ID E6ZGR5_DICLA Unreviewed; 547 AA.
AC E6ZGR5;
DT 08-MAR-2011, integrated into UniProtKB/TrEMBL.
DT 08-MAR-2011, sequence version 1.
DT 24-JAN-2024, entry version 54.
DE RecName: Full=histone acetyltransferase {ECO:0000256|ARBA:ARBA00013184};
DE EC=2.3.1.48 {ECO:0000256|ARBA:ARBA00013184};
GN Name=MYST2 {ECO:0000313|EMBL:CBN81249.1};
GN ORFNames=DLA_Ib00910 {ECO:0000313|EMBL:CBN81249.1};
OS Dicentrarchus labrax (European seabass) (Morone labrax).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Eupercaria; Moronidae; Dicentrarchus.
OX NCBI_TaxID=13489 {ECO:0000313|EMBL:CBN81249.1};
RN [1] {ECO:0000313|EMBL:CBN81249.1}
RP NUCLEOTIDE SEQUENCE.
RA Kuhl H., Tine M., Hecht J., Knaust F., Reinhardt R.;
RT "Analysis of single nucleotide polymorphisms in three chromosomes of
RT European sea bass Dicentrarchus labrax.";
RL Comp. Biochem. Physiol. Part D Genomics Proteomics 6:70-75(2011).
RN [2] {ECO:0000313|EMBL:CBN81249.1}
RP NUCLEOTIDE SEQUENCE.
RX DOI=10.1016/j.ygeno.2011.06.004;
RA Kuhl H., Tine M., Beck A., Timmermann B., Kodira C., Reinhardt R.;
RT "Directed sequencing and annotation of three Dicentrarchus labrax L.
RT chromosomes by applying Sanger- and pyrosequencing technologies on pooled
RT DNA of comparatively mapped BAC clones.";
RL Genomics 0:0-0(2011).
RN [3] {ECO:0000313|EMBL:CBN81249.1}
RP NUCLEOTIDE SEQUENCE.
RA Tine M., Kuhl H., Beck A., Bargelloni L., Reinhardt R.;
RT "Comparative analysis of intronless genes in teleost fish genomes: Insights
RT into their evolution and molecular function.";
RL Mar. Genomics 4:109-119(2011).
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
CC -!- SIMILARITY: Belongs to the MYST (SAS/MOZ) family.
CC {ECO:0000256|ARBA:ARBA00010107}.
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; FQ310507; CBN81249.1; -; Genomic_DNA.
DR AlphaFoldDB; E6ZGR5; -.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0004402; F:histone acetyltransferase activity; IEA:UniProtKB-EC.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0006355; P:regulation of DNA-templated transcription; IEA:InterPro.
DR Gene3D; 3.40.630.30; -; 1.
DR Gene3D; 4.10.320.30; -; 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; IPR002717; HAT_MYST-type.
DR InterPro; IPR036388; WH-like_DNA-bd_sf.
DR InterPro; IPR040706; Zf-MYST.
DR InterPro; IPR002515; Znf_C2H2C.
DR InterPro; IPR036060; Znf_C2H2C_sf.
DR PANTHER; PTHR10615; HISTONE ACETYLTRANSFERASE; 1.
DR PANTHER; PTHR10615:SF210; HISTONE ACETYLTRANSFERASE KAT7; 1.
DR Pfam; PF01853; MOZ_SAS; 1.
DR Pfam; PF01530; zf-C2HC; 1.
DR Pfam; PF17772; zf-MYST; 1.
DR SUPFAM; SSF55729; Acyl-CoA N-acyltransferases (Nat); 1.
DR SUPFAM; SSF103637; CCHHC domain; 1.
DR PROSITE; PS51726; MYST_HAT; 1.
DR PROSITE; PS51802; ZF_CCHHC; 1.
PE 3: Inferred from homology;
KW Acetylation {ECO:0000256|ARBA:ARBA00022990};
KW Acyltransferase {ECO:0000256|ARBA:ARBA00023315};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Nucleus {ECO:0000256|ARBA:ARBA00023242};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Transcription {ECO:0000256|ARBA:ARBA00023163};
KW Transcription regulation {ECO:0000256|ARBA:ARBA00023015};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000313|EMBL:CBN81249.1};
KW Zinc {ECO:0000256|ARBA:ARBA00022833};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW ProRule:PRU01143}.
FT DOMAIN 268..543
FT /note="MYST-type HAT"
FT /evidence="ECO:0000259|PROSITE:PS51726"
FT REGION 1..112
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 166..232
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 21..51
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 66..90
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 91..112
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 166..183
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 197..228
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 444
FT /note="Proton donor/acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR602717-51"
SQ SEQUENCE 547 AA; 62960 MW; A71A4BC160D8A80D CRC64;
MAGSGSDGTE DSDSSAEREQ TNSSESDGNM PKRQRLTRAS TRLSQSSQDT PDLKRTADHD
ESPPLTPTGN APSSESELDI SSPNASHDES QSKDQANRDS DKDLSHRPKR RRCHETYNFN
MKCPTPGCNS LGHLTGKHER HFAVSGCPLY HNLSADECKV KAISREKQEE ELKGQEESNS
RHATRHQTPT PKQSRYKEQV AEMRKGRNSG LQKEQKEKHM ENRQAHGNTR EPLLENITSD
YDLELFRKAQ ARASEDLEKL RIQGQITEGS NMIKTILFGR YELDTWYHSP YPEEYARLGR
LYVCEFCLKY MKSQTILRRH MAKCVWKHPP GDEVYRKGAI SVFEVDGKKN KIYCQNLCLL
AKLFLDHKTL YYDVEPFLFY VMTEADNTGC HLVGYFSKEK NSFLNYNVSC ILTMPQYMRQ
GFGKMLIDFS YLLSKVEEKV GSPERPLSDL GLISYRSYWK EVLLRYMYNF QGKEISIKEI
SQETAVNPVD IVSTLQSLQM LKYWKGKHLV LKRQDLIDEW KAKEIKRGNS NKTIDPSSLK
WTPPKGT
//
