ID A0A0D8CMC7_9PROT Unreviewed; 181 AA.
AC A0A0D8CMC7;
DT 27-MAY-2015, integrated into UniProtKB/TrEMBL.
DT 27-MAY-2015, sequence version 1.
DT 27-MAR-2024, entry version 38.
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=UF64_03355 {ECO:0000313|EMBL:KJE36717.1};
OS Thalassospira sp. HJ.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodospirillales;
OC Thalassospiraceae; Thalassospira.
OX NCBI_TaxID=1616823 {ECO:0000313|EMBL:KJE36717.1, ECO:0000313|Proteomes:UP000032356};
RN [1] {ECO:0000313|EMBL:KJE36717.1, ECO:0000313|Proteomes:UP000032356}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=HJ {ECO:0000313|EMBL:KJE36717.1,
RC ECO:0000313|Proteomes:UP000032356};
RA Kiseleva L., Garushyants S.K., Goryanin I.;
RT "Complete genome of Thalassospira sp. strain HJ.";
RL Submitted (FEB-2015) 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}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:KJE36717.1}.
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DR EMBL; JYII01000006; KJE36717.1; -; Genomic_DNA.
DR RefSeq; WP_044827182.1; NZ_JYII01000006.1.
DR AlphaFoldDB; A0A0D8CMC7; -.
DR STRING; 1616823.UF64_03355; -.
DR PATRIC; fig|1616823.3.peg.2227; -.
DR OrthoDB; 9816040at2; -.
DR Proteomes; UP000032356; Unassembled WGS sequence.
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};
KW Reference proteome {ECO:0000313|Proteomes:UP000032356}.
FT DOMAIN 25..166
FT /note="Nudix hydrolase"
FT /evidence="ECO:0000259|PROSITE:PS51462"
FT REGION 1..21
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 58..79
FT /note="Nudix box"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00298"
SQ SEQUENCE 181 AA; 20632 MW; 64F7BA483B169309 CRC64;
MAKKSDKPKQ TETGTPDKVT AEDLPYRPCV GIALFNADGL VWMGNRFGFE GAWQLPQGGI
DDGETPIEAA LRELKEEIGT DKAEIVAETP NWLTYDLPEH LVGKAFKGKY RGQKQKWFAM
RFTGKDKHIN IDVPNPEFDS WRWNDFATLP DLIVPFKRPV YLQIAAEFHD VPQRIREMGR
A
//
