ID A8PR62_MALGO Unreviewed; 358 AA.
AC A8PR62;
DT 15-JAN-2008, integrated into UniProtKB/TrEMBL.
DT 15-JAN-2008, sequence version 1.
DT 27-MAR-2024, entry version 90.
DE RecName: Full=Guanine nucleotide-binding protein alpha-3 subunit {ECO:0008006|Google:ProtNLM};
GN ORFNames=MGL_0613 {ECO:0000313|EMBL:EDP45624.1};
OS Malassezia globosa (strain ATCC MYA-4612 / CBS 7966) (Dandruff-associated
OS fungus).
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Ustilaginomycotina;
OC Malasseziomycetes; Malasseziales; Malasseziaceae; Malassezia.
OX NCBI_TaxID=425265 {ECO:0000313|EMBL:EDP45624.1, ECO:0000313|Proteomes:UP000008837};
RN [1] {ECO:0000313|EMBL:EDP45624.1, ECO:0000313|Proteomes:UP000008837}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC MYA-4612 / CBS 7966 {ECO:0000313|Proteomes:UP000008837};
RX PubMed=18000048; DOI=10.1073/pnas.0706756104;
RA Xu J., Saunders C.W., Hu P., Grant R.A., Boekhout T., Kuramae E.E.,
RA Kronstad J.W., Deangelis Y.M., Reeder N.L., Johnstone K.R., Leland M.,
RA Fieno A.M., Begley W.M., Sun Y., Lacey M.P., Chaudhary T., Keough T.,
RA Chu L., Sears R., Yuan B., Dawson T.L.Jr.;
RT "Dandruff-associated Malassezia genomes reveal convergent and divergent
RT virulence traits shared with plant and human fungal pathogens.";
RL Proc. Natl. Acad. Sci. U.S.A. 104:18730-18735(2007).
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:EDP45624.1}.
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DR EMBL; AAYY01000001; EDP45624.1; -; Genomic_DNA.
DR RefSeq; XP_001732838.1; XM_001732786.1.
DR AlphaFoldDB; A8PR62; -.
DR STRING; 425265.A8PR62; -.
DR GeneID; 5857144; -.
DR KEGG; mgl:MGL_0613; -.
DR VEuPathDB; FungiDB:MGL_0613; -.
DR InParanoid; A8PR62; -.
DR OMA; EFIVIIY; -.
DR OrthoDB; 2897309at2759; -.
DR Proteomes; UP000008837; Unassembled WGS sequence.
DR GO; GO:0005834; C:heterotrimeric G-protein complex; IEA:InterPro.
DR GO; GO:0001664; F:G protein-coupled receptor binding; IEA:InterPro.
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; 1.
DR InterPro; IPR002975; Fungi_Gprotein_alpha.
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:SF363; GUANINE NUCLEOTIDE-BINDING PROTEIN ALPHA-2 SUBUNIT; 1.
DR Pfam; PF00503; G-alpha; 1.
DR PRINTS; PR00318; GPROTEINA.
DR PRINTS; PR01241; GPROTEINAFNG.
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 4: Predicted;
KW GTP-binding {ECO:0000256|ARBA:ARBA00023134};
KW Lipoprotein {ECO:0000256|ARBA:ARBA00023288};
KW Myristate {ECO:0000256|ARBA:ARBA00022707};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Palmitate {ECO:0000256|ARBA:ARBA00023139};
KW Reference proteome {ECO:0000313|Proteomes:UP000008837};
KW Transducer {ECO:0000256|ARBA:ARBA00023224}.
FT REGION 1..23
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 358 AA; 40832 MW; 29A77C9126068CF8 CRC64;
MGLCGSKPEA SGADQDARQR SSEIDKHLVE STKQGKQEYK ILLLGSGESG KSTIVKQMKI
IHQNGYSKEE LYMFRLTVIK NVVDSARAIA LALRLLGMEP ERLENREAAD ILTQYEVPAD
PNAFLPADMG KLIESLWSDP VIPRLMERRD EFYLMDNAEY FLNSVARIAT DTYIPTQEDV
LHARSKTFGV SETRFQTGDM SIHLVDVGGQ RSERSKWIHS FDSVTSVIFC VALSEYDQVL
LEDSSQNRMA ESLVLFESII NSRWFQRSSI ILFLNKIDIF KQKLARRPLS DYFPEYTGGN
DVNKAAKYIL WRFTRVNHAR LNIYPHITQA TDTTNIRLVF AAVKETILQN SLRETGFL
//
