ID R4XA24_TAPDE Unreviewed; 527 AA.
AC R4XA24;
DT 24-JUL-2013, integrated into UniProtKB/TrEMBL.
DT 24-JUL-2013, sequence version 1.
DT 22-FEB-2023, entry version 26.
DE SubName: Full=GTPase activating protein Rga6 {ECO:0000313|EMBL:CCG81119.1};
GN ORFNames=TAPDE_000817 {ECO:0000313|EMBL:CCG81119.1};
OS Taphrina deformans (strain PYCC 5710 / ATCC 11124 / CBS 356.35 / IMI 108563
OS / JCM 9778 / NBRC 8474) (Peach leaf curl fungus) (Lalaria deformans).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Taphrinomycotina; Taphrinomycetes;
OC Taphrinales; Taphrinaceae; Taphrina.
OX NCBI_TaxID=1097556 {ECO:0000313|EMBL:CCG81119.1, ECO:0000313|Proteomes:UP000013776};
RN [1] {ECO:0000313|EMBL:CCG81119.1, ECO:0000313|Proteomes:UP000013776}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PYCC 5710 / ATCC 11124 / CBS 356.35 / IMI 108563 / JCM 9778 /
RC NBRC 8474 {ECO:0000313|Proteomes:UP000013776};
RX PubMed=23631913; DOI=10.1128/mBio.00055-13;
RA Cisse O.H., Almeida J.M.G.C.F., Fonseca A., Kumar A.A., Salojaervi J.,
RA Overmyer K., Hauser P.M., Pagni M.;
RT "Genome sequencing of the plant pathogen Taphrina deformans, the causal
RT agent of peach leaf curl.";
RL MBio 4:e00055-e00013(2013).
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:CCG81119.1}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; CAHR02000025; CCG81119.1; -; Genomic_DNA.
DR AlphaFoldDB; R4XA24; -.
DR STRING; 1097556.R4XA24; -.
DR VEuPathDB; FungiDB:TAPDE_000817; -.
DR eggNOG; ENOG502SAYM; Eukaryota.
DR Proteomes; UP000013776; Unassembled WGS sequence.
DR GO; GO:0005938; C:cell cortex; IEA:UniProt.
DR GO; GO:0032153; C:cell division site; IEA:UniProt.
DR GO; GO:0005096; F:GTPase activator activity; IEA:UniProt.
DR GO; GO:0007165; P:signal transduction; IEA:InterPro.
DR CDD; cd00159; RhoGAP; 1.
DR Gene3D; 1.10.555.10; Rho GTPase activation protein; 1.
DR InterPro; IPR008936; Rho_GTPase_activation_prot.
DR InterPro; IPR000198; RhoGAP_dom.
DR PANTHER; PTHR45808; RHO GTPASE-ACTIVATING PROTEIN 68F; 1.
DR PANTHER; PTHR45808:SF2; RHO GTPASE-ACTIVATING PROTEIN 68F; 1.
DR Pfam; PF00620; RhoGAP; 1.
DR SMART; SM00324; RhoGAP; 1.
DR SUPFAM; SSF48350; GTPase activation domain, GAP; 1.
DR PROSITE; PS50238; RHOGAP; 1.
PE 4: Predicted;
KW Coiled coil {ECO:0000256|SAM:Coils};
KW Reference proteome {ECO:0000313|Proteomes:UP000013776}.
FT DOMAIN 151..389
FT /note="Rho-GAP"
FT /evidence="ECO:0000259|PROSITE:PS50238"
FT REGION 18..73
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 475..516
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 44..66
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 527 AA; 58047 MW; F863ED157DBFADC2 CRC64;
MLDPEASLFA SYMLGSSAGT VSENGEDSDI GQPLASPLER SDTAQKSESS EQEWRLGREG
RSKSVLSTRE DSMTSISSTS SKWYKRLHRA GSANRLSKAM DTAEAANNQP TGKLYNPFSR
RRSVPVLAAR PIRTILGQTA TQAIDIGGHS ANASALLPRE ILPSQSIELP YMVDACITWL
IENHAYMIPG IFRVNGSSQA IRTIIEHFST GCLRMPLEDI ILPAKQLVSV HDVASCLKKF
LVLLPGGLLG EQVFEQLKTI VGSGDKLVPE VIGKEISVVL RTISEEPRYN TLIVLLAFLC
HISRQVPSTT SETAPKQESG HMNAFSLGIV FSPTCLGSRD GATDMVRSAT SQSEQSVQSE
STPIEEAVAV ARAGAKVMQW LISSWPEISK HLSDSPSNVS LNKDDDVSLL DVVSFRLDSD
ETEPRNQLHT IIDSPVKPRQ HGTRTHDRSE SNVTVTMKGK ENDDESVLML RDAQIDLLKA
RIKQAEIERD DAITNLRQQE SENAKLFTRN LLLERENKTL RTKKWTS
//
