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Database: UniProt
Entry: A0A1J9S0P6_9PEZI
LinkDB: A0A1J9S0P6_9PEZI
Original site: A0A1J9S0P6_9PEZI 
ID   A0A1J9S0P6_9PEZI        Unreviewed;       348 AA.
AC   A0A1J9S0P6;
DT   15-FEB-2017, integrated into UniProtKB/TrEMBL.
DT   15-FEB-2017, sequence version 1.
DT   27-MAR-2024, entry version 20.
DE   SubName: Full=Snare domain-containing protein {ECO:0000313|EMBL:OJD33237.1};
GN   ORFNames=BKCO1_32000112 {ECO:0000313|EMBL:OJD33237.1};
OS   Diplodia corticola.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC   Dothideomycetes incertae sedis; Botryosphaeriales; Botryosphaeriaceae;
OC   Diplodia.
OX   NCBI_TaxID=236234 {ECO:0000313|EMBL:OJD33237.1, ECO:0000313|Proteomes:UP000183809};
RN   [1] {ECO:0000313|EMBL:OJD33237.1, ECO:0000313|Proteomes:UP000183809}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CBS 112549 {ECO:0000313|EMBL:OJD33237.1,
RC   ECO:0000313|Proteomes:UP000183809};
RA   Fernandes I., De Jonge R., Van De Peer Y., Devreese B., Alves A.,
RA   Esteves A.C.;
RT   "Proteomics and genomics reveal pathogen-plant mechanisms compatible with a
RT   hemibiotrophic lifestyle of Diplodia corticola.";
RL   Submitted (OCT-2016) to the EMBL/GenBank/DDBJ databases.
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:OJD33237.1}.
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DR   EMBL; MNUE01000032; OJD33237.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1J9S0P6; -.
DR   STRING; 236234.A0A1J9S0P6; -.
DR   OrthoDB; 2879355at2759; -.
DR   Proteomes; UP000183809; Unassembled WGS sequence.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR   GO; GO:0016192; P:vesicle-mediated transport; IEA:InterPro.
DR   CDD; cd15849; SNARE_Sso1; 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:SF435; T-SNARE COILED-COIL HOMOLOGY DOMAIN-CONTAINING PROTEIN; 1.
DR   Pfam; PF00804; Syntaxin; 1.
DR   SMART; SM00503; SynN; 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:UP000183809};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        310..332
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          235..297
FT                   /note="T-SNARE coiled-coil homology"
FT                   /evidence="ECO:0000259|PROSITE:PS50192"
FT   REGION          1..73
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1..65
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   348 AA;  38878 MW;  66F7D81017BD9AC1 CRC64;
     MSYQQYSGNP YGNDGYGDSN PYGGQSTTGA GYGSSNPYGG QAPPLQHHDS SNYSQDPSYT
     EMGNLNAPPQ AAPRVLGNDE FLARVDGCKK RIRQLTSQIG EITTVHQRLL ADTAEAGAHS
     QLEHLATQTS LLNSQIKDEI KFLETDAVRS GGNVTKDSQV RNLKNSFKAE LQSYQDVEKK
     YRDRYAEQIR RQIYIVNPEA TDAEVEQALS TADGPQQIFA SALQSNRSAH ANSVLGSVRA
     RHNDLQRIEK SMEELAELFI QLNEQVVLQE PQVQRTEEQT ENVLEQGKQA HVELDKGIEH
     IKRRNRLRRW TLFVFILIIC IIALVLGLYF GLKAKNDNNN TNNTNNSA
//
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