ID   AF9_EMENI               Reviewed;         275 AA.
AC   Q5BC71; C8VKF8;
DT   20-DEC-2005, integrated into UniProtKB/Swiss-Prot.
DT   26-APR-2005, sequence version 1.
DT   25-MAY-2022, entry version 88.
DE   RecName: Full=Protein AF-9 homolog;
GN   Name=yaf9; ORFNames=AN1859;
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 histones H4 and H2A. The NuA4 complex is
CC       also involved in DNA repair. Yaf9 may also be required for viability in
CC       conditions in which the structural integrity of the spindle is
CC       compromised (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: Cytoplasm {ECO:0000250}. Nucleus
CC       {ECO:0000255|PROSITE-ProRule:PRU00376}.
CC   -!- DOMAIN: The coiled-coil domain is required for assembly into the NuA4
CC       complex. {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the YAF9 family. {ECO:0000305}.
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DR   EMBL; AACD01000029; EAA65024.1; -; Genomic_DNA.
DR   EMBL; BN001307; CBF85706.1; -; Genomic_DNA.
DR   RefSeq; XP_659463.1; XM_654371.1.
DR   AlphaFoldDB; Q5BC71; -.
DR   SMR; Q5BC71; -.
DR   STRING; 162425.CADANIAP00008513; -.
DR   EnsemblFungi; CBF85706; CBF85706; ANIA_01859.
DR   EnsemblFungi; EAA65024; EAA65024; AN1859.2.
DR   GeneID; 2875410; -.
DR   KEGG; ani:AN1859.2; -.
DR   VEuPathDB; FungiDB:AN1859; -.
DR   eggNOG; KOG3149; Eukaryota.
DR   HOGENOM; CLU_051385_2_0_1; -.
DR   InParanoid; Q5BC71; -.
DR   OMA; HQWRVFV; -.
DR   OrthoDB; 1482359at2759; -.
DR   Proteomes; UP000000560; Chromosome VII.
DR   Proteomes; UP000005890; Unassembled WGS sequence.
DR   GO; GO:0000781; C:chromosome, telomeric region; IEA:GOC.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
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:0042393; F:histone binding; IBA:GO_Central.
DR   GO; GO:0006338; P:chromatin remodeling; IBA:GO_Central.
DR   GO; GO:0006281; P:DNA repair; IEA:UniProtKB-KW.
DR   GO; GO:0016573; P:histone acetylation; IBA:GO_Central.
DR   GO; GO:0043486; P:histone exchange; IEA:EnsemblFungi.
DR   GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR   GO; GO:0031509; P:subtelomeric heterochromatin assembly; IEA:EnsemblFungi.
DR   Gene3D; 2.60.40.1970; -; 1.
DR   InterPro; IPR038704; YEAST_sf.
DR   InterPro; IPR005033; YEATS.
DR   Pfam; PF03366; YEATS; 1.
DR   PROSITE; PS51037; YEATS; 1.
PE   3: Inferred from homology;
KW   Activator; Chromatin regulator; Coiled coil; Cytoplasm; DNA damage;
KW   DNA repair; Nucleus; Reference proteome; Transcription;
KW   Transcription regulation.
FT   CHAIN           1..275
FT                   /note="Protein AF-9 homolog"
FT                   /id="PRO_0000215927"
FT   DOMAIN          9..160
FT                   /note="YEATS"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00376"
FT   REGION          161..207
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          239..275
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          202..242
FT                   /evidence="ECO:0000255"
FT   COMPBIAS        161..199
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   275 AA;  31364 MW;  C1C456F49FFA522A CRC64;
     MPSATGTKRV RGVSIFRPFV FGSEAQPFDP ATKPSNVSSD HTHQWRVYVR GVNGEDISYW
     IKKVQFKLHE TYVQNVRTVE HPPYEVTETG WGEFEIQIKI YFVPESMEKP QTLWHSLKLH
     PYGPDAEGKK ERREVVVSQN YEEVVFNEPV EQFYDYLTGG SGTQQMQKGK SGKNAKQAQQ
     QRGGRTAEIP FNETPENPYS RTAENKELDR LAEANKTVEQ MIKDEKERLI AREKRLAELR
     ASEGVPAQPL KKSFSGRIPV HSQQRMAGTV GPPDS