ID C4YGD1_CANAW Unreviewed; 684 AA.
AC C4YGD1;
DT 28-JUL-2009, integrated into UniProtKB/TrEMBL.
DT 28-JUL-2009, sequence version 1.
DT 27-MAR-2024, entry version 60.
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=CAWG_03107 {ECO:0000313|EMBL:EEQ44813.1};
OS Candida albicans (strain WO-1) (Yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Debaryomycetaceae; Candida/Lodderomyces clade; Candida.
OX NCBI_TaxID=294748 {ECO:0000313|EMBL:EEQ44813.1, ECO:0000313|Proteomes:UP000001429};
RN [1] {ECO:0000313|EMBL:EEQ44813.1, ECO:0000313|Proteomes:UP000001429}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=WO-1 {ECO:0000313|EMBL:EEQ44813.1,
RC ECO:0000313|Proteomes:UP000001429};
RX PubMed=19465905; DOI=10.1038/nature08064;
RA Butler G., Rasmussen M.D., Lin M.F., Santos M.A., Sakthikumar S.,
RA Munro C.A., Rheinbay E., Grabherr M., Forche A., Reedy J.L., Agrafioti I.,
RA Arnaud M.B., Bates S., Brown A.J., Brunke S., Costanzo M.C.,
RA Fitzpatrick D.A., de Groot P.W., Harris D., Hoyer L.L., Hube B., Klis F.M.,
RA Kodira C., Lennard N., Logue M.E., Martin R., Neiman A.M., Nikolaou E.,
RA Quail M.A., Quinn J., Santos M.C., Schmitzberger F.F., Sherlock G.,
RA Shah P., Silverstein K.A., Skrzypek M.S., Soll D., Staggs R.,
RA Stansfield I., Stumpf M.P., Sudbery P.E., Srikantha T., Zeng Q., Berman J.,
RA Berriman M., Heitman J., Gow N.A., Lorenz M.C., Birren B.W., Kellis M.,
RA Cuomo C.A.;
RT "Evolution of pathogenicity and sexual reproduction in eight Candida
RT genomes.";
RL Nature 459:657-662(2009).
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 ---------------------------------------------------------------------------
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; CH672349; EEQ44813.1; -; Genomic_DNA.
DR AlphaFoldDB; C4YGD1; -.
DR PaxDb; 5476-C4YGD1; -.
DR VEuPathDB; FungiDB:CAWG_03107; -.
DR HOGENOM; CLU_006174_1_0_1; -.
DR OMA; HENHINQ; -.
DR Proteomes; UP000001429; Chromosome 4, Supercontig 1.4.
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; SM00573; HSA; 1.
DR SMART; SM00717; SANT; 1.
DR SUPFAM; SSF46689; Homeodomain-like; 1.
DR PROSITE; PS51204; HSA; 1.
DR PROSITE; PS50090; MYB_LIKE; 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 Transcription {ECO:0000256|ARBA:ARBA00023163};
KW Transcription regulation {ECO:0000256|ARBA:ARBA00023015}.
FT DOMAIN 202..280
FT /note="HSA"
FT /evidence="ECO:0000259|PROSITE:PS51204"
FT DOMAIN 358..416
FT /note="Myb-like"
FT /evidence="ECO:0000259|PROSITE:PS50090"
FT REGION 71..91
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 495..517
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 537..615
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 655..684
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 495..511
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 553..572
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 573..615
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 684 AA; 79448 MW; 7CE241D67A6DE69A CRC64;
MNDTWRSRLK EISHITADPF LRNFHKLHTN DKEQIYSILH NPDNVVEQTF KNTIIKSMEE
SMFRPLIPTQ QMKRRQNDHH HQGPPPKIQK STVDSLKSQH QIDQQNLDWF LSQPLEDLEV
MTVPEQYPLT VPAVLPLAEL YYLTQTLASI KLLPGSHKVL MTENFESALA EGKIAVLYSR
IEELKRQGKW SLRQPQKFYD PFKFIRKSKK KSFHWDYLLQ EGKWMADDFR ESSKYKKWCC
VVIAEAVEQY WKGRKVSHQT FVDVADLKKI DKSIIRNLPV YTGLGGDSRE PPIATVSKLV
YPAEDNHWYK IALKPHHHHH RHQTTHQGLF GSTRKYNTLK PPKPPTPKNI EYRIPTIWLP
EDDKRLIHYV AEFCFNWDLI SEHISSSSTA VSLKKYESNI ERRTPWQCFE RYIQLNDKFQ
FSDMKGVYAY HAQQWLEQAH RAQSTTKRRI SPLGVGPESV QRGNRKLRWA SMFDAMRKAM
KKREIAAAKI NHRKSTAELQ ANQNVTEPKP NSDRIPTPAE LSRLKFERDK TLHENHINQQ
ATRARMVQAV AKPAPAPAPP PPQPPKPVKR PTTPNGTPLT NEQIQHLLQM QKHRRMLQQQ
QQQQQQQQHQ QQQRRIHFPP AQVSKVINDI QQQNPGLSKD QVTKLAAQYL ASLSQQGYGV
PSSPVPPHQK NQTASPMSGS PNNA
//
