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Database: UniProt
Entry: A0A061FVB2_THECC
LinkDB: A0A061FVB2_THECC
Original site: A0A061FVB2_THECC 
ID   A0A061FVB2_THECC        Unreviewed;       559 AA.
AC   A0A061FVB2;
DT   03-SEP-2014, integrated into UniProtKB/TrEMBL.
DT   03-SEP-2014, sequence version 1.
DT   27-MAR-2024, entry version 41.
DE   RecName: Full=apyrase {ECO:0000256|ARBA:ARBA00012148};
DE            EC=3.6.1.5 {ECO:0000256|ARBA:ARBA00012148};
DE   AltName: Full=ATP-diphosphatase {ECO:0000256|ARBA:ARBA00031428};
DE   AltName: Full=ATP-diphosphohydrolase {ECO:0000256|ARBA:ARBA00032306};
DE   AltName: Full=Adenosine diphosphatase {ECO:0000256|ARBA:ARBA00030084};
DE   AltName: Full=NTPDase {ECO:0000256|ARBA:ARBA00031370};
GN   ORFNames=TCM_012154 {ECO:0000313|EMBL:EOY20807.1};
OS   Theobroma cacao (Cacao) (Cocoa).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   rosids; malvids; Malvales; Malvaceae; Byttnerioideae; Theobroma.
OX   NCBI_TaxID=3641 {ECO:0000313|EMBL:EOY20807.1, ECO:0000313|Proteomes:UP000026915};
RN   [1] {ECO:0000313|EMBL:EOY20807.1, ECO:0000313|Proteomes:UP000026915}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. Matina 1-6 {ECO:0000313|Proteomes:UP000026915};
RX   PubMed=23731509; DOI=10.1186/gb-2013-14-6-r53;
RA   Motamayor J.C., Mockaitis K., Schmutz J., Haiminen N., Iii D.L.,
RA   Cornejo O., Findley S.D., Zheng P., Utro F., Royaert S., Saski C.,
RA   Jenkins J., Podicheti R., Zhao M., Scheffler B.E., Stack J.C., Feltus F.A.,
RA   Mustiga G.M., Amores F., Phillips W., Marelli J.P., May G.D., Shapiro H.,
RA   Ma J., Bustamante C.D., Schnell R.J., Main D., Gilbert D., Parida L.,
RA   Kuhn D.N.;
RT   "The genome sequence of the most widely cultivated cacao type and its use
RT   to identify candidate genes regulating pod color.";
RL   Genome Biol. 14:R53.1-R53.24(2013).
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=a ribonucleoside 5'-triphosphate + 2 H2O = a ribonucleoside
CC         5'-phosphate + 2 H(+) + 2 phosphate; Xref=Rhea:RHEA:36795,
CC         ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:43474,
CC         ChEBI:CHEBI:58043, ChEBI:CHEBI:61557; EC=3.6.1.5;
CC         Evidence={ECO:0000256|ARBA:ARBA00000211};
CC   -!- SIMILARITY: Belongs to the GDA1/CD39 NTPase family.
CC       {ECO:0000256|ARBA:ARBA00009283}.
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DR   EMBL; CM001881; EOY20807.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A061FVB2; -.
DR   EnsemblPlants; EOY20807; EOY20807; TCM_012154.
DR   Gramene; EOY20807; EOY20807; TCM_012154.
DR   eggNOG; KOG1386; Eukaryota.
DR   HOGENOM; CLU_010246_2_2_1; -.
DR   InParanoid; A0A061FVB2; -.
DR   OMA; TVNTTIW; -.
DR   Proteomes; UP000026915; Chromosome 3.
DR   GO; GO:0016020; C:membrane; IBA:GO_Central.
DR   GO; GO:0004050; F:apyrase activity; IEA:UniProtKB-EC.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0017110; F:nucleoside diphosphate phosphatase activity; IBA:GO_Central.
DR   GO; GO:0009134; P:nucleoside diphosphate catabolic process; IBA:GO_Central.
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:SF92; APYRASE; 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:UP000026915};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        21..43
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        510..530
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   ACT_SITE        199
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR600407-1"
FT   BINDING         230..234
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR600407-2"
SQ   SEQUENCE   559 AA;  61894 MW;  392D57C0D6157B4E CRC64;
     MEPKSPSKVK LSVMGFKRWK RVLKVFTFGF LILLSCIGVY LAFNFVKAWN VLESSYYTVV
     VDCGSTGTRV NVFEWEKGGL VNQGLPYLVH SYPDYSTKSP LWRNSCHYHC MQTEPGLDKF
     VGNASGMRAS LEPLIAWAEQ MVPHERHGDT PIIVLATAGL RRLAAKDARQ VLDDVEIVVR
     GHSFVYSKNW IRVLTGKEEA YYGWVALNYK LGSLGNSLKA STFGLLDLGG SSLQVVVEVA
     EENGNENVMT SNIGSTDHNI LAYSLPAFGL TEAFDRTVVM LSQNQTDRGN TTNRFEVRHP
     CLSSDFVQNY TCSGCPMPNV TDLENSESLM YKSQFSLTYL VGDPNWEQCK ELVRAAAMNY
     SGSDWSHQIV GRNCEANSSP YGGSNMLNLT AVAHHSGRFH ALSGFFVVND MLHLSPRASV
     TEIWEKGEQL CSRSSTELSS ISQRQTYAGQ SCFRVPYVAS LIEDSLCLGN GEIVFGPGDV
     SWTLGAALIH GLDSIETPAS ISTTKDMDIF SSPVFLFVLL LFLLFVVYCS QITLPMLGRK
     VADVGVSLPS YVHPRRRQT
//
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