ID   SWC4_YARLI              Reviewed;         504 AA.
AC   Q6C9M6;
DT   20-DEC-2005, integrated into UniProtKB/Swiss-Prot.
DT   16-AUG-2004, sequence version 1.
DT   25-MAY-2022, entry version 89.
DE   RecName: Full=SWR1-complex protein 4;
GN   Name=SWC4; OrderedLocusNames=YALI0D09911g;
OS   Yarrowia lipolytica (strain CLIB 122 / E 150) (Yeast) (Candida lipolytica).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Dipodascaceae; Yarrowia.
OX   NCBI_TaxID=284591;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CLIB 122 / E 150;
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 SWR1 complex which mediates the ATP-
CC       dependent exchange of histone H2A for the H2A variant HZT1 leading to
CC       transcriptional regulation of selected genes by chromatin remodeling.
CC       Component of the NuA4 histone acetyltransferase complex which is
CC       involved in transcriptional activation of selected genes principally by
CC       acetylation of nucleosomal histone H4 and H2A. The NuA4 complex is also
CC       involved in DNA repair (By similarity). {ECO:0000250}.
CC   -!- SUBUNIT: Component of the SWR1 chromatin-remodeling complex and of the
CC       NuA4 histone acetyltransferase complex. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the SWC4 family. {ECO:0000305}.
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DR   EMBL; CR382130; CAG80824.1; -; Genomic_DNA.
DR   RefSeq; XP_502636.1; XM_502636.1.
DR   AlphaFoldDB; Q6C9M6; -.
DR   SMR; Q6C9M6; -.
DR   STRING; 4952.CAG80824; -.
DR   EnsemblFungi; CAG80824; CAG80824; YALI0_D09911g.
DR   GeneID; 2910927; -.
DR   KEGG; yli:YALI0D09911g; -.
DR   VEuPathDB; FungiDB:YALI0_D09911g; -.
DR   HOGENOM; CLU_018539_3_1_1; -.
DR   InParanoid; Q6C9M6; -.
DR   OMA; MYQSSQG; -.
DR   Proteomes; UP000001300; Chromosome D.
DR   GO; GO:0035267; C:NuA4 histone acetyltransferase complex; IBA:GO_Central.
DR   GO; GO:0000812; C:Swr1 complex; IBA:GO_Central.
DR   GO; GO:0003714; F:transcription corepressor activity; IBA:GO_Central.
DR   GO; GO:0006281; P:DNA repair; IEA:UniProtKB-KW.
DR   GO; GO:0043486; P:histone exchange; IBA:GO_Central.
DR   GO; GO:0043968; P:histone H2A acetylation; IBA:GO_Central.
DR   GO; GO:0043967; P:histone H4 acetylation; IBA:GO_Central.
DR   GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR   InterPro; IPR032563; DAMP1_SANT-like.
DR   InterPro; IPR008468; DMAP1.
DR   InterPro; IPR027109; Swc4/Dmap1.
DR   PANTHER; PTHR12855; PTHR12855; 1.
DR   Pfam; PF05499; DMAP1; 1.
DR   Pfam; PF16282; SANT_DAMP1_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..504
FT                   /note="SWR1-complex protein 4"
FT                   /id="PRO_0000076346"
FT   REGION          1..36
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          181..235
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          346..391
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        10..24
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        187..235
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        373..391
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   504 AA;  56599 MW;  461E39BE83DAA4F9 CRC64;
     MASSSDVRDV LDLPDLEPND KLTQQPKRQK LAAPVGGKRM DGMQRELFAL MGENTPSVSV
     TKDSHTSLFK DKPQWQAKLT PWMWTPFQNQ AREDGLILSH WVRGGELTQG DQYPFAALNT
     QISFPELTQE DYDGLKLATP GWTLEETRYL MHLCSEFDLR WPVIHDRWEW QTDQDVTMAT
     GETKGAEGTE SKVKEEDKDV EMADVKEEKE NKDESNKEKS EKKESAPPDG TARTVEDLKE
     RFYNVVSAMS KHPEKYTAEG YNMTTVKFPR DMEIKRKQYL ERLLARSPAE IAEEEALILK
     SRKLELSATK MLQERQELLK LLDAPQPTSS VAQFQTSQGL AHLTSTLNDK SKKGGKPTKE
     GSVGPQAPDR GGSVEKTTKK EDTKEAKKAT KEDKKAATTI AAAISKKLTT KEEAAYGISY
     HDKLTPGVYL RSSKVTTFKP TIQTKIVAAL QDIGIPPKPV MPTAKVCAKF ESIQHSMSVL
     LETKRAADKL ETEIRLLRGQ KGQL