EAF1_YARLI
ID EAF1_YARLI Reviewed; 967 AA.
AC Q6C7K8;
DT 20-DEC-2005, integrated into UniProtKB/Swiss-Prot.
DT 16-AUG-2004, sequence version 1.
DT 03-AUG-2022, entry version 107.
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=YALI0D27258g;
OS Yarrowia lipolytica (strain CLIB 122 / E 150) (Yeast) (Candida lipolytica).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Dipodascaceae; Yarrowia.
OX NCBI_TaxID=284591;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CLIB 122 / E 150;
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; CR382130; CAG81560.1; -; Genomic_DNA.
DR RefSeq; XP_503354.1; XM_503354.1.
DR AlphaFoldDB; Q6C7K8; -.
DR SMR; Q6C7K8; -.
DR STRING; 4952.CAG81560; -.
DR PRIDE; Q6C7K8; -.
DR EnsemblFungi; CAG81560; CAG81560; YALI0_D27258g.
DR GeneID; 2910300; -.
DR KEGG; yli:YALI0D27258g; -.
DR VEuPathDB; FungiDB:YALI0_D27258g; -.
DR HOGENOM; CLU_006174_0_1_1; -.
DR InParanoid; Q6C7K8; -.
DR OMA; LNTHETH; -.
DR Proteomes; UP000001300; Chromosome D.
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 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..967
FT /note="Chromatin modification-related protein EAF1"
FT /id="PRO_0000065824"
FT DOMAIN 195..276
FT /note="HSA"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00549"
FT DOMAIN 469..529
FT /note="Myb-like"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00133"
FT REGION 60..97
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 264..283
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 311..352
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 587..621
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 653..680
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 774..806
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 864..967
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 72..97
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 653..674
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 787..806
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 967 AA; 108946 MW; B18FC53C7BA208FF CRC64;
MMDPRQETCG DIVSTRKRRL EELYYVSLHP RYPQGLDAKQ KLKQFQDQFD LTQNRLFDEN
KLPKAVEEPK PVPTLQTSTP DAGSSPELKR RRTSSIAQLS PTFSRTSLKT NEQQLQEMLL
FLVPSNIPEP TTETKSLAEL YYTTQTLPLS KLIPSAHKTL TTDSYHLALL EGKLAVAHAR
IEELKRAGKW GPRQPKRFQD PIRRKTHWDH VLDEMEWMST DFREERKFKQ AMACEIAFSV
LEYHKYGKEA CCVKTKPIKF LPEEINESED TESKMDIDTS MPPPSINPVE VTNISAADSV
TVVDYDTLLS QPRTLSSTEE SEDKPEEPST DSEEVVGGEV PKRPAAPKLP ESSPFKLYAS
VDKLDPLSKA LFDNLPVTTP PGSAVNALQV PYSDPLDNSK LAPVTHLLAA PPEQDDWWSV
CLEDSPADED PLPLRSNTRS TLFNSETMRR HVVIKAPQPP QTKYLDFRTP TMWLLADDSQ
LLRLVKEYSY NWDIVSAHML PQKTYGFTAN IERRTSWQCF ERWFQLNPTF SLTDLRGPYA
QAAQQWMAAA AKAQAQSKRR ISPLGVSNES IQRGHRKLRW ASMFDGIRKS MRKRETTPRP
NPQPPRKSQL SESNKKDIAS PLDLCKMKFE QDKNLAKAYA QQRMMPGQMP GQMPPVPSNI
PANRQFPGQR PPPPQTAAQI QAHTQAQARA AAAASGHMQQ RMAGVGMNRM PGQMNDQHQM
MQFDRQRQLM EQQKMLQQQQ QQQFMRTQGQ VPPQPGQVQG QVNQNVQGAQ VAAGQAGMAQ
RPAGQIPQGQ MPAQQGQVPP GQAGNQAQMM RPNMRMRPGG PQAAAPNEHL NALIRQLQNQ
NPALSLEAAT KLAHVQVQRF VQKQQRVARQ AQGQTPPQGQ MRPGQPQGQP SPQMRSGSST
PMNMQSPQLM NVQLQQQQQQ RSASPGQSPA QQHAMLMRMN QQQQQQQQQQ QNQGQTQGQN
QGQGPSE
