ID C5FYU7_ARTOC Unreviewed; 1136 AA.
AC C5FYU7;
DT 28-JUL-2009, integrated into UniProtKB/TrEMBL.
DT 28-JUL-2009, sequence version 1.
DT 27-MAR-2024, entry version 69.
DE SubName: Full=Rho-GTPase-activating protein {ECO:0000313|EMBL:EEQ34695.1};
GN ORFNames=MCYG_07514 {ECO:0000313|EMBL:EEQ34695.1};
OS Arthroderma otae (strain ATCC MYA-4605 / CBS 113480) (Microsporum canis).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Onygenales; Arthrodermataceae; Microsporum.
OX NCBI_TaxID=554155 {ECO:0000313|EMBL:EEQ34695.1, ECO:0000313|Proteomes:UP000002035};
RN [1] {ECO:0000313|Proteomes:UP000002035}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC MYA-4605 / CBS 113480 {ECO:0000313|Proteomes:UP000002035};
RX PubMed=22951933; DOI=10.1128/mbio.00259-12;
RA Martinez D.A., Oliver B.G., Graeser Y., Goldberg J.M., Li W.,
RA Martinez-Rossi N.M., Monod M., Shelest E., Barton R.C., Birch E.,
RA Brakhage A.A., Chen Z., Gurr S.J., Heiman D., Heitman J., Kosti I.,
RA Rossi A., Saif S., Samalova M., Saunders C.W., Shea T., Summerbell R.C.,
RA Xu J., Young S., Zeng Q., Birren B.W., Cuomo C.A., White T.C.;
RT "Comparative genome analysis of Trichophyton rubrum and related
RT dermatophytes reveals candidate genes involved in infection.";
RL MBio 3:E259-E259(2012).
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DR EMBL; DS995707; EEQ34695.1; -; Genomic_DNA.
DR RefSeq; XP_002843731.1; XM_002843685.1.
DR AlphaFoldDB; C5FYU7; -.
DR STRING; 554155.C5FYU7; -.
DR GeneID; 9225237; -.
DR VEuPathDB; FungiDB:MCYG_07514; -.
DR eggNOG; KOG1703; Eukaryota.
DR eggNOG; KOG2710; Eukaryota.
DR HOGENOM; CLU_001321_1_0_1; -.
DR OMA; WQMQSSV; -.
DR OrthoDB; 1329523at2759; -.
DR Proteomes; UP000002035; 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; cd04397; RhoGAP_fLRG1; 1.
DR Gene3D; 2.10.110.10; Cysteine Rich Protein; 4.
DR Gene3D; 1.10.555.10; Rho GTPase activation protein; 1.
DR InterPro; IPR042869; ARHGAP11A/B.
DR InterPro; IPR008936; Rho_GTPase_activation_prot.
DR InterPro; IPR000198; RhoGAP_dom.
DR InterPro; IPR001781; Znf_LIM.
DR PANTHER; PTHR15670; RHO GTPASE ACTIVATING PROTEIN 11A; 1.
DR PANTHER; PTHR15670:SF4; RHO GTPASE-ACTIVATING PROTEIN 11A; 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); 2.
DR SUPFAM; SSF48350; GTPase activation domain, GAP; 1.
DR PROSITE; PS00478; LIM_DOMAIN_1; 1.
DR PROSITE; PS50023; LIM_DOMAIN_2; 2.
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:UP000002035};
KW Zinc {ECO:0000256|PROSITE-ProRule:PRU00125}.
FT DOMAIN 104..165
FT /note="LIM zinc-binding"
FT /evidence="ECO:0000259|PROSITE:PS50023"
FT DOMAIN 168..228
FT /note="LIM zinc-binding"
FT /evidence="ECO:0000259|PROSITE:PS50023"
FT DOMAIN 841..1043
FT /note="Rho-GAP"
FT /evidence="ECO:0000259|PROSITE:PS50238"
FT REGION 1..101
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 574..682
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 21..41
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 54..68
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 69..87
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 606..636
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 637..653
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 654..682
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1136 AA; 125893 MW; 869EA0F333FC5A7B CRC64;
MASAGGRHIP ANLLPGNRGE DGGLQTTNTS GFQSQSPIDS PDASRGAPWS DIPPSAPSES
TVNPEERSSR QPDSYRSPGR NKSRDRHGNS NGPSTSKSPS GNTRICRVCG EALLGQFVRA
LGGTFHLECF QCKDCGEIVA SKFFPVDSED GTSQHPLCER DYFRRLNLLC FECGGALRGS
YITALDHKYH IEHFTCSVCP TVFGAQDSYY EHEGKVYCHY HYSTQFAQRC NGCQTAILKQ
FVEIFRNGQN QHWHPECYMI HKFWNVRLSP SGKPFEPPEI DRDVTTEERE QIRDDEEKME
EKVYRIWSVL SAFEESSAAC ISDMLLHVSN GAYVDGVVVA KKFIFHIEVL FKGTDQLAAQ
ISLLGIKEIA YGREAKLLCK KVVSFFSLLS KTQETGVRKL GVTQELLALV TGLAHYLKLL
IRIGLQGSLR LERETKSPEA LYNFLDLTAD LEEVNNITAS DLNADTSQLA NSQSDCCAAC
TEPIDDECIV LGRRLWHKKP PHLVCGACQD DLTHSLERAR WSEKNDRPFC QNCAVQRGHD
PQAVAGFENV TKLQQYVFLL RVALARLLSV LRSGGTLPHT SDDPNLKQYE ANDGHRIPPQ
ADPHLPPQRS NTRSMSYTGE PNSEPTPSSL EQTVGEMRRL RSTRNERAIS TTFKKARTSR
IISGPESSSV QPGAPGGANS SQNQNFQIVE ERDADGEPVA DLTFGNQDAL TLDDIPRIVA
AEQAKEQRPN AYKHAGQNLI GSGGPAAKLV NGHQRGVSVD QRGAMERPRA KKYFSELSAL
EYFIVRHVAV LSMEPLLEGS FNLEELLGLI EPRKPTIWNI FNRAFKNDPR KVGKKKGVFG
VALEVIVERD GTESTHGVGP GTLRIPTFID DAISAMRQMD MSVEGVFRKN GNIKRLRETA
ELIDTKYEAA ELDKESAVQV AALMKKFLRE MPDPLLTFKL HSLFVIAQKI ADPVKRKRVL
HLTCCLLPKS HRDTMEVLFS FLNWASSFCH VDDETGSKMD IHNLATVMTP NILYSNTKVA
GVDDSFLAIE AVTSLIENND TMCEVPEDLL SILTDSTLFN GSAEITTKEI LKRYGALGKL
PVPQRAPTVA ETIPVRSGSS KGNNSPIAAR IDTDPSQATA WQMQSSHTEA ALLLFK
//
