ID A0A0P1BAI6_9BASI Unreviewed; 1129 AA.
AC A0A0P1BAI6;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 27-MAR-2024, entry version 33.
DE SubName: Full=Predicted Rho/Rac guanine nucleotide exchange factor/faciogenital dysplasia protein 3 {ECO:0000313|EMBL:CEH13055.1};
OS Ceraceosorus bombacis.
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Ustilaginomycotina;
OC Exobasidiomycetes; Ceraceosorales; Ceraceosoraceae; Ceraceosorus.
OX NCBI_TaxID=401625 {ECO:0000313|EMBL:CEH13055.1, ECO:0000313|Proteomes:UP000054845};
RN [1] {ECO:0000313|EMBL:CEH13055.1, ECO:0000313|Proteomes:UP000054845}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Magalhaes I.L.F., Oliveira U., Santos F.R., Vidigal T.H.D.A.,
RA Brescovit A.D., Santos A.J.;
RL Submitted (SEP-2014) to the EMBL/GenBank/DDBJ databases.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton
CC {ECO:0000256|ARBA:ARBA00004245}.
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DR EMBL; CCYA01000192; CEH13055.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0P1BAI6; -.
DR STRING; 401625.A0A0P1BAI6; -.
DR OrthoDB; 53554at2759; -.
DR Proteomes; UP000054845; Unassembled WGS sequence.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
DR GO; GO:0005856; C:cytoskeleton; IEA:UniProtKB-SubCell.
DR GO; GO:0005085; F:guanyl-nucleotide exchange factor activity; IEA:InterPro.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR CDD; cd00160; RhoGEF; 1.
DR Gene3D; 1.20.900.10; Dbl homology (DH) domain; 1.
DR Gene3D; 2.30.29.30; Pleckstrin-homology domain (PH domain)/Phosphotyrosine-binding domain (PTB); 1.
DR Gene3D; 3.30.40.10; Zinc/RING finger domain, C3HC4 (zinc finger); 1.
DR InterPro; IPR035899; DBL_dom_sf.
DR InterPro; IPR000219; DH-domain.
DR InterPro; IPR011993; PH-like_dom_sf.
DR InterPro; IPR001849; PH_domain.
DR InterPro; IPR000306; Znf_FYVE.
DR InterPro; IPR017455; Znf_FYVE-rel.
DR InterPro; IPR011011; Znf_FYVE_PHD.
DR InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR PANTHER; PTHR12673; FACIOGENITAL DYSPLASIA PROTEIN; 1.
DR PANTHER; PTHR12673:SF159; RAC GUANINE NUCLEOTIDE EXCHANGE FACTOR JJ; 1.
DR Pfam; PF01363; FYVE; 1.
DR Pfam; PF00621; RhoGEF; 1.
DR SMART; SM00064; FYVE; 1.
DR SMART; SM00233; PH; 1.
DR SMART; SM00325; RhoGEF; 1.
DR SUPFAM; SSF48065; DBL homology domain (DH-domain); 1.
DR SUPFAM; SSF57903; FYVE/PHD zinc finger; 1.
DR SUPFAM; SSF50729; PH domain-like; 1.
DR PROSITE; PS50010; DH_2; 1.
DR PROSITE; PS50003; PH_DOMAIN; 1.
DR PROSITE; PS50178; ZF_FYVE; 1.
PE 4: Predicted;
KW Coiled coil {ECO:0000256|SAM:Coils};
KW Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
KW Cytoskeleton {ECO:0000256|ARBA:ARBA00023212};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Reference proteome {ECO:0000313|Proteomes:UP000054845};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Zinc {ECO:0000256|ARBA:ARBA00022833};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW ProRule:PRU00091}.
FT DOMAIN 207..453
FT /note="DH"
FT /evidence="ECO:0000259|PROSITE:PS50010"
FT DOMAIN 483..664
FT /note="PH"
FT /evidence="ECO:0000259|PROSITE:PS50003"
FT DOMAIN 793..858
FT /note="FYVE-type"
FT /evidence="ECO:0000259|PROSITE:PS50178"
FT REGION 1..34
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 52..94
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 130..195
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 287..329
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 709..734
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 879..919
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 933..1097
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 659..686
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 303..321
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 881..902
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 958..978
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 979..995
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1021..1038
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1129 AA; 119677 MW; 9DAD678DEA7F37A0 CRC64;
MHASSVGSSS SRPSSVASNS SGHSSQGYAQ GQLAAQPSLL SPTLASALGI NVAGSSKSGR
PGSAGGASKS RNGVARPSLT ADGWSRRPSL PNVPSMINRV SMISIASFES LPEGEPVNFA
ASPLSVTSAT DAPHEDLSAS TSTATDSPTL SQGDSWQSPS SPTDEASVGS ISMNRSSSTA
SRPGHALQRS ATDPTHSMIA FEGMMRRRHA IAMELLETER VFIASLKLIN ESYYQPLMAL
SKGLTAPVGV TSAAPVLSRQ ALNEIFSNFS DILSLNSELF SRLDDRLSGR ARQPPPSRPA
SVASPTSPRD AAPSSAKAGS TNAGRLDPWH AETDTIGDTL VPIVPYLKMY SLYVKNFSAA
MARIETERKA NDAFNRFLKD TERATWGKAS ASGGFGFGLG FQAHLLTIVQ RIPRYKMMVG
DLVKYTPSNH RDYPDLLKAF GVIDQVAAYI NENVRQHEMI LVMLGLQRSL TGLTEPLIVP
GRALLKRGTL LKACRKNIQP REFFLFTDCL VYASPVGGGL ESASAAWTAL ARGGGLGVYG
GSVQDTGSPS APNSPRTIVD KLPLAPISAD AIDTASRSRT SSADAVLANG RPLSVSLQGF
QLQFRAKFPL QDCTVVGVEK ATSPFHQGLR HSIEIRTPDK SFAVYAESAE AKETWLSTIR
DARDDLMTAR RTLQAEEDTS EILRERRRSL YGRAGPSYCT PQQARRISAP STGWSFTGNT
SADTSGRPTS PLASSASVSA DWHGAFGPKS ESGNSLATLL SSGCPSSDAG ITARSRTGLR
VLEDYNAPVW VPDSSADKCI ICSEAFGMWR RKHHCRLCGQ VVCWACSQRS FLIARYEDDA
GEAEKPARAC DACYDSVFPA EEEHSSPQMG TAAVVLPEPS PAAQSDTSRS TDFSTSDSAT
PDYPATPAEH GPSNGVDSGQ ISHIAIHVQD ENEVAAEAEN EGSKPSRSAA TRPQKIWGAQ
GRPSTPSWSQ VQTSEDAGHL TSHQDRSDEP RRTTPPSRRG PALQLQRASG AGPQLFKGGL
TPQVQAATSG SGTFRLVTPR LTTPEAEMPP RSRHGAQGEG DGSTRIGDGG SYFAGAVSED
HLGDMPPPIP RARKKPLSAA ARLSTFYGVS PASMPSIAKK SPLDSPAPP
//
