ID A8B8D6_DROSI Unreviewed; 827 AA.
AC A8B8D6;
DT 13-NOV-2007, integrated into UniProtKB/TrEMBL.
DT 13-NOV-2007, sequence version 1.
DT 24-JAN-2024, entry version 67.
DE RecName: Full=Histone acetyltransferase {ECO:0000256|ARBA:ARBA00013184, ECO:0000256|RuleBase:RU361211};
DE EC=2.3.1.48 {ECO:0000256|ARBA:ARBA00013184, ECO:0000256|RuleBase:RU361211};
OS Drosophila simulans (Fruit fly).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC Drosophilidae; Drosophila; Sophophora.
OX NCBI_TaxID=7240 {ECO:0000313|EMBL:ABU97237.1};
RN [1] {ECO:0000313|EMBL:ABU97237.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=Congo 11 {ECO:0000313|EMBL:ABU97237.1};
RX PubMed=17878295; DOI=10.1073/pnas.0707445104;
RA Rodriguez M.A., Vermaak D., Bayes J.J., Malik H.S.;
RT "Species-specific positive selection of the male-specific lethal complex
RT that participates in dosage compensation in Drosophila.";
RL Proc. Natl. Acad. Sci. U.S.A. 104:15412-15417(2007).
CC -!- CATALYTIC ACTIVITY:
CC Reaction=acetyl-CoA + L-lysyl-[protein] = CoA + H(+) + N(6)-acetyl-L-
CC lysyl-[protein]; Xref=Rhea:RHEA:45948, Rhea:RHEA-COMP:9752,
CC Rhea:RHEA-COMP:10731, ChEBI:CHEBI:15378, ChEBI:CHEBI:29969,
CC ChEBI:CHEBI:57287, ChEBI:CHEBI:57288, ChEBI:CHEBI:61930; EC=2.3.1.48;
CC Evidence={ECO:0000256|RuleBase:RU361211};
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|RuleBase:RU361211}.
CC -!- SIMILARITY: Belongs to the MYST (SAS/MOZ) family.
CC {ECO:0000256|ARBA:ARBA00010107, ECO:0000256|RuleBase:RU361211}.
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DR EMBL; EF630394; ABU97237.1; -; Genomic_DNA.
DR AlphaFoldDB; A8B8D6; -.
DR GO; GO:0072487; C:MSL complex; IEA:EnsemblMetazoa.
DR GO; GO:0044545; C:NSL complex; IEA:EnsemblMetazoa.
DR GO; GO:0000228; C:nuclear chromosome; IEA:EnsemblMetazoa.
DR GO; GO:0005705; C:polytene chromosome interband; IEA:EnsemblMetazoa.
DR GO; GO:0005667; C:transcription regulator complex; IEA:EnsemblMetazoa.
DR GO; GO:0016456; C:X chromosome located dosage compensation complex, transcription activating; IEA:EnsemblMetazoa.
DR GO; GO:0003682; F:chromatin binding; IEA:EnsemblMetazoa.
DR GO; GO:0046972; F:histone H4K16 acetyltransferase activity; IEA:EnsemblMetazoa.
DR GO; GO:0030330; P:DNA damage response, signal transduction by p53 class mediator; IEA:EnsemblMetazoa.
DR GO; GO:0140861; P:DNA repair-dependent chromatin remodeling; IEA:EnsemblMetazoa.
DR GO; GO:0051091; P:positive regulation of DNA-binding transcription factor activity; IEA:EnsemblMetazoa.
DR GO; GO:0007549; P:sex-chromosome dosage compensation; IEA:EnsemblMetazoa.
DR CDD; cd18984; CBD_MOF_like; 1.
DR CDD; cd04301; NAT_SF; 1.
DR Gene3D; 2.30.30.140; -; 1.
DR Gene3D; 3.40.630.30; -; 1.
DR Gene3D; 3.30.60.60; N-acetyl transferase-like; 1.
