ID A0A165MNM3_9AGAM Unreviewed; 486 AA.
AC A0A165MNM3;
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:KZT18573.1};
GN ORFNames=NEOLEDRAFT_1143248 {ECO:0000313|EMBL:KZT18573.1};
OS Neolentinus lepideus HHB14362 ss-1.
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC Gloeophyllales; Gloeophyllaceae; Neolentinus.
OX NCBI_TaxID=1314782 {ECO:0000313|EMBL:KZT18573.1, ECO:0000313|Proteomes:UP000076761};
RN [1] {ECO:0000313|EMBL:KZT18573.1, ECO:0000313|Proteomes:UP000076761}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=HHB14362 ss-1 {ECO:0000313|EMBL:KZT18573.1,
RC ECO:0000313|Proteomes:UP000076761};
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; KV425672; KZT18573.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A165MNM3; -.
DR STRING; 1314782.A0A165MNM3; -.
DR InParanoid; A0A165MNM3; -.
DR OrthoDB; 1864818at2759; -.
DR Proteomes; UP000076761; 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; 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:UP000076761};
KW Transducer {ECO:0000256|ARBA:ARBA00023224}.
FT REGION 172..196
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 486 AA; 55581 MW; 2FFB6C137783F352 CRC64;
MGRLSIENDP FACMTVPPTN ETWEQKMARE RCEAEAQQVS DEIDQKLRSE RAALKKNKKS
VKVLLLGQAE SGKSTTLKNF QLAYAREAWQ EERASWRAVI QLNLIRSVRT VFDAVLQEMS
GNTLSCDSDD DEFANPTARS PFQFTEKHQL LRFRLMPLRR VEADLKRRLG AASEEATASL
SPMTTPPLEE PDRVASPRPF EVSVRSWKDA FEMHCRSPKT SSIGHSSLES DDATDVIAEC
REDIKALWED HIVKQVLKRR KVRVEESAGF FLNDIDRIAV HSYNPTDEDV MRARLRTVGI
QEHHMTLDEG ESRVSRPEFG RDWIIYDVGG CRTQRAAWVP YFEDVNAIIF LAPVSCFNER
LTEDPRVNRL EDTFMLWKSL ASSPLLAGVA IVLFMNKCDL LELKIKQGIS VKKYMPSYGE
RENSARQVLK YLRGKFKEML KQHSPRPRPF YAHATSVVDT KATAVTLTSV RDAILRDHLK
EAEFVV
//
