ID A0A0J9XB69_GEOCN Unreviewed; 205 AA.
AC A0A0J9XB69;
DT 14-OCT-2015, integrated into UniProtKB/TrEMBL.
DT 14-OCT-2015, sequence version 1.
DT 24-JAN-2024, entry version 42.
DE SubName: Full=Similar to Saccharomyces cerevisiae YKL196C YKT6 Vesicle membrane protein (V-SNARE) with acyltransferase activity {ECO:0000313|EMBL:CDO54433.1};
GN ORFNames=BN980_GECA07s04674g {ECO:0000313|EMBL:CDO54433.1},
GN DV451_001360 {ECO:0000313|EMBL:KAF5103620.1};
OS Geotrichum candidum (Oospora lactis) (Dipodascus geotrichum).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Dipodascaceae; Geotrichum.
OX NCBI_TaxID=1173061 {ECO:0000313|EMBL:CDO54433.1, ECO:0000313|Proteomes:UP000242525};
RN [1] {ECO:0000313|EMBL:CDO54433.1, ECO:0000313|Proteomes:UP000242525}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CLIB 918 {ECO:0000313|EMBL:CDO54433.1,
RC ECO:0000313|Proteomes:UP000242525};
RA Casaregola S.;
RL Submitted (MAR-2014) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:KAF5103620.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=LMA-70 {ECO:0000313|EMBL:KAF5103620.1};
RX PubMed=32457706;
RA Perkins V., Vignola S., Lessard M.H., Plante P.L., Corbeil J.,
RA Dugat-Bony E., Frenette M., Labrie S.;
RT "Phenotypic and Genetic Characterization of the Cheese Ripening Yeast
RT Geotrichum candidum.";
RL Front. Microbiol. 11:0-0(2020).
RN [3] {ECO:0000313|EMBL:KAF5103620.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=LMA-70 {ECO:0000313|EMBL:KAF5103620.1};
RA Perkins V., Lessard M.-H., Dugat-Bony E., Frenette M., Labrie S.;
RL Submitted (JAN-2020) to the EMBL/GenBank/DDBJ databases.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004423}; Lipid-
CC anchor {ECO:0000256|ARBA:ARBA00004423}; Cytoplasmic side
CC {ECO:0000256|ARBA:ARBA00004423}.
CC -!- SIMILARITY: Belongs to the synaptobrevin family.
CC {ECO:0000256|ARBA:ARBA00008025}.
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DR EMBL; CCBN010000007; CDO54433.1; -; Genomic_DNA.
DR EMBL; QQZK01000020; KAF5103620.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0J9XB69; -.
DR STRING; 1173061.A0A0J9XB69; -.
DR OrthoDB; 24529at2759; -.
DR Proteomes; UP000242525; Unassembled WGS sequence.
DR Proteomes; UP000750522; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0016746; F:acyltransferase activity; IEA:UniProtKB-KW.
DR CDD; cd14824; Longin; 1.
DR CDD; cd15867; R-SNARE_YKT6; 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; IPR045848; R-SNARE_YKT6.
DR InterPro; IPR042855; V_SNARE_CC.
DR PANTHER; PTHR45806; SYNAPTOBREVIN HOMOLOG YKT6; 1.
DR PANTHER; PTHR45806:SF1; SYNAPTOBREVIN HOMOLOG YKT6; 1.
DR Pfam; PF13774; Longin; 1.
DR Pfam; PF00957; Synaptobrevin; 1.
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 Acyltransferase {ECO:0000313|EMBL:CDO54433.1};
KW Coiled coil {ECO:0000256|PROSITE-ProRule:PRU00290};
KW Lipoprotein {ECO:0000256|ARBA:ARBA00023288};
KW Methylation {ECO:0000256|ARBA:ARBA00022481};
KW Palmitate {ECO:0000256|ARBA:ARBA00023139};
KW Prenylation {ECO:0000256|ARBA:ARBA00023289};
KW Reference proteome {ECO:0000313|Proteomes:UP000750522};
KW Transferase {ECO:0000313|EMBL:CDO54433.1}.
FT DOMAIN 7..107
FT /note="Longin"
FT /evidence="ECO:0000259|PROSITE:PS50859"
FT DOMAIN 145..205
FT /note="V-SNARE coiled-coil homology"
FT /evidence="ECO:0000259|PROSITE:PS50892"
SQ SEQUENCE 205 AA; 22983 MW; 8F01E7A2860EC418 CRC64;
MKLFYIGIIR NNTKGEGLEL ASVKDVSSFS FFERSSVTQF MSFFADTVAS RTNPGQRQSV
QEGTTYTGHV YARTEGIAGV VITDQEYPVR VAYSLLNKVL DEYLVKYQVT PAFLSAATKA
NEPQYALESL NDYIKRYQDP QQADTMLKVQ QELDETKIVL HKTIESVLDR GEKLDSLVEK
SGALSQTSKL FYSQAKKTNS CCLIA
//
