ID A0A2W1FAU2_9PLEO Unreviewed; 579 AA.
AC A0A2W1FAU2;
DT 12-SEP-2018, integrated into UniProtKB/TrEMBL.
DT 12-SEP-2018, sequence version 1.
DT 27-MAR-2024, entry version 27.
DE RecName: Full=guanosine-diphosphatase {ECO:0000256|ARBA:ARBA00038903};
DE EC=3.6.1.42 {ECO:0000256|ARBA:ARBA00038903};
GN ORFNames=Ptr86124_012777 {ECO:0000313|EMBL:KAI1508289.1}, PtrM4_06006
GN {ECO:0000313|EMBL:PWO12957.1}, PtrM4_103560
GN {ECO:0000313|EMBL:KAF7570354.1};
OS Pyrenophora tritici-repentis.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC Pleosporomycetidae; Pleosporales; Pleosporineae; Pleosporaceae;
OC Pyrenophora.
OX NCBI_TaxID=45151 {ECO:0000313|EMBL:PWO12957.1};
RN [1] {ECO:0000313|EMBL:PWO12957.1, ECO:0000313|Proteomes:UP000245464}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=M4 {ECO:0000313|EMBL:PWO12957.1,
RC ECO:0000313|Proteomes:UP000245464};
RX PubMed=29685100; DOI=10.1186/s12864-018-4680-3;
RA Moolhuijzen P., See P.T., Hane J.K., Shi G., Liu Z., Oliver R.P.,
RA Moffat C.S.;
RT "Comparative genomics of the wheat fungal pathogen Pyrenophora tritici-
RT repentis reveals chromosomal variations and genome plasticity.";
RL BMC Genomics 19:279-279(2018).
RN [2] {ECO:0000313|EMBL:KAI1508289.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=86-124 {ECO:0000313|EMBL:KAI1508289.1};
RA Moolhuijzen P.M., Moffat C.S.;
RL Submitted (MAY-2021) to the EMBL/GenBank/DDBJ databases.
RN [3] {ECO:0000313|EMBL:KAI1508289.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=86-124 {ECO:0000313|EMBL:KAI1508289.1};
RA Moolhuijzen P., See P.T., Shi G., Powell H.R., Cockram J., Jorgensen L.N.,
RA Benslimane H., Strelkov S.E., Turner J., Liu Z., Moffat C.S.;
RT "A global pangenome for the wheat fungal pathogen Pyrenophora tritici-
RT repentis and prediction of effector protein structural homology.";
RL bioRxiv 0:0-0(2022).
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:PWO12957.1}.
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DR EMBL; NQIK02000005; KAF7570354.1; -; Genomic_DNA.
DR EMBL; NRDI02000027; KAI1508289.1; -; Genomic_DNA.
DR EMBL; NQIK01000004; PWO12957.1; -; Genomic_DNA.
DR OMA; WTCRIKE; -.
DR Proteomes; UP000245464; Unassembled WGS sequence.
DR Proteomes; UP000249757; 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 Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 83..101
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT REGION 30..65
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 41..64
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 271
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR600407-1"
FT BINDING 302..306
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PIRSR:PIRSR600407-2"
SQ SEQUENCE 579 AA; 64018 MW; A283848AA3B4CCB6 CRC64;
MSSGVEVPGR SQRRPGIWSY FSFSGPRRRV SVSLPRNFDP NRDSSDPHEK PDRHSRHRST
YSDAFMNEHK GGAVMNQGQR LRYLKTGGVI AFILFALYMI APRDGLSRPT VSQPSGGNTA
AGDAKAQCTK SYSKDKPLIQ YAMMIDAGST GSRIHVYKFN NCGPSPELEG ENFEMTPKKQ
GGSGLSAYGD DPEAAARSLD VLMDVALKHV PKEYQSCSPI AVKATAGLRK LGEKKSNDIL
AAVRRHLEND YPFPLVSEEK KGVEVMPGEM EGVYAWITVN YLLGKIGGPD KNPTAAVLDL
GGGSTQIIFE PTFPDKPRGG LPTKLAEGDH KYSLNFGNRN FDLYQHSYLG YGLMEARNNL
HSTILAGLHE THKDNRDYLK KPIVNPCIAP GMTREIEVHM PKGHELGDSI TVNMTGPSHP
SPTQCRGLAE KTLHKDDECA IAPCAFRGVH QPPFDQTFAT EAVYLLSYFY DRTQDLGMPE
SFTLRELQDL ADKVCSGEKG WDVFSAVPKA LDELKGRPEW CLDLNFQYEL LRSGYGMPID
REVKIAKKIK GNELGWCLGA SLPLLEANSG WQCKIKQVE
//
