ID J4DP19_THEOR Unreviewed; 312 AA.
AC J4DP19;
DT 31-OCT-2012, integrated into UniProtKB/TrEMBL.
DT 31-OCT-2012, sequence version 1.
DT 28-JUN-2023, entry version 35.
DE RecName: Full=t-SNARE coiled-coil homology domain-containing protein {ECO:0000259|PROSITE:PS50192};
GN ORFNames=TOT_020000210 {ECO:0000313|EMBL:BAM39939.1};
OS Theileria orientalis strain Shintoku.
OC Eukaryota; Sar; Alveolata; Apicomplexa; Aconoidasida; Piroplasmida;
OC Theileriidae; Theileria.
OX NCBI_TaxID=869250 {ECO:0000313|EMBL:BAM39939.1, ECO:0000313|Proteomes:UP000003786};
RN [1] {ECO:0000313|EMBL:BAM39939.1, ECO:0000313|Proteomes:UP000003786}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Shintoku {ECO:0000313|EMBL:BAM39939.1,
RC ECO:0000313|Proteomes:UP000003786};
RX PubMed=22951932;
RA Hayashida K., Hara Y., Abe T., Yamasaki C., Toyoda A., Kosuge T.,
RA Suzuki Y., Sato Y., Kawashima S., Katayama T., Wakaguri H., Inoue N.,
RA Homma K., Tada-Umezaki M., Yagi Y., Fujii Y., Habara T., Kanehisa M.,
RA Watanabe H., Ito K., Gojobori T., Sugawara H., Imanishi T., Weir W.,
RA Gardner M., Pain A., Shiels B., Hattori M., Nene V., Sugimoto C.;
RT "Comparative genome analysis of three eukaryotic parasites with differing
RT abilities to transform leukocytes reveals key mediators of Theileria-
RT induced leukocyte transformation.";
RL MBio 3:e00204-e00212(2012).
CC -!- SIMILARITY: Belongs to the syntaxin family.
CC {ECO:0000256|ARBA:ARBA00009063}.
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DR EMBL; AP011947; BAM39939.1; -; Genomic_DNA.
DR RefSeq; XP_009690240.1; XM_009691945.1.
DR AlphaFoldDB; J4DP19; -.
DR STRING; 869250.J4DP19; -.
DR EnsemblProtists; BAM39939; BAM39939; TOT_020000210.
DR GeneID; 20714381; -.
DR KEGG; tot:TOT_020000210; -.
DR VEuPathDB; PiroplasmaDB:TOT_020000210; -.
DR eggNOG; KOG0810; Eukaryota.
DR OrthoDB; 2879355at2759; -.
DR Proteomes; UP000003786; Chromosome 2.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
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; 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; SM00397; t_SNARE; 1.
DR SUPFAM; SSF47661; t-snare proteins; 1.
DR PROSITE; PS50192; T_SNARE; 1.
PE 3: Inferred from homology;
KW Membrane {ECO:0000256|SAM:Phobius};
KW Reference proteome {ECO:0000313|Proteomes:UP000003786};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 288..309
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 216..278
FT /note="T-SNARE coiled-coil homology"
FT /evidence="ECO:0000259|PROSITE:PS50192"
SQ SEQUENCE 312 AA; 35600 MW; C2C8844AAB3B340E CRC64;
MFNRTLQLKD VYNGVPCDFS YNREFLITTS ENKFIADSNF GVMVETTFSS DFTKFMDEIE
TIKKMIDTIE EGARSITKLM HLNTEVVTEK QRTDISTNMN ALINRTNMVC TQCKESTTSL
QKFLDKGSSS TENRMRANAY NVAVKHFRNA LKRYQTSQID YKKSITDKSK RQLHLIYPEM
DEEELDKLAN NPNAQQTVEQ IARSNFLGNV SLRDAVSNIQ GKYNDILALE QSMEQLKQMM
VELAAVVSYQ GELIDQIEHN ALKAVDYTGR ANEQLQKAQD NKKKGSKLLT WFTAIVVLVG
LGIMIPILLK IT
//