ID A0A165PAV0_EXIGL Unreviewed; 450 AA.
AC A0A165PAV0;
DT 06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT 06-JUL-2016, sequence version 1.
DT 27-MAR-2024, entry version 30.
DE SubName: Full=Guanine nucleotide binding protein, alpha subunit {ECO:0000313|EMBL:KZW01907.1};
GN ORFNames=EXIGLDRAFT_638099 {ECO:0000313|EMBL:KZW01907.1};
OS Exidia glandulosa HHB12029.
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC Auriculariales; Exidiaceae; Exidia.
OX NCBI_TaxID=1314781 {ECO:0000313|EMBL:KZW01907.1, ECO:0000313|Proteomes:UP000077266};
RN [1] {ECO:0000313|EMBL:KZW01907.1, ECO:0000313|Proteomes:UP000077266}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=HHB12029 {ECO:0000313|EMBL:KZW01907.1,
RC ECO:0000313|Proteomes:UP000077266};
RX PubMed=26659563; DOI=10.1093/molbev/msv337;
RA Nagy L.G., Riley R., Tritt A., Adam C., Daum C., Floudas D., Sun H.,
RA Yadav J.S., Pangilinan J., Larsson K.H., Matsuura K., Barry K., Labutti K.,
RA Kuo R., Ohm R.A., Bhattacharya S.S., Shirouzu T., Yoshinaga Y.,
RA Martin F.M., Grigoriev I.V., Hibbett D.S.;
RT "Comparative Genomics of Early-Diverging Mushroom-Forming Fungi Provides
RT Insights into the Origins of Lignocellulose Decay Capabilities.";
RL Mol. Biol. Evol. 33:959-970(2016).
CC -!- SIMILARITY: Belongs to the G-alpha family.
CC {ECO:0000256|ARBA:ARBA00005804}.
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DR EMBL; KV425891; KZW01907.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A165PAV0; -.
DR STRING; 1314781.A0A165PAV0; -.
DR InParanoid; A0A165PAV0; -.
DR OrthoDB; 1864818at2759; -.
DR Proteomes; UP000077266; 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; 2.
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:SF302; GUANINE NUCLEOTIDE-BINDING PROTEIN ALPHA-8 SUBUNIT-RELATED; 1.
DR Pfam; PF00503; G-alpha; 1.
DR PRINTS; PR00318; GPROTEINA.
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 Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Reference proteome {ECO:0000313|Proteomes:UP000077266};
KW Transducer {ECO:0000256|ARBA:ARBA00023224}.
FT REGION 1..28
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 450 AA; 50898 MW; FB578F6EE778F7F9 CRC64;
MLRHDVLEDP LTAALQPPLD ETPEEKTKRL KREIKAKRVS DGIDVALRAE RDELKRRRAQ
RPEVKLLLLG QASSGKSTLL KQFQLYYAPD MVDAQRSSWR PVVYFNIIKA IAGILDALEQ
VAYFDSHPEL AQLRMTLLPL ADLEPALAVQ ISGGVYVTGT GTSSPYGQDA YVRPGWQTLA
KGKMKSSRTT GDSAYSSHIP AAEETAAWRI AACKDDIHAL WLHPAVQALS KKQLQLEDSA
AFFLESIQRI AWPDYVPSVD DVLHVRLQTL GVTEHQFEVS LLGKNVNLCL YDVGGARGHR
PKWVPYFDSA HAIIFLAPLS AYDQYLEEDR RTNRIDDSLQ LWTEICKNQV LKNLHLVLFL
NKTDVLKAKL AAGIKVKKYI TSFGDRPNEY TEVSQYFRAH FLQVHRRNVT GRRVLYTHFT
SVIDTKATQT IIVNVADSIM RDYFAEARLV
//
