ID A0A093YV70_9PEZI Unreviewed; 1152 AA.
AC A0A093YV70;
DT 26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT 26-NOV-2014, sequence version 1.
DT 27-MAR-2024, entry version 34.
DE RecName: Full=Rho-type GTPase-activating protein 1 {ECO:0008006|Google:ProtNLM};
GN ORFNames=V492_05789 {ECO:0000313|EMBL:KFY08921.1};
OS Pseudogymnoascus sp. VKM F-4246.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Leotiomycetes;
OC Leotiomycetes incertae sedis; Pseudeurotiaceae; Pseudogymnoascus.
OX NCBI_TaxID=1420902 {ECO:0000313|EMBL:KFY08921.1, ECO:0000313|Proteomes:UP000029299};
RN [1] {ECO:0000313|EMBL:KFY08921.1, ECO:0000313|Proteomes:UP000029299}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=VKM F-4246 {ECO:0000313|EMBL:KFY08921.1,
RC ECO:0000313|Proteomes:UP000029299};
RA Leushkin E.V., Logacheva M.D., Penin A.A., Sutormin R.A., Gerasimov E.S.,
RA Kochkina G.A., Ivanushkina N.E., Vasilenko O.V., Kondrashov A.S.,
RA Ozerskaya S.M.;
RT "Population genomics of a fungus Geomyces pannorum provides evidence of
RT horizontal gene transfer but not of sexual reproduction.";
RL Submitted (JUL-2014) 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:KFY08921.1}.
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DR EMBL; JPJU01002057; KFY08921.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A093YV70; -.
DR STRING; 1420902.A0A093YV70; -.
DR HOGENOM; CLU_001321_1_0_1; -.
DR Proteomes; UP000029299; 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; cd09392; LIM2_Lrg1p_like; 1.
DR CDD; cd04397; RhoGAP_fLRG1; 1.
DR Gene3D; 2.10.110.10; Cysteine Rich Protein; 3.
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; 2.
DR Pfam; PF00620; RhoGAP; 1.
DR SMART; SM00132; LIM; 2.
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; 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:UP000029299};
KW Zinc {ECO:0000256|PROSITE-ProRule:PRU00125}.
FT DOMAIN 165..225
FT /note="LIM zinc-binding"
FT /evidence="ECO:0000259|PROSITE:PS50023"
FT DOMAIN 492..555
FT /note="LIM zinc-binding"
FT /evidence="ECO:0000259|PROSITE:PS50023"
FT DOMAIN 864..1067
FT /note="Rho-GAP"
FT /evidence="ECO:0000259|PROSITE:PS50238"
FT REGION 1..114
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 588..697
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1103..1152
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 24..86
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 88..108
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 588..608
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 617..643
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 644..676
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1134..1152
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1152 AA; 128840 MW; 55A954B6167C66DF CRC64;
MGPQSEGGPP GPSWAYGGPP PSGEDNRYQS SRDMGPSGYP QQQQQQQQLQ LQQQQQQNLP
RQNQNNGYDQ ANRGPPPPSL QVSQRKDNLG GDAHRDSSER DRSRHRGGKR TGSGQLRLCK
KCGEPLTGQF DCGQIVASKF FPVDDESGQG QYPLCETDYF RRLGLLCHQC GGALRGSYIT
ALERKYHIDH FTCSVCPTVF GAQDSYYEHD DKVYCHYHYS TQFAQRCNGC QTAILKQFVE
IFRNGQNQHW HPECYMIHKF WNVRLAEASS EPLPERPLLK DASDVEARNL VRDEEERMEE
KVYRIWSVLS TFEESSAANI SDMLLHVSNG AYVDGVLTAK KFIWHVDLLF KSADKLDAVI
SQQGVKGTSS HMASRDKKLT QNAGLSYSRE AKLLCKKIVA FFALLSKTQE TGVRKLGVTQ
ELLSLVTGLA HYLKLLIRIC LQGALRVERE MKNTHGLDLF LGDLGDVDQV RDDEKSLEET
TGTTGLAGAT SDQCTQCQRP IEDECAIIGE KRWHLACLSC SNCSRDLSHN LEDVRWSDSD
RVLYCNNCQN RSPDSVSGFT HVTRLQQYVF LLRVALARLL MMLRNSGTLP HTSDDPNLNG
YNSQEGHRLG ESSEPHPAAL TQESRSKSYG GTSEENPRES SYENTLNDVR RLRSTRMDKH
LSSTIKKART SRIMDGPESR SVRPGSAGAD GSDTRNNDFH IVEERDNQGE PRSELLFGHQ
DALTLDDIPR IVAAEQAKEQ RPNAYKHARH ELFKTSITEP KLLNGHQRTY SNANELDIPS
LENEPSPQRG PPGKRYFSEL SALEYFIVRH VAVLSMQPLL DGHFTLEELL GLIESRKPTF
WDKFGKAFKN DGRKGAKKKG VFGVPLDAII ERDGADSTDG VGPGSLRIPA LVDDAISTMR
KMDLSVEGVF RKNGNIKRLN DAVAAIDKDG CDAVDLSTEN VVQVAALLKK YLRELPDPLL
TFKLHRLYIT SQKIADQDKR RRVLHLTCCL LPKAHRDCLE ILCSFLNWTA SFHQVDEESG
SKMDTHNLAT VIAPNILFTN TKNAGMDDSF LAIEAVHSLI EFNDQMCEVP EDLQSILNDS
TLFTNSSDIT TKEILKRYGD IAASGGPRHQ VETTQGPARS ADSRSGAHAP VVTRVETETS
QNGTWQNETS PE
//
