ID A0A183H7F2_9BILA Unreviewed; 411 AA.
AC A0A183H7F2;
DT 07-SEP-2016, integrated into UniProtKB/TrEMBL.
DT 07-SEP-2016, sequence version 1.
DT 27-MAR-2024, entry version 26.
DE RecName: Full=diphosphoinositol-polyphosphate diphosphatase {ECO:0000256|ARBA:ARBA00012527};
DE EC=3.6.1.52 {ECO:0000256|ARBA:ARBA00012527};
GN ORFNames=OFLC_LOCUS3414 {ECO:0000313|EMBL:VDO36419.1};
OS Onchocerca flexuosa.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Spirurina; Spiruromorpha; Filarioidea; Onchocercidae; Onchocerca.
OX NCBI_TaxID=387005 {ECO:0000313|Proteomes:UP000050787, ECO:0000313|WBParaSite:OFLC_0000341301-mRNA-1};
RN [1] {ECO:0000313|WBParaSite:OFLC_0000341301-mRNA-1}
RP IDENTIFICATION.
RG WormBaseParasite;
RL Submitted (JUN-2016) to UniProtKB.
RN [2] {ECO:0000313|EMBL:VDO36419.1, ECO:0000313|Proteomes:UP000267606}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RG Pathogen Informatics;
RL Submitted (NOV-2018) to the EMBL/GenBank/DDBJ databases.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=diphospho-myo-inositol polyphosphate + H2O = myo-inositol
CC polyphosphate + phosphate.; EC=3.6.1.52;
CC Evidence={ECO:0000256|ARBA:ARBA00033994};
CC -!- SIMILARITY: Belongs to the Nudix hydrolase family. DIPP subfamily.
CC {ECO:0000256|ARBA:ARBA00008266}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; UZAJ01002271; VDO36419.1; -; Genomic_DNA.
DR STRING; 387005.A0A183H7F2; -.
DR WBParaSite; OFLC_0000341301-mRNA-1; OFLC_0000341301-mRNA-1; OFLC_0000341301.
DR Proteomes; UP000050787; Unplaced.
DR Proteomes; UP000267606; Unassembled WGS sequence.
DR GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0016462; F:pyrophosphatase activity; IEA:InterPro.
DR CDD; cd04666; Nudix_Hydrolase_9; 1.
DR Gene3D; 3.90.79.10; Nucleoside Triphosphate Pyrophosphohydrolase; 1.
DR Gene3D; 3.80.30.20; tm_1862 like domain; 1.
DR InterPro; IPR047198; DDP-like_NUDIX.
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; IPR007197; rSAM.
DR InterPro; IPR023404; rSAM_horseshoe.
DR InterPro; IPR002792; TRAM_dom.
DR PANTHER; PTHR11918; RADICAL SAM PROTEINS; 1.
DR PANTHER; PTHR11918:SF45; THREONYLCARBAMOYLADENOSINE TRNA METHYLTHIOTRANSFERASE; 1.
DR Pfam; PF00293; NUDIX; 1.
DR PRINTS; PR00502; NUDIXFAMILY.
DR SUPFAM; SSF55811; Nudix; 1.
DR SUPFAM; SSF102114; Radical SAM enzymes; 1.
DR PROSITE; PS51462; NUDIX; 1.
DR PROSITE; PS00893; NUDIX_BOX; 1.
DR PROSITE; PS51918; RADICAL_SAM; 1.
DR PROSITE; PS50926; TRAM; 1.
PE 3: Inferred from homology;
KW 4Fe-4S {ECO:0000256|ARBA:ARBA00022485};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Iron {ECO:0000256|ARBA:ARBA00023004};
KW Iron-sulfur {ECO:0000256|ARBA:ARBA00023014};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW S-adenosyl-L-methionine {ECO:0000256|ARBA:ARBA00022691}.
FT DOMAIN 1..140
FT /note="Radical SAM core"
FT /evidence="ECO:0000259|PROSITE:PS51918"
FT DOMAIN 141..203
FT /note="TRAM"
FT /evidence="ECO:0000259|PROSITE:PS50926"
FT DOMAIN 285..410
FT /note="Nudix hydrolase"
FT /evidence="ECO:0000259|PROSITE:PS51462"
SQ SEQUENCE 411 AA; 47442 MW; 40487B85E0389F1E CRC64;
MTNPPYILDF LEEISKILNH PRVYSFLHIP VQSASDAVLS DMKREYTCAD FCRVVDYMIQ
NVPNIYIATD FICAYPTETK NDFEESMALV QKYRFPSLFI NQFYPRTGTP AANLKKIDTI
EARRRTAEMS SLFRSYSRYD KERIGEKHRV LVCELATDQL HYVGHNKYYE HFLIPSKKCL
LGSWVEVRIV DVSKFYMKAV LISTDSTAWS LMTGISVLTY SYWMTAFSTG VVSVVMRWGL
PELSGGCFQG FLLVFGSDDF TVTPNRLFWL MRKNNGERVR DAEGFRLRAA GICIRGEGSN
REILLITGGK DDGRWIIPGG GIEKNENESD AALREVFEEA GVKAEILARV GEFRNEERRH
RTVVFLLTVK EELKEWEDGC FGRQREWVSL EEALRRVKHS QTCIIEHICR M
//