ID G1X299_ARTOA Unreviewed; 243 AA.
AC G1X299;
DT 16-NOV-2011, integrated into UniProtKB/TrEMBL.
DT 16-NOV-2011, sequence version 1.
DT 27-MAR-2024, entry version 45.
DE RecName: Full=t-SNARE coiled-coil homology domain-containing protein {ECO:0000259|PROSITE:PS50192};
GN ORFNames=AOL_s00007g408 {ECO:0000313|EMBL:EGX52625.1};
OS Arthrobotrys oligospora (strain ATCC 24927 / CBS 115.81 / DSM 1491)
OS (Nematode-trapping fungus) (Didymozoophaga oligospora).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Orbiliomycetes;
OC Orbiliales; Orbiliaceae; Orbilia; Orbilia oligospora.
OX NCBI_TaxID=756982 {ECO:0000313|EMBL:EGX52625.1, ECO:0000313|Proteomes:UP000008784};
RN [1] {ECO:0000313|EMBL:EGX52625.1, ECO:0000313|Proteomes:UP000008784}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 24927 / CBS 115.81 / DSM 1491
RC {ECO:0000313|Proteomes:UP000008784};
RX PubMed=21909256; DOI=10.1371/journal.ppat.1002179;
RA Yang J., Wang L., Ji X., Feng Y., Li X., Zou C., Xu J., Ren Y., Mi Q.,
RA Wu J., Liu S., Liu Y., Huang X., Wang H., Niu X., Li J., Liang L., Luo Y.,
RA Ji K., Zhou W., Yu Z., Li G., Liu Y., Li L., Qiao M., Feng L., Zhang K.-Q.;
RT "Genomic and proteomic analyses of the fungus Arthrobotrys oligospora
RT provide insights into nematode-trap formation.";
RL PLoS Pathog. 7:E1002179-E1002179(2011).
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004211}; Single-
CC pass type IV membrane protein {ECO:0000256|ARBA:ARBA00004211}.
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:EGX52625.1}.
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DR EMBL; ADOT01000017; EGX52625.1; -; Genomic_DNA.
DR RefSeq; XP_011118611.1; XM_011120309.1.
DR AlphaFoldDB; G1X299; -.
DR STRING; 756982.G1X299; -.
DR GeneID; 22889532; -.
DR eggNOG; KOG3202; Eukaryota.
DR HOGENOM; CLU_061883_0_0_1; -.
DR InParanoid; G1X299; -.
DR OMA; EHDPYRF; -.
DR OrthoDB; 2729919at2759; -.
DR Proteomes; UP000008784; Unassembled WGS sequence.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProt.
DR GO; GO:0012505; C:endomembrane system; IEA:UniProt.
DR GO; GO:0043231; C:intracellular membrane-bounded organelle; IEA:UniProt.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0048193; P:Golgi vesicle transport; IEA:InterPro.
DR CDD; cd21444; SNARE_NTD_Tlg1p-like; 1.
DR CDD; cd15851; SNARE_Syntaxin6; 1.
DR Gene3D; 1.20.5.110; -; 1.
DR Gene3D; 1.20.58.90; -; 1.
DR InterPro; IPR010989; SNARE.
DR InterPro; IPR015260; Syntaxin-6_N.
DR InterPro; IPR000727; T_SNARE_dom.
DR InterPro; IPR048036; Tlg1p-like_N.
DR PANTHER; PTHR12791; GOLGI SNARE BET1-RELATED; 1.
DR PANTHER; PTHR12791:SF60; SYNTAXIN-8A; 1.
DR Pfam; PF09177; Syntaxin-6_N; 1.
DR SMART; SM00397; t_SNARE; 1.
DR SUPFAM; SSF58038; SNARE fusion complex; 1.
DR SUPFAM; SSF47661; t-snare proteins; 1.
DR PROSITE; PS50192; T_SNARE; 1.
PE 4: Predicted;
KW Coiled coil {ECO:0000256|SAM:Coils};
KW Golgi apparatus {ECO:0000256|ARBA:ARBA00023034};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Reference proteome {ECO:0000313|Proteomes:UP000008784};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius}; Transport {ECO:0000256|ARBA:ARBA00022448}.
FT TRANSMEM 221..242
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 151..213
FT /note="T-SNARE coiled-coil homology"
FT /evidence="ECO:0000259|PROSITE:PS50192"
FT REGION 114..138
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 47..74
FT /evidence="ECO:0000256|SAM:Coils"
SQ SEQUENCE 243 AA; 27408 MW; 1BFA69408C191C88 CRC64;
MNGDDPFIQV QQDVTALLHT TRQLFSSYLR IRSLASSRTS PELTSAHSEL EDALADLEID
LEDLRLAVSE GERDPYRFGL EVEAVAKRRK WLREVEGELS DIKEELGKEA AIMAGSAKGR
QPTTVVSSYD DDNGSRAGDD SYTQFEHLHQ QELMRNQDDQ LESVYRTVGN LRMQANDMGR
ELEEQAVILD ETDAIAERVD GRLKKGMKNL TEFARANEDK YSSCCIAILI FVLILLLVLL
LVL
//
