ID RPPH_HAMD5 Reviewed; 163 AA.
AC C4K4A2;
DT 22-SEP-2009, integrated into UniProtKB/Swiss-Prot.
DT 07-JUL-2009, sequence version 1.
DT 27-MAR-2024, entry version 65.
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=HDEF_0654;
OS Hamiltonella defensa subsp. Acyrthosiphon pisum (strain 5AT).
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; aphid secondary symbionts; Hamiltonella.
OX NCBI_TaxID=572265;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=5AT;
RX PubMed=19451630; DOI=10.1073/pnas.0900194106;
RA Degnan P.H., Yu Y., Sisneros N., Wing R.A., Moran N.A.;
RT "Hamiltonella defensa, genome evolution of protective bacterial
RT endosymbiont from pathogenic ancestors.";
RL Proc. Natl. Acad. Sci. U.S.A. 106:9063-9068(2009).
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; CP001277; ACQ67395.1; -; Genomic_DNA.
DR RefSeq; WP_015873216.1; NC_012751.1.
DR AlphaFoldDB; C4K4A2; -.
DR SMR; C4K4A2; -.
DR STRING; 572265.HDEF_0654; -.
DR GeneID; 66260522; -.
DR KEGG; hde:HDEF_0654; -.
DR eggNOG; COG0494; Bacteria.
DR HOGENOM; CLU_087195_3_1_6; -.
DR Proteomes; UP000002334; Chromosome.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0016462; F:pyrophosphatase activity; IEA:UniProt.
DR GO; GO:0016070; P:RNA metabolic process; 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; Metal-binding.
FT CHAIN 1..163
FT /note="RNA pyrophosphohydrolase"
FT /id="PRO_1000204935"
FT DOMAIN 6..149
FT /note="Nudix hydrolase"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00298"
FT MOTIF 38..59
FT /note="Nudix box"
SQ SEQUENCE 163 AA; 19576 MW; 77A815C6A6D6714E CRC64;
MIDNDGYRLN VGIVICNKKG QVLWAKRYGQ YSWQFPQGGI HLTESPEEAM YRELFEELGL
NKKDVRILTS THYWLRYKLP KHLVRWNTDP VCIGQKQRWF LLELTCDDSN INVECTKAPE
FDGWCWVSFW YPVRQVVSFK RDVYRQVMKE FFSFVSLIQK HLI
//
