EAF1_DEBHA
ID EAF1_DEBHA Reviewed; 1193 AA.
AC Q6BI82;
DT 20-DEC-2005, integrated into UniProtKB/Swiss-Prot.
DT 16-DEC-2008, sequence version 2.
DT 03-AUG-2022, entry version 110.
DE RecName: Full=Chromatin modification-related protein EAF1;
DE AltName: Full=ESA1-associated factor 1;
DE AltName: Full=Vacuolar import and degradation protein 21;
GN Name=EAF1; Synonyms=VID21; OrderedLocusNames=DEHA2G12716g;
OS Debaryomyces hansenii (strain ATCC 36239 / CBS 767 / BCRC 21394 / JCM 1990
OS / NBRC 0083 / IGC 2968) (Yeast) (Torulaspora hansenii).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Debaryomycetaceae; Debaryomyces.
OX NCBI_TaxID=284592;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 36239 / CBS 767 / BCRC 21394 / JCM 1990 / NBRC 0083 / IGC 2968;
RX PubMed=15229592; DOI=10.1038/nature02579;
RA Dujon B., Sherman D., Fischer G., Durrens P., Casaregola S., Lafontaine I.,
RA de Montigny J., Marck C., Neuveglise C., Talla E., Goffard N., Frangeul L.,
RA Aigle M., Anthouard V., Babour A., Barbe V., Barnay S., Blanchin S.,
RA Beckerich J.-M., Beyne E., Bleykasten C., Boisrame A., Boyer J.,
RA Cattolico L., Confanioleri F., de Daruvar A., Despons L., Fabre E.,
RA Fairhead C., Ferry-Dumazet H., Groppi A., Hantraye F., Hennequin C.,
RA Jauniaux N., Joyet P., Kachouri R., Kerrest A., Koszul R., Lemaire M.,
RA Lesur I., Ma L., Muller H., Nicaud J.-M., Nikolski M., Oztas S.,
RA Ozier-Kalogeropoulos O., Pellenz S., Potier S., Richard G.-F.,
RA Straub M.-L., Suleau A., Swennen D., Tekaia F., Wesolowski-Louvel M.,
RA Westhof E., Wirth B., Zeniou-Meyer M., Zivanovic Y., Bolotin-Fukuhara M.,
RA Thierry A., Bouchier C., Caudron B., Scarpelli C., Gaillardin C.,
RA Weissenbach J., Wincker P., Souciet J.-L.;
RT "Genome evolution in yeasts.";
RL Nature 430:35-44(2004).
CC -!- FUNCTION: Component of the NuA4 histone acetyltransferase complex which
CC is involved in transcriptional activation of selected genes principally
CC by acetylation of nucleosomal histone H4 and H2A. The NuA4 complex is
CC also involved in DNA repair (By similarity). {ECO:0000250}.
CC -!- SUBUNIT: Component of the NuA4 histone acetyltransferase complex.
CC {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the EAF1 family. {ECO:0000305}.
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DR EMBL; CR382139; CAG90575.2; -; Genomic_DNA.
DR RefSeq; XP_462089.2; XM_462089.1.
DR AlphaFoldDB; Q6BI82; -.
DR SMR; Q6BI82; -.
DR STRING; 4959.XP_462089.2; -.
DR EnsemblFungi; CAG90575; CAG90575; DEHA2G12716g.
DR GeneID; 2905001; -.
DR KEGG; dha:DEHA2G12716g; -.
DR VEuPathDB; FungiDB:DEHA2G12716g; -.
DR eggNOG; ENOG502QSEY; Eukaryota.
DR HOGENOM; CLU_006174_0_1_1; -.
DR InParanoid; Q6BI82; -.
DR OMA; LNTHETH; -.
DR OrthoDB; 314765at2759; -.
DR Proteomes; UP000000599; Chromosome G.
DR GO; GO:0035267; C:NuA4 histone acetyltransferase complex; IEA:UniProt.
DR GO; GO:0006325; P:chromatin organization; IEA:UniProtKB-KW.
DR GO; GO:0006281; P:DNA repair; IEA:UniProtKB-KW.
DR GO; GO:0016573; P:histone acetylation; IEA:UniProt.
DR CDD; cd00167; SANT; 1.
