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Database: UniProt
Entry: A0A150UWG3_9PEZI
LinkDB: A0A150UWG3_9PEZI
Original site: A0A150UWG3_9PEZI 
ID   A0A150UWG3_9PEZI        Unreviewed;       373 AA.
AC   A0A150UWG3;
DT   08-JUN-2016, integrated into UniProtKB/TrEMBL.
DT   08-JUN-2016, sequence version 1.
DT   28-JUN-2023, entry version 19.
DE   RecName: Full=t-SNARE coiled-coil homology domain-containing protein {ECO:0000259|PROSITE:PS50192};
GN   ORFNames=M433DRAFT_73775 {ECO:0000313|EMBL:KYG42435.1};
OS   Acidomyces richmondensis BFW.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC   Dothideomycetidae; Mycosphaerellales; Teratosphaeriaceae; Acidomyces.
OX   NCBI_TaxID=766039 {ECO:0000313|EMBL:KYG42435.1, ECO:0000313|Proteomes:UP000075602};
RN   [1] {ECO:0000313|EMBL:KYG42435.1, ECO:0000313|Proteomes:UP000075602}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=BFW {ECO:0000313|EMBL:KYG42435.1,
RC   ECO:0000313|Proteomes:UP000075602};
RX   PubMed=26973616; DOI=10.3389/fmicb.2016.00238;
RA   Mosier A.C., Miller C.S., Frischkorn K.R., Ohm R.A., Li Z., LaButti K.,
RA   Lapidus A., Lipzen A., Chen C., Johnson J., Lindquist E.A., Pan C.,
RA   Hettich R.L., Grigoriev I.V., Singer S.W., Banfield J.F.;
RT   "Fungi Contribute Critical but Spatially Varying Roles in Nitrogen and
RT   Carbon Cycling in Acid Mine Drainage.";
RL   Front. Microbiol. 7:238-238(2016).
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:KYG42435.1}.
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DR   EMBL; JPDO01000457; KYG42435.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A150UWG3; -.
DR   STRING; 766039.A0A150UWG3; -.
DR   Proteomes; UP000075602; 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:SF307; SYNTAXIN-1A; 1.
DR   Pfam; PF05739; SNARE; 1.
DR   Pfam; PF00804; Syntaxin; 1.
DR   SMART; SM00503; SynN; 1.
DR   SUPFAM; SSF47661; t-snare proteins; 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:UP000075602};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        308..331
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          234..296
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   COILED          163..190
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COMPBIAS        1..49
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   373 AA;  41076 MW;  EB51D1DF9A70F8AF CRC64;
     MSYNQYSGYG GNPYGEQQYG GSNPYTNDGG NPYGGDSTYS QSNYSQPTAG PGAPVGPGQP
     GQGDRIQYVS PGPSVLSNQD FLSRVEAVKA DIRTLTTHVG QIAVLHQRTL SSPDSSSSDQ
     LEAMITQTQI LNTSIKDQIK FLETDAARSK NNQVKNTQVS QLKSSFQKQL QEYRVEEANY
     EKRYREQIAR QYRIVNPDAT DAEVQEATQA DWGNEGVFQT ALKTNRSATA TTVLGAVRAR
     HNDIQKIERT LIELNQLMED LATAIVLQEE PIQQIEQQTE NVKKDTEAGN VQLDKGIKSA
     RNARRLKWWC FGICVAIVII LGLVLGLYFG LPSSPGHPKA KAKRAILVSG PQSPAIGYGR
     IWSRWQLDGT AHV
//
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