ID RPPH_ACIET Reviewed; 229 AA.
AC B9MDZ9;
DT 28-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT 24-MAR-2009, sequence version 1.
DT 27-MAR-2024, entry version 67.
DE RecName: Full=RNA pyrophosphohydrolase {ECO:0000255|HAMAP-Rule:MF_00298};
DE EC=3.6.1.- {ECO:0000255|HAMAP-Rule:MF_00298};
DE AltName: Full=(Di)nucleoside polyphosphate hydrolase {ECO:0000255|HAMAP-Rule:MF_00298};
GN Name=rppH {ECO:0000255|HAMAP-Rule:MF_00298};
GN Synonyms=nudH {ECO:0000255|HAMAP-Rule:MF_00298};
GN OrderedLocusNames=Dtpsy_0774;
OS Acidovorax ebreus (strain TPSY) (Diaphorobacter sp. (strain TPSY)).
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Comamonadaceae; Diaphorobacter.
OX NCBI_TaxID=535289;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=TPSY;
RG US DOE Joint Genome Institute;
RA Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Tice H., Bruce D.,
RA Goodwin L., Pitluck S., Chertkov O., Brettin T., Detter J.C., Han C.,
RA Larimer F., Land M., Hauser L., Kyrpides N., Mikhailova N., Coates J.D.;
RT "Complete sequence of Diaphorobacter sp. TPSY.";
RL Submitted (JAN-2009) 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:0000255|HAMAP-Rule:MF_00298}.
CC -!- COFACTOR:
CC Name=a divalent metal cation; Xref=ChEBI:CHEBI:60240;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_00298};
CC -!- SIMILARITY: Belongs to the Nudix hydrolase family. RppH subfamily.
CC {ECO:0000255|HAMAP-Rule:MF_00298}.
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DR EMBL; CP001392; ACM32253.1; -; Genomic_DNA.
DR RefSeq; WP_012655756.1; NC_011992.1.
DR AlphaFoldDB; B9MDZ9; -.
DR SMR; B9MDZ9; -.
DR KEGG; dia:Dtpsy_0774; -.
DR eggNOG; COG0494; Bacteria.
DR HOGENOM; CLU_087195_1_1_4; -.
DR Proteomes; UP000000450; 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; PTHR43736; ADP-RIBOSE PYROPHOSPHATASE; 1.
DR PANTHER; PTHR43736:SF4; DIHYDRONEOPTERIN TRIPHOSPHATE DIPHOSPHATASE; 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.
FT CHAIN 1..229
FT /note="RNA pyrophosphohydrolase"
FT /id="PRO_1000191841"
FT DOMAIN 6..149
FT /note="Nudix hydrolase"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00298"
FT REGION 191..229
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 38..59
FT /note="Nudix box"
SQ SEQUENCE 229 AA; 26821 MW; 74C78845CC611F09 CRC64;
MLDRDGFRPN VGIILLNQRN QVFWGKRIRT HSWQFPQGGI DRGETPEQAM FRELHEEVGL
LPPQVRVIAR TRDWLRYEVP DRFIRRDARG HYKGQKQIWY LLQLLGHDWD LNLRATNHPE
FDAWRWNDYW VPLDVVVEFK RGVYEMALTE LARFLPRHEQ RNRYLRSGMR TREHESSGQA
SLARTSSLLV KPGMELPPGA SFDPDPQNSV PAPLEALPTL PVPKKPLDA
//
