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Database: UniProt
Entry: A0A1L0GLD5_9ASCO
LinkDB: A0A1L0GLD5_9ASCO
Original site: A0A1L0GLD5_9ASCO 
ID   A0A1L0GLD5_9ASCO        Unreviewed;       971 AA.
AC   A0A1L0GLD5;
DT   15-FEB-2017, integrated into UniProtKB/TrEMBL.
DT   15-FEB-2017, sequence version 1.
DT   27-MAR-2024, entry version 25.
DE   SubName: Full=CIC11C00000001030 {ECO:0000313|EMBL:SGZ56989.1};
GN   ORFNames=SAMEA4029010_CIC11G00000001030 {ECO:0000313|EMBL:SGZ56989.1};
OS   [Candida] intermedia.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Metschnikowiaceae; Metschnikowiaceae incertae sedis;
OC   Candida/Metschnikowiaceae.
OX   NCBI_TaxID=45354 {ECO:0000313|EMBL:SGZ56989.1, ECO:0000313|Proteomes:UP000182334};
RN   [1] {ECO:0000313|EMBL:SGZ56989.1, ECO:0000313|Proteomes:UP000182334}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CBS 141442 {ECO:0000313|EMBL:SGZ56989.1,
RC   ECO:0000313|Proteomes:UP000182334};
RA   de Groot N.N.;
RL   Submitted (OCT-2016) to the EMBL/GenBank/DDBJ databases.
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DR   EMBL; LT635761; SGZ56989.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1L0GLD5; -.
DR   STRING; 45354.A0A1L0GLD5; -.
DR   OrthoDB; 25690at2759; -.
DR   Proteomes; UP000182334; Chromosome vi.
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; 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:UP000182334}.
FT   DOMAIN          526..637
FT                   /note="PH"
FT                   /evidence="ECO:0000259|PROSITE:PS50003"
FT   DOMAIN          762..971
FT                   /note="Rho-GAP"
FT                   /evidence="ECO:0000259|PROSITE:PS50238"
FT   REGION          92..131
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          164..184
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          319..379
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          715..734
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        93..124
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        164..178
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   971 AA;  108711 MW;  4EC8967E09A96A28 CRC64;
     MSDSGSDSKD DGLHHQMIED QDEMVNRMLL PSHPNFDRRE HTSEEFIELL LSEINDLKIA
     LKSKDIMITN FQAQLEHFNV DSTGVLIANT HSHLRTPDED VPQRSARRKL SQKGPEEAVS
     SAESDSRRES IASITSNGPI AAIDGMPLSS NFRSELSAAL GITTSNELSP QTSRHDLNVP
     GLDETPRILN SDDVVDLTVL NTNIQGVEFD QNASNKDVEG TANELVSSRK ASNPSVNSYK
     SRIKLPPTLK QPDLTCNAPS TPLINQESHP MNNQISFKNK ADLAAEAAKN QEPRLPLTPD
     GLSSNGKFFA RTEASGQLSE DSHSYFGSPF TNSPPNSSMT PTTNSNMEIS KTPNTHTFAS
     TDSFHSYQRP SSQTPGSSFH VLSTPKLEDE SVELFIKPEE FQSIRIHVVS TISANTKKAD
     DPNCTLSIND KETSKEMWRI RKTLSQLVAF DAEIRPVVEF FGLPPLPEKS LFSSTTPLKV
     DSRRISLQNY FNTLFVMPHV PRLVLFRICR FLSLDFVNLL DDFRTGAKKE GFLIRRYKGL
     GLGTAWKVRW CQVDGPELEI YDSPGGNLLE LIKLIGSQIG RQSSDTVAEQ RGYRHAFLIL
     ENAKISKLSA SSSKHFFCSE SDSERDEWVA AMVEYTENDP LASNDDQNSL QELDSPHVML
     NEDFDQSNRY LSGTSSNYAH LSFEADSSFV TILDESQREA KRATRKKSRF PFRNRVSTHS
     ETHVNQQENQ IVSSPQRSEL PMQTYLDQMK LSDEPARVIF GRDIEEAFRL SNHSYNGRQV
     PSICYRCLDF LSKTGAVYEE GIFRLSGSAS SIRQLKENFN SVHDVDLFES PLRPDMHTVA
     GLLKTYLREL PNPVFGRKAY SELQSLVSQT GGSPNSSTVY MMRDFLRDSG LVSKVNFDFC
     VTIFGYLRSV ITKSSTNKMS LRNVCIVFVP TLNISIDILS VCLTDFDCIF GNGDPIPDEK
     RLVLDLQIPT F
//
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