SWC4_ASHGO
ID SWC4_ASHGO Reviewed; 488 AA.
AC Q752S6;
DT 20-DEC-2005, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 25-MAY-2022, entry version 103.
DE RecName: Full=SWR1-complex protein 4;
GN Name=SWC4; OrderedLocusNames=AFR497C;
OS Ashbya gossypii (strain ATCC 10895 / CBS 109.51 / FGSC 9923 / NRRL Y-1056)
OS (Yeast) (Eremothecium gossypii).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Eremothecium.
OX NCBI_TaxID=284811;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 10895 / CBS 109.51 / FGSC 9923 / NRRL Y-1056;
RX PubMed=15001715; DOI=10.1126/science.1095781;
RA Dietrich F.S., Voegeli S., Brachat S., Lerch A., Gates K., Steiner S.,
RA Mohr C., Poehlmann R., Luedi P., Choi S., Wing R.A., Flavier A.,
RA Gaffney T.D., Philippsen P.;
RT "The Ashbya gossypii genome as a tool for mapping the ancient Saccharomyces
RT cerevisiae genome.";
RL Science 304:304-307(2004).
RN [2]
RP GENOME REANNOTATION.
RC STRAIN=ATCC 10895 / CBS 109.51 / FGSC 9923 / NRRL Y-1056;
RX PubMed=23749448; DOI=10.1534/g3.112.002881;
RA Dietrich F.S., Voegeli S., Kuo S., Philippsen P.;
RT "Genomes of Ashbya fungi isolated from insects reveal four mating-type
RT loci, numerous translocations, lack of transposons, and distinct gene
RT duplications.";
RL G3 (Bethesda) 3:1225-1239(2013).
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; AE016819; AAS53868.1; -; Genomic_DNA.
DR RefSeq; NP_986044.1; NM_212180.1.
DR AlphaFoldDB; Q752S6; -.
DR SMR; Q752S6; -.
DR STRING; 33169.AAS53868; -.
DR EnsemblFungi; AAS53868; AAS53868; AGOS_AFR497C.
DR GeneID; 4622323; -.
DR KEGG; ago:AGOS_AFR497C; -.
DR eggNOG; KOG2656; Eukaryota.
DR HOGENOM; CLU_018539_4_0_1; -.
DR InParanoid; Q752S6; -.
DR OMA; MYQSSQG; -.
DR Proteomes; UP000000591; Chromosome VI.
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; IPR027109; Swc4/Dmap1.
DR PANTHER; PTHR12855; PTHR12855; 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..488
FT /note="SWR1-complex protein 4"
FT /id="PRO_0000076335"
FT DOMAIN 137..190
FT /note="SANT"
FT REGION 1..37
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 290..387
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 305..327
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 346..360
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 488 AA; 56132 MW; 0A1EACE37A904EA1 CRC64;
MSSSDIFDVL NIQPKSSSPH PQTSQSNAGA SKTPKPQVTG MQRELYNLLG DNTPPIVIQP
TSKFKDRLAS LTKPSPWTHT EFEATPYVKL SHWVKGSKEL LEGQSPKSSF AKYDQKLTLP
EFTEGEYQEF MAQAAKGANS DAPTWSYEEV QYLFDLCRRY DLRWHIVYDR YMYDESRTME
DIREMFYTVC QKYFQAKDPG NPLLPSLAYS KDQEIQRKKY LTRLLSRSAA EIAEEEALIM
ESRKFEMAAK KTLQEREAML RLLDHPQGDA NVSQFLTSQG MNQLYNNLLN DKQRRRKPDS
APPENPWMKQ QQQFAQQKQQ LQLQHQQHHQ LRDQKRIEVK TDPVTPGSPK QDSPSPGRKA
SDQSAAPRMN KKQKLEMQTA MRRKQDSEYA QHLLKNFSSE ERKSLGVTLH GEKLAPGVFL
RSSKISTFKP SIQNKVVSVL QELGLPVRPA MPSAAVVQHH DELLRRIVTL LDLKRQQDKL
EAEKAIVK