ID E6ZMM0_SPORE Unreviewed; 1188 AA.
AC E6ZMM0;
DT 08-MAR-2011, integrated into UniProtKB/TrEMBL.
DT 08-MAR-2011, sequence version 1.
DT 27-MAR-2024, entry version 57.
DE SubName: Full=Related to GTPase-activating protein beta-chimerin {ECO:0000313|EMBL:CBQ68477.1};
GN ORFNames=sr14766 {ECO:0000313|EMBL:CBQ68477.1};
OS Sporisorium reilianum (strain SRZ2) (Maize head smut fungus).
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Ustilaginomycotina;
OC Ustilaginomycetes; Ustilaginales; Ustilaginaceae; Sporisorium.
OX NCBI_TaxID=999809 {ECO:0000313|EMBL:CBQ68477.1, ECO:0000313|Proteomes:UP000008867};
RN [1] {ECO:0000313|EMBL:CBQ68477.1, ECO:0000313|Proteomes:UP000008867}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SRZ2 {ECO:0000313|Proteomes:UP000008867};
RX PubMed=21148393; DOI=10.1126/science.1195330;
RA Schirawski J., Mannhaupt G., Muench K., Brefort T., Schipper K.,
RA Doehlemann G., Di Stasio M., Roessel N., Mendoza-Mendoza A., Pester D.,
RA Mueller O., Winterberg B., Meyer E., Ghareeb H., Wollenberg T.,
RA Muensterkoetter M., Wong P., Walter M., Stukenbrock E., Gueldener U.,
RA Kahmann R.;
RT "Pathogenicity determinants in smut fungi revealed by genome comparison.";
RL Science 330:1546-1548(2010).
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DR EMBL; FQ311431; CBQ68477.1; -; Genomic_DNA.
DR AlphaFoldDB; E6ZMM0; -.
DR EnsemblFungi; CBQ68477; CBQ68477; sr14766.
DR VEuPathDB; FungiDB:sr14766; -.
DR eggNOG; KOG1453; Eukaryota.
DR eggNOG; KOG1704; Eukaryota.
DR HOGENOM; CLU_003874_0_0_1; -.
DR OrthoDB; 5482027at2759; -.
DR Proteomes; UP000008867; Chromosome 10.
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; cd00029; C1; 1.
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; 2.
DR Gene3D; 1.10.555.10; Rho GTPase activation protein; 1.
DR InterPro; IPR046349; C1-like_sf.
DR InterPro; IPR036280; Multihaem_cyt_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; RHO/RAC/CDC GTPASE-ACTIVATING PROTEIN; 1.
DR PANTHER; PTHR23176:SF141; TRANSDUCER, PUTATIVE-RELATED; 1.
DR Pfam; PF00130; C1_1; 1.
DR Pfam; PF00412; LIM; 2.
DR Pfam; PF00620; RhoGAP; 1.
DR SMART; SM00109; C1; 1.
DR SMART; SM00132; LIM; 2.
DR SMART; SM00324; RhoGAP; 1.
DR SUPFAM; SSF57889; Cysteine-rich domain; 1.
DR SUPFAM; SSF48350; GTPase activation domain, GAP; 1.
DR SUPFAM; SSF48695; Multiheme cytochromes; 1.
DR PROSITE; PS00478; LIM_DOMAIN_1; 2.
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};
KW Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|PROSITE-ProRule:PRU00125}.
FT DOMAIN 33..101
FT /note="LIM zinc-binding"
FT /evidence="ECO:0000259|PROSITE:PS50023"
FT DOMAIN 926..974
FT /note="Phorbol-ester/DAG-type"
FT /evidence="ECO:0000259|PROSITE:PS50081"
FT DOMAIN 996..1187
FT /note="Rho-GAP"
FT /evidence="ECO:0000259|PROSITE:PS50238"
FT REGION 155..221
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 236..408
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 461..557
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 789..846
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 880..899
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 566..673
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 719..781
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 177..221
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 273..309
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 341..357
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 485..499
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 536..557
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 831..846
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1188 AA; 129010 MW; A7EDC70AA6941088 CRC64;
MPALHQEQLA LRDQQVDTDD AHAHDVEDEL PEAYCGGCGR LIDEESVEEG VIQFATKLWH
VECFRCAKCK NRVSTERDDI LLLSDGHPIC GECNYSCNIC NLPIMEEAIM TGDESYHASC
FTCRSCHSKI EELVFAKTSQ GIYCMKCHNE RVARSRKHAE QKRAKARREK QLQDAHAAEL
NQRNNLATPT LDQPPSLPSK QSPLASPSPS VLASPAPNAS SLSPCISQAG SAGAAAAVAR
PNSANGKRPM HAPPPPSREG RSPAMGTHAK LEGRSVSANN TSRADSRTSL SSNTADDQLQ
PQNSEYEVTA PLSPRKKAFA AGSSSPLGSP AAAKTMLPAG EAPTSPSSPS TSPLKKSVPM
DGSPRADVAR SLRPSTSREG LGVNLRTSSI KPGAGARNPL NASGSSSRLS KVYSFYDPDF
LNLVESFGDF GSTDELHSPA PPVPALPTSV PAVPAVLATS KDVSPSSSTD LPTSVPLHPH
GLESSAAPSA STSASEIEAD DRQASAPPHH ISSDLAESVE SEEELLDDDR RNTITSTGSL
KEVSSKVRAS MQQARDGQVS MDISFVETIL HDLEQTRQRM ESLQLRYDRI RRASQQAAHG
FSMAKEEFEH EVNARHDAEL EMARLRRQLA EQALKLATAN SERRQQEQLE RRSQDVKASL
KGMERDLAKL TVERDLTVAE VAELVALQDG TASSTSQTAA VSSSSATGTV DAAITQNLTS
RLEAVKSRYR NEIDELTIER DSLLIEIEEL KQSKELFLEE AQSLNAKNDE LNTMLGQLNR
KIELAAQSRD QLPPLPPLPK DLSSTSAKSS GGFSFGSRHR HVHKHTAHSA SISSHDAPPS
SAGYDTVSVD TAVQQVIKPG RVEPAPAVKK FKWMKPKLSE TTKANQPASQ AGAVPPVSPK
GGAALGAGAG TAAMTRATSH DVVVREHLFQ PFNVLRPTRC FACQKNMWGQ SEMRCALCAH
VCHSRCLQSL PVSCNQPYTR PDEAHAENTG PSMFGRSLTE QAAHEGRDVP LIVDKCIQAV
EAFGMDYEGI YRKSGGTSQL KVITQLFERG NAFDLEDTDR FNDVSAITSV LKNYFRELPT
PLLTFELYDE LIKVVESKTE DVAGKLALVK QLVDRLPRQH FCTLQHLVLH LYRVQERSAD
NRMNARNLGV VFGPTLMRSA DPTQEFAHMG GKAMTVEFFI DHAPELFV
//
