ID I1PUI6_ORYGL Unreviewed; 390 AA.
AC I1PUI6;
DT 13-JUN-2012, integrated into UniProtKB/TrEMBL.
DT 13-JUN-2012, sequence version 1.
DT 27-MAR-2024, entry version 58.
DE RecName: Full=Guanine nucleotide-binding protein alpha subunit {ECO:0000256|RuleBase:RU368109};
DE Short=GP-alpha {ECO:0000256|RuleBase:RU368109};
OS Oryza glaberrima (African rice).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; BOP clade;
OC Oryzoideae; Oryzeae; Oryzinae; Oryza.
OX NCBI_TaxID=4538 {ECO:0000313|EnsemblPlants:ORGLA05G0103400.1, ECO:0000313|Proteomes:UP000007306};
RN [1] {ECO:0000313|Proteomes:UP000007306}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=IRGC 96717 {ECO:0000313|Proteomes:UP000007306};
RA Wing R.A., Yu Y., Rounsley S., Reddy-Marri P., Goicoechea J.L.,
RA Sisneros N., Lee S., Song X., Angelova A., Kudrna D.P., de Baynast K.,
RA Zuccolo A.;
RT "The complete genome of Oryza glaberrima.";
RL Submitted (JUN-2010) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EnsemblPlants:ORGLA05G0103400.1}
RP IDENTIFICATION.
RG EnsemblPlants;
RL Submitted (JUN-2015) to UniProtKB.
CC -!- FUNCTION: Guanine nucleotide-binding proteins (G proteins) are involved
CC as modulators or transducers in various transmembrane signaling
CC systems. {ECO:0000256|RuleBase:RU368109}.
CC -!- SUBUNIT: G proteins are composed of 3 units; alpha, beta and gamma. The
CC alpha chain contains the guanine nucleotide binding site.
CC {ECO:0000256|RuleBase:RU368109}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000256|RuleBase:RU368109}.
CC -!- DOMAIN: The helical domain is required for self-activation.
CC {ECO:0000256|RuleBase:RU368109}.
CC -!- SIMILARITY: Belongs to the G-alpha family.
CC {ECO:0000256|ARBA:ARBA00005804, ECO:0000256|RuleBase:RU368109}.
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DR AlphaFoldDB; I1PUI6; -.
DR STRING; 4538.I1PUI6; -.
DR EnsemblPlants; ORGLA05G0102900.1; ORGLA05G0102900.1; ORGLA05G0102900.
DR EnsemblPlants; ORGLA05G0103400.1; ORGLA05G0103400.1; ORGLA05G0103400.
DR Gramene; ORGLA05G0102900.1; ORGLA05G0102900.1; ORGLA05G0102900.
DR Gramene; ORGLA05G0103400.1; ORGLA05G0103400.1; ORGLA05G0103400.
DR eggNOG; KOG0082; Eukaryota.
DR HOGENOM; CLU_014184_4_0_1; -.
DR OMA; QVIWADA; -.
DR Proteomes; UP000007306; Unassembled WGS sequence.
DR GO; GO:0005834; C:heterotrimeric G-protein complex; IEA:UniProtKB-UniRule.
DR GO; GO:0001664; F:G protein-coupled receptor binding; IEA:UniProtKB-UniRule.
DR GO; GO:0031683; F:G-protein beta/gamma-subunit complex binding; IEA:UniProtKB-UniRule.
DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0003924; F:GTPase activity; IEA:InterPro.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-UniRule.
DR GO; GO:0007188; P:adenylate cyclase-modulating G protein-coupled receptor signaling pathway; IEA:UniProtKB-UniRule.
DR CDD; cd00066; G-alpha; 1.
DR Gene3D; 1.10.400.10; GI Alpha 1, domain 2-like; 1.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
DR InterPro; IPR001019; Gprotein_alpha_su.
DR InterPro; IPR011025; GproteinA_insert.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR002976; Plant_Gprotein_alpha.
DR PANTHER; PTHR10218; GTP-BINDING PROTEIN ALPHA SUBUNIT; 1.
DR PANTHER; PTHR10218:SF302; GUANINE NUCLEOTIDE-BINDING PROTEIN ALPHA-8 SUBUNIT-RELATED; 1.
DR Pfam; PF00503; G-alpha; 1.
DR PRINTS; PR00318; GPROTEINA.
DR PRINTS; PR01242; GPROTEINAPLT.
DR SMART; SM00275; G_alpha; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR SUPFAM; SSF47895; Transducin (alpha subunit), insertion domain; 1.
DR PROSITE; PS51882; G_ALPHA; 1.
PE 3: Inferred from homology;
KW Cell membrane {ECO:0000256|RuleBase:RU368109};
KW GTP-binding {ECO:0000256|ARBA:ARBA00023134, ECO:0000256|PIRSR:PIRSR602976-
KW 1}; Lipoprotein {ECO:0000256|RuleBase:RU368109};
KW Magnesium {ECO:0000256|PIRSR:PIRSR602976-2, ECO:0000256|RuleBase:RU368109};
KW Membrane {ECO:0000256|RuleBase:RU368109};
KW Metal-binding {ECO:0000256|PIRSR:PIRSR602976-2,
KW ECO:0000256|RuleBase:RU368109}; Myristate {ECO:0000256|RuleBase:RU368109};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW ECO:0000256|RuleBase:RU368109};
KW Palmitate {ECO:0000256|ARBA:ARBA00023139, ECO:0000256|RuleBase:RU368109};
KW Transducer {ECO:0000256|ARBA:ARBA00023224, ECO:0000256|RuleBase:RU368109}.
FT BINDING 59..64
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000256|PIRSR:PIRSR602976-1"
FT BINDING 63
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|PIRSR:PIRSR602976-2"
FT BINDING 173
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000256|PIRSR:PIRSR602976-1"
FT BINDING 198..199
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000256|PIRSR:PIRSR602976-1"
FT BINDING 204
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000256|PIRSR:PIRSR602976-1"
FT BINDING 204
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|PIRSR:PIRSR602976-2"
FT BINDING 232
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000256|PIRSR:PIRSR602976-1"
FT BINDING 298..301
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000256|PIRSR:PIRSR602976-1"
FT BINDING 366
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000256|PIRSR:PIRSR602976-1"
SQ SEQUENCE 390 AA; 45267 MW; F24F3505D14608EF CRC64;
MSVLTCVLDN MGSSCSRSHS LSEAETTKNA KSADIDRRIL QETKAEQHIH KLLLLGAGES
GKSTIFKQIK LLFQTGFDEA ELRSYTSVIH ANVFQTIKIL YEGAKELSQV ESDSSKYVIS
PDNQEIGEKL SDIDGRLDYP LLNKELVLDV KRLWQDPAIQ ETYLRGSILQ LPDCAQYFME
NLDRLAEAGY VPTKEDVLYA RVRTNGVVQI QFSPVGENKR GGEVYRLYDV GGQRNERRKW
IHLFEGVNAV IFCAAISEYD QMLFEDETKN RMMETKELFD WVLKQRCFEK TSFILFLNKF
DIFEKKIQKV PLSVCEWFKD YQPIAPGKQE VEHAYEFVKK KFEELYFQSS KPDRVDRVFK
IYRTTALDQK LVKKTFKLID ESMRRSREGT
//
