ID A0A2H3J1D8_WOLCO Unreviewed; 359 AA.
AC A0A2H3J1D8;
DT 31-JAN-2018, integrated into UniProtKB/TrEMBL.
DT 31-JAN-2018, sequence version 1.
DT 27-MAR-2024, entry version 21.
DE SubName: Full=Syntaxin {ECO:0000313|EMBL:PCH33603.1};
GN ORFNames=WOLCODRAFT_86876 {ECO:0000313|EMBL:PCH33603.1};
OS Wolfiporia cocos (strain MD-104) (Brown rot fungus).
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC Polyporales; Phaeolaceae; Wolfiporia.
OX NCBI_TaxID=742152 {ECO:0000313|EMBL:PCH33603.1, ECO:0000313|Proteomes:UP000218811};
RN [1] {ECO:0000313|EMBL:PCH33603.1, ECO:0000313|Proteomes:UP000218811}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MD-104 {ECO:0000313|EMBL:PCH33603.1,
RC ECO:0000313|Proteomes:UP000218811};
RX PubMed=22745431; DOI=10.1126/science.1221748;
RA Floudas D., Binder M., Riley R., Barry K., Blanchette R.A., Henrissat B.,
RA Martinez A.T., Otillar R., Spatafora J.W., Yadav J.S., Aerts A., Benoit I.,
RA Boyd A., Carlson A., Copeland A., Coutinho P.M., de Vries R.P.,
RA Ferreira P., Findley K., Foster B., Gaskell J., Glotzer D., Gorecki P.,
RA Heitman J., Hesse C., Hori C., Igarashi K., Jurgens J.A., Kallen N.,
RA Kersten P., Kohler A., Kuees U., Kumar T.K.A., Kuo A., LaButti K.,
RA Larrondo L.F., Lindquist E., Ling A., Lombard V., Lucas S., Lundell T.,
RA Martin R., McLaughlin D.J., Morgenstern I., Morin E., Murat C., Nagy L.G.,
RA Nolan M., Ohm R.A., Patyshakuliyeva A., Rokas A., Ruiz-Duenas F.J.,
RA Sabat G., Salamov A., Samejima M., Schmutz J., Slot J.C., St John F.,
RA Stenlid J., Sun H., Sun S., Syed K., Tsang A., Wiebenga A., Young D.,
RA Pisabarro A., Eastwood D.C., Martin F., Cullen D., Grigoriev I.V.,
RA Hibbett D.S.;
RT "The Paleozoic origin of enzymatic lignin decomposition reconstructed from
RT 31 fungal genomes.";
RL Science 336:1715-1719(2012).
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DR EMBL; KB467831; PCH33603.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2H3J1D8; -.
DR STRING; 742152.A0A2H3J1D8; -.
DR OMA; QASVRSW; -.
DR OrthoDB; 1357185at2759; -.
DR Proteomes; UP000218811; 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; IPR045242; Syntaxin.
DR InterPro; IPR000727; T_SNARE_dom.
DR PANTHER; PTHR19957; SYNTAXIN; 1.
DR PANTHER; PTHR19957:SF257; SYNTAXIN-LIKE PROTEIN FSV1-RELATED; 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 Coiled coil {ECO:0000256|SAM:Coils};
KW Reference proteome {ECO:0000313|Proteomes:UP000218811}.
FT DOMAIN 2..118
FT /note="PX"
FT /evidence="ECO:0000259|PROSITE:PS50195"
FT DOMAIN 296..358
FT /note="T-SNARE coiled-coil homology"
FT /evidence="ECO:0000259|PROSITE:PS50192"
FT REGION 235..266
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 327..354
FT /evidence="ECO:0000256|SAM:Coils"
SQ SEQUENCE 359 AA; 40005 MW; 273661BF16870CF0 CRC64;
MAAIQAIHIR GFEERAEPKP HVVYRIEIQA SVRSWQMWRR YSEFADLHVE LTKSSGAAPP
AELPPKKSLA FFKARDAAFL EERRAGLELY LRAILSAKDD RWRESFAFRD FLGVPVGKQP
GADGAAPSQF TSSSWLDEHQ DLLARVRDVR ADINKRDALS DRGDIAGSHQ SNVQAKKKLA
GILTRVGVLE DGLRALGLGG MSEGELQRRT DMVSRLRDDC EKLAKMVTVA RMTSRGLGSA
AERNPASPSD RAALLDSPSS SGFSRPVTRV FGAAARPQET EQTRPLDDHG VFQLQQTQME
NQDQQLAQLS TILQRQKHLG LAIHSEISEQ NEMLDDLTSE VDRVGNKLTR TKRQMNRLG
//
