EAF1_ASPFU
ID EAF1_ASPFU Reviewed; 1467 AA.
AC Q4WP03;
DT 20-DEC-2005, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2005, sequence version 1.
DT 03-AUG-2022, entry version 111.
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=AFUA_4G07560;
OS Neosartorya fumigata (strain ATCC MYA-4609 / Af293 / CBS 101355 / FGSC
OS A1100) (Aspergillus fumigatus).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC Aspergillus subgen. Fumigati.
OX NCBI_TaxID=330879;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC MYA-4609 / Af293 / CBS 101355 / FGSC A1100;
RX PubMed=16372009; DOI=10.1038/nature04332;
RA Nierman W.C., Pain A., Anderson M.J., Wortman J.R., Kim H.S., Arroyo J.,
RA Berriman M., Abe K., Archer D.B., Bermejo C., Bennett J.W., Bowyer P.,
RA Chen D., Collins M., Coulsen R., Davies R., Dyer P.S., Farman M.L.,
RA Fedorova N., Fedorova N.D., Feldblyum T.V., Fischer R., Fosker N.,
RA Fraser A., Garcia J.L., Garcia M.J., Goble A., Goldman G.H., Gomi K.,
RA Griffith-Jones S., Gwilliam R., Haas B.J., Haas H., Harris D.E.,
RA Horiuchi H., Huang J., Humphray S., Jimenez J., Keller N., Khouri H.,
RA Kitamoto K., Kobayashi T., Konzack S., Kulkarni R., Kumagai T., Lafton A.,
RA Latge J.-P., Li W., Lord A., Lu C., Majoros W.H., May G.S., Miller B.L.,
RA Mohamoud Y., Molina M., Monod M., Mouyna I., Mulligan S., Murphy L.D.,
RA O'Neil S., Paulsen I., Penalva M.A., Pertea M., Price C., Pritchard B.L.,
RA Quail M.A., Rabbinowitsch E., Rawlins N., Rajandream M.A., Reichard U.,
RA Renauld H., Robson G.D., Rodriguez de Cordoba S., Rodriguez-Pena J.M.,
RA Ronning C.M., Rutter S., Salzberg S.L., Sanchez M., Sanchez-Ferrero J.C.,
RA Saunders D., Seeger K., Squares R., Squares S., Takeuchi M., Tekaia F.,
RA Turner G., Vazquez de Aldana C.R., Weidman J., White O., Woodward J.R.,
RA Yu J.-H., Fraser C.M., Galagan J.E., Asai K., Machida M., Hall N.,
RA Barrell B.G., Denning D.W.;
RT "Genomic sequence of the pathogenic and allergenic filamentous fungus
RT Aspergillus fumigatus.";
RL Nature 438:1151-1156(2005).
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; AAHF01000005; EAL90031.1; -; Genomic_DNA.
DR RefSeq; XP_752069.1; XM_746976.1.
DR AlphaFoldDB; Q4WP03; -.
DR STRING; 746128.CADAFUBP00006290; -.
DR PRIDE; Q4WP03; -.
DR EnsemblFungi; EAL90031; EAL90031; AFUA_4G07560.
DR GeneID; 3509005; -.
DR KEGG; afm:AFUA_4G07560; -.
DR VEuPathDB; FungiDB:Afu4g07560; -.
DR eggNOG; ENOG502RGMX; Eukaryota.
DR HOGENOM; CLU_001331_1_0_1; -.
DR InParanoid; Q4WP03; -.
DR OMA; SKTQYFR; -.
DR OrthoDB; 195829at2759; -.
DR Proteomes; UP000002530; Chromosome 4.
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:0003682; F:chromatin binding; IBA:GO_Central.
DR GO; GO:0006325; P:chromatin organization; IEA:UniProtKB-KW.
DR GO; GO:0006281; P:DNA repair; IBA:GO_Central.
