ID C6YUE5_9GAMM Unreviewed; 155 AA. AC C6YUE5; DT 22-SEP-2009, integrated into UniProtKB/TrEMBL. DT 22-SEP-2009, sequence version 1. DT 16-APR-2014, entry version 24. DE RecName: Full=RNA pyrophosphohydrolase; DE EC=3.6.1.-; DE AltName: Full=(Di)nucleoside polyphosphate hydrolase; GN Name=rppH; Synonyms=nudH; ORFNames=FTPG_01503; OS Francisella philomiragia subsp. philomiragia ATCC 25015. OC Bacteria; Proteobacteria; Gammaproteobacteria; Thiotrichales; OC Francisellaceae; Francisella. OX NCBI_TaxID=539329; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=ATCC 25015; RG The Broad Institute Genome Sequencing Platform; RG Broad Institute Microbial Sequencing Center; RA Bearden S., Schriefer M.E., Young S., Kodira C.D., Zeng Q., RA Koehrsen M., Alvarado L., Berlin A.M., Borenstein D., Chen Z., RA Engels R., Freedman E., Gellesch M., Goldberg J., Griggs A., Gujja S., RA Heiman D.I., Hepburn T.A., Howarth C., Jen D., Larson L., Lewis B., RA Mehta T., Park D., Pearson M., Roberts A., Saif S., Shea T.D., RA Shenoy N., Sisk P., Stolte C., Sykes S.N., Walk T., White J., RA Yandava C., Ilzarbe M., Galagan J., Nusbaum C., Birren B.; RT "Annotation of Francisella philomiragia subsp. philomiragia strain RT ATCC 25015."; RL Submitted (NOV-2008) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Accelerates the degradation of transcripts by removing CC pyrophosphate from the 5'-end of triphosphorylated RNA, leading to CC a more labile monophosphorylated state that can stimulate CC subsequent ribonuclease cleavage (By similarity). CC -!- COFACTOR: Divalent ions (By similarity). CC -!- SIMILARITY: Belongs to the Nudix hydrolase family. RppH subfamily. CC -!- SIMILARITY: Contains 1 nudix hydrolase domain. CC -!- SIMILARITY: Contains nudix hydrolase domain. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; DS999312; EET20819.1; -; Genomic_DNA. DR ProteinModelPortal; C6YUE5; -. DR EnsemblBacteria; EET20819; EET20819; FTPG_01503. DR PATRIC; 27631566; VBIFraPhi76072_0714. DR GO; GO:0016818; F:hydrolase activity, acting on acid anhydrides, in phosphorus-containing anhydrides; IEA:UniProtKB-HAMAP. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-HAMAP. DR Gene3D; 3.90.79.10; -; 1. DR HAMAP; MF_00298; Nudix_RppH; 1. DR InterPro; IPR020476; Nudix_hydrolase. DR InterPro; IPR020084; NUDIX_hydrolase_CS. DR InterPro; IPR000086; NUDIX_hydrolase_dom. DR InterPro; IPR015797; NUDIX_hydrolase_dom-like. DR InterPro; IPR022927; RppH. DR Pfam; PF00293; NUDIX; 1. DR PRINTS; PR00502; NUDIXFAMILY. DR SUPFAM; SSF55811; SSF55811; 1. DR PROSITE; PS51462; NUDIX; 1. DR PROSITE; PS00893; NUDIX_BOX; 1. PE 3: Inferred from homology; KW Hydrolase; Metal-binding. FT DOMAIN 6 148 Nudix hydrolase (By similarity). FT MOTIF 38 59 Nudix box (By similarity). SQ SEQUENCE 155 AA; 18577 MW; 2913D6E3BD0B5A27 CRC64; MIDKSGYRAN VAIVLLNRQD RVFWGQRKSR TSWQFPQGGV AIGETPLQAM YRELYEEVGL RPHDVEVIAS TRDWFKYDIP DSLVRSREPV CIGQKQKWFL LRLKTSESNI NLEANDSPEF DNWRWVSYWY PINHVVYFKQ DVYRKALTYF KEYIN //