ID A0A238FKD3_9BASI Unreviewed; 1246 AA.
AC A0A238FKD3;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 24-JAN-2024, entry version 22.
DE SubName: Full=BQ2448_3216 protein {ECO:0000313|EMBL:SCV71628.1};
GN ORFNames=BQ2448_3216 {ECO:0000313|EMBL:SCV71628.1};
OS Microbotryum intermedium.
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Pucciniomycotina;
OC Microbotryomycetes; Microbotryales; Microbotryaceae; Microbotryum.
OX NCBI_TaxID=269621 {ECO:0000313|EMBL:SCV71628.1, ECO:0000313|Proteomes:UP000198372};
RN [1] {ECO:0000313|Proteomes:UP000198372}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Jeantristanb JTB J.-T., Ricardo R.;
RL Submitted (SEP-2016) to the EMBL/GenBank/DDBJ databases.
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DR EMBL; FMSP01000007; SCV71628.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A238FKD3; -.
DR STRING; 269621.A0A238FKD3; -.
DR OrthoDB; 5482027at2759; -.
DR Proteomes; UP000198372; Unassembled WGS sequence.
DR GO; GO:0005096; F:GTPase activator activity; IEA:UniProt.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0007165; P:signal transduction; IEA:InterPro.
DR CDD; cd09395; LIM2_Rga; 1.
DR CDD; cd00159; RhoGAP; 1.
DR Gene3D; 3.30.60.20; -; 1.
DR Gene3D; 2.10.110.10; Cysteine Rich Protein; 1.
DR Gene3D; 1.10.555.10; Rho GTPase activation protein; 1.
DR InterPro; IPR046349; C1-like_sf.
DR InterPro; IPR002219; PE/DAG-bd.
DR InterPro; IPR008936; Rho_GTPase_activation_prot.
DR InterPro; IPR000198; RhoGAP_dom.
DR InterPro; IPR001781; Znf_LIM.
DR PANTHER; PTHR23176:SF129; RHO GTPASE ACTIVATING PROTEIN AT 16F, ISOFORM E-RELATED; 1.
DR PANTHER; PTHR23176; RHO/RAC/CDC GTPASE-ACTIVATING PROTEIN; 1.
DR Pfam; PF00130; C1_1; 1.
DR Pfam; PF00412; LIM; 1.
DR Pfam; PF00620; RhoGAP; 1.
DR SMART; SM00109; C1; 1.
DR SMART; SM00132; LIM; 1.
DR SMART; SM00324; RhoGAP; 1.
DR SUPFAM; SSF57889; Cysteine-rich domain; 1.
DR SUPFAM; SSF48350; GTPase activation domain, GAP; 1.
DR PROSITE; PS00478; LIM_DOMAIN_1; 1.
DR PROSITE; PS50023; LIM_DOMAIN_2; 1.
DR PROSITE; PS50238; RHOGAP; 1.
DR PROSITE; PS00479; ZF_DAG_PE_1; 1.
DR PROSITE; PS50081; ZF_DAG_PE_2; 1.
PE 4: Predicted;
KW Coiled coil {ECO:0000256|SAM:Coils};
KW LIM domain {ECO:0000256|PROSITE-ProRule:PRU00125};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723, ECO:0000256|PROSITE-
KW ProRule:PRU00125}; Reference proteome {ECO:0000313|Proteomes:UP000198372};
KW Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|PROSITE-ProRule:PRU00125}.
FT DOMAIN 186..245
FT /note="LIM zinc-binding"
FT /evidence="ECO:0000259|PROSITE:PS50023"
FT DOMAIN 981..1029
FT /note="Phorbol-ester/DAG-type"
FT /evidence="ECO:0000259|PROSITE:PS50081"
FT DOMAIN 1054..1243
FT /note="Rho-GAP"
FT /evidence="ECO:0000259|PROSITE:PS50238"
FT REGION 1..76
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 246..279
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 296..419
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 545..587
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 863..894
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 927..946
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 644..671
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 695..760
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 23..44
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 45..63
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 264..279
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 296..317
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 331..379
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 545..561
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1246 AA; 135552 MW; 85FF9F5B5E71FFA9 CRC64;
MTTPAAAYSR PLPVPPSIPS KTSTPLLGPG QHRGASASST SHEPTPAPTP APAPAPAPAP
APAPANGGGG GGGASTSAMS YETLLARDQK ATVPTSPFLS DRQTSCNSCK LGLEQTLDST
VVTCGKYLYQ SVVDARPSTV RSLLPPTPLD PHTRSFRCAK CNNLVEHDTN LLLLSDGLPV
CQNCSYICSK CHKSIDNSAV VTGEHSYHTE CFRCCHCAER IEGLTYAKTQ LGIWCMACHN
ERIAQGRKKT EAKKAARAGR KKKEAGRTKA ERDKERSERA HAVAIAAING DQVLASSGTG
GHARSPSSSS NFALRKSGDY DQGSYDASPS PKDKDFSTQQ YYSHDTSRPN SSPQSLHWRP
QHTPLPTSAT TTAISSLGGR LSSDAKDPPP RPSLPVPPQE RSPAISIGTS DGAGGASPTF
SAYMVRRESE SSTLQPMNAD QKQMNRRSGF YGFAQRPSID DGAPVASDDL DVTFERVEHV
EEEEKADPSL AKDVEEDPTE ALRYSALQHV PSAASNPPSS TYLSDLHNSM SFYDPDTLLF
LNHVASPRNH SPSNSLSHDP TPPRKSLDEK NTHQQQRGPS ESSTASDAIE HLSPDLAGAE
FNSSRDVATA GGRSVARKVR ESIRLSRDGM EGKNSGASLD VELVELLLNE LEETKKEMQE
WQARYDAFRV SAGRFVLLRA SRTAFEGFSM AREEYDREVA ARREVESRLE ELRIKFVEQA
RRLADVDQDQ KTRDSLRSQT QELRSSVVAT ERQLSSLRAE VELSTAQAAE LKVTESPTTT
ANDRIVEALN ERLEEVKDRH RAEITALVEQ RDALTREVDA LQDARSFLIE ESATLQARHV
SLEGQTVEAS KQLESLRDQM SKLRVAPSPG PGGHHASASV SSMGKLALPR PSMSPSIGDL
ESIARLEAPT VKKFKWGKAK TVTTASISGP QLQAGSHDPH DRKGSVMGLN MGSAASAAGL
NRSPQISRSA SVSIDHGSMR SHAFQPTSIL RPIRCEYCGE KMWGLNEVRC TGCGCYSHTK
CIPYLSTPCS HGSVALASDD TMTLLAQSSE MFGNYLTAQA RSENREVPLV VSKCIAAVEV
FGMYQEGIYR KSGGMGQTKR ITQLFESGQD FNLEDGNQFN DPAAITSCLK NYFRCLPDPL
FTFDLHEEFV SCTEISSPED RLAKIEATLA KMPEVHYKTA RCLIQHLHRV HSRSAENKMT
PVNLGVVFGP TVMRSRVVER EWSDMGAKAK MIELLVENSP RFFGVA
//