DR GO; GO:0043967; P:histone H4 acetylation; 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 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..1467
FT /note="Chromatin modification-related protein eaf1"
FT /id="PRO_0000065814"
FT DOMAIN 607..686
FT /note="HSA"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00549"
FT DOMAIN 877..935
FT /note="Myb-like"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00133"
FT REGION 154..314
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 329..402
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 469..522
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 970..1058
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1113..1202
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1216..1307
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1377..1467
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 154..178
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 186..201
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 240..268
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 353..370
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 387..402
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 485..503
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 504..520
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 970..993
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 996..1029
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1030..1053
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1377..1452
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1453..1467
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1467 AA; 161131 MW; 24C135790B3A2EEA CRC64;
MLRDELLRSK NDEIARCLLS RKRKLSELYF ATVGFAGATE NAPTNALYHQ KEQTFLDAND
LTKGRYFNEA TLPPFPDFAA LIPRPEEQHS SLEITEPVVQ TDDVSSVIAP KAEGAVRGIA
PSFQQQEGQT AQVIEQRLVE DSLKKDDARI HQQPALATTS EIPQVANSPT TPAQPDQLPQ
KASFAVPDTP PTSTSHESVD ASVSPALKGL PPSEVAPPRA VSNQLPSAQR KPESRPSLVL
AQPSEDQPLS PASSAGPYSN NTPAPVAVSP DTSPAEEVTE GADEVALSPK RVGPVQLQPG
LVPSTPDEQL QLEAAQSLQQ NALASKSIGD VTTASSLSNE VIKEDVGPTP SAAADSSKET
QDQTSTSVEA PEPKRPDGVV VAPEESQPPA QSIQEETQSQ VGAEVKVVAS TTPAGKKPTA
AAVLPAQPER MTTRVSSGAI RHKSVSEILG ETPKPSAVQP EKAHAIEKPA DMVRAPASAS
PESAAKMRLK DRKAREKERS KLSTVVFPKQ QQQQQQQQEK DDSLDIVRQY AGELARLNEE
QDYLFTLFQN KAYAPPRGTN LSTLLASAHK TLTTSNHLLE YQEQMDCRTL RRIYALQNAN
RWPLRQLKRS VEPPRQGTHW DVLLDHMKWM RTDYREERKW KIAAAKSCAD WCAEYVNSDP
EHRALLRVPC RIPSKFEKKE AHASSMISPP EETTEEMLVV SQPTPDLIPS AEDESVSDGF
NDEIRHDIRD TVAPAAIFSL GSDEFTFSLD MTPAAQKLLD ELPIYTPVKI APGANVPMFE
QPPDSAWKTE LLPVSKYASG RIKFHETESP RKRSRYDYSQ YDSNPEHGML DLPPEQTNVA
LFRPENKPIR DRIHPGHSFR PPTEYPMPSV GFFESRQSSQ WTYAEDDELR RLVKEYSYNW
SLISSCLTPS SQFTSGAERR TPWECFERWV GLEGLPADMS KTQYFRAYHQ RIETAQRTVL
AQQQAAQQQQ QQQQQQQQQG GNNSGQAQPP IRRRTTQPVR VDRRRSSKHL ALLDAMRKLA
KKRETMLQKQ QHASHLASLR KVNDANQPKP PISSPAEFSR LKYDRELKLQ ERQEQYRQQM
IAQQRANLAA QRAGQIPSQQ PMMNAPPGRT PNGIPHNPGT PGIPGATPNG MHNGMPNALP
NGIPPGMGVS QGRPHMQGVP AGGPPMNGPI PPNPMAMKMM PQTGMPQGPG GRPGMPMQTS
PDNTRVMREA NRLQEQQRIL QSRQQQPQPP QHQQPQAQQA QQQFHNQQQF GPQGSHSPNM
NLPNVNGTPN NPAMMAAIQA GSGMQSPSLH NAMPQGVSTP SPRMGQPNLL SGGVVPTISS
IQSQIQRSNP NMPPEQVNKL ATDRLHQYQQ QRMSQVAMNA AAGNMASVQA NYQVPHDGNF
QSPQPGMNGT PGMQVPQSQG FSPMMRVPQP AQQNRMGVGN SPAMNVALPQ QSRSATPQTQ
RSGSAQAGPV PGSSKSPHPP QAQIPSG
