EAF11_USTMA
ID EAF11_USTMA Reviewed; 1654 AA.
AC Q4P209; A0A0D1CGL6;
DT 20-DEC-2005, integrated into UniProtKB/Swiss-Prot.
DT 19-JUL-2005, sequence version 1.
DT 03-AUG-2022, entry version 100.
DE RecName: Full=Chromatin modification-related protein EAF1;
DE AltName: Full=ESA1-associated factor 1;
DE AltName: Full=Vacuolar import and degradation protein 21;
GN Name=EAF1; Synonyms=VID21; ORFNames=UMAG_05854;
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 NuA4 histone acetyltransferase complex which
CC is involved in transcriptional activation of selected genes principally
CC by acetylation of nucleosomal histone H4 and H2A. The NuA4 complex is
CC also involved in DNA repair (By similarity). {ECO:0000250}.
CC -!- SUBUNIT: Component of the NuA4 histone acetyltransferase complex.
CC {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the EAF1 family. {ECO:0000305}.
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DR EMBL; CM003159; KIS66113.1; -; Genomic_DNA.
DR RefSeq; XP_011392216.1; XM_011393914.1.
DR AlphaFoldDB; Q4P209; -.
DR STRING; 5270.UM05854P0; -.
DR EnsemblFungi; KIS66113; KIS66113; UMAG_05854.
DR GeneID; 23565630; -.
DR KEGG; uma:UMAG_05854; -.
DR VEuPathDB; FungiDB:UMAG_05854; -.
DR eggNOG; ENOG502RGMX; Eukaryota.
DR HOGENOM; CLU_001948_0_0_1; -.
DR InParanoid; Q4P209; -.
DR OMA; LNTHETH; -.
DR OrthoDB; 252194at2759; -.
DR Proteomes; UP000000561; Chromosome 20.
DR GO; GO:0035267; C:NuA4 histone acetyltransferase complex; IEA:UniProt.
DR GO; GO:0004672; F:protein kinase activity; IBA:GO_Central.
DR GO; GO:0006325; P:chromatin organization; IEA:UniProtKB-KW.
DR GO; GO:0006281; P:DNA repair; IEA:UniProtKB-KW.
DR GO; GO:0016573; P:histone acetylation; IEA:UniProt.
DR GO; GO:0006468; P:protein phosphorylation; IBA:GO_Central.
DR CDD; cd00167; SANT; 1.
DR InterPro; IPR009057; Homeobox-like_sf.
DR InterPro; IPR014012; HSA_dom.
DR InterPro; IPR001005; SANT/Myb.
DR Pfam; PF07529; HSA; 1.
DR SMART; SM00573; HSA; 1.
DR SUPFAM; SSF46689; SSF46689; 1.
DR PROSITE; PS51204; HSA; 1.
DR PROSITE; PS50090; MYB_LIKE; 1.
PE 3: Inferred from homology;
KW Activator; Chromatin regulator; DNA damage; DNA repair; Nucleus;
KW Reference proteome; Transcription; Transcription regulation.
