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Database: UniProt
Entry: S8D2Z5_9LAMI
LinkDB: S8D2Z5_9LAMI
Original site: S8D2Z5_9LAMI 
ID   S8D2Z5_9LAMI            Unreviewed;       384 AA.
AC   S8D2Z5;
DT   16-OCT-2013, integrated into UniProtKB/TrEMBL.
DT   16-OCT-2013, sequence version 1.
DT   27-MAR-2024, entry version 40.
DE   RecName: Full=Guanine nucleotide-binding protein alpha subunit {ECO:0000256|RuleBase:RU368109};
DE            Short=GP-alpha {ECO:0000256|RuleBase:RU368109};
GN   ORFNames=M569_00991 {ECO:0000313|EMBL:EPS73765.1};
OS   Genlisea aurea.
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   asterids; lamiids; Lamiales; Lentibulariaceae; Genlisea.
OX   NCBI_TaxID=192259 {ECO:0000313|EMBL:EPS73765.1, ECO:0000313|Proteomes:UP000015453};
RN   [1] {ECO:0000313|EMBL:EPS73765.1, ECO:0000313|Proteomes:UP000015453}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=23855885;
RA   Leushkin E.V., Sutormin R.A., Nabieva E.R., Penin A.A., Kondrashov A.S.,
RA   Logacheva M.D.;
RT   "The miniature genome of a carnivorous plant Genlisea aurea contains a low
RT   number of genes and short non-coding sequences.";
RL   BMC Genomics 14:476-476(2013).
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}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:EPS73765.1}.
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DR   EMBL; AUSU01000313; EPS73765.1; -; Genomic_DNA.
DR   AlphaFoldDB; S8D2Z5; -.
DR   OrthoDB; 2897309at2759; -.
DR   Proteomes; UP000015453; 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|RuleBase:RU368109};
KW   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   Reference proteome {ECO:0000313|Proteomes:UP000015453};
KW   Transducer {ECO:0000256|ARBA:ARBA00023224, ECO:0000256|RuleBase:RU368109}.
FT   BINDING         52
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR602976-2"
FT   BINDING         194
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR602976-2"
SQ   SEQUENCE   384 AA;  44754 MW;  1703DA4B260BEE4D CRC64;
     MGLLCSRQQH NRADSEEIER TAEIERRIER ETKAEKHIQK LLLLGAGDSG KSTIFKQIKL
     LFQSGFDDAE LKSYIPVIHA NVYQTIKILY DGSKEFSQSA GDCSKFRISD ENATIGENLS
     NIGGRLDYPP LTTEIANEIE SLWRDNGIQQ ETYSRGNEFQ VPDCALYFME NLRRFSDPGY
     IPTKEDVLHA RVQTTGVVEI QFSPVRENKM SGEVYRLFDV GGQKNERRKW IHLFEGVTVV
     IFCAAISEYD QTLFEDDKKN RMVEAKELFE WVLKQPCFEK TSFMLFLNKF DLFEKKVLKV
     PLNACEWFKD YQPVSTGKQE IEHAYEFVKK RFEELYFQST KLDCVDRVFK IYRTTALDQK
     LVKKTFKLVD ETLRRRNLLE AGVL
//
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