EAF1_NEUCR
ID EAF1_NEUCR Reviewed; 2189 AA.
AC Q7SBU6;
DT 20-DEC-2005, integrated into UniProtKB/Swiss-Prot.
DT 15-DEC-2003, sequence version 1.
DT 03-AUG-2022, entry version 114.
DE RecName: Full=Chromatin modification-related protein eaf-1;
DE AltName: Full=Esa-1-associated factor 1;
DE AltName: Full=Vacuolar import and degradation protein 21;
GN Name=eaf-1; Synonyms=vid-21; ORFNames=NCU07863;
OS Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 /
OS FGSC 987).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Sordariomycetidae; Sordariales; Sordariaceae; Neurospora.
OX NCBI_TaxID=367110;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987;
RX PubMed=12712197; DOI=10.1038/nature01554;
RA Galagan J.E., Calvo S.E., Borkovich K.A., Selker E.U., Read N.D.,
RA Jaffe D.B., FitzHugh W., Ma L.-J., Smirnov S., Purcell S., Rehman B.,
RA Elkins T., Engels R., Wang S., Nielsen C.B., Butler J., Endrizzi M.,
RA Qui D., Ianakiev P., Bell-Pedersen D., Nelson M.A., Werner-Washburne M.,
RA Selitrennikoff C.P., Kinsey J.A., Braun E.L., Zelter A., Schulte U.,
RA Kothe G.O., Jedd G., Mewes H.-W., Staben C., Marcotte E., Greenberg D.,
RA Roy A., Foley K., Naylor J., Stange-Thomann N., Barrett R., Gnerre S.,
RA Kamal M., Kamvysselis M., Mauceli E.W., Bielke C., Rudd S., Frishman D.,
RA Krystofova S., Rasmussen C., Metzenberg R.L., Perkins D.D., Kroken S.,
RA Cogoni C., Macino G., Catcheside D.E.A., Li W., Pratt R.J., Osmani S.A.,
RA DeSouza C.P.C., Glass N.L., Orbach M.J., Berglund J.A., Voelker R.,
RA Yarden O., Plamann M., Seiler S., Dunlap J.C., Radford A., Aramayo R.,
RA Natvig D.O., Alex L.A., Mannhaupt G., Ebbole D.J., Freitag M., Paulsen I.,
RA Sachs M.S., Lander E.S., Nusbaum C., Birren B.W.;
RT "The genome sequence of the filamentous fungus Neurospora crassa.";
RL Nature 422:859-868(2003).
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; CM002238; EAA33888.1; -; Genomic_DNA.
DR RefSeq; XP_963124.1; XM_958031.2.
DR AlphaFoldDB; Q7SBU6; -.
DR SMR; Q7SBU6; -.
DR STRING; 5141.EFNCRP00000007527; -.
DR EnsemblFungi; EAA33888; EAA33888; NCU07863.
DR GeneID; 3879263; -.
DR KEGG; ncr:NCU07863; -.
DR VEuPathDB; FungiDB:NCU07863; -.
DR HOGENOM; CLU_001331_0_0_1; -.
DR InParanoid; Q7SBU6; -.
DR OMA; SKTQYFR; -.
DR Proteomes; UP000001805; Chromosome 3, Linkage Group III.
DR GO; GO:0035267; C:NuA4 histone acetyltransferase complex; IEA:UniProt.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0008094; F:ATP-dependent activity, acting on DNA; IBA:GO_Central.
DR GO; GO:0003677; F:DNA binding; 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 CDD; cd00167; SANT; 1.
DR InterPro; IPR009057; Homeobox-like_sf.
DR InterPro; IPR014012; HSA_dom.
DR InterPro; IPR001005; SANT/Myb.
