AEF1_GIBZE
ID AEF1_GIBZE Reviewed; 1630 AA.
AC Q4IB96; A0A098E1Z8; A0A0E0SMF9; V6RA16;
DT 20-DEC-2005, integrated into UniProtKB/Swiss-Prot.
DT 07-SEP-2016, sequence version 2.
DT 03-AUG-2022, entry version 110.
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=FGRRES_05512, FGSG_05512;
OS Gibberella zeae (strain ATCC MYA-4620 / CBS 123657 / FGSC 9075 / NRRL 31084
OS / PH-1) (Wheat head blight fungus) (Fusarium graminearum).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Hypocreales; Nectriaceae; Fusarium.
OX NCBI_TaxID=229533;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC MYA-4620 / CBS 123657 / FGSC 9075 / NRRL 31084 / PH-1;
RX PubMed=17823352; DOI=10.1126/science.1143708;
RA Cuomo C.A., Gueldener U., Xu J.-R., Trail F., Turgeon B.G., Di Pietro A.,
RA Walton J.D., Ma L.-J., Baker S.E., Rep M., Adam G., Antoniw J., Baldwin T.,
RA Calvo S.E., Chang Y.-L., DeCaprio D., Gale L.R., Gnerre S., Goswami R.S.,
RA Hammond-Kosack K., Harris L.J., Hilburn K., Kennell J.C., Kroken S.,
RA Magnuson J.K., Mannhaupt G., Mauceli E.W., Mewes H.-W., Mitterbauer R.,
RA Muehlbauer G., Muensterkoetter M., Nelson D., O'Donnell K., Ouellet T.,
RA Qi W., Quesneville H., Roncero M.I.G., Seong K.-Y., Tetko I.V., Urban M.,
RA Waalwijk C., Ward T.J., Yao J., Birren B.W., Kistler H.C.;
RT "The Fusarium graminearum genome reveals a link between localized
RT polymorphism and pathogen specialization.";
RL Science 317:1400-1402(2007).
RN [2]
RP GENOME REANNOTATION.
RC STRAIN=ATCC MYA-4620 / CBS 123657 / FGSC 9075 / NRRL 31084 / PH-1;
RX PubMed=20237561; DOI=10.1038/nature08850;
RA Ma L.-J., van der Does H.C., Borkovich K.A., Coleman J.J., Daboussi M.-J.,
RA Di Pietro A., Dufresne M., Freitag M., Grabherr M., Henrissat B.,
RA Houterman P.M., Kang S., Shim W.-B., Woloshuk C., Xie X., Xu J.-R.,
RA Antoniw J., Baker S.E., Bluhm B.H., Breakspear A., Brown D.W.,
RA Butchko R.A.E., Chapman S., Coulson R., Coutinho P.M., Danchin E.G.J.,
RA Diener A., Gale L.R., Gardiner D.M., Goff S., Hammond-Kosack K.E.,
RA Hilburn K., Hua-Van A., Jonkers W., Kazan K., Kodira C.D., Koehrsen M.,
RA Kumar L., Lee Y.-H., Li L., Manners J.M., Miranda-Saavedra D.,
RA Mukherjee M., Park G., Park J., Park S.-Y., Proctor R.H., Regev A.,
RA Ruiz-Roldan M.C., Sain D., Sakthikumar S., Sykes S., Schwartz D.C.,
RA Turgeon B.G., Wapinski I., Yoder O., Young S., Zeng Q., Zhou S.,
RA Galagan J., Cuomo C.A., Kistler H.C., Rep M.;
RT "Comparative genomics reveals mobile pathogenicity chromosomes in
RT Fusarium.";
RL Nature 464:367-373(2010).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC MYA-4620 / CBS 123657 / FGSC 9075 / NRRL 31084 / PH-1;
RX PubMed=26198851; DOI=10.1186/s12864-015-1756-1;
RA King R., Urban M., Hammond-Kosack M.C.U., Hassani-Pak K.,
RA Hammond-Kosack K.E.;
RT "The completed genome sequence of the pathogenic ascomycete fungus Fusarium
RT graminearum.";
RL BMC Genomics 16:544-544(2015).
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}.
CC -!- SEQUENCE CAUTION:
CC Sequence=ESU11483.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; DS231665; ESU11483.1; ALT_SEQ; Genomic_DNA.
DR EMBL; HG970334; CEF87622.1; -; Genomic_DNA.
DR RefSeq; XP_011324059.1; XM_011325757.1.
DR AlphaFoldDB; Q4IB96; -.
DR SMR; Q4IB96; -.
DR STRING; 5518.FGSG_05512P0; -.
DR PRIDE; Q4IB96; -.
DR EnsemblFungi; ESU11483; ESU11483; FGSG_05512.
DR GeneID; 23552691; -.
DR KEGG; fgr:FGSG_05512; -.
DR eggNOG; ENOG502RGMX; Eukaryota.
