ID   A0A1G4J014_9SACH        Unreviewed;      1020 AA.
AC   A0A1G4J014;
DT   18-JAN-2017, integrated into UniProtKB/TrEMBL.
DT   18-JAN-2017, sequence version 1.
DT   27-MAR-2024, entry version 29.
DE   SubName: Full=LADA_0C08548g1_1 {ECO:0000313|EMBL:SCU82893.1};
GN   ORFNames=LADA_0C08548G {ECO:0000313|EMBL:SCU82893.1};
OS   Lachancea dasiensis.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Saccharomycetaceae; Lachancea.
OX   NCBI_TaxID=1072105 {ECO:0000313|EMBL:SCU82893.1, ECO:0000313|Proteomes:UP000190274};
RN   [1] {ECO:0000313|Proteomes:UP000190274}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Devillers H.;
RL   Submitted (MAR-2016) to the EMBL/GenBank/DDBJ databases.
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DR   EMBL; LT598459; SCU82893.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1G4J014; -.
DR   STRING; 1266660.A0A1G4J014; -.
DR   OrthoDB; 25690at2759; -.
DR   Proteomes; UP000190274; Chromosome C.
DR   GO; GO:0005933; C:cellular bud; IEA:UniProt.
DR   GO; GO:0005096; F:GTPase activator activity; IEA:UniProt.
DR   GO; GO:0035091; F:phosphatidylinositol binding; IEA:InterPro.
DR   GO; GO:0007165; P:signal transduction; IEA:InterPro.
DR   CDD; cd13277; PH_Bem3; 1.
DR   CDD; cd06093; PX_domain; 1.
DR   Gene3D; 3.30.1520.10; Phox-like domain; 1.
DR   Gene3D; 2.30.29.30; Pleckstrin-homology domain (PH domain)/Phosphotyrosine-binding domain (PTB); 1.
DR   Gene3D; 1.10.555.10; Rho GTPase activation protein; 1.
DR   InterPro; IPR011993; PH-like_dom_sf.
DR   InterPro; IPR001849; PH_domain.
DR   InterPro; IPR001683; PX_dom.
DR   InterPro; IPR036871; PX_dom_sf.
DR   InterPro; IPR008936; Rho_GTPase_activation_prot.
DR   InterPro; IPR000198; RhoGAP_dom.
DR   PANTHER; PTHR23176:SF129; RHO GTPASE ACTIVATING PROTEIN AT 16F, ISOFORM E-RELATED; 1.
DR   PANTHER; PTHR23176; RHO/RAC/CDC GTPASE-ACTIVATING PROTEIN; 1.
DR   Pfam; PF00169; PH; 1.
DR   Pfam; PF00787; PX; 1.
DR   Pfam; PF00620; RhoGAP; 1.
DR   SMART; SM00233; PH; 1.
DR   SMART; SM00324; RhoGAP; 1.
DR   SUPFAM; SSF48350; GTPase activation domain, GAP; 1.
DR   SUPFAM; SSF50729; PH domain-like; 1.
DR   SUPFAM; SSF64268; PX domain; 1.
DR   PROSITE; PS50003; PH_DOMAIN; 1.
DR   PROSITE; PS50238; RHOGAP; 1.
PE   4: Predicted;
KW   Reference proteome {ECO:0000313|Proteomes:UP000190274}.
FT   DOMAIN          560..667
FT                   /note="PH"
FT                   /evidence="ECO:0000259|PROSITE:PS50003"
FT   DOMAIN          804..1020
FT                   /note="Rho-GAP"
FT                   /evidence="ECO:0000259|PROSITE:PS50238"
FT   REGION          1..57
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          98..179
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          200..277
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          317..351
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          681..770
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        11..31
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        32..57
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        102..123
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        200..215
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        229..272
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        317..334
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        681..702
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        725..739
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        743..770
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1020 AA;  113619 MW;  AF9B54869531B426 CRC64;
     MLEPEESSIS ARSEGGATTL SGTMQLLSQY NDHTQERDKS LEQVEDREQH AGQADYDDLF
     KENVKLKLQL EEYETEIISL RKFIEVLKNN RGLSPDSIEQ KLLVDEPPKE PTLPPRSAER
     KRNTKGLSLN APSELHGSDL KTRHLLSPAD PVPRGKSSIK SNPTVLPKPQ DNDPLLSPRE
     LDRIRRSSSS YSNMIAASPA TSMAYTTSRI SPSKSNKQGA KDDEQTTLAS ERSSLSRQES
     KIGGTPIRDT VSSPLRQTFG GNMQQALGDN PASKSYPKSP VPNLLANERG NLDFSPSSKQ
     NLNNFAEMLE SSFENQNSAA VDNGPSTRRS ASPFLGSPVT LKKPMKSPLL SPNAQTRMKS
     LQFSADERPP TNLTSQTLLF PDQFSPRSFS NRSFPTAPNP SGAFTAQINR EGSTKSLTDS
     QSVVSDIPLF IQPAELDSIR IDVISTFHRD HDALDDVDNI LFSVIDKKSS QEMFRFSKTI
     DRIYELDVYL KCHMDTIILP PLPERQYFEA TSPVKVDYRR EKLNDYFSCL YSSPQLPPSV
     RLKMAKFIST DTVMNPPTGD YAKEGVLLLR KSKTLGTPSS WRVVYAALHG GCLSFLDKGH
     VTENIKLQHA VIELQANLPD DKHGTKNGFI VVVPKKGGLS SGTKYYFCCE SPRERESWIS
     NLTEFVEVSA ATSFSVHNKS ENSSVLDHSS VGNDTSTDIA PSYLGPMANL QEPVTAAPTQ
     GSDVNITDEE RESKRSRMRS FFPFKKASSQ TPTHSEFSHS NGNERGASTT ATNELSIEKS
     LQAMDLNAEP ASDKVFGSTL VNCLSLSSHL YQGSYNVPSI VYRCMEYLYR NHGIEEEGIF
     RISGSTVLIK SLQERFDRDY DVDLCDFNKS VATGNNESSY TSGLVDVNTV TGLLKLYLRK
     LPHSIFGDDM FIEFKEVVDS NLRSPGQIAL EYRRLINSNE MRNENLSLIY VLFELLVKIN
     QKSAINKMNL RNLCIVFSPT LNIPVNVIQP FVVDFNCIFK NDDPISEAMR EELDVNIPQL
//