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Database: UniProt
Entry: G8BZV5_TETPH
LinkDB: G8BZV5_TETPH
Original site: G8BZV5_TETPH 
ID   G8BZV5_TETPH            Unreviewed;       660 AA.
AC   G8BZV5;
DT   25-JAN-2012, integrated into UniProtKB/TrEMBL.
DT   25-JAN-2012, sequence version 1.
DT   24-JAN-2024, entry version 47.
DE   RecName: Full=Golgi apyrase {ECO:0008006|Google:ProtNLM};
GN   Name=TPHA0L00770 {ECO:0000313|EMBL:CCE65433.1};
GN   OrderedLocusNames=TPHA_0L00770 {ECO:0000313|EMBL:CCE65433.1};
OS   Tetrapisispora phaffii (strain ATCC 24235 / CBS 4417 / NBRC 1672 / NRRL
OS   Y-8282 / UCD 70-5) (Yeast) (Fabospora phaffii).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Saccharomycetaceae; Tetrapisispora.
OX   NCBI_TaxID=1071381 {ECO:0000313|EMBL:CCE65433.1, ECO:0000313|Proteomes:UP000005666};
RN   [1] {ECO:0000313|EMBL:CCE65433.1, ECO:0000313|Proteomes:UP000005666}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 24235 / CBS 4417 / NBRC 1672 / NRRL Y-8282 / UCD 70-5
RC   {ECO:0000313|Proteomes:UP000005666};
RX   PubMed=22123960; DOI=10.1073/pnas.1112808108;
RA   Gordon J.L., Armisen D., Proux-Wera E., OhEigeartaigh S.S., Byrne K.P.,
RA   Wolfe K.H.;
RT   "Evolutionary erosion of yeast sex chromosomes by mating-type switching
RT   accidents.";
RL   Proc. Natl. Acad. Sci. U.S.A. 108:20024-20029(2011).
CC   -!- SIMILARITY: Belongs to the GDA1/CD39 NTPase family.
CC       {ECO:0000256|ARBA:ARBA00009283}.
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DR   EMBL; HE612867; CCE65433.1; -; Genomic_DNA.
DR   RefSeq; XP_003687867.1; XM_003687819.1.
DR   AlphaFoldDB; G8BZV5; -.
DR   STRING; 1071381.G8BZV5; -.
DR   GeneID; 11531701; -.
DR   KEGG; tpf:TPHA_0L00770; -.
DR   eggNOG; KOG1386; Eukaryota.
DR   HOGENOM; CLU_010246_3_3_1; -.
DR   OMA; WHDALFD; -.
DR   OrthoDB; 180318at2759; -.
DR   Proteomes; UP000005666; Chromosome 12.
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.
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:UP000005666};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        494..513
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   ACT_SITE        146
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   660 AA;  74437 MW;  CBE40D3DB9B7EE71 CRC64;
     MLTDGLLNEN YGIVIDAGSS GSRIHVYKWN NSKPDSEDAR NSVPQIHQEA DWTSKTTPGL
     SSYEKKPHKA FKKHIKPLLD YAEKIVPKNK IKETPVFIQA TAGMRLLPEK RQQQILSDLC
     DGFKHSSNFL MKNCEAQIQI IDGETEGLYG WLSLNYLKGM FNNYDAKSDT HFTFGFMDMG
     GASTQIAFSP SDKEQVKKHK EDIPTIYLRT LNGEIQKWDV FVSSWLGFGA NQARKRYFAQ
     LVNSLPENVN DYDDDNYATR KISDPCMPKG CESKFELYDK KFTAVGTGHS EQCEKLIYPL
     LLKQLPCIDE PCLFNGVHAP QIDFLNDKFV GVSEYWYTAN DVFKLGGEYN FQDFSSGVKE
     FCNSNWSDIK KKGDEGYYNS IPDSYLAASC FKANWVLNVL HEGFGLPFEK PADASQSMVD
     HPTFQSAEKI DSHEISWTLG RILLYASGSI LAGSKDAIVG IQPSKLSAQH FGKKFIPGSL
     EDFSNQIESS IGAIFNKLVV VLLVIFIVCF MLLKLKIINK SDLPPFINSI HETVQMKINS
     YYHYNRMVDS LSNLEEGISM EASNYVTKPT RDIDLKLRSK SMQGLDEISA KHGMDFGLKV
     RSKTHVGAPF NKSRNDTSPT SQGKLKTAFS LADFSKYKLE KITIRICHFC LLKSSLSNIM
//
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