ID J7SBS0_NAUDC Unreviewed; 407 AA.
AC J7SBS0;
DT 31-OCT-2012, integrated into UniProtKB/TrEMBL.
DT 31-OCT-2012, sequence version 1.
DT 27-MAR-2024, entry version 61.
DE RecName: Full=t-SNARE coiled-coil homology domain-containing protein {ECO:0000259|PROSITE:PS50192};
GN Name=NDAI0G05320 {ECO:0000313|EMBL:CCK73515.1};
GN OrderedLocusNames=NDAI_0G05320 {ECO:0000313|EMBL:CCK73515.1};
OS Naumovozyma dairenensis (strain ATCC 10597 / BCRC 20456 / CBS 421 / NBRC
OS 0211 / NRRL Y-12639) (Saccharomyces dairenensis).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Naumovozyma.
OX NCBI_TaxID=1071378 {ECO:0000313|EMBL:CCK73515.1, ECO:0000313|Proteomes:UP000000689};
RN [1] {ECO:0000313|EMBL:CCK73515.1, ECO:0000313|Proteomes:UP000000689}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 10597 / BCRC 20456 / CBS 421 / NBRC 0211 / NRRL Y-12639
RC {ECO:0000313|Proteomes:UP000000689};
RX PubMed=22123960; DOI=10.1073/pnas.1112808108;
RA Gordon J.L., Armisen D., Proux-Wera E., OhEigeartaigh S.S., Byrne K.P.,
RA Wolfe K.H.;
RT "Evolutionary erosion of yeast sex chromosomes by mating-type switching
RT accidents.";
RL Proc. Natl. Acad. Sci. U.S.A. 108:20024-20029(2011).
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; HE580273; CCK73515.1; -; Genomic_DNA.
DR RefSeq; XP_003980191.1; XM_003980142.1.
DR AlphaFoldDB; J7SBS0; -.
DR STRING; 1071378.J7SBS0; -.
DR GeneID; 13926987; -.
DR KEGG; ndi:NDAI_0G05320; -.
DR eggNOG; KOG0809; Eukaryota.
DR HOGENOM; CLU_038177_0_1_1; -.
DR OMA; NRKMCII; -.
DR OrthoDB; 2876074at2759; -.
DR Proteomes; UP000000689; Chromosome 7.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005484; F:SNAP receptor activity; IEA:InterPro.
DR GO; GO:0006886; P:intracellular protein transport; IEA:InterPro.
DR GO; GO:0006996; P:organelle organization; IEA:UniProt.
DR GO; GO:0016192; P:vesicle-mediated transport; IEA:InterPro.
DR CDD; cd15845; SNARE_syntaxin16; 1.
DR Gene3D; 1.20.58.70; -; 1.
DR InterPro; IPR010989; SNARE.
DR InterPro; IPR045242; Syntaxin.
DR InterPro; IPR006012; Syntaxin/epimorphin_CS.
DR InterPro; IPR000727; T_SNARE_dom.
DR PANTHER; PTHR19957; SYNTAXIN; 1.
DR PANTHER; PTHR19957:SF83; SYNTAXIN-16; 1.
DR Pfam; PF05739; SNARE; 1.
DR SMART; SM00397; t_SNARE; 1.
DR SUPFAM; SSF47661; t-snare proteins; 1.
DR PROSITE; PS00914; SYNTAXIN; 1.
DR PROSITE; PS50192; T_SNARE; 1.
PE 3: Inferred from homology;
KW Membrane {ECO:0000256|SAM:Phobius};
KW Reference proteome {ECO:0000313|Proteomes:UP000000689};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 316..333
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 242..304
FT /note="T-SNARE coiled-coil homology"
FT /evidence="ECO:0000259|PROSITE:PS50192"
FT REGION 339..389
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 347..365
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 407 AA; 46697 MW; 1FF245CEF671A48F CRC64;
MFRDRTNLFL SYRRTFPHNV QYSTIGLGIN IHNDGVFDKD LEAYPMMDLS PHDNDDKNIL
KSQPPLFVEM AHDIDGYLSD VKTLMIKLTK LYKKNSLPGF EDKTGDEKLI EDLSYKVIQN
FQKCYNVTKK LETIFNSQML NGKQMNKGEL VILDNILKMY AQKIQTESNK FKVLQNNYLK
FLNKDDLKPI LPKNSKETSQ LLLLEEEEGN QNDGGVAGQA QRQDDIDAYS RKTLQRQMDS
SQQYLQERDE EITQLARGVL EVSTIFREMQ SLIIDQGTVV DRIDYNLENT VIELKEANKE
LGQATVYQKR TQKCKVILLL TLCVIALFFF VMLRPRSSGG GTRSPEADGH SDSDISEKPN
PDEEESPELV DIGIDESPAA LQQEHPNNMK LRLIKRGQNS SLIQQFQ
//
