ID A0A3T0N6M0_9RHOB Unreviewed; 160 AA.
AC A0A3T0N6M0;
DT 08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT 08-MAY-2019, sequence version 1.
DT 27-MAR-2024, entry version 20.
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 ORFNames=EBB79_18650 {ECO:0000313|EMBL:AZV79694.1};
OS Parasedimentitalea marina.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC Paracoccaceae; Parasedimentitalea.
OX NCBI_TaxID=2483033 {ECO:0000313|EMBL:AZV79694.1, ECO:0000313|Proteomes:UP000283063};
RN [1] {ECO:0000313|EMBL:AZV79694.1, ECO:0000313|Proteomes:UP000283063}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=W43 {ECO:0000313|EMBL:AZV79694.1,
RC ECO:0000313|Proteomes:UP000283063};
RA Cao J.;
RT "Parasedimentitalea marina sp. nov., a psychrophilic bacterium isolated
RT from deep seawater of the New Britain Trench.";
RL Submitted (OCT-2018) 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; CP033219; AZV79694.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A3T0N6M0; -.
DR KEGG; sedi:EBB79_18650; -.
DR OrthoDB; 9816040at2; -.
DR Proteomes; UP000283063; 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; PTHR11839; UDP/ADP-SUGAR PYROPHOSPHATASE; 1.
DR PANTHER; PTHR11839:SF15; URIDINE DIPHOSPHATE GLUCOSE PYROPHOSPHATASE NUDT14; 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 10..154
FT /note="Nudix hydrolase"
FT /evidence="ECO:0000259|PROSITE:PS51462"
FT MOTIF 44..65
FT /note="Nudix box"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00298"
SQ SEQUENCE 160 AA; 18436 MW; 91ACDF1C4F048DEA CRC64;
MTPSEIAKLP YRPNVGVMMI NADGDVFVGQ RKDRFKDAWQ MPQGGIDPGE DPRAAVLREL
EEETGVTPDL VTIIAESDGW LPYDLPHDVV PKFWGGKYRG QEQKWYLMRF TGTDDQVNID
TDHPEFSTWC WQPVDQLVDK IVPFKREVYA RVIVEFKAHL
//
