ID A0A0D2AMH9_9EURO Unreviewed; 1516 AA.
AC A0A0D2AMH9;
DT 29-APR-2015, integrated into UniProtKB/TrEMBL.
DT 29-APR-2015, sequence version 1.
DT 27-MAR-2024, entry version 33.
DE RecName: Full=Exocyst complex component Sec3 PIP2-binding N-terminal domain-containing protein {ECO:0000259|SMART:SM01313};
GN ORFNames=PV06_06729 {ECO:0000313|EMBL:KIW41146.1};
OS Exophiala oligosperma.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Chaetothyriomycetidae; Chaetothyriales; Herpotrichiellaceae; Exophiala.
OX NCBI_TaxID=215243 {ECO:0000313|EMBL:KIW41146.1, ECO:0000313|Proteomes:UP000053342};
RN [1] {ECO:0000313|EMBL:KIW41146.1, ECO:0000313|Proteomes:UP000053342}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 72588 {ECO:0000313|EMBL:KIW41146.1,
RC ECO:0000313|Proteomes:UP000053342};
RG The Broad Institute Genomics Platform;
RA Cuomo C., de Hoog S., Gorbushina A., Stielow B., Teixiera M.,
RA Abouelleil A., Chapman S.B., Priest M., Young S.K., Wortman J., Nusbaum C.,
RA Birren B.;
RT "The Genome Sequence of Exophiala oligosperma CBS72588.";
RL Submitted (JAN-2015) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the SEC3 family.
CC {ECO:0000256|ARBA:ARBA00006518}.
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DR EMBL; KN847337; KIW41146.1; -; Genomic_DNA.
DR RefSeq; XP_016261362.1; XM_016407882.1.
DR STRING; 215243.A0A0D2AMH9; -.
DR GeneID; 27358803; -.
DR VEuPathDB; FungiDB:PV06_06729; -.
DR HOGENOM; CLU_002075_1_0_1; -.
DR OrthoDB; 1547052at2759; -.
DR Proteomes; UP000053342; Unassembled WGS sequence.
DR GO; GO:0000145; C:exocyst; IEA:InterPro.
DR GO; GO:0006887; P:exocytosis; IEA:UniProtKB-KW.
DR CDD; cd13315; PH_Sec3; 1.
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:UP000053342};
KW Transport {ECO:0000256|ARBA:ARBA00022448}.
FT DOMAIN 100..201
FT /note="Exocyst complex component Sec3 PIP2-binding N-
FT terminal"
FT /evidence="ECO:0000259|SMART:SM01313"
FT REGION 1..55
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 218..575
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 588..712
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..44
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 241..267
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 314..332
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 343..374
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 452..466
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 472..487
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 521..542
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 551..567
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 662..676
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1516 AA; 168782 MW; 1BB695C9E88E2ECE CRC64;
MNQLQYQSGH RQQQQPPPSL SNGARNGSLG SASGVKQPEP LETNQSRAAR FEDEKRRIVE
SCFNKRDQDG MQVESYITHV RILEDASYPS SPPPPESPAA NKKNRVILVA VRRSGKVRVH
KARENPNGTF SIGKTWNLDE LNAILSYSSL VPATPQQQME KQWASNTGFT ITLGKPYFWS
APTPKEKDFF IASLIKIYRK YTGGKVPDLI GFSPQDAAQL IGNPAPQSAP PPRGAGTFSP
AAPSDRSTPP AQPPSVAALN ANRPQSPYTA HHPPPSRDGN RIVSQEQERA YSRQDQPQMA
RDGPVPPPQF DNRAPSRQER STPVQDLPRN QPPSAQYRRD DGRAPSLTNN MQSTPPRPSL
SPKTSKTSLS RNEPGLEPQP LRTNGVGAAI MPAGLDFAGK RLGPKASQDS FRNAGGNSGI
GSPRPSIAPA DRRAPSESRP DVPAFVEPLP ERKRPVAPPP EPVADQLGPP SQDGDTFVTP
MGTPTNLKEE ESQKRAPDYF AARQPQKESQ PDEPKPALLS NATHEPSSQD APPSQITNER
VTAEPAETVP PPPKVEEEHR PGLGPMIKKK SGKDIANQFR RAALAAQAFQ PRQGGAGARL
KALQEKEKQS NEPDGITSVV PAPLQRGMSG DSARTGTPDL TTPSVEKELP VVKPNDAIPK
VQIERTATSD SVARPQTPVQ KPIPVTETPE KQARGESPDK ARSRSPQRRR RLKLEAEVEK
YCSTLGVDPR IMDGRGADFN ELLTEFGWEG KLADEEKVED FETSIRREIG RAQASGWLGH
VEQQETKVQE LAKAFEKAIA ECEELDGLLT LYAHELDTLH DDIEYIEAQG QGLQVQTANQ
KLLQSELESL LKNLTISSGD LRALRAAPID SYDGLQAIEG SLALLYRAML TIDPEIRQNK
LRQADASTGR VGVGQFADAE IGQMRAVQQK KDEYKEESTV FLNRLNQHMK AMFQMAEQRT
SEENATASIS SGTSTNLNLR AYGASRQDLW MYNTMMLFVR EVNQYEWQTL ISSYEINVKS
IYQSQFRDYS MSLKKTARKP TGEEQEILFT HQEKEKAEES LTSTAARKLT VKRGRTVKTS
ALRQSIGGER RDGRPEAWTI FDTVLEQQAT AISEEQNFIV HFFHLDSQSN TDFAEIVQSR
SPDQRKVPNL QAKQSYDPDR NMAKIVQNTV GGIYSFWEMD LQNLITWVLK MDEIQGVGVL
VSLEQCLAKY EETNQEFITR TVRILHERLT GKFHAFVEQQ VKAIEETKVK VKKRKGLISF
MRVFPEFTAA VEDMIPQEFT LDSLDVRFTV NDAYTRLLKA MWESLNFIAK DNPAGASGPT
SANAPTSGDP EDKEALNYHI LLIENMNYFV EEVKTHNNGV LDEWVERAGQ DQVSHLGQYT
DAVIRRPLGK WLDFLESTEA MMKNISSGDY ASIASKPSHS RSSAKKILGV YDMKEVRKGV
ETLKKRIEKH FSDADEGGLG ASTSSLSRGL IGRVCEECAT RYAHAWDRMR VVIDRVYEGG
LEIEWRKEDV QMMFRR
//
