ID   G1XBN5_ARTOA            Unreviewed;      1122 AA.
AC   G1XBN5;
DT   16-NOV-2011, integrated into UniProtKB/TrEMBL.
DT   16-NOV-2011, sequence version 1.
DT   27-MAR-2024, entry version 52.
DE   RecName: Full=Rho-type GTPase-activating protein 1 {ECO:0008006|Google:ProtNLM};
GN   ORFNames=AOL_s00078g332 {ECO:0000313|EMBL:EGX49299.1};
OS   Arthrobotrys oligospora (strain ATCC 24927 / CBS 115.81 / DSM 1491)
OS   (Nematode-trapping fungus) (Didymozoophaga oligospora).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Orbiliomycetes;
OC   Orbiliales; Orbiliaceae; Orbilia; Orbilia oligospora.
OX   NCBI_TaxID=756982 {ECO:0000313|EMBL:EGX49299.1, ECO:0000313|Proteomes:UP000008784};
RN   [1] {ECO:0000313|EMBL:EGX49299.1, ECO:0000313|Proteomes:UP000008784}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 24927 / CBS 115.81 / DSM 1491
RC   {ECO:0000313|Proteomes:UP000008784};
RX   PubMed=21909256; DOI=10.1371/journal.ppat.1002179;
RA   Yang J., Wang L., Ji X., Feng Y., Li X., Zou C., Xu J., Ren Y., Mi Q.,
RA   Wu J., Liu S., Liu Y., Huang X., Wang H., Niu X., Li J., Liang L., Luo Y.,
RA   Ji K., Zhou W., Yu Z., Li G., Liu Y., Li L., Qiao M., Feng L., Zhang K.-Q.;
RT   "Genomic and proteomic analyses of the fungus Arthrobotrys oligospora
RT   provide insights into nematode-trap formation.";
RL   PLoS Pathog. 7:E1002179-E1002179(2011).
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:EGX49299.1}.
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DR   EMBL; ADOT01000134; EGX49299.1; -; Genomic_DNA.
DR   RefSeq; XP_011121897.1; XM_011123595.1.
DR   AlphaFoldDB; G1XBN5; -.
DR   STRING; 756982.G1XBN5; -.
DR   GeneID; 22892810; -.
DR   eggNOG; KOG1703; Eukaryota.
DR   eggNOG; KOG2710; Eukaryota.
DR   HOGENOM; CLU_001321_1_0_1; -.
DR   InParanoid; G1XBN5; -.
DR   OMA; WQMQSSV; -.
DR   OrthoDB; 1329523at2759; -.
DR   Proteomes; UP000008784; 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; 3.
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:UP000008784};
KW   Zinc {ECO:0000256|PROSITE-ProRule:PRU00125}.
FT   DOMAIN          67..128
FT                   /note="LIM zinc-binding"
FT                   /evidence="ECO:0000259|PROSITE:PS50023"
FT   DOMAIN          131..191
FT                   /note="LIM zinc-binding"
FT                   /evidence="ECO:0000259|PROSITE:PS50023"
FT   DOMAIN          439..501
FT                   /note="LIM zinc-binding"
FT                   /evidence="ECO:0000259|PROSITE:PS50023"
FT   DOMAIN          781..983
FT                   /note="Rho-GAP"
FT                   /evidence="ECO:0000259|PROSITE:PS50238"
FT   REGION          1..62
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1021..1122
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1083..1122
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1122 AA;  126129 MW;  F75FC1A8D613D087 CRC64;
     MASPYSDPQI RGHNIPNALI PGPPASVSAP PPPTLDISSQ RRSDDRPNLS PTDGKPRGSS
     KSEATRRICK KCELPLTGQF VRALGGTFHL DCFRCRDCGT IVAQKFFPVD SEDGTTQYPL
     CETDYFRRLD LLCHACGGAL RGSYITALER KYHIEHFTCC VCPTVFGPQD SYYEHDGEVY
     CHYHYSTKFA ARCQGCQTAI LKQFVEIFRN GVNQHWHPEC YMIHKFWNVK LAESDSSEIP
     TIQEEGEKDP SSARRSIVRD AEEKMEEKVY RIWSVLSTYE ESSAANISDM LLHVSNGAYV
     DGVFVAEKFI WHVELLFTSA DNLDIELYRI GGEGLAYSRE AKLLCKKIVA FFTLLSKTQE
     TGVRKLGVTQ ELLSLVTGLA HYLKLLIRIS LQGALKLERD YSNVDAFNRF LAELSDLEAA
     KDVKPTFEVN TALADLNSDL CYGCHNTIED ECMKFGMLKW HINCFNCSNC NNSLKNDIDS
     ARLSPASTIL CASCVVHFPD AQKGFQHVSR LKQYVYLLRV ALARLLNMLK EGGTLPHTSD
     DPNLTGYDDA GHSLAPGALT AESRSKSYHG EGEGYNSTVS DVRRLRSTRL DQKLTSSGRK
     ARQSRIIENE NFGAEGSHER ERFRIVEDRD VNGEAINELT FGDEKTLTLD DIPRIAAQEQ
     AREQRPNAFK HRTSGFFSTG GMHQPKLMNG YQRDSTGSGQ PQQPVRMRRY FSELSAIDYF
     IIRHLACMCM LPLVSDHFNL EELLDLIERS GKQTLWNKFT KGFKQDGTKN KKQKKNAVFG
     VPLEQLIEKD HAESSLGIGP GTLRVPALLD DSISAMKQLD MSVEGVFRKN GNIRRLKDLT
     AQIDSGAENV DLVKEGPVQV AALLKKFLRE LPDPLLTFKL YKLFIVSQKL EDDEKKRRVL
     HLTCCLLPKY HRDSIEILFS FLNWVASFSH VDEESGSKMD VHNLATVITP NILYMKNQVP
     GMDDSFLAIE AIHTLIEYNE QMCEVPEDLL VILSDPTMMA TSDMSTKEIL KKYGDVAKFS
     SVPGKHPGGR GGNAQNTDKP TLHHVNNDRT GEGWYKDQTV RQVSTPPAPE PHRLPEPMYA
     NENGNHSHHS HSFSFDQDPS ANGRRMDYPS NHQNPNLSAH AG
//