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Database: UniProt
Entry: A0A317WQN1_9EURO
LinkDB: A0A317WQN1_9EURO
Original site: A0A317WQN1_9EURO 
ID   A0A317WQN1_9EURO        Unreviewed;       932 AA.
AC   A0A317WQN1;
DT   10-OCT-2018, integrated into UniProtKB/TrEMBL.
DT   10-OCT-2018, sequence version 1.
DT   27-MAR-2024, entry version 19.
DE   SubName: Full=Rho guanyl nucleotide exchange factor {ECO:0000313|EMBL:PWY87592.1};
GN   ORFNames=BO70DRAFT_287815 {ECO:0000313|EMBL:PWY87592.1};
OS   Aspergillus heteromorphus CBS 117.55.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus.
OX   NCBI_TaxID=1448321 {ECO:0000313|EMBL:PWY87592.1, ECO:0000313|Proteomes:UP000247233};
RN   [1] {ECO:0000313|EMBL:PWY87592.1, ECO:0000313|Proteomes:UP000247233}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CBS 117.55 {ECO:0000313|EMBL:PWY87592.1,
RC   ECO:0000313|Proteomes:UP000247233};
RG   DOE Joint Genome Institute;
RA   Vesth T.C., Nybo J., Theobald S., Brandl J., Frisvad J.C., Nielsen K.F.,
RA   Lyhne E.K., Kogle M.E., Kuo A., Riley R., Clum A., Nolan M., Lipzen A.,
RA   Salamov A., Henrissat B., Wiebenga A., De Vries R.P., Grigoriev I.V.,
RA   Mortensen U.H., Andersen M.R., Baker S.E.;
RT   "The genomes of Aspergillus section Nigri reveals drivers in fungal
RT   speciation.";
RL   Submitted (DEC-2016) 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:PWY87592.1}.
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DR   EMBL; MSFL01000006; PWY87592.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A317WQN1; -.
DR   STRING; 1448321.A0A317WQN1; -.
DR   VEuPathDB; FungiDB:BO70DRAFT_287815; -.
DR   OrthoDB; 23973at2759; -.
DR   Proteomes; UP000247233; Unassembled WGS sequence.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
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.
DR   PROSITE; PS51745; PB1; 1.
PE   4: Predicted;
KW   Glycosyltransferase {ECO:0000256|ARBA:ARBA00022676};
KW   Reference proteome {ECO:0000313|Proteomes:UP000247233};
KW   Transferase {ECO:0000256|ARBA:ARBA00022676}.
FT   DOMAIN          178..357
FT                   /note="DH"
FT                   /evidence="ECO:0000259|PROSITE:PS50010"
FT   DOMAIN          834..930
FT                   /note="PB1"
FT                   /evidence="ECO:0000259|PROSITE:PS51745"
FT   REGION          566..726
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          759..828
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        566..581
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        608..666
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        675..690
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        759..792
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   932 AA;  104913 MW;  98352CE12F0F46ED CRC64;
     MAETVIMSGA PIAEDNIINR RGGESMYQTC VNLKKRLAEV PNFEPHMREM EEADMAQGNT
     DPVASLWNCL RTGYPLLTIY NASGPEEYLE IDTTKVAEAK RPKAATFKFL QASLQKLDFP
     QQDCFLITDL YGENTTGFTK VIKMVNLVLD ILEMQGQLKR PSDDASRAPA QGTIKLTKRE
     HILKELLETE RDYVHHLQNL QALKKELEET GALTGDASHQ IFLNLNNLLD FAQRFLIRIE
     QHYALPEERQ NWGELFIQHE DAFPQYEPFI ANQMRCDEVC LRDWDKIHEA PRSKDLLQMV
     AQPATLNGFF VKPFQRLTKY PLMLGELLKQ TENPDLRIDI QRAIDTIQSV LDSANDAIDK
     EHLQTAVKDL AERVDDWKTL KIEAFGDLLR FGTFSVIKGD SAKDSEREYH IYLFERILLC
     CKDINPNKQK SKLNLGKDKP ATTARGKARL QLKGRIYMAN VTDVLCMPKP GSYRIQIFWK
     GDPNVVDNFI IRYQNESIMR KWANDIDAQR LIQTEQRNVR NTGTSETEFT YMKSVTNMPN
     PYLENDEEQA ATKEAAFFSE FPMSRNASST SLRTRSATGG SGGSGPPPPL SVGRPPRFAV
     PDPSLSVHTH FSGGSMSPAE RNAPSYFSPV ADTASTRSSS QSTGFSYTSS SRQTTPTNTW
     NEENARYTAP ALSRATSRDG PNSNTFFSGA PGRAAQRPSL PPMSGPQAAN GIARMRSASS
     PDIHAHNPEM RRYMGAHTMQ TVDNVPVPPI PAHMASMKAP VNRSQTNSPT NGNLPIPSAN
     HLSNSQQHPD QRHMTPTHFH EPQYSDHRPG TSAGDQPTSP LSYEPDEEPL MPTQLKVKVN
     FDDNYVTLVI ASNIMFRSLI DRVDAKLARF THRSIGSKSV RLRYRDEDGD FVTIDSDEAV
     QLAFMEWREQ QRDMLARGQV GEIQLYCQAV ET
//
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