ID J1EKC4_9BURK Unreviewed; 234 AA.
AC J1EKC4;
DT 03-OCT-2012, integrated into UniProtKB/TrEMBL.
DT 03-OCT-2012, sequence version 1.
DT 24-JAN-2024, entry version 60.
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=PMI14_02658 {ECO:0000313|EMBL:EJE52659.1};
OS Acidovorax sp. CF316.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Comamonadaceae; Acidovorax.
OX NCBI_TaxID=1144317 {ECO:0000313|EMBL:EJE52659.1, ECO:0000313|Proteomes:UP000004811};
RN [1] {ECO:0000313|EMBL:EJE52659.1, ECO:0000313|Proteomes:UP000004811}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CF316 {ECO:0000313|EMBL:EJE52659.1,
RC ECO:0000313|Proteomes:UP000004811};
RX PubMed=23045501; DOI=10.1128/JB.01243-12;
RA Brown S.D., Utturkar S.M., Klingeman D.M., Johnson C.M., Martin S.L.,
RA Land M.L., Lu T.Y., Schadt C.W., Doktycz M.J., Pelletier D.A.;
RT "Twenty-one genome sequences from Pseudomonas species and 19 genome
RT sequences from diverse bacteria isolated from the rhizosphere and
RT endosphere of Populus deltoides.";
RL J. Bacteriol. 194:5991-5993(2012).
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:EJE52659.1}.
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DR EMBL; AKJX01000110; EJE52659.1; -; Genomic_DNA.
DR RefSeq; WP_007854562.1; NZ_AKJX01000110.1.
DR AlphaFoldDB; J1EKC4; -.
DR PATRIC; fig|1144317.3.peg.2348; -.
DR Proteomes; UP000004811; 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};
KW Reference proteome {ECO:0000313|Proteomes:UP000004811}.
FT DOMAIN 6..149
FT /note="Nudix hydrolase"
FT /evidence="ECO:0000259|PROSITE:PS51462"
FT REGION 193..234
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 38..59
FT /note="Nudix box"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00298"
SQ SEQUENCE 234 AA; 27173 MW; 363484B5B2C30FEF CRC64;
MLDRDGFRPN VGIILLNQKN QVFWGKRIRT HSWQFPQGGI DRGETPEQAM FRELHEEVGL
HPNHVRLVAR TRDWLRYEVP DRYIRRDARG HYKGQKQIWY LLQLVGHDWD LNLRATNHPE
FDAWRWNDYW VPLDVVVEFK RGVYEMALTE LARFLPRNEQ RNRYLRSGMR ARDGEHAGSA
MFRTGSLLVN PGMELPPGAS FDPDPQSSRP MGLEGLPVSS PEPVVASSAP PPLK
//