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Database: UniProt
Entry: G8JVT9_ERECY
LinkDB: G8JVT9_ERECY
Original site: G8JVT9_ERECY 
ID   G8JVT9_ERECY            Unreviewed;      1029 AA.
AC   G8JVT9;
DT   25-JAN-2012, integrated into UniProtKB/TrEMBL.
DT   25-JAN-2012, sequence version 1.
DT   27-MAR-2024, entry version 60.
DE   RecName: Full=Rho-GAP domain-containing protein {ECO:0008006|Google:ProtNLM};
GN   OrderedLocusNames=Ecym_7102 {ECO:0000313|EMBL:AET40954.1};
OS   Eremothecium cymbalariae (strain CBS 270.75 / DBVPG 7215 / KCTC 17166 /
OS   NRRL Y-17582) (Yeast).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Saccharomycetaceae; Eremothecium.
OX   NCBI_TaxID=931890 {ECO:0000313|EMBL:AET40954.1, ECO:0000313|Proteomes:UP000006790};
RN   [1] {ECO:0000313|Proteomes:UP000006790}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CBS 270.75 / DBVPG 7215 / KCTC 17166 / NRRL Y-17582
RC   {ECO:0000313|Proteomes:UP000006790};
RX   DOI=10.1534/g3.111.000745;
RA   Leh Louis V., Despons L., Friedrich A., Martin T., Durrens P.,
RA   Casaregola S., Neuveglise C., Fairhead C., Marck C., Cruz J.A.,
RA   Straub M.L., Kugler V., Sacerdot C., Uzunov Z., Thierry A., Weiss S.,
RA   Bleykasten C., De Montigny J., Jacques N., Jung P., Lemaire M., Mallet S.,
RA   Morel G., Richard G.F., Sarkar A., Savel G., Schacherer J., Seret M.L.,
RA   Talla E., Samson G., Jubin C., Poulain J., Vacherie B., Barbe V.,
RA   Pelletier E., Sherman D.J., Westhof E., Weissenbach J., Baret P.V.,
RA   Wincker P., Gaillardin C., Dujon B., Souciet J.L.;
RT   "Pichia sorbitophila, an interspecies yeast hybrid reveals early steps of
RT   genome resolution following polyploidization.";
RL   G3 (Bethesda) 2:299-311(2012).
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DR   EMBL; CP002503; AET40954.1; -; Genomic_DNA.
DR   RefSeq; XP_003647771.1; XM_003647723.1.
DR   AlphaFoldDB; G8JVT9; -.
DR   STRING; 931890.G8JVT9; -.
DR   GeneID; 11471237; -.
DR   KEGG; erc:Ecym_7102; -.
DR   eggNOG; KOG4269; Eukaryota.
DR   HOGENOM; CLU_010436_0_0_1; -.
DR   InParanoid; G8JVT9; -.
DR   OrthoDB; 25690at2759; -.
DR   Proteomes; UP000006790; Chromosome 7.
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; 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:UP000006790}.
FT   DOMAIN          570..677
FT                   /note="PH"
FT                   /evidence="ECO:0000259|PROSITE:PS50003"
FT   DOMAIN          815..1029
FT                   /note="Rho-GAP"
FT                   /evidence="ECO:0000259|PROSITE:PS50238"
FT   REGION          266..307
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          385..437
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        277..304
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        385..410
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1029 AA;  113844 MW;  489A69329E9FD387 CRC64;
     MDNDSDADNR SYSGSSTLQL LAQYDKYTME RDRSIESIEK NRFSESSRPS YDDLFKENVK
     LKLQLKETHL EIESLKSIIA HFQDSGRFEA TKLEQRERSE PSALIRDLAL PPRSADRKRN
     TKNLTLGTSS PLFADHFSSA LSGVALKELS NSSRLSASSS VLAPRSADIL VSRSSPIEEK
     QLLSPMKAVS RSSSTYSTVL GSPATSVLYK TSRISINSPA KSSATSKAAS TLSLPDNINF
     ENEGNQLSPQ KTDRVTQLIK SELQVLQRER VDKRSASRSN SPGISVDKTG SRSRKPSDLS
     TGTRADLGNF KDMVDNVFNE NDQAVESSVN SSEDSINKSM DHLNTPNISI KDGENVETPL
     TLNRGAASDV YTQTPFVLTT STGEKLESPA ASANTGHMAS LSSTGKLPQA ATPSADPHLM
     SASVEGSTPH SNQEVRSADV PLFVQPEDLG TIKMEVISTL YHEPGNSANI LFSVIDRKSS
     KEMFKFAKTI DSVIEFDMYI RSNMDSLALP PLPDKQLFAT NIPVKVDTRR ENLNDYFSSL
     LYMTNLLPGP ALKLAEFIST TPVMNPVMGD YSKEGILLVR KAKTLGSAAS WRVRYCTVEG
     NVMYLNEQSF VTDTIKLAYS TIELQANLPD DRYGTKNGFI INEHKKSGLS SSTKYYFCAE
     TSREREQWIS VLTIMCDAPG GGNLNVSFNN RSEASSLVDQ GSASDSSYLG PIANLEVNND
     INSPPKIPDG TGNICIPEDE KEVKRRRMKS FFAFKKLSNP APYSSGNDNV SIFSQDEEVN
     STTTGTESTI HKSLQSMHLY SNNKVVFGAD LKTALQLSSH AYQGRYEIPS IVFRTLEFLY
     KNRGIHEEGI FRLSGSSLLI KSLQEQFDRD HDVDLCNYNK NVVVSPENEN QGGIYVDVNT
     VTGLLKLYLR RLPHMIFGDD AFSAFKQIVD KPGGKDTKFV AQEFKTLLFS GKIPKENISL
     MYALFELLVK INDNNNINKM NLRNLCIVFS PTLNIPVNIL QPFILDFGYI FQDKALVNNG
     QNVNLHIPL
//
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