ID A2QNB9_ASPNC Unreviewed; 1198 AA.
AC A2QNB9;
DT 06-MAR-2007, integrated into UniProtKB/TrEMBL.
DT 06-MAR-2007, sequence version 1.
DT 27-MAR-2024, entry version 87.
DE SubName: Full=Contig An07c0130, genomic contig {ECO:0000313|EMBL:CAK39428.1};
GN ORFNames=An07g05090 {ECO:0000313|EMBL:CAK39428.1};
OS Aspergillus niger (strain ATCC MYA-4892 / CBS 513.88 / FGSC A1513).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC Aspergillus subgen. Circumdati.
OX NCBI_TaxID=425011 {ECO:0000313|EMBL:CAK39428.1, ECO:0000313|Proteomes:UP000006706};
RN [1] {ECO:0000313|EMBL:CAK39428.1, ECO:0000313|Proteomes:UP000006706}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 513.88 / FGSC A1513 / ATCC MYA-4892
RC {ECO:0000313|Proteomes:UP000006706};
RX PubMed=17259976; DOI=10.1038/nbt1282;
RA Pel H.J., de Winde J.H., Archer D.B., Dyer P.S., Hofmann G., Schaap P.J.,
RA Turner G., de Vries R.P., Albang R., Albermann K., Andersen M.R.,
RA Bendtsen J.D., Benen J.A., van den Berg M., Breestraat S., Caddick M.X.,
RA Contreras R., Cornell M., Coutinho P.M., Danchin E.G., Debets A.J.,
RA Dekker P., van Dijck P.W., van Dijk A., Dijkhuizen L., Driessen A.J.,
RA d'Enfert C., Geysens S., Goosen C., Groot G.S., de Groot P.W.,
RA Guillemette T., Henrissat B., Herweijer M., van den Hombergh J.P.,
RA van den Hondel C.A., van der Heijden R.T., van der Kaaij R.M., Klis F.M.,
RA Kools H.J., Kubicek C.P., van Kuyk P.A., Lauber J., Lu X.,
RA van der Maarel M.J., Meulenberg R., Menke H., Mortimer M.A., Nielsen J.,
RA Oliver S.G., Olsthoorn M., Pal K., van Peij N.N., Ram A.F., Rinas U.,
RA Roubos J.A., Sagt C.M., Schmoll M., Sun J., Ussery D., Varga J.,
RA Vervecken W., van de Vondervoort P.J., Wedler H., Wosten H.A., Zeng A.P.,
RA van Ooyen A.J., Visser J., Stam H.;
RT "Genome sequencing and analysis of the versatile cell factory Aspergillus
RT niger CBS 513.88.";
RL Nat. Biotechnol. 25:221-231(2007).
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DR EMBL; AM270131; CAK39428.1; -; Genomic_DNA.
DR RefSeq; XP_001391592.1; XM_001391555.2.
DR AlphaFoldDB; A2QNB9; -.
DR EnsemblFungi; CAK39428; CAK39428; An07g05090.
DR GeneID; 4981776; -.
DR KEGG; ang:An07g05090; -.
DR VEuPathDB; FungiDB:An07g05090; -.
DR HOGENOM; CLU_001251_6_0_1; -.
DR OrthoDB; 5100844at2759; -.
DR Proteomes; UP000006706; Chromosome 4L.
DR GO; GO:0005085; F:guanyl-nucleotide exchange factor activity; IEA:InterPro.
DR GO; GO:0035556; P:intracellular signal transduction; IEA:InterPro.
DR CDD; cd04435; DEP_fRom2; 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 Gene3D; 1.10.10.10; Winged helix-like DNA-binding domain superfamily/Winged helix DNA-binding domain; 1.
DR InterPro; IPR001180; CNH_dom.
DR InterPro; IPR035899; DBL_dom_sf.
DR InterPro; IPR000591; DEP_dom.
DR InterPro; IPR000219; DH-domain.
DR InterPro; IPR011993; PH-like_dom_sf.
DR InterPro; IPR041675; PH_5.
DR InterPro; IPR036388; WH-like_DNA-bd_sf.
DR InterPro; IPR036390; WH_DNA-bd_sf.
DR PANTHER; PTHR46572; RHO1 GDP-GTP EXCHANGE PROTEIN 1-RELATED; 1.
DR PANTHER; PTHR46572:SF2; RHO1 GDP-GTP EXCHANGE PROTEIN 1-RELATED; 1.
