ID A0A165CXD9_9BASI Unreviewed; 490 AA.
AC A0A165CXD9;
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:KZT51604.1};
GN ORFNames=CALCODRAFT_476965 {ECO:0000313|EMBL:KZT51604.1};
OS Calocera cornea HHB12733.
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Dacrymycetes;
OC Dacrymycetales; Dacrymycetaceae; Calocera.
OX NCBI_TaxID=1353952 {ECO:0000313|EMBL:KZT51604.1, ECO:0000313|Proteomes:UP000076842};
RN [1] {ECO:0000313|EMBL:KZT51604.1, ECO:0000313|Proteomes:UP000076842}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=HHB12733 {ECO:0000313|EMBL:KZT51604.1,
RC ECO:0000313|Proteomes:UP000076842};
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; KV424100; KZT51604.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A165CXD9; -.
DR STRING; 1353952.A0A165CXD9; -.
DR InParanoid; A0A165CXD9; -.
DR OrthoDB; 1438431at2759; -.
DR Proteomes; UP000076842; 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: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:UP000076842};
KW Transducer {ECO:0000256|ARBA:ARBA00023224}.
FT REGION 1..41
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 9..41
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 490 AA; 56409 MW; 1CD5DBB6E1D8ECEF CRC64;
MSVQTRRMDR PVELSERYYS SDDPLDRVLR PDPHETPDQR SARLMAEFEA KQRSDAIDEM
LRQERVAQKK KKEVKILLLG QSESGKSTTL KQFQLLWAPN ILDAERLYWR PVIFLNLVVS
VRRILECLSV RPDEEARPGT GSSAMSVEET YSRYAELKLK LSPLLQLESV LLNELGAPAD
FDSANVYDRT SPLPGASGHK RDILVRMEWQ ERLAKSKAAR GSRGPGLGDR VAFADPGDAG
AIISACRPEL QRLWDDPFVH AVMARRKLRL EESSGFFVND LNRIARYEYI PTDEDILRAR
VRTIGVSEHR FTPPSTEREP AEWVIYDVGG TRGQRPKWVP YFEDAQAIIF LAPVSAFDQF
LAEDRKVNRL ADSFQLFEHI CKQELLKGSS IILFLNKADL LKAKLDAGVR FNKWIERYGD
RPNEFEAVAN YLKGKFVELY KFHRNKVSPR DSRELYVHLT SVVDIRTTHA IFQDVKETII
RDYLRNTKLI
//