DR Gene3D; 1.10.10.10; Winged helix-like DNA-binding domain superfamily/Winged helix DNA-binding domain; 1.
DR InterPro; IPR016181; Acyl_CoA_acyltransferase.
DR InterPro; IPR016197; Chromo-like_dom_sf.
DR InterPro; IPR002717; HAT_MYST-type.
DR InterPro; IPR025995; Tudor-knot.
DR InterPro; IPR036388; WH-like_DNA-bd_sf.
DR InterPro; IPR040706; Zf-MYST.
DR PANTHER; PTHR10615; HISTONE ACETYLTRANSFERASE; 1.
DR PANTHER; PTHR10615:SF82; HISTONE ACETYLTRANSFERASE KAT8; 1.
DR Pfam; PF01853; MOZ_SAS; 1.
DR Pfam; PF11717; Tudor-knot; 1.
DR Pfam; PF17772; zf-MYST; 1.
DR SUPFAM; SSF55729; Acyl-CoA N-acyltransferases (Nat); 1.
DR SUPFAM; SSF54160; Chromo domain-like; 1.
DR PROSITE; PS51726; MYST_HAT; 1.
PE 3: Inferred from homology;
KW Acetylation {ECO:0000256|ARBA:ARBA00022990};
KW Nucleus {ECO:0000256|RuleBase:RU361211};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 538..813
FT /note="MYST-type HAT"
FT /evidence="ECO:0000259|PROSITE:PS51726"
FT REGION 1..190
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 239..274
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 289..311
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 324..364
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 448..476
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..16
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 55..74
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 80..94
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 95..117
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 137..152
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 154..170
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 241..258
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 331..351
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 714
FT /note="Proton donor/acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR602717-51"
SQ SEQUENCE 827 AA; 92632 MW; 82CF7363145FAF85 CRC64;
MSEAELEQTP SAGHVQEQPT EEEHEPEQEP TNAYTIGGPP RTPVEDAAAE LSASLDVSGS
DQSAEQSLDL SGAQTEAAEE SEPPAKRQHR DISPISEDST PASSTSTSST RSSSSSRYDD
VSEAEEAPPE PEPEQPQQQQ QEEKEEDGQE QVKSPVSVEL QAQEPAQPQE QEVEVDQEMD
TEDEPSSNTV ICVADINAYG TGSNIDDFVM DPDAPSNAII TEVVTIPAPL HLKGAQQLGL
PLAAPPPPPP PPVAEEVPET PASPTDDGEE PPAVGLSSYM RVRYMQESTP GLPTRLAPRD
PRQRNMPPPA VVLPVQTILS ANVEAISDDS SESSSSDDDE EEEEDEDDAL TMEHDSTSRE
TVITTGDPLM QKIDISENPD KIYYIRREDG TVHRGQVLQS RTTENPAAPE EYYVHYVGLN
RRLDGWVGRH RISDNADDLG GITVLPAPPL APDQPSTSRE MLAQQAAAAA AASSERQKRT
GNKDYYLSYC ENSRYDYSDR KMTRYQKRRY DEINHVQKSH AELTATQAAL EKEHESITKI
KYIDKLQFGN YEIDTWYFSP FPEEYGKART LYVCEYCLKY MRFRASYAYH LHECGRRRPP
GREIYRKGNI SIYEVNGKEE SLYCQLLCLM AKLFLDHKVL YFDMDPFLFY ILCETDKEGS
HIVGYFSKEK KSLENYNVAC ILVLPPHQRK GFGKLLIAFS YELSRKEGVI GSPEKPLSDL
GRLSYRSYWA YTLLELMKTR CAPEQITIKE LSEMSGITHD DIIYTLQSMK MIKYWKGQNV
ICVTSKTIQD HLQLPQFKQP KLTIDTDYLV WSPQNAASVV RAPGNSG
//
