ID A0A165GHK3_9APHY Unreviewed; 507 AA.
AC A0A165GHK3;
DT 06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT 06-JUL-2016, sequence version 1.
DT 27-MAR-2024, entry version 31.
DE SubName: Full=G-alpha-domain-containing protein {ECO:0000313|EMBL:KZT10357.1};
GN ORFNames=LAESUDRAFT_721694 {ECO:0000313|EMBL:KZT10357.1};
OS Laetiporus sulphureus 93-53.
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC Polyporales; Laetiporus.
OX NCBI_TaxID=1314785 {ECO:0000313|EMBL:KZT10357.1, ECO:0000313|Proteomes:UP000076871};
RN [1] {ECO:0000313|EMBL:KZT10357.1, ECO:0000313|Proteomes:UP000076871}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=93-53 {ECO:0000313|EMBL:KZT10357.1,
RC ECO:0000313|Proteomes:UP000076871};
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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; KV427609; KZT10357.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A165GHK3; -.
DR STRING; 1314785.A0A165GHK3; -.
DR InParanoid; A0A165GHK3; -.
DR OrthoDB; 1864818at2759; -.
DR Proteomes; UP000076871; 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; 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:UP000076871};
KW Transducer {ECO:0000256|ARBA:ARBA00023224}.
FT REGION 17..42
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 27..42
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 507 AA; 57465 MW; 0CA1020D73937B12 CRC64;
MTVYVDKMFT AYSPSTDPLE LALAPPPDES EQDRRNRLAA EAEAKRISDI IDEEIQRQEK
TEKKGPKPIK ILLLGQSESG KSTTLKNFQL MNSPKAFRAE RASWRAVIHL NVVRSIRLIL
EAMSDAHAAQ VPGAKFLTSH SSTRASSSRS LLDPDGGIPR ALPQLTAEHL KLKMRLSPLL
QVEQALIRKL TPPGSAEFEA THLAQMSNVS YMDRMHAKEV AVNTTFAWKG IFSKFMSDTR
DSIDSREAID WDDPEDPGRI IYACGEDMIR LWNDDTIQAL LRAQNIRLED QPGFFLDSLD
RVTSPRYVPS DEDVLRARLK TLGVTEYRFS IKEGNMGGGT REWRIYDVGG HRSLVRAAWA
PYFDDMNAIL FLAPISCFDQ MLEEDANVNR LEDSVLLWKS IVSNPLLKKT SIVLFLNKVD
IFKAKLEAGI KLGKYIVSYG NRPNDFESTS NYLRRKFAQI HKERSPEQRQ FYCHFTTVTD
TKSTQHILVD VQDTVIIKNL KNSSLIA
//
