RPPH_BRASO
ID RPPH_BRASO Reviewed; 168 AA.
AC A4YKE4;
DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT 29-MAY-2007, sequence version 1.
DT 03-AUG-2022, entry version 70.
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=BRADO0423;
OS Bradyrhizobium sp. (strain ORS 278).
OC Bacteria; Proteobacteria; Alphaproteobacteria; Hyphomicrobiales;
OC Bradyrhizobiaceae; Bradyrhizobium; unclassified Bradyrhizobium.
OX NCBI_TaxID=114615;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ORS 278;
RX PubMed=17540897; DOI=10.1126/science.1139548;
RA Giraud E., Moulin L., Vallenet D., Barbe V., Cytryn E., Avarre J.-C.,
RA Jaubert M., Simon D., Cartieaux F., Prin Y., Bena G., Hannibal L.,
RA Fardoux J., Kojadinovic M., Vuillet L., Lajus A., Cruveiller S., Rouy Z.,
RA Mangenot S., Segurens B., Dossat C., Franck W.L., Chang W.-S., Saunders E.,
RA Bruce D., Richardson P., Normand P., Dreyfus B., Pignol D., Stacey G.,
RA Emerich D., Vermeglio A., Medigue C., Sadowsky M.;
RT "Legumes symbioses: absence of nod genes in photosynthetic bradyrhizobia.";
RL Science 316:1307-1312(2007).
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; CU234118; CAL74370.1; -; Genomic_DNA.
DR RefSeq; WP_011923646.1; NC_009445.1.
DR AlphaFoldDB; A4YKE4; -.
DR SMR; A4YKE4; -.
DR STRING; 114615.BRADO0423; -.
DR EnsemblBacteria; CAL74370; CAL74370; BRADO0423.
DR KEGG; bra:BRADO0423; -.
DR eggNOG; COG0494; Bacteria.
DR HOGENOM; CLU_087195_3_0_5; -.
DR OMA; WAAAKRE; -.
DR OrthoDB; 1345242at2; -.
DR BioCyc; BSP114615:BRADO_RS02010-MON; -.
DR Proteomes; UP000001994; Chromosome.
DR GO; GO:0016462; F:pyrophosphatase activity; IEA:UniProt.
DR CDD; cd03671; Ap4A_hydrolase_plant_like; 1.
DR HAMAP; MF_00298; Nudix_RppH; 1.
DR InterPro; IPR015797; NUDIX_hydrolase-like_dom_sf.
DR InterPro; IPR000086; NUDIX_hydrolase_dom.
DR InterPro; IPR022927; RppH.
DR Pfam; PF00293; NUDIX; 1.
DR SUPFAM; SSF55811; SSF55811; 1.
DR PROSITE; PS51462; NUDIX; 1.
PE 3: Inferred from homology;
KW Hydrolase; Reference proteome.
FT CHAIN 1..168
FT /note="RNA pyrophosphohydrolase"
FT /id="PRO_1000021930"
FT DOMAIN 8..160
FT /note="Nudix hydrolase"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00298"
FT MOTIF 47..68
FT /note="Nudix box"
SQ SEQUENCE 168 AA; 19269 MW; 503E62A2BE5BB339 CRC64;
MTRYEDLPYR TCVGIALINS EGLVFIGRRA GGIEHVDDTH VWQMPQGGVD PGEDAWEAAK
RELYEETSVR SVEKLAEIDD WLTYDIPRTV AGRAWKGRYR GQRQKWFALR FTGKDSEIDV
EHPGGGHHKA EFITWRWEPL QNLPTLIVPF KRPVYERVAK EFATLAGG