,
RA   Adlem E., Kerhornou A., Lord A., Murphy L., Seeger K., Squares R.,
RA   Rutter S., Quail M.A., Rajandream M.A., Harris D., Churcher C.,
RA   Bentley S.D., Parkhill J., Thomson N.R., Avison M.B.;
RT   "The complete genome, comparative and functional analysis of
RT   Stenotrophomonas maltophilia reveals an organism heavily shielded by
RT   drug resistance determinants.";
RL   Genome Biol. 9:R74.1-R74.13(2008).
CC   -!- FUNCTION: Involved in mRNA degradation. Catalyzes the
CC       phosphorolysis of single-stranded polyribonucleotides processively
CC       in the 3'- to 5'-direction (By similarity).
CC   -!- CATALYTIC ACTIVITY: RNA(n+1) + phosphate = RNA(n) + a nucleoside
CC       diphosphate.
CC   -!- COFACTOR: Magnesium (By similarity).
CC   -!- SUBUNIT: Component of the RNA degradosome, which is a multiprotein
CC       complex involved in RNA processing and mRNA degradation (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; AM743169; CAQ46813.1; -; Genomic_DNA.
DR   RefSeq; YP_001973103.1; NC_010943.1.
DR   STRING; 522373.Smlt3385; -.
DR   EnsemblBacteria; CAQ46813; CAQ46813; Smlt3385.
DR   GeneID; 6393877; -.
DR   KEGG; sml:Smlt3385; -.
DR   PATRIC; 23702235; VBISteMal45202_3174.
DR   eggNOG; COG1185; -.
DR   HOGENOM; HOG000218326; -.
DR   KO; K00962; -.
DR   OMA; PRWDWVA; -.
DR   OrthoDB; EOG6WT8CC; -.
DR   BioCyc; SMAL522373:GJE8-3273-MONOMER; -.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
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; RNA-binding_domain_S1.
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    702       Polyribonucleotide
FT                                nucleotidyltransferase.
FT                                /FTId=PRO_1000192493.
FT   DOMAIN      554    613       KH.
FT   DOMAIN      623    691       S1 motif.
FT   METAL       487    487       Magnesium (By similarity).
FT   METAL       493    493       Magnesium (By similarity).
SQ   SEQUENCE   702 AA;  75382 MW;  900DCDD5244C0603 CRC64;
     MAKITKTFQY GKHTVTLETG EVARQASGAV IVKMDDTVLL VTAVAAKSAR EGQDFFPLTV
     DYQEKFYAGG RIPGGFFKRE GRATEKETLI SRLIDRPIRP LFPEDYKNDV QIIATVMSLN
     PDVDGDIPAL IGASAALALA GTPFMGPIGA AKVGYKNGEY ILNPTVSELA DSQLELVVAG
     TSNAVLMVES EAALLSEEVM LGAVTFGHRE MQKVINAINE LTVEAGTKPS TWEAPAKNDA
     LISALKEAIG PRLGEAFQVR DKLQRRDAIS AIKKDVFETL AGRVAAEGWN PAELSKEFGE
     LEYRTMRDSV LDTKVRIDGR ALDTVRPIAV KTGVLPRTHG SSLFTRGETQ AIVTITLGTA
     RDGQVIDAVA GEYKENFLFH YNFPPFSVGE CGRMMGPKRR EIGHGRLAKR GVLAVMPSLE
     AFPYTIRVVS EITESNGSSS MASVCGSSLA LMDAGVPVKA PVAGIAMGLV KEGERFVVLS
     DILGDEDHLG DMDFKVAGTA EGISALQMDI KIEGITEEIM KQALQQAKAG RLHILGEMAH
     GLTAPREELS DYAPRLLTIK IHPDKIREVI GKGGSTIQAI TKETGTQIDI QDDGTIVIAS
     VNAIAAQAAK ARIEQITSDV EPGRIYEGKV AKIMDFGAFV TILPGKDGLV HVSQISSDRV
     EKVGDVLKEG DVVKVKVLEV DKQGRIRLSM KAVEEGDAAS AE
//
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