ID D4D2N3_TRIVH Unreviewed; 384 AA.
AC D4D2N3;
DT 18-MAY-2010, integrated into UniProtKB/TrEMBL.
DT 18-MAY-2010, sequence version 1.
DT 13-SEP-2023, entry version 62.
DE RecName: Full=G protein complex alpha subunit GanA {ECO:0008006|Google:ProtNLM};
GN ORFNames=TRV_01339 {ECO:0000313|EMBL:EFE43897.1};
OS Trichophyton verrucosum (strain HKI 0517).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Onygenales; Arthrodermataceae; Trichophyton.
OX NCBI_TaxID=663202 {ECO:0000313|EMBL:EFE43897.1, ECO:0000313|Proteomes:UP000008383};
RN [1] {ECO:0000313|Proteomes:UP000008383}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=HKI 0517 {ECO:0000313|Proteomes:UP000008383};
RX PubMed=21247460; DOI=10.1186/gb-2011-12-1-r7;
RA Burmester A., Shelest E., Gloeckner G., Heddergott C., Schindler S.,
RA Staib P., Heidel A., Felder M., Petzold A., Szafranski K., Feuermann M.,
RA Pedruzzi I., Priebe S., Groth M., Winkler R., Li W., Kniemeyer O.,
RA Schroeckh V., Hertweck C., Hube B., White T.C., Platzer M., Guthke R.,
RA Heitman J., Woestemeyer J., Zipfel P.F., Monod M., Brakhage A.A.;
RT "Comparative and functional genomics provide insights into the
RT pathogenicity of dermatophytic fungi.";
RL Genome Biol. 12:R7.1-R7.16(2011).
CC -!- SIMILARITY: Belongs to the G-alpha family. G(q) subfamily.
CC {ECO:0000256|ARBA:ARBA00007976}.
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:EFE43897.1}.
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DR EMBL; ACYE01000073; EFE43897.1; -; Genomic_DNA.
DR RefSeq; XP_003024508.1; XM_003024462.1.
DR AlphaFoldDB; D4D2N3; -.
DR GeneID; 9579731; -.
DR KEGG; tve:TRV_01339; -.
DR HOGENOM; CLU_014184_6_0_1; -.
DR OrthoDB; 2897309at2759; -.
DR Proteomes; UP000008383; 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:SF242; GUANINE NUCLEOTIDE-BINDING PROTEIN ALPHA-1 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 3: Inferred from homology;
KW GTP-binding {ECO:0000256|ARBA:ARBA00023134};
KW Membrane {ECO:0000256|SAM:Phobius};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Transducer {ECO:0000256|ARBA:ARBA00023224};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 158..179
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
SQ SEQUENCE 384 AA; 43712 MW; 404DDD43CBE5FCA1 CRC64;
MGCMNSKDIS PEMKEQGKHS AAIDKVIRAD KKKYDRTVKI LLLGAGESGK STIIKQMRII
HSGGFPIDER RQTRAVIYSN MIVAFKLLIE IMEAENISFE HEATEPLAHF IQTSEADVEC
DEAFTDIKVR EAVKTMWEDA GVQKAVARGH DKFGQESLSL SLSLTIAVLS AFFFLKLAIL
TDCGSYFNSL DRIFTPGWLP NNQDMLHSRL RTTGITETLF ELGQINFRMM DVGGQRSERK
KWIHCFEGVQ CLLFMVALSG YDQCLVEDQT ANQMHEAMML FESLVNGEWF KRKPVILFLN
KIDLFKEKLA ISPVSKHFPD YSGRDGDFEA SAKYFADRFR GITRVPEREI YTHYTNATDT
TLLKATMDSV QDMIIQKNLN NLIL
//
