ID   SWC4_EMENI              Reviewed;         586 AA.
AC   Q5B4T5; C8V8J5;
DT   20-DEC-2005, integrated into UniProtKB/Swiss-Prot.
DT   26-APR-2005, sequence version 1.
DT   25-MAY-2022, entry version 101.
DE   RecName: Full=SWR1-complex protein 4;
GN   Name=swc4; ORFNames=AN4445;
OS   Emericella nidulans (strain FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 /
OS   M139) (Aspergillus nidulans).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC   Aspergillus subgen. Nidulantes.
OX   NCBI_TaxID=227321;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139;
RX   PubMed=16372000; DOI=10.1038/nature04341;
RA   Galagan J.E., Calvo S.E., Cuomo C., Ma L.-J., Wortman J.R., Batzoglou S.,
RA   Lee S.-I., Bastuerkmen M., Spevak C.C., Clutterbuck J., Kapitonov V.,
RA   Jurka J., Scazzocchio C., Farman M.L., Butler J., Purcell S., Harris S.,
RA   Braus G.H., Draht O., Busch S., D'Enfert C., Bouchier C., Goldman G.H.,
RA   Bell-Pedersen D., Griffiths-Jones S., Doonan J.H., Yu J., Vienken K.,
RA   Pain A., Freitag M., Selker E.U., Archer D.B., Penalva M.A., Oakley B.R.,
RA   Momany M., Tanaka T., Kumagai T., Asai K., Machida M., Nierman W.C.,
RA   Denning D.W., Caddick M.X., Hynes M., Paoletti M., Fischer R., Miller B.L.,
RA   Dyer P.S., Sachs M.S., Osmani S.A., Birren B.W.;
RT   "Sequencing of Aspergillus nidulans and comparative analysis with A.
RT   fumigatus and A. oryzae.";
RL   Nature 438:1105-1115(2005).
RN   [2]
RP   GENOME REANNOTATION.
RC   STRAIN=FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139;
RX   PubMed=19146970; DOI=10.1016/j.fgb.2008.12.003;
RA   Wortman J.R., Gilsenan J.M., Joardar V., Deegan J., Clutterbuck J.,
RA   Andersen M.R., Archer D., Bencina M., Braus G., Coutinho P., von Dohren H.,
RA   Doonan J., Driessen A.J., Durek P., Espeso E., Fekete E., Flipphi M.,
RA   Estrada C.G., Geysens S., Goldman G., de Groot P.W., Hansen K.,
RA   Harris S.D., Heinekamp T., Helmstaedt K., Henrissat B., Hofmann G.,
RA   Homan T., Horio T., Horiuchi H., James S., Jones M., Karaffa L.,
RA   Karanyi Z., Kato M., Keller N., Kelly D.E., Kiel J.A., Kim J.M.,
RA   van der Klei I.J., Klis F.M., Kovalchuk A., Krasevec N., Kubicek C.P.,
RA   Liu B., Maccabe A., Meyer V., Mirabito P., Miskei M., Mos M., Mullins J.,
RA   Nelson D.R., Nielsen J., Oakley B.R., Osmani S.A., Pakula T., Paszewski A.,
RA   Paulsen I., Pilsyk S., Pocsi I., Punt P.J., Ram A.F., Ren Q., Robellet X.,
RA   Robson G., Seiboth B., van Solingen P., Specht T., Sun J.,
RA   Taheri-Talesh N., Takeshita N., Ussery D., vanKuyk P.A., Visser H.,
RA   van de Vondervoort P.J., de Vries R.P., Walton J., Xiang X., Xiong Y.,
RA   Zeng A.P., Brandt B.W., Cornell M.J., van den Hondel C.A., Visser J.,
RA   Oliver S.G., Turner G.;
RT   "The 2008 update of the Aspergillus nidulans genome annotation: a community
RT   effort.";
RL   Fungal Genet. Biol. 46:S2-13(2009).
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}.
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; AACD01000077; EAA60210.1; -; Genomic_DNA.
DR   EMBL; BN001303; CBF77504.1; -; Genomic_DNA.
DR   RefSeq; XP_662049.1; XM_656957.1.
DR   AlphaFoldDB; Q5B4T5; -.
DR   SMR; Q5B4T5; -.
DR   BioGRID; 1953018; 1.
DR   STRING; 162425.CADANIAP00006006; -.
DR   PRIDE; Q5B4T5; -.
DR   EnsemblFungi; CBF77504; CBF77504; ANIA_04445.
DR   EnsemblFungi; EAA60210; EAA60210; AN4445.2.
DR   GeneID; 2872244; -.
DR   KEGG; ani:AN4445.2; -.
DR   eggNOG; KOG2656; Eukaryota.
DR   HOGENOM; CLU_018539_3_1_1; -.
DR   InParanoid; Q5B4T5; -.
DR   OMA; MYQSSQG; -.
DR   OrthoDB; 918816at2759; -.
DR   Proteomes; UP000000560; Chromosome III.
DR   Proteomes; UP000005890; Unassembled WGS sequence.
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; IPR001005; SANT/Myb.
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..586
FT                   /note="SWR1-complex protein 4"
FT                   /id="PRO_0000076340"
FT   DOMAIN          137..190
FT                   /note="SANT"
FT   REGION          1..30
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          325..383
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          486..586
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        12..30
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        335..373
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        486..507
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        528..578
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   586 AA;  66337 MW;  7E4EFE86EAA7E5B1 CRC64;
     MAAADVRDML DLPAEGQPRP HKKQKVVEKR PEGITRELFA LLGERAPPIA INENRYKGRP
     KWQTKARVRP CARSDDLVLR HWQREPESTN IPAIEDTRAE GETKEQGEHK TADREYPFAK
     YNIKLKFSNR YTTDEYNRHL RSEDWSREET DYLMDLVEEY DLRWVVIADR YDFQPQRVDN
     TEETSSALVP SKQFRTMEQM KARYYFVAAS MLALEHPPSE MSEAEFDLHE RMMKFDPERE
     RHRKELAALQ LNRTADEVRE ETVLLEELKR ITANEQEFVT ERRELYSRLD VPISVSNATN
     YHNSQGLSHL LQTLLQADKS KKRRSILGPD GIAPTSGGQT PTIPNAPGSA RDSSRADTPN
     GGTTQSTTTK KAAAAANREA AQQAIRTLTP AEEARYGVQH HDRLAPGVQF RSDRAQKLTQ
     AKSHVQTQKL ASALAELEVP LRLFMPTERV VKEFEKLIHS VNLLLDARKV AEKVESEIRV
     LEAAKEERER KAKELREKDK PEVKSEQQDN DVPIPPAPAP VAAGDASQTG QPAKTNEGQA
     ELNGSSTTNN VADSEPSTQE QEGVSHKRSA SVLSNGSDKS SKRQKK