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Database: UniProt
Entry: R9PBU3_PSEHS
LinkDB: R9PBU3_PSEHS
Original site: R9PBU3_PSEHS 
ID   R9PBU3_PSEHS            Unreviewed;       310 AA.
AC   R9PBU3;
DT   24-JUL-2013, integrated into UniProtKB/TrEMBL.
DT   24-JUL-2013, sequence version 1.
DT   27-MAR-2024, entry version 41.
DE   RecName: Full=t-SNARE coiled-coil homology domain-containing protein {ECO:0000259|PROSITE:PS50192};
GN   ORFNames=PHSY_006306 {ECO:0000313|EMBL:GAC98712.1};
OS   Pseudozyma hubeiensis (strain SY62) (Yeast).
OC   Eukaryota; Fungi; Dikarya; Basidiomycota; Ustilaginomycotina;
OC   Ustilaginomycetes; Ustilaginales; Ustilaginaceae; Pseudozyma.
OX   NCBI_TaxID=1305764 {ECO:0000313|EMBL:GAC98712.1, ECO:0000313|Proteomes:UP000014071};
RN   [1] {ECO:0000313|Proteomes:UP000014071}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SY62 {ECO:0000313|Proteomes:UP000014071};
RX   PubMed=23814110; DOI=10.1128/genomea.00409-13;
RA   Konishi M., Hatada Y., Horiuchi J.;
RT   "Draft genome sequence of the basidiomycetous yeast-like fungus Pseudozyma
RT   hubeiensis SY62, which produces an abundant amount of the biosurfactant
RT   mannosylerythritol lipids.";
RL   Genome Announc. 1:E0040913-E0040913(2013).
CC   -!- SIMILARITY: Belongs to the syntaxin family.
CC       {ECO:0000256|ARBA:ARBA00009063}.
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DR   EMBL; DF238821; GAC98712.1; -; Genomic_DNA.
DR   RefSeq; XP_012192299.1; XM_012336909.1.
DR   AlphaFoldDB; R9PBU3; -.
DR   STRING; 1305764.R9PBU3; -.
DR   GeneID; 24111578; -.
DR   eggNOG; KOG0811; Eukaryota.
DR   HOGENOM; CLU_059257_2_0_1; -.
DR   OrthoDB; 2049889at2759; -.
DR   Proteomes; UP000014071; 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; cd15840; SNARE_Qa; 1.
DR   Gene3D; 1.20.5.110; -; 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:SF38; LD27581P; 1.
DR   PANTHER; PTHR19957; SYNTAXIN; 1.
DR   Pfam; PF05739; SNARE; 1.
DR   Pfam; PF14523; Syntaxin_2; 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:UP000014071};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        290..309
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          217..279
FT                   /note="T-SNARE coiled-coil homology"
FT                   /evidence="ECO:0000259|PROSITE:PS50192"
FT   REGION          1..39
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          156..193
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1..24
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   310 AA;  33773 MW;  6DFD993A6D6D2FA3 CRC64;
     MSFNDLERGS SSRQGGSGSG GGGSGSRKTP LPLYRDEVSS SLPPEFEKLT SKIGIQIFKI
     QSNVTAIQKL ISLSSSNSSA KAASQDWSKR INDLIETTRE LVKDATTDIK QLSTFPLGPA
     NGGAKLTQGK LQRDFQAAAL QFQRVQKEAV AKTRAKLEQD KQKERQMLKS RNSQQLLIDT
     EESDRAGAPG GAEGALQAEE LDLLPEGPTQ ADLEYQESLI TSREAEIREI ESGVQELNEI
     FRDLGNIVQE QGGMIDNIEF NINSIADNTA GADRELVVAH EYQRRAGRRC ICLLLVVGFV
     VAIVLLAILN
//
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