ID   A0A2B7ZIB9_9EURO        Unreviewed;       563 AA.
AC   A0A2B7ZIB9;
DT   20-DEC-2017, integrated into UniProtKB/TrEMBL.
DT   20-DEC-2017, sequence version 1.
DT   27-MAR-2024, entry version 20.
DE   RecName: Full=guanosine-diphosphatase {ECO:0000256|ARBA:ARBA00038903};
DE            EC=3.6.1.42 {ECO:0000256|ARBA:ARBA00038903};
GN   ORFNames=GX50_04094 {ECO:0000313|EMBL:PGH33111.1};
OS   Emmonsia crescens.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Onygenales; Ajellomycetaceae; Emmonsia.
OX   NCBI_TaxID=73230 {ECO:0000313|EMBL:PGH33111.1, ECO:0000313|Proteomes:UP000226031};
RN   [1] {ECO:0000313|EMBL:PGH33111.1, ECO:0000313|Proteomes:UP000226031}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=UAMH4076 {ECO:0000313|EMBL:PGH33111.1,
RC   ECO:0000313|Proteomes:UP000226031};
RA   Munoz J.F., Mcewen J.G., Clay O.K., Cuomo C.A.;
RT   "Comparative genomics in systemic dimorphic fungi from Ajellomycetaceae.";
RL   Submitted (OCT-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:PGH33111.1}.
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DR   EMBL; PDND01000072; PGH33111.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A2B7ZIB9; -.
DR   STRING; 73230.A0A2B7ZIB9; -.
DR   VEuPathDB; FungiDB:EMCG_00331; -.
DR   OrthoDB; 180318at2759; -.
DR   Proteomes; UP000226031; 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:UP000226031};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        75..93
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   REGION          25..52
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        255
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR600407-1"
FT   BINDING         286..290
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR600407-2"
SQ   SEQUENCE   563 AA;  61485 MW;  EF584619E9FD4CFF CRC64;
     MSTGVHARAR VGIWSYLPFG SNPRRRSVSL PAKSTRDPFE KPGRHSGDPL RSTTTFSFRD
     TFTVVEMTQS QRTRYIKTAG VIAVLLLFLY VLVPGGQPSP ASLKTLVSTS KCTKPHDSSK
     PLIQYALMID AGSTGSRIHV YRFNNCGPTP ELENEDFKMT EKKKGGAGLS SYAEDPEAAA
     RSLDPLMQVA LKSVPQEYQS CSPVAVKATA GLRFLGQETS DKILDAVRNR LETVYPFPVV
     SKEQGGVEIM DGKYEGVYAW ITTNYLLGNI GTKERTPTAA VFDLGGGSTQ IVFEPTFKGV
     PGAAPEKLAD GAHKFSLNFG GRNFDLYQHS HLGYGLMKAR DTIHKAIVEA KHESSPTDQT
     WLSKPLVNPC LSTGTSLTVN VTLGEGHPLG EVVEVKMAGP KDISSAAQCR GIADKILKKD
     AECKLAPCSF NGAHQPPLQK TFAQEDLFIM SYFYDRTAPL GMPESFTLRD LQDLTATVCS
     GKGSWGVFEG IKDALNELQE RPEHCLDLSF MLSLLHTGYD LPLNRQVKIA KQINGNELGW
     CLGASLPLLN KESGWQCRVK QVS
//