ID A0A0D2E1C7_9EURO Unreviewed; 1186 AA.
AC A0A0D2E1C7;
DT 29-APR-2015, integrated into UniProtKB/TrEMBL.
DT 29-APR-2015, sequence version 1.
DT 27-MAR-2024, entry version 38.
DE RecName: Full=Rho-type GTPase-activating protein 1 {ECO:0008006|Google:ProtNLM};
GN ORFNames=Z517_03112 {ECO:0000313|EMBL:KIW83866.1};
OS Fonsecaea pedrosoi CBS 271.37.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Chaetothyriomycetidae; Chaetothyriales; Herpotrichiellaceae; Fonsecaea.
OX NCBI_TaxID=1442368 {ECO:0000313|EMBL:KIW83866.1, ECO:0000313|Proteomes:UP000053029};
RN [1] {ECO:0000313|EMBL:KIW83866.1, ECO:0000313|Proteomes:UP000053029}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 271.37 {ECO:0000313|EMBL:KIW83866.1,
RC ECO:0000313|Proteomes:UP000053029};
RG The Broad Institute Genomics Platform;
RA Cuomo C., de Hoog S., Gorbushina A., Stielow B., Teixiera M.,
RA Abouelleil A., Chapman S.B., Priest M., Young S.K., Wortman J., Nusbaum C.,
RA Birren B.;
RT "The Genome Sequence of Fonsecaea pedrosoi CBS 271.37.";
RL Submitted (JAN-2015) to the EMBL/GenBank/DDBJ databases.
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; KN846970; KIW83866.1; -; Genomic_DNA.
DR RefSeq; XP_013287674.1; XM_013432220.1.
DR AlphaFoldDB; A0A0D2E1C7; -.
DR STRING; 1442368.A0A0D2E1C7; -.
DR GeneID; 25302602; -.
DR VEuPathDB; FungiDB:Z517_03112; -.
DR HOGENOM; CLU_001321_1_0_1; -.
DR OrthoDB; 1329523at2759; -.
DR Proteomes; UP000053029; 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); 3.
DR SUPFAM; SSF48350; GTPase activation domain, GAP; 1.
DR PROSITE; PS00478; LIM_DOMAIN_1; 2.
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:UP000053029};
KW Zinc {ECO:0000256|PROSITE-ProRule:PRU00125}.
FT DOMAIN 97..158
FT /note="LIM zinc-binding"
FT /evidence="ECO:0000259|PROSITE:PS50023"
FT DOMAIN 161..221
FT /note="LIM zinc-binding"
FT /evidence="ECO:0000259|PROSITE:PS50023"
FT DOMAIN 470..535
FT /note="LIM zinc-binding"
FT /evidence="ECO:0000259|PROSITE:PS50023"
FT DOMAIN 832..1041
FT /note="Rho-GAP"
FT /evidence="ECO:0000259|PROSITE:PS50238"
FT REGION 1..99
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 587..642
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 655..674
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1121..1186
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 12..61
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 62..77
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 78..99
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 605..626
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 627..642
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1121..1143
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1186 AA; 131610 MW; 1D981E91D83D86FE CRC64;
MAAPLDELHQ GNSGNMRYTI GTSRNQNELA PQNSNGQYPY TPPTQANGNT NEVPYDSDAR
YSSDSRTGRK RSVGGQGERS RSRTNGSAGK SSNSGTRQCR KCGEPLTGQF VRALGGTFHL
DCFKCADCGQ IVASKFFPVD AEDGSGQFPL CETDYFRRLD LLCFECGGAL RGSYITALDR
KYHIEHFTCS VCPTVFGAQD SYYEHDGRVY CHYHYSTQFA QRCNGCQTAI LKQFVEIFRN
GQNQHWHPEC YMIHKFWNVR LAQSEAVVER RDMHAPVTED ERETVKEDEE KMEDKVYRIW
STLSTFEESS ASCISDMLLH VSNGVYVDGV IVARKFIWHV DILFGAIDTL AALIIKAQLK
ELAYGREAKL LCKKVVAFFT LLSKTQETGV RKLGVTQELL SLVTGLAHYL KLLIRIGLQG
ALKLEREKGS PEGLHAFLDE LADLETIKEQ EMKSLDLQES VAGLASQESD CCSACMEPID
DECVMIYGRR WHVKPRHLTC SVCQRDLTSD LGIAMYNERE EKVYCVDHAK RTPDTVSGFA
HVTKLQQYVF LLRVALARLL EVLKSGGTLP HTSDDPNLTP YKTNDGHHIS GSGEPVMPHQ
MMGSRSRSYA GTSSQQQSSL EQTVGEMKRL RSTRNERALS TTFRKARESR ILYDGAGVRP
GSEGAEGHDH RNPGGFEIVQ EKDLDGRMKS ELTFNNQEGL TLDDIPRIVA AEQAKEQRPN
AFRHAGTNLI GHRGNEPRLV NGHQRNSSGG GADLLAGEHP LRTKRYFSEL SALEYFIVRH
VAVLSMQPLL DGEYTLEDLL GLIEQRKQTF WGKVSRALRG DAGVKKKGTF GVPLEVLVER
EGAESTNGVG PGALTVPAIV DDCVSAMKQM DMSVEGVFRK NGNIKRLKET AEAIDANQTP
DLNRENPVQV AALLKKFLRE MPEPLLTYKL QKLFITSQKI VDDERRRRVL HLTCCLMPKS
HRDTMEVLFS FLKWAASFSQ VDEESGSKMD IHNLATVMAP NILYAKEKAP GARQPQVPQV
DESFLAIEAV NTLIEYNDLF CQVPEDLQSI LTDTNLHGVS AELTTKEILS RYGHIAKGQV
QRQTVAAPDA PVRSPVSASN SLGPVATRVD VDPYQATAWQ KQSSVRPVQN MASATSTPAH
EFNFGVPNSP YARDRAGSAD SSGSRGGGPG GRQSYQPRPG QMGVTG
//
