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Database: UniProt
Entry: A0A3F3QK46_9EURO
LinkDB: A0A3F3QK46_9EURO
Original site: A0A3F3QK46_9EURO 
ID   A0A3F3QK46_9EURO        Unreviewed;       400 AA.
AC   A0A3F3QK46;
DT   16-JAN-2019, integrated into UniProtKB/TrEMBL.
DT   16-JAN-2019, sequence version 1.
DT   27-MAR-2024, entry version 20.
DE   RecName: Full=SNARE complex subunit {ECO:0008006|Google:ProtNLM};
GN   ORFNames=BDQ94DRAFT_165089 {ECO:0000313|EMBL:RDH39370.1};
OS   Aspergillus welwitschiae.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus.
OX   NCBI_TaxID=1341132 {ECO:0000313|EMBL:RDH39370.1, ECO:0000313|Proteomes:UP000253729};
RN   [1] {ECO:0000313|EMBL:RDH39370.1, ECO:0000313|Proteomes:UP000253729}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CBS 139.54b {ECO:0000313|EMBL:RDH39370.1,
RC   ECO:0000313|Proteomes:UP000253729};
RG   DOE Joint Genome Institute;
RA   Vesth T.C., Nybo J., Theobald S., Brandl J., Frisvad J.C., Nielsen K.F.,
RA   Lyhne E.K., Kogle M.E., Kuo A., Riley R., Clum A., Nolan M., Lipzen A.,
RA   Salamov A., Henrissat B., Wiebenga A., De vries R.P., Grigoriev I.V.,
RA   Mortensen U.H., Andersen M.R., Baker S.E.;
RT   "The genomes of Aspergillus section Nigri reveals drivers in fungal
RT   speciation.";
RL   Submitted (JUL-2018) to the EMBL/GenBank/DDBJ databases.
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DR   EMBL; KZ852032; RDH39370.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A3F3QK46; -.
DR   STRING; 1341132.A0A3F3QK46; -.
DR   OrthoDB; 1357185at2759; -.
DR   Proteomes; UP000253729; Unassembled WGS sequence.
DR   GO; GO:0043226; C:organelle; IEA:UniProt.
DR   GO; GO:0035091; F:phosphatidylinositol binding; IEA:InterPro.
DR   CDD; cd06897; PX_SNARE; 1.
DR   CDD; cd15858; SNARE_VAM7; 1.
DR   Gene3D; 1.20.5.110; -; 1.
DR   Gene3D; 3.30.1520.10; Phox-like domain; 1.
DR   InterPro; IPR001683; PX_dom.
DR   InterPro; IPR036871; PX_dom_sf.
DR   InterPro; IPR000727; T_SNARE_dom.
DR   PANTHER; PTHR22775; SORTING NEXIN; 1.
DR   PANTHER; PTHR22775:SF3; SORTING NEXIN-13; 1.
DR   Pfam; PF00787; PX; 1.
DR   SMART; SM00312; PX; 1.
DR   SMART; SM00397; t_SNARE; 1.
DR   SUPFAM; SSF64268; PX domain; 1.
DR   SUPFAM; SSF58038; SNARE fusion complex; 1.
DR   PROSITE; PS50195; PX; 1.
DR   PROSITE; PS50192; T_SNARE; 1.
PE   4: Predicted;
KW   Reference proteome {ECO:0000313|Proteomes:UP000253729}.
FT   DOMAIN          3..118
FT                   /note="PX"
FT                   /evidence="ECO:0000259|PROSITE:PS50195"
FT   DOMAIN          337..399
FT                   /note="T-SNARE coiled-coil homology"
FT                   /evidence="ECO:0000259|PROSITE:PS50192"
FT   REGION          209..255
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        209..252
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   400 AA;  44103 MW;  88791299B626448E CRC64;
     MPPTSLEISI PTTSISATQP PYTLYNITLR LPLRSFTISK RYSEFTTFHN TLVSQTNLPP
     PAPLPPKSWF QNTINNATLR ESRREALEAY LRAINESEDP RWRNSPAWRA FLNLPSLPSN
     NNNNNGGAST RLHAAITDPG DSEGGGITDP ILWLDCFRDM KGHLHDARLY LTRRDQETTP
     QRQHESSARA KSELVRAGGL IASLESGLRN LSNSSSGGGE ENNAGSRPGS KLGRRNTATT
     ATAWSVSGNN TLGEGEMRRR KDLLINARKE KDGLEDLLNA MAAKSRIDSA VASIQDKEAL
     MGTQGGKKAI RSSGRVLGRE TERTRELDNS GVVQLQKQMM EDQDVAVDEL MRIVNRQKEL
     GIAINNELQV QNELLNLADE DATRLGGKID IGKKRIGRIS
//
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