ID A0A4P1QT77_LUPAN Unreviewed; 722 AA.
AC A0A4P1QT77;
DT 03-JUL-2019, integrated into UniProtKB/TrEMBL.
DT 03-JUL-2019, sequence version 1.
DT 24-JAN-2024, entry version 15.
DE RecName: Full=Apyrase 7 {ECO:0008006|Google:ProtNLM};
GN ORFNames=TanjilG_25452 {ECO:0000313|EMBL:OIV94390.1};
OS Lupinus angustifolius (Narrow-leaved blue lupine).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; fabids; Fabales; Fabaceae; Papilionoideae; 50 kb inversion clade;
OC genistoids sensu lato; core genistoids; Genisteae; Lupinus.
OX NCBI_TaxID=3871 {ECO:0000313|EMBL:OIV94390.1, ECO:0000313|Proteomes:UP000188354};
RN [1] {ECO:0000313|EMBL:OIV94390.1, ECO:0000313|Proteomes:UP000188354}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Tanjil {ECO:0000313|Proteomes:UP000188354};
RC TISSUE=Whole plant {ECO:0000313|EMBL:OIV94390.1};
RX PubMed=27557478; DOI=10.1111/pbi.12615;
RA Hane J.K., Ming Y., Kamphuis L.G., Nelson M.N., Garg G., Atkins C.A.,
RA Bayer P.E., Bravo A., Bringans S., Cannon S., Edwards D., Foley R.,
RA Gao L.L., Harrison M.J., Huang W., Hurgobin B., Li S., Liu C.W.,
RA McGrath A., Morahan G., Murray J., Weller J., Jian J., Singh K.B.;
RT "A comprehensive draft genome sequence for lupin (Lupinus angustifolius),
RT an emerging health food: insights into plant-microbe interactions and
RT legume evolution.";
RL Plant Biotechnol. J. 15:318-330(2017).
CC -!- SIMILARITY: Belongs to the GDA1/CD39 NTPase family.
CC {ECO:0000256|ARBA:ARBA00009283}.
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DR EMBL; CM007377; OIV94390.1; -; Genomic_DNA.
DR RefSeq; XP_019422289.1; XM_019566744.1.
DR RefSeq; XP_019422290.1; XM_019566745.1.
DR RefSeq; XP_019422291.1; XM_019566746.1.
DR AlphaFoldDB; A0A4P1QT77; -.
DR GeneID; 109331937; -.
DR KEGG; lang:109331937; -.
DR OrthoDB; 1222189at2759; -.
DR Proteomes; UP000188354; Chromosome LG17.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
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:SF115; GDA1/CD39 NUCLEOSIDE PHOSPHATASE FAMILY PROTEIN; 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:UP000188354};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 76..97
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 556..579
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT REGION 698..722
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 246
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR600407-1"
FT BINDING 277..281
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PIRSR:PIRSR600407-2"
SQ SEQUENCE 722 AA; 80556 MW; AC6FBEC0AEC359C0 CRC64;
MIFGKIARAI SNNNLRVSSS LQDLSSYRNL DLEHAHDVTI DPVAVPTYLK QPLYAPAPKG
SIFSSRRNWV RLIKHALCLT LFIFLVYVIF MLVSSFWNQG SGKYFVVLDC GSTGTRVYVY
HAFIEHKKYS TLPIVVKSLN DGVKKKSSSL RGRAYNRIET EPGLDKLVHN VSGLKGALKP
LIRWAERQIP THAHRSTAAF LYATAGLRRL PGSDSKWLLD NAWSVLKDSP FVCQKDWVRI
ISGTEEAYFG WISLNYYSGI LGVRPRKATY GALDLGGSSL QVTFESDQQL NNETSLYVRI
GSVNHHLTAY LLSGYGLNEA FDKSVVHLFK KEFRSTNISN KKVVLKHPCL QSGYKNQYMC
SRCSSNNKEG GSRVINGKML GNKGESGTPV VLFGAPNWQE CSALAKVAVN LSEWSDFSRG
LDCQVQPCAL RDNLPRPYGH FFVISGFYVV YRFFSLTSEA TLDDVLEKGR GFCEKRWNVA
KKSVPPQPFI EQYCFRAPYI ASLLREGLHI SDNQITIGSG SITWTLGVAL LEAGKAYSTP
FGLHSFELFR MKINPLILIP ILLLSIILLL CALSCVGNWM PSFFRRQYLP IFRHKNVSSA
SGLNIPSPFE FQRCSPINSG DGRTKMPHSL TDACSRGSPL GLGHGVSDNG SGIQLMESSL
YPSASSVSYS YSSNNLGQMQ FDNSNLGSFW SPHRSQMRLQ SRRSQSPEDL NSLEAEAHMV
KL
//