ID A0A0W0SUC2_9GAMM Unreviewed; 174 AA.
AC A0A0W0SUC2;
DT 16-MAR-2016, integrated into UniProtKB/TrEMBL.
DT 16-MAR-2016, sequence version 1.
DT 24-JAN-2024, entry version 32.
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=Lbru_0173 {ECO:0000313|EMBL:KTC86944.1};
OS Legionella brunensis.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Legionellales;
OC Legionellaceae; Legionella.
OX NCBI_TaxID=29422 {ECO:0000313|EMBL:KTC86944.1, ECO:0000313|Proteomes:UP000054742};
RN [1] {ECO:0000313|EMBL:KTC86944.1, ECO:0000313|Proteomes:UP000054742}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 43878 {ECO:0000313|EMBL:KTC86944.1,
RC ECO:0000313|Proteomes:UP000054742};
RA Burstein D., Amaro F., Zusman T., Lifshitz Z., Cohen O., Gilbert J.A.,
RA Pupko T., Shuman H.A., Segal G.;
RT "Genomic analysis of 38 Legionella species identifies large and diverse
RT effector repertoires.";
RL Submitted (NOV-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:KTC86944.1}.
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DR EMBL; LNXV01000003; KTC86944.1; -; Genomic_DNA.
DR RefSeq; WP_058440288.1; NZ_LNXV01000003.1.
DR AlphaFoldDB; A0A0W0SUC2; -.
DR STRING; 29422.Lbru_0173; -.
DR PATRIC; fig|29422.6.peg.178; -.
DR OrthoDB; 9816040at2; -.
DR Proteomes; UP000054742; 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; 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 {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|HAMAP-Rule:MF_00298}.
FT DOMAIN 7..150
FT /note="Nudix hydrolase"
FT /evidence="ECO:0000259|PROSITE:PS51462"
FT MOTIF 39..60
FT /note="Nudix box"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00298"
SQ SEQUENCE 174 AA; 20666 MW; B5EDE085F3FBBF08 CRC64;
MVIDRAGYRL NVGIILVNGS GRVFWGRRQG HDAWQFPQGG LATGETALEA MFRELREEVG
LDREDIEVLG STKRWLKYRL PKQYLRHGSE PLVIGQKQKW YLLKLVTSEQ KIRLDLSDSP
EFDSWRWIDY HEPQEQVIFF KRQVYSQAMK ELEHLLKRRR TPFGARRKRG NHSR
//
