ID A0A066XPJ5_COLSU Unreviewed; 1186 AA.
AC A0A066XPJ5;
DT 03-SEP-2014, integrated into UniProtKB/TrEMBL.
DT 03-SEP-2014, sequence version 1.
DT 27-MAR-2024, entry version 37.
DE SubName: Full=Putative RhoGAP domain-containing protein {ECO:0000313|EMBL:KDN71138.1};
GN ORFNames=CSUB01_03065 {ECO:0000313|EMBL:KDN71138.1};
OS Colletotrichum sublineola (Sorghum anthracnose fungus).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Glomerellales; Glomerellaceae; Colletotrichum;
OC Colletotrichum graminicola species complex.
OX NCBI_TaxID=1173701 {ECO:0000313|EMBL:KDN71138.1, ECO:0000313|Proteomes:UP000027238};
RN [1] {ECO:0000313|Proteomes:UP000027238}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=TX430BB {ECO:0000313|Proteomes:UP000027238};
RX PubMed=24926053; DOI=10.1128/genomeA.00540-14;
RA Baroncelli R., Sanz-Martin J.M., Rech G.E., Sukno S.A., Thon M.R.;
RT "Draft genome sequence of Colletotrichum sublineola, a destructive pathogen
RT of cultivated sorghum.";
RL Genome Announc. 2:E0054014-E0054014(2014).
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:KDN71138.1}.
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DR EMBL; JMSE01000244; KDN71138.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A066XPJ5; -.
DR STRING; 1173701.A0A066XPJ5; -.
DR eggNOG; KOG1703; Eukaryota.
DR eggNOG; KOG2710; Eukaryota.
DR HOGENOM; CLU_001321_0_0_1; -.
DR OMA; WQMQSSV; -.
DR OrthoDB; 1329523at2759; -.
DR Proteomes; UP000027238; 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; cd09391; LIM1_Lrg1p_like; 1.
DR CDD; cd09392; LIM2_Lrg1p_like; 1.
DR CDD; cd09393; LIM3_Lrg1p_like; 1.
DR Gene3D; 2.10.110.10; Cysteine Rich Protein; 4.
DR Gene3D; 1.10.555.10; Rho GTPase activation protein; 1.
DR InterPro; IPR008936; Rho_GTPase_activation_prot.
DR InterPro; IPR000198; RhoGAP_dom.
DR InterPro; IPR001781; Znf_LIM.
DR PANTHER; PTHR45808; RHO GTPASE-ACTIVATING PROTEIN 68F; 1.
DR PANTHER; PTHR45808:SF2; RHO GTPASE-ACTIVATING PROTEIN 68F; 1.
DR Pfam; PF00412; LIM; 3.
DR Pfam; PF00620; RhoGAP; 1.
DR SMART; SM00132; LIM; 3.
DR SMART; SM00324; RhoGAP; 1.
DR SUPFAM; SSF57716; Glucocorticoid receptor-like (DNA-binding domain); 3.
DR SUPFAM; SSF48350; GTPase activation domain, GAP; 1.
DR PROSITE; PS00478; LIM_DOMAIN_1; 3.
DR PROSITE; PS50023; LIM_DOMAIN_2; 3.
DR PROSITE; PS50238; RHOGAP; 1.
PE 4: Predicted;
KW LIM domain {ECO:0000256|PROSITE-ProRule:PRU00125};
KW Metal-binding {ECO:0000256|PROSITE-ProRule:PRU00125};
KW Reference proteome {ECO:0000313|Proteomes:UP000027238};
KW Zinc {ECO:0000256|PROSITE-ProRule:PRU00125}.
FT DOMAIN 94..157
FT /note="LIM zinc-binding"
FT /evidence="ECO:0000259|PROSITE:PS50023"
FT DOMAIN 158..218
FT /note="LIM zinc-binding"
FT /evidence="ECO:0000259|PROSITE:PS50023"
FT DOMAIN 464..527
FT /note="LIM zinc-binding"
FT /evidence="ECO:0000259|PROSITE:PS50023"
FT DOMAIN 825..1029
FT /note="Rho-GAP"
FT /evidence="ECO:0000259|PROSITE:PS50238"
FT REGION 1..93
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 560..594
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 630..685
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 708..747
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1071..1186
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 27..62
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 66..83
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 630..646
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 665..685
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 716..735
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1110..1124
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1127..1142
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1171..1186
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1186 AA; 134082 MW; F4462EC2999561AF CRC64;
MASDYDHGTP DDRFPTHPAA SMDSSYPGDR GWQQQQQLQQ QNGGRRTPDN SYRTQQPSRS
PGPRTPGRDG DSRRSRERSR SNGRGGRSAS GQQRICKKCG EPLTGQFVRA LDGTFHLDCF
KCRDCGQIVA SKFFPVDDES GEGQYPLCET DYFRRLGLLC YKCGGALRGS YITALDRKYH
VDHFTCSLCP TVFGAQDSYY EHDGNVYCHY HYSTQFAQRC NGCQTAILKQ FVEIYRNGQN
QHWHPECYMI HKFWNVRLTQ PSDSSEIPQE IDDPATREII REEEERMEEK VYRIWSVLST
FEESSAACIS DMLLHVSNGA YVDGVLVAKK FIWHVEVLFQ SADRLDYSMD QLKLKGLSYG
REAKLLCKKI VSFFSLLSKT QDTGARKLGV TQELLSLVTG LAHYLKLLIR ICLQGALRLE
KESKSSEGIY QFLDDLSELD NVNPDDNTLQ AITSNPRLSA KDSDHCALCN KSVEDECAKH
SDRRWHIACV SCSRCTRDIG RKLEDAHYNA FDKKIYCNNC IGANSEDMPP FEHVTKLQQY
VFLLKVALAR LLDILRSNGA LPRQNDDQNM DGYGPGEGPR TLAPGEAPYL NLDNRSKSYA
GDQREHNRES SYENTLNDVR RLRSTRLDKH LSSSFRKART SRIMDGPEGR SVRPGSAGED
LRQADGDLQI VEDRRGPKDE GTTDKMFNHQ DALTLDDIPR IVAAEQVKEQ QYKPNRQELF
RSPATDPSGH QRSQSAGREA DIRMGDPMPQ RLGRKYFSEL SGLEYFIVRH LAVLTLAPAV
EQEFSLDELL SFIELRKQPT FWKNLGKAFK NDRPKNVKKK GIFGVPLDVI IDKDGAESTD
GVGPGTLKIP AIIDDLVSSM RKMDLSVEGV FRKNGNIKKL NELCEKIDRE GCDSINFMDQ
PVVQVAALLK RYLRELPDPL MTFKLQRLWI AAAKIQDDAK RKQYLHLICC LLPKAHRDCL
EILFCFLKWA GSFHQIDEEA GSRMDIKNLA TVIAPNILYN SNKAPALDSD PMFAIVAVND
MITSIEEMCL VPDELMDLVN DPFVFGNTAD LTTKDILKRY QDRMGQRLGL SGEVGEVFNR
PDNSTRPPPR RVETDPALWQ QQESSVRPVQ EPPMPIPPFN PANHGTPPQR WRAQQEENGN
PSPYGGGAQF EHSDTEGPSE AQKREWRQSG GVWGRQNNGV GVGGNL
//
