ID A0A074W8L9_9PEZI Unreviewed; 624 AA.
AC A0A074W8L9;
DT 01-OCT-2014, integrated into UniProtKB/TrEMBL.
DT 01-OCT-2014, sequence version 1.
DT 27-MAR-2024, entry version 36.
DE SubName: Full=RhoGAP-domain-containing protein {ECO:0000313|EMBL:KEQ66267.1};
DE Flags: Fragment;
GN ORFNames=M437DRAFT_39264 {ECO:0000313|EMBL:KEQ66267.1};
OS Aureobasidium melanogenum CBS 110374.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC Dothideomycetidae; Dothideales; Saccotheciaceae; Aureobasidium.
OX NCBI_TaxID=1043003 {ECO:0000313|EMBL:KEQ66267.1, ECO:0000313|Proteomes:UP000030672};
RN [1] {ECO:0000313|EMBL:KEQ66267.1, ECO:0000313|Proteomes:UP000030672}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 110374 {ECO:0000313|EMBL:KEQ66267.1,
RC ECO:0000313|Proteomes:UP000030672};
RX PubMed=24984952;
RA Gostin Ar C., Ohm R.A., Kogej T., Sonjak S., Turk M., Zajc J., Zalar P.,
RA Grube M., Sun H., Han J., Sharma A., Chiniquy J., Ngan C.Y., Lipzen A.,
RA Barry K., Grigoriev I.V., Gunde-Cimerman N.;
RT "Genome sequencing of four Aureobasidium pullulans varieties:
RT biotechnological potential, stress tolerance, and description of new
RT species.";
RL BMC Genomics 15:549-549(2014).
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DR EMBL; KL584825; KEQ66267.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A074W8L9; -.
DR STRING; 1043003.A0A074W8L9; -.
DR HOGENOM; CLU_010730_3_0_1; -.
DR OrthoDB; 5482027at2759; -.
DR Proteomes; UP000030672; Unassembled WGS sequence.
DR GO; GO:0005096; F:GTPase activator activity; IEA:UniProt.
DR GO; GO:0007165; P:signal transduction; IEA:InterPro.
DR CDD; cd07652; F-BAR_Rgd1; 1.
DR Gene3D; 1.20.1270.60; Arfaptin homology (AH) domain/BAR domain; 1.
DR Gene3D; 1.10.555.10; Rho GTPase activation protein; 1.
DR InterPro; IPR027267; AH/BAR_dom_sf.
DR InterPro; IPR031160; F_BAR.
DR InterPro; IPR001060; FCH_dom.
DR InterPro; IPR008936; Rho_GTPase_activation_prot.
DR InterPro; IPR000198; RhoGAP_dom.
DR PANTHER; PTHR23176:SF138; RHO GTPASE ACTIVATOR; 1.
DR PANTHER; PTHR23176; RHO/RAC/CDC GTPASE-ACTIVATING PROTEIN; 1.
DR Pfam; PF00611; FCH; 1.
DR Pfam; PF00620; RhoGAP; 1.
DR SMART; SM00055; FCH; 1.
DR SMART; SM00324; RhoGAP; 1.
DR SUPFAM; SSF103657; BAR/IMD domain-like; 1.
DR SUPFAM; SSF48350; GTPase activation domain, GAP; 1.
DR PROSITE; PS51741; F_BAR; 1.
DR PROSITE; PS50238; RHOGAP; 1.
PE 4: Predicted;
KW Coiled coil {ECO:0000256|PROSITE-ProRule:PRU01077};
KW Reference proteome {ECO:0000313|Proteomes:UP000030672}.
FT DOMAIN 1..260
FT /note="F-BAR"
FT /evidence="ECO:0000259|PROSITE:PS51741"
FT DOMAIN 431..621
FT /note="Rho-GAP"
FT /evidence="ECO:0000259|PROSITE:PS50238"
FT REGION 288..416
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 290..327
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 328..342
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 349..368
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 376..415
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:KEQ66267.1"
SQ SEQUENCE 624 AA; 68851 MW; E2C7F86A6A4B876E CRC64;
IGINTLLNRL KQSIASSRDF SDFLKKRGAV EEDHAKGLRR LVKSTTDNIH SKESRQGSYV
TKLDEAMRLH DRIADNGMQF SLALHQMHED LNELSLNMEK GRKHWKHEGL NAEKRATDAE
SAMEKAKSKY DGLAEDYDRA RTGDAKSSRR IGLKGMKSAP QHEEDLLRKL QVADSDYQAK
VQAAKAQREE LIKTARPQAV KALQELINEC DSGLALQLQK FASFNEKLLL GNGIALSPLP
PNDPSAPVQH SLRDIVLEID NKADFDNYMS GHISKVPSRI SEIKYEQHPT LRPKQQTPTP
ASRQPSSTLP GPALPETPTT SVPTQQPTYS TPPGPALPPT TQYPSQPSYG NPGNPPYPTD
PPQQYNTAPY PTSPGAPRGF STSTQGTSAP YSPVTPGGMG AQQSFSSQSR SLSPGPVATA
LPPPLKPVFG VSLDELYNRD QTAVPMIVYQ CMQAVDLFGL DVEGIYRLSG TASHVQQIKA
LFDHDSQVVD FRNPASFYHD VNSVAGLLKQ FFRELPDPLL TRRSYNSFID AARIEDDTTR
RDAVHSVINE LPDPNYATLR ALVLHLNRVQ EHYAKNRMST SNLAICFAPS LMGSHTGPQI
ADASLQARVL DTILTNTFQI FDED
//
