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Database: UniProt
Entry: A0A0F0I300_ASPPU
LinkDB: A0A0F0I300_ASPPU
Original site: A0A0F0I300_ASPPU 
ID   A0A0F0I300_ASPPU        Unreviewed;       370 AA.
AC   A0A0F0I300;
DT   24-JUN-2015, integrated into UniProtKB/TrEMBL.
DT   24-JUN-2015, sequence version 1.
DT   27-MAR-2024, entry version 23.
DE   SubName: Full=The phosphoinositide binding Phox Homology domain of SNARE protein from fungi {ECO:0000313|EMBL:KJK60348.1};
GN   ORFNames=P875_00053474 {ECO:0000313|EMBL:KJK60348.1};
OS   Aspergillus parasiticus (strain ATCC 56775 / NRRL 5862 / SRRC 143 / SU-1).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus.
OX   NCBI_TaxID=1403190 {ECO:0000313|EMBL:KJK60348.1, ECO:0000313|Proteomes:UP000033540};
RN   [1] {ECO:0000313|EMBL:KJK60348.1, ECO:0000313|Proteomes:UP000033540}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 56775 / NRRL 5862 / SRRC 143 / SU-1
RC   {ECO:0000313|Proteomes:UP000033540};
RA   Yu J., Fedorova N., Yin Y., Losada L., Zafar N., Taujale R., Ehrlich K.C.,
RA   Bhatnagar D., Cleveland T.E., Bennett J.W., Nierman W.C.;
RT   "Draft genome sequence of Aspergillus parasiticus SU-1.";
RL   Submitted (FEB-2015) to the EMBL/GenBank/DDBJ databases.
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:KJK60348.1}.
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DR   EMBL; JZEE01000744; KJK60348.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0F0I300; -.
DR   STRING; 1403190.A0A0F0I300; -.
DR   Proteomes; UP000033540; 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   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:UP000033540}.
FT   DOMAIN          2..117
FT                   /note="PX"
FT                   /evidence="ECO:0000259|PROSITE:PS50195"
FT   DOMAIN          307..369
FT                   /note="T-SNARE coiled-coil homology"
FT                   /evidence="ECO:0000259|PROSITE:PS50192"
FT   REGION          166..187
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          207..227
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   370 AA;  41251 MW;  1CC54A18643A710C CRC64;
     MSPNLEITIP TTSLSPTSPP YTVYNLTLRL PLRSFTISKR YSDFLNFHKT LLTQTNVPPP
     APLPQKTWFK NTVSNASLRE DRRQALEAYL QAINDADDPR WRNSPAWRAF LNLPSAANAS
     HTSTRLHAAI TDPGSSADNP ISDPTLWLDV YRDMKSHLHD ARLHLTRRDQ ETTPQKQHES
     SARAKSSLVR AGSLVAALEE GLKVMGETAS RAQSPSGRGR GGSLGDGELR RRKDLLINAR
     KEKDGLEDLL NAMAAKSRVD HAVASVQDKE ALVGSASRKP ARSGRVLGKE TERTRELDNQ
     GVLQLQRQTM EDQDQSVEEL LKIIRRQKEL GIAINEEVEI QNALLSMANE DAERVHRKID
     IGKKRIGKIS
//
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