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Database: UniProt
Entry: A0A319DFL7_9EURO
LinkDB: A0A319DFL7_9EURO
Original site: A0A319DFL7_9EURO 
ID   A0A319DFL7_9EURO        Unreviewed;       934 AA.
AC   A0A319DFL7;
DT   10-OCT-2018, integrated into UniProtKB/TrEMBL.
DT   10-OCT-2018, sequence version 1.
DT   27-MAR-2024, entry version 18.
DE   SubName: Full=Rho guanyl nucleotide exchange factor {ECO:0000313|EMBL:PYH93017.1};
GN   ORFNames=BO71DRAFT_328684 {ECO:0000313|EMBL:PYH93017.1};
OS   Aspergillus ellipticus CBS 707.79.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus.
OX   NCBI_TaxID=1448320 {ECO:0000313|EMBL:PYH93017.1, ECO:0000313|Proteomes:UP000247810};
RN   [1] {ECO:0000313|EMBL:PYH93017.1, ECO:0000313|Proteomes:UP000247810}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CBS 707.79 {ECO:0000313|EMBL:PYH93017.1,
RC   ECO:0000313|Proteomes:UP000247810};
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 (FEB-2018) to the EMBL/GenBank/DDBJ databases.
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DR   EMBL; KZ825902; PYH93017.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A319DFL7; -.
DR   STRING; 1448320.A0A319DFL7; -.
DR   Proteomes; UP000247810; 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:UP000247810};
KW   Transferase {ECO:0000256|ARBA:ARBA00022676}.
FT   DOMAIN          178..357
FT                   /note="DH"
FT                   /evidence="ECO:0000259|PROSITE:PS50010"
FT   DOMAIN          836..932
FT                   /note="PB1"
FT                   /evidence="ECO:0000259|PROSITE:PS51745"
FT   REGION          567..730
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          761..830
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        606..663
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        672..692
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        761..794
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   934 AA;  105086 MW;  FB2FD16AC221C2E0 CRC64;
     MAETVIMSGA PIAEDNIINR RGGESMYQSC VNLKKRLAEV PNFEPHMREM EEADSEQGNT
     DPVASLWNCL RTGYPLLTIY NASGPDEYLE IDTTKVAEAK RPKAATFKFL QASLQELAFP
     QQDCFLITDL YGENTTGFTK VIKMVNRVLD ILEMQGQLKR PSDSTSRAPA QGTVKLTKRE
     HILKELLETE RDYVHHLQNL QALKKELEET GALTGDASHQ IFLNLNNLLD FAQRFLIRIE
     QHYALPEERQ NWGELFIQHE DAFPQYEPFI ANQMRCDEVC LRDWDKIHVA PRSKDLLQMV
     AQPATLNGFF VKPFQRLTKY PLMLGELLKQ TENPDLRIDI QRAIDTIQSV LDSANDAIDK
     EHLQTAVKDL DERVDDWKAL KIDAFGDLLR FGTFSVIKGD NGKDSEREYH IYLFERILLC
     CKDINPNKQK SKLNLGKDKP SATAKGKARL QLKGRIYMAN VTDVLCMPKP GSYRIQIFWK
     GDPGVVDNFI IRYQNESIMR KWSGDIEAQR SIQAEQRNVR NTGTSETEFT YMKSMANMPN
     PYLENDEEQA ATKEAAFFSE FPMSRNASST SLRTRSATGG SGGAGPPLSI GRPPRFPVPD
     PSLSVHTHFS GGSMSPAERN ANSYFSPVAD TASTRSSSQS TGFSYTSSRQ TTPTNNWNEE
     NARYTAPALS RATSRDGPNS NPYFNGNPPN GRAAQRPSLP PMSGAQAAAA NGMAQRMRSA
     SSPDIHNHNP EVRRYMGAHT MQTVDNVPVP PIPAHMASMK APVNRSQTNS PTNGSLPIRN
     VNHLSNSQQH PDQRHMTPTH FHEPQYGDHR PGTSAGDQPT SPLSYEPDEE PLMPTQLKVK
     VNFDDNYVTL VIASNIMFRS LIDRVDAKLA RFTHRSIGSK SVRLRYRDED GDFVTIDSDE
     AVQLAFMEWR EQQRDMLARG QVGEIQLYCQ AVET
//
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