ID A0A139IE77_9PEZI Unreviewed; 272 AA.
AC A0A139IE77;
DT 11-MAY-2016, integrated into UniProtKB/TrEMBL.
DT 11-MAY-2016, sequence version 1.
DT 27-MAR-2024, entry version 28.
DE RecName: Full=t-SNARE coiled-coil homology domain-containing protein {ECO:0000259|PROSITE:PS50192};
GN ORFNames=AC579_4060 {ECO:0000313|EMBL:KXT12969.1};
OS Pseudocercospora musae.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC Dothideomycetidae; Mycosphaerellales; Mycosphaerellaceae; Pseudocercospora.
OX NCBI_TaxID=113226 {ECO:0000313|EMBL:KXT12969.1, ECO:0000313|Proteomes:UP000073492};
RN [1] {ECO:0000313|EMBL:KXT12969.1, ECO:0000313|Proteomes:UP000073492}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 116634 {ECO:0000313|EMBL:KXT12969.1,
RC ECO:0000313|Proteomes:UP000073492};
RA Chang T.-C., Salvucci A., Crous P.W., Stergiopoulos I.;
RT "Comparative genomics of the Sigatoka disease complex on banana suggests a
RT link between parallel evolutionary changes in Pseudocercospora fijiensis
RT and Pseudocercospora eumusae and increased virulence on the banana host.";
RL Submitted (JUL-2015) to the EMBL/GenBank/DDBJ databases.
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:KXT12969.1}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; LFZO01000134; KXT12969.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A139IE77; -.
DR STRING; 113226.A0A139IE77; -.
DR Proteomes; UP000073492; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005484; F:SNAP receptor activity; IEA:InterPro.
DR GO; GO:0006886; P:intracellular protein transport; IEA:InterPro.
DR GO; GO:0016192; P:vesicle-mediated transport; IEA:InterPro.
DR CDD; cd15840; SNARE_Qa; 1.
DR Gene3D; 1.20.5.110; -; 1.
DR Gene3D; 1.20.58.70; -; 1.
DR InterPro; IPR010989; SNARE.
DR InterPro; IPR045242; Syntaxin.
DR InterPro; IPR006012; Syntaxin/epimorphin_CS.
DR InterPro; IPR006011; Syntaxin_N.
DR InterPro; IPR000727; T_SNARE_dom.
DR PANTHER; PTHR19957:SF38; LD27581P; 1.
DR PANTHER; PTHR19957; SYNTAXIN; 1.
DR Pfam; PF05739; SNARE; 1.
DR Pfam; PF14523; Syntaxin_2; 1.
DR SMART; SM00397; t_SNARE; 1.
DR SUPFAM; SSF47661; t-snare proteins; 1.
DR PROSITE; PS00914; SYNTAXIN; 1.
DR PROSITE; PS50192; T_SNARE; 1.
PE 3: Inferred from homology;
KW Membrane {ECO:0000256|SAM:Phobius};
KW Reference proteome {ECO:0000313|Proteomes:UP000073492};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 251..271
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 178..240
FT /note="T-SNARE coiled-coil homology"
FT /evidence="ECO:0000259|PROSITE:PS50192"
FT REGION 1..28
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 132..168
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 151..168
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 272 AA; 30466 MW; E3B68DA20CCA23F7 CRC64;
MSFNDSSNLE SQPTTWRRED DPQYADDPEF QQYTTQLSDK LFSLTSNISR LSSQIALLGT
RRETDRVRER VSDLLSETQD GFREVGEGLK KVQAWHDLGP SQKYTAGKLS QEFRASLTEF
QGLQRQALDK QRASASAAKA ALDEAGPMSP SGPGGQQQLQ QQQEQLRLAD QSEVDFQESL
IIERESEIRN IESSVSELNE LFRDVATMVH DQGHTLDIIS ENVMQTRDDT RNADQQLRTA
SRHQKSARGK ACCLLIILAI VLAVVILAVV LS
//
