ID A0A1Y2BDX4_9TREE Unreviewed; 636 AA.
AC A0A1Y2BDX4;
DT 30-AUG-2017, integrated into UniProtKB/TrEMBL.
DT 30-AUG-2017, sequence version 1.
DT 27-MAR-2024, entry version 18.
DE SubName: Full=Rho GTPase activation protein {ECO:0000313|EMBL:ORY33022.1};
GN ORFNames=BCR39DRAFT_564013 {ECO:0000313|EMBL:ORY33022.1};
OS Naematelia encephala.
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Tremellomycetes;
OC Tremellales; Naemateliaceae; Naematelia.
OX NCBI_TaxID=71784 {ECO:0000313|EMBL:ORY33022.1, ECO:0000313|Proteomes:UP000193986};
RN [1] {ECO:0000313|EMBL:ORY33022.1, ECO:0000313|Proteomes:UP000193986}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=68-887.2 {ECO:0000313|EMBL:ORY33022.1,
RC ECO:0000313|Proteomes:UP000193986};
RG DOE Joint Genome Institute;
RA Mondo S.J., Dannebaum R.O., Kuo R.C., Labutti K., Haridas S., Kuo A.,
RA Salamov A., Ahrendt S.R., Lipzen A., Sullivan W., Andreopoulos W.B.,
RA Clum A., Lindquist E., Daum C., Ramamoorthy G.K., Gryganskyi A., Culley D.,
RA Magnuson J.K., James T.Y., O'Malley M.A., Stajich J.E., Spatafora J.W.,
RA Visel A., Grigoriev I.V.;
RT "Pervasive Adenine N6-methylation of Active Genes in Fungi.";
RL Submitted (JUL-2016) to the EMBL/GenBank/DDBJ databases.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:ORY33022.1}.
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DR EMBL; MCFC01000007; ORY33022.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1Y2BDX4; -.
DR STRING; 71784.A0A1Y2BDX4; -.
DR InParanoid; A0A1Y2BDX4; -.
DR OrthoDB; 5482027at2759; -.
DR Proteomes; UP000193986; Unassembled WGS sequence.
DR GO; GO:0005096; F:GTPase activator activity; IEA:UniProt.
DR GO; GO:0007165; P:signal transduction; IEA:InterPro.
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:SF134; ACTIVATING PROTEIN, PUTATIVE-RELATED; 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:UP000193986}.
FT DOMAIN 23..328
FT /note="F-BAR"
FT /evidence="ECO:0000259|PROSITE:PS51741"
FT DOMAIN 425..617
FT /note="Rho-GAP"
FT /evidence="ECO:0000259|PROSITE:PS50238"
FT REGION 188..207
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 340..415
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 366..413
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 636 AA; 69552 MW; 7717461C7F866093 CRC64;
MGSAGSLKVG GNGLEVKEDV VPVGFDEGLL RGLCEMDCAL PLLADRIKQS IASCKQVAVF
FRSRAEIEEK YARSLTELCR TTGDVYSRAD CKAGTFVAAY QSSLKLQNSL AENRIRFSQR
LNEMSDELLG LAREGEKLRK MHKENGARYQ GILQESEMVM DKAKARFDAT AEELERVLVA
KEGESIKESG MRSGGAGSSS GGNKGRGIGK AMTKGGLLFK GKGAASMQRQ EDDVRARMAQ
ASETFRKAVL ESQALRQEYF NFQLPKILRL LKECADELDM GTQYHLARFA FLYESTVVGE
GTLLNPMGAP DDGPGLKAIF EGIDNRTDFK SYMQNYAVAR GTPRGPRREG PYEEGFLPPL
PPHVQKGESN PNQVSQQSNG ISNTNGHPSG ANNNLPTPLP VSQAPSSEGY SVPGIPASSG
ATFGVDLGEQ LARDGVEVPK VVEKCAEAIE AYGLESMGIY RLSGTTSRVQ ALKNALDKDV
DSVDVLSEEW SADINVVSGA LKLWFRELPE PLLTFGLYHQ FIEAARYEND RLRHIRLHEQ
VNDLPDPNYA TLKFFMGHLD RVRRKDSINQ MSVSNLSIVF GPTLLGAPPN EGGLNLEHMS
FQCKAIETIL EKYHEIFVEE EESAGTGAGT ATLEVS
//