ID A0A1V9YU87_9STRA Unreviewed; 184 AA.
AC A0A1V9YU87;
DT 07-JUN-2017, integrated into UniProtKB/TrEMBL.
DT 07-JUN-2017, sequence version 1.
DT 27-MAR-2024, entry version 25.
DE RecName: Full=HSF-type DNA-binding domain-containing protein {ECO:0000259|SMART:SM00415};
GN ORFNames=ACHHYP_06384 {ECO:0000313|EMBL:OQR89268.1};
OS Achlya hypogyna.
OC Eukaryota; Sar; Stramenopiles; Oomycota; Saprolegniales; Saprolegniaceae;
OC Achlya.
OX NCBI_TaxID=1202772 {ECO:0000313|EMBL:OQR89268.1, ECO:0000313|Proteomes:UP000243579};
RN [1] {ECO:0000313|EMBL:OQR89268.1, ECO:0000313|Proteomes:UP000243579}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 48635 {ECO:0000313|EMBL:OQR89268.1,
RC ECO:0000313|Proteomes:UP000243579};
RX PubMed=25527045; DOI=10.1093/gbe/evu276;
RA Misner I., Blouin N., Leonard G., Richards T.A., Lane C.E.;
RT "The secreted proteins of Achlya hypogyna and Thraustotheca clavata
RT identify the ancestral oomycete secretome and reveal gene acquisitions by
RT horizontal gene transfer.";
RL Genome Biol. Evol. 7:120-135(2014).
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
CC -!- SIMILARITY: Belongs to the HSF family. {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:OQR89268.1}.
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DR EMBL; JNBR01000869; OQR89268.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1V9YU87; -.
DR STRING; 1202772.A0A1V9YU87; -.
DR OrthoDB; 1117127at2759; -.
DR Proteomes; UP000243579; 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:UP000243579}.
FT DOMAIN 32..127
FT /note="HSF-type DNA-binding"
FT /evidence="ECO:0000259|SMART:SM00415"
FT REGION 1..31
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 134..161
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 9..31
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 184 AA; 21552 MW; 34FAB5EBCE067267 CRC64;
MDAILNPYDE QDMSHDDDHD DDHPHTSTSS EKPKFYMEKL HCLLDDCPAD IALWNADGTA
FTVLDAPAFE RRVLPLYFKR IKFDSFARQL NSYGFKRGKK RHGHIYEFQH PQFRRGERDQ
LPTMKSRMGA PDTQETLQTR IDQLTDVTET LKAEVDAMKE MLHMLLQKKL LKAKQRQRAA
SRDE
//
