ID A5E351_LODEL Unreviewed; 1003 AA.
AC A5E351;
DT 12-JUN-2007, integrated into UniProtKB/TrEMBL.
DT 12-JUN-2007, sequence version 1.
DT 27-MAR-2024, entry version 81.
DE RecName: Full=HSF-type DNA-binding domain-containing protein {ECO:0000259|PROSITE:PS00434};
GN ORFNames=LELG_04038 {ECO:0000313|EMBL:EDK45859.1};
OS Lodderomyces elongisporus (strain ATCC 11503 / CBS 2605 / JCM 1781 / NBRC
OS 1676 / NRRL YB-4239) (Yeast) (Saccharomyces elongisporus).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Debaryomycetaceae; Candida/Lodderomyces clade;
OC Lodderomyces.
OX NCBI_TaxID=379508 {ECO:0000313|EMBL:EDK45859.1, ECO:0000313|Proteomes:UP000001996};
RN [1] {ECO:0000313|EMBL:EDK45859.1, ECO:0000313|Proteomes:UP000001996}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 11503 / BCRC 21390 / CBS 2605 / JCM 1781 / NBRC 1676 /
RC NRRL YB-4239 {ECO:0000313|Proteomes:UP000001996};
RX PubMed=19465905; DOI=10.1038/nature08064;
RA Butler G., Rasmussen M.D., Lin M.F., Santos M.A., Sakthikumar S.,
RA Munro C.A., Rheinbay E., Grabherr M., Forche A., Reedy J.L., Agrafioti I.,
RA Arnaud M.B., Bates S., Brown A.J., Brunke S., Costanzo M.C.,
RA Fitzpatrick D.A., de Groot P.W., Harris D., Hoyer L.L., Hube B., Klis F.M.,
RA Kodira C., Lennard N., Logue M.E., Martin R., Neiman A.M., Nikolaou E.,
RA Quail M.A., Quinn J., Santos M.C., Schmitzberger F.F., Sherlock G.,
RA Shah P., Silverstein K.A., Skrzypek M.S., Soll D., Staggs R.,
RA Stansfield I., Stumpf M.P., Sudbery P.E., Srikantha T., Zeng Q., Berman J.,
RA Berriman M., Heitman J., Gow N.A., Lorenz M.C., Birren B.W., Kellis M.,
RA Cuomo C.A.;
RT "Evolution of pathogenicity and sexual reproduction in eight Candida
RT genomes.";
RL Nature 459:657-662(2009).
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; CH981528; EDK45859.1; -; Genomic_DNA.
DR RefSeq; XP_001525006.1; XM_001524956.1.
DR AlphaFoldDB; A5E351; -.
DR STRING; 379508.A5E351; -.
DR GeneID; 5232143; -.
DR KEGG; lel:LELG_04038; -.
DR VEuPathDB; FungiDB:LELG_04038; -.
DR eggNOG; KOG0627; Eukaryota.
DR HOGENOM; CLU_299170_0_0_1; -.
DR InParanoid; A5E351; -.
DR OMA; GEAHHAT; -.
DR OrthoDB; 1117127at2759; -.
DR Proteomes; UP000001996; Unassembled WGS sequence.
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; IPR036388; WH-like_DNA-bd_sf.
DR InterPro; IPR036390; WH_DNA-bd_sf.
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:UP000001996}.
FT DOMAIN 63..87
FT /note="HSF-type DNA-binding"
FT /evidence="ECO:0000259|PROSITE:PS00434"
FT REGION 173..195
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 246..285
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 352..392
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 426..461
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 477..544
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 564..705
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 796..837
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 867..943
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 957..1003
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 174..188
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 246..263
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 264..278
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 433..452
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 489..503
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 504..544
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 564..704
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 883..929
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 960..976
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 988..1003
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1003 AA; 111111 MW; 3D70F185B2AFE298 CRC64;
MTRKSQGEEL APVPPRVKKN AFVHKLYTML SDPSLDNLIW WSTNNPEQNT FSLYPGKEFA
NCLTRYFKHG NVASFVRQLH MYGFHKVTDP NFNGNNNNNN INNDLSNHNN NINNSGLAGT
TDAYGNLIQS IPGSDPNSVE KEVPPIWEFK HLSGKFKKGD ENSLIYIKRR SSSNHDTRNH
HHHHHHHSYT GDTSYQVRSN SLPQTGHDPY YMHHQYAQQL HQQQSYAGGF YGYDPVTQQP
IFYQQVPTSQ HQQPQQPLQP QQPQYYYSPA PPPHLSHGPP QAVEIARPPF NRPLLVPSDI
PTYQQQHLQQ QQQQEQHLQQ QQQQHLQQQQ QQQQQQQQQQ QQQQQQQQQQ QQQQQLQQQP
PPLRSYGSYP PVEGSKHQYG SSPYHDGRNN SEPQAMTYSY LQQSQPSQTL QPTYTHRLSA
IPPHVQRESP IDPVQRKSPS SSTSNDPVRR RSPLSQSGLH FRKVWDQDAA SRQRNPSLFY
DPLAPAPPAS VTEQKPTPPP PSQFNEQQQQ QQQQQQQHYD GSQRLSARMS AVDPKSSFSV
PSGASLSLSI SRFSSLRPSI ATMKMSQSSQ SSQATLLASP PNSSRKNSSA TPLLAPIPQR
RSSTANAVEH TNNHTPVNGI TNPQTHGQAQ ASTLASSSST TRTTTTGEAH HATTLPPLQT
LPETTAATTT AAAAAATTAT TTTCSRTPSA SSTSPSNPFK KSSISSFHEK LRPSVFEVHS
AGKFTQPLRH HSNGTDSMIN SIAGSVASQS SSTSIFSNGS SISSVHLFPY RTSSFGSIAY
NSSKSSISIA PHEQTMIGNP YSQSSTSTSS NTTNTTAISF DDQRTNTPQS PLHTGPTSLQ
QSYFKLAYSG SFSLYTLPPL LQRSNSAMMK QSPRPPTPNQ NKPKSPLSNA PSNTIDATIS
TGNINNSGNT MTSTTKPNKK ISVTSMLDDS DNYKTKDKGG GETMADVSSE LKIETDMGKV
SPHLNSSNNA HDKSKTPLYL SSLIREERSS QSSDEDSKRR RVV
//
