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Database: UniProt
Entry: EAF1_KLULA
LinkDB: EAF1_KLULA
Original site: EAF1_KLULA 
ID   EAF1_KLULA              Reviewed;        1005 AA.
AC   Q6CMB8;
DT   20-DEC-2005, integrated into UniProtKB/Swiss-Prot.
DT   16-AUG-2004, sequence version 1.
DT   24-JAN-2024, entry version 119.
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=KLLA0E21538g;
OS   Kluyveromyces lactis (strain ATCC 8585 / CBS 2359 / DSM 70799 / NBRC 1267 /
OS   NRRL Y-1140 / WM37) (Yeast) (Candida sphaerica).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Saccharomycetaceae; Kluyveromyces.
OX   NCBI_TaxID=284590;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 8585 / CBS 2359 / DSM 70799 / NBRC 1267 / NRRL Y-1140 / WM37;
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}.
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DR   EMBL; CR382125; CAH00008.1; -; Genomic_DNA.
DR   RefSeq; XP_454921.1; XM_454921.1.
DR   AlphaFoldDB; Q6CMB8; -.
DR   SMR; Q6CMB8; -.
DR   STRING; 284590.Q6CMB8; -.
DR   PaxDb; 284590-Q6CMB8; -.
DR   GeneID; 2894627; -.
DR   KEGG; kla:KLLA0_E21451g; -.
DR   eggNOG; ENOG502QSEY; Eukaryota.
DR   HOGENOM; CLU_004795_0_0_1; -.
DR   InParanoid; Q6CMB8; -.
DR   OMA; DEMQWMS; -.
DR   Proteomes; UP000000598; Chromosome E.
DR   GO; GO:0035267; C:NuA4 histone acetyltransferase complex; IEA:UniProt.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
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.
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..1005
FT                   /note="Chromatin modification-related protein EAF1"
FT                   /id="PRO_0000065820"
FT   DOMAIN          386..460
FT                   /note="HSA"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00549"
FT   DOMAIN          684..744
FT                   /note="Myb-like"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00133"
FT   REGION          72..180
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          193..214
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          222..241
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          468..543
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          807..844
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          874..930
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          981..1005
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        93..115
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        116..179
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        227..241
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        470..484
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        517..543
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        874..926
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1005 AA;  114703 MW;  C01058C4E0F77D04 CRC64;
     MSSASKGNAT GSKSPEQLLE ERRHLLVQLY CISQITELKN VENHERIGKE IEKFLDQHTL
     IKDKPIDINA LPKFRPRDVS SDRKLNNRSK SSSPSEVKRE LKKQRSKDVS PSGSEEHDVD
     TQTLPQSQTR VVPRVQSQQS IQQSSRQSMV QAQSSRQLQQ QQLQKQRSVS PTQKLPITHN
     NVPPVVVQAH MEPKSVQYPE TQSKPSTSGK RLLDEEQQDI SENQISKRQR LDSGNLSNST
     AARNAATMEI PPHPYSQMID ISQLHADPTP IGVKEPQPYI IESIINNVSK EERKTFFEDD
     INVKEAVYMI TKENAPTKLA KGMPIQEIKY LSQTLPLLRL IPQSQKALTT DLINTALNER
     RITVVASRIE ELRRLNLWSL RQPRKFIDPV TASQPVTHHN VLIEEAKWMR EDFRESLNYK
     IAMCTQMAQA VMEFWTYGKV CCINCKSIPP PSKDIEDIAS SQDMGTKIST VEPEQKDKES
     NTSPDQSNDD GSSKIAEDVE MSEDGVKSST GLTDGSEAVE EKSENGIKEG DKETDKNSSE
     EPTIDIQKLL KRVNPKDEIV APSLPVTSME VYLAKKSSSP FRNYIDIKEL STLGAAISNS
     LPLYGLLDEK NLDSSRPLPF EPVSKAISPL DEDHFMKLVE KQFVDEEPSL VPLSKRRGMF
     YGNRRSHYLR PPNAPSLRYL KFRTPTIWLP EDDQELVKNI NQYAYNWDLI SSQMSNHHKR
     EYVSNIERRT PWQCFERFVQ LNEKFNIADM KGPKAHNAQI WLYEAHKLQQ QQKRRISPLG
     VGSESIQRGH RRLRWASMFE AMRKCIKKRE NAPRPNPSQP RKPFDVKNMS VPTPQEMSDL
     KAQRDEALRR DMQIKRAAKQ RMQMAQLQQG KLPLTTASSP NLPMANNPNS KDSRIRSKQS
     TPQSAPPLGE KEKVTTQTPT QRNTKPANKR EIIEGYAKKI LFQKPNFTPE LALMAAENIY
     RSLPLSDQQR KTVIYDNVAQ PKVRPPEMKH SSPTPQEILQ RAQKK
//
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