EAF7_CANAL
ID EAF7_CANAL Reviewed; 445 AA.
AC Q5A6Q7; A0A1D8PSN4;
DT 20-DEC-2005, integrated into UniProtKB/Swiss-Prot.
DT 26-APR-2005, sequence version 1.
DT 03-AUG-2022, entry version 86.
DE RecName: Full=Chromatin modification-related protein EAF7;
GN Name=EAF7; OrderedLocusNames=CAALFM_CR04130CA;
GN ORFNames=CaO19.497, CaO19.8127;
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:0000250}.
CC -!- SIMILARITY: Belongs to the EAF7 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; CP017630; AOW31151.1; -; Genomic_DNA.
DR RefSeq; XP_717360.1; XM_712267.2.
DR AlphaFoldDB; Q5A6Q7; -.
DR BioGRID; 1224002; 1.
DR STRING; 237561.Q5A6Q7; -.
DR PRIDE; Q5A6Q7; -.
DR GeneID; 3640973; -.
DR KEGG; cal:CAALFM_CR04130CA; -.
DR CGD; CAL0000190105; EAF7.
DR VEuPathDB; FungiDB:CR_04130C_A; -.
DR eggNOG; KOG4051; Eukaryota.
DR HOGENOM; CLU_615372_0_0_1; -.
DR InParanoid; Q5A6Q7; -.
DR OMA; MRCILER; -.
DR OrthoDB; 1476852at2759; -.
DR PRO; PR:Q5A6Q7; -.
DR Proteomes; UP000000559; Chromosome R.
DR GO; GO:0035267; C:NuA4 histone acetyltransferase complex; IDA:CGD.
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; IBA:GO_Central.
DR GO; GO:0043967; P:histone H4 acetylation; IC:CGD.
DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR InterPro; IPR012423; Eaf7/MRGBP.
DR PANTHER; PTHR13581; PTHR13581; 1.
DR Pfam; PF07904; Eaf7; 1.
PE 3: Inferred from homology;
KW Chromatin regulator; DNA damage; DNA repair; Nucleus; Reference proteome;
KW Transcription; Transcription regulation.
FT CHAIN 1..445
FT /note="Chromatin modification-related protein EAF7"
FT /id="PRO_0000215878"
FT REGION 85..445
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 85..112
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 113..137
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 147..193
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 194..209
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 210..255
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 282..300
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 301..365
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 407..423
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 445 AA; 50718 MW; D5281A9D3D2FB08C CRC64;
MATLDENNPS KQTHRHWSIE NEIKLFSLLC DYKPAGKNKQ HNIKIIINNI NESLDSKEEP
FSEYDVWNKL RSLYDLEKID QIEELSTENT STEETTNQVS SGSANITKDT KNAKTTLDAK
EPIQDKKEMD KEKSESSSLS TPEPPQRRTR SARDTTKSKR NLRDTPKEKS QYNDEEITSG
GAEKSKVEVS STSDHTDDQS PTPGSTKKGL DEQTNDDMSD IEDVDKDKGD ETIAKIKKEN
TSEQEEDKNK KQTEEEAEEE EEEGDHVSGD ERESKNKDTS EDEDGEDNED QDEDDVEVIE
DSHTDKENES SSEESSPEPM TKRTRQRTRS THEKTEHTSP NIKKRTRQSV KFDDKPAEPS
DTGSRKRRAP PGSVSPPHPP KTRRRTRSVT HEIEEEDAST QSADDAEPEI IKVETRHTTR
RSSRISMEPS SSTPNVRVRR SSRKR
