ID A0A1Y2I0P9_9FUNG Unreviewed; 587 AA.
AC A0A1Y2I0P9;
DT 30-AUG-2017, integrated into UniProtKB/TrEMBL.
DT 30-AUG-2017, sequence version 1.
DT 27-MAR-2024, entry version 22.
DE RecName: Full=guanosine-diphosphatase {ECO:0000256|ARBA:ARBA00038903};
DE EC=3.6.1.42 {ECO:0000256|ARBA:ARBA00038903};
GN ORFNames=BCR44DRAFT_1424821 {ECO:0000313|EMBL:ORZ40319.1};
OS Catenaria anguillulae PL171.
OC Eukaryota; Fungi; Fungi incertae sedis; Blastocladiomycota;
OC Blastocladiomycetes; Blastocladiales; Catenariaceae; Catenaria.
OX NCBI_TaxID=765915 {ECO:0000313|EMBL:ORZ40319.1, ECO:0000313|Proteomes:UP000193411};
RN [1] {ECO:0000313|EMBL:ORZ40319.1, ECO:0000313|Proteomes:UP000193411}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PL171 {ECO:0000313|EMBL:ORZ40319.1,
RC ECO:0000313|Proteomes:UP000193411};
RG DOE Joint Genome Institute;
RA Mondo S.J., Dannebaum R.O., Kuo R.C., Labutti K., Haridas S., Kuo A.,
RA Salamov A., Ahrendt S.R., Lipzen A., Sullivan W., Andreopoulos W.B.,
RA Clum A., Lindquist E., Daum C., Ramamoorthy G.K., Gryganskyi A., Culley D.,
RA Magnuson J.K., James T.Y., O'Malley M.A., Stajich J.E., Spatafora J.W.,
RA Visel A., Grigoriev I.V.;
RT "Pervasive Adenine N6-methylation of Active Genes in Fungi.";
RL Submitted (JUL-2016) 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 -!- SIMILARITY: Belongs to the GDA1/CD39 NTPase family.
CC {ECO:0000256|ARBA:ARBA00009283}.
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:ORZ40319.1}.
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DR EMBL; MCFL01000003; ORZ40319.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1Y2I0P9; -.
DR STRING; 765915.A0A1Y2I0P9; -.
DR OrthoDB; 180318at2759; -.
DR Proteomes; UP000193411; Unassembled WGS sequence.
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:SF83; NTPASE, ISOFORM F; 1.
DR Pfam; PF01150; GDA1_CD39; 1.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|PIRSR:PIRSR600407-2};
KW Membrane {ECO:0000256|SAM:Phobius};
KW Nucleotide-binding {ECO:0000256|PIRSR:PIRSR600407-2};
KW Reference proteome {ECO:0000313|Proteomes:UP000193411};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 55..74
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT REGION 16..36
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 439..477
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 252
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR600407-1"
FT BINDING 281..285
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PIRSR:PIRSR600407-2"
SQ SEQUENCE 587 AA; 62650 MW; 3528B0F3E2913AD6 CRC64;
MKASNYALLP LFERERDQQS RRSAARSPSR AGPGAVRQLH SLAHSLRQLL TTRRGLVLTA
AGILTLFLVI SAFTHPSSPL SSASKTPADK VRYVGSLQST VCGTRRSPDA ADLPAVEYGL
MIDAGSTGSR IHVYRFNHCQ SRIPDVEHEV FEQIKPGLSA YANSPKRAAD SLKPLLEIAL
QAVPKEFHSC TGIQIKATAG LRLLGADVAK QILSETRQLI RTQYPFPLVD TNEPKQPTVD
GDAVAIMDGA DEGVFAWVTI NSLLDSVRRG GHTAAIMDLG GASTQIVYAP ASPKVPDTYR
ATMSFGGSDH VLYQHSYLGY GLKEALKSIR RFAVEQATHG SPIDHPCYHA GYTTSVDLPQ
QARTAVIQGK PDAEKCAALV RSALFKTSNA TVCDHAPCAF NGVHMPAIPD AAPIFAFSYF
YDLLNQVLSV AHAFSESDVP PATGAAASAD TPDDDAPASG PAAIPPPPAA ASSNKPNADL
VRASTTPAEL ATIQQLACTA PDHLDDNPAL AGHAARTVLG DLVHEDPEYC ASVTYLGQLL
RAYKVPKNRA VTVMKKIRGF EMGWCLGATM AMLDAAERVG GRCRVRT
//
