EAF1_EMENI
ID EAF1_EMENI Reviewed; 1447 AA.
AC Q5B4Q8; C8V8G3;
DT 20-DEC-2005, integrated into UniProtKB/Swiss-Prot.
DT 26-APR-2005, sequence version 1.
DT 03-AUG-2022, entry version 108.
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=AN4472;
OS Emericella nidulans (strain FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 /
OS M139) (Aspergillus nidulans).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC Aspergillus subgen. Nidulantes.
OX NCBI_TaxID=227321;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139;
RX PubMed=16372000; DOI=10.1038/nature04341;
RA Galagan J.E., Calvo S.E., Cuomo C., Ma L.-J., Wortman J.R., Batzoglou S.,
RA Lee S.-I., Bastuerkmen M., Spevak C.C., Clutterbuck J., Kapitonov V.,
RA Jurka J., Scazzocchio C., Farman M.L., Butler J., Purcell S., Harris S.,
RA Braus G.H., Draht O., Busch S., D'Enfert C., Bouchier C., Goldman G.H.,
RA Bell-Pedersen D., Griffiths-Jones S., Doonan J.H., Yu J., Vienken K.,
RA Pain A., Freitag M., Selker E.U., Archer D.B., Penalva M.A., Oakley B.R.,
RA Momany M., Tanaka T., Kumagai T., Asai K., Machida M., Nierman W.C.,
RA Denning D.W., Caddick M.X., Hynes M., Paoletti M., Fischer R., Miller B.L.,
RA Dyer P.S., Sachs M.S., Osmani S.A., Birren B.W.;
RT "Sequencing of Aspergillus nidulans and comparative analysis with A.
RT fumigatus and A. oryzae.";
RL Nature 438:1105-1115(2005).
RN [2]
RP GENOME REANNOTATION.
RC STRAIN=FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139;
RX PubMed=19146970; DOI=10.1016/j.fgb.2008.12.003;
RA Wortman J.R., Gilsenan J.M., Joardar V., Deegan J., Clutterbuck J.,
RA Andersen M.R., Archer D., Bencina M., Braus G., Coutinho P., von Dohren H.,
RA Doonan J., Driessen A.J., Durek P., Espeso E., Fekete E., Flipphi M.,
RA Estrada C.G., Geysens S., Goldman G., de Groot P.W., Hansen K.,
RA Harris S.D., Heinekamp T., Helmstaedt K., Henrissat B., Hofmann G.,
RA Homan T., Horio T., Horiuchi H., James S., Jones M., Karaffa L.,
RA Karanyi Z., Kato M., Keller N., Kelly D.E., Kiel J.A., Kim J.M.,
RA van der Klei I.J., Klis F.M., Kovalchuk A., Krasevec N., Kubicek C.P.,
RA Liu B., Maccabe A., Meyer V., Mirabito P., Miskei M., Mos M., Mullins J.,
RA Nelson D.R., Nielsen J., Oakley B.R., Osmani S.A., Pakula T., Paszewski A.,
RA Paulsen I., Pilsyk S., Pocsi I., Punt P.J., Ram A.F., Ren Q., Robellet X.,
RA Robson G., Seiboth B., van Solingen P., Specht T., Sun J.,
RA Taheri-Talesh N., Takeshita N., Ussery D., vanKuyk P.A., Visser H.,
RA van de Vondervoort P.J., de Vries R.P., Walton J., Xiang X., Xiong Y.,
RA Zeng A.P., Brandt B.W., Cornell M.J., van den Hondel C.A., Visser J.,
RA Oliver S.G., Turner G.;
RT "The 2008 update of the Aspergillus nidulans genome annotation: a community
RT effort.";
RL Fungal Genet. Biol. 46:S2-13(2009).
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 ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AACD01000078; EAA60815.1; -; Genomic_DNA.
DR EMBL; BN001303; CBF77440.1; -; Genomic_DNA.
DR RefSeq; XP_662076.1; XM_656984.1.
DR AlphaFoldDB; Q5B4Q8; -.
DR SMR; Q5B4Q8; -.
DR STRING; 162425.CADANIAP00005974; -.
DR EnsemblFungi; CBF77440; CBF77440; ANIA_04472.
DR EnsemblFungi; EAA60815; EAA60815; AN4472.2.
DR GeneID; 2872267; -.
DR KEGG; ani:AN4472.2; -.
DR eggNOG; ENOG502RGMX; Eukaryota.
