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Database: UniProt
Entry: A0A2V5ITQ3_9EURO
LinkDB: A0A2V5ITQ3_9EURO
Original site: A0A2V5ITQ3_9EURO 
ID   A0A2V5ITQ3_9EURO        Unreviewed;       306 AA.
AC   A0A2V5ITQ3;
DT   12-SEP-2018, integrated into UniProtKB/TrEMBL.
DT   12-SEP-2018, sequence version 1.
DT   27-MAR-2024, entry version 14.
DE   SubName: Full=t-SNARE {ECO:0000313|EMBL:PYI27367.1};
GN   ORFNames=BP00DRAFT_22513 {ECO:0000313|EMBL:PYI27367.1};
OS   Aspergillus indologenus CBS 114.80.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus.
OX   NCBI_TaxID=1450541 {ECO:0000313|EMBL:PYI27367.1, ECO:0000313|Proteomes:UP000248817};
RN   [1] {ECO:0000313|EMBL:PYI27367.1, ECO:0000313|Proteomes:UP000248817}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CBS 114.80 {ECO:0000313|EMBL:PYI27367.1,
RC   ECO:0000313|Proteomes:UP000248817};
RG   DOE Joint Genome Institute;
RA   Vesth T.C., Nybo J., Theobald S., Brandl J., Frisvad J.C., Nielsen K.F.,
RA   Lyhne E.K., Kogle M.E., Kuo A., Riley R., Clum A., Nolan M., Lipzen A.,
RA   Salamov A., Henrissat B., Wiebenga A., De vries R.P., Grigoriev I.V.,
RA   Mortensen U.H., Andersen M.R., Baker S.E.;
RT   "The genomes of Aspergillus section Nigri reveals drivers in fungal
RT   speciation.";
RL   Submitted (FEB-2018) to the EMBL/GenBank/DDBJ databases.
CC   -!- SIMILARITY: Belongs to the syntaxin family.
CC       {ECO:0000256|ARBA:ARBA00009063}.
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DR   EMBL; KZ825571; PYI27367.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A2V5ITQ3; -.
DR   Proteomes; UP000248817; Unassembled WGS sequence.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR   GO; GO:0016192; P:vesicle-mediated transport; IEA:InterPro.
DR   Gene3D; 1.20.5.110; -; 1.
DR   Gene3D; 1.20.58.70; -; 1.
DR   InterPro; IPR010989; SNARE.
DR   InterPro; IPR045242; Syntaxin.
DR   InterPro; IPR006011; Syntaxin_N.
DR   InterPro; IPR000727; T_SNARE_dom.
DR   PANTHER; PTHR19957; SYNTAXIN; 1.
DR   PANTHER; PTHR19957:SF307; SYNTAXIN-1A; 1.
DR   Pfam; PF05739; SNARE; 1.
DR   Pfam; PF00804; Syntaxin; 1.
DR   SMART; SM00397; t_SNARE; 1.
DR   SUPFAM; SSF47661; t-snare proteins; 1.
DR   PROSITE; PS50192; T_SNARE; 1.
PE   3: Inferred from homology;
KW   Membrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        280..300
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          206..268
FT                   /note="T-SNARE coiled-coil homology"
FT                   /evidence="ECO:0000259|PROSITE:PS50192"
FT   REGION          1..28
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        11..28
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   306 AA;  34254 MW;  FACECF5E94FAAFDA CRC64;
     MSGGYGQYNP YGEQGYNQNP YDQANAVEQG QGNGTYEMNA IAEQPADATT LLNKCREIND
     GIADLKAKRE GQLAAAQNAM LDSSTGKEDQ VARQTLDYIE DEINNGFRYL RDLLKKIKQT
     PGSGDNRVQT QVDVTSRNLR REIEQYQRCQ SDFQKRLREQ VRRRYEIANP EATPEEIEQG
     VDSVLMGQEQ SFQVTGSRTR QANDARQAAL ERSAAIRKIE QDMIELGRLY QEVAELVHMQ
     EPAVEQISQD AENVAGNVAN ANTQITEAIA SARRARKWKW YALLVVILII AIVVGVAVGV
     TEANKK
//
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