ID   GNAQ_GEOCY              Reviewed;         355 AA.
AC   Q9XZV4;
DT   30-APR-2003, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1999, sequence version 1.
DT   03-AUG-2022, entry version 87.
DE   RecName: Full=Guanine nucleotide-binding protein G(q) subunit alpha;
DE   AltName: Full=Guanine nucleotide-binding protein alpha-q;
OS   Geodia cydonium (Sponge).
OC   Eukaryota; Metazoa; Porifera; Demospongiae; Heteroscleromorpha;
OC   Tetractinellida; Astrophorina; Geodiidae; Geodia.
OX   NCBI_TaxID=6047;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   PubMed=9459489; DOI=10.1016/s0167-4889(97)00121-3;
RA   Seack J., Kruse M., Mueller W.E.G.;
RT   "Evolutionary analysis of G-proteins in early metazoans: cloning of
RT   alpha- and beta-subunits from the sponge Geodia cydonium.";
RL   Biochim. Biophys. Acta 1401:93-103(1998).
CC   -!- FUNCTION: Guanine nucleotide-binding proteins (G proteins) are involved
CC       as modulators or transducers in various transmembrane signaling
CC       systems.
CC   -!- SUBUNIT: G proteins are composed of 3 units; alpha, beta and gamma. The
CC       alpha chain contains the guanine nucleotide binding site.
CC   -!- SIMILARITY: Belongs to the G-alpha family. G(q) subfamily.
CC       {ECO:0000305}.
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DR   EMBL; Y14248; CAB43527.1; -; mRNA.
DR   AlphaFoldDB; Q9XZV4; -.
DR   SMR; Q9XZV4; -.
DR   GO; GO:0001664; F:G protein-coupled receptor binding; IEA:InterPro.
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:0046872; F:metal ion binding; IEA:UniProtKB-KW.
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; IPR000654; Gprotein_alpha_Q.
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   PRINTS; PR00442; GPROTEINAQ.
DR   SMART; SM00275; G_alpha; 1.
DR   SUPFAM; SSF47895; SSF47895; 1.
DR   SUPFAM; SSF52540; SSF52540; 1.
DR   PROSITE; PS51882; G_ALPHA; 1.
PE   2: Evidence at transcript level;
KW   GTP-binding; Lipoprotein; Magnesium; Metal-binding; Nucleotide-binding;
KW   Palmitate; Transducer.
FT   CHAIN           1..355
FT                   /note="Guanine nucleotide-binding protein G(q) subunit
FT                   alpha"
FT                   /id="PRO_0000203764"
FT   DOMAIN          32..355
FT                   /note="G-alpha"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01230"
FT   REGION          35..48
FT                   /note="G1 motif"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01230"
FT   REGION          172..180
FT                   /note="G2 motif"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01230"
FT   REGION          195..204
FT                   /note="G3 motif"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01230"
FT   REGION          265..272
FT                   /note="G4 motif"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01230"
FT   REGION          324..329
FT                   /note="G5 motif"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01230"
FT   BINDING         40..47
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000250"
FT   BINDING         47
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000250"
FT   BINDING         174..180
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000250"
FT   BINDING         180
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000250"
FT   BINDING         199..203
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000250"
FT   BINDING         269..272
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000250"
FT   BINDING         326
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000250"
FT   LIPID           3
FT                   /note="S-palmitoyl cysteine"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   355 AA;  41364 MW;  6828C29643F2CE91 CRC64;
     MSCLLSEEER LQKRINTRIN RELQRDHKDA KKEIKLLLLG TGESGKSTFI KQMRIIHGKG
     YSKQDCLEYK NLVFRNILMS MHSMLQATAE LKIAYIDPDA QRHVQLLMAL RPETAQSLGG
     ETCEAIRKLW QDAGVQECYQ RRNEYQLSDS TKYYLDDLPR ISSNDYVPTT QDVLRVRVPT
     TGINEYPFTI NKIIFKMVDV GGQRSERRKW IHCFDHVTSV MFLVAISEYD QILVEADSRV
     NRMVESLHLF NTIISYPWFN KSSIILFLNK KDLLEEKVMH SHLIDYFEEY DGPKCDHVSA
     RESIAKMFIS INDMRSADIY PHFTCATDTE NIKFVFDVVK NHILQQHITE VVPGL