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Database: UniProt
Entry: A0A1G4ISJ3_9SACH
LinkDB: A0A1G4ISJ3_9SACH
Original site: A0A1G4ISJ3_9SACH 
ID   A0A1G4ISJ3_9SACH        Unreviewed;       955 AA.
AC   A0A1G4ISJ3;
DT   18-JAN-2017, integrated into UniProtKB/TrEMBL.
DT   18-JAN-2017, sequence version 1.
DT   27-MAR-2024, entry version 30.
DE   SubName: Full=LADA_0B03774g1_1 {ECO:0000313|EMBL:SCU79879.1};
GN   ORFNames=LADA_0B03774G {ECO:0000313|EMBL:SCU79879.1};
OS   Lachancea dasiensis.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Saccharomycetaceae; Lachancea.
OX   NCBI_TaxID=1072105 {ECO:0000313|EMBL:SCU79879.1, 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; LT598456; SCU79879.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1G4ISJ3; -.
DR   STRING; 1266660.A0A1G4ISJ3; -.
DR   OrthoDB; 5482027at2759; -.
DR   Proteomes; UP000190274; Chromosome B.
DR   GO; GO:0005933; C:cellular bud; IEA:UniProt.
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; cd09394; LIM1_Rga; 1.
DR   CDD; cd09395; LIM2_Rga; 1.
DR   CDD; cd00159; RhoGAP; 1.
DR   Gene3D; 2.10.110.10; Cysteine Rich Protein; 2.
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; PTHR23176:SF121; RHO-TYPE GTPASE-ACTIVATING PROTEIN 1-RELATED; 1.
DR   PANTHER; PTHR23176; RHO/RAC/CDC GTPASE-ACTIVATING PROTEIN; 1.
DR   Pfam; PF00620; RhoGAP; 1.
DR   SMART; SM00132; LIM; 2.
DR   SMART; SM00324; RhoGAP; 1.
DR   SUPFAM; SSF48350; GTPase activation domain, GAP; 1.
DR   PROSITE; PS00478; LIM_DOMAIN_1; 1.
DR   PROSITE; PS50023; LIM_DOMAIN_2; 1.
DR   PROSITE; PS50238; RHOGAP; 1.
PE   4: Predicted;
KW   Coiled coil {ECO:0000256|SAM:Coils};
KW   LIM domain {ECO:0000256|PROSITE-ProRule:PRU00125};
KW   Metal-binding {ECO:0000256|PROSITE-ProRule:PRU00125};
KW   Reference proteome {ECO:0000313|Proteomes:UP000190274};
KW   Zinc {ECO:0000256|PROSITE-ProRule:PRU00125}.
FT   DOMAIN          66..127
FT                   /note="LIM zinc-binding"
FT                   /evidence="ECO:0000259|PROSITE:PS50023"
FT   DOMAIN          741..954
FT                   /note="Rho-GAP"
FT                   /evidence="ECO:0000259|PROSITE:PS50238"
FT   REGION          165..248
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          268..295
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          408..553
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          637..668
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          591..618
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COMPBIAS        186..248
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        408..431
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        447..462
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        512..553
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        637..660
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   955 AA;  105781 MW;  6EBF0342E599F53C CRC64;
     MGNPTVETPT CVRCKDHLVM GHAYELGGDR WHTHCFSCYK CDKPLSCDSN FLVLGTGALI
     CYACSDSCKN CGKKIDDLAI ILASSNEAYC QDCFKCCKCG CKIEDLRYAK TKRGLFCIGC
     HERLLEKRKN YEERKRRLKK QLPLIPPNGS NSDVDTASAV IESTPDLTIP ERSMNRPMSP
     GKETHLVSYK DQSSLHSSPR NHGHHVSSAS SLAGPIDFSE TNSASGEPPT TSEKHDQTDL
     TANNSNIHSN SESVVAQFLI DGDYMSTADE ESVRGPPVSE VAPEDQDKVA SNHVTPKRTH
     KTNLSIDDML KNTLDLDNDE VQDAKSLNLL PNQHKKVLLN RTPLRNSHEE RINKSPTAYR
     QGLIFTDEDV VAINSPEMSQ DQNRSASPGL GIITPSKSAV VSNENDTMGI SYESLPPHNS
     VPGSAGSQIS RSPPPPGHHR RSSSGNAKKL GRSLSMRSKS IMMNLRPKSK DAKGGSWSTA
     ENDLDTHSGW GVAANSFADS PSARERQASK HTSDSTLYQP TRQDGAHHNR SSSGTTGVSI
     FRTPPLTSQS GFVRNGSLNS KLLDHGALQI DEHDEENDKT PTNDQFFRKD VQEAELTLRR
     LKLEVSQLRA TKAQLLSDVD SLRSSKDSLL DEIELSKAHK KHSATQSTES LEHDNFEDSV
     ERQAATASVA TTEKPKFWKL FSASKHAPGH AGGHGKFDIS PPVLQNPNEF EDVKLLPVQK
     DSKGLSSSPP AANDGNSLYG STLIARCSYE GRDVPVIIDT CIKHIESRKE FLQSDGLYRK
     SGSNVLIEQI EAAFGQWKPE EPISDKLRLQ LNQDIHAVTG VLKRYLRKLP DPVFCFQVYE
     PLMAFVRERD LVNALPLKGN YVGANKTVFQ NAVDQLSSLL RQLPRQHYTL LLVLVRHIEE
     VSRHSDHNLM NLHNLSLVFT PGLIRDYSGE KDITDMRERN YLVAFVLANH RHLLN
//
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