ID A0A2K1QUW1_9PEZI Unreviewed; 691 AA.
AC A0A2K1QUW1;
DT 28-MAR-2018, integrated into UniProtKB/TrEMBL.
DT 28-MAR-2018, sequence version 1.
DT 24-JAN-2024, entry version 23.
DE SubName: Full=Golgi apyrase {ECO:0000313|EMBL:PNS18809.1};
GN ORFNames=CAC42_5348 {ECO:0000313|EMBL:PNS18809.1};
OS Sphaceloma murrayae.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC Dothideomycetidae; Myriangiales; Elsinoaceae; Sphaceloma.
OX NCBI_TaxID=2082308 {ECO:0000313|EMBL:PNS18809.1, ECO:0000313|Proteomes:UP000243797};
RN [1] {ECO:0000313|EMBL:PNS18809.1, ECO:0000313|Proteomes:UP000243797}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CQ-2017a {ECO:0000313|EMBL:PNS18809.1,
RC ECO:0000313|Proteomes:UP000243797};
RA Cheng Q.;
RT "Draft genome sequence of a variant of Elsinoe murrayae.";
RL Submitted (JUN-2017) to the EMBL/GenBank/DDBJ databases.
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:PNS18809.1}.
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DR EMBL; NKHZ01000039; PNS18809.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2K1QUW1; -.
DR STRING; 2082308.A0A2K1QUW1; -.
DR InParanoid; A0A2K1QUW1; -.
DR OrthoDB; 180318at2759; -.
DR Proteomes; UP000243797; Unassembled WGS sequence.
DR GO; GO:0005794; C:Golgi apparatus; IEA:UniProt.
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:SF121; NUCLEOSIDE-DIPHOSPHATASE MIG-23; 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:UP000243797};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 522..541
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT REGION 616..691
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 664..678
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 145
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR600407-1"
FT BINDING 182..186
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PIRSR:PIRSR600407-2"
SQ SEQUENCE 691 AA; 76131 MW; 75AD2551201D13C7 CRC64;
MGKWRYGVIL DAGSSGTRAY VYRWLKPEKA RKKADKDDLG KLPELHTKKK WTKKIHPGVS
TFGEKPEMVG NDHLKELVEH ALQVVPKDDV EDTPIFMLAT AGMRLLPDQQ RKDVLSNVCS
YLRRTTRFQL PDCDLHIQVI PGSTEGLYGW VAANYLLGGF DDADEHDHGK DHHTYGFLDM
GGASAQIAFA PNVTEAEKHA NDLTLLRLRT IGGQQKEYRV FVTTWLEYGV NEARRRYLKA
LLESSPQAKE LPDPCLPTGL RETKTGEVVA AGSKEDKSEA LLLGTGKFEE CLRQTFPLLD
KDAPCADKPC LLHGVHVPAI DFDVNHFVGV SEYWHTTHSV FEMGHKDMAY DFKTYQTKVS
EFCSQDWSAI KSGVASQKWG KKVDETTAAE VCFKASWLIN MLHDGIGVPR VGLEQSKDSD
VKAENKTKQA LESAKHRGFL DAFQAVDKID GTEVSWTLGK MVLYAASQHP PEDHAMAVGF
GSNVAGQKLP SDFQYAGGNE PQLPDDLEWH DKLFASAGNR RVPGLLLFSA ILLLALFLLC
GRERRQNLIS KLRPASPSRF SKKKRGIFSR IFSKGAKYAP LAPSGPEDFE LGDVDSDSDI
EADKASIKSA RASGWATPKL QGASDSPALG PGTGKNYFEY PAGPGLTSRT ESRERLGLAP
GLGLNSSGSR SRHASPTRRS SPLGPIKPDL D
//
