ID A0A0C3MVS8_PISTI Unreviewed; 667 AA.
AC A0A0C3MVS8;
DT 01-APR-2015, integrated into UniProtKB/TrEMBL.
DT 01-APR-2015, sequence version 1.
DT 27-MAR-2024, entry version 35.
DE RecName: Full=Rho-GAP domain-containing protein {ECO:0008006|Google:ProtNLM};
GN ORFNames=M404DRAFT_17350 {ECO:0000313|EMBL:KIN93029.1};
OS Pisolithus tinctorius Marx 270.
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC Agaricomycetidae; Boletales; Sclerodermatineae; Pisolithaceae; Pisolithus.
OX NCBI_TaxID=870435 {ECO:0000313|EMBL:KIN93029.1, ECO:0000313|Proteomes:UP000054217};
RN [1] {ECO:0000313|EMBL:KIN93029.1, ECO:0000313|Proteomes:UP000054217}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Marx 270 {ECO:0000313|EMBL:KIN93029.1,
RC ECO:0000313|Proteomes:UP000054217};
RG DOE Joint Genome Institute;
RA Kuo A., Kohler A., Costa M.D., Nagy L.G., Floudas D., Copeland A.,
RA Barry K.W., Cichocki N., Veneault-Fourrey C., LaButti K., Lindquist E.A.,
RA Lipzen A., Lundell T., Morin E., Murat C., Sun H., Tunlid A., Henrissat B.,
RA Grigoriev I.V., Hibbett D.S., Martin F., Nordberg H.P., Cantor M.N.,
RA Hua S.X.;
RL Submitted (APR-2014) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Proteomes:UP000054217}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Marx 270 {ECO:0000313|Proteomes:UP000054217};
RG DOE Joint Genome Institute;
RG Mycorrhizal Genomics Consortium;
RA Kohler A., Kuo A., Nagy L.G., Floudas D., Copeland A., Barry K.W.,
RA Cichocki N., Veneault-Fourrey C., LaButti K., Lindquist E.A., Lipzen A.,
RA Lundell T., Morin E., Murat C., Riley R., Ohm R., Sun H., Tunlid A.,
RA Henrissat B., Grigoriev I.V., Hibbett D.S., Martin F.;
RT "Evolutionary Origins and Diversification of the Mycorrhizal Mutualists.";
RL Submitted (JAN-2015) to the EMBL/GenBank/DDBJ databases.
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DR EMBL; KN832247; KIN93029.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0C3MVS8; -.
DR STRING; 870435.A0A0C3MVS8; -.
DR HOGENOM; CLU_010730_1_0_1; -.
DR InParanoid; A0A0C3MVS8; -.
DR OrthoDB; 5482027at2759; -.
DR Proteomes; UP000054217; 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, ECO:0000256|SAM:Coils};
KW Reference proteome {ECO:0000313|Proteomes:UP000054217}.
FT DOMAIN 97..389
FT /note="F-BAR"
FT /evidence="ECO:0000259|PROSITE:PS51741"
FT DOMAIN 462..659
FT /note="Rho-GAP"
FT /evidence="ECO:0000259|PROSITE:PS50238"
FT REGION 1..74
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 195..247
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 12..54
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 667 AA; 74406 MW; 7D94F2C44704DF5E CRC64;
MGDDAYPARK STADHSDSSN PADGVTSLGH HSVIQEGVTS PTLTQVSLKP SSPPPRSSLD
SPVRSPVSRH RESIPLTVER RDTLSTIPSD VVSLVEPSFD ENVLRALCEL DCGVPLLLDR
IKQSLVSCRE ASAFFKKRAG LEEEYGKTLQ KLSRSTSEVY SMNDGKAGSF VTAWQSSMRL
HELMAENRIR FAHRLNEMSE ELASLAKEVD KNRKQTKELA SRYERALQEA EINMEKSKAR
LDVSSEELER VLLQKEGESF SESAVQAKPG VLGSKRVLGK AVAKGGLLLK GKNPNILRQE
DDIRLRVSNA SDSYRKALHD TQAMRQEYFN FQLPRILRAL KECVDEIDLG TKYHLTRYAF
LFESIVLSDG STLVPIAPEE GAGLKALYDA IDNRVDFKTY MQNYAYARGG AARGPRREGP
AEEGFLPPLP THNASYAAAQ PPQSVVNGNT QITDRSRPTF GVDLAEQMAR DQVELPPVLE
KCCAAIEKYG IRSQGIYRIS GMARRVGMLK ERLDKDMNSV DLDSEEWTTD INNVTSVLKM
WFRELPEPVL TFNLHQGFVD AAKIENDRLR HIRLHERVND LPDPNYATLK YFMGHLHKIA
QYEGDNSMSI QNLAIVFGPT LFGQVGNGST SGHANVTMAD APYQNRAIET ILEHYTDIFV
DESEVTT
//