DR HOGENOM; CLU_001331_0_0_1; -.
DR InParanoid; Q4IB96; -.
DR PHI-base; PHI:1546; -.
DR Proteomes; UP000070720; Chromosome 3.
DR GO; GO:0035267; C:NuA4 histone acetyltransferase complex; IEA:UniProt.
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 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 SMART; SM00717; SANT; 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..1630
FT /note="Chromatin modification-related protein EAF1"
FT /id="PRO_0000065819"
FT DOMAIN 773..847
FT /note="HSA"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00549"
FT DOMAIN 1043..1097
FT /note="Myb-like"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00133"
FT REGION 196..619
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 638..699
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 959..994
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1176..1215
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1308..1332
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1380..1412
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1550..1630
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 196..254
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 276..293
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 303..380
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 393..439
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 447..477
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 486..514
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 638..660
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 959..976
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1184..1210
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1630 AA; 176980 MW; D2BE55DAD9F1C847 CRC64;
MRKDTYSSLI STAFSALSCK PPKHHSIVSP ETENLTPSSD VALNIDTPKS INNNLFHRQK
PVHSSQETSN YFLQRPFHPK TDVAAVDAMT EVGAADLSRL LQSKRNECSS IVTSRKRKLR
ELFVVATQSE GLPHPVLTNP DAPTTTPAEW QFLQANDINQ SKTLNEASIP TRPTFSLEVL
KKSLAKSIFI ANESVPKQTS ENSNKSHVTD AQDEQQSNRA SLSTKSDAAA TSTRPNTPET
STESATTANP VPPPAKNTQA VLPPADAIEK PIPTTSPDVP ASTGANANSI TNEEDRSDPN
EVASVPRQPQ VTFETGTKGE HVETGTSSVK SGHGVGDSAV TTGVPSTVKP SADVTRSADA
LSSPGSTAQS ATTPAVHDDA STDTSPEHEG PQYVEPAEQK KIEDGTHERD TDKYHQSHQD
GDIRAPSTKD LEDRVLEAPP DSAEAQLLQE SIRSNVAAEN EAALNSESTS QEADTAISAP
VSEDVNMSDV DDRVVKAAPT VGEKVEEKRA QQILDTDAKS ALATGAPAEI SGSKEIPDSQ
EEAPEQMDVD APEPKASTES QIGAPISLEK LDAADTGPSS PTPAHIAEVA TPPEPVRQNS
PPKAERAVTR VSSGAMRPKS VSEIVGVTPR QTPTLEHIST NKSTNHQLTP LTSTPKSPTL
RHRHISAHQR QASRSQPSTV VFGKQSKKGE EKSMVTSQHD TILPTEDYYT PLFVQGFAGS
SSWMQPIEKI LYTANKTVTT PDANLAIQDH QACKVLRRVY HLQQHDKWSL RQPKRCPEPT
RPPSHWDVVL QEMKWMRTDF REERKWKRAV AKNLAYACAE WHEATPEERK TLQVQAVVPP
KMKPASDVAM VDAEGTNHLT PDLVSSEDVE SIDNLDDLIE DFPETIAPSA IFNLQDEDVV
FGLRRTAAAD QLLEELPMFG APLQVPKFDL TGPEWDPDAH WRRPALPLSK YVEGHMKLVS
DGPPRKRSRY NYQNEDSDDE GEAGFVSSDS TPSLPLPSAT DEVALFNPEM KHIRDRLYVG
HQFRPPSEYP MPSQSFFECR SPSQWTIAED DELRSLVREH SYNWSLISSI LAPRSIFNSG
AERRTPWECF ERWINLEGLP ADMSKTQYFK AYMGRINTAQ NMINIQNQAM AQQQVNQANG
AVTPGRRRHQ SIPFRVERRR NQKHLTMLDA MRKLAKKRET TAQKQQHTAS QNAANKKTNE
SASQRPTKTP GEYSRLRYER DQALAEKMAQ FASRQEAQRR AVLQARAQGQ AAQMAAGTPA
AVQAGQNSAQ AAAAAAAAAA AANGMNGVGR VNVPNQLAAA AAAATGQARP RMPMQSPAPA
SMGGVPAHMA SGLVPPNQMN SVQQAQMQAM QAMQGQHNRM PMPNPPPDVS LMMRAQRISE
QQRAAQMHAQ GGPGTPGQGA VGAQQSPPAQ MRNAMNGVNG INSNPMNQQS FLNNAQAMMA
QFNQGNLSSP QANGLHMPSG PAGSIAPRPQ TQLPAAIQAQ LNQLEAQYRA KNSSLTSEQA
RQMATEHLTR LMMAQRSAMN AAAGTAGGQG GLAGSIAATT SPHQYAALLR QQQQQQASAA
AGSPGQQHQQ PHQAQHQPQQ QQSQQQQAQA KQQQPQQQVQ AHAHAQAQHQ AQQQQQQQRQ
ASGSATPSAG
