ID PNP_ANAVT Reviewed; 718 AA. AC Q3M7Z9; DT 29-APR-2008, integrated into UniProtKB/Swiss-Prot. DT 25-OCT-2005, sequence version 1. DT 16-JUN-2009, entry version 24. DE RecName: Full=Polyribonucleotide nucleotidyltransferase; DE EC=2.7.7.8; DE AltName: Full=Polynucleotide phosphorylase; DE Short=PNPase; GN Name=pnp; OrderedLocusNames=Ava_3279; OS Anabaena variabilis (strain ATCC 29413 / PCC 7937). OC Bacteria; Cyanobacteria; Nostocales; Nostocaceae; Anabaena. OX NCBI_TaxID=240292; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina T., RA Hammon N., Israni S., Pitluck S., Saunders E.H., Schmutz J., RA Larimer F., Land M., Kyrpides N., Mavrommatis K., Richardson P.; RT "Complete sequence of Anabaena variabilis ATCC 29413."; RL Submitted (SEP-2005) 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; CP000117; ABA22887.1; -; Genomic_DNA. DR RefSeq; YP_323782.1; -. DR GeneID; 3680310; -. DR GenomeReviews; CP000117_GR; Ava_3279. DR KEGG; ava:Ava_3279; -. DR NMPDR; fig|240292.3.peg.2302; -. DR HOGENOM; Q3M7Z9; -. DR OMA; Q3M7Z9; GHGNLAK. DR BioCyc; AVAR240292:AVA_3279-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 1 718 Polyribonucleotide FT nucleotidyltransferase. FT /FTId=PRO_0000329497. FT DOMAIN 563 622 KH. FT DOMAIN 632 700 S1 motif. SQ SEQUENCE 718 AA; 77751 MW; 3526BD49C8984685 CRC64; MAEFEKSISF DGRDIRLKVG LLAPQAGGSV LIESGDTAVL VTATRSAGRE GIDFLPLTVD YEERLYAAGR IPGGIMRREG RPPEKTILTS RLIDRPLRPL FPSWLRDDLQ IVALTMSMDE QVPPDVLAVT GASIATLIAK IPFNGPMAAV RVGLVGDDFI INPTYAEIEA GDLDLVVAGS PHGVIMVEAG ANQLPERDII EAIDFGYEAV RDLIKAQLDL VAELGLEIVQ EAPPEVDQTL ENYIRDRASD EIKKILAQFE LTKPERDAAL DVVKDNIATA IAELPEEDPI RLAATANSKA LGNTFKDITK YFMRRQIVED NVRVDGRKLD QVRPVSSQVG VLPKRVHGSG LFNRGLTQVL SACTLGTPGD AQNLNDDLQT DQSKRYLHHY NFPPFSVGET KPLRAPGRRE IGHGALAERA ILPVLPPKEQ FPYVIRVVSE VLSSNGSTSM GSVCGSTLAL MDAGVPILKP VSGAAMGLIK EGDEVRVLTD IQGIEDFLGD MDFKVAGTDA GITALQMDMK ISGLSLEVIA QAIHQAKDAR LHILDKMLQT IDTPRTETSP YAPRLLTIKI DPDMIGLVIG PGGKTIKGIT EETGAKIDIE DDGTVTISAV DENKAKRARN IVQGMTRKLN EGDVYAGRVT RIIPIGAFVE FLPGKEGMIH ISQLADYRVG KVEDEVAVGD EVIVKVREID NKGRINLTRL GIHPDQAAAA REAAAVNR //