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). 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; 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 //