ID A0A1G4KAN4_9SACH Unreviewed; 617 AA.
AC A0A1G4KAN4;
DT 18-JAN-2017, integrated into UniProtKB/TrEMBL.
DT 18-JAN-2017, sequence version 1.
DT 27-MAR-2024, entry version 26.
DE SubName: Full=LAMI_0G10462g1_1 {ECO:0000313|EMBL:SCV01279.1};
GN ORFNames=LAMI_0G10462G {ECO:0000313|EMBL:SCV01279.1};
OS Lachancea mirantina.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Lachancea.
OX NCBI_TaxID=1230905 {ECO:0000313|EMBL:SCV01279.1, ECO:0000313|Proteomes:UP000191024};
RN [1] {ECO:0000313|EMBL:SCV01279.1, ECO:0000313|Proteomes:UP000191024}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 11717 {ECO:0000313|EMBL:SCV01279.1};
RA Devillers H.;
RL Submitted (MAR-2016) to the EMBL/GenBank/DDBJ databases.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
CC -!- SIMILARITY: Belongs to the HSF family. {ECO:0000256|RuleBase:RU004020}.
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DR EMBL; LT598469; SCV01279.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1G4KAN4; -.
DR STRING; 1230905.A0A1G4KAN4; -.
DR OrthoDB; 1117127at2759; -.
DR Proteomes; UP000191024; Chromosome g.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0003700; F:DNA-binding transcription factor activity; IEA:InterPro.
DR GO; GO:0043565; F:sequence-specific DNA binding; IEA:InterPro.
DR Gene3D; 1.10.10.10; Winged helix-like DNA-binding domain superfamily/Winged helix DNA-binding domain; 1.
DR InterPro; IPR000232; HSF_DNA-bd.
DR InterPro; IPR027725; HSF_fam.
DR InterPro; IPR036388; WH-like_DNA-bd_sf.
DR InterPro; IPR036390; WH_DNA-bd_sf.
DR PANTHER; PTHR10015:SF206; HEAT SHOCK FACTOR PROTEIN; 1.
DR PANTHER; PTHR10015; HEAT SHOCK TRANSCRIPTION FACTOR; 1.
DR Pfam; PF00447; HSF_DNA-bind; 1.
DR PRINTS; PR00056; HSFDOMAIN.
DR SMART; SM00415; HSF; 1.
DR SUPFAM; SSF46785; Winged helix' DNA-binding domain; 1.
DR PROSITE; PS00434; HSF_DOMAIN; 1.
PE 3: Inferred from homology;
KW DNA-binding {ECO:0000256|ARBA:ARBA00023125};
KW Reference proteome {ECO:0000313|Proteomes:UP000191024}.
FT DOMAIN 199..223
FT /note="HSF-type DNA-binding"
FT /evidence="ECO:0000259|PROSITE:PS00434"
FT REGION 259..280
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 396..426
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 442..464
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 499..545
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 572..617
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 442..462
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 499..517
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 522..545
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 593..617
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 617 AA; 68392 MW; DEEFD8F2A3B0CAEA CRC64;
MSKYSNQKDP SALNIKDLEN IIEPDDSTAP VIDANSQHPG LATVNDANSV IEDIVNPSLD
PAMMMPQPRT ASQEITQFSP SIPVASLAPH DQNIVRRGTP VGIYQPQGSP SAGQAQLHEN
LLSDTLLMPY RTRFLQNPNH RPSPPPNKRK LTATKTRPAF INKLWSMVND TTNQKLIKWS
DDGKSFIVTN REKFVHEILP KYFKHSNFAS FVRQLNMYGW HKVQDVRSGS IQGSSDERWQ
FKNDHFVRGR EEMLDEIVRQ KPSSNSNNNN NSKDSFGTQT NEDMDIGIML NELETVKFNQ
MAIAEDLKRM SKDNEMLWKE NMLARERHQA QQQALNKILH LLASLLGSNT TKLLGGDLIN
ELTRTNSNME NQAAAHPWDP THAAPIARPR LLLKNRTTPV PTSPDEGSIY HTNSRNASAS
TMPQTAGISP IQELDRWSIH QPSTASEATS PGFGSSRISE VPFEPQSPAV DTTFLNDLQT
NIKHQGESIQ ELQDWISRIS PDEDPHGGAH HSEPEQHAAS HVTMLPDSST MGSGPGSGSG
HGTASVYEDT AASTQPAHAK FDLQDYLSTP ANTALTPLLQ EESPAGSPAQ MDDNPKSRKR
SDAEIQELPN PTKKQHL
//
