SKN7_CHATD
ID SKN7_CHATD Reviewed; 765 AA.
AC G0SB31;
DT 20-DEC-2017, integrated into UniProtKB/Swiss-Prot.
DT 19-OCT-2011, sequence version 1.
DT 25-MAY-2022, entry version 59.
DE RecName: Full=Transcription factor SKN7;
GN Name=SKN7 {ECO:0000303|PubMed:26727489}; ORFNames=CTHT_0048700;
OS Chaetomium thermophilum (strain DSM 1495 / CBS 144.50 / IMI 039719).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Sordariomycetidae; Sordariales; Chaetomiaceae; Chaetomium.
OX NCBI_TaxID=759272;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 1495 / CBS 144.50 / IMI 039719;
RX PubMed=21784248; DOI=10.1016/j.cell.2011.06.039;
RA Amlacher S., Sarges P., Flemming D., van Noort V., Kunze R., Devos D.P.,
RA Arumugam M., Bork P., Hurt E.;
RT "Insight into structure and assembly of the nuclear pore complex by
RT utilizing the genome of a eukaryotic thermophile.";
RL Cell 146:277-289(2011).
RN [2] {ECO:0007744|PDB:5D5W, ECO:0007744|PDB:5D5X, ECO:0007744|PDB:5D5Y}
RP X-RAY CRYSTALLOGRAPHY (1.03 ANGSTROMS) OF 40-143 AND 160-209 IN COMPLEX
RP WITH DNA, SUBUNIT, AND MUTAGENESIS OF LYS-100.
RX PubMed=26727489; DOI=10.1038/nsmb.3149;
RA Neudegger T., Verghese J., Hayer-Hartl M., Hartl F.U., Bracher A.;
RT "Structure of human heat-shock transcription factor 1 in complex with
RT DNA.";
RL Nat. Struct. Mol. Biol. 23:140-146(2016).
CC -!- FUNCTION: Transcription factor that is part of a SLN1-YPD1-SKN7 two-
CC component regulatory system, which controls gene expression in response
CC to changes in the osmolarity of the extracellular environment. Under
CC low osmotic conditions, phosphorylated and activated by the
CC phosphorelay intermediate protein YPD1. Also activated in response to
CC oxidative stress, independent on the two-component regulatory system.
CC Regulates heat shock genes in response to oxidative stress and genes
CC involved in cell wall integrity in response to osmotic changes.
CC {ECO:0000250|UniProtKB:P38889}.
CC -!- SUBUNIT: Homotrimer. {ECO:0000269|PubMed:26727489}.
CC -!- INTERACTION:
CC G0SB31; G0SB31: SKN7; NbExp=4; IntAct=EBI-16190261, EBI-16190261;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:P38889}.
CC -!- DOMAIN: Homotrimerization occurs through formation of a three-stranded
CC coiled-coil structure generated by intermolecular interactions between
CC HR-A/B regions allowing DNA-binding activity.
CC {ECO:0000269|PubMed:26727489}.
CC -!- SIMILARITY: Belongs to the SKN7 family. {ECO:0000305}.
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DR EMBL; GL988044; EGS19411.1; -; Genomic_DNA.
DR RefSeq; XP_006695233.1; XM_006695170.1.
DR PDB; 5D5W; X-ray; 2.35 A; B=40-143.
DR PDB; 5D5X; X-ray; 2.40 A; B/E=40-143.
DR PDB; 5D5Y; X-ray; 1.03 A; A/B=160-209.
DR PDB; 5D5Z; X-ray; 1.70 A; A/B/C/D/E=160-209.
DR PDB; 5D60; X-ray; 1.90 A; A/B/C/D=160-220.
DR PDBsum; 5D5W; -.
DR PDBsum; 5D5X; -.
DR PDBsum; 5D5Y; -.
DR PDBsum; 5D5Z; -.
DR PDBsum; 5D60; -.
DR AlphaFoldDB; G0SB31; -.
DR SMR; G0SB31; -.
DR DIP; DIP-61979N; -.
DR STRING; 759272.G0SB31; -.
DR EnsemblFungi; EGS19411; EGS19411; CTHT_0048700.
DR GeneID; 18258908; -.
DR KEGG; cthr:CTHT_0048700; -.
DR eggNOG; KOG0519; Eukaryota.
DR eggNOG; KOG0627; Eukaryota.
DR HOGENOM; CLU_008776_2_0_1; -.
DR OrthoDB; 1154048at2759; -.
DR Proteomes; UP000008066; Unassembled WGS sequence.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0001228; F:DNA-binding transcription activator activity, RNA polymerase II-specific; IEA:InterPro.
DR GO; GO:0042802; F:identical protein binding; IPI:IntAct.
DR GO; GO:0043565; F:sequence-specific DNA binding; IEA:InterPro.
DR GO; GO:0000160; P:phosphorelay signal transduction system; IEA:UniProtKB-KW.
DR Gene3D; 1.10.10.10; -; 1.
DR InterPro; IPR011006; CheY-like_superfamily.
DR InterPro; IPR000232; HSF_DNA-bd.
DR InterPro; IPR027725; HSF_fam.
DR InterPro; IPR001789; Sig_transdc_resp-reg_receiver.
