EAF1_ASHGO
ID EAF1_ASHGO Reviewed; 957 AA.
AC Q756L0;
DT 20-DEC-2005, integrated into UniProtKB/Swiss-Prot.
DT 09-JAN-2013, sequence version 2.
DT 03-AUG-2022, entry version 119.
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=AER244C;
OS Ashbya gossypii (strain ATCC 10895 / CBS 109.51 / FGSC 9923 / NRRL Y-1056)
OS (Yeast) (Eremothecium gossypii).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Eremothecium.
OX NCBI_TaxID=284811;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 10895 / CBS 109.51 / FGSC 9923 / NRRL Y-1056;
RX PubMed=15001715; DOI=10.1126/science.1095781;
RA Dietrich F.S., Voegeli S., Brachat S., Lerch A., Gates K., Steiner S.,
RA Mohr C., Poehlmann R., Luedi P., Choi S., Wing R.A., Flavier A.,
RA Gaffney T.D., Philippsen P.;
RT "The Ashbya gossypii genome as a tool for mapping the ancient Saccharomyces
RT cerevisiae genome.";
RL Science 304:304-307(2004).
RN [2]
RP GENOME REANNOTATION, AND SEQUENCE REVISION TO 38.
RC STRAIN=ATCC 10895 / CBS 109.51 / FGSC 9923 / NRRL Y-1056;
RX PubMed=23749448; DOI=10.1534/g3.112.002881;
RA Dietrich F.S., Voegeli S., Kuo S., Philippsen P.;
RT "Genomes of Ashbya fungi isolated from insects reveal four mating-type
RT loci, numerous translocations, lack of transposons, and distinct gene
RT duplications.";
RL G3 (Bethesda) 3:1225-1239(2013).
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; AE016818; AAS52925.2; -; Genomic_DNA.
DR RefSeq; NP_985101.2; NM_210455.2.
DR AlphaFoldDB; Q756L0; -.
DR SMR; Q756L0; -.
DR STRING; 33169.AAS52925; -.
DR PRIDE; Q756L0; -.
DR EnsemblFungi; AAS52925; AAS52925; AGOS_AER244C.
DR GeneID; 4621311; -.
DR KEGG; ago:AGOS_AER244C; -.
DR eggNOG; ENOG502QSEY; Eukaryota.
DR HOGENOM; CLU_004795_0_0_1; -.
DR InParanoid; Q756L0; -.
DR OMA; KPLDCKN; -.
DR Proteomes; UP000000591; Chromosome V.
DR GO; GO:0035267; C:NuA4 histone acetyltransferase complex; IBA:GO_Central.
DR GO; GO:0000812; C:Swr1 complex; IBA:GO_Central.
DR GO; GO:0003682; F:chromatin binding; IBA:GO_Central.
DR GO; GO:0006325; P:chromatin organization; IEA:UniProtKB-KW.
DR GO; GO:0006281; P:DNA repair; IBA:GO_Central.
DR GO; GO:0043967; P:histone H4 acetylation; IBA:GO_Central.
DR GO; GO:0065003; P:protein-containing complex assembly; IEA:EnsemblFungi.
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..957
FT /note="Chromatin modification-related protein EAF1"
FT /id="PRO_0000065813"
FT DOMAIN 334..409
FT /note="HSA"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00549"
FT DOMAIN 576..638
FT /note="Myb-like"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00133"
FT REGION 72..115
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 160..196
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 703..804
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 922..957
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 99..115
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 164..196
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 735..754
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 759..804
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 957 AA; 109651 MW; F191E1F89D487395 CRC64;
MSVLKKDSTS EKRTQLESIL EERNNKLTQL FWLSRLNELK SGGDLQSVRQ ELAEFLVQND
LTKNLTFDIS SLRTYRPQEP PMDRRPLRSK SSTPLENGTI NRKREDAEPH MEETRKRLRE
HIIPEEDDDR EHEQRPVKLQ KVGLSHDEEL PKRLEPPTIP IRKISSAGDN QETGSVIGEK
KSEQPVSTSR NRPIHTQLST NPFYQHMDIS TLRAEPTPVE VKRKRNYIID EIIKTQSKST
DTSDSHSTAG GRDSVYLVMK ETVPSKLARA IPLSELKYVS QTLPLIRLIP PTHKALTTDL
YNTALNEGRI TVVSSRIEEL RRLNLWSLRQ PKKFLDPWRQ KQPSTHRGYM LEEARWMRED
FHEFKKFKVS VCAVNSKAIM DYWKYGKACC IKRRSISHLQ KSVNEVQEAD TLGNIDDLLN
KISDKKLAGM IEEQKKVIAV DAKLSSSKIA PSEEIHAPHI WEDPLDELDE QGCKPIFKTY
MSYNGVSPLE KTILEDLPIY KGILDEQAAE DNSVPFVPIS KSTVLLDDDY FMKLIEKDIV
DDEPSFVALS KRRGMFYGNR RSHYLKPPSA PALRYLKFRT PTIWSPEDDQ ELVKNINQYA
YNWDLIGALV SSSNGRSYIS NIERRTPWQC FERFVQLNEK FSVHDMKGPR ANAAQMWLYE
AHKLQQQQKR RISPLGVGSE SIQRGHRRLR WATMFEAMRK TIKKRENAPR PNPSQPRKPL
DVKSAAVPTP AEMSELKAQR DETLRREGQM RRAAKQRIHL AQLQQQQQRV QQDVVQQRPQ
SRSQPDPPLS QQIPRVQSPR PQQPLAQQLI EDKGKLLPGV SVSAPTSKEA SNNGKNLMAL
RQVQSSPVNG DLQKATAQVP PRGPNKPLTE KEIIESYARK IIAQKPDFTP ELALKAAESY
YQNVTLKQNT IGKQIVSQPL SAATVSTPPS NGRAVHKIRS PTPQEILQRI QQKKNDS
