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Database: UniProt
Entry: A5DFS3_PICGU
LinkDB: A5DFS3_PICGU
Original site: A5DFS3_PICGU 
ID   A5DFS3_PICGU            Unreviewed;       283 AA.
AC   A5DFS3;
DT   12-JUN-2007, integrated into UniProtKB/TrEMBL.
DT   12-JUN-2007, sequence version 1.
DT   27-MAR-2024, entry version 86.
DE   RecName: Full=t-SNARE coiled-coil homology domain-containing protein {ECO:0000259|PROSITE:PS50192};
GN   ORFNames=PGUG_02124 {ECO:0000313|EMBL:EDK38026.1};
OS   Meyerozyma guilliermondii (strain ATCC 6260 / CBS 566 / DSM 6381 / JCM 1539
OS   / NBRC 10279 / NRRL Y-324) (Yeast) (Candida guilliermondii).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Debaryomycetaceae; Meyerozyma.
OX   NCBI_TaxID=294746 {ECO:0000313|EMBL:EDK38026.1, ECO:0000313|Proteomes:UP000001997};
RN   [1] {ECO:0000313|EMBL:EDK38026.1, ECO:0000313|Proteomes:UP000001997}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 6260 / CBS 566 / DSM 6381 / JCM 1539 / NBRC 10279 / NRRL
RC   Y-324 {ECO:0000313|Proteomes:UP000001997};
RX   PubMed=19465905; DOI=10.1038/nature08064;
RA   Butler G., Rasmussen M.D., Lin M.F., Santos M.A., Sakthikumar S.,
RA   Munro C.A., Rheinbay E., Grabherr M., Forche A., Reedy J.L., Agrafioti I.,
RA   Arnaud M.B., Bates S., Brown A.J., Brunke S., Costanzo M.C.,
RA   Fitzpatrick D.A., de Groot P.W., Harris D., Hoyer L.L., Hube B., Klis F.M.,
RA   Kodira C., Lennard N., Logue M.E., Martin R., Neiman A.M., Nikolaou E.,
RA   Quail M.A., Quinn J., Santos M.C., Schmitzberger F.F., Sherlock G.,
RA   Shah P., Silverstein K.A., Skrzypek M.S., Soll D., Staggs R.,
RA   Stansfield I., Stumpf M.P., Sudbery P.E., Srikantha T., Zeng Q., Berman J.,
RA   Berriman M., Heitman J., Gow N.A., Lorenz M.C., Birren B.W., Kellis M.,
RA   Cuomo C.A.;
RT   "Evolution of pathogenicity and sexual reproduction in eight Candida
RT   genomes.";
RL   Nature 459:657-662(2009).
CC   -!- SIMILARITY: Belongs to the syntaxin family.
CC       {ECO:0000256|ARBA:ARBA00009063, ECO:0000256|RuleBase:RU003858}.
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DR   EMBL; CH408156; EDK38026.1; -; Genomic_DNA.
DR   RefSeq; XP_001486453.1; XM_001486403.1.
DR   AlphaFoldDB; A5DFS3; -.
DR   STRING; 294746.A5DFS3; -.
DR   GeneID; 5128434; -.
DR   KEGG; pgu:PGUG_02124; -.
DR   VEuPathDB; FungiDB:PGUG_02124; -.
DR   eggNOG; KOG0810; Eukaryota.
DR   HOGENOM; CLU_042423_0_1_1; -.
DR   InParanoid; A5DFS3; -.
DR   OMA; VLHASHY; -.
DR   OrthoDB; 2879355at2759; -.
DR   Proteomes; UP000001997; Unassembled WGS sequence.
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: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; IPR006012; Syntaxin/epimorphin_CS.
DR   InterPro; IPR006011; Syntaxin_N.
DR   InterPro; IPR000727; T_SNARE_dom.
DR   PANTHER; PTHR19957; SYNTAXIN; 1.
DR   PANTHER; PTHR19957:SF307; SYNTAXIN-1A; 1.
DR   Pfam; PF05739; SNARE; 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; PS00914; SYNTAXIN; 1.
DR   PROSITE; PS50192; T_SNARE; 1.
PE   3: Inferred from homology;
KW   Coiled coil {ECO:0000256|SAM:Coils}; Membrane {ECO:0000256|SAM:Phobius};
KW   Reference proteome {ECO:0000313|Proteomes:UP000001997};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        259..280
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          185..247
FT                   /note="T-SNARE coiled-coil homology"
FT                   /evidence="ECO:0000259|PROSITE:PS50192"
FT   COILED          77..104
FT                   /evidence="ECO:0000256|SAM:Coils"
SQ   SEQUENCE   283 AA;  32631 MW;  B13157094E40AC41 CRC64;
     MSNPYNSYEL QNVNKYSSSG DDDFVSFMNE IQDINNSLDQ YGNLINLISN KQRNLLQELD
     LNEEDSDYSS QQIDALISEA QSLQLDLKNR IKNVQTQAAT ARDQTKMDQA ETCRKRFLEL
     IQDYRMTEAN NREQTKVQAE RQYRIVKPEA SDAEVKAVVE DGNGQQYFQQ ALMQSNRRGE
     ARTVLNEVQI RHRELLKLER TMAELTQLFH DMEELVIEQD QPIQQIDEQI GAAQHDIEQG
     VGHTNKAVVS AKKARRKRLW CFIICLIIVI IIAVILGAYF GTK
//
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