AF9_ASHGO
ID AF9_ASHGO Reviewed; 208 AA.
AC Q755P0;
DT 20-DEC-2005, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 25-MAY-2022, entry version 93.
DE RecName: Full=Protein AF-9 homolog;
GN Name=YAF9; OrderedLocusNames=AFL227C;
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 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; AE016819; AAS53147.1; -; Genomic_DNA.
DR RefSeq; NP_985323.1; NM_210677.1.
DR AlphaFoldDB; Q755P0; -.
DR SMR; Q755P0; -.
DR STRING; 33169.AAS53147; -.
DR EnsemblFungi; AAS53147; AAS53147; AGOS_AFL227C.
DR GeneID; 4621543; -.
DR KEGG; ago:AGOS_AFL227C; -.
DR eggNOG; KOG3149; Eukaryota.
DR HOGENOM; CLU_051385_2_1_1; -.
DR InParanoid; Q755P0; -.
DR OMA; PYHNEDM; -.
DR Proteomes; UP000000591; Chromosome VI.
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:0006357; P:regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR Gene3D; 2.60.40.1970; -; 1.
DR InterPro; IPR037989; Yaf9.
DR InterPro; IPR038704; YEAST_sf.
DR InterPro; IPR005033; YEATS.
DR PANTHER; PTHR23195; PTHR23195; 1.
DR PANTHER; PTHR23195:SF15; PTHR23195:SF15; 1.
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..208
FT /note="Protein AF-9 homolog"
FT /id="PRO_0000215922"
FT DOMAIN 8..157
FT /note="YEATS"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00376"
FT COILED 176..208
FT /evidence="ECO:0000255"
SQ SEQUENCE 208 AA; 23916 MW; FD0B084EB169DB85 CRC64;
MAPAQAKRIK TLSVARPIVY GNTAKKMGDV RPAIAPSEHT HMWTIFVRGP QGEDISYFIK
KVVFKLHETY PNPVRVVDAP PFELTETGWG EFEINVKVHF VDEANEKMLN FYHHLRLHPY
TEEDGRRSDG DEVSSVFYDE IVFNEPNEAF FAKMIEQPGN LLPSNKTPDC VFSLQLEQEE
IDRIQQGIGK VDEEIEQLKQ KLEQDLAK