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Database: UniProt
Entry: A0A195F7F4_9HYME
LinkDB: A0A195F7F4_9HYME
Original site: A0A195F7F4_9HYME 
ID   A0A195F7F4_9HYME        Unreviewed;       380 AA.
AC   A0A195F7F4;
DT   05-OCT-2016, integrated into UniProtKB/TrEMBL.
DT   05-OCT-2016, sequence version 1.
DT   27-MAR-2024, entry version 30.
DE   RecName: Full=Adenylate cyclase-stimulating G alpha protein {ECO:0000256|ARBA:ARBA00042247};
GN   ORFNames=ALC56_09790 {ECO:0000313|EMBL:KYN35999.1};
OS   Trachymyrmex septentrionalis.
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC   Neoptera; Endopterygota; Hymenoptera; Apocrita; Aculeata; Formicoidea;
OC   Formicidae; Myrmicinae; Trachymyrmex.
OX   NCBI_TaxID=34720 {ECO:0000313|EMBL:KYN35999.1, ECO:0000313|Proteomes:UP000078541};
RN   [1] {ECO:0000313|EMBL:KYN35999.1, ECO:0000313|Proteomes:UP000078541}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Tsep2-gDNA-1 {ECO:0000313|EMBL:KYN35999.1};
RC   TISSUE=Whole body {ECO:0000313|EMBL:KYN35999.1};
RA   Nygaard S., Hu H., Boomsma J., Zhang G.;
RT   "Trachymyrmex septentrionalis WGS genome.";
RL   Submitted (MAR-2016) to the EMBL/GenBank/DDBJ databases.
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; KQ981768; KYN35999.1; -; Genomic_DNA.
DR   RefSeq; XP_018347105.1; XM_018491603.1.
DR   AlphaFoldDB; A0A195F7F4; -.
DR   STRING; 34720.A0A195F7F4; -.
DR   GeneID; 108751415; -.
DR   OrthoDB; 2897309at2759; -.
DR   Proteomes; UP000078541; 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:UP000078541};
KW   Transducer {ECO:0000256|ARBA:ARBA00023224}.
FT   REGION          1..27
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        12..27
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   380 AA;  44283 MW;  6DBF526A5886BF32 CRC64;
     MGCFGSQNKD SQDESKNQKR RSDAITRQLQ KDKQVYRATH RLLLLGAGES GKSTIVKQMR
     ILHVNGFSEA EKRQKIEDIK KNIRDAILTI TSAMSTLTPP VTLGDTSNQS RMDYVLEVSS
     SPDFDYPAEF YNIVETLWKD RGVQQSFERS NEYQLIDCAK YFLDKVAIVK QPDYTPTEQD
     ILRCRVLTSG IFETRFQVDK VNFHMFDVGG QRDERRKWIQ CFNDVTAIIF VTACSSYNMV
     LREDPTKLRL RESLDLFKSI WNNRWLRTIS VILFLNKQDL LAEKVKAGKH KLEDYFPEFA
     RYQTPVEPGM AADPSEIPDV IRAKYFIRDE FLRISTASGD GKHYCYPHFT CAVDTENIKR
     VFNDCRDIIQ RMHLRQYELL
//
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