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Database: UniProt
Entry: A0A183H7F2_9BILA
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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}.
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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
//
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