ID PNP_BRUSI Reviewed; 714 AA. AC B0CK15; DT 20-MAY-2008, integrated into UniProtKB/Swiss-Prot. DT 26-FEB-2008, sequence version 1. DT 16-JUN-2009, entry version 11. DE RecName: Full=Polyribonucleotide nucleotidyltransferase; DE EC=2.7.7.8; DE AltName: Full=Polynucleotide phosphorylase; DE Short=PNPase; GN Name=pnp; OrderedLocusNames=BSUIS_A2006; OS Brucella suis (strain ATCC 23445 / NCTC 10510). OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhizobiales; OC Brucellaceae; Brucella. OX NCBI_TaxID=470137; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RA Setubal J.C., Bowns C., Boyle S., Crasta O.R., Czar M.J., RA Dharmanolla C., Gillespie J.J., Kenyon R.W., Lu J., Mane S., RA Mohapatra S., Nagrani S., Purkayastha A., Rajasimha H.K., RA Shallom J.M., Shallom S., Shukla M., Snyder E.E., Sobral B.W., RA Wattam A.R., Will R., Williams K., Yoo H., Bruce D., Detter C., RA Munk C., Brettin T.S.; RT "Brucella suis ATCC 23445 whole genome shotgun sequencing project."; RL Submitted (DEC-2007) to the EMBL/GenBank/DDBJ databases. 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. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP000911; ABY39016.1; -; Genomic_DNA. DR RefSeq; YP_001628587.1; -. DR GeneID; 5838194; -. DR GenomeReviews; CP000911_GR; BSUIS_A2006. DR KEGG; bmt:BSUIS_A2006; -. DR OMA; B0CK15; LHISEIR. 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 1 714 Polyribonucleotide FT nucleotidyltransferase. FT /FTId=PRO_1000087985. FT DOMAIN 555 614 KH. FT DOMAIN 624 692 S1 motif. SQ SEQUENCE 714 AA; 77730 MW; 61E6696AD66B29F7 CRC64; MFNTHKVEIE WGGRPLTLET GKIARQADGA VLATYGETAV LATVVSAKEP KPGQDFFPLT VNYQEKTYAA GKIPGGYFKR EGRPSENETL VSRLIDRPIR PLFVDGYKND TQVVITVLQH DLENNPDILS MVAASAALTI SGVPFMGPIS GARVGYIDGE YVLNPNIDEM PESKLDLVVA GTSEAVLMVE SEAQELPEDV MLGAVMFGHK SFQPVIDAII KLAEVAAKEP RDFQPEDLSE LEAKVLAVVE NDLREAYKIT EKQARYAAVD AAKAKAKEHF FPEGVEETEM SAEQFATIFK HLQAKIVRWN ILDTGNRIDG RDLSTVRPIV SEVGILPRTH GSALFTRGET QAIVVATLGT GEDEQMIDAL TGTYKESFML HYNFPPYSVG ETGRMGSPGR REIGHGKLAW RAIHPMLPAA EQFPYTIRAV SEITESNGSS SMATVCGTSL ALMDAGVPIV RPVAGIAMGL IKEGERFAVL SDILGDEDHL GDMDFKVAGT EFGITSLQMD IKIDGITEEI MKVALEQAKG GRVHILGEMA KAISSSRAEL GEFAPRIEVM NIPTDKIRDV IGSGGKVIRE IVEKTGAKIN IEDDGTVKIA SSNGKEIEAA KKWIHSIVAE PEVGEIYEGT VVKTADFGAF VNFFGPRDGL VHISQLAADR VAKTTDVVKE GQKVWVKLMG FDERGKVRLS MKVVDQETGK EIVAEKKKEE VDAE //