ID M3JWZ6_CANMX Unreviewed; 1012 AA.
AC M3JWZ6;
DT 01-MAY-2013, integrated into UniProtKB/TrEMBL.
DT 01-MAY-2013, sequence version 1.
DT 27-MAR-2024, entry version 41.
DE RecName: Full=Chromatin modification-related protein EAF1 {ECO:0000256|ARBA:ARBA00018561};
DE AltName: Full=ESA1-associated factor 1 {ECO:0000256|ARBA:ARBA00032084};
DE AltName: Full=Vacuolar import and degradation protein 21 {ECO:0000256|ARBA:ARBA00029670};
GN ORFNames=G210_2218 {ECO:0000313|EMBL:EMG47445.1};
OS Candida maltosa (strain Xu316) (Yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Debaryomycetaceae; Candida/Lodderomyces clade; Candida.
OX NCBI_TaxID=1245528 {ECO:0000313|EMBL:EMG47445.1, ECO:0000313|Proteomes:UP000011777};
RN [1] {ECO:0000313|EMBL:EMG47445.1, ECO:0000313|Proteomes:UP000011777}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Xu316 {ECO:0000313|Proteomes:UP000011777};
RA Yu J., Wang Q., Geng X., Bao W., He P., Cai J.;
RT "Genome sequence of Candida maltosa Xu316, a potential industrial strain
RT for xylitol and ethanol production.";
RL Submitted (FEB-2013) to the EMBL/GenBank/DDBJ databases.
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. {ECO:0000256|ARBA:ARBA00025178}.
CC -!- SIMILARITY: Belongs to the EAF1 family.
CC {ECO:0000256|ARBA:ARBA00008913}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:EMG47445.1}.
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DR EMBL; AOGT01001572; EMG47445.1; -; Genomic_DNA.
DR AlphaFoldDB; M3JWZ6; -.
DR STRING; 1245528.M3JWZ6; -.
DR eggNOG; ENOG502RGMX; Eukaryota.
DR HOGENOM; CLU_006174_0_1_1; -.
DR OMA; HDWMLAR; -.
DR OrthoDB; 1334563at2759; -.
DR Proteomes; UP000011777; Unassembled WGS sequence.
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 CDD; cd00167; SANT; 1.
DR Gene3D; 1.10.10.60; Homeodomain-like; 1.
DR InterPro; IPR009057; Homeobox-like_sf.
DR InterPro; IPR014012; HSA_dom.
DR InterPro; IPR001005; SANT/Myb.
DR PANTHER; PTHR46459:SF1; E1A-BINDING PROTEIN P400; 1.
DR PANTHER; PTHR46459; E1A-BINDING PROTEIN P400-RELATED; 1.
DR Pfam; PF07529; HSA; 1.
DR Pfam; PF13921; Myb_DNA-bind_6; 1.
DR SMART; SM00717; SANT; 1.
DR SUPFAM; SSF46689; Homeodomain-like; 1.
DR PROSITE; PS51204; HSA; 1.
PE 3: Inferred from homology;
KW Chromatin regulator {ECO:0000256|ARBA:ARBA00022853};
KW DNA damage {ECO:0000256|ARBA:ARBA00022763};
KW DNA repair {ECO:0000256|ARBA:ARBA00023204};
KW Reference proteome {ECO:0000313|Proteomes:UP000011777};
KW Transcription {ECO:0000256|ARBA:ARBA00023163};
KW Transcription regulation {ECO:0000256|ARBA:ARBA00023015}.
FT DOMAIN 212..292
FT /note="HSA"
FT /evidence="ECO:0000259|PROSITE:PS51204"
FT REGION 333..363
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 612..645
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 661..680
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 697..794
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 832..879
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 922..1012
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 613..644
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 665..680
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 714..733
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 748..794
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 832..869
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1012 AA; 116267 MW; A5D4A1BE53E07E98 CRC64;
MSETWKSRLI EISHITADPF LRDFSKLHTT DQDKIISLIE YPDNVVEQIF KETIIKSMEE
SMFCPVVPPE ELKKRQETQL EGNVRKIQKN GINSKREIKP SQVKSLKTQQ QIDSEELNAF
LKKSLEDLDV ITAPEHYPTN PQTVSPLAEL YYLTQTLPLI KLLPGSHKVL LTDNFESALA
EGKIAVLYSR IEELKRQGKW SLRQPQKFYD PFKFVRRSKK KSFHWDYLLS EAKWMADDFR
ESSKYRKWCC VIIAEAIEEY WACGKEVCIK RKPIQHLEPE ITEEVNEEII TESAEKVVQE
ASQDTVETII PDSEDMHEPE AIDTALLVAP KDPNEDKQEV IPAPQPSAQQ QPPSSSTSRD
SPSIFKSYVD VHSLKKIDQS IIRNLPTFSP FDNHLQNGLQ PKEPPIATVS RLLYPIENDE
QWYKIILSER HEELNNSNGP PEFQKGLFGS QSHKRFNPLK PPKPPLIKNI EYRSPTIWLP
HDDKRLIHYV AEFCFNWDLI AEHISASSSS VTLKKYESNI ERRTPWQCFE RYIQLNDKFQ
FSDMKGLYAY HAQQWLEQAH RAQSTTKRRI SPLGVGADSI QRGSRKLRWA SMFDAIRKAM
KKREIVAAKM NHRKSTNELQ ANQQQQVQQQ MNAPSPQPNN DRVPTPQELA KLKFERDKSL
HEAHMNQQAT RTRMMQAVAQ QQKQQQLQQQ QQQQQQQQQQ QQQVPPVPPT SAQPHQQLPQ
SSPQLQQQRN VGPASKPVAP RGQQPPLPNG RVSVNHNQGS PQPGPQGNVP VRPPNAQNGQ
VPIKRPTTPN GTPLTNEQIQ HLLQLQKHRR MLQQQQQQQQ QQINNNQQPM RVNAANPQPV
RPNQHLQGHV QTPNPAGQQQ ISGSIPPNQQ QPPQQAPRRI HFPPQQVSMV INEIQKQNPG
LAKEEVTKLA ARYLANLQQQ QQNRLNTQSP QHQQQQQQFR MQQQQIQQMQ RNNVSPNARM
GLAQENQQMP MMQGSPSSPA PQQYNKNQSA SPMSGSPNLQ YSNIPPGRNN GS
//
