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Database: UniProt
Entry: A0A2G5I1T9_CERBT
LinkDB: A0A2G5I1T9_CERBT
Original site: A0A2G5I1T9_CERBT 
ID   A0A2G5I1T9_CERBT        Unreviewed;       498 AA.
AC   A0A2G5I1T9;
DT   31-JAN-2018, integrated into UniProtKB/TrEMBL.
DT   31-JAN-2018, sequence version 1.
DT   27-MAR-2024, entry version 18.
DE   RecName: Full=G protein-coupled receptor GPR1 C-terminal domain-containing protein {ECO:0000259|Pfam:PF11970};
GN   ORFNames=CB0940_03733 {ECO:0000313|EMBL:PIA98718.1};
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:PIA98718.1, ECO:0000313|Proteomes:UP000230605};
RN   [1] {ECO:0000313|EMBL:PIA98718.1, ECO:0000313|Proteomes:UP000230605}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=09-40 {ECO:0000313|EMBL:PIA98718.1,
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   -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-
CC       pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
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:PIA98718.1}.
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DR   EMBL; LKMD01000101; PIA98718.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A2G5I1T9; -.
DR   OrthoDB; 2682754at2759; -.
DR   Proteomes; UP000230605; Chromosome 3.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0007165; P:signal transduction; IEA:UniProt.
DR   Gene3D; 1.20.1070.10; Rhodopsin 7-helix transmembrane proteins; 1.
DR   InterPro; IPR022596; GPR1_C.
DR   PANTHER; PTHR23112; G PROTEIN-COUPLED RECEPTOR 157-RELATED; 1.
DR   PANTHER; PTHR23112:SF0; G-PROTEIN COUPLED RECEPTOR 157; 1.
DR   Pfam; PF11970; GPR_Gpa2_C; 1.
DR   SUPFAM; SSF81321; Family A G protein-coupled receptor-like; 1.
PE   4: Predicted;
KW   G-protein coupled receptor {ECO:0000256|ARBA:ARBA00023040};
KW   Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW   Receptor {ECO:0000256|ARBA:ARBA00023170};
KW   Transducer {ECO:0000256|ARBA:ARBA00023224};
KW   Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW   ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        26..52
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        64..87
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        107..128
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        140..163
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        191..212
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        233..254
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          225..293
FT                   /note="G protein-coupled receptor GPR1 C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF11970"
FT   REGION          330..349
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          389..462
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          475..498
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        390..417
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        418..438
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        439..453
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        475..491
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   498 AA;  55944 MW;  F53ADD1C2878882D CRC64;
     MATDAIHAPN GAKSLSPLPP VIHRGLSAIT AFGLLSLLST AVLFIHLVYR LFRRDKSTFP
     RFHQYLILLI NLLFADLQQA LGFVLSLQWL ADNGIFALTP SCWTQAWFLN TGDVSSCVST
     LAMACHLFGD IIFDYRLSRI PFLISIAGIW TFSLFLATIG IIMHPHDFYM RAGMWCWINE
     EYMHERLWLH YVWILFTEFA VVGLYTTMFI VLQRRIKDFF YVSSQHQMRA ESAARSVIIY
     PVVYVICTLP AVVARLRDMT GHSVGYAELT FVGVMMTSNG WLDVLVYALT RQSLVFGMQA
     PDGEDENVHG LDTFTSWDPY HHDELRDQLT DLSPPMSYGS KGRKKEQQAF NRKDSMTGLL
     PGDPFAKQPP VVQYYDQGLA APQSVVRITR SEGDLRKPGM RFPRRRDPSR NVRTASPEEE
     KQVTLLQCSA APGEQSKNGK TSEQRHDSIQ AEDGIDPDGI GIAIDGIRTA TDSIGIARSE
     SPSTSGSHQV VKEPAERT
//
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