ID   A0A2T3ZM73_9HYPO        Unreviewed;      1395 AA.
AC   A0A2T3ZM73;
DT   18-JUL-2018, integrated into UniProtKB/TrEMBL.
DT   18-JUL-2018, sequence version 1.
DT   27-MAR-2024, entry version 16.
DE   RecName: Full=Exocyst complex component Sec3 PIP2-binding N-terminal domain-containing protein {ECO:0000259|SMART:SM01313};
GN   ORFNames=M441DRAFT_43882 {ECO:0000313|EMBL:PTB45904.1};
OS   Trichoderma asperellum CBS 433.97.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Hypocreomycetidae; Hypocreales; Hypocreaceae; Trichoderma.
OX   NCBI_TaxID=1042311 {ECO:0000313|EMBL:PTB45904.1, ECO:0000313|Proteomes:UP000240493};
RN   [1] {ECO:0000313|EMBL:PTB45904.1, ECO:0000313|Proteomes:UP000240493}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CBS 433.97 {ECO:0000313|EMBL:PTB45904.1,
RC   ECO:0000313|Proteomes:UP000240493};
RG   DOE Joint Genome Institute;
RA   Aerts A., Atanasova L., Chenthamara K., Zhang J., Grujic M., Henrissat B.,
RA   Kuo A., Salamov A., Lipzen A., Labutti K., Barry K., Miao Y., Rahimi M.J.,
RA   Shen Q., Grigoriev I.V., Kubicek C.P., Druzhinina I.S.;
RT   "Multiple horizontal gene transfer events from other fungi enriched the
RT   ability of initially mycotrophic Trichoderma (Ascomycota) to feed on dead
RT   plant biomass.";
RL   Submitted (JUL-2016) to the EMBL/GenBank/DDBJ databases.
CC   -!- SIMILARITY: Belongs to the SEC3 family.
CC       {ECO:0000256|ARBA:ARBA00006518}.
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DR   EMBL; KZ679257; PTB45904.1; -; Genomic_DNA.
DR   STRING; 1042311.A0A2T3ZM73; -.
DR   OrthoDB; 1547052at2759; -.
DR   Proteomes; UP000240493; 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:UP000240493};
KW   Transport {ECO:0000256|ARBA:ARBA00022448}.
FT   DOMAIN          69..166
FT                   /note="Exocyst complex component Sec3 PIP2-binding N-
FT                   terminal"
FT                   /evidence="ECO:0000259|SMART:SM01313"
FT   REGION          190..489
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          530..563
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        193..217
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        224..240
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        241..288
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        313..327
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        328..343
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        415..445
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1395 AA;  154721 MW;  7C294F0F9E42D87E CRC64;
     MDQTNVSSSS AAANRAERFE DEKRRIIESC FNKKDTDGLL QETYITHIRV TEFSSHSSMP
     PPPEARGHNA EKPRVIVVAV RKSGRVRVHK SKENSSGSFS IGKTWNLDDL SHIESYTGPK
     VPPSLRDRAG ETGFLVTLGK PYFWQAQTEK EKKFFIASLI KIYGKYTGGR LPELSGFDQK
     ELDQILGAGK RSTGASPRQQ TIDSAASQQS IAAASNTPKT GPGEVPRHPR PSPLSRPPPN
     DTMSPTGSFD STASRERSVP RWTAQNNKSQ ESISNSIATK SDDVSSLPPR SRSGMAGPSG
     LSGLGELRSV PEPTHDSVST ATRPSQESKP PPERRRPPMD PSRPQDKDLV PAPLMSSAAK
     REPVVPPPRS SDRVPPQAVP TVLQPGLAFG RAHDEGPPHI TDASDDVEQK PGNVGFNSDI
     KSSPAASLVD TNGSDQPSTN NAGAPEKTVI EPEEETRPGL GPMIKAKKNV GEAAEEETRP
     GLGPMIKAKK SKGDVAGAFW KAASAANAFR PRPGGAGERL RQIAAKANEG PDGITSVVPA
     PPRPVSRDAN LPTLELPKPP TGDLPIPEVK ILAVEPGNQA SSQELTKEAN EVEKDATIPK
     EASRHPTIVG QDARYFQKLG VDPNLLDDRG EEFGKWLDFF GWVPGSQMHS LSMDDISNDL
     ERELNTVQAG GWLARFREED ERVNTIKRGI DLAMSECEEL DNLLTLYSVE LSTLSDDIAY
     IEAQGQGLQV QTANQKLLRK ELESLLETCA ITSNDLQALQ QAPLDNPRGL EEVELSLVTL
     FRAMTKIDPS LGVDDTAKAM DTVLDADNAL GLNSNYGEMR IVQEKREMYL HESRYFMKRL
     LDFMAIQFGE AYVETKRALD GALSKKIDPA HHSVGRDLLW KYSPLMLYAR DADLENWSHL
     MQIYQDKSSP LYKHEFQHVV ALWRKNARKL TGEEAELIFS SQVEKQQEGV ATAARKLTVK
     RSQTLAKALR SPLADGGSTK VHADRNGADT RSLPYEIFSG VLDDLLPLVE MEQNFIVDFF
     HATTLEQTDF PEAVAACPPQ DRRGGDLRRH RLMEPDRELA RRVTRSMETI FAFLEAELRR
     LMEWAIAQDP LQGVGVLATL ERKLSEMGQS NQDFLNALLQ KLHVSLEGQF KKFVDEQIRA
     IEDTKVKIKK RKGVISFIRI FPAFMTAVEN MIAGVDHNQI LRRTIDREYD RILKTMFESL
     MVIAREHPAV GIAGGTADPE DKEALNFHIL LIENMNHFLE ETDTRGLDVL EGWKTQANTE
     YHEHMALYLN TVMRRPLGRL LEQIENIEAQ LQTGKSAMAI ARQPSNNKAA FNKVLGSYDS
     KEVRKGIETL RKRVEKHFGD ADDPTLSRGL VIRVLKECEE FYVGVENRIG RIITDVYSGE
     VIFEWPRADV KAAFR
//