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Database: UniProt
Entry: A0A1V9ZAA5_9STRA
LinkDB: A0A1V9ZAA5_9STRA
Original site: A0A1V9ZAA5_9STRA 
ID   A0A1V9ZAA5_9STRA        Unreviewed;       285 AA.
AC   A0A1V9ZAA5;
DT   07-JUN-2017, integrated into UniProtKB/TrEMBL.
DT   07-JUN-2017, sequence version 1.
DT   28-JUN-2023, entry version 17.
DE   SubName: Full=Syntaxin {ECO:0000313|EMBL:OQR94857.1};
GN   ORFNames=ACHHYP_00859 {ECO:0000313|EMBL:OQR94857.1};
OS   Achlya hypogyna.
OC   Eukaryota; Sar; Stramenopiles; Oomycota; Saprolegniales; Saprolegniaceae;
OC   Achlya.
OX   NCBI_TaxID=1202772 {ECO:0000313|EMBL:OQR94857.1, ECO:0000313|Proteomes:UP000243579};
RN   [1] {ECO:0000313|EMBL:OQR94857.1, ECO:0000313|Proteomes:UP000243579}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 48635 {ECO:0000313|EMBL:OQR94857.1,
RC   ECO:0000313|Proteomes:UP000243579};
RX   PubMed=25527045; DOI=10.1093/gbe/evu276;
RA   Misner I., Blouin N., Leonard G., Richards T.A., Lane C.E.;
RT   "The secreted proteins of Achlya hypogyna and Thraustotheca clavata
RT   identify the ancestral oomycete secretome and reveal gene acquisitions by
RT   horizontal gene transfer.";
RL   Genome Biol. Evol. 7:120-135(2014).
CC   -!- SIMILARITY: Belongs to the syntaxin family.
CC       {ECO:0000256|ARBA:ARBA00009063, ECO:0000256|RuleBase:RU003858}.
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:OQR94857.1}.
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DR   EMBL; JNBR01000349; OQR94857.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1V9ZAA5; -.
DR   STRING; 1202772.A0A1V9ZAA5; -.
DR   OrthoDB; 2879355at2759; -.
DR   Proteomes; UP000243579; Unassembled WGS sequence.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
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; cd15848; SNARE_syntaxin1-like; 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; 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   Membrane {ECO:0000256|SAM:Phobius};
KW   Reference proteome {ECO:0000313|Proteomes:UP000243579};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        264..284
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          190..252
FT                   /note="T-SNARE coiled-coil homology"
FT                   /evidence="ECO:0000259|PROSITE:PS50192"
SQ   SEQUENCE   285 AA;  31927 MW;  48B6EF4DBCE25B23 CRC64;
     MNDRLAELTG KSSEVTIDIS EFMEKFFVDV EDMQADLGKI VLATDRISEL NHQALLATAA
     GEEQTISQEL CLVIDATNKI AAHAKGMLEL IKKESAEKKK DKTVAASEIR IRDNMSTTLT
     RKFMDTMKEY QKAQQKFKAD MKNKVKRQVQ IVKPDASEQE IDMVMRSADP GAIYRSAILQ
     GSAESIKEVY MNCHDKYQDV LKLEQSVAEL HQMFLDLALL VEQQGEMLDH IEFQVKAASN
     YIEAGNKEVT KAIKTQKSMR KKQCCLLVFG LVIVLIAVAA AGGFK
//
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