SWC4_CANAL
ID SWC4_CANAL Reviewed; 635 AA.
AC Q5AAJ7; A0A1D8PRQ9;
DT 20-DEC-2005, integrated into UniProtKB/Swiss-Prot.
DT 26-APR-2005, sequence version 1.
DT 03-AUG-2022, entry version 109.
DE RecName: Full=SWR1-complex protein 4;
GN Name=SWC4; OrderedLocusNames=CAALFM_CR00400CA; ORFNames=CaO19.7492;
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 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; CP017630; AOW30811.1; -; Genomic_DNA.
DR RefSeq; XP_718649.1; XM_713556.1.
DR AlphaFoldDB; Q5AAJ7; -.
DR SMR; Q5AAJ7; -.
DR STRING; 237561.Q5AAJ7; -.
DR PRIDE; Q5AAJ7; -.
DR GeneID; 3639679; -.
DR KEGG; cal:CAALFM_CR00400CA; -.
DR CGD; CAL0000199374; SWC4.
DR VEuPathDB; FungiDB:CR_00400C_A; -.
DR eggNOG; KOG2656; Eukaryota.
DR HOGENOM; CLU_018539_4_0_1; -.
DR InParanoid; Q5AAJ7; -.
DR OMA; MYQSSQG; -.
DR OrthoDB; 918816at2759; -.
DR Proteomes; UP000000559; Chromosome R.
DR GO; GO:0035267; C:NuA4 histone acetyltransferase complex; IDA:CGD.
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; IPR009057; Homeobox-like_sf.
DR InterPro; IPR001005; SANT/Myb.
DR InterPro; IPR027109; Swc4/Dmap1.
DR PANTHER; PTHR12855; PTHR12855; 2.
DR Pfam; PF05499; DMAP1; 1.
DR Pfam; PF16282; SANT_DAMP1_like; 1.
DR SMART; SM00717; SANT; 1.
DR SUPFAM; SSF46689; SSF46689; 1.
PE 3: Inferred from homology;
KW Activator; Chromatin regulator; DNA damage; DNA repair; Nucleus;
KW Reference proteome; Transcription; Transcription regulation.
FT CHAIN 1..635
FT /note="SWR1-complex protein 4"
FT /id="PRO_0000076337"
FT DOMAIN 303..353
FT /note="SANT"
FT REGION 1..38
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 148..305
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 458..486
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..16
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 148..179
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 193..238
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 239..255
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 267..305
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 635 AA; 74039 MW; 63D13B88267DBBF4 CRC64;
MSANDILDVL NIQRDESNQP PKKKQKSSST PTLPDGKQLT GMARELYNLV GPNTPPINLN
SNSYTANKEK MKKFKPSPWT RMPFTPKQGI ELNHWVKGSK ELIEQQEFEE DGTPKPYFFE
KYNVQLEIPE FVDEDTYDLY MIEIKEYESK MKEERARREK ERKEREKRDL EEKKKKQQQQ
QQKSQQNPQN QIKDDEKNQD TRNNTDKKDS EQKSEDKPTV EAKKETDEKK DDVVLKDNTN
ETKPVTETTK SETETTEQNN SEKTNENETN KTNDKDGEGN LTKSKDSATE DQSNNKKEND
EDTESEWTYK ETKHLFELCQ AFELKWPIIH DRFPNPNRTA EDLKEQFYRI CIKILENQKN
KNQALIDSLK AYCKPRELER KQYLENLLKR TPAEIAEEES LVIEARRFEI AAKKMLMERS
NLLTLLDSPQ TTQNVSQYQS SQGITNLYNN LLIYDKHQKK KQMANKSNPQ QEPVPPPIPL
AASSSVKRDR GFQTQLQQYL SSFLKQNHHT NPAVKQEINS IQQLLMKRLT QKEEEAYGLY
FHGTEKLNPG VMLRSQQKLP GLNQRQSILK SVNILLQEMD IPTGGGTSWK PIMPTRKTMA
KYDELIRSVV TLLDVKKAKD KLESEIKLIK SQRGL
