ID   I4YBP3_WALMC            Unreviewed;       353 AA.
AC   I4YBP3;
DT   05-SEP-2012, integrated into UniProtKB/TrEMBL.
DT   05-SEP-2012, sequence version 1.
DT   27-NOV-2024, entry version 57.
DE   RecName: Full=Guanine nucleotide binding protein, alpha subunit {ECO:0008006|Google:ProtNLM};
DE   Flags: Fragment;
GN   ORFNames=WALSEDRAFT_7927 {ECO:0000313|EMBL:EIM21385.1};
OS   Wallemia mellicola (strain ATCC MYA-4683 / CBS 633.66) (Wallemia sebi (CBS
OS   633.66)).
OC   Eukaryota; Fungi; Dikarya; Basidiomycota; Wallemiomycotina;
OC   Wallemiomycetes; Wallemiales; Wallemiaceae; Wallemia.
OX   NCBI_TaxID=671144 {ECO:0000313|EMBL:EIM21385.1, ECO:0000313|Proteomes:UP000005242};
RN   [1] {ECO:0000313|EMBL:EIM21385.1, ECO:0000313|Proteomes:UP000005242}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC MYA-4683 / CBS 633.66 {ECO:0000313|Proteomes:UP000005242};
RX   PubMed=22326418; DOI=10.1016/j.fgb.2012.01.007;
RA   Padamsee M., Kumar T.K.A., Riley R., Binder M., Boyd A., Calvo A.M.,
RA   Furukawa K., Hesse C., Hohmann S., James T.Y., LaButti K., Lapidus A.,
RA   Lindquist E., Lucas S., Miller K., Shantappa S., Grigoriev I.V.,
RA   Hibbett D.S., McLaughlin D.J., Spatafora J.W., Aime M.C.;
RT   "The genome of the xerotolerant mold Wallemia sebi reveals adaptations to
RT   osmotic stress and suggests cryptic sexual reproduction.";
RL   Fungal Genet. Biol. 49:217-226(2012).
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DR   EMBL; JH668233; EIM21385.1; -; Genomic_DNA.
DR   RefSeq; XP_006958572.1; XM_006958510.1.
DR   AlphaFoldDB; I4YBP3; -.
DR   STRING; 671144.I4YBP3; -.
DR   GeneID; 18475831; -.
DR   KEGG; wse:WALSEDRAFT_7927; -.
DR   eggNOG; KOG0082; Eukaryota.
DR   HOGENOM; CLU_014184_6_0_1; -.
DR   InParanoid; I4YBP3; -.
DR   OMA; EHQSEFY; -.
DR   OrthoDB; 1708070at2759; -.
DR   Proteomes; UP000005242; 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:0007189; P:adenylate cyclase-activating G protein-coupled receptor signaling pathway; IEA:TreeGrafter.
DR   CDD; cd00066; G-alpha; 1.
DR   FunFam; 1.10.400.10:FF:000007; Guanine nucleotide-binding protein subunit alpha; 1.
DR   FunFam; 3.40.50.300:FF:000181; Guanine nucleotide-binding protein subunit alpha; 1.
DR   FunFam; 3.40.50.300:FF:000692; Guanine nucleotide-binding protein subunit 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, ECO:0000256|PIRSR:PIRSR601019-
KW   1}; Lipoprotein {ECO:0000256|ARBA:ARBA00023288};
KW   Magnesium {ECO:0000256|PIRSR:PIRSR601019-2};
KW   Metal-binding {ECO:0000256|PIRSR:PIRSR601019-2};
KW   Myristate {ECO:0000256|ARBA:ARBA00022707};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW   ECO:0000256|PIRSR:PIRSR601019-1};
KW   Palmitate {ECO:0000256|ARBA:ARBA00023139};
KW   Reference proteome {ECO:0000313|Proteomes:UP000005242};
KW   Transducer {ECO:0000256|ARBA:ARBA00023224}.
FT   BINDING         43..48
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR601019-1"
FT   BINDING         47
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR601019-2"
FT   BINDING         151..152
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR601019-1"
FT   BINDING         176..182
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR601019-1"
FT   BINDING         182
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR601019-2"
FT   BINDING         201..205
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR601019-1"
FT   BINDING         270..273
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR601019-1"
FT   BINDING         325
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR601019-1"
FT   NON_TER         353
FT                   /evidence="ECO:0000313|EMBL:EIM21385.1"
SQ   SEQUENCE   353 AA;  40592 MW;  964D19236A32C34D CRC64;
     MGLCSSKQDK NGKQRSLEID KQLEDDAKKM RRDCKILLLG SGESGKSTIV KQMKIIHQNG
     YSKEELIGFR LIVFKNVVDS AQSVVLALRK LSMEPISNTN QHYADYILGF RLDLEPGMTL
     NKELVNAIDS LWNDPIIPKL LDRSSEWYLM DSAPYFFQNV HRIGNQDYIP NENDVLRARI
     KTTGITETRF TMGQLSIHMF DVGGQRSERK KWIHCFEAVT SIIFCVAISE YDQTLLEESG
     QNRMQESLVL FESVINSRWF LRTSIILFMN KVDVFRVKIT KVPLEKYFPE YSGGAELNKA
     AKYILWRFTQ TNRARLSIYP HLTQATDTSN IRLVFAAVKE TILQNALRDS GIL
//