ID A0A2G5HRI3_CERBT Unreviewed; 1049 AA.
AC A0A2G5HRI3;
DT 31-JAN-2018, integrated into UniProtKB/TrEMBL.
DT 31-JAN-2018, sequence version 1.
DT 22-FEB-2023, entry version 17.
DE SubName: Full=Rho guanine nucleotide exchange factor scd1 {ECO:0000313|EMBL:PIA95136.1};
GN ORFNames=CB0940_08341 {ECO:0000313|EMBL:PIA95136.1};
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:PIA95136.1, ECO:0000313|Proteomes:UP000230605};
RN [1] {ECO:0000313|EMBL:PIA95136.1, ECO:0000313|Proteomes:UP000230605}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=09-40 {ECO:0000313|EMBL:PIA95136.1,
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 -!- 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:PIA95136.1}.
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; LKMD01000104; PIA95136.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2G5HRI3; -.
DR OrthoDB; 23973at2759; -.
DR Proteomes; UP000230605; Chromosome 6.
DR GO; GO:0005085; F:guanyl-nucleotide exchange factor activity; IEA:InterPro.
DR CDD; cd05992; PB1; 1.
DR CDD; cd13246; PH_Scd1; 1.
DR CDD; cd00160; RhoGEF; 1.
DR Gene3D; 1.20.900.10; Dbl homology (DH) domain; 1.
DR Gene3D; 2.30.29.30; Pleckstrin-homology domain (PH domain)/Phosphotyrosine-binding domain (PTB); 1.
DR InterPro; IPR010481; Cdc24/Scd1_N.
DR InterPro; IPR033511; Cdc24/Scd1_PH_dom.
DR InterPro; IPR035899; DBL_dom_sf.
DR InterPro; IPR000219; DH-domain.
DR InterPro; IPR000270; PB1_dom.
DR InterPro; IPR011993; PH-like_dom_sf.
DR InterPro; IPR001849; PH_domain.
DR PANTHER; PTHR47339; CELL DIVISION CONTROL PROTEIN 24; 1.
DR PANTHER; PTHR47339:SF1; CELL DIVISION CONTROL PROTEIN 24; 1.
DR Pfam; PF06395; CDC24; 1.
DR Pfam; PF00564; PB1; 1.
DR Pfam; PF15411; PH_10; 1.
DR Pfam; PF00621; RhoGEF; 1.
DR SMART; SM00233; PH; 1.
DR SMART; SM00325; RhoGEF; 1.
DR SUPFAM; SSF54277; CAD & PB1 domains; 1.
DR SUPFAM; SSF48065; DBL homology domain (DH-domain); 1.
DR SUPFAM; SSF50729; PH domain-like; 1.
DR PROSITE; PS50010; DH_2; 1.
PE 4: Predicted;
FT DOMAIN 270..450
FT /note="DH"
FT /evidence="ECO:0000259|PROSITE:PS50010"
FT REGION 1..103
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 602..910
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 33..103
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 614..636
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 666..702
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 715..767
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 821..837
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 882..897
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1049 AA; 116174 MW; 37D58AC1695921D7 CRC64;
MEIASHAHFR ALTAPFSTPG AAPDHAKQQH HPNMSADAAQ SQLLQSQAHT GSNYSIQSQL
TNRSSGATQD TAHSTLFTPP PMPTNASNLS TASMSTPNGS SDVVRTDNIM NSVADASSSL
FQICVALRRR LLGVPGFSES LAEEEEEADD DTDPVTLLWR TFRRGYPLML LYNELRPQQP
LAMPQGVKEE KKAKAATFKF IQACMNDLGM HSEELFIITD LYGDDTTGFV KVARVVNRVL
DVLVQRGLVE DVRPTASDFE EAEKGMKRTQ RQHIIAELVS SERTYVQHLE LLQAFKHLVE
EKGVIPGDAV HDIFLNLNSL LDFQRRFLIR VEQTNYLPEE EQNWGKLFLL YCEAFKVYEP
YIANQRKCEK TVIAEFGKLR EAGGSIEMRQ MVESPTALHS FLMKPFQRLT KYPLLLEQLH
KKGDLDEERK QDLMNGMQAA TSVLNSTNRA VDQEEKREAV QELKHRVEDW KGHRVEGFGE
LLLYGTFTVL KSENLANGKD GERQYHVYLF ETILLCCKNI DPSKPKNKLS NKPMVDNKGK
PKLQLKGRIF MQNVTDLVSL AKPGSYTCQI FWKGDPSIEN FIIRFTTEET LRKWAQQIEV
QRRRYRERAS TTRNSDSSTR GGTSATEFTF MQNQALENPY KEAIDEDDDE DDAETAVGSG
HWSGSGGYPS GLSQSRNGSS SSLRSRSTTG ESSVSNLSGS TARVPPPRLP SGTMQGPLSL
RTRELQQAAQ SPGGQAGMDS YFSPTDSPMS SMSARTSTSS GMYSFPRQNM PANGYYEEGH
GATRFTAPAM GRQPPNGYGP AARVPSTGRP GPAGMHSSMQ MPGPRNRSAS SPDIHNGQRM
QPRGAGHPPL PEMPAPYSNP NRSQNNSPAY PEGIPERGSP QMLRERQSSN ADQTSPVEYN
YPPRPGMMQH ASARAMAPGS TRPPMGGPGP AGFVPPTPVD EEGSKPTPAQ LKVRVICPAA
GQTLTLVVST NISYQTLKDR IDAKLQRSTN LSLGDRGPKE NHVKLKYLDE EDLVSMQSDE
DVQTAFETWK EQRGEGIGGL GEVELYCQR
//
