ID U7Q114_SPOS1 Unreviewed; 762 AA.
AC U7Q114;
DT 22-JAN-2014, integrated into UniProtKB/TrEMBL.
DT 22-JAN-2014, sequence version 1.
DT 24-JAN-2024, entry version 36.
DE RecName: Full=Golgi apyrase {ECO:0008006|Google:ProtNLM};
GN ORFNames=HMPREF1624_02794 {ECO:0000313|EMBL:ERT01543.1};
OS Sporothrix schenckii (strain ATCC 58251 / de Perez 2211183) (Rose-picker's
OS disease fungus).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Sordariomycetidae; Ophiostomatales; Ophiostomataceae; Sporothrix.
OX NCBI_TaxID=1391915 {ECO:0000313|EMBL:ERT01543.1, ECO:0000313|Proteomes:UP000018087};
RN [1] {ECO:0000313|Proteomes:UP000018087}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 58251 / de Perez 2211183
RC {ECO:0000313|Proteomes:UP000018087};
RX PubMed=24855299; DOI=10.1128/genomea.00446-14;
RA Cuomo C.A., Rodriguez-Del Valle N., Perez-Sanchez L., Abouelleil A.,
RA Goldberg J., Young S., Zeng Q., Birren B.W.;
RT "Genome sequence of the pathogenic fungus Sporothrix schenckii (ATCC
RT 58251).";
RL Genome Announc. 2:E0044614-E0044614(2014).
CC -!- SIMILARITY: Belongs to the GDA1/CD39 NTPase family.
CC {ECO:0000256|ARBA:ARBA00009283, ECO:0000256|RuleBase:RU003833}.
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DR EMBL; KI440843; ERT01543.1; -; Genomic_DNA.
DR AlphaFoldDB; U7Q114; -.
DR STRING; 1391915.U7Q114; -.
DR eggNOG; KOG1386; Eukaryota.
DR HOGENOM; CLU_010246_3_0_1; -.
DR OrthoDB; 180318at2759; -.
DR Proteomes; UP000018087; 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:UP000018087};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 551..569
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT REGION 592..614
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 725..762
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 600..614
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 762 AA; 82861 MW; 8DA55D57CB3CF95A CRC64;
MGRKHRWGVI IDAGSSGSRL HVYRWKDPSK AIKDASKEEL HSLPKIKTKW TKKIRPGIST
FGERPAQVGA DHLQELIDYA LEVVPEDMVA DTPIFLMATA GMRFLPQLQQ TALLRETCSY
LQQHTKFSLP DCAQNIQVIP GETEGLYGWL AANYLLGGFD HPEEHNHGQN HNTYGFLDMG
GASAQIAFAP NTTEAAQHAD NLKLIRLRTL DGNPAEHRVF TATWLGFGVN KARESYVKSL
TDAHQDLITN GVDVPDPCMP KGLRTTLDGT LAGPAGSGIP TLVGTGDFAN CLIETKPLLA
KDTTCGEGSQ PCLIHDPVPS IDFNINHFVG VSEYYHSTHG FFGEKGDLAY DFSTYQKKVL
DFCNQDWSKI DAKIEGTSGS DKETRKKKDK DINRTLQDAQ QACFKASWVI NVLHEGIGIP
RIGLDKLPGL NVSGDAVEES KSSSYLTPFR PVDKIDSVEV SWTLGRILLY ASGQIPPRNV
RGSGGGSTIG AGKGVAVGFG SNSKDGSIPS DFTYAGSTWE PLKVGSGGSK SDDDWSDKAD
DIFDKAREKS AIPSAFFFLL IVLLFVFLLR KKERRVRLYN KFGTLIRRSR WPGSPRKPGR
FSSTIGSGSG STNNGNGALA GLAKMLFRRH SRDYERVLEE GQMDQFELND VDLEDTDLSS
EGSDGPGSAS SSIRLASAGA ARRSGLATPT LSVDKFDDLR TSAGSNSAMD RSGLVVRTES
RERLGLGGLG APSLQMLNAG RRSRATSPTR LKSPMMAPLQ ED
//