ID   A0A5C3DW71_9BASI        Unreviewed;      1192 AA.
AC   A0A5C3DW71;
DT   13-NOV-2019, integrated into UniProtKB/TrEMBL.
DT   13-NOV-2019, sequence version 1.
DT   02-APR-2025, entry version 18.
DE   SubName: Full=Related to Exocyst complex component Sec3 {ECO:0000313|EMBL:SPO22585.1};
GN   ORFNames=UTRI_01263 {ECO:0000313|EMBL:SPO22585.1};
OS   Ustilago trichophora.
OC   Eukaryota; Fungi; Dikarya; Basidiomycota; Ustilaginomycotina;
OC   Ustilaginomycetes; Ustilaginales; Ustilaginaceae; Ustilago.
OX   NCBI_TaxID=86804 {ECO:0000313|EMBL:SPO22585.1, ECO:0000313|Proteomes:UP000324022};
RN   [1] {ECO:0000313|EMBL:SPO22585.1, ECO:0000313|Proteomes:UP000324022}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NBRC100155 {ECO:0000313|EMBL:SPO22585.1,
RC   ECO:0000313|Proteomes:UP000324022};
RA   Guldener U.;
RL   Submitted (MAR-2018) to the EMBL/GenBank/DDBJ databases.
CC   -!- SIMILARITY: Belongs to the SEC3 family.
CC       {ECO:0000256|ARBA:ARBA00006518}.
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DR   EMBL; OOIN01000004; SPO22585.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A5C3DW71; -.
DR   OrthoDB; 27109at2759; -.
DR   Proteomes; UP000324022; Unassembled WGS sequence.
DR   GO; GO:0000145; C:exocyst; IEA:InterPro.
DR   GO; GO:0005886; C:plasma membrane; IEA:TreeGrafter.
DR   GO; GO:0005546; F:phosphatidylinositol-4,5-bisphosphate binding; IEA:TreeGrafter.
DR   GO; GO:0006887; P:exocytosis; IEA:UniProtKB-KW.
DR   GO; GO:0006893; P:Golgi to plasma membrane transport; IEA:TreeGrafter.
DR   Gene3D; 2.30.29.90; -; 1.
DR   InterPro; IPR028258; Sec3-PIP2_bind.
DR   InterPro; IPR048628; Sec3_C.
DR   InterPro; IPR019160; Sec3_CC.
DR   PANTHER; PTHR16092:SF14; EXOCYST COMPLEX COMPONENT 1 ISOFORM X1; 1.
DR   PANTHER; PTHR16092; SEC3/SYNTAXIN-RELATED; 1.
DR   Pfam; PF15277; Sec3-PIP2_bind; 1.
DR   Pfam; PF20654; Sec3_C-term; 1.
DR   Pfam; PF09763; Sec3_CC; 1.
DR   SMART; SM01313; Sec3-PIP2_bind; 1.
PE   3: Inferred from homology;
KW   Coiled coil {ECO:0000256|ARBA:ARBA00023054};
KW   Exocytosis {ECO:0000256|ARBA:ARBA00022483};
KW   Reference proteome {ECO:0000313|Proteomes:UP000324022};
KW   Transport {ECO:0000256|ARBA:ARBA00022448}.
FT   DOMAIN          66..151
FT                   /note="Exocyst complex component Sec3 PIP2-binding N-
FT                   terminal"
FT                   /evidence="ECO:0000259|SMART:SM01313"
FT   REGION          1..21
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          171..338
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          373..436
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        190..201
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        202..213
FT                   /note="Low complexity"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        214..232
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        243..256
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        277..295
FT                   /note="Low complexity"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        296..305
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        327..337
FT                   /note="Gly residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        373..382
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        415..429
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1192 AA;  129362 MW;  01AEED156E1373DE CRC64;
     MSAQLNINGG GGGGAATASS APNKTKDLFN AALQARNPHN AYIAHLKIWE ELAQEGGAEA
     AASSGATKKA RYLILAVQKD TGKVTINKAK RNANGSFSIG KDWDLNTLRE VHVMQPDVFS
     ITLTRPYQWQ TQQPIEQQLF LQSLVKVYRK YTQDDGPRLV GIDVPLSSTT IPPAIADSAN
     LSDRPGSGYR SDNSLAGSSN GTAIPPATAA PAIKTSSLPS SRLDSGASPT RSPSRDGIPA
     NSREMNGSQS TTTSPSKSRR EGGLQPSPLS RPVQLPSRSS AESQRSAASE TASAQPRQPS
     GSTTLAVPRQ APPRKHSGDS LSIKSGSSGG LAGGGGDARA RLSSIEPIRG GAAYERMLLA
     GTGLAGVTEV DDDEAADEED DPYGGAVLTD KDPAPHASFN SKRATLGRPA IARLETSKTH
     NSDRTKTGDE MDEDEDENST LVAVEEMLEG LEWRNASSKG YGTASGKGTA DMIEARLLDE
     LSALESANIH AIIESDDRVA LVVKHMEEAL ADLDMMDSMI AGFKVQLNAR ADDISHIESQ
     NRGLQVQTSN QRTLMSEIEN LINTINVDED AIHALSAGRL ENPDGVAQLE LAAASLYKSM
     LQARRDGDGG GADMAAAAER LADHEAISSR FCKRVLDYLN VTFNAEAQRL LSDPARQKAL
     QPPHPSLPDH APMEEALGQY CGLLLYMKEV SSATFSRVSA AYFASASECY RTEMQQLFVA
     YRKQLRKASD EDMNDSSFVG PSSTSAGTAI RSGTIRRVQR EKTIRVGRDR GEISGQDGLQ
     RILSSIFPVL LREQSFISDL LHINDNNITF ADYMDLEPYF RRRAAGMFTS SAGPLREMKG
     AMDLIFGFVA PELQAFTDDA LSKDRMSIVG LLATLDRGII EADEVNCESL QRVLAKLHLR
     LASQLERFVQ EQIKGIEQTK LTVKKRKGVV HFMRIFPVFV DRVESQLVNA ETLNIRNAVD
     GYYEQICRAM FDALQTISRV ETAGVSGDED KGQLNHLVIL IENMYYFISE INKASRQRGN
     SALAGLVKRA ESIYGDSLGS YTQFVLRRSL AKMMDFGDGI DALLRSTPAI EVSLHSAYSK
     SSFKKLVKDF TAKDTRKAVE ALSKRVAKHF DDDDVPSLAT TGPVQATANG EGEQGEVEVL
     SRVWSSCEEG YMREFERVNR IGKECYPDVG ASLELGPNEL RRLFTSLAPK RR
//