ID B0YCD9_ASPFC Unreviewed; 790 AA.
AC B0YCD9;
DT 08-APR-2008, integrated into UniProtKB/TrEMBL.
DT 08-APR-2008, sequence version 1.
DT 03-MAY-2023, entry version 75.
DE SubName: Full=RhoGAP and Fes/CIP4 domain protein {ECO:0000313|EMBL:EDP48270.1};
GN ORFNames=AFUB_089840 {ECO:0000313|EMBL:EDP48270.1};
OS Aspergillus fumigatus (strain CBS 144.89 / FGSC A1163 / CEA10) (Neosartorya
OS fumigata).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC Aspergillus subgen. Fumigati.
OX NCBI_TaxID=451804 {ECO:0000313|EMBL:EDP48270.1, ECO:0000313|Proteomes:UP000001699};
RN [1] {ECO:0000313|EMBL:EDP48270.1, ECO:0000313|Proteomes:UP000001699}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CEA10 / CBS 144.89 / FGSC A1163
RC {ECO:0000313|Proteomes:UP000001699};
RX PubMed=18404212; DOI=10.1371/journal.pgen.1000046;
RA Fedorova N.D., Khaldi N., Joardar V.S., Maiti R., Amedeo P., Anderson M.J.,
RA Crabtree J., Silva J.C., Badger J.H., Albarraq A., Angiuoli S., Bussey H.,
RA Bowyer P., Cotty P.J., Dyer P.S., Egan A., Galens K., Fraser-Liggett C.M.,
RA Haas B.J., Inman J.M., Kent R., Lemieux S., Malavazi I., Orvis J.,
RA Roemer T., Ronning C.M., Sundaram J.P., Sutton G., Turner G., Venter J.C.,
RA White O.R., Whitty B.R., Youngman P., Wolfe K.H., Goldman G.H.,
RA Wortman J.R., Jiang B., Denning D.W., Nierman W.C.;
RT "Genomic islands in the pathogenic filamentous fungus Aspergillus
RT fumigatus.";
RL PLoS Genet. 4:E1000046-E1000046(2008).
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DR EMBL; DS499601; EDP48270.1; -; Genomic_DNA.
DR AlphaFoldDB; B0YCD9; -.
DR EnsemblFungi; EDP48270; EDP48270; AFUB_089840.
DR HOGENOM; CLU_008201_1_0_1; -.
DR PhylomeDB; B0YCD9; -.
DR Proteomes; UP000001699; Unassembled WGS sequence.
DR GO; GO:0005096; F:GTPase activator activity; IEA:UniProt.
DR GO; GO:0035556; P:intracellular signal transduction; IEA:InterPro.
DR Gene3D; 1.20.1270.60; Arfaptin homology (AH) domain/BAR domain; 2.
DR Gene3D; 1.10.555.10; Rho GTPase activation protein; 1.
DR InterPro; IPR027267; AH/BAR_dom_sf.
DR InterPro; IPR000591; DEP_dom.
DR InterPro; IPR031160; F_BAR.
DR InterPro; IPR001060; FCH_dom.
DR InterPro; IPR008936; Rho_GTPase_activation_prot.
DR InterPro; IPR000198; RhoGAP_dom.
DR InterPro; IPR036390; WH_DNA-bd_sf.
DR PANTHER; PTHR23065; PROLINE-SERINE-THREONINE PHOSPHATASE INTERACTING PROTEIN 1; 1.
DR PANTHER; PTHR23065:SF17; RHO-GTPASE-ACTIVATING PROTEIN RGD2; 1.
DR Pfam; PF00610; DEP; 1.
DR Pfam; PF00611; FCH; 1.
DR Pfam; PF00620; RhoGAP; 1.
DR SMART; SM00055; FCH; 1.
DR SUPFAM; SSF103657; BAR/IMD domain-like; 1.
DR SUPFAM; SSF48350; GTPase activation domain, GAP; 1.
DR SUPFAM; SSF46785; Winged helix' DNA-binding domain; 1.
DR PROSITE; PS50186; DEP; 1.
DR PROSITE; PS51741; F_BAR; 1.
DR PROSITE; PS50238; RHOGAP; 1.
PE 4: Predicted;
KW Coiled coil {ECO:0000256|PROSITE-ProRule:PRU01077, ECO:0000256|SAM:Coils}.
FT DOMAIN 2..430
FT /note="F-BAR"
FT /evidence="ECO:0000259|PROSITE:PS51741"
FT DOMAIN 227..295
FT /note="DEP"
FT /evidence="ECO:0000259|PROSITE:PS50186"
FT DOMAIN 362..568
FT /note="Rho-GAP"
FT /evidence="ECO:0000259|PROSITE:PS50238"
FT REGION 329..351
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 578..790
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 115..142
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 591..609
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 616..631
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 658..710
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 711..725
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 768..790
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 790 AA; 87516 MW; C9A8B1B21A75D226 CRC64;
MPGFADSFWT PDYATGLGVL YGKLQQGVTE NRQILTIASL RADAEEQYGL KLGEIAPSVD
RMTAGFAKDD GASVRKAYEG VRSEMIEASK NHQKIASNIR ELVVSPFRRW CDQHEARIQN
SHDDLQARIK EHTKQVELTK KLRSHYFNKC RVVEDLEEEN KLAFQDPETS PKVKATPKIV
LPEEQAEEEE PIELGDRVYA PEDLKKLLTH MLDNIKIGEV KVPIIGTYQN TSNGADIVEY
IQKYMNGTSI SYAERIGQDL VDNGFLRLVG NIGSTFANSS KMNYQWRPKV FQITGIPEKK
KPLMRVTSIA SSEDGSESPI ASVSEMLAGW NPLNNPHPNE TPADKLRREA READERYRAA
VRKLDQIRCK LEEEIVENLR FMEQCELDRL KAIKAVVLDF SGAISNVIPN LQSTVDHMML
YQETIQPLGD LRYLLENYRT GGFVPRVQAY ENYYGSVEDS LVSSQVYEIV KTIYSTTAHE
TTEDGRIKVL QSTLGQLRLN NIATLDAIMT HFTRLIDLTS ADEAYISALA QTLAPCILRP
RVENSLTMNE RHNYRLIRDL FAHKDAIFGE LKRQSSVLGL GSTSNRPRAI STDESNRRAA
MEARNRAIVD RSRANSPAPP RKHRRDRSSG ASEAGRFPIH VTSPTERKAA TRSSLEVPAS
AEAPTTGEQF TTVNIQANDS ATNGTSSDSP ASAVAGENTS SESSSPPPAG NSDGSPTPTP
TPGYVTAPGE PEKRSSIPRS GAMFNRKPGL GNRSSFPAVA SAESEPDSKR NSLAESEPKG
VTLEDKPMDD
//
