AF9_USTMA
ID AF9_USTMA Reviewed; 431 AA.
AC Q4PFI5; A0A0D1E5E4;
DT 20-DEC-2005, integrated into UniProtKB/Swiss-Prot.
DT 19-JUL-2005, sequence version 1.
DT 25-MAY-2022, entry version 86.
DE RecName: Full=Protein AF-9 homolog;
GN Name=YAF9; ORFNames=UMAG_01128;
OS Ustilago maydis (strain 521 / FGSC 9021) (Corn smut fungus).
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Ustilaginomycotina;
OC Ustilaginomycetes; Ustilaginales; Ustilaginaceae; Ustilago.
OX NCBI_TaxID=237631;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=521 / FGSC 9021;
RX PubMed=17080091; DOI=10.1038/nature05248;
RA Kaemper J., Kahmann R., Boelker M., Ma L.-J., Brefort T., Saville B.J.,
RA Banuett F., Kronstad J.W., Gold S.E., Mueller O., Perlin M.H.,
RA Woesten H.A.B., de Vries R., Ruiz-Herrera J., Reynaga-Pena C.G.,
RA Snetselaar K., McCann M., Perez-Martin J., Feldbruegge M., Basse C.W.,
RA Steinberg G., Ibeas J.I., Holloman W., Guzman P., Farman M.L.,
RA Stajich J.E., Sentandreu R., Gonzalez-Prieto J.M., Kennell J.C., Molina L.,
RA Schirawski J., Mendoza-Mendoza A., Greilinger D., Muench K., Roessel N.,
RA Scherer M., Vranes M., Ladendorf O., Vincon V., Fuchs U., Sandrock B.,
RA Meng S., Ho E.C.H., Cahill M.J., Boyce K.J., Klose J., Klosterman S.J.,
RA Deelstra H.J., Ortiz-Castellanos L., Li W., Sanchez-Alonso P.,
RA Schreier P.H., Haeuser-Hahn I., Vaupel M., Koopmann E., Friedrich G.,
RA Voss H., Schlueter T., Margolis J., Platt D., Swimmer C., Gnirke A.,
RA Chen F., Vysotskaia V., Mannhaupt G., Gueldener U., Muensterkoetter M.,
RA Haase D., Oesterheld M., Mewes H.-W., Mauceli E.W., DeCaprio D., Wade C.M.,
RA Butler J., Young S.K., Jaffe D.B., Calvo S.E., Nusbaum C., Galagan J.E.,
RA Birren B.W.;
RT "Insights from the genome of the biotrophic fungal plant pathogen Ustilago
RT maydis.";
RL Nature 444:97-101(2006).
RN [2]
RP GENOME REANNOTATION.
RC STRAIN=521 / FGSC 9021;
RA Gueldener U., Muensterkoetter M., Walter M.C., Mannhaupt G., Kahmann R.;
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 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; CM003141; KIS71224.1; -; Genomic_DNA.
DR RefSeq; XP_011387079.1; XM_011388777.1.
DR AlphaFoldDB; Q4PFI5; -.
DR SMR; Q4PFI5; -.
DR STRING; 5270.UM01128P0; -.
DR EnsemblFungi; KIS71224; KIS71224; UMAG_01128.
DR GeneID; 23562235; -.
DR KEGG; uma:UMAG_01128; -.
DR VEuPathDB; FungiDB:UMAG_01128; -.
DR eggNOG; KOG3149; Eukaryota.
DR HOGENOM; CLU_051385_2_1_1; -.
DR InParanoid; Q4PFI5; -.
DR OMA; IKRVQFK; -.
DR OrthoDB; 1482359at2759; -.
DR Proteomes; UP000000561; Chromosome 2.
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..431
FT /note="Protein AF-9 homolog"
FT /id="PRO_0000215932"
FT DOMAIN 5..309
FT /note="YEATS"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00376"
FT REGION 80..113
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 193..274
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 383..419
FT /evidence="ECO:0000255"
FT COMPBIAS 80..100
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 194..208
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 211..235
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 243..262
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 431 AA; 45757 MW; E2564AEF2AB33DDF CRC64;
MSNKRVRGLA IHRPILYGST STPLTPAEKL AAPPDHTHKW TVAVRSAASL PLPSLSAISG
ASDGSSFEPG SEVGAINAAS GMATPSSSSA AGGSAATVST RGRDQEHDYH KMVGNKDDIS
HFIKRVQFKL HETYSQPTRN VDKFPFHITE TGWGEFEIQI KIFFVAEANE KPLTLFHHLK
LHPWLQNVAA VETEPPAPPA PSLPAPLPPA DMSATNSSVE QDGQASTSAN GTKQEAGPDS
MEVDPTASST TEQQTSTDAK VESTPVAEPA VATTEPLKPA LPPVVHSWQY DEIVFPEPME
AFYDILSTHP PTPLPVVSAL AFADPAAYRS YLYAKADAAK GNSTGPPPIP PHPLHTPTGY
LFDALSLEAQ NAEGERLEMA RIAAIKDLEK GREQLIKAEK ALKDARNRIA ALNNAALASC
TAVSGTVPPA S
