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Database: UniProt
Entry: Q2HNW3_9POAL
LinkDB: Q2HNW3_9POAL
Original site: Q2HNW3_9POAL 
ID   Q2HNW3_9POAL            Unreviewed;       128 AA.
AC   Q2HNW3;
DT   21-MAR-2006, integrated into UniProtKB/TrEMBL.
DT   21-MAR-2006, sequence version 1.
DT   27-MAR-2024, entry version 54.
DE   RecName: Full=Guanine nucleotide-binding protein alpha subunit {ECO:0000256|RuleBase:RU368109};
DE            Short=GP-alpha {ECO:0000256|RuleBase:RU368109};
DE   Flags: Fragment;
GN   Name=GPA1 {ECO:0000313|EMBL:AAX58187.1};
OS   Ehrharta erecta.
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; BOP clade;
OC   Oryzoideae; Ehrharteae; Ehrharta.
OX   NCBI_TaxID=96049 {ECO:0000313|EMBL:AAX58187.1};
RN   [1] {ECO:0000313|EMBL:AAX58187.1}
RP   NUCLEOTIDE SEQUENCE.
RX   AGRICOLA=IND43738818;
RA   Guo Y.L., Ge S.;
RT   "Molecular phylogeny of Oryzeae (Poaceae) based on DNA sequences from
RT   chloroplast, mitochondrial, and nuclear genomes.";
RL   Am. J. Bot. 92:1548-1558(2005).
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   EMBL; AY792564; AAX58187.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q2HNW3; -.
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   Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
DR   InterPro; IPR001019; Gprotein_alpha_su.
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   PROSITE; PS51882; G_ALPHA; 1.
PE   3: Inferred from homology;
KW   Cell membrane {ECO:0000256|RuleBase:RU368109};
KW   GTP-binding {ECO:0000256|RuleBase:RU368109};
KW   Lipoprotein {ECO:0000256|RuleBase:RU368109};
KW   Magnesium {ECO:0000256|RuleBase:RU368109};
KW   Membrane {ECO:0000256|RuleBase:RU368109};
KW   Metal-binding {ECO:0000256|RuleBase:RU368109};
KW   Myristate {ECO:0000256|RuleBase:RU368109};
KW   Nucleotide-binding {ECO:0000256|RuleBase:RU368109};
KW   Palmitate {ECO:0000256|ARBA:ARBA00023139, ECO:0000256|RuleBase:RU368109};
KW   Transducer {ECO:0000256|RuleBase:RU368109}.
FT   NON_TER         1
FT                   /evidence="ECO:0000313|EMBL:AAX58187.1"
FT   NON_TER         128
FT                   /evidence="ECO:0000313|EMBL:AAX58187.1"
SQ   SEQUENCE   128 AA;  15403 MW;  933858FE16D5C90D CRC64;
     VEIQFSPVGE SKRGGEVYRL YDVGGQRNER RKWIHLFEGV NAVIFCAAIS EYDQMLFEDE
     TKNRMMETKE LFDWVLKQRC FEKTSFMLFL NKFDIFERKI QKVPLSVCEW FKDYQPIAPE
     KQEVEHAY
//
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