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Database: UniProt
Entry: A0A163KAB1_ABSGL
LinkDB: A0A163KAB1_ABSGL
Original site: A0A163KAB1_ABSGL 
ID   A0A163KAB1_ABSGL        Unreviewed;       341 AA.
AC   A0A163KAB1;
DT   06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT   06-JUL-2016, sequence version 1.
DT   27-MAR-2024, entry version 25.
DE   RecName: Full=t-SNARE coiled-coil homology domain-containing protein {ECO:0000259|PROSITE:PS50192};
GN   Name=ABSGL_14992.1 scaffold 15162 {ECO:0000313|EMBL:SAM09316.1};
OS   Absidia glauca (Pin mould).
OC   Eukaryota; Fungi; Fungi incertae sedis; Mucoromycota; Mucoromycotina;
OC   Mucoromycetes; Mucorales; Cunninghamellaceae; Absidia.
OX   NCBI_TaxID=4829 {ECO:0000313|EMBL:SAM09316.1};
RN   [1] {ECO:0000313|EMBL:SAM09316.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CBS 101.48 {ECO:0000313|EMBL:SAM09316.1};
RA   Evans L.H., Alamgir A., Owens N., Weber N.D., Virtaneva K., Barbian K.,
RA   Babar A., Rosenke K.;
RL   Submitted (APR-2016) to the EMBL/GenBank/DDBJ databases.
CC   -!- SIMILARITY: Belongs to the syntaxin family.
CC       {ECO:0000256|ARBA:ARBA00009063}.
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DR   EMBL; LT555008; SAM09316.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A163KAB1; -.
DR   STRING; 4829.A0A163KAB1; -.
DR   InParanoid; A0A163KAB1; -.
DR   OMA; ANIEQKG; -.
DR   OrthoDB; 2879355at2759; -.
DR   Proteomes; UP000078561; Unassembled WGS sequence.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR   GO; GO:0016192; P:vesicle-mediated transport; IEA:InterPro.
DR   CDD; cd15849; SNARE_Sso1; 1.
DR   Gene3D; 1.20.58.70; -; 1.
DR   InterPro; IPR010989; SNARE.
DR   InterPro; IPR045242; Syntaxin.
DR   InterPro; IPR006011; Syntaxin_N.
DR   InterPro; IPR000727; T_SNARE_dom.
DR   PANTHER; PTHR19957; SYNTAXIN; 1.
DR   PANTHER; PTHR19957:SF307; SYNTAXIN-1A; 1.
DR   Pfam; PF05739; SNARE; 1.
DR   Pfam; PF00804; Syntaxin; 1.
DR   SMART; SM00503; SynN; 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   Coiled coil {ECO:0000256|SAM:Coils}; Membrane {ECO:0000256|SAM:Phobius};
KW   Reference proteome {ECO:0000313|Proteomes:UP000078561};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        303..324
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          229..291
FT                   /note="T-SNARE coiled-coil homology"
FT                   /evidence="ECO:0000259|PROSITE:PS50192"
FT   REGION          1..48
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          67..94
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COMPBIAS        1..19
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        20..35
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   341 AA;  39543 MW;  1D183311A58FB3A4 CRC64;
     MSFSRDRTAE LRDSFEGTQR MNDDFGSART GYNTNPFPQE PPPVHRHNNP TRVDTFEMQP
     PSDIKNMDGF FDEIEKLKDQ VRVINENIDE IEHIHNSALV SHNEQQWTQM SADLDRWKTD
     TQKRNLDVKN RLKAVEASNG RFNKSDAQIR RTQSGAIKKR FLDTIQRYQD IERSYQQKYR
     QRVERQIRIV KPDASEQEID QIIDSDESPQ VFSQSLMQAG RRGQARAVLS EVQNRHDDIK
     KIEKTIIELH QLFMDMQMLV EQQGETIDQI EEHAETTAVQ MEEGNKFVSR AINSARATRH
     KKWCCFVICI ILAVVIAILV WWFGFGHPGV GGSSNGGQQQ Q
//
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