EAF1_CRYNJ
ID EAF1_CRYNJ Reviewed; 985 AA.
AC P0CO98; Q55V60; Q5KL22;
DT 28-JUN-2011, integrated into UniProtKB/Swiss-Prot.
DT 28-JUN-2011, sequence version 1.
DT 03-AUG-2022, entry version 52.
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; OrderedLocusNames=CNC01040;
OS Cryptococcus neoformans var. neoformans serotype D (strain JEC21 / ATCC
OS MYA-565) (Filobasidiella neoformans).
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Tremellomycetes;
OC Tremellales; Cryptococcaceae; Cryptococcus;
OC Cryptococcus neoformans species complex.
OX NCBI_TaxID=214684;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JEC21 / ATCC MYA-565;
RX PubMed=15653466; DOI=10.1126/science.1103773;
RA Loftus B.J., Fung E., Roncaglia P., Rowley D., Amedeo P., Bruno D.,
RA Vamathevan J., Miranda M., Anderson I.J., Fraser J.A., Allen J.E.,
RA Bosdet I.E., Brent M.R., Chiu R., Doering T.L., Donlin M.J., D'Souza C.A.,
RA Fox D.S., Grinberg V., Fu J., Fukushima M., Haas B.J., Huang J.C.,
RA Janbon G., Jones S.J.M., Koo H.L., Krzywinski M.I., Kwon-Chung K.J.,
RA Lengeler K.B., Maiti R., Marra M.A., Marra R.E., Mathewson C.A.,
RA Mitchell T.G., Pertea M., Riggs F.R., Salzberg S.L., Schein J.E.,
RA Shvartsbeyn A., Shin H., Shumway M., Specht C.A., Suh B.B., Tenney A.,
RA Utterback T.R., Wickes B.L., Wortman J.R., Wye N.H., Kronstad J.W.,
RA Lodge J.K., Heitman J., Davis R.W., Fraser C.M., Hyman R.W.;
RT "The genome of the basidiomycetous yeast and human pathogen Cryptococcus
RT neoformans.";
RL Science 307:1321-1324(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; AE017343; AAW42657.1; -; Genomic_DNA.
DR RefSeq; XP_569964.1; XM_569964.1.
DR AlphaFoldDB; P0CO98; -.
DR STRING; 5207.AAW42657; -.
DR PaxDb; P0CO98; -.
DR EnsemblFungi; AAW42657; AAW42657; CNC01040.
DR eggNOG; KOG0391; Eukaryota.
DR HOGENOM; CLU_268842_0_0_1; -.
DR InParanoid; P0CO98; -.
DR OMA; LNTHETH; -.
DR OrthoDB; 157253at2759; -.
DR Proteomes; UP000002149; Chromosome 3.
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; IPR017930; Myb_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.
PE 3: Inferred from homology;
KW Activator; Chromatin regulator; Coiled coil; DNA damage; DNA repair;
KW Nucleus; Reference proteome; Transcription; Transcription regulation.
FT CHAIN 1..985
FT /note="Chromatin modification-related protein EAF1"
FT /id="PRO_0000065816"
FT DOMAIN 24..100
FT /note="HSA"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00549"
FT DOMAIN 412..471
FT /note="Myb-like"
FT REGION 124..230
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 275..295
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 475..575
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 773..813
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 932..985
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 591..664
FT /evidence="ECO:0000255"
FT COMPBIAS 130..167
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 171..200
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 215..229
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 495..542
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 561..575
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 773..802
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 985 AA; 106869 MW; DED28589A7573AB3 CRC64;
MRHVRAMERI EAKKAENRWS LRQPKKARGP GVPKSHWDYM LEEMEWMRTD FAEERRWKVV
EAREFAYQVV EWHLASPEEK KALMVGGRGW GECRNVPIPG HAGKRKEVTV EVEAEDEDVE
MLVGQEGELD GEGEANKVLE SIDEMRVNEK ERENRPEDPR ETVNINQDIG EEVDAEGEAD
ADGEPENGEA DAEGEADADG GPVGDDVVGL SEIDAAQDDT RETSERPSYR RDTVLPNGLV
IHKRFANAYE IAIARGPVLD TPLANATVDL DTLTKSSSAA TPATVPAEPS VSPDEPASFD
QLFPDLAMYS GPAPPENDKK YRRDEGGTYS HRMAHTSRIM DIRPILVSTL QPAKNLIDGE
WDLHDGPYYE EVKGAADIPP NVVAAFNTPF GGKASRPLEH MRVPEVPKPA AHHLRAQLLW
SPEEDKCLLK LVAMYPFNWD LIADSFNTEM ILIPVEKRNP YECWERWYYT FGEGKNKPRQ
DAPPSAPPPA PASATQPGTA TATPVPQSAV TTPGVPPSAN LPSASGRPQQ TGGNSVSSLP
TPTGEALPDG APPPPGMSKR DRMAAKPKYE GTKRSVRHQA IYDAVKRMNR RREAARAKSH
KDNAQRKVIN VHESHSMSFP HVAASTPWEL VEAKYQRDVQ IAQQRQQRAM QEQQRQLAIR
QQQAMMSAQQ QAQMRPPNMP NVPNMPNAQP IRMGPNGQPM PTMAPSQQQL LNAVAAATAA
NRQNANGAVQ GNPNVRPMPV VQGQSPQVQQ QMLLQAQQMA AQQARVLQAQ AQAQAQQGRA
PSMGGNLQPP QLGVSSPFAQ SRTPDLPAEG AGPSGINPTP SPAMQAAAIG AQSSPQIATM
GRAPSNNVPP HLRVPNAGTS SPQISSPMAL PQGIPNGAGM PVQGAQTQGI QIPAAMMNNA
TVQQLLATLA ASGQQMTPEQ LRGLMLRSAH MQAQAQSQVG NPGTPQMGVQ NIQGVQHFAR
SPSLQNAQSQ PRSSPKPGPA NGQGT
