ID   M7WN26_RHOT1            Unreviewed;       491 AA.
AC   M7WN26;
DT   29-MAY-2013, integrated into UniProtKB/TrEMBL.
DT   29-MAY-2013, sequence version 1.
DT   24-JAN-2024, entry version 33.
DE   SubName: Full=Rho GTPase-activating protein {ECO:0000313|EMBL:EMS19481.1};
GN   ORFNames=RHTO_04255 {ECO:0000313|EMBL:EMS19481.1};
OS   Rhodotorula toruloides (strain NP11) (Yeast) (Rhodosporidium toruloides).
OC   Eukaryota; Fungi; Dikarya; Basidiomycota; Pucciniomycotina;
OC   Microbotryomycetes; Sporidiobolales; Sporidiobolaceae; Rhodotorula.
OX   NCBI_TaxID=1130832 {ECO:0000313|EMBL:EMS19481.1, ECO:0000313|Proteomes:UP000016926};
RN   [1] {ECO:0000313|EMBL:EMS19481.1, ECO:0000313|Proteomes:UP000016926}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NP11 {ECO:0000313|EMBL:EMS19481.1,
RC   ECO:0000313|Proteomes:UP000016926};
RX   PubMed=23047670; DOI=10.1038/ncomms2112;
RA   Zhu Z., Zhang S., Liu H., Shen H., Lin X., Yang F., Zhou Y.J., Jin G.,
RA   Ye M., Zou H., Zou H., Zhao Z.K.;
RT   "A multi-omic map of the lipid-producing yeast Rhodosporidium toruloides.";
RL   Nat. Commun. 3:1112-1112(2012).
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DR   EMBL; KB722668; EMS19481.1; -; Genomic_DNA.
DR   RefSeq; XP_016270600.1; XM_016417923.1.
DR   AlphaFoldDB; M7WN26; -.
DR   GeneID; 27368268; -.
DR   eggNOG; KOG4406; Eukaryota.
DR   HOGENOM; CLU_035054_0_0_1; -.
DR   OrthoDB; 1423134at2759; -.
DR   Proteomes; UP000016926; Unassembled WGS sequence.
DR   GO; GO:0005096; F:GTPase activator activity; IEA:UniProt.
DR   GO; GO:0007165; P:signal transduction; IEA:InterPro.
DR   CDD; cd00159; RhoGAP; 1.
DR   Gene3D; 3.40.525.10; CRAL-TRIO lipid binding domain; 1.
DR   Gene3D; 1.10.555.10; Rho GTPase activation protein; 1.
DR   InterPro; IPR001251; CRAL-TRIO_dom.
DR   InterPro; IPR036865; CRAL-TRIO_dom_sf.
DR   InterPro; IPR008936; Rho_GTPase_activation_prot.
DR   InterPro; IPR000198; RhoGAP_dom.
DR   PANTHER; PTHR45808; RHO GTPASE-ACTIVATING PROTEIN 68F; 1.
DR   PANTHER; PTHR45808:SF2; RHO GTPASE-ACTIVATING PROTEIN 68F; 1.
DR   Pfam; PF13716; CRAL_TRIO_2; 1.
DR   Pfam; PF00620; RhoGAP; 1.
DR   SMART; SM00324; RhoGAP; 1.
DR   SUPFAM; SSF48350; GTPase activation domain, GAP; 1.
DR   PROSITE; PS50238; RHOGAP; 1.
PE   4: Predicted;
FT   DOMAIN          274..484
FT                   /note="Rho-GAP"
FT                   /evidence="ECO:0000259|PROSITE:PS50238"
FT   REGION          1..90
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        47..90
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   491 AA;  52192 MW;  EE52A19534E58FE0 CRC64;
     MSATEWGGTL SAMFGVGGKA RGGASNGREG GRGAATVAAP GGLQQKQKTD VRRRLPDWSA
     GEAGEEVGHP SEEDGLEDGK ENQDSSDSQL EGDELDKLAA AILWQAGITT DASPHPFLVV
     AASRSPPSSE VSHPDLLTRL RLRLEQFAER GPYSVILFVN PAPNSPSTAH LVAAYLALSR
     TARKNVQHVY VVGGGWWSSI LVTLFSATLL SVRTITSRGK LVQCPSLSSL AESVGGKAFV
     QIDVPLEIYV ANAAVEKAIK LPEADDQVPR TFGVSLEQLV GKDRKRLPRL VRDCLAVLAA
     GGPASVGIFR RSPSASTVSH LAAAYDRGHP VTLSSAPDAP YIAASLLKKL LHDLPDPFIP
     RDTWDAIKAC PLDDDLAVPY LRTNFLPLLP SASRHLLSRL VSVLSAIAAN HSHNLMTSSN
     LVICLCPALM GGLGASRDEL EMCRVPGMEV GSMRGLETIK RRERAGNTLG GVLRVMIDRQ
     SDLVDPPEPS A
//