ID A0A0M3QZQ2_DROBS Unreviewed; 1660 AA.
AC A0A0M3QZQ2;
DT 09-DEC-2015, integrated into UniProtKB/TrEMBL.
DT 09-DEC-2015, sequence version 1.
DT 27-MAR-2024, entry version 31.
DE SubName: Full=CG43658 {ECO:0000313|EMBL:ALC49813.1};
GN ORFNames=Dbus_chrXg1669 {ECO:0000313|EMBL:ALC49813.1};
OS Drosophila busckii (Fruit fly).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC Drosophilidae; Drosophila.
OX NCBI_TaxID=30019 {ECO:0000313|EMBL:ALC49813.1, ECO:0000313|Proteomes:UP000494163};
RN [1] {ECO:0000313|EMBL:ALC49813.1, ECO:0000313|Proteomes:UP000494163}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC TISSUE=Whole larvae {ECO:0000313|EMBL:ALC49813.1};
RA Zhou Q., Bachtrog D.;
RT "Ancestral chromatin configuration constrains chromatin evolution on
RT differentiating sex chromosomes in Drosophila.";
RL Submitted (AUG-2015) to the EMBL/GenBank/DDBJ databases.
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DR EMBL; CP012528; ALC49813.1; -; Genomic_DNA.
DR SMR; A0A0M3QZQ2; -.
DR STRING; 30019.A0A0M3QZQ2; -.
DR OMA; ANRFDMD; -.
DR Proteomes; UP000494163; Chromosome x sequence.
DR GO; GO:0005085; F:guanyl-nucleotide exchange factor activity; IEA:InterPro.
DR GO; GO:0016043; P:cellular component organization; IEA:UniProt.
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; IPR039919; ARHGEF10/ARHGEF17.
DR InterPro; IPR035899; DBL_dom_sf.
DR InterPro; IPR000219; DH-domain.
DR InterPro; IPR011993; PH-like_dom_sf.
DR InterPro; IPR011047; Quinoprotein_ADH-like_supfam.
DR PANTHER; PTHR12877; RHO GUANINE NUCLEOTIDE EXCHANGE FACTOR; 1.
DR PANTHER; PTHR12877:SF7; RHO GUANINE NUCLEOTIDE EXCHANGE FACTOR 10-LIKE PROTEIN; 1.
DR Pfam; PF19057; PH_19; 2.
DR Pfam; PF00621; RhoGEF; 1.
DR Pfam; PF19056; WD40_2; 1.
DR SMART; SM00325; RhoGEF; 1.
DR SUPFAM; SSF48065; DBL homology domain (DH-domain); 1.
DR SUPFAM; SSF50729; PH domain-like; 1.
DR SUPFAM; SSF50998; Quinoprotein alcohol dehydrogenase-like; 1.
DR PROSITE; PS50010; DH_2; 1.
PE 4: Predicted;
KW Coiled coil {ECO:0000256|SAM:Coils};
KW Reference proteome {ECO:0000313|Proteomes:UP000494163}.
FT DOMAIN 382..569
FT /note="DH"
FT /evidence="ECO:0000259|PROSITE:PS50010"
FT REGION 72..253
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1289..1326
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1354..1390
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1497..1586
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1606..1639
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 549..582
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 74..89
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 108..134
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 143..169
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 176..250
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1497..1526
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1566..1584
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1660 AA; 178605 MW; 8B602B072B347050 CRC64;
MTNASCLHSA FSRRIAEQQQ QQQQQQQLEQ QHRLRSDCSK EVATIAGGSF SSANGGNQAA
VGVGLGLGLS HARGVGGSSS SSSSERDTKS PCRLVGGGGG GGEESSSTAA AAIGTPTAAA
ATSSRATAPT VSHSDEEVLT EEEQSSSSVS SLSAGNQRNS QLRSTFNKAK QHLSFDKWRT
ANSSTTSSTT SNPTPPQLLL NSDPPTNANM IMRRASACNV PSPGSQQQQQ QQQQQQQHRE
EITTPGESPT VGRLSRWFSI RRASSHLYDV GARQSFDMPD AAAAMSSAKS SPAASSAADV
GSPQKLANLG ASKMMPDVPE YEDDEGAVAG STGDAGATGR YDMDLMLPSG SRANGSARAV
NSRLIVPALP PAPPGLSQQQ LKRRHIVAAI VHSENSYVAT LQRLVNDYKK PLEECSPPVL
NSVKIATLFH CLPDILHSHK LFRISLAECV RNWDRDEKIG DCFVSAFGKP QLLEIYSGFI
NNFSVAMELA KMEEKRKSAL ADFFKVKQIS AHDRLSFFGL MVKPVQRFPQ FILFLQDLLK
YTPQGHHDRM SLQLALSQLE LLAELLNERK REAEQYQAFK EMLGHISGTF NTRALSSVAS
DASGNRARYL LREDNVTHME FNQAGSIIKC KQRRLLLLND KVICVSVAPK QSHDFGATEK
LTFKWMFPVN DVEIVDNSTS ATLSRILTAG LNRGGSLKSN ASNGPCSSAY ANATLGAHGG
AGGSPFGGFG DSHSSPAAQL TNGADNLCNE MSTLMYDYEV ISRIHDLVGS LKGSYKELNT
NTTRNVLNLI QGSIQRKDEE MAWVDACCLQ LIGRHKSGKE ETFTFQTQTP NVKKEWITEL
RLAQLALDPN NSPAWERSTN ATSHAQQHAQ MQALHLSSQL SGACAAPLAA AEQQQRQSRK
MPLFVKAMPV YRSQHQTEVR CGCYYSIAND TKQSGNARRR HKQLNYLWMC SSDGSSSHIT
VLAQHPQQAG NLREAGAFDL VETQVAALEF VKGVDQVRTR EEHSSLLGDL VWLGTESRRL
LIYSARNPEQ EEQLGSYAVP GAVQRILYHF DAVYVALSNA SVLIYRRAHD GVWQLRDPQL
VALGDSGLPV PSLLPINMNI YASCANRVYV LNALNGELQR SFEVHHGASQ QVNLMAHSGI
GLWISLKHST MLCLYHTETF KHLQDINIAS SVLRHDAKKE QPLNNSSVYV TALMACKGLL
WVGTNVGIAV TIPLPRLEGV PIISGGINMS CHAHFGPITF LLPLIPKVYP AYKPPAMPLV
PSMGDDLQLP AIDADPKSDL DETSGVVLRR DLPKEESPSA ATAATPSAGA AACSPRSSKL
DKQHSLDQSF TAKIRASLAN SPAFHRKRFR DLGDASSARM SKTLPRGLGS SAAAGGGASG
APASSSSSSG GQAYGEHGYC DVYGLYGKLI FVKEDYDAEE GTQGNLMDMM YEGMRRSDPE
LAAIPGKVCT LDRRLRMKAS RPRSLDLSNW SVDSKSSSLY TSSGSEESMG IRLFGGRSVS
RNSSSASHKT SGTGSDLGNI SENGLMTITD HMPPKEEPLL PAQPALEAEK QAAAAAAPPA
AVATLKRKQK QNSKQQQQAS ADGPRTVITL MGGRGYWRHV WYNSSASSPG HKSSGSSSGS
GSISGAGGSN APGSSGGASC CSPLTANSND AHIVVWEKKL
//