DR InterPro; IPR027718; TF_Skn7.
DR InterPro; IPR036388; WH-like_DNA-bd_sf.
DR InterPro; IPR036390; WH_DNA-bd_sf.
DR PANTHER; PTHR10015; PTHR10015; 1.
DR PANTHER; PTHR10015:SF361; PTHR10015:SF361; 1.
DR Pfam; PF00447; HSF_DNA-bind; 1.
DR Pfam; PF00072; Response_reg; 1.
DR PRINTS; PR00056; HSFDOMAIN.
DR SMART; SM00415; HSF; 1.
DR SMART; SM00448; REC; 1.
DR SUPFAM; SSF46785; SSF46785; 1.
DR SUPFAM; SSF52172; SSF52172; 1.
DR PROSITE; PS00434; HSF_DOMAIN; 1.
DR PROSITE; PS50110; RESPONSE_REGULATORY; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Coiled coil; DNA-binding; Nucleus; Phosphoprotein;
KW Reference proteome; Transcription; Transcription regulation;
KW Two-component regulatory system.
FT CHAIN 1..765
FT /note="Transcription factor SKN7"
FT /id="PRO_0000442464"
FT DOMAIN 398..514
FT /note="Response regulatory"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00169"
FT REGION 1..42
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 40..145
FT /note="DNA-binding domain"
FT /evidence="ECO:0000305|PubMed:26727489"
FT REGION 160..220
FT /note="Hydrophobic repeat HR-A/B"
FT /evidence="ECO:0000305|PubMed:26727489"
FT REGION 371..391
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 542..765
FT /note="Transactivation domain"
FT /evidence="ECO:0000305|PubMed:26727489"
FT REGION 550..647
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 686..765
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 157..198
FT /evidence="ECO:0000255"
FT COMPBIAS 1..41
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 371..386
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 623..643
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 449
FT /note="4-aspartylphosphate"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00169"
FT MUTAGEN 100
FT /note="K->M: Abolishes the binding to SSRE (SLN1 star
FT response element) motifs in DNA, but preserves binding to
FT HSE (heat-shock element) motifs."
FT /evidence="ECO:0000269|PubMed:26727489"
FT HELIX 42..51
FT /evidence="ECO:0007829|PDB:5D5W"
FT HELIX 54..56
FT /evidence="ECO:0007829|PDB:5D5W"
FT TURN 57..59
FT /evidence="ECO:0007829|PDB:5D5W"
FT STRAND 60..62
FT /evidence="ECO:0007829|PDB:5D5W"
FT STRAND 66..72
FT /evidence="ECO:0007829|PDB:5D5W"
FT HELIX 74..80
FT /evidence="ECO:0007829|PDB:5D5W"
FT HELIX 82..85
FT /evidence="ECO:0007829|PDB:5D5W"
FT HELIX 91..100
FT /evidence="ECO:0007829|PDB:5D5W"
FT STRAND 118..125
FT /evidence="ECO:0007829|PDB:5D5W"
FT HELIX 135..137
FT /evidence="ECO:0007829|PDB:5D5W"
FT HELIX 161..207
FT /evidence="ECO:0007829|PDB:5D5Y"
FT HELIX 215..219
FT /evidence="ECO:0007829|PDB:5D60"
SQ SEQUENCE 765 AA; 81456 MW; 386204E161FC0670 CRC64;
MPPTNGEGGS QQPQQQQQQQ QQQQQQQQQQ QQQQQGGSGS SDFVRKLYKM LEDPSYHSVV
RWSDDGDSFV VLENEKFTKT ILPKHFKHSN FASFVRQLNK YDFHKVRHND ENGESPYGRD
AWEFKHPEFR ADRKDNLDNI RRKAPAPRKQ QQSEEAFNAS QQQIAALSES LQATQQQLQA
LQQQCYELEK TNRLLVSEVM TLQKMVKAQN QASNEIINHL GSMEDRRRNN RGATQAAPNF
HAGAMSFLTD GAEEPAPELR RARELLSVVG PDLQANRELE RLYMTYNQNG APAEPAATNS
SAVMFTQAAA PGTQATAPGM PLVHNPLNDP QNMMYPVAQT PSIDPSFHTD QMHNMPYSRP
LSNPAVVAET SSSQITPSQI TPPPKDQMSS MWRDKKPRVL LVEDDKTCAR IGAKFLSTLD
CGVDTAGDGL EAVERINQDS TRFDLIFMDI IMPNMDGVSA TAMIRMVSPH VPIIAMTSNI
RGEDINTYFQ YGMNDVLAKP FTRDNMSRLL RRHLAHLLKD PQSAASTGIV LTTDDLTLAG
QTAGPATTGV GVGVAGAPSG GAHGPGPPAQ HQQGYAMAPP TTMQPAPPQV KFEQSPTAAP
APGLDPSSAA AAPTWQSTNP AGVQLQPPPP PTPTQPSPTS AAPPAGLDPA SAVAAAAAAA
AAAAAAAASM TPGGYLAAAP PPPPPPGAMV LTPAGTPTGV GHPAPSGAGS AAGARGPPGP
GPVGPGSVVD DSRPEKRQRL MQGGYASVSG HGHGHPGVGV AGFVQ
