EAF1_KLULA
ID EAF1_KLULA Reviewed; 1005 AA.
AC Q6CMB8;
DT 20-DEC-2005, integrated into UniProtKB/Swiss-Prot.
DT 16-AUG-2004, sequence version 1.
DT 03-AUG-2022, entry version 113.
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=KLLA0E21538g;
OS Kluyveromyces lactis (strain ATCC 8585 / CBS 2359 / DSM 70799 / NBRC 1267 /
OS NRRL Y-1140 / WM37) (Yeast) (Candida sphaerica).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Kluyveromyces.
OX NCBI_TaxID=284590;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 8585 / CBS 2359 / DSM 70799 / NBRC 1267 / NRRL Y-1140 / WM37;
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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; CR382125; CAH00008.1; -; Genomic_DNA.
DR RefSeq; XP_454921.1; XM_454921.1.
DR AlphaFoldDB; Q6CMB8; -.
DR SMR; Q6CMB8; -.
DR STRING; 28985.XP_454921.1; -.
DR PRIDE; Q6CMB8; -.
DR EnsemblFungi; CAH00008; CAH00008; KLLA0_E21451g.
DR GeneID; 2894627; -.
DR KEGG; kla:KLLA0_E21451g; -.
DR eggNOG; ENOG502QSEY; Eukaryota.
DR HOGENOM; CLU_004795_0_0_1; -.
DR InParanoid; Q6CMB8; -.
DR OMA; WLLRTEM; -.
DR Proteomes; UP000000598; Chromosome E.
DR GO; GO:0035267; C:NuA4 histone acetyltransferase complex; IEA:EnsemblFungi.
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:EnsemblFungi.
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; 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..1005
FT /note="Chromatin modification-related protein EAF1"
FT /id="PRO_0000065820"
FT DOMAIN 386..460
FT /note="HSA"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00549"
FT DOMAIN 684..744
FT /note="Myb-like"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00133"
FT REGION 72..180
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 193..214
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 222..241
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 468..543
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 807..844
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 874..930
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 981..1005
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 93..115
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 116..179
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 227..241
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 470..484
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 517..543
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 874..926
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1005 AA; 114703 MW; C01058C4E0F77D04 CRC64;
MSSASKGNAT GSKSPEQLLE ERRHLLVQLY CISQITELKN VENHERIGKE IEKFLDQHTL
IKDKPIDINA LPKFRPRDVS SDRKLNNRSK SSSPSEVKRE LKKQRSKDVS PSGSEEHDVD
TQTLPQSQTR VVPRVQSQQS IQQSSRQSMV QAQSSRQLQQ QQLQKQRSVS PTQKLPITHN
NVPPVVVQAH MEPKSVQYPE TQSKPSTSGK RLLDEEQQDI SENQISKRQR LDSGNLSNST
AARNAATMEI PPHPYSQMID ISQLHADPTP IGVKEPQPYI IESIINNVSK EERKTFFEDD
INVKEAVYMI TKENAPTKLA KGMPIQEIKY LSQTLPLLRL IPQSQKALTT DLINTALNER
RITVVASRIE ELRRLNLWSL RQPRKFIDPV TASQPVTHHN VLIEEAKWMR EDFRESLNYK
IAMCTQMAQA VMEFWTYGKV CCINCKSIPP PSKDIEDIAS SQDMGTKIST VEPEQKDKES
NTSPDQSNDD GSSKIAEDVE MSEDGVKSST GLTDGSEAVE EKSENGIKEG DKETDKNSSE
EPTIDIQKLL KRVNPKDEIV APSLPVTSME VYLAKKSSSP FRNYIDIKEL STLGAAISNS
LPLYGLLDEK NLDSSRPLPF EPVSKAISPL DEDHFMKLVE KQFVDEEPSL VPLSKRRGMF
YGNRRSHYLR PPNAPSLRYL KFRTPTIWLP EDDQELVKNI NQYAYNWDLI SSQMSNHHKR
EYVSNIERRT PWQCFERFVQ LNEKFNIADM KGPKAHNAQI WLYEAHKLQQ QQKRRISPLG
VGSESIQRGH RRLRWASMFE AMRKCIKKRE NAPRPNPSQP RKPFDVKNMS VPTPQEMSDL
KAQRDEALRR DMQIKRAAKQ RMQMAQLQQG KLPLTTASSP NLPMANNPNS KDSRIRSKQS
TPQSAPPLGE KEKVTTQTPT QRNTKPANKR EIIEGYAKKI LFQKPNFTPE LALMAAENIY
RSLPLSDQQR KTVIYDNVAQ PKVRPPEMKH SSPTPQEILQ RAQKK