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Database: UniProt
Entry: M1UZD5_MEDTR
LinkDB: M1UZD5_MEDTR
Original site: M1UZD5_MEDTR 
ID   M1UZD5_MEDTR            Unreviewed;       456 AA.
AC   M1UZD5;
DT   01-MAY-2013, integrated into UniProtKB/TrEMBL.
DT   01-MAY-2013, sequence version 1.
DT   27-MAR-2024, entry version 28.
DE   SubName: Full=Apyrase {ECO:0000313|EMBL:BAM84271.1};
GN   Name=MtAPY1;1 {ECO:0000313|EMBL:BAM84271.1};
OS   Medicago truncatula (Barrel medic) (Medicago tribuloides).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   rosids; fabids; Fabales; Fabaceae; Papilionoideae; 50 kb inversion clade;
OC   NPAAA clade; Hologalegina; IRL clade; Trifolieae; Medicago.
OX   NCBI_TaxID=3880 {ECO:0000313|EMBL:BAM84271.1};
RN   [1] {ECO:0000313|EMBL:BAM84271.1}
RP   NUCLEOTIDE SEQUENCE.
RA   Toyoda K., Kawakami E., Nagai H., Shiobara-Komatsu T., Tanaka K.,
RA   Inagaki Y., Ichinose Y., Shiraishi T.;
RT   "Expression of Medicago truncatula ecto-apyrase MtAPY1;1 in leaves of
RT   Nicotiana benthamiana restricts necrotic lesions induced by a virulent
RT   fungus.";
RL   J. Gen. Plant Pathol. 80:222-229(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; AB793274; BAM84271.1; -; mRNA.
DR   AlphaFoldDB; M1UZD5; -.
DR   ExpressionAtlas; M1UZD5; differential.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
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:SF80; GDA1_CD39 NUCLEOSIDE PHOSPHATASE FAMILY PROTEIN; 1.
DR   Pfam; PF01150; GDA1_CD39; 1.
DR   PROSITE; PS01238; GDA1_CD39_NTPASE; 1.
PE   2: Evidence at transcript level;
KW   ATP-binding {ECO:0000256|PIRSR:PIRSR600407-2};
KW   Hydrolase {ECO:0000256|RuleBase:RU003833};
KW   Nucleotide-binding {ECO:0000256|PIRSR:PIRSR600407-2};
KW   Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..22
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           23..456
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5004018130"
FT   ACT_SITE        169
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR600407-1"
FT   BINDING         199..203
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR600407-2"
SQ   SEQUENCE   456 AA;  50120 MW;  6F1917F44F52DF55 CRC64;
     MEFLITLITT VLLLLMPAIT SSQYLGNNLL TNRKIFQQQE TISSYAVVFD AGSTGSRIHV
     YHFDQNLDLL HIGKDVEFFN KITPGLSSYA NDPEHAAKSL IPLLQQAENV VPIDLHHKTP
     IRLGATAGLR LLNGDASEKI LQAVRDMFSN RSTFNVQPDA VSIIDGTQEG SYLWVTVNYA
     LGNLGKKYTK TVGVMDLGGG SVQMAYAVSK KTAKNAPKAA DGVDPYIKKL VLKGKPYDLY
     VHSYLHFGRE ASRAEIMKVT RSSPNTCILA GFDGTYTYAG VEFKAKAPAS GANFNGCKKI
     IRKALKLNYP CPYQNCTFGG IWNGGGGNGQ KHLFASSSFF YLPEDVGMVN PKTPNFKIRP
     VDLVSEAKKA CALNFEDAKS TYPFLAKKNI ASYVCMDLIY QYVLLVDGFG LDPLQEITSG
     KEIEYQDAVL EAAWALGNAV EAISSLPKFE RMMYFV
//
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