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Database: UniProt
Entry: A0A1Y1U8D5_9TREE
LinkDB: A0A1Y1U8D5_9TREE
Original site: A0A1Y1U8D5_9TREE 
ID   A0A1Y1U8D5_9TREE        Unreviewed;       629 AA.
AC   A0A1Y1U8D5;
DT   30-AUG-2017, integrated into UniProtKB/TrEMBL.
DT   30-AUG-2017, sequence version 1.
DT   27-MAR-2024, entry version 21.
DE   RecName: Full=guanosine-diphosphatase {ECO:0000256|ARBA:ARBA00038903};
DE            EC=3.6.1.42 {ECO:0000256|ARBA:ARBA00038903};
GN   ORFNames=BD324DRAFT_643770 {ECO:0000313|EMBL:ORX33804.1};
OS   Kockovaella imperatae.
OC   Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Tremellomycetes;
OC   Tremellales; Cuniculitremaceae; Kockovaella.
OX   NCBI_TaxID=4999 {ECO:0000313|EMBL:ORX33804.1, ECO:0000313|Proteomes:UP000193218};
RN   [1] {ECO:0000313|EMBL:ORX33804.1, ECO:0000313|Proteomes:UP000193218}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NRRL Y-17943 {ECO:0000313|EMBL:ORX33804.1,
RC   ECO:0000313|Proteomes:UP000193218};
RG   DOE Joint Genome Institute;
RA   Mondo S.J., Dannebaum R.O., Kuo R.C., Louie K.B., Bewick A.J., Labutti K.,
RA   Haridas S., Kuo A., Salamov A., Ahrendt S.R., Lau R., Bowen B.P.,
RA   Lipzen A., Sullivan W., Andreopoulos W.B., Clum A., Lindquist E., Daum C.,
RA   Northen T.R., Ramamoorthy G., Schmitz R.J., Gryganskyi A., Culley D.,
RA   Magnuson J., James T.Y., O'Malley M.A., Stajich J.E., Spatafora J.W.,
RA   Visel A., Grigoriev I.V.;
RT   "Widespread Adenine N6-methylation of Active Genes in Fungi.";
RL   Submitted (MAR-2017) 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:ORX33804.1}.
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DR   EMBL; NBSH01000017; ORX33804.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1Y1U8D5; -.
DR   STRING; 4999.A0A1Y1U8D5; -.
DR   InParanoid; A0A1Y1U8D5; -.
DR   OrthoDB; 180318at2759; -.
DR   Proteomes; UP000193218; Unassembled WGS sequence.
DR   GO; GO:0000139; C:Golgi membrane; IEA:UniProtKB-SubCell.
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.
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:UP000193218};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        28..46
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   REGION          1..20
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          112..163
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1..19
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        142..163
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        322
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR600407-1"
FT   BINDING         354..358
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR600407-2"
SQ   SEQUENCE   629 AA;  68882 MW;  1B9EB7466F9EC067 CRC64;
     MFSSRKYTPL PTSSGPQRRS GMPVWKRWAF IGTGVLVLMV VGYARFPSTR STYDETWETD
     NAYTPQLGGE KLENDMTDYS EFKSPPFRPI GAGSIAEPGV ADTDEGRVHA LPFNHLRPKP
     GFNDDASGTE ADEDEEEAAN SPHNPLSDQA QEAQGAQNDF TEIDNTPEVV VMTFETDPDP
     ASTTACADPY DSKRPLVQYA LTIDAGSTGS RIHVYKFHNC GPSPTLEYET FKMLNPGLSA
     YARDPTAAAA SLDPLLREAK RVVPKSLWSC TPVEVKATAG LRLLGTDESN AILDEVRNRL
     ETYWPFSVPN QNAVEIMDGK DEGVYAWITA NYLLGKIGEG AKSTDTLAVM DLGGASTQIV
     FEPKFPADST QELVDGEHKY QLSFGGKDFT LYQHSYLGYG LMRARRSVHN LVAFTWSFGH
     SNLDWDTLSE NEQVPNPCLS RGTTRRVELD PPGRTAVNVT MHGSNGGFDA CNRVVELVMA
     KDDVCEVKPC SFAGQYQPSL LDTFPHGQLL ALSYFTDRIK PLLSGRTADL KIADLTEMAK
     DVCDGPEAWR LRWGSDAAAM AELEDRPEYC LDLTFMNALL GLGYELGPER DLLVEKKLNG
     VELGWALGAG LALVEKATLT CTASANASM
//
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