ID G1XAA5_ARTOA Unreviewed; 240 AA.
AC G1XAA5;
DT 16-NOV-2011, integrated into UniProtKB/TrEMBL.
DT 16-NOV-2011, sequence version 1.
DT 27-MAR-2024, entry version 60.
DE RecName: Full=Synaptobrevin homolog YKT6 {ECO:0000256|ARBA:ARBA00026133};
GN ORFNames=AOL_s00076g563 {ECO:0000313|EMBL:EGX49922.1};
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:EGX49922.1, ECO:0000313|Proteomes:UP000008784};
RN [1] {ECO:0000313|EMBL:EGX49922.1, 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 -!- SIMILARITY: Belongs to the synaptobrevin family.
CC {ECO:0000256|ARBA:ARBA00008025}.
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:EGX49922.1}.
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DR EMBL; ADOT01000129; EGX49922.1; -; Genomic_DNA.
DR RefSeq; XP_011121417.1; XM_011123115.1.
DR AlphaFoldDB; G1XAA5; -.
DR STRING; 756982.G1XAA5; -.
DR GeneID; 22892355; -.
DR eggNOG; KOG0859; Eukaryota.
DR HOGENOM; CLU_064620_1_1_1; -.
DR InParanoid; G1XAA5; -.
DR OMA; NTKLMIM; -.
DR OrthoDB; 664519at2759; -.
DR Proteomes; UP000008784; Unassembled WGS sequence.
DR GO; GO:0005737; C:cytoplasm; 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:0016192; P:vesicle-mediated transport; IEA:InterPro.
DR CDD; cd14824; Longin; 1.
DR CDD; cd15843; R-SNARE; 1.
DR Gene3D; 1.20.5.110; -; 1.
DR Gene3D; 3.30.450.50; Longin domain; 1.
DR InterPro; IPR011012; Longin-like_dom_sf.
DR InterPro; IPR010908; Longin_dom.
DR InterPro; IPR001388; Synaptobrevin-like.
DR InterPro; IPR042855; V_SNARE_CC.
DR PANTHER; PTHR21136; SNARE PROTEINS; 1.
DR PANTHER; PTHR21136:SF168; VESICLE-ASSOCIATED MEMBRANE PROTEIN 9; 1.
DR Pfam; PF13774; Longin; 1.
DR Pfam; PF00957; Synaptobrevin; 1.
DR PRINTS; PR00219; SYNAPTOBREVN.
DR SMART; SM01270; Longin; 1.
DR SUPFAM; SSF58038; SNARE fusion complex; 1.
DR SUPFAM; SSF64356; SNARE-like; 1.
DR PROSITE; PS50859; LONGIN; 1.
DR PROSITE; PS00417; SYNAPTOBREVIN; 1.
DR PROSITE; PS50892; V_SNARE; 1.
PE 3: Inferred from homology;
KW Coiled coil {ECO:0000256|PROSITE-ProRule:PRU00290};
KW Membrane {ECO:0000256|SAM:Phobius};
KW Reference proteome {ECO:0000313|Proteomes:UP000008784};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius};
KW Transport {ECO:0000256|ARBA:ARBA00022448}.
FT TRANSMEM 207..232
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 6..124
FT /note="Longin"
FT /evidence="ECO:0000259|PROSITE:PS50859"
FT DOMAIN 143..203
FT /note="V-SNARE coiled-coil homology"
FT /evidence="ECO:0000259|PROSITE:PS50892"
SQ SEQUENCE 240 AA; 26829 MW; 8416406F04B3A6AD CRC64;
MATHPLLYTC VAHRTTVLAE YTPFPSSSKN SSSVAQIASV VLPKISHDQP QKLTYTYGEH
LINYVSTSTS ASSLTFLLVT DKSVARKTSF GFLQKVQEEF GLKYTPAMVE DAPPYGCAEF
NKVLKEQVQI YAAGNGEDLG GNNARNVQAE IDAVRGIMTE NIERVLERGE RIDLLVDKTD
RLGEGARGFR VGARRLRRQM WWKNMKLMVL LWVVIIFLVY LFVGFGCGLP GWQRCIGKSN
//
