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 01-MAY-2013, entry version 39.
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. 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; 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; YTMRVVS; -.
DR ProtClustDB; PRK11824; -.
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:0004654; F:polyribonucleotide nucleotidyltransferase activity; IEA:HAMAP.
DR GO; GO:0003723; F:RNA binding; IEA:HAMAP.
DR GO; GO:0006402; P:mRNA catabolic process; IEA: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 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; 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; 3_ExoRNase; 1.
DR SUPFAM; SSF55666; 3_ExoRNase; 2.
DR SUPFAM; SSF50249; Nucleic_acid_OB; 1.
DR SUPFAM; SSF54211; Ribosomal_S5_D2-typ_fold; 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; Nucleotidyltransferase; RNA-binding;
KW Transferase.
FT CHAIN 1 702 Polyribonucleotide
FT nucleotidyltransferase.
FT /FTId=PRO_1000192493.
FT DOMAIN 554 613 KH.
FT DOMAIN 623 691 S1 motif.
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
//
