ID A8PTM5_MALGO Unreviewed; 339 AA.
AC A8PTM5;
DT 15-JAN-2008, integrated into UniProtKB/TrEMBL.
DT 15-JAN-2008, sequence version 1.
DT 27-MAR-2024, entry version 63.
DE RecName: Full=Protein AF-9 homolog {ECO:0000256|ARBA:ARBA00022408, ECO:0000256|RuleBase:RU367117};
GN Name=YAF9 {ECO:0000256|RuleBase:RU367117};
GN ORFNames=MGL_0448 {ECO:0000313|EMBL:EDP45459.1};
OS Malassezia globosa (strain ATCC MYA-4612 / CBS 7966) (Dandruff-associated
OS fungus).
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Ustilaginomycotina;
OC Malasseziomycetes; Malasseziales; Malasseziaceae; Malassezia.
OX NCBI_TaxID=425265 {ECO:0000313|EMBL:EDP45459.1, ECO:0000313|Proteomes:UP000008837};
RN [1] {ECO:0000313|EMBL:EDP45459.1, ECO:0000313|Proteomes:UP000008837}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC MYA-4612 / CBS 7966 {ECO:0000313|Proteomes:UP000008837};
RX PubMed=18000048; DOI=10.1073/pnas.0706756104;
RA Xu J., Saunders C.W., Hu P., Grant R.A., Boekhout T., Kuramae E.E.,
RA Kronstad J.W., Deangelis Y.M., Reeder N.L., Johnstone K.R., Leland M.,
RA Fieno A.M., Begley W.M., Sun Y., Lacey M.P., Chaudhary T., Keough T.,
RA Chu L., Sears R., Yuan B., Dawson T.L.Jr.;
RT "Dandruff-associated Malassezia genomes reveal convergent and divergent
RT virulence traits shared with plant and human fungal pathogens.";
RL Proc. Natl. Acad. Sci. U.S.A. 104:18730-18735(2007).
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:EDP45459.1}.
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DR EMBL; AAYY01000001; EDP45459.1; -; Genomic_DNA.
DR RefSeq; XP_001732673.1; XM_001732621.1.
DR AlphaFoldDB; A8PTM5; -.
DR STRING; 425265.A8PTM5; -.
DR GeneID; 5856979; -.
DR KEGG; mgl:MGL_0448; -.
DR VEuPathDB; FungiDB:MGL_0448; -.
DR InParanoid; A8PTM5; -.
DR OMA; DYHKMVG; -.
DR OrthoDB; 128693at2759; -.
DR Proteomes; UP000008837; Unassembled WGS sequence.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0035267; C:NuA4 histone acetyltransferase complex; IEA:UniProtKB-UniRule.
DR GO; GO:0000812; C:Swr1 complex; IEA:UniProtKB-UniRule.
DR GO; GO:0006325; P:chromatin organization; IEA:UniProtKB-KW.
DR GO; GO:0006281; P:DNA repair; IEA:UniProtKB-UniRule.
DR GO; GO:0006355; P:regulation of DNA-templated transcription; IEA:InterPro.
DR CDD; cd16908; YEATS_Yaf9_like; 1.
DR Gene3D; 2.60.40.1970; YEATS domain; 1.
DR InterPro; IPR038704; YEAST_sf.
DR InterPro; IPR005033; YEATS.
DR PANTHER; PTHR23195; YEATS DOMAIN; 1.
DR PANTHER; PTHR23195:SF15; YEATS DOMAIN-CONTAINING PROTEIN 4; 1.
DR Pfam; PF03366; YEATS; 1.
DR PROSITE; PS51037; YEATS; 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 Nucleus {ECO:0000256|ARBA:ARBA00023242, ECO:0000256|PROSITE-
KW ProRule:PRU00376}; Reference proteome {ECO:0000313|Proteomes:UP000008837};
KW Transcription {ECO:0000256|RuleBase:RU367117};
KW Transcription regulation {ECO:0000256|RuleBase:RU367117}.
FT REGION 169..206
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 339 AA; 36778 MW; 85A563F20861B617 CRC64;
MSNKRIRGLS ISRPILIGST STPLTPEEKL SAPPDHTHKW TVAVRSAASA PLASISTNGS
ASRESESGGM IGTRLHESEL DLHRAIGGKD DLSYFIKRVQ FRLHDTYAQP TRNVDRSPFS
VTETGWGEFE VQIKIFFVPE AGEKPLTILH HLKLHPWSSS VATVGAQSNA PVSDASAHAS
QAASSLPPSS QSEPHTRNDT QQHAQQDVSL PAAISPPPVV HSWQYEEIVF PEPLEAFYDI
LIAHPPTPWP ATSADALLNT DSLSSSSHNV HTPTGQLIDA LSLEAQRAEA DRIDLARIDA
VQQLDADRAK LIHTEKLLRD TLARLSKLEP ASSLPTPSS
//
