ID A0A2T3AUV7_AMORE Unreviewed; 682 AA.
AC A0A2T3AUV7;
DT 18-JUL-2018, integrated into UniProtKB/TrEMBL.
DT 18-JUL-2018, sequence version 1.
DT 27-MAR-2024, entry version 20.
DE RecName: Full=Rho-GAP domain-containing protein {ECO:0008006|Google:ProtNLM};
GN ORFNames=M430DRAFT_106801 {ECO:0000313|EMBL:PSS12444.1};
OS Amorphotheca resinae ATCC 22711.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Leotiomycetes;
OC Helotiales; Amorphothecaceae; Amorphotheca.
OX NCBI_TaxID=857342 {ECO:0000313|EMBL:PSS12444.1, ECO:0000313|Proteomes:UP000241818};
RN [1] {ECO:0000313|EMBL:PSS12444.1, ECO:0000313|Proteomes:UP000241818}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 22711 {ECO:0000313|EMBL:PSS12444.1,
RC ECO:0000313|Proteomes:UP000241818};
RX PubMed=29315638; DOI=10.1111/nph.14974;
RA Martino E., Morin E., Grelet G.A., Kuo A., Kohler A., Daghino S.,
RA Barry K.W., Cichocki N., Clum A., Dockter R.B., Hainaut M., Kuo R.C.,
RA LaButti K., Lindahl B.D., Lindquist E.A., Lipzen A., Khouja H.R.,
RA Magnuson J., Murat C., Ohm R.A., Singer S.W., Spatafora J.W., Wang M.,
RA Veneault-Fourrey C., Henrissat B., Grigoriev I.V., Martin F.M., Perotto S.;
RT "Comparative genomics and transcriptomics depict ericoid mycorrhizal fungi
RT as versatile saprotrophs and plant mutualists.";
RL New Phytol. 217:1213-1229(2018).
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DR EMBL; KZ679015; PSS12444.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2T3AUV7; -.
DR STRING; 857342.A0A2T3AUV7; -.
DR InParanoid; A0A2T3AUV7; -.
DR OrthoDB; 5482027at2759; -.
DR Proteomes; UP000241818; 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 CDD; cd04398; RhoGAP_fRGD1; 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:UP000241818}.
FT DOMAIN 34..307
FT /note="F-BAR"
FT /evidence="ECO:0000259|PROSITE:PS51741"
FT DOMAIN 489..679
FT /note="Rho-GAP"
FT /evidence="ECO:0000259|PROSITE:PS50238"
FT REGION 1..31
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 323..478
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 348..474
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 682 AA; 74670 MW; 6F4FA8C267CB6313 CRC64;
MSSGAPGDDA SVTNGDAAPS APAAPPPAQV DPNAKIVHDV VNSEIGVTTL LTRLKQSIAS
AKEFALFLKR RSTLEEEHSN GLKKLCRVTA ESIRKPEHRH GSLLHAYEEV TMIHERMADN
GAQFAMSLQK MQEDLLEMVG NIERSRKHWK ATGLAAEQRV ADTEAAMKKS KAKYDALAED
YDRARTGDRQ SGKIFGIKGP KFAAQHEEDL LKKVQAADAD YASKVQTAQN QRAELWSKLR
PETVSALQDL IKECDSALTL QMQKFASFNE KLLLSNGLNI SPLKGNAQGN QTRSLREAVH
SIDNPKDLSN YIVSYEKRVP PRASEIRYER NPVLNPTQPP ISAAPPQRQS DPPASFSSRQ
GPPPSFGTTP SPQQTHASQS FNSQGPPPAS QHHERSFSSQ GQPLQQYNSG SMGSMGSTAK
EPPSHGSYNT GSITSSSPPQ ISSLPFQTSP TLQPSFPQQQ VAPPTHSQPP ATSNGVGYLP
PPLKPVFGIS LDQLFERDSS AVPMVVYQCI QAVDLFGLEV EGIYRLSGTA SHITKIRAMF
DNDASQVDFR NPENFFHDVN SVAGLLKQFF RELPDPLMTR EHYAGFIEAA KNEDDIVRRD
SLHAIINSLP DPNYATLRAL TLHLNRVQEN SAANRMNAAN LAIVFGPTLM GASTGPNIQD
AGWQVRVIET ILNNTYQIFD DD
//