DR InterPro; IPR009057; Homeobox-like_sf.
DR InterPro; IPR014012; HSA_dom.
DR InterPro; IPR001005; SANT/Myb.
DR Pfam; PF07529; HSA; 1.
DR SMART; SM00573; HSA; 1.
DR SMART; SM00717; SANT; 1.
DR SUPFAM; SSF46689; SSF46689; 1.
DR PROSITE; PS51204; HSA; 1.
DR PROSITE; PS50090; MYB_LIKE; 1.
PE 3: Inferred from homology;
KW Activator; Chromatin regulator; DNA damage; DNA repair; Nucleus;
KW Reference proteome; Transcription; Transcription regulation.
FT CHAIN 1..1193
FT /note="Chromatin modification-related protein EAF1"
FT /id="PRO_0000065817"
FT DOMAIN 253..332
FT /note="HSA"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00549"
FT DOMAIN 586..642
FT /note="Myb-like"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00133"
FT REGION 92..147
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 368..414
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 716..756
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 787..867
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 885..976
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1020..1193
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 92..118
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 119..142
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 375..392
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 722..746
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 787..806
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 827..867
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1020..1038
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1047..1112
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1137..1193
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1193 AA; 133415 MW; C5983FD50702FD17 CRC64;
MMIKEEAEGI LKQRNSKLEE LLHLAADPLL TDISSHKSRV SEFLNDNDIT KEKTFVVSSL
PGVSGSGSFA EAMSQSVSKS IYKVEEAKER TENAAIEQGL KRRTESISDD RKLKISRKSS
SQLSDSRSGS ISKSTSEITK PVAPPVKSQK ENIHLETKDF LNRDIGELEI LSVPEHYPTK
PPNVSSLAEL YYLTQTLPLI KLLPGSHKTL ITENYELALL EGKIAVLYSR IEELKRQGKW
SLRQPKRYYD PYIYTKSNNG KKTFHGDSLL EEGKWMAADF KEGSKYKKAC CVTMAQAVND
YWTYGKVMCI RRKRIWHIGE RREEEEIHGD LETDLVDGAD SMAIDDINVD NDCAPLEITG
NELQNIVVSD DKVSTEPISN DEPQRKEEDD IDSAEVADQE VSEDPSQDKP VDELIPEEEV
ELSSIDVKLL LSRPKPEDEI VPTNLPTFSE DDLKEMGRDS KDSAPFKLHA NLNDLKKIDQ
SIIKNLPKFT AFDNEDSNMP APALKPVDSP MIAVSRLLHP FEEDDEWYKI VLKEGDSHKS
KSNVSSGPPE YQKGLFGFQS HRRFNYLKPP KPPLIKNIEF RSPTIWLPQD DKHLIHYVAE
FCFNWDLISE HLSPSAATLR KYESNIERRT PWQCFERYIQ LNEKFQFSDM KGIYSYQAQS
WLEHAHRAQS TTKRRISPLG VGNESIQRGH RRLRWASLFD AMRKSMKKRE DAIAKLNHRR
TPVDYSANNT NVNSPEASNN GTPGPNNGKR PMDRVPTPAE LSKLKFERDK SIQEAYLNQQ
ATRSRMIAAV AQQQKQQQNN QGNIPRPPSQ GPGPNVGVPP PQRGQIGVQG GPTNTPTGSL
GNQVPPSQQP SQAAQGGMTK RPTTPNGTAY TAEQIQQLLQ IQKQRRLMQQ QNQPGKTGIS
PSQPNTPALM QNMPLSSNKT TVGGSNMPLS GMPNSTQQVS LSQQGQKQQL GPSQRQQVPV
SQPSQGQGSS TGVPANKSRI HFAPAQVSAI INSIQTKNPN LTKEQVTKLA ATYLANIQQQ
QQNRANQQQQ QPPSQHSGAI GQGPAAHRPG QSQSPSNQKK PQVATLTPQE RNQLQMLKAA
KTAQQQQLQH QQQQQQQQQQ QQQQQQQRRP GSPMVPNAPL DPNNMAKLEY EQRKNLLIQK
HQQQQRLGNN SNIPGQSTPN LASMPPSSSS SPSSSVSGPA SNLPNSNKNV PKK
