ID A0A093VGW0_TALMA Unreviewed; 349 AA.
AC A0A093VGW0;
DT 26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT 26-NOV-2014, sequence version 1.
DT 27-MAR-2024, entry version 26.
DE SubName: Full=Integral membrane protein sed5 {ECO:0000313|EMBL:KFX51782.1};
GN ORFNames=GQ26_0041780 {ECO:0000313|EMBL:KFX51782.1};
OS Talaromyces marneffei PM1.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Trichocomaceae; Talaromyces;
OC Talaromyces sect. Talaromyces.
OX NCBI_TaxID=1077442 {ECO:0000313|EMBL:KFX51782.1, ECO:0000313|Proteomes:UP000029285};
RN [1] {ECO:0000313|Proteomes:UP000029285}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PM1 {ECO:0000313|Proteomes:UP000029285};
RX PubMed=25330172; DOI=10.1371/journal.pgen.1004662;
RA Yang E., Wang G., Cai J., Woo P.C., Lau S.K., Yuen K.-Y., Chow W.-N.,
RA Lin X.;
RT "Signature Gene Expression Reveals Novel Clues to the Molecular Mechanisms
RT of Dimorphic Transition in Penicillium marneffei.";
RL PLoS Genet. 10:e1004662-e1004662(2014).
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004211}; Single-
CC pass type IV membrane protein {ECO:0000256|ARBA:ARBA00004211}.
CC -!- SIMILARITY: Belongs to the syntaxin family.
CC {ECO:0000256|ARBA:ARBA00009063}.
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:KFX51782.1}.
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DR EMBL; JPOX01000004; KFX51782.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A093VGW0; -.
DR eggNOG; KOG0812; Eukaryota.
DR HOGENOM; CLU_044998_0_1_1; -.
DR Proteomes; UP000029285; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0016192; P:vesicle-mediated transport; IEA:InterPro.
DR CDD; cd15844; SNARE_syntaxin5; 1.
DR Gene3D; 1.20.58.70; -; 1.
DR InterPro; IPR010989; SNARE.
DR InterPro; IPR045242; Syntaxin.
DR InterPro; IPR021538; Syntaxin-5_N.
DR InterPro; IPR000727; T_SNARE_dom.
DR PANTHER; PTHR19957; SYNTAXIN; 1.
DR PANTHER; PTHR19957:SF3; SYNTAXIN-5; 1.
DR Pfam; PF05739; SNARE; 1.
DR Pfam; PF11416; Syntaxin-5_N; 1.
DR SMART; SM00397; t_SNARE; 1.
DR SUPFAM; SSF47661; t-snare proteins; 1.
DR PROSITE; PS50192; T_SNARE; 1.
PE 3: Inferred from homology;
KW Membrane {ECO:0000256|SAM:Phobius};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 328..347
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 257..319
FT /note="T-SNARE coiled-coil homology"
FT /evidence="ECO:0000259|PROSITE:PS50192"
FT REGION 25..58
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 174..241
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 25..47
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 174..197
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 223..241
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 349 AA; 38818 MW; 5731F3D3A8EC4A70 CRC64;
MTMASIQDRT TEFRSILGQA QKRMASNKVG AQRQALLSDS QRRQANGSPE GPGKRRSEFA
RRAAEIGRGI TGTTAKLQRL AELAKRKTLF DDRPVEISEL TYVIKQDLAS LNQQIAQLQA
LTLSQHPRAS RNKTDQEGEH NDNVVVMLQG KLADVGANFK EVLEVRTKNI QASRSRTENF
VSSVSSKSQT QFDPQRSDSP LYIAPRSRTP QPGFRHGGGN SSDLLTLEPS SSSVLGQSNR
GASDQQLLMM EEAQPENTYI QARGEAIEAI ERTINELGGI FGQLATMVSE QSEMIQRIDA
NTEDVVDNVE GAQRELMKYW SRMSGNRWLI AKMFGVLMIF FLLWVLISG
//
