ID Q84UE1_MEDTR Unreviewed; 467 AA.
AC Q84UE1;
DT 01-JUN-2003, integrated into UniProtKB/TrEMBL.
DT 01-JUN-2003, sequence version 1.
DT 27-MAR-2024, entry version 76.
DE SubName: Full=Apyrase-like protein {ECO:0000313|EMBL:AAO23004.1};
GN Name=APY1;3 {ECO:0000313|EMBL:AAO23004.1};
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:AAO23004.1};
RN [1] {ECO:0000313|EMBL:AAO23004.1}
RP NUCLEOTIDE SEQUENCE.
RX PubMed=12644663; DOI=10.1104/pp.102.010926;
RA Navarro-Gochicoa M.T., Camut S., Niebel A., Cullimore J.V.;
RT "Expression of the apyrase-like APY1 genes in roots of Medicago truncatula
RT is induced rapidly and transiently by stress and not by Sinorhizobium
RT meliloti or Nod factors.";
RL Plant Physiol. 131:1124-1136(2003).
CC -!- SIMILARITY: Belongs to the GDA1/CD39 NTPase family.
CC {ECO:0000256|ARBA:ARBA00009283, ECO:0000256|RuleBase:RU003833}.
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DR EMBL; AY180379; AAO23004.1; -; mRNA.
DR AlphaFoldDB; Q84UE1; -.
DR ProMEX; Q84UE1; -.
DR EnsemblPlants; AES80802; AES80802; MTR_7g085150.
DR Gramene; AES80802; AES80802; MTR_7g085150.
DR OMA; LSYKDEW; -.
DR ExpressionAtlas; Q84UE1; 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}.
FT ACT_SITE 179
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR600407-1"
FT BINDING 209..213
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PIRSR:PIRSR600407-2"
SQ SEQUENCE 467 AA; 51736 MW; FFEDEC128DB45086 CRC64;
MVLLWQNTKN MMNFMTLITF LLFIMPSISY SQYLGNNILL TNRKIFPKQE PISSYAVVFD
AGSTGSRVHV YHFDQNLNLL HVGKDVEFYN KTTPGLSAYA DNPEEAAKSL IPLLEQAESV
VPEDQRSKTP IRLGATAGLR LLNGDASEKI LQSVRDLFSN RSTFNVQPDA VSIIDGTQEG
SYLWVTVNYA LGKLGKKFTK TVGVMDLGGG SVQMAYAVSK YTAKNAPKVA DGEDPYIKKL
VLKGKKYDLY VHSYLHFGRE ASRAEILKVT HNSPNPCILA GFDGTYTYAG EEFKANAPAS
GANFKKCKKI VREALKLNYP CPYQNCTFGG IWSGGGGSGQ RILFAASSFF YLAEDIGLVD
PNTPYSLTLR PVDLETEAKK ACTLNLEEAK STYPLLVDFN IVEYVCMDLI YQYVLLVDGF
GLDPLQEITA GKQIEYQDSL VEAAWPLGNA VEAISSLPKF ERLMYFI
//
