ID A0A0F4YFI3_TALEM Unreviewed; 1211 AA.
AC A0A0F4YFI3;
DT 24-JUN-2015, integrated into UniProtKB/TrEMBL.
DT 24-JUN-2015, sequence version 1.
DT 27-MAR-2024, entry version 35.
DE SubName: Full=Rho GTPase activator (Lrg11) {ECO:0000313|EMBL:KKA16681.1};
GN ORFNames=T310_9729 {ECO:0000313|EMBL:KKA16681.1};
OS Rasamsonia emersonii CBS 393.64.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Trichocomaceae; Rasamsonia.
OX NCBI_TaxID=1408163 {ECO:0000313|EMBL:KKA16681.1, ECO:0000313|Proteomes:UP000053958};
RN [1] {ECO:0000313|EMBL:KKA16681.1, ECO:0000313|Proteomes:UP000053958}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 393.64 {ECO:0000313|EMBL:KKA16681.1,
RC ECO:0000313|Proteomes:UP000053958};
RA Heijne W.H., Fedorova N.D., Nierman W.C., Vollebregt A.W., Zhao Z., Wu L.,
RA Kumar M., Stam H., van den Berg M.A., Pel H.J.;
RL Submitted (APR-2015) to the EMBL/GenBank/DDBJ databases.
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:KKA16681.1}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; LASV01000745; KKA16681.1; -; Genomic_DNA.
DR RefSeq; XP_013323293.1; XM_013467839.1.
DR AlphaFoldDB; A0A0F4YFI3; -.
DR STRING; 1408163.A0A0F4YFI3; -.
DR GeneID; 25321661; -.
DR OrthoDB; 1329523at2759; -.
DR Proteomes; UP000053958; 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; IPR008936; Rho_GTPase_activation_prot.
DR InterPro; IPR000198; RhoGAP_dom.
DR InterPro; IPR001781; Znf_LIM.
DR PANTHER; PTHR14963; RHO GTPASE ACTIVATING PROTEIN 18,19-RELATED; 1.
DR PANTHER; PTHR14963:SF1; RHO GTPASE-ACTIVATING PROTEIN CONUNDRUM; 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; 2.
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:UP000053958};
KW Zinc {ECO:0000256|PROSITE-ProRule:PRU00125}.
FT DOMAIN 117..178
FT /note="LIM zinc-binding"
FT /evidence="ECO:0000259|PROSITE:PS50023"
FT DOMAIN 181..241
FT /note="LIM zinc-binding"
FT /evidence="ECO:0000259|PROSITE:PS50023"
FT DOMAIN 861..1063
FT /note="Rho-GAP"
FT /evidence="ECO:0000259|PROSITE:PS50238"
FT REGION 1..116
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 592..658
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 741..790
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1109..1211
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 19..40
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 47..67
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 68..105
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 592..651
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1109..1197
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1211 AA; 134261 MW; 1E939F68202E0791 CRC64;
MPPDRALPDI LMPGNGGANS PRNWANQAGS QSQSPISPLD ESVPLDSPLS RTGNAPWNGG
AQSSRDDVQQ QDDPKRQDTG NDPQDHDQAD QRDRSNPRER PRPPARSNTK SPGSTTRICK
KCGETLTGQF VRALGGTYHL ECFKCNDCGE IVASKFFPVD AEDGSGQYPL CETDYFRRLN
LLCHACGGAL RGSYITALDR KYHIEHFTCS VCPTVFGAQD SYYEHEGNVY CHYHYSTQFA
QRCNGCHTAI LKQFVEIFRN GHNQHWHPEC YMIHKFWNVR LAPAGQPLER PEVGIDATDE
ERERVRQEED MMEEKVYKIW SILSSFEESS AACISDMLLH VSNGAYVDGV QVAKKFISHV
EILFTAIDML STMFKEQGIK DLSYGREAKL LCKKIVAFFS LLSKTQETGV RKLGVTQELL
SLVTGLAHYL KLLIRIGLQG ALKLERERNT SDGLYRFLDH LGDHIEELKA AEEESTDLMT
GVENLADQYS DCCAACKEPI DDACVILGDR RWHIKPPHLV CGVCQKDLTV DLPDGLWSEK
DDRPFCRNCA IQKGRVPAAQ GGFAYVSKLQ QYVFLLKVAL ARLLSVLRSS GTLSQTSDDP
NVNEHEANEG NRVSTTGELV SSSPQKTNTR SRAYTSSHAT EESSSLEQTV GEMRRLRSIR
NERTLSTTYK KARASRIIDG PEGSSVRPGS SGGDAVDARN QRFQIVEEKD ANGDTVNSLT
FGNQDALTLD DIPRIVAAEQ AKEQRPNAYR HAGTNLVGSG PPAKYSPGHR REVSGPPAEP
PPPDNAPTKT KKYFSELSAL EYFIVRHVAV LSMEPLVEGH FSLEELLSLI ESRKPTIWNI
FGRAFNKEGK RPGKKKGVFG VSLDYLVEKE GAESTHGVGP GALRVPALID DAVSAMRQMD
MSVEGVFRKN GNIRRLKDLA DMIDNKYDQV DLSKESPVQI AALLKKFLRE MPDPLLTFKL
HRLFVISQKI PDPEKQKRLL HLTCCLLPKA HRDTMEVLFA FLNWTSSFSH VDEESGSKMD
IHNLATVMTP NILYPNTKNS SMDESFLAIE AVSSLITYND TMCEVPEDLQ SILNDASFFK
DNADITTKEI LKRYGDFGKG NLAQKILQSG EMSGSTGSTR SNNAAATARI ETDPSQAAAW
QMQSSVRHVQ APGSSQQSTE HAQQQTQQGD YRDRSASAAS QQAMGRPSQS DAQQQLPYRP
HAGTGPMGVA G
//
