EAF1_CANAL
ID EAF1_CANAL Reviewed; 686 AA.
AC Q5A119; A0A1D8PMS9; Q5A189; Q5A190;
DT 20-DEC-2005, integrated into UniProtKB/Swiss-Prot.
DT 15-MAR-2017, sequence version 2.
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=VID21; Synonyms=EAF1; OrderedLocusNames=CAALFM_C407230CA;
GN ORFNames=CaO19.10589/10590, CaO19.3077;
OS Candida albicans (strain SC5314 / ATCC MYA-2876) (Yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Debaryomycetaceae; Candida/Lodderomyces clade; Candida.
OX NCBI_TaxID=237561;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SC5314 / ATCC MYA-2876;
RX PubMed=15123810; DOI=10.1073/pnas.0401648101;
RA Jones T., Federspiel N.A., Chibana H., Dungan J., Kalman S., Magee B.B.,
RA Newport G., Thorstenson Y.R., Agabian N., Magee P.T., Davis R.W.,
RA Scherer S.;
RT "The diploid genome sequence of Candida albicans.";
RL Proc. Natl. Acad. Sci. U.S.A. 101:7329-7334(2004).
RN [2]
RP GENOME REANNOTATION.
RC STRAIN=SC5314 / ATCC MYA-2876;
RX PubMed=17419877; DOI=10.1186/gb-2007-8-4-r52;
RA van het Hoog M., Rast T.J., Martchenko M., Grindle S., Dignard D.,
RA Hogues H., Cuomo C., Berriman M., Scherer S., Magee B.B., Whiteway M.,
RA Chibana H., Nantel A., Magee P.T.;
RT "Assembly of the Candida albicans genome into sixteen supercontigs aligned
RT on the eight chromosomes.";
RL Genome Biol. 8:RESEARCH52.1-RESEARCH52.12(2007).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND GENOME REANNOTATION.
RC STRAIN=SC5314 / ATCC MYA-2876;
RX PubMed=24025428; DOI=10.1186/gb-2013-14-9-r97;
RA Muzzey D., Schwartz K., Weissman J.S., Sherlock G.;
RT "Assembly of a phased diploid Candida albicans genome facilitates allele-
RT specific measurements and provides a simple model for repeat and indel
RT structure.";
RL Genome Biol. 14:RESEARCH97.1-RESEARCH97.14(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; CP017626; AOW29444.1; -; Genomic_DNA.
DR RefSeq; XP_715387.2; XM_710294.2.
DR AlphaFoldDB; Q5A119; -.
DR SMR; Q5A119; -.
DR STRING; 237561.Q5A119; -.
DR PRIDE; Q5A119; -.
DR GeneID; 3642946; -.
DR KEGG; cal:CAALFM_C407230CA; -.
DR CGD; CAL0000190942; VID21.
DR VEuPathDB; FungiDB:C4_07230C_A; -.
DR eggNOG; ENOG502RGMX; Eukaryota.
DR HOGENOM; CLU_006174_1_0_1; -.
DR InParanoid; Q5A119; -.
DR OrthoDB; 314765at2759; -.
DR PRO; PR:Q5A119; -.
DR Proteomes; UP000000559; Chromosome 4.
DR GO; GO:0035267; C:NuA4 histone acetyltransferase complex; IDA:CGD.
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..686
FT /note="Chromatin modification-related protein EAF1"
FT /id="PRO_0000065815"
FT DOMAIN 202..280
FT /note="HSA"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00549"
FT DOMAIN 354..418
FT /note="Myb-like"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00133"
FT REGION 71..97
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 493..517
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 544..617
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 657..686
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 82..97
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 495..511
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 554..574
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 575..617
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 686 AA; 79535 MW; 53BA80011576C079 CRC64;
MNDTWRSRLK EISHITADPF LRDFHKLHTN DKEQIYSILH NPDNVVEQTF KNTIIKSMEE
SMFRPLIPTQ QMKRRQNDHH NQGPPPKVQK 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
KKREIAAAKV NHRKSTAELQ ANQNVTEPKP NSDRIPTPAE LSRLKFERDK TLHENHINQQ
ATRARMVQAV AKPAPAPAPA PPPPPPPKPV KRPTTPNGTP LTNEQIQHLL QMQKHRRMLQ
QQQQQQQQQQ HQQQQRRIHF PPAQVSKVIN DIQQQNPGLS KDQVTKLAAQ YLASLSQQGY
GVPSSPVPPH QKNQTASPMS GSPNNA
