ID A0A1Y2B659_9TREE Unreviewed; 308 AA.
AC A0A1Y2B659;
DT 30-AUG-2017, integrated into UniProtKB/TrEMBL.
DT 30-AUG-2017, sequence version 1.
DT 27-MAR-2024, entry version 17.
DE SubName: Full=t-SNARE {ECO:0000313|EMBL:ORY30214.1};
GN ORFNames=BCR39DRAFT_529992 {ECO:0000313|EMBL:ORY30214.1};
OS Naematelia encephala.
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Tremellomycetes;
OC Tremellales; Naemateliaceae; Naematelia.
OX NCBI_TaxID=71784 {ECO:0000313|EMBL:ORY30214.1, ECO:0000313|Proteomes:UP000193986};
RN [1] {ECO:0000313|EMBL:ORY30214.1, ECO:0000313|Proteomes:UP000193986}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=68-887.2 {ECO:0000313|EMBL:ORY30214.1,
RC ECO:0000313|Proteomes:UP000193986};
RG DOE Joint Genome Institute;
RA Mondo S.J., Dannebaum R.O., Kuo R.C., Labutti K., Haridas S., Kuo A.,
RA Salamov A., Ahrendt S.R., Lipzen A., Sullivan W., Andreopoulos W.B.,
RA Clum A., Lindquist E., Daum C., Ramamoorthy G.K., Gryganskyi A., Culley D.,
RA Magnuson J.K., James T.Y., O'Malley M.A., Stajich J.E., Spatafora J.W.,
RA Visel A., Grigoriev I.V.;
RT "Pervasive Adenine N6-methylation of Active Genes in Fungi.";
RL Submitted (JUL-2016) 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}.
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:ORY30214.1}.
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DR EMBL; MCFC01000021; ORY30214.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1Y2B659; -.
DR STRING; 71784.A0A1Y2B659; -.
DR InParanoid; A0A1Y2B659; -.
DR OrthoDB; 70739at2759; -.
DR Proteomes; UP000193986; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:InterPro.
DR GO; GO:0016192; P:vesicle-mediated transport; IEA:InterPro.
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; 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:UP000193986}.
FT DOMAIN 258..308
FT /note="T-SNARE coiled-coil homology"
FT /evidence="ECO:0000259|PROSITE:PS50192"
FT REGION 1..53
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 8..22
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 23..37
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 308 AA; 33271 MW; E287CCBAF44A6A36 CRC64;
MPPKDRTSEF HSTLNSIKSR TALPSKGKER DESKQRLLPS APGKAAGGAD AKKSEFGRMA
GQIARDINGT TMKLQKLAQL AKRKTLFDDR PIEISELTYI IRQDIASLNT QIASLQSFIR
AQKPSGSGKG QVEEHNSNVV MLLQSRLAEM GMGFKDVLEL RTQNMKASKD RSEQFMHTAS
SAVVPPPAGN SLLFSQSQTG GPGSGFPPDR KGKARAIPDT NGNGDSKDFL ALDIDGDRGE
SGVGIGGYQQ MQLVDQQDTY IQSRSTAIES IESTIAELGQ IFSQLAGMVA EQRETVQRID
ADTTDIAA
//