FT CHAIN 1..1654
FT /note="Chromatin modification-related protein EAF1"
FT /id="PRO_0000065823"
FT DOMAIN 536..611
FT /note="HSA"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00549"
FT DOMAIN 995..1048
FT /note="Myb-like"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00133"
FT REGION 1..66
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 204..229
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 609..679
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 693..720
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 883..902
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 974..993
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1057..1159
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1257..1304
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1449..1523
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1570..1654
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 20..55
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 622..636
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 643..657
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1075..1103
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1113..1131
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1132..1159
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1262..1304
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1449..1485
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1570..1604
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1612..1639
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1654 AA; 177844 MW; 00A3776E9BC93529 CRC64;
MSTEPVSSLA LPAPAILPTT PIPASTQQAS SLVSDQIQEA STASQKSVTS ITQPPIPSQQ
QPPQHITANH PASIAAAATV ALSATLLNPN EWNALASTSM VTLDDLRSAF LEQRQQQLKD
LERSHRESLR EMIFMSENYD KEDVAGSPWK LGQSLQVAED DAREHVKSFL DQHRLALDPK
MSIKDHILEQ PKLLRQRVSQ ELKTGPIELA PPPTPTSATA PSAGEAQRDR DLKREIEQNN
LHRSQAVARA AAAVQAHAIA EGVAKIKPLT ITAAESQGVR VAPLQPGQVP SFVIESTTPI
AHIVASSDSS TAVLVASDAQ KVDSHTTMSA AEAVTPAIKV ESTDNIDASP SKASHALEKA
VSPVPGLARN ASTQSTSLRV PPSPMVVPTI PENITAPPLH PTLQVLAPNP LSVTYAASLR
PLPPDPTRRI TGAGLSGGAI HHRSGRKITS LSNHSNVNSY SSIAAAKIGP AGSGQADLYR
WYVRARASPG AGMVGKADKC LMTSDWRVAF NEQRFVRAMA RIEKLKAQGE WSFRQPKKQK
GPVVRKAHWD HLLEEMKWLQ TDFREERRWK MTVAFHLAHE VAAWHRARTP AERAQFCVHV
QRSYRHRTIS DNVEQHNTDK LSAKEVVSSS QPFQAAAASL DDVEMTHSTS SSHIQKDGEP
ATVKAESGQP VEDADVTMDG GADADEAVTQ AVESALQTTN EAASARAEEM DADGEDDADT
DANDVEAATA ALVSGEPSKP PKVEVVREPL SQPQPMPTLA DVSVPTTSSA TPTVPASSTP
TTAANDKLVH ALRSQPKDAD STLTAEMPPQ LLATLRAPIF STSVTTTVVS PAALLDSLNP
EAAAALLGIE VSDLANAADL LEPGSLSFSK MFPELPLYGG VSLPESNSKS DRRWDEGSLN
QPPRLTHVTK LLDSRPLLVS TLEPSKNRAN GRWLADSDWV VAAEQSDPLR GVTDGADTAL
PPMPGSLLFA RKSNRAAKDA SGPASTTPAE PASPDARAAL FVWTPDEDNY LMTLAKQYHN
NWALVADLFN STRLNTATDK REAWDCYDRC KRIEQAAAEG KPPPGPPPMP APAADADKDS
KKGDGKDADA SSSKRDKLSK KSGSKHDGSK RKQRRSNLME VMRRSAKRRE ATKQAQQTQQ
TKKVNLNTHE THAQIKAGPA ITPQSLSALK TERDQAALRQ YYEQQRAQLA YQQQQQQQQR
LLAQQAQAQR MAQQQGTAGT SAPAATAVTQ AGKAGTAIVA GGTGGVGNVS LLPAGTPAAS
AGPAGQAQQK AATGQGTNQA IAQQTQQQQQ QPQSQQTAQM QVQQPPAAAA AAQQQQQQQV
QLQSQLQASQ AAQMQNLYAQ MQQQQQQQQR QQQQQLGQAA AGLAQVRPGV GALTQQQLAT
LTPQQQQQYH AQLAAATAAA QQQQLRSQMA AVAAAQGGQA GFQLPNAQAQ AQAQAQAQFQ
LMQQQQQQQN VMQNQGRPAM AQQAQQAALQ MYQQQQRQAQ MRPPQPTQPF AARPNARPGT
AASSQAKPQA AARSATPAPP MPATVQALQQ QLAISLATSN LSAEQINGLA IQLYKQAQQQ
QQQQQQQQQQ QQQQQQQQQQ QQQQQQQQQQ QQQQQQQQQQ PQQPAPTQQR PPPQQLLNQA
IQALAAQTQK NQQPAPTVHG VTGSPVRPPT PRPS