DR HOGENOM; CLU_001331_1_0_1; -.
DR InParanoid; Q5B4Q8; -.
DR OMA; SKTQYFR; -.
DR OrthoDB; 195829at2759; -.
DR Proteomes; UP000000560; Chromosome III.
DR Proteomes; UP000005890; Unassembled WGS sequence.
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..1447
FT /note="Chromatin modification-related protein eaf1"
FT /id="PRO_0000065818"
FT DOMAIN 569..644
FT /note="HSA"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00549"
FT DOMAIN 841..899
FT /note="Myb-like"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00133"
FT REGION 60..271
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 300..443
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 636..689
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 923..970
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1003..1023
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1180..1248
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1381..1447
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 114..133
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 149..175
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 219..252
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 300..328
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 349..387
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 923..953
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1381..1397
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1406..1447
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1447 AA; 158520 MW; B13142FE1969F736 CRC64;
MRSRYAGATE TFADSAYREK EQAFLDANDI TKGRYFNEAT LPALRSYAVP PVRETKVASL
PVPATTPASP NVAPAPALPQ AEARASEVAS QGALDAETQR VTAPHPVEKH PSYSGPQPSD
SRAAPQLAPG TTEISQKADG PAPEVRHAAQ NLQQGQKATS SLPDTPRSSQ DPSDATVRAD
QKDATKAIPS AQPAISTPKP QHDLPASPLP GRPVHVTDQP LSPVSSAGPY SNNTPAPTAA
SPATSTTEDV SAEKLPTPKR IAATQERSSF VPTTPDEQLR FEEAQSLQQN ALLVSQVKDG
AGTGPLTNQV ISEDLPSTST TANVAEGASE QVSKDLLPES KMPESTPAAI VESKSQPQSP
LGQASSQAET VVKDVAPGTQ LTKKTSSSPH PGPPPERMTT RVSSGAIRHK SVSEILGEAP
KTPVSPIEKP HTVEKPTDSA RAGVYDSTDS AKLRLKDRRA REKERNKFST VVFPKQQQQP
DKDGDMDLVR QQSGALIKLN EERDYLFTLF QNKAYAPPRG TALTALLSSA HKTLTTNNYL
LDYQEQMDCR ILRRIYDLQH ANRWPLRQLK RSAEPPRQAA HWDVLLDHMK WMRTDFREER
KWKLAAAKSC ADWCAEYIHS DPESRSMLRV QARIPPKDSP CKNGPQSATM VSPPAELGND
AMEISHPTPD LVPSSEEDSV SEGFPDEPRH GLQDTVAPAA IFSLGSDEFT FSLDMTPTAQ
KLLDELPIYT PVQIAPDTNL PRFKDLPDAS WKTEILPVSK YARGKIMFRE DEPARKRSRY
DYSQYSSGSE HPVVELPPEQ TNVALFQPEN RHIRDRIHPA QPFRPPTEYP MPSLGFLESR
QSSQWTYAED EELRSLVEEY SYNWSLISSC LTPSSQFTSG AERRTPWECF ERWAGIEGLP
SDMSKTAYFR AYHQRIDTAQ RNVMAQQAAA QQQQQQQQQQ GSNGNNQQPM PLIRRRGTQP
IRVDRRRSSK HLALLDAMRK LAKKRETILQ KQQHASQLAS LRKVNEANQP KPPISSPAEF
SRLKHERELK LQERQEQYRQ QMIAQQRASL AARAGQMPNQ QQMMNAPGRA PNAIPHNPNA
PPVSTSTANG LPNGISNPLA NGMPNGLPQN VGVNQGRPHV QGMHGSGGPV NNHISPNPMA
MKMMPQASMQ QNNAPRPNMA MQASPDNARV IREANRLQEQ QRILQSRQQP SQHPLQQQQP
PQAQNQQQQL PQQPQQAQQQ FHAQPQFVPQ GSNSPNLNMP TVNGTPNNPA MIAALQAGGG
MQSPPFHNSA PQGVSTPSPR MGQPNTLSSG AVPTTISTIQ SQIQRSNPNM PLEQVKQLTT
ERLHQYQQQQ QQRMSQVAMN AAAGNLGVQP NYQVSHDGNF QPQSGMSGGP NMQVPQAQGF
SPMMRVPQPS QQNRIGAGGS PAMGVAVPQQ SRSATPQTQR SGSIQTGTIA GASKSPNTHS
QTQSMGA
