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Database: UniProt
Entry: H2AS68_KAZAF
LinkDB: H2AS68_KAZAF
Original site: H2AS68_KAZAF 
ID   H2AS68_KAZAF            Unreviewed;       613 AA.
AC   H2AS68;
DT   21-MAR-2012, integrated into UniProtKB/TrEMBL.
DT   21-MAR-2012, sequence version 1.
DT   27-MAR-2024, entry version 61.
DE   RecName: Full=HSF-type DNA-binding domain-containing protein {ECO:0000259|PROSITE:PS00434};
GN   Name=KAFR0C02250 {ECO:0000313|EMBL:CCF57218.1};
GN   ORFNames=KAFR_0C02250 {ECO:0000313|EMBL:CCF57218.1};
OS   Kazachstania africana (strain ATCC 22294 / BCRC 22015 / CBS 2517 / CECT
OS   1963 / NBRC 1671 / NRRL Y-8276) (Yeast) (Kluyveromyces africanus).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Saccharomycetaceae; Kazachstania.
OX   NCBI_TaxID=1071382 {ECO:0000313|EMBL:CCF57218.1, ECO:0000313|Proteomes:UP000005220};
RN   [1] {ECO:0000313|EMBL:CCF57218.1, ECO:0000313|Proteomes:UP000005220}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 22294 / BCRC 22015 / CBS 2517 / CECT 1963 / NBRC 1671 /
RC   NRRL Y-8276 {ECO:0000313|Proteomes:UP000005220};
RX   PubMed=22123960; DOI=10.1073/pnas.1112808108;
RA   Gordon J.L., Armisen D., Proux-Wera E., OhEigeartaigh S.S., Byrne K.P.,
RA   Wolfe K.H.;
RT   "Evolutionary erosion of yeast sex chromosomes by mating-type switching
RT   accidents.";
RL   Proc. Natl. Acad. Sci. U.S.A. 108:20024-20029(2011).
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; HE650823; CCF57218.1; -; Genomic_DNA.
DR   RefSeq; XP_003956353.1; XM_003956304.1.
DR   AlphaFoldDB; H2AS68; -.
DR   STRING; 1071382.H2AS68; -.
DR   GeneID; 13885137; -.
DR   KEGG; kaf:KAFR_0C02250; -.
DR   eggNOG; KOG0627; Eukaryota.
DR   HOGENOM; CLU_017670_1_0_1; -.
DR   InParanoid; H2AS68; -.
DR   OrthoDB; 1117127at2759; -.
DR   Proteomes; UP000005220; Chromosome 3.
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:UP000005220}.
FT   DOMAIN          191..215
FT                   /note="HSF-type DNA-binding"
FT                   /evidence="ECO:0000259|PROSITE:PS00434"
FT   REGION          33..52
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          375..399
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          411..473
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          564..613
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        411..434
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        444..471
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        573..596
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   613 AA;  70360 MW;  5F7C9D425FDC27C2 CRC64;
     MNNGKQDTNS NELSLLNDEE IDQILHQNNI FPDEIILPPN DTPTTTTESI QRQKDTDEIN
     DIINPSIIDI PRDVQDRSLT LARDASNIYH PATTDLIRRP TTPLQNSFQR PLPADQLYSS
     RILEQNSNYE MSNLTSSTQQ RRYHPHKSRP AFVNKLWSML NDNSNLDLIQ WSNDGKSFVV
     TNREQFVHEI LPKYFKHSNF ASFVRQLNMY GWHKVQDVKS GSIQNSSDEK WQFENEYFQR
     DREDLLEKIV RQKSNSNNTT SKEKIMNTKP ILHLMNEPST GLDNTIDING GSTTTDHVSK
     VLNELEAIKY NQLAISKDLL RINKDNELLW KENMMARERY RSQQQTLEKI FRFLASIMPQ
     KMIMDGVMNN SDNTNSSIDL NSLRNKGNSD NNNSESMNTN INEKNLFDEL VNNEGNNNNS
     NNNNYDTLNR ASSPLRPQPR YLLKNRSNKG QSMTTTPTSA ATSSSPNKIL ELNDDDNMHP
     IVEEYDTNEN ETNRGNASDD SLEFLNNLQS NISEQDNRIQ HLEDIIIQEF SPKNNVMHAN
     ASNNNGNSNT ADFSLHDYFN SDAIPNSPIG ESDEGSKYKR YIEEISDDES RHLHDDATTT
     TTSTANIKKP RRS
//
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