ID B0DL86_LACBS Unreviewed; 500 AA.
AC B0DL86;
DT 26-FEB-2008, integrated into UniProtKB/TrEMBL.
DT 26-FEB-2008, sequence version 1.
DT 27-MAR-2024, entry version 77.
DE SubName: Full=G protein a subunit 5 {ECO:0000313|EMBL:EDR04519.1};
GN ORFNames=LACBIDRAFT_304258 {ECO:0000313|EMBL:EDR04519.1};
OS Laccaria bicolor (strain S238N-H82 / ATCC MYA-4686) (Bicoloured deceiver)
OS (Laccaria laccata var. bicolor).
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC Agaricomycetidae; Agaricales; Agaricineae; Hydnangiaceae; Laccaria.
OX NCBI_TaxID=486041 {ECO:0000313|Proteomes:UP000001194};
RN [1] {ECO:0000313|EMBL:EDR04519.1, ECO:0000313|Proteomes:UP000001194}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=S238N-H82 / ATCC MYA-4686 {ECO:0000313|Proteomes:UP000001194};
RX PubMed=18322534; DOI=10.1038/nature06556;
RA Martin F., Aerts A., Ahren D., Brun A., Danchin E.G.J., Duchaussoy F.,
RA Gibon J., Kohler A., Lindquist E., Pereda V., Salamov A., Shapiro H.J.,
RA Wuyts J., Blaudez D., Buee M., Brokstein P., Canbaeck B., Cohen D.,
RA Courty P.E., Coutinho P.M., Delaruelle C., Detter J.C., Deveau A.,
RA DiFazio S., Duplessis S., Fraissinet-Tachet L., Lucic E., Frey-Klett P.,
RA Fourrey C., Feussner I., Gay G., Grimwood J., Hoegger P.J., Jain P.,
RA Kilaru S., Labbe J., Lin Y.C., Legue V., Le Tacon F., Marmeisse R.,
RA Melayah D., Montanini B., Muratet M., Nehls U., Niculita-Hirzel H.,
RA Oudot-Le Secq M.P., Peter M., Quesneville H., Rajashekar B., Reich M.,
RA Rouhier N., Schmutz J., Yin T., Chalot M., Henrissat B., Kuees U.,
RA Lucas S., Van de Peer Y., Podila G.K., Polle A., Pukkila P.J.,
RA Richardson P.M., Rouze P., Sanders I.R., Stajich J.E., Tunlid A.,
RA Tuskan G., Grigoriev I.V.;
RT "The genome of Laccaria bicolor provides insights into mycorrhizal
RT symbiosis.";
RL Nature 452:88-92(2008).
CC -!- SIMILARITY: Belongs to the G-alpha family.
CC {ECO:0000256|ARBA:ARBA00005804}.
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DR EMBL; DS547117; EDR04519.1; -; Genomic_DNA.
DR RefSeq; XP_001884691.1; XM_001884656.1.
DR AlphaFoldDB; B0DL86; -.
DR STRING; 486041.B0DL86; -.
DR GeneID; 6080466; -.
DR KEGG; lbc:LACBIDRAFT_304258; -.
DR HOGENOM; CLU_014184_1_1_1; -.
DR InParanoid; B0DL86; -.
DR OrthoDB; 1438431at2759; -.
DR Proteomes; UP000001194; 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 Gene3D; 1.10.400.10; GI Alpha 1, domain 2-like; 2.
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; 2.
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:UP000001194};
KW Transducer {ECO:0000256|ARBA:ARBA00023224}.
FT REGION 1..24
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 115..213
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 247..282
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 316..353
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 8..24
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 115..136
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 149..166
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 179..197
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 264..282
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 327..353
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 500 AA; 55196 MW; DC61071D8EFF68AA CRC64;
MPVRTADDPL DEVLKPPPDE SPEDRVVRLQ NEAEAKRVSL AIDASIKAER HARRKKRIVR
LLLLGQSESG KSTTLRQFQR LYTPTAFREE RILWRAVIQL NIIRSIRTIL DALTFPSTST
SSPHTSPYSS PRSRARTISR PPLPNHPHEQ HNGNGNDTTL TFGSSSPPRV RHHHHHHSPP
SNPDSDGDSE SDFVHPHHHI HHRSPRSTSP LTLAQNTPLD ALKARLLPLR HIEALLIAKL
VPPNEEEATH FARPGPPGVG VGAGTSAGSS SGASSTSGGT GNHAYRNQEI FVRPGTGWKG
GLARARVTYP GSGYGYGDHH DGAKQNKNGK GSSGGNGTRP MSAGTTGSET QDEPQEVLNM
CRRDMIALWN DEGVREVLRR RKIRIEEESG FFLDDLERLT SLKYMPTDAN PCEQPDDVLK
ARLKTVGGSE YRFEMEATAG RDSGTEWRIV DVGGSRSQRP TWAPFFDDVD AIIFLAPISG
FDQVLSEDRT VNRLVSFLSF
//
