ID A0A1X7RXL7_ZYMTR Unreviewed; 946 AA.
AC A0A1X7RXL7;
DT 05-JUL-2017, integrated into UniProtKB/TrEMBL.
DT 05-JUL-2017, sequence version 1.
DT 13-SEP-2023, entry version 23.
DE RecName: Full=Rho-GAP domain-containing protein {ECO:0008006|Google:ProtNLM};
GN ORFNames=ZT3D7_G7337 {ECO:0000313|EMBL:SMQ52184.1};
OS Zymoseptoria tritici ST99CH_3D7.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC Dothideomycetidae; Mycosphaerellales; Mycosphaerellaceae; Zymoseptoria.
OX NCBI_TaxID=1276538 {ECO:0000313|EMBL:SMQ52184.1, ECO:0000313|Proteomes:UP000215127};
RN [1] {ECO:0000313|EMBL:SMQ52184.1, ECO:0000313|Proteomes:UP000215127}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Kjaerup R.B., Dalgaard T.S., Juul-Madsen H.R.;
RL Submitted (JUN-2016) to the EMBL/GenBank/DDBJ databases.
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DR EMBL; LT853698; SMQ52184.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1X7RXL7; -.
DR STRING; 1276538.A0A1X7RXL7; -.
DR Proteomes; UP000215127; Chromosome 7.
DR GO; GO:0005096; F:GTPase activator activity; IEA:UniProt.
DR GO; GO:0035556; P:intracellular signal transduction; IEA:InterPro.
DR CDD; cd04399; RhoGAP_fRGD2; 1.
DR Gene3D; 1.20.1270.60; Arfaptin homology (AH) domain/BAR domain; 2.
DR Gene3D; 1.10.555.10; Rho GTPase activation protein; 1.
DR InterPro; IPR027267; AH/BAR_dom_sf.
DR InterPro; IPR000591; DEP_dom.
DR InterPro; IPR031160; F_BAR.
DR InterPro; IPR001060; FCH_dom.
DR InterPro; IPR008936; Rho_GTPase_activation_prot.
DR InterPro; IPR000198; RhoGAP_dom.
DR InterPro; IPR036390; WH_DNA-bd_sf.
DR PANTHER; PTHR23065; PROLINE-SERINE-THREONINE PHOSPHATASE INTERACTING PROTEIN 1; 1.
DR PANTHER; PTHR23065:SF17; RHO-GTPASE-ACTIVATING PROTEIN RGD2; 1.
DR Pfam; PF00610; DEP; 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 SUPFAM; SSF46785; Winged helix' DNA-binding domain; 1.
DR PROSITE; PS50186; DEP; 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:UP000215127}.
FT DOMAIN 1..441
FT /note="F-BAR"
FT /evidence="ECO:0000259|PROSITE:PS51741"
FT DOMAIN 216..301
FT /note="DEP"
FT /evidence="ECO:0000259|PROSITE:PS50186"
FT DOMAIN 475..673
FT /note="Rho-GAP"
FT /evidence="ECO:0000259|PROSITE:PS50238"
FT REGION 171..197
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 681..946
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 681..695
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 696..712
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 715..740
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 764..809
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 946 AA; 103474 MW; 1E61BE084804B879 CRC64;
MSSFATSFWS SDYAGGLGVL FGKLQQGVQE NDQVLTIARM RADAEDLYGQ KLGEIQYATD
RIEGGFQRDD GASVKKAYDG VRTEMGEASR SHRKIASNIR ELVVNPFARW CDQHASRVQN
SQDDLQGRIK AHDRQAETVR QYRSQYYNKC RRVEDLDEEE KLAFQAPDAV ALTGSPKPSP
ISVPSIKVEE DNDPEPVEIG DETYQPEQVK KMLTHALNNV PLGETKVPIL GTYQNVSSGA
DITEYIQKHL GANSLAYAER VGQDMVSNGF LRLIGNVGNT FANSSRMKYQ WRPKVFQITG
VPDKKPTLLS RSSTIMSAGS DSSIPGAPVI GDKISEYMGQ WNPLNNPYPN ETPAEKLRRE
AREADERYKA AVRKLDGLRC SLEEAMIEHM KFMERCELDR LKAIKSVVLD FSGAISNVIP
SLQSTVDNMM LFQETVQPLS DLRYLLENYR TGNYFPKVTT YENYYNNVDE QAFGVDIEAR
ARSDRKRVPL IITTILTFLD SHYPDLEGDE ARRSIWTVDV PLGATHHLRN QLNTGKPLSP
DLLEKYEVPI VASVLKLYLL ELPDSLVSSH VYEIIKTIYT TTSQTSSEAA RIQVIQSTLG
QLRLANIATL DALVTHFTRL IELTSADEAY INSLAGVLAP CIMRPKQESS LSMTEKFNVR
LLKDLFAHKD AIFGELKRQS SLTHTASGST RQVRAISTDE SKRKEHMEER QRAIAAATAS
SSGGPSHMHT MSTPVAHTKS VRQPSPGPGH RRDRSRGPET RFPVSATAAQ NSGKVMSPTQ
SVSSSQRDSL GVPQSPTATR TQRQGDANFS PPARSDGPNG SAAGLYQSPP VDQEESPAGG
GRARSGTFAE RALASSKLSG PGESADSAFG GKLSNGAAEN DDSTPETPSK KDSLTRSSGR
GAAGAKRSSA TAAGGLARKS LVAGGGEEGE AAVKGVQLED KPMDFD
//