ID   A0A0V1PES0_9BILA        Unreviewed;       811 AA.
AC   A0A0V1PES0;
DT   16-MAR-2016, integrated into UniProtKB/TrEMBL.
DT   16-MAR-2016, sequence version 1.
DT   27-MAR-2024, entry version 28.
DE   SubName: Full=Heat shock factor protein 3 {ECO:0000313|EMBL:KRZ94737.1};
GN   Name=HSF3 {ECO:0000313|EMBL:KRZ94737.1};
GN   ORFNames=T08_2445 {ECO:0000313|EMBL:KRZ94737.1};
OS   Trichinella sp. T8.
OC   Eukaryota; Metazoa; Ecdysozoa; Nematoda; Enoplea; Dorylaimia;
OC   Trichinellida; Trichinellidae; Trichinella.
OX   NCBI_TaxID=92180 {ECO:0000313|EMBL:KRZ94737.1, ECO:0000313|Proteomes:UP000054924};
RN   [1] {ECO:0000313|EMBL:KRZ94737.1, ECO:0000313|Proteomes:UP000054924}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ISS272 {ECO:0000313|EMBL:KRZ94737.1};
RA   Korhonen P.K., Edoardo P., Giuseppe L.R., Gasser R.B.;
RT   "Evolution of Trichinella species and genotypes.";
RL   Submitted (JAN-2015) to the EMBL/GenBank/DDBJ databases.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
CC   -!- SIMILARITY: Belongs to the HSF family. {ECO:0000256|ARBA:ARBA00006403,
CC       ECO:0000256|RuleBase:RU004020}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:KRZ94737.1}.
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DR   EMBL; JYDM01000016; KRZ94737.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0V1PES0; -.
DR   Proteomes; UP000054924; 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; 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.
PE   3: Inferred from homology;
KW   Coiled coil {ECO:0000256|SAM:Coils};
KW   DNA-binding {ECO:0000256|ARBA:ARBA00023125};
KW   Reference proteome {ECO:0000313|Proteomes:UP000054924};
KW   Stress response {ECO:0000313|EMBL:KRZ94737.1}.
FT   DOMAIN          6..111
FT                   /note="HSF-type DNA-binding"
FT                   /evidence="ECO:0000259|SMART:SM00415"
FT   REGION          237..282
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          314..339
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          534..565
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          650..760
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          137..164
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COMPBIAS        261..282
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        316..331
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        650..738
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        745..760
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   811 AA;  89389 MW;  7104262836C207CE CRC64;
     MSSKFKVSSF LSTLRFILDS EEYNNAVCWD DTGTVFCIKD QEWLVDVILP KFFRHKNFAS
     FIRQLNNCKS NGFHKVNAVN IVPPLHANVP CFSHKYFLRG EPSLDVNIRR KCYQEKSPPP
     LTRNEETVTY ADVIRVVMRM NEQLSEITKR VSKLEKEMVD ARKYMPNWCI TTFLQLLTAA
     SQKQGTVDLL HLLHMLTQTQ YKANRQNSNG KSVPYVPIVK SQSPKNGLRV NTIGHRKRKQ
     ELNSVESTPP PVVGNDANPS VIAGPTDTTA TPSLPTSGED VSESFAVCTT PAYTDAIMTY
     NNVENQGNVL LDGGCLDPFP PPPPQQQQHQ PQPQPHPAGD SMITYPCTWD LPGFDDISAN
     FLTDDNDSLM NMEFDYYGGI NWRTESADLI TFTGGDRVQR VHSASSTSSF SSCIDENDKN
     STLNKTMEFG QWIMSNNNID GAEENNSNNN SNDNNMLFCP KELTLAEPEA LNSQIDDMFF
     KNLTIPQYSL AIDTNSADHY SLSGNCDFSL TYPTYQEIEF PNSNNLSTVQ EVSAVSNVQP
     SGTQPAPSNE PNNGGMENNT VFKPLTNSGS MLDDDVYLSN AYNDMLNTPK VDELSHEDLI
     AEFLLPMTQN DCETFSNECD LMISIPQPSF VSEQPMAILQ SDVQNLEIPL ANNNPLNNGD
     QGSLNSTGLS SMLSTVPSSA TIQSRDESQL PLVGPENGSQ KEENHINVSS SILGRRSSTT
     SDVPCSDAFQ SSSVKSRKRS KSLILKKQQI QTSGKNSGDT AAANTAAAAA AVGDSGGAEK
     KNDPKAASCL KMFNLTDAKT GKKITCRVIR R
//