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..2189
FT /note="Chromatin modification-related protein eaf-1"
FT /id="PRO_0000065821"
FT DOMAIN 722..797
FT /note="HSA"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00549"
FT DOMAIN 985..1045
FT /note="Myb-like"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00133"
FT REGION 183..400
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 415..438
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 477..602
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1320..1428
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1622..1644
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1663..1831
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1846..2189
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 262..278
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 280..337
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 524..552
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 565..586
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1320..1402
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1410..1428
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1846..2087
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2099..2189
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 2189 AA; 239181 MW; 1CF53297CE03FE59 CRC64;
MTEVGPADRR KLLHSKRAEA NSIVTSRKRK LRELYAVATD EDGFPNHDLN DLDTRPASPG
EAKFLFDCEI LQGRRLAERL LPVFQRPRFD TLQHIATADE SSLGHGPHVV QQVQPSPLIH
PNHTIPKNVQ HNGLPSPAPP ASSIRHEPER TVPYNQVPNG AAGPQEALKA FAPRQEFQKL
APVQGSAVKT ADGPSGESKP PAKETPVLLA PAAPHGNGRW NGIINNAPQG RVLPTPQTVA
PPATAPTSTT KTANLGEGRA GPKDDTVSRG DAEEKARPKP TITSVNQLLS NGDSIRYPDT
LSSPSSTVQS APTPLGNEAS ASTSPDNEAS QSFDKPVSRP EQELRRATTD NKGVGQFTGP
SVAVPELRPQ PQQPGVYANG APEVPISSAP SVRPAASGAE AQLLQESAAT RTSQVIGKAG
VAGPHGAHST GGLQTQHPSA VNGEVRNMMN GDIPGKHVAS QASVSTGVAV TKAALPEVAK
QGPLPQGPES RNNRADVGPT PMDLDRIPTA QAPKPIPSVH AVQEKAPSQE SARQPQPSST
APSTTPPSAQ PAVSLEKTVP GIQINAPPET ETETQARTSQ SSHPDTESAV ADEEGDMPPG
LLTHRLKSLS TRLRERRRKS VPTVVFGKQY RKPRFSDDTA LIVNKPKPPG HIPSEDYFVT
LFIESFARTS SWMKPLEKLL HSAHKTVSTS DQTLSILDHQ ACKILRRVYH LQQHDKWSLR
QPVRCLEPAR PASHQDLLIK EMKWMRTDFR EERKWKRAVA RNLAYACAEW YYSSPADRKL
LQVDAKIPPV RAVDNADTSM ADAPETGESL VPELDHSDSP VGNDEEVPEL PITTIAPATI
FALQDDEVVF ELQPSRTADL LLENLPMYGS PLKVPKFDWI IPDYDPDAKW KRPAVPLSKY
VEGEMVLDVK PQPQKRSRFQ FQGEDEEEEE EYVFGAQPDK GAKLPPTSTD VALFAPEMKL
TRDRLHAGHQ FRPPSEHPMP VQSFFESRIA SQWTLAEDDQ LRALVREYSY NWSLISSMIS
SRSSFPSAVE RRTPWECFER WVNLEGLPSD FAKTPYFKAY QARIDAAGRT ILQHNQNAAQ
GQQVGPNGAV APIPRKRPTN TMRVERRRNQ KHLALFDAMR KLAKKREAAA QKQQAQATMT
AMRKTNEQQR QQPQQQLHLQ AKTPQEYSLM RAARDQQIAE KMAHLAARQH EIIQKRLLTQ
RQAQLAATPG VAQVPQTAAQ LAAANSLNNA AARLNIPGQM AVTAQKLAPG RVPMQAPAGI
PTVPAQLAAS GLVPPLPVAA IPQAQLQAMQ AQHRLPMVNP TPDINLVMQA RRIQDQQRAV
AVQLQQQQHQ QHQHQQHPQQ PQQQGQVQQQ VVSQQQQQQH QPQQQQQPQQ QQQLQQQQPQ
QQQPQHQQVQ TPQPAQQQPQ QPQVTQQPPP VPQVQINGVQ GSPTPMRPVV NSLNNGVYMS
SVSAQAMMAS FNAANSVAGM VTSPGAGLSM PMLPAGSPRG PQIPAQQLPY THIHTRLKEF
ETHFRNKNPG ATQDQIRQMA TEHLGRLIVQ TQQHAMNAAA GGVGHSLGTV ATTTSPHQYA
QLLRAQQQAQ AQQAQAQQQA PQPAQSQLTP AQLAQAQAAA AQKQKQAAAA AAQAKVLAQA
QMQTQTPAHQ PHQPQAQPHV QAQAMAAAQL QAQVQLQAQA AAQKQAAQAH PQAQSQGQGQ
PPQQTQRAHQ VQQVQGQQAH QLPQGSQSQQ IQQQVQQSPQ ARQQSQQPQM VRQPVQQAQQ
PQQLQQPQQS QKTPQMQPQQ QVQTPHQQAQ KAQQSQQAQL AQQQQHQQQQ QQQQHGQAQS
QGQIQGQGQA PGQGQAPGQG HAQGQVQGQV QGQVQGQVQG QVQGQVQGQV QGQAPGQVQP
QHAQHSRHTP NSQHAQHTQQ AQHARNAQQA HHTQQVQQAQ HVQQPQGLQG QRHGQVHGNG
QQLHQQHQHQ QQQPQQAQQT QQQRQQVHPA PQLPQAQPPQ HSHQAQAQHP QTQQAQAPQA
QAQQPQPPQQ AQAQQVQQPQ QAKLTQQAQQ AQQAQGQQAQ GQQAQGQQAQ SQQARAQQAQ
VQQAQVQQAQ VQQAQAQQAQ AQQAQAQQAQ AQAQAQSHGQ MQPQTQPQQQ PQPQPQSQPQ
AHQPQQASQQ VQHGLVGQQG QQNRQGQQGQ QSHQVQQAQQ PQVQQAQQPV ATPQSASQTS
QNSQPAQQAG MAQQQQGQGS GSAAPAPTK
