ID   F8GAQ2_FRAST            Unreviewed;       155 AA.
AC   F8GAQ2;
DT   21-SEP-2011, integrated into UniProtKB/TrEMBL.
DT   21-SEP-2011, sequence version 1.
DT   27-MAR-2024, entry version 64.
DE   RecName: Full=RNA pyrophosphohydrolase {ECO:0000256|HAMAP-Rule:MF_00298};
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   OrderedLocusNames=F7308_0660 {ECO:0000313|EMBL:AEI35587.1};
OS   Francisella salina.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Thiotrichales;
OC   Francisellaceae; Francisella.
OX   NCBI_TaxID=573569 {ECO:0000313|EMBL:AEI35587.1, ECO:0000313|Proteomes:UP000000490};
RN   [1] {ECO:0000313|Proteomes:UP000000490}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=TX07-7308 {ECO:0000313|Proteomes:UP000000490};
RA   Kuske C.R., Challacombe J.F., Siddaramappa S., Petersen J.M.;
RT   "The complete genome of Francisella sp. TX077308.";
RL   Submitted (MAY-2011) 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 a
CC       more labile monophosphorylated state that can stimulate subsequent
CC       ribonuclease cleavage. {ECO:0000256|HAMAP-Rule:MF_00298}.
CC   -!- COFACTOR:
CC       Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC         Evidence={ECO:0000256|ARBA:ARBA00001936};
CC   -!- COFACTOR:
CC       Name=a divalent metal cation; Xref=ChEBI:CHEBI:60240;
CC         Evidence={ECO:0000256|HAMAP-Rule:MF_00298};
CC   -!- SIMILARITY: Belongs to the Nudix hydrolase family. RppH subfamily.
CC       {ECO:0000256|HAMAP-Rule:MF_00298}.
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DR   EMBL; CP002872; AEI35587.1; -; Genomic_DNA.
DR   RefSeq; WP_013922429.1; NC_015696.1.
DR   AlphaFoldDB; F8GAQ2; -.
DR   STRING; 573569.F7308_0660; -.
DR   KEGG; frt:F7308_0660; -.
DR   eggNOG; COG0494; Bacteria.
DR   HOGENOM; CLU_087195_3_1_6; -.
DR   OrthoDB; 9816040at2; -.
DR   Proteomes; UP000000490; Chromosome.
DR   GO; GO:0016462; F:pyrophosphatase activity; IEA:UniProt.
DR   CDD; cd03671; Ap4A_hydrolase_plant_like; 1.
DR   Gene3D; 3.90.79.10; Nucleoside Triphosphate Pyrophosphohydrolase; 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   PANTHER; PTHR23114; M7GPPPN-MRNA HYDROLASE; 1.
DR   PANTHER; PTHR23114:SF17; M7GPPPN-MRNA HYDROLASE; 1.
DR   Pfam; PF00293; NUDIX; 1.
DR   PRINTS; PR00502; NUDIXFAMILY.
DR   SUPFAM; SSF55811; Nudix; 1.
DR   PROSITE; PS51462; NUDIX; 1.
DR   PROSITE; PS00893; NUDIX_BOX; 1.
PE   3: Inferred from homology;
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|HAMAP-Rule:MF_00298}.
FT   DOMAIN          6..148
FT                   /note="Nudix hydrolase"
FT                   /evidence="ECO:0000259|PROSITE:PS51462"
FT   MOTIF           38..59
FT                   /note="Nudix box"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00298"
SQ   SEQUENCE   155 AA;  18617 MW;  13BBBA36DE55CC18 CRC64;
     MIDKSGYRAN VAIVLLNRQN RVFWGQRKSR TSWQFPQGGV AVGETPLQAM YRELYEEIGL
     RPHDVEVIAS TRDWFKYDIP DSLVRSREPV CIGQKQKWFL LRLKTSENNI NLEANDSPEF
     DNWRWVSYWY PINHVVYFKQ EVYRKALTYF KEYIN
//