ID B9WGR5_CANDC Unreviewed; 697 AA.
AC B9WGR5;
DT 24-MAR-2009, integrated into UniProtKB/TrEMBL.
DT 24-MAR-2009, sequence version 1.
DT 24-JAN-2024, entry version 67.
DE SubName: Full=Golgi apyrase, putative {ECO:0000313|EMBL:CAX42441.1};
GN OrderedLocusNames=Cd36_45750 {ECO:0000313|CGD:CAL0000160002};
GN ORFNames=CD36_45750 {ECO:0000313|EMBL:CAX42441.1};
OS Candida dubliniensis (strain CD36 / ATCC MYA-646 / CBS 7987 / NCPF 3949 /
OS NRRL Y-17841) (Yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Debaryomycetaceae; Candida/Lodderomyces clade; Candida.
OX NCBI_TaxID=573826 {ECO:0000313|EMBL:CAX42441.1, ECO:0000313|Proteomes:UP000002605};
RN [1] {ECO:0000313|EMBL:CAX42441.1, ECO:0000313|Proteomes:UP000002605}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CD36 / ATCC MYA-646 / CBS 7987 / NCPF 3949 / NRRL Y-17841
RC {ECO:0000313|Proteomes:UP000002605};
RX PubMed=19745113; DOI=10.1101/gr.097501.109;
RA Jackson A.P., Gamble J.A., Yeomans T., Moran G.P., Saunders D., Harris D.,
RA Aslett M., Barrell J.F., Butler G., Citiulo F., Coleman D.C.,
RA de Groot P.W.J., Goodwin T.J., Quail M.A., McQuillan J., Munro C.A.,
RA Pain A., Poulter R.T., Rajandream M.A., Renauld H., Spiering M.J.,
RA Tivey A., Gow N.A.R., Barrell B., Sullivan D.J., Berriman M.;
RT "Comparative genomics of the fungal pathogens Candida dubliniensis and
RT Candida albicans.";
RL Genome Res. 19:2231-2244(2009).
CC -!- SIMILARITY: Belongs to the GDA1/CD39 NTPase family.
CC {ECO:0000256|ARBA:ARBA00009283, ECO:0000256|RuleBase:RU003833}.
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DR EMBL; FM992691; CAX42441.1; -; Genomic_DNA.
DR RefSeq; XP_002420218.1; XM_002420173.1.
DR AlphaFoldDB; B9WGR5; -.
DR GeneID; 8047739; -.
DR KEGG; cdu:CD36_45750; -.
DR CGD; CAL0000160002; Cd36_45750.
DR VEuPathDB; FungiDB:CD36_45750; -.
DR eggNOG; KOG1386; Eukaryota.
DR HOGENOM; CLU_010246_3_3_1; -.
DR OrthoDB; 180318at2759; -.
DR Proteomes; UP000002605; Chromosome 4.
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.
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 Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 519..537
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT REGION 676..697
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 158
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR600407-1"
FT BINDING 194..198
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PIRSR:PIRSR600407-2"
SQ SEQUENCE 697 AA; 78753 MW; 33CAA3F2B6E4953B CRC64;
MSNLKRSDNS NEKYGIVIDS GSSGSRIQIY KWTDQQFELK SSKDQSVLQS PPKITQEKGW
TKKITPGIST YNSKDKSGRI WQDHYSELLK FAEDIIPSDK QPDTPVFVLS TAGMRLLSKK
DQKSILKETC SGIKQNTNFY IPTENCENFV EIIDGSTEGI YGWLGLNYLM KQFNNYDSSQ
DSLHESIGFM DMGGASTQIA FVPSSKEEVI KHKEDLSTVT LRNINGETQT WDLFVATWLG
FGANEARKRF LNQLINLAIV NGENWNNEIN DPCLPKGASM KYEHEKKQYL VQGVGNYEMC
IKTIYPLLMK NMVCIDEPCL FNGIHGPKFN FEKDKFIGIS EYWYTANDIF QSGGEYNFKA
FNAKVKEYCE SNWDDILKNS KQGQYSNLDP DKFLKDACFK ASWVMNILHE GFELPRIGFE
TEKEDQTEED KKITNSHVPF KSADSVEGEE LSWTLGKILL FASSQIEPKE GDADAKQIGI
YPSEISGRKF VPGGGSLSGE GDYSTDDEDD DFGSQFSHIL YSLIFIFLLL FFLFHFGKSH
FGRWSNKLRR FQIPVEVKRA VNTIGSKIPG VRHYFENIVM FSDLQDQSII LEEGIFDNTS
NNTNFKTLQN QQQPASASVL RTRSAIGLNE NSGNDYKGGS GQSLTNLSSY NPKGNSYYNK
SFSSPKKNIY ISANNSRESL ARGSSNASIP RSKSSLD
//