ID T1JHJ8_STRMM Unreviewed; 391 AA.
AC T1JHJ8;
DT 16-OCT-2013, integrated into UniProtKB/TrEMBL.
DT 16-OCT-2013, sequence version 1.
DT 27-MAR-2024, entry version 44.
DE RecName: Full=Adenylate cyclase-stimulating G alpha protein {ECO:0000256|ARBA:ARBA00042247};
OS Strigamia maritima (European centipede) (Geophilus maritimus).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Myriapoda; Chilopoda;
OC Pleurostigmophora; Geophilomorpha; Linotaeniidae; Strigamia.
OX NCBI_TaxID=126957 {ECO:0000313|EnsemblMetazoa:SMAR013329-PA, ECO:0000313|Proteomes:UP000014500};
RN [1] {ECO:0000313|Proteomes:UP000014500}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=Brora {ECO:0000313|Proteomes:UP000014500};
RA Richards S.R., Qu J., Jiang H., Jhangiani S.N., Agravi P., Goodspeed R.,
RA Gross S., Mandapat C., Jackson L., Mathew T., Pu L., Thornton R., Saada N.,
RA Wilczek-Boney K.B., Lee S., Kovar C., Wu Y., Scherer S.E., Worley K.C.,
RA Muzny D.M., Gibbs R.;
RL Submitted (MAY-2011) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EnsemblMetazoa:SMAR013329-PA}
RP IDENTIFICATION.
RG EnsemblMetazoa;
RL Submitted (FEB-2015) to UniProtKB.
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|ARBA:ARBA00011356}.
CC -!- SIMILARITY: Belongs to the G-alpha family. G(s) subfamily.
CC {ECO:0000256|ARBA:ARBA00007172}.
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DR EMBL; JH431711; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR AlphaFoldDB; T1JHJ8; -.
DR STRING; 126957.T1JHJ8; -.
DR EnsemblMetazoa; SMAR013329-RA; SMAR013329-PA; SMAR013329.
DR eggNOG; KOG0099; Eukaryota.
DR HOGENOM; CLU_014184_3_0_1; -.
DR OMA; DHVAKCW; -.
DR OrthoDB; 2897309at2759; -.
DR PhylomeDB; T1JHJ8; -.
DR Proteomes; UP000014500; Unassembled WGS sequence.
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; GI Alpha 1, domain 2-like; 1.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
DR InterPro; IPR000367; Gprotein_alpha_S.
DR InterPro; IPR001019; Gprotein_alpha_su.
DR InterPro; IPR011025; GproteinA_insert.
DR InterPro; IPR027417; P-loop_NTPase.
DR PANTHER; PTHR10218:SF212; G PROTEIN ALPHA S SUBUNIT; 1.
DR PANTHER; PTHR10218; GTP-BINDING PROTEIN ALPHA SUBUNIT; 1.
DR Pfam; PF00503; G-alpha; 1.
DR PRINTS; PR00318; GPROTEINA.
DR PRINTS; PR00443; GPROTEINAS.
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 GTP-binding {ECO:0000256|ARBA:ARBA00023134};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Reference proteome {ECO:0000313|Proteomes:UP000014500};
KW Transducer {ECO:0000256|ARBA:ARBA00023224}.
FT REGION 1..22
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 391 AA; 45785 MW; B1009119A630B520 CRC64;
MGCFGSASTK TDAEEDKRRK EANKKIEKQL QKDKQIYRAT HRLLLLGAGE SGKSTIVKQM
RILHIEGGFT EDSLKGRVVF NCREKKLKIE DIKKNVRDAI LTITGAMSTL TPPVQLENPD
NQFRVDYIQD VASSPDFDYP LEFYDHTEIL WKDRGVQSCF ERANEYQLID CAKYFLDRVS
IVRKPDYTPS EQDILRCRVL TSGIFETRFQ VEKVNFHMFD VGGQRDERRK WIQCFNDVTA
IIFVTACSSY NMVLREDSSQ NRLRESLELF KSIWNNRWLK TISVILFLNK QDLLAEKIKS
GKSKLEDYFS DFTRYQIPLD ATSEPGEDQE VIRAKYFIRD EFLRVSTASG DGKHYCYPHF
TCAVDTENIR RVFNDCRDII QRMHLRQYEL L
//