ID A0A2B7YG14_9EURO Unreviewed; 708 AA.
AC A0A2B7YG14;
DT 20-DEC-2017, integrated into UniProtKB/TrEMBL.
DT 20-DEC-2017, sequence version 1.
DT 24-JAN-2024, entry version 20.
DE RecName: Full=Golgi apyrase {ECO:0008006|Google:ProtNLM};
GN ORFNames=AJ80_03883 {ECO:0000313|EMBL:PGH19547.1};
OS Polytolypa hystricis UAMH7299.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Onygenales; Onygenales incertae sedis; Polytolypa.
OX NCBI_TaxID=1447883 {ECO:0000313|EMBL:PGH19547.1, ECO:0000313|Proteomes:UP000224634};
RN [1] {ECO:0000313|EMBL:PGH19547.1, ECO:0000313|Proteomes:UP000224634}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=UAMH7299 {ECO:0000313|EMBL:PGH19547.1,
RC ECO:0000313|Proteomes:UP000224634};
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 -!- SIMILARITY: Belongs to the GDA1/CD39 NTPase family.
CC {ECO:0000256|ARBA:ARBA00009283}.
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:PGH19547.1}.
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DR EMBL; PDNA01000046; PGH19547.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2B7YG14; -.
DR STRING; 1447883.A0A2B7YG14; -.
DR OrthoDB; 180318at2759; -.
DR Proteomes; UP000224634; 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 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.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|PIRSR:PIRSR600407-2};
KW Membrane {ECO:0000256|SAM:Phobius};
KW Nucleotide-binding {ECO:0000256|PIRSR:PIRSR600407-2};
KW Reference proteome {ECO:0000313|Proteomes:UP000224634};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 532..551
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT REGION 618..640
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 668..708
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 621..640
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 684..708
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 708 AA; 77798 MW; CE3105636B1D3854 CRC64;
MVPWRYAVIL DAGSSGTRVH VYRWPDSAAA REAGRRKVLK SLPAIKTKSS WSKKIKPGVS
SFSKAPENVG ADHLKPLLDH ALDIVPQDHV ADTPIFVLAT AGMRLLPDSE QKAILKKVCS
HIQETTHFLL PDCDSHVQVI DGKTEGLYGW TATNYLLGSF DAPQLHDHGK DHHTYGFLDM
GGASSQIAFA PNATEAQKHA DDLTLLRLRK VNGRTAEHKV FVTSWLGFGV HEARNRYVKA
LLETSGSLDT GKHEDPCLPA GLKMAVDGTM LEADSAVAVN DPYLVGTGKF DQCLLKTYPL
LEKDAPCEDE PCLIHGVHVP AIDFDVNHFV GISGFWHTTH EIFASAHKDE AYDHTTYQER
VKEFCSLKWS DMQAGVLTSK WGKKVDEKTA YEVCFKASWL INILHDGIGV PRIDIDTMNG
PGYNGTKAVS TNEKPEGYLD AFQAVDKIDA TEVSWTLGKA VLYSSSQVRP ARDDDLPVGF
GSNVPGVPDD FQYPGPKLPP IPHLEVIESG NTTTTDDHWH DTLFNGDTPR RIPGVFLFLL
IVLIALFFLC GRERRSRIYR RLYLSSHRGG GAYRKRPLFG GKLPFFGHRN TVAYERVLEE
GAPDFELDGF ASEDDLSPKA ARFPSSSSSS SSRSSQGLKY GFDNGSSQSV GLGIGGHAAL
DRAGLVVRTE SREQLVPPAL NPTFNGRRSR TSSPVRHKAP KTSGFSND
//
