ID   A0A0G4MDH6_9PEZI        Unreviewed;       852 AA.
AC   A0A0G4MDH6;
DT   16-SEP-2015, integrated into UniProtKB/TrEMBL.
DT   16-SEP-2015, sequence version 1.
DT   27-MAR-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=BN1708_005688 {ECO:0000313|EMBL:CRK32297.1};
OS   Verticillium longisporum.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Hypocreomycetidae; Glomerellales; Plectosphaerellaceae; Verticillium.
OX   NCBI_TaxID=100787 {ECO:0000313|EMBL:CRK32297.1, ECO:0000313|Proteomes:UP000044602};
RN   [1] {ECO:0000313|EMBL:CRK32297.1, ECO:0000313|Proteomes:UP000044602}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=VL1 {ECO:0000313|EMBL:CRK32297.1};
RA   Wang D.B., Wang M.;
RL   Submitted (MAY-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}.
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DR   EMBL; CVQH01022083; CRK32297.1; -; Genomic_DNA.
DR   STRING; 100787.A0A0G4MDH6; -.
DR   OrthoDB; 180318at2759; -.
DR   Proteomes; UP000044602; 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; 2.
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; 2.
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:UP000044602};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        49..67
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   REGION          1..26
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          76..102
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        240
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR600407-1"
FT   BINDING         271..275
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR600407-2"
SQ   SEQUENCE   852 AA;  93388 MW;  D6FC9ACD6A3FB890 CRC64;
     MRRSSVSLPH TKNARDPFEK PGRFAPAQKP GLLGALKAVI MSQTQKARWI KTAAVVFFIV
     LGFIWLSPKG VDMYNNRVSP TKSNDGQVPS DNSYGTDRCT KSSSKSKPIV QYVLMIDAGS
     TGSRIHVYKF NNCGAAPELE KEEFKMTEKS VGGLSKYKDD PEAAAKTLDA LMDVAMKEVP
     DKLKGCSPVA VKATAGLRMV GAEAADKILK TVRSHLETKY PFPVVSEEQN GVAIMDGSDE
     GVYAWITTNY LLGKIGGPDK NPTAAVFDLG GGSTQIVFEP TFKGPAGGMP EKLSEGDHKY
     NLDFGGQKFE LYQHSHLGYG LMAARDALHT VFLDELLXSK KNDKSVLEGP VVHPCIAPGF
     SKETEVKLPE NHQLGQSISL NFTGPTNAAP AQCRALAERI LKKEADCKLA PCSFNGIHQP
     SLAKTFGRED VYIFSFFYDR TKPLGMPDSF TLREMHDLTN TVCGGEQSWD LFSTIPGALD
     ELRDRPDHCL DLNFMMALLH TGYEMPIERE VKIAKKIKGN ELGWCLGASL PLLAPGSGWE
     CKIKQGVYAW ITTNYLLGKI GGPDKNPTAA VFDLGGGSTQ IVFEPTFKGP AGGMPEKLSE
     GDHKYNLDFG GQKFELYQHS HLGYGLMAAR DALHTVFLDE LLESKKNDKS VLEGPVVHPC
     IAPGFAKETE VKLPENRQLG QSISLNFTGP TNAAPAQCRA LAERILKKEA DCKLAPCSFN
     GIHQPSLAKT FGREDVYIFS FFYDRTKPLG MPDSFTLREM HDLTNTVCGG EQSWDLFSTI
     PGALDELRDR PDHCLDLNFM MALLHTGYEM PIEREVKIAK KIKGNELGWC LGASLPLLAP
     GSGWECNVKQ VQ
//