ID PNP_BUCAP Reviewed; 707 AA. AC Q8K9H5; DT 15-NOV-2002, integrated into UniProtKB/Swiss-Prot. DT 01-OCT-2002, sequence version 1. DT 16-JUN-2009, entry version 50. DE RecName: Full=Polyribonucleotide nucleotidyltransferase; DE EC=2.7.7.8; DE AltName: Full=Polynucleotide phosphorylase; DE Short=PNPase; GN Name=pnp; OrderedLocusNames=BUsg_361; OS Buchnera aphidicola subsp. Schizaphis graminum. OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales; OC Enterobacteriaceae; Buchnera. OX NCBI_TaxID=98794; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX MEDLINE=22084549; PubMed=12089438; DOI=10.1126/science.1071278; RA Tamas I., Klasson L., Canbaeck B., Naeslund A.K., Eriksson A.-S., RA Wernegreen J.J., Sandstroem J.P., Moran N.A., Andersson S.G.E.; RT "50 million years of genomic stasis in endosymbiotic bacteria."; RL Science 296:2376-2379(2002). 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; AE013218; AAM67914.1; -; Genomic_DNA. DR RefSeq; NP_660703.1; -. DR HSSP; P05055; 1SRO. DR SMR; Q8K9H5; 617-691. DR GeneID; 1005794; -. DR GenomeReviews; AE013218_GR; BUsg_361. DR KEGG; bas:BUsg361; -. DR HOGENOM; Q8K9H5; -. DR OMA; Q8K9H5; GHGNLAK. DR BioCyc; BAPH198804:BUSG361-MON; -. 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 1 707 Polyribonucleotide FT nucleotidyltransferase. FT /FTId=PRO_0000197911. FT DOMAIN 553 612 KH. FT DOMAIN 622 690 S1 motif. SQ SEQUENCE 707 AA; 78389 MW; 9D5367E96E91520A CRC64; MLNPIVRKFQ YGQHTITLET GIMARQATAA VMASMDDTAV FVTVVGEKTT NSSQKFFPLT VNYQERTYAV GRIPGGFFRR EGRPSENEIL TARLIDRPIR PLFPKGFCNE IQIIATVVSV NPQINPDIIS IIGASAALSL SGIPFYGPIG AARVGFVNNQ YVLNPTIDDM KSSFLDLVVS GTQNAVLMVE AESKVLSEDK ILGAIMFGHQ QQQVVINNIR SLSNEASKLP WIISYPEINT ELELKITKLA EKDISNAYLI FNKQERYEKL NFLKEEIIKL FFSENSNIDI SEIEDIFEKI EKNIVRKRIL NNENRIDGRE KDMIRALDIR TGVLPRTHGS SLFTRGETQS LVSVTLGTSR DAQNLDELLG DKTDNFLFHY NFPPYSVGEI GIVGSPKRRE IGHGRLAKRS LLAVMPKLDD FPYTIRIVSE ITESNGSSSM ASVCGASLAL MDAGVPIKSA VAGISMGLVK EGDKYVLLSD ILGDEDHLGD MDFKVSGTEE GITALQMDIK IEGITNEIMR IALNKAKSAR LHILNVMKQA LSKPRNEISE FAPRIHKIKI NPEKIKDVIG KGGSVIRMLT EETGTIIEIE DDGTIKISAT IGEKAKNAIR RIEEITAEIE VGRIYSGKVT RIVDFGAFIS IGIGKEGLVH ISQISNKRVE KVSDHLTVDQ IISVKVLEID RQGRLRLSIK EVENSIISNK SINNIYI //