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Database: UniProt
Entry: W5QJF7_9ORYZ
LinkDB: W5QJF7_9ORYZ
Original site: W5QJF7_9ORYZ 
ID   W5QJF7_9ORYZ            Unreviewed;       177 AA.
AC   W5QJF7;
DT   16-APR-2014, integrated into UniProtKB/TrEMBL.
DT   16-APR-2014, sequence version 1.
DT   27-MAR-2024, entry version 32.
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:ACU33013.1};
OS   Oryza alta.
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; BOP clade;
OC   Oryzoideae; Oryzeae; Oryzinae; Oryza.
OX   NCBI_TaxID=52545 {ECO:0000313|EMBL:ACU33013.1};
RN   [1] {ECO:0000313|EMBL:ACU33013.1}
RP   NUCLEOTIDE SEQUENCE.
RA   Ma Y.-T., Gong P.-C., Bao Y.;
RL   Submitted (JAN-2009) to the EMBL/GenBank/DDBJ databases.
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; FJ602728; ACU33010.1; -; Genomic_DNA.
DR   EMBL; FJ602730; ACU33012.1; -; Genomic_DNA.
DR   EMBL; FJ602731; ACU33013.1; -; Genomic_DNA.
DR   AlphaFoldDB; W5QJF7; -.
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:ACU33013.1"
SQ   SEQUENCE   177 AA;  21326 MW;  B2C7C8D87C486A8F CRC64;
     PVGENKRGGE VYRLYDVGGQ RNERRKWIHL FEGVNAVIFC AAISEYDQML FEDETKNRMM
     ETKELFDWVL KQRCFEKTSF MLFLNKFDIF EKKIQKVPLS VCEWFKDYQP IAPGKQEVEH
     AYEFVKKKFE ELYFQSSKPD RVDRVFKIYR TTALDQKLVK KTFKLIDESM RRSREGT
//
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