ID A0A2G5H9T8_CERBT Unreviewed; 267 AA.
AC A0A2G5H9T8;
DT 31-JAN-2018, integrated into UniProtKB/TrEMBL.
DT 31-JAN-2018, sequence version 1.
DT 27-MAR-2024, entry version 19.
DE RecName: Full=Protein AF-9 homolog {ECO:0000256|ARBA:ARBA00022408, ECO:0000256|RuleBase:RU367117};
GN Name=YAF9 {ECO:0000256|RuleBase:RU367117};
GN ORFNames=CB0940_07460 {ECO:0000313|EMBL:PIA89291.1};
OS Cercospora beticola (Sugarbeet leaf spot fungus).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC Dothideomycetidae; Mycosphaerellales; Mycosphaerellaceae; Cercospora.
OX NCBI_TaxID=122368 {ECO:0000313|EMBL:PIA89291.1, ECO:0000313|Proteomes:UP000230605};
RN [1] {ECO:0000313|EMBL:PIA89291.1, ECO:0000313|Proteomes:UP000230605}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=09-40 {ECO:0000313|EMBL:PIA89291.1,
RC ECO:0000313|Proteomes:UP000230605};
RA De Jonge R., Ebert M.K., Suttle J.C., Jurick Ii W.M., Secor G.A.,
RA Thomma B.P., Van De Peer Y., Bolton M.D.;
RT "The cercosporin biosynthetic gene cluster was horizontally transferred to
RT several fungal lineages and shown to be expanded in Cercospora beticola
RT based on microsynteny with recipient genomes.";
RL Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Component of the SWR1 complex which mediates the ATP-
CC dependent exchange of histone H2A for an H2A variant 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. {ECO:0000256|RuleBase:RU367117}.
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. {ECO:0000256|ARBA:ARBA00025636}.
CC -!- SUBUNIT: Component of the SWR1 chromatin-remodeling complex and of the
CC NuA4 histone acetyltransferase complex. {ECO:0000256|ARBA:ARBA00038745,
CC ECO:0000256|RuleBase:RU367117}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|RuleBase:RU367117}.
CC Cytoplasm {ECO:0000256|RuleBase:RU367117}.
CC -!- DOMAIN: The coiled-coil domain is required for assembly into the NuA4
CC complex. {ECO:0000256|RuleBase:RU367117}.
CC -!- SIMILARITY: Belongs to the YAF9 family. {ECO:0000256|ARBA:ARBA00038419,
CC ECO:0000256|RuleBase:RU367117}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:PIA89291.1}.
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DR EMBL; LKMD01000108; PIA89291.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2G5H9T8; -.
DR OrthoDB; 9679at2759; -.
DR Proteomes; UP000230605; Chromosome 5.
DR GO; GO:0000785; C:chromatin; IEA:UniProt.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0006355; P:regulation of DNA-templated transcription; IEA:InterPro.
DR Gene3D; 2.60.40.1970; YEATS domain; 1.
DR Gene3D; 3.30.40.10; Zinc/RING finger domain, C3HC4 (zinc finger); 1.
DR InterPro; IPR038704; YEAST_sf.
DR InterPro; IPR005033; YEATS.
DR InterPro; IPR027370; Znf-RING_euk.
DR InterPro; IPR001841; Znf_RING.
DR InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR InterPro; IPR017907; Znf_RING_CS.
DR PANTHER; PTHR23195; YEATS DOMAIN; 1.
DR PANTHER; PTHR23195:SF15; YEATS DOMAIN-CONTAINING PROTEIN 4; 1.
DR Pfam; PF03366; YEATS; 1.
DR Pfam; PF13445; zf-RING_UBOX; 1.
DR SMART; SM00184; RING; 1.
DR SUPFAM; SSF57850; RING/U-box; 1.
DR PROSITE; PS51037; YEATS; 1.
DR PROSITE; PS00518; ZF_RING_1; 1.
DR PROSITE; PS50089; ZF_RING_2; 1.
PE 3: Inferred from homology;
KW Activator {ECO:0000256|ARBA:ARBA00023159, ECO:0000256|RuleBase:RU367117};
KW Chromatin regulator {ECO:0000256|ARBA:ARBA00022853,
KW ECO:0000256|RuleBase:RU367117};
KW Coiled coil {ECO:0000256|RuleBase:RU367117};
KW Cytoplasm {ECO:0000256|ARBA:ARBA00022490, ECO:0000256|RuleBase:RU367117};
KW DNA damage {ECO:0000256|ARBA:ARBA00022763, ECO:0000256|RuleBase:RU367117};
KW DNA repair {ECO:0000256|ARBA:ARBA00023204, ECO:0000256|RuleBase:RU367117};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Nucleus {ECO:0000256|ARBA:ARBA00023242, ECO:0000256|PROSITE-
KW ProRule:PRU00376}; Transcription {ECO:0000256|RuleBase:RU367117};
KW Transcription regulation {ECO:0000256|RuleBase:RU367117};
KW Zinc {ECO:0000256|ARBA:ARBA00022833};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW ProRule:PRU00175}.
FT DOMAIN 69..131
FT /note="RING-type"
FT /evidence="ECO:0000259|PROSITE:PS50089"
FT REGION 1..64
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 14..38
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 45..64
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 267 AA; 30012 MW; F3BAD4AD2B598653 CRC64;
MASQVSSSEP APPRRSARNR HTALEDRKPA ETRQRARPKA SSARRKTQKP ADEPSTPRPE
ENIDEDDLCP ICQVLLYRPV TTQCNHTMCE SCMAHWADVS VNSQMKIVDV DEEPQTFDAV
SGIEAKCPMC RTQTTASYNP DLAARLGRDY PATTRERSVE EADSLGEQGS IQTLTVYVGN
RHRYIADAET ANCHEWTFFV KPSRTDIIEE VQLVLHPTFR PNRVIRQRAP YEVKRLGWGT
FAVTAYVILK AGYTWVSSEA ENSPDGA
//
