ID A0A0C9M6B3_9FUNG Unreviewed; 476 AA.
AC A0A0C9M6B3;
DT 29-APR-2015, integrated into UniProtKB/TrEMBL.
DT 29-APR-2015, sequence version 1.
DT 27-MAR-2024, entry version 34.
DE RecName: Full=Protein AF-9 homolog {ECO:0000256|ARBA:ARBA00022408, ECO:0000256|RuleBase:RU367117};
GN Name=YAF9 {ECO:0000256|RuleBase:RU367117};
GN ORFNames=MAM1_0087c04776 {ECO:0000313|EMBL:GAN05306.1};
OS Mucor ambiguus.
OC Eukaryota; Fungi; Fungi incertae sedis; Mucoromycota; Mucoromycotina;
OC Mucoromycetes; Mucorales; Mucorineae; Mucoraceae; Mucor.
OX NCBI_TaxID=91626 {ECO:0000313|EMBL:GAN05306.1};
RN [1] {ECO:0000313|EMBL:GAN05306.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=NBRC 6742 {ECO:0000313|EMBL:GAN05306.1};
RA Takeda I., Yamane N., Morita T., Tamano K., Machida M., Baker S., Koike H.;
RT "Draft genome sequence of an oleaginous Mucoromycotina fungus Mucor
RT ambiguus NBRC6742.";
RL Submitted (SEP-2014) 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}.
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DR EMBL; DF836376; GAN05306.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0C9M6B3; -.
DR STRING; 91626.A0A0C9M6B3; -.
DR OrthoDB; 1364895at2759; -.
DR Proteomes; UP000053815; 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:0003743; F:translation initiation factor activity; IEA:UniProtKB-KW.
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; cd16905; YEATS_Taf14_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 Initiation factor {ECO:0000313|EMBL:GAN05306.1};
KW Nucleus {ECO:0000256|ARBA:ARBA00023242, ECO:0000256|PROSITE-
KW ProRule:PRU00376}; Protein biosynthesis {ECO:0000313|EMBL:GAN05306.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000053815};
KW Transcription {ECO:0000256|RuleBase:RU367117};
KW Transcription regulation {ECO:0000256|RuleBase:RU367117}.
FT REGION 138..278
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 405..476
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 138..185
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 193..252
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 255..269
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 405..444
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 476 AA; 53128 MW; 05EA296C99271AA1 CRC64;
MAVVTQDIKI SCHNSVIKGH GAKSNDGHPW RNWKITLVAM DGEREVKGKL SMILDHVEYI
LHPTFEEPRR VKKEEPYVLQ EKGWGEFDMR VVLYFTDNIT DPQVLLFDLN FALASYSITH
SVEFPNASTE LVRLLSRDPS SASTSTATSA ASTPRKGGKK PAPSTSTNEG RQAKKKPISS
SPHSKTAKKA KPDTKSTTPI SSKKLRKSST SSSSPAPAPA AVTTSQSPVY DQPSPSDYST
HSSPSLIATT TPDLHPADTE EEETKALHSR SSSDSSSNRI VDHTYKIADV YNLNSIHHAK
LDKRLRDKWD IPDINMMELA KRIYRMSPEQ TTEFGSIIFE NTPEGIKTVI DPDGGIGIDL
YSLGKPLLEK LWDFLADMAS DDNESFTSQD HHESDLEFDS DAELGEYKSD DNDNNHYTDM
DEPGFFHQSD MESDYTDPHT NHRQTNGHHH YTHPAAATEN GYHDNSDMDI QDDDDY
//
