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Database: UniProt
Entry: A0A2G5I9H4_CERBT
LinkDB: A0A2G5I9H4_CERBT
Original site: A0A2G5I9H4_CERBT 
ID   A0A2G5I9H4_CERBT        Unreviewed;       353 AA.
AC   A0A2G5I9H4;
DT   31-JAN-2018, integrated into UniProtKB/TrEMBL.
DT   31-JAN-2018, sequence version 1.
DT   27-MAR-2024, entry version 21.
DE   SubName: Full=Guanine nucleotide-binding protein subunit alpha {ECO:0000313|EMBL:PIB01467.1};
GN   ORFNames=CB0940_00321 {ECO:0000313|EMBL:PIB01467.1};
OS   Cercospora beticola (Sugarbeet leaf spot fungus).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC   Dothideomycetidae; Mycosphaerellales; Mycosphaerellaceae; Cercospora.
OX   NCBI_TaxID=122368 {ECO:0000313|EMBL:PIB01467.1, ECO:0000313|Proteomes:UP000230605};
RN   [1] {ECO:0000313|EMBL:PIB01467.1, ECO:0000313|Proteomes:UP000230605}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=09-40 {ECO:0000313|EMBL:PIB01467.1,
RC   ECO:0000313|Proteomes:UP000230605};
RA   De Jonge R., Ebert M.K., Suttle J.C., Jurick Ii W.M., Secor G.A.,
RA   Thomma B.P., Van De Peer Y., Bolton M.D.;
RT   "The cercosporin biosynthetic gene cluster was horizontally transferred to
RT   several fungal lineages and shown to be expanded in Cercospora beticola
RT   based on microsynteny with recipient genomes.";
RL   Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
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:PIB01467.1}.
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DR   EMBL; LKMD01000100; PIB01467.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A2G5I9H4; -.
DR   OrthoDB; 2897309at2759; -.
DR   Proteomes; UP000230605; Chromosome 1.
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:0046872; F:metal ion binding; IEA:UniProtKB-KW.
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:SF355; GUANINE NUCLEOTIDE-BINDING PROTEIN G(O) SUBUNIT ALPHA; 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   Coiled coil {ECO:0000256|SAM:Coils};
KW   GTP-binding {ECO:0000256|ARBA:ARBA00023134};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW   Transducer {ECO:0000256|ARBA:ARBA00023224}.
FT   COILED          9..36
FT                   /evidence="ECO:0000256|SAM:Coils"
SQ   SEQUENCE   353 AA;  40691 MW;  5D1BE7A0FD8F1FEE CRC64;
     MGCGQSSESK EGKQRNEEIE NQLKRDKMNL RNEIKMLLLG AGESGKSTIL KQMKLIHEGG
     YSRDERESFR EIIFSNTVQS MRVILEAMES LELPLDDQRA EYHVQTIFMQ PAQIEGDVLP
     PEVGQAIKTL WADAGVQSAF QRSREYQLND SAKYYFDSID TIASPTYIPS DQDVLRSRVK
     TTGITETTFI IGDLTYRMFD VGGQRSERKK WIHCFENVTT ILFLVAISEY DQLLFEDETV
     NRMQEALTLF DSICNSRWFT KTSIILFLNK IDRFKEKLPV SPMKNYFPDY EGGQDYGAAC
     DYILNRFVSL NQHPTKQIYT HFTCATDTMQ IRFVMAAVND IIIQENLRMC GLI
//
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