ID   GPA1_TRIVA              Reviewed;         402 AA.
AC   Q86D96;
DT   10-OCT-2003, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2003, sequence version 1.
DT   03-AUG-2022, entry version 87.
DE   RecName: Full=Guanine nucleotide-binding protein subunit alpha-1;
DE            Short=G alpha-1;
DE   AltName: Full=GTP-binding protein subunit alpha 1;
GN   Name=GA1;
OS   Trichomonas vaginalis.
OC   Eukaryota; Metamonada; Parabasalia; Trichomonadida; Trichomonadidae;
OC   Trichomonas.
OX   NCBI_TaxID=5722;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=ATCC PRA-98 / G3;
RX   PubMed=12850262; DOI=10.1016/s0166-6851(03)00122-1;
RA   Hirt R.P., Lal K., Pinxteren J., Warwicker J., Healy B., Coombs G.H.,
RA   Field M.C., Embley T.M.;
RT   "Biochemical and genetic evidence for a family of heterotrimeric G-proteins
RT   in Trichomonas vaginalis.";
RL   Mol. Biochem. Parasitol. 129:179-189(2003).
CC   -!- FUNCTION: Guanine nucleotide-binding proteins (G proteins) are involved
CC       as modulators or transducers in various transmembrane signaling
CC       systems. {ECO:0000250}.
CC   -!- SUBUNIT: G proteins are composed of 3 units; alpha, beta and gamma. The
CC       alpha chain contains the guanine nucleotide binding site.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm. Cytoplasm, perinuclear region.
CC       Endomembrane system; Lipid-anchor. Note=Predominantly perinuclear.
CC   -!- SIMILARITY: Belongs to the G-alpha family. {ECO:0000305}.
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DR   EMBL; AY138840; AAN39541.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q86D96; -.
DR   SMR; Q86D96; -.
DR   STRING; 5722.XP_001580284.1; -.
DR   PRIDE; Q86D96; -.
DR   VEuPathDB; TrichDB:TVAG_452120; -.
DR   eggNOG; KOG0082; Eukaryota.
DR   OMA; CAYMESK; -.
DR   GO; GO:0012505; C:endomembrane system; IEA:UniProtKB-SubCell.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR   GO; GO:0048471; C:perinuclear region of cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0031683; F:G-protein beta/gamma-subunit complex binding; IEA:InterPro.
DR   GO; GO:0005525; F:GTP binding; IEA:UniProtKB-KW.
DR   GO; GO:0003924; F:GTPase activity; IEA:InterPro.
DR   GO; GO:0007186; P:G protein-coupled receptor signaling pathway; IEA:InterPro.
DR   CDD; cd00066; G-alpha; 1.
DR   Gene3D; 1.10.400.10; -; 1.
DR   Gene3D; 3.40.50.300; -; 1.
DR   InterPro; IPR001019; Gprotein_alpha_su.
DR   InterPro; IPR011025; GproteinA_insert.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   PANTHER; PTHR10218; PTHR10218; 1.
DR   Pfam; PF00503; G-alpha; 1.
DR   PRINTS; PR00318; GPROTEINA.
DR   SMART; SM00275; G_alpha; 1.
DR   SUPFAM; SSF47895; SSF47895; 1.
DR   SUPFAM; SSF52540; SSF52540; 1.
DR   PROSITE; PS51882; G_ALPHA; 1.
PE   3: Inferred from homology;
KW   Cytoplasm; GTP-binding; Lipoprotein; Membrane; Myristate;
KW   Nucleotide-binding; Palmitate; Transducer.
FT   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0000255"
FT   CHAIN           2..402
FT                   /note="Guanine nucleotide-binding protein subunit alpha-1"
FT                   /id="PRO_0000203668"
FT   DOMAIN          82..402
FT                   /note="G-alpha"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01230"
FT   REGION          1..70
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          85..98
FT                   /note="G1 motif"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01230"
FT   REGION          221..229
FT                   /note="G2 motif"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01230"
FT   REGION          244..253
FT                   /note="G3 motif"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01230"
FT   REGION          313..320
FT                   /note="G4 motif"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01230"
FT   REGION          375..380
FT                   /note="G5 motif"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01230"
FT   COMPBIAS        31..68
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         90..97
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000250"
FT   BINDING         223..229
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000250"
FT   BINDING         248..252
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000250"
FT   BINDING         317..320
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000250"
FT   BINDING         377
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000250"
FT   LIPID           2
FT                   /note="N-myristoyl glycine"
FT                   /evidence="ECO:0000255"
FT   LIPID           3
FT                   /note="S-palmitoyl cysteine"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   402 AA;  45231 MW;  09814946FFAA8FF3 CRC64;
     MGCSASKPSE PSNAKLPSAP VPKKVEQVPE PKPEPQPQPE PQPQPEPPKP AEPAPAPAPA
     PEPQKPAEPA PKVVAVEDDT NEAYGLLLCG AGESGKTTFT RQLKLRYLNG FNEKDCRDFL
     RTIRGNLVET MQLLLVWLEH NNIEIEDSEL SSMAQDIIDV DPQDCEFNEE LVEKLKALWE
     NEQIKKAFEH KDETAVPDHM PYFFAKIDEL AGEDYIPSNE DVLRARIRSI GIEAITFDLQ
     GARIRIFDVG GQKSERSKWA NVMNQVEGVI FCVSFAEFDK PMFEDQNVLR INDSLEIFGN
     ITHQEKFSNS PIFLVCNKFD VFTEKIKNTD AFVKIFPEFS GDSHNPEACA DYLIQRFLDK
     AAPLSEDRPI IQYKIVALNG DQVVETADAI CKFISDKYYQ DA