ID A0A3M2SBU2_9HYPO Unreviewed; 668 AA.
AC A0A3M2SBU2;
DT 13-FEB-2019, integrated into UniProtKB/TrEMBL.
DT 13-FEB-2019, sequence version 1.
DT 24-JAN-2024, entry version 20.
DE RecName: Full=Golgi apyrase {ECO:0008006|Google:ProtNLM};
GN ORFNames=CDV36_005659 {ECO:0000313|EMBL:RMJ14685.1};
OS Fusarium kuroshium.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Hypocreales; Nectriaceae; Fusarium;
OC Fusarium solani species complex.
OX NCBI_TaxID=2010991 {ECO:0000313|EMBL:RMJ14685.1, ECO:0000313|Proteomes:UP000277212};
RN [1] {ECO:0000313|EMBL:RMJ14685.1, ECO:0000313|Proteomes:UP000277212}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=UCR3666 {ECO:0000313|EMBL:RMJ14685.1};
RA Stajich J.E., Carrillo J., Kijimoto T., Eskalen A., O'Donnell K.,
RA Kasson M.;
RT "Comparative genomic analysis of Ambrosia Fusariam Clade fungi.";
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:RMJ14685.1}.
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DR EMBL; NKUJ01000080; RMJ14685.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A3M2SBU2; -.
DR STRING; 2010991.A0A3M2SBU2; -.
DR Proteomes; UP000277212; 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:UP000277212};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 506..524
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT REGION 470..497
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 575..668
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 644..668
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 144
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR600407-1"
FT BINDING 181..185
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PIRSR:PIRSR600407-2"
SQ SEQUENCE 668 AA; 73096 MW; C503FE258715825E CRC64;
MGKSSQYGVV LDAGSSGTRV YIYKWKNHAA AVKDASVTQL KTLPKIKLKE SKKIHPGVST
FADKPSEIGV NHLDELIKIA LKEVPADKVS ETPIYLMATA GMRLLPKPKQ TALLQSMCTY
LQASTKFILP DCNAHIQVIS GETEGLYGWI AANYLLGGFD HPEEHDHGKN HHTYGFLDMG
GASAQIAFAP NATESEKHSN DLKLVRMRTL DGSPAEYKVF TATWLGFGAN EARNRYVESL
WDQYGGKTIQ EVPDPCMPVG LTTTLRGDYV EGKVNEPVLV GTGKFDECLS VTYPLLGKDK
PCPDQPCLVN GQHVPGIDFD INHFVGVSEY WHTTHGVFGG KHTAYDLASY QSIVHDFCTS
DWQDIESELE KRKKSPEKKA EEARAACFKA SWLINMLYDG IGIPRVGLEG GHGNSTAKET
DKMEDPFKPV DKIDGIELSW TLGKMVLYAA GQVPPQGTAL PVGFGTNVEK GTPDDFEHAG
SVPIGSHSGD DDDDDLDDIL KKPGSSTSGI IAFVFVLLLV AYLLRKPERR RKIFGMVHRR
RRSGRPGRSL ASKLFGRNSL GSYERVMEEG DLSDFELGDV DSDENDHSDS SSNGSRKGRA
SGLATPSIGL GRADDLLRPP LAMDRAGLVI RTESRERLSP SLLSAGRKSR NGSPTRTKSP
FMTPLQED
//