DR Pfam; PF00780; CNH; 1.
DR Pfam; PF00610; DEP; 1.
DR Pfam; PF15405; PH_5; 1.
DR Pfam; PF00621; RhoGEF; 1.
DR SMART; SM00036; CNH; 1.
DR SMART; SM00049; DEP; 1.
DR SMART; SM00325; RhoGEF; 1.
DR SUPFAM; SSF48065; DBL homology domain (DH-domain); 1.
DR SUPFAM; SSF46785; Winged helix' DNA-binding domain; 1.
DR PROSITE; PS50219; CNH; 1.
DR PROSITE; PS50186; DEP; 1.
DR PROSITE; PS50010; DH_2; 1.
PE 4: Predicted;
KW Reference proteome {ECO:0000313|Proteomes:UP000006706}.
FT DOMAIN 330..405
FT /note="DEP"
FT /evidence="ECO:0000259|PROSITE:PS50186"
FT DOMAIN 500..692
FT /note="DH"
FT /evidence="ECO:0000259|PROSITE:PS50010"
FT DOMAIN 876..1174
FT /note="CNH"
FT /evidence="ECO:0000259|PROSITE:PS50219"
FT REGION 1..207
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 221..250
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 453..478
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 35..62
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 64..78
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 91..105
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 171..192
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1198 AA; 135422 MW; F6B8C32936EC0978 CRC64;
MADLGGQQGR NYRPYGHPSA FQRDAAFSEI FGGAPGRSQT MTSQTPQFSQ DRAHTMSSHV
PHPQMQRGPP PPARQMQNGY PPGTPNGYYQ PYGGSAATMT SQHPSQNPPR PYPGRSAYPQ
PQRLDSRPNH GPQYPDAKGY ARQVPHPALN SDAYRSRSMA RLGGPPIYQP PSSGFNHTSA
TYSRQQPYNP GAAPMTPQGR VVPERNQNER SMSLTTYSTD RDHAHTTQTG RVIPPRRQPS
GPSPPPEASY PADVINAYEV NGKSRPPSDG SMNSRTMSMA STVVPDRTMS MQSQIAPKPS
NTSTLVPSNS RRSKVPLVYP ALLSKVADVF RERITLAERQ KNGLSYQNAF SGAEAVDLIA
YIIKTMDRNL ALLLGRALDA QKFFHDVTYD HRLRDAPGEL YQFKETMGEE APSSEVNGVF
TLLTECYSPT CTRDSLCYSI ACPRRLEQQA RLNLKPQPGL RSSASKGSLH GDDDDNDNQK
LWINMVPKEI SDGIDDREKK RQEIIFEIMY TERDFVKDLE YLRDFWMRPL RSAGNANLSP
IPEHRREKFI RTVFGNCLEV LKVNGGLCEA LNARQKENHV VKTVGDIFLQ HVPRFDPFIK
YGANQLYGKY EFEKEKASNP AFARFVEETE RLKESRKLEL NGYLTKPTTR LARYPLLLEQ
VAKNTADDNP DKQDIPKAIK LIKDFLSRVN AESGRAENHF NLVQLNSALK FPPGEYVDLK
LTEENRQMLT KMAFKKTPTD SSEVTAYLFD HAVLLVRIKI VNKREEYRVY RKPIPLELLV
IAQMDEVIPR VGVAKRPSSS LLSNKAAANP PTTKDGLPIT FRHLGKGGYE QTLYATSPTQ
RRKFIEMVEE QQRKLRERNS NFYNKTVLCE KFFTSVNRVN CLVPVDGGRK LVYGTDSGIY
LSERWPKDKS ARPRRVLDVS QVTQMDTLEE YQLLLVLSNK TLSSYPMEAL EISESQNTVA
KRPKKIQGHA NFFKAGIGLG RHLVCSVKTS ALSTTIKVYE PMDNLAKGKK KSAVSKMFQS
GQDSLKLFKE FYIPAESSSI HFLRSTLCVG CARGFEVVSL ETTETQSLLD QADTSLDFVA
RKENVKPIHI ERMNGEFLLN YSDFSFFVNR NGWRARPDWK ISWEGNPNAF ALSYPYILAF
EPNFIEIRHI ETSELVHIMT GKNIRMLHSS TREILYAYED ESGEDVVASL DFWNKPQH
//