ID A0A165YR16_9AGAM Unreviewed; 228 AA.
AC A0A165YR16;
DT 06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT 06-JUL-2016, sequence version 1.
DT 27-MAR-2024, entry version 29.
DE RecName: Full=Synaptobrevin homolog YKT6 {ECO:0000256|ARBA:ARBA00026133};
GN ORFNames=SISSUDRAFT_1054146 {ECO:0000313|EMBL:KZT33512.1};
OS Sistotremastrum suecicum HHB10207 ss-3.
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC Trechisporales; Trechisporales incertae sedis; Sistotremastrum.
OX NCBI_TaxID=1314776 {ECO:0000313|EMBL:KZT33512.1, ECO:0000313|Proteomes:UP000076798};
RN [1] {ECO:0000313|EMBL:KZT33512.1, ECO:0000313|Proteomes:UP000076798}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=HHB10207 ss-3 {ECO:0000313|EMBL:KZT33512.1,
RC ECO:0000313|Proteomes:UP000076798};
RX PubMed=26659563; DOI=10.1093/molbev/msv337;
RA Nagy L.G., Riley R., Tritt A., Adam C., Daum C., Floudas D., Sun H.,
RA Yadav J.S., Pangilinan J., Larsson K.H., Matsuura K., Barry K., Labutti K.,
RA Kuo R., Ohm R.A., Bhattacharya S.S., Shirouzu T., Yoshinaga Y.,
RA Martin F.M., Grigoriev I.V., Hibbett D.S.;
RT "Comparative Genomics of Early-Diverging Mushroom-Forming Fungi Provides
RT Insights into the Origins of Lignocellulose Decay Capabilities.";
RL Mol. Biol. Evol. 33:959-970(2016).
CC -!- SIMILARITY: Belongs to the synaptobrevin family.
CC {ECO:0000256|ARBA:ARBA00008025}.
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DR EMBL; KV428236; KZT33512.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A165YR16; -.
DR STRING; 1314776.A0A165YR16; -.
DR Proteomes; UP000076798; 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; 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:UP000076798};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius};
KW Transport {ECO:0000256|ARBA:ARBA00022448}.
FT TRANSMEM 193..217
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 7..84
FT /note="Longin"
FT /evidence="ECO:0000259|PROSITE:PS50859"
FT DOMAIN 129..189
FT /note="V-SNARE coiled-coil homology"
FT /evidence="ECO:0000259|PROSITE:PS50892"
SQ SEQUENCE 228 AA; 25412 MW; 96D948B5452CEBBA CRC64;
MSLIHALVAN AESSTILVES STGKRDFSQA VQTILSKIPP NNSKLTYVWE QYLFHYVAES
GVVYLVMADD SVGRRLPFTF LTRLQALLPP STALSTESSH HGLQLTYGDK LEKLMKEFNE
NPNEAGKDAL TNAQNELNQV KDIMVHNVEQ ILSRGERIDL LVDKTDNMAT QAVAFRRGAR
AQRRRQFWRN QKILWLSGGV GILIIYLIIA GFCGAGLNQC GKKNDSSS
//
