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Database: UniProt
Entry: T5AK73_OPHSC
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Original site: T5AK73_OPHSC 
ID   T5AK73_OPHSC            Unreviewed;       355 AA.
AC   T5AK73;
DT   13-NOV-2013, integrated into UniProtKB/TrEMBL.
DT   13-NOV-2013, sequence version 1.
DT   27-MAR-2024, entry version 44.
DE   SubName: Full=G protein alpha subunit Tga3 {ECO:0000313|EMBL:EQL02137.1};
GN   ORFNames=OCS_02158 {ECO:0000313|EMBL:EQL02137.1};
OS   Ophiocordyceps sinensis (strain Co18 / CGMCC 3.14243) (Yarsagumba
OS   caterpillar fungus) (Hirsutella sinensis).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Hypocreomycetidae; Hypocreales; Ophiocordycipitaceae; Ophiocordyceps.
OX   NCBI_TaxID=911162 {ECO:0000313|EMBL:EQL02137.1, ECO:0000313|Proteomes:UP000019374};
RN   [1] {ECO:0000313|EMBL:EQL02137.1, ECO:0000313|Proteomes:UP000019374}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Co18 / CGMCC 3.14243 {ECO:0000313|Proteomes:UP000019374};
RC   TISSUE=Fruit-body {ECO:0000313|EMBL:EQL02137.1};
RX   DOI=10.1007/s11434-013-5929-5;
RA   Hu X., Zhang Y., Xiao G., Zheng P., Xia Y., Zhang X., St Leger R.J.,
RA   Liu X., Wang C.;
RT   "Genome survey uncovers the secrets of sex and lifestyle in caterpillar
RT   fungus.";
RL   Chin. Sci. Bull. 58:2846-2854(2013).
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(q) subfamily.
CC       {ECO:0000256|ARBA:ARBA00007976}.
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DR   EMBL; KE652347; EQL02137.1; -; Genomic_DNA.
DR   AlphaFoldDB; T5AK73; -.
DR   eggNOG; KOG0082; Eukaryota.
DR   HOGENOM; CLU_014184_0_1_1; -.
DR   Proteomes; UP000019374; Unassembled WGS sequence.
DR   GO; GO:0005834; C:heterotrimeric G-protein complex; IEA:InterPro.
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: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; IPR002975; Fungi_Gprotein_alpha.
DR   InterPro; IPR001019; Gprotein_alpha_su.
DR   InterPro; IPR011025; GproteinA_insert.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   PANTHER; PTHR10218; GTP-BINDING PROTEIN ALPHA SUBUNIT; 1.
DR   PANTHER; PTHR10218:SF363; GUANINE NUCLEOTIDE-BINDING PROTEIN ALPHA-2 SUBUNIT; 1.
DR   Pfam; PF00503; G-alpha; 1.
DR   PRINTS; PR00318; GPROTEINA.
DR   PRINTS; PR01241; GPROTEINAFNG.
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   Magnesium {ECO:0000256|ARBA:ARBA00022842};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW   Reference proteome {ECO:0000313|Proteomes:UP000019374};
KW   Transducer {ECO:0000256|ARBA:ARBA00023224}.
FT   REGION          1..26
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        10..26
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   355 AA;  40776 MW;  4AABC2F5808A2BE1 CRC64;
     MGGCMSSSAE EAEQKKKSQA IDKGIEEDSK RLRKECKILL LGSGESGKST IVKQMKIIHL
     KGYSEDELYN YRSTVFKNLV DCAKAIIAAM EQFDIKLQSP DNRRHVDFLM EYQAEPGPEA
     HIDPEVGVAV RALWSDPAKD ELMTRQTEFY LMDSAVYFFH EAMRIVAPDY LPNEMDVLRA
     RTKTTGIYET RFQMGQLSIH MFDVGGQRSE RKKWIHCFEN VTSIIFCVAL SEYDQVLLEE
     SSQNRMMESL LLFDSVVNSR WFMRTSIILF LNKVDIFKQK LSRSPLNNYF PDYSGGNDVN
     KAAKYLLWRF NQVNRAHLNL YPHLTQATDT SNIRLVFAAV KETILNNALK DSGIL
//
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