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-JAN-2019, entry version 54. DE RecName: Full=RNA pyrophosphohydrolase {ECO:0000256|HAMAP-Rule:MF_00298, ECO:0000256|SAAS:SAAS01081979}; DE EC=3.6.1.- {ECO:0000256|HAMAP-Rule:MF_00298}; DE AltName: Full=(Di)nucleoside polyphosphate hydrolase {ECO:0000256|HAMAP-Rule:MF_00298}; GN Name=rppH {ECO:0000256|HAMAP-Rule:MF_00298}; GN Synonyms=nudH {ECO:0000256|HAMAP-Rule:MF_00298}; GN ORFNames=BZ13_967 {ECO:0000313|EMBL:AJI74797.1}; OS Francisella philomiragia subsp. philomiragia ATCC 25015. OC Bacteria; Proteobacteria; Gammaproteobacteria; Thiotrichales; OC Francisellaceae; Francisella. OX NCBI_TaxID=539329 {ECO:0000313|EMBL:AJI74797.1}; RN [1] {ECO:0000313|EMBL:AJI74797.1} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=O#319L {ECO:0000313|EMBL:AJI74797.1}; RX PubMed=25931589; RA Johnson S.L., Daligault H.E., Davenport K.W., Coyne S.R., Frey K.G., RA Koroleva G.I., Broomall S.M., Bishop-Lilly K.A., Bruce D.C., RA Chertkov O., Freitas T., Jaissle J., Ladner J.T., Rosenzweig C.N., RA Gibbons H.S., Palacios G.F., Redden C.L., Xu Y., Minogue T.D., RA Chain P.S.; RT "Genome sequencing of 18 francisella strains to aid in assay RT development and testing."; RL Genome Announc. 3:0-0(2015). 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. {ECO:0000256|HAMAP- CC Rule:MF_00298, ECO:0000256|SAAS:SAAS01081973}. CC -!- COFACTOR: CC Name=a divalent metal cation; Xref=ChEBI:CHEBI:60240; CC Evidence={ECO:0000256|HAMAP-Rule:MF_00298, CC ECO:0000256|SAAS:SAAS01082865}; CC -!- SIMILARITY: Belongs to the Nudix hydrolase family. RppH subfamily. CC {ECO:0000256|HAMAP-Rule:MF_00298, ECO:0000256|SAAS:SAAS01081978}. 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; CP010019; AJI74797.1; -; Genomic_DNA. DR RefSeq; WP_004287076.1; NZ_DS999312.1. DR ProteinModelPortal; C6YUE5; -. DR EnsemblBacteria; AJI74797; AJI74797; BZ13_967. DR KEGG; fpt:BZ13_967; -. DR PATRIC; fig|539329.6.peg.955; -. DR KO; K08311; -. DR OrthoDB; 1345242at2; -. DR GO; GO:0016818; F:hydrolase activity, acting on acid anhydrides, in phosphorus-containing anhydrides; IEA:UniProtKB-UniRule. DR CDD; cd03671; Ap4A_hydrolase_plant_like; 1. DR HAMAP; MF_00298; Nudix_RppH; 1. DR InterPro; IPR020476; Nudix_hydrolase. DR InterPro; IPR015797; NUDIX_hydrolase-like_dom_sf. DR InterPro; IPR020084; NUDIX_hydrolase_CS. DR InterPro; IPR000086; NUDIX_hydrolase_dom. 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 {ECO:0000256|HAMAP-Rule:MF_00298, KW ECO:0000256|RuleBase:RU003476, ECO:0000256|SAAS:SAAS00499465}. FT DOMAIN 6 148 Nudix hydrolase. {ECO:0000259|PROSITE: FT PS51462}. FT MOTIF 38 59 Nudix box. {ECO:0000256|HAMAP-Rule: FT MF_00298}. SQ SEQUENCE 155 AA; 18577 MW; 2913D6E3BD0B5A27 CRC64; MIDKSGYRAN VAIVLLNRQD RVFWGQRKSR TSWQFPQGGV AIGETPLQAM YRELYEEVGL RPHDVEVIAS TRDWFKYDIP DSLVRSREPV CIGQKQKWFL LRLKTSESNI NLEANDSPEF DNWRWVSYWY PINHVVYFKQ DVYRKALTYF KEYIN //