ID A0A0W0FSG5_9AGAR Unreviewed; 643 AA.
AC A0A0W0FSG5;
DT 16-MAR-2016, integrated into UniProtKB/TrEMBL.
DT 16-MAR-2016, sequence version 1.
DT 24-JAN-2024, entry version 26.
DE RecName: Full=guanosine-diphosphatase {ECO:0000256|ARBA:ARBA00038903};
DE EC=3.6.1.42 {ECO:0000256|ARBA:ARBA00038903};
GN ORFNames=WG66_8157 {ECO:0000313|EMBL:KTB39265.1};
OS Moniliophthora roreri.
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC Agaricomycetidae; Agaricales; Marasmiineae; Marasmiaceae; Moniliophthora.
OX NCBI_TaxID=221103 {ECO:0000313|EMBL:KTB39265.1, ECO:0000313|Proteomes:UP000054988};
RN [1] {ECO:0000313|EMBL:KTB39265.1, ECO:0000313|Proteomes:UP000054988}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MCA 2952 {ECO:0000313|EMBL:KTB39265.1,
RC ECO:0000313|Proteomes:UP000054988};
RA Aime M.C., Diaz-Valderrama J.R., Kijpornyongpan T., Phillips-Mora W.;
RT "Draft genome sequence of Moniliophthora roreri, the causal agent of frosty
RT pod rot of cacao.";
RL Submitted (DEC-2015) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: After transfer of sugars to endogenous macromolecular
CC acceptors, the enzyme converts nucleoside diphosphates to nucleoside
CC monophosphates which in turn exit the Golgi lumen in a coupled
CC antiporter reaction, allowing entry of additional nucleotide sugar from
CC the cytosol. {ECO:0000256|ARBA:ARBA00037742}.
CC -!- SUBCELLULAR LOCATION: Golgi apparatus membrane
CC {ECO:0000256|ARBA:ARBA00004323}; Single-pass type II membrane protein
CC {ECO:0000256|ARBA:ARBA00004323}.
CC -!- SIMILARITY: Belongs to the GDA1/CD39 NTPase family.
CC {ECO:0000256|ARBA:ARBA00009283, ECO:0000256|RuleBase:RU003833}.
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:KTB39265.1}.
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DR EMBL; LATX01001693; KTB39265.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0W0FSG5; -.
DR eggNOG; KOG1385; Eukaryota.
DR Proteomes; UP000054988; Unassembled WGS sequence.
DR GO; GO:0005794; C:Golgi apparatus; IEA:UniProt.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0017110; F:nucleoside diphosphate phosphatase activity; IEA:UniProt.
DR CDD; cd00012; NBD_sugar-kinase_HSP70_actin; 1.
DR Gene3D; 3.30.420.40; -; 1.
DR Gene3D; 3.30.420.150; Exopolyphosphatase. Domain 2; 1.
DR InterPro; IPR000407; GDA1_CD39_NTPase.
DR PANTHER; PTHR11782; ADENOSINE/GUANOSINE DIPHOSPHATASE; 1.
DR PANTHER; PTHR11782:SF3; NTPASE, ISOFORM F; 1.
DR Pfam; PF01150; GDA1_CD39; 1.
DR PROSITE; PS01238; GDA1_CD39_NTPASE; 1.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|PIRSR:PIRSR600407-2};
KW Hydrolase {ECO:0000256|RuleBase:RU003833};
KW Membrane {ECO:0000256|SAM:Phobius};
KW Nucleotide-binding {ECO:0000256|PIRSR:PIRSR600407-2};
KW Reference proteome {ECO:0000313|Proteomes:UP000054988};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 96..115
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT REGION 1..88
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 124..189
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 40..56
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 323
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR600407-1"
FT BINDING 356..360
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PIRSR:PIRSR600407-2"
SQ SEQUENCE 643 AA; 70758 MW; 4BD1B150C9C48BED CRC64;
MDPWRGRSWL RPATVLNSET PPPLSSSPPP SARTTGSESH ISHNHARSRS ITSPEEIEFD
PRSLSTPMAL SPRSSNYERL EGGMGPSKLP NKKKFAWKKF AIGAAVIIGL VWLFGPRERR
EKLSTPWSTW DDSKVEGPPT YNPAVPNNQH MGHDDDTEPL PPSGSTSKPH GHPTSFEEDT
DPSKTTYCTS PHSSASRLVQ WALMIDAGST GSRIHIYKFN NCNKNPTFEY EVFKMTRPGL
SSYAEEPQKA AASLDELLNE AIRVVPKSLH KCAPVAVKAT AGLRLLPGSQ SADILKAIED
KLQKDYPFQL PNDAVSIMDG KDEGVFAWIT ANYLLDTIRG TSGASADTYA VLDLGGASTQ
IVFEPKFTKP DSSLADGEHK YDLDFLGKKY ELYQHSYLGY GLMRARARVH QLVEFMASLK
LPDVTTGSSE AIPVIGNPCL AKGTKKDIEV EDERSKTSRN VTMDGELVGS FEACNRVMEL
VMAKDAICEK KPCSFDGVYQ PSLLDTFATG KVLLLSYFFD RLDPLLSTQP KSLDTGIIPP
TNPDDNPKLR ISSIASLAKV ICQGKSAWLE HFKAISPELM GELEDRPEWC LDLTFMHALL
RLGYEFDETR EVTIGKKIAG TELGWCLGAT IAMVGGGEIK CRI
//