ID A0A1E3Q147_LIPST Unreviewed; 640 AA.
AC A0A1E3Q147;
DT 18-JAN-2017, integrated into UniProtKB/TrEMBL.
DT 18-JAN-2017, sequence version 1.
DT 27-MAR-2024, entry version 28.
DE RecName: Full=Chromatin modification-related protein EAF1 {ECO:0000256|ARBA:ARBA00018561};
DE AltName: Full=ESA1-associated factor 1 {ECO:0000256|ARBA:ARBA00032084};
DE AltName: Full=Vacuolar import and degradation protein 21 {ECO:0000256|ARBA:ARBA00029670};
GN ORFNames=LIPSTDRAFT_112780 {ECO:0000313|EMBL:ODQ71278.1};
OS Lipomyces starkeyi NRRL Y-11557.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Lipomycetaceae; Lipomyces.
OX NCBI_TaxID=675824 {ECO:0000313|EMBL:ODQ71278.1, ECO:0000313|Proteomes:UP000094385};
RN [1] {ECO:0000313|EMBL:ODQ71278.1, ECO:0000313|Proteomes:UP000094385}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NRRL Y-11557 {ECO:0000313|EMBL:ODQ71278.1,
RC ECO:0000313|Proteomes:UP000094385};
RX PubMed=27535936; DOI=10.1073/pnas.1603941113;
RA Riley R., Haridas S., Wolfe K.H., Lopes M.R., Hittinger C.T., Goeker M.,
RA Salamov A.A., Wisecaver J.H., Long T.M., Calvey C.H., Aerts A.L.,
RA Barry K.W., Choi C., Clum A., Coughlan A.Y., Deshpande S., Douglass A.P.,
RA Hanson S.J., Klenk H.-P., LaButti K.M., Lapidus A., Lindquist E.A.,
RA Lipzen A.M., Meier-Kolthoff J.P., Ohm R.A., Otillar R.P., Pangilinan J.L.,
RA Peng Y., Rokas A., Rosa C.A., Scheuner C., Sibirny A.A., Slot J.C.,
RA Stielow J.B., Sun H., Kurtzman C.P., Blackwell M., Grigoriev I.V.,
RA Jeffries T.W.;
RT "Comparative genomics of biotechnologically important yeasts.";
RL Proc. Natl. Acad. Sci. U.S.A. 113:9882-9887(2016).
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. {ECO:0000256|ARBA:ARBA00025178}.
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DR EMBL; KV454298; ODQ71278.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1E3Q147; -.
DR STRING; 675824.A0A1E3Q147; -.
DR OrthoDB; 1334563at2759; -.
DR Proteomes; UP000094385; Unassembled WGS sequence.
DR GO; GO:0006325; P:chromatin organization; IEA:UniProtKB-KW.
DR CDD; cd00167; SANT; 1.
DR InterPro; IPR014012; HSA_dom.
DR InterPro; IPR001005; SANT/Myb.
DR PANTHER; PTHR46459:SF1; E1A-BINDING PROTEIN P400; 1.
DR PANTHER; PTHR46459; E1A-BINDING PROTEIN P400-RELATED; 1.
DR Pfam; PF07529; HSA; 1.
DR Pfam; PF13921; Myb_DNA-bind_6; 1.
DR SMART; SM00573; HSA; 1.
DR SMART; SM00717; SANT; 1.
DR PROSITE; PS50090; MYB_LIKE; 1.
PE 4: Predicted;
KW Chromatin regulator {ECO:0000256|ARBA:ARBA00022853};
KW Reference proteome {ECO:0000313|Proteomes:UP000094385};
KW Transcription {ECO:0000256|ARBA:ARBA00023163};
KW Transcription regulation {ECO:0000256|ARBA:ARBA00023015}.
FT DOMAIN 510..564
FT /note="Myb-like"
FT /evidence="ECO:0000259|PROSITE:PS50090"
FT REGION 112..166
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 436..476
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 129..143
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 149..166
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 439..469
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 640 AA; 72794 MW; 20DAC4363177737F CRC64;
MDFSSDRLDR LRFENIERRR QLCSDVVKSR KRKLSELYFL SRSPLLPITD EIISSEDDFL
MAFLEKNDLE SGHLFEESSL PQILYTNKVK KLDTIESIHQ AATHQHRVHA HAVSQPGATA
QHVPPSPEQR IAAPRPPQHP PQHQPLNGHA AQLHHTTPTS PHERMTTRVS SGALKHKSVT
ELLGATPKAA PRRVSNASTI EAVLVAKPKP TLRVMATEEP PVKPGVPLVK IYYNIQASAL
ANLIPSAHKS LTTDNFLTIY TESILQRTFG RIDELKREGK WSLRQPQRFR APKRSKSHWD
HVLGEMQITA LDFANKHKRK VTESTDIASS IRDYWTYGKS VCIKTRPPRI LTDEEVEAAN
SGETTNGLKD SASHGSLFSM NGMNKLTGIF AEQHYASIDP SKDELFRDSI EELPIVPINK
FAMLITNISP ERVASWKHQH SENANSTETV NDALQAPQPP SLQQPQRGEG EDNSTHRPLF
LSEATRRGVY IKAPPPPSLK YVEFGVPTIW LPQDDANLLR LASEFMYNWD VVSANMSSRQ
SWGFHSNIER RTPWECFERW MQLEPNFQLS DLRGPYARAA QFWIEATSRA QLATKRRMVP
MGITPDNSQR GQRRLRWSGI FEAIRKSIRK RENSRRFGSR
//
