ID A0A061H0W5_9BASI Unreviewed; 458 AA.
AC A0A061H0W5;
DT 03-SEP-2014, integrated into UniProtKB/TrEMBL.
DT 03-SEP-2014, sequence version 1.
DT 27-MAR-2024, entry version 46.
DE RecName: Full=t-SNARE coiled-coil homology domain-containing protein {ECO:0000259|PROSITE:PS50192};
GN ORFNames=PFL1_06756 {ECO:0000313|EMBL:EPQ25684.1};
OS Pseudozyma flocculosa PF-1.
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Ustilaginomycotina;
OC Ustilaginomycetes; Ustilaginales; Ustilaginaceae; Pseudozyma.
OX NCBI_TaxID=1277687 {ECO:0000313|EMBL:EPQ25684.1, ECO:0000313|Proteomes:UP000053664};
RN [1] {ECO:0000313|EMBL:EPQ25684.1, ECO:0000313|Proteomes:UP000053664}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PF-1 {ECO:0000313|EMBL:EPQ25684.1,
RC ECO:0000313|Proteomes:UP000053664};
RX PubMed=23800965; DOI=10.1105/tpc.113.113969;
RA Lefebvre F., Joly D.L., Labbe C., Teichmann B., Linning R., Belzile F.,
RA Bakkeren G., Belanger R.R.;
RT "The transition from a phytopathogenic smut ancestor to an anamorphic
RT biocontrol agent deciphered by comparative whole-genome analysis.";
RL Plant Cell 25:1946-1959(2013).
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}.
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DR EMBL; KE361652; EPQ25684.1; -; Genomic_DNA.
DR RefSeq; XP_007882493.1; XM_007884302.1.
DR AlphaFoldDB; A0A061H0W5; -.
DR GeneID; 19320827; -.
DR KEGG; pfp:PFL1_06756; -.
DR eggNOG; KOG0809; Eukaryota.
DR HOGENOM; CLU_038177_0_0_1; -.
DR OrthoDB; 2876074at2759; -.
DR Proteomes; UP000053664; 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; cd15845; SNARE_syntaxin16; 1.
DR Gene3D; 1.20.58.70; -; 1.
DR InterPro; IPR010989; SNARE.
DR InterPro; IPR045242; Syntaxin.
DR InterPro; IPR006012; Syntaxin/epimorphin_CS.
DR InterPro; IPR000727; T_SNARE_dom.
DR PANTHER; PTHR19957; SYNTAXIN; 1.
DR PANTHER; PTHR19957:SF83; SYNTAXIN-16; 1.
DR Pfam; PF05739; SNARE; 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:UP000053664};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 414..434
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 339..401
FT /note="T-SNARE coiled-coil homology"
FT /evidence="ECO:0000259|PROSITE:PS50192"
FT REGION 1..140
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 274..296
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..52
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 60..77
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 94..117
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 276..290
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 458 AA; 49397 MW; BAEE35CD198DEBA7 CRC64;
MSTRYGRGPY AASSTPSTSA AAMAGFPSSS SASSSSAVSP HLGQTRSRTL LFLSYRDTAA
RTTKRPSGPS SSLYFQAPYT DGDGDDDHDP LHASSVNNGE QQGLLGGSSP SSARNSHDRP
HTSIELGATS DDGGSELPPK WMDISDQVDA ILASIRPRMD SLSRLHEKHL RPGFTDKSAE
EKQIEALALS ITQDFRRSSR LVAGLASFTQ HLIREAKKGN SSTTVRQIAL AQNVQTALAT
RVQDLSGAFR KQQSLYLRRM KGMEVRDRDI RAAQGLATGG TSSASASTSA RERNEFRDNE
MAVREDMELS RTASMAAKGQ SQQAQDLVVL ESSTSTAADA EIAQRDREIT EIAKSIQELA
NLFGDLQTLV IDQGTMLDRI DFNVELMSRE MEGAVKELEV ATGYQRRTGR RQCILFLILC
IALLVAILII KPFWRFFAAG GGASPPSVPA PPPAPSSS
//
