ID A0A120E7F9_9BASI Unreviewed; 574 AA.
AC A0A120E7F9;
DT 13-APR-2016, integrated into UniProtKB/TrEMBL.
DT 13-APR-2016, sequence version 1.
DT 24-JAN-2024, entry version 38.
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};
GN ORFNames=RHOSPDRAFT_18612 {ECO:0000313|EMBL:KWU44014.1};
OS Rhodotorula sp. JG-1b.
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Pucciniomycotina;
OC Microbotryomycetes; Sporidiobolales; Sporidiobolaceae; Rhodotorula.
OX NCBI_TaxID=1305733 {ECO:0000313|EMBL:KWU44014.1, ECO:0000313|Proteomes:UP000062823};
RN [1] {ECO:0000313|EMBL:KWU44014.1, ECO:0000313|Proteomes:UP000062823}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JG-1b {ECO:0000313|EMBL:KWU44014.1,
RC ECO:0000313|Proteomes:UP000062823};
RG DOE Joint Genome Institute;
RA Goordial J., Raymond-Bouchard I., Riley R., