ID A0A165KAI1_9BASI Unreviewed; 365 AA.
AC A0A165KAI1;
DT 06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT 06-JUL-2016, sequence version 1.
DT 28-JUN-2023, entry version 17.
DE RecName: Full=t-SNARE coiled-coil homology domain-containing protein {ECO:0000259|PROSITE:PS50192};
GN ORFNames=CALCODRAFT_425438 {ECO:0000313|EMBL:KZT62895.1};
OS Calocera cornea HHB12733.
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Dacrymycetes;
OC Dacrymycetales; Dacrymycetaceae; Calocera.
OX NCBI_TaxID=1353952 {ECO:0000313|EMBL:KZT62895.1, ECO:0000313|Proteomes:UP000076842};
RN [1] {ECO:0000313|EMBL:KZT62895.1, ECO:0000313|Proteomes:UP000076842}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=HHB12733 {ECO:0000313|EMBL:KZT62895.1,
RC ECO:0000313|Proteomes:UP000076842};
RX PubMed=26659563; DOI=10.1093/molbev/msv337;
RA Nagy L.G., Riley R., Tritt A., Adam C., Daum C., Floudas D., Sun H.,
RA Yadav J.S., Pangilinan J., Larsson K.H., Matsuura K., Barry K., Labutti K.,
RA Kuo R., Ohm R.A., Bhattacharya S.S., Shirouzu T., Yoshinaga Y.,
RA Martin F.M., Grigoriev I.V., Hibbett D.S.;
RT "Comparative Genomics of Early-Diverging Mushroom-Forming Fungi Provides
RT Insights into the Origins of Lignocellulose Decay Capabilities.";
RL Mol. Biol. Evol. 33:959-970(2016).
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; KV423914; KZT62895.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A165KAI1; -.
DR STRING; 1353952.A0A165KAI1; -.
DR InParanoid; A0A165KAI1; -.
DR OrthoDB; 2056029at2759; -.
DR Proteomes; UP000076842; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0015031; P:protein transport; IEA:UniProtKB-KW.
DR Gene3D; 1.20.5.110; -; 1.
DR InterPro; IPR019529; Syntaxin-18_N.
DR InterPro; IPR000727; T_SNARE_dom.
DR PANTHER; PTHR15959; SYNTAXIN-18; 1.
DR PANTHER; PTHR15959:SF0; SYNTAXIN-18; 1.
DR Pfam; PF10496; Syntaxin-18_N; 1.
DR SUPFAM; SSF58038; SNARE fusion complex; 1.
DR PROSITE; PS50192; T_SNARE; 1.
PE 3: Inferred from homology;
KW Coiled coil {ECO:0000256|ARBA:ARBA00023054};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Protein transport {ECO:0000256|ARBA:ARBA00022927};
KW Reference proteome {ECO:0000313|Proteomes:UP000076842};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius}; Transport {ECO:0000256|ARBA:ARBA00022448}.
FT TRANSMEM 346..364
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 283..336
FT /note="T-SNARE coiled-coil homology"
FT /evidence="ECO:0000259|PROSITE:PS50192"
FT REGION 15..43
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 365 AA; 40801 MW; 7FF5102F37EE75FF CRC64;
MVSIDITADF RTSVQSALKT LPEPKRRTKP RPKHSKADGQ GEPSYADAYL QEAYAILEHI
NTLNSMLTSI RHAYLSVDSG SGFSGPSRRG KAFDVQEKQG WEGVKRLTNQ ERDEIDLQAK
VIMKRCMDRV KALEALEAKR ASSAPHKTAL LRLLPTRLTS TPSLASSDLL AAHYLSITWF
LNARLARVSA VQREMQEERV RRQLERARSL GGEVPGSRDG GPGEGVVRRF DATAVPRHPS
LRTTSAYTAS GEEDDAPLTA EQAQLFELEN ASILRSAENV LAQVQRAESS LHDISALQSE
LVHHLTVQSE MTDRLYEEAM STQREVERGN DQLRKARERG GDARRWLLVF LIGASLALLF
VHYYR
//
