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Database: UniProt
Entry: A0A0J0XL03_9TREE
LinkDB: A0A0J0XL03_9TREE
Original site: A0A0J0XL03_9TREE 
ID   A0A0J0XL03_9TREE        Unreviewed;       345 AA.
AC   A0A0J0XL03;
DT   14-OCT-2015, integrated into UniProtKB/TrEMBL.
DT   14-OCT-2015, sequence version 1.
DT   27-MAR-2024, entry version 26.
DE   SubName: Full=t-SNARE {ECO:0000313|EMBL:KLT41765.1};
GN   ORFNames=CC85DRAFT_296876 {ECO:0000313|EMBL:KLT41765.1};
OS   Cutaneotrichosporon oleaginosum.
OC   Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Tremellomycetes;
OC   Trichosporonales; Trichosporonaceae; Cutaneotrichosporon.
OX   NCBI_TaxID=879819 {ECO:0000313|EMBL:KLT41765.1, ECO:0000313|Proteomes:UP000053611};
RN   [1] {ECO:0000313|EMBL:KLT41765.1, ECO:0000313|Proteomes:UP000053611}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=IBC0246 {ECO:0000313|EMBL:KLT41765.1,
RC   ECO:0000313|Proteomes:UP000053611};
RG   DOE Joint Genome Institute;
RA   Kourist R., Kracht O., Bracharz F., Lipzen A., Nolan M., Ohm R.,
RA   Grigoriev I., Sun S., Heitman J., Bruck T., Nowrousian M.;
RT   "Genomics and transcriptomics of the oil-accumulating basidiomycete yeast
RT   T. oleaginosus allow insights into substrate utilization and the diverse
RT   evolutionary trajectories of mating systems in fungi.";
RL   Submitted (MAR-2015) to the EMBL/GenBank/DDBJ databases.
CC   -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004211}; Single-
CC       pass type IV membrane protein {ECO:0000256|ARBA:ARBA00004211}.
CC   -!- SIMILARITY: Belongs to the syntaxin family.
CC       {ECO:0000256|ARBA:ARBA00009063}.
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DR   EMBL; KQ087213; KLT41765.1; -; Genomic_DNA.
DR   RefSeq; XP_018278256.1; XM_018424990.1.
DR   AlphaFoldDB; A0A0J0XL03; -.
DR   STRING; 879819.A0A0J0XL03; -.
DR   GeneID; 28985593; -.
DR   OrthoDB; 70739at2759; -.
DR   Proteomes; UP000053611; Unassembled WGS sequence.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR   GO; GO:0016192; P:vesicle-mediated transport; IEA:InterPro.
DR   CDD; cd15844; SNARE_syntaxin5; 1.
DR   Gene3D; 1.20.58.70; -; 1.
DR   InterPro; IPR010989; SNARE.
DR   InterPro; IPR045242; Syntaxin.
DR   InterPro; IPR021538; Syntaxin-5_N.
DR   InterPro; IPR000727; T_SNARE_dom.
DR   PANTHER; PTHR19957; SYNTAXIN; 1.
DR   PANTHER; PTHR19957:SF3; SYNTAXIN-5; 1.
DR   Pfam; PF05739; SNARE; 1.
DR   Pfam; PF11416; Syntaxin-5_N; 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   Reference proteome {ECO:0000313|Proteomes:UP000053611};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        324..343
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          253..315
FT                   /note="T-SNARE coiled-coil homology"
FT                   /evidence="ECO:0000259|PROSITE:PS50192"
FT   REGION          18..43
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          207..228
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   345 AA;  37719 MW;  0CBE4AD136814D4F CRC64;
     MPPRDRTAEF HSALSSIRAR TAAPAKRDPA KAPLLPAGGA SGSKSEFGRL AGNIAKDINA
     TTLKLQKLAQ LAKRKTLFDD RPIEISELTY IIRQDIASLN TQIASLQAYV RAQKAGKGRQ
     QVEEHNSNVV MMLQSRLANM GMGFKDVLEL RTQNMKASKD RTEQFMHTAS NAAVLPPAKG
     ESARVRARRG LGKHLGAPKS YSLLFASGPG AGTDDRKGKS RAPPDAGNDF LALNIDGPQG
     GDYMQTQLVE QQDNYIQSRS TAIESIESTI AELGQIFSQL ANMVAEQRET VQRIDADVTD
     ISANVSGAQR ELLKYYASIS SNRWLMLKIF GVLIIFFLVF ILVSR
//
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