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Database: UniProt
Entry: A0A395NUF5_TRIAR
LinkDB: A0A395NUF5_TRIAR
Original site: A0A395NUF5_TRIAR 
ID   A0A395NUF5_TRIAR        Unreviewed;       314 AA.
AC   A0A395NUF5;
DT   05-DEC-2018, integrated into UniProtKB/TrEMBL.
DT   05-DEC-2018, sequence version 1.
DT   28-JUN-2023, entry version 16.
DE   SubName: Full=Syntaxin 5 {ECO:0000313|EMBL:RFU79658.1};
GN   ORFNames=TARUN_2573 {ECO:0000313|EMBL:RFU79658.1};
OS   Trichoderma arundinaceum.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Hypocreomycetidae; Hypocreales; Hypocreaceae; Trichoderma.
OX   NCBI_TaxID=490622 {ECO:0000313|EMBL:RFU79658.1, ECO:0000313|Proteomes:UP000266272};
RN   [1] {ECO:0000313|EMBL:RFU79658.1, ECO:0000313|Proteomes:UP000266272}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=IBT 40837 {ECO:0000313|EMBL:RFU79658.1,
RC   ECO:0000313|Proteomes:UP000266272};
RX   PubMed=29649280; DOI=10.1371/journal.ppat.1006946;
RA   Proctor R.H., McCormick S.P., Kim H.S., Cardoza R.E., Stanley A.M.,
RA   Lindo L., Kelly A., Brown D.W., Lee T., Vaughan M.M., Alexander N.J.,
RA   Busman M., Gutierrez S.;
RT   "Evolution of structural diversity of trichothecenes, a family of toxins
RT   produced by plant pathogenic and entomopathogenic fungi.";
RL   PLoS Pathog. 14:e1006946-e1006946(2018).
CC   -!- SIMILARITY: Belongs to the syntaxin family.
CC       {ECO:0000256|ARBA:ARBA00009063}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:RFU79658.1}.
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DR   EMBL; PXOA01000146; RFU79658.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A395NUF5; -.
DR   STRING; 490622.A0A395NUF5; -.
DR   Proteomes; UP000266272; Unassembled WGS sequence.
DR   GO; GO:0016020; C:membrane; IEA:InterPro.
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   Reference proteome {ECO:0000313|Proteomes:UP000266272}.
FT   DOMAIN          229..291
FT                   /note="T-SNARE coiled-coil homology"
FT                   /evidence="ECO:0000259|PROSITE:PS50192"
FT   REGION          23..53
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          173..206
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        23..42
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   314 AA;  34925 MW;  0A7F7E7540C56D41 CRC64;
     MAVASIQDRT AEFKSVLAQA QRRQNANKVG AQRRSLLNDA QKSAANGDAR ARRSDFARKA
     AEIGRGISAT MGKLEKLAQL AKRRTLFDDR PVEINELTFV IKQDLSSLNQ QIGALQTMSK
     QQHPKADQEG EHNKNVVYLL QGKLTDVSVN FKDVLEARTK NIQASRSRTE NFISSVSQHA
     QPSLQQSASP LYGTPNRASP APGNDTLSLN PGPMGDQQLM MMEEANPTNA YIQQRGEAIE
     AIERTINELG GIFSQLATMV SEQSEMIERI DANTEDIVDN VEGAQRELMK YWSRVSSNRW
     LIAKMFGVLM IFFL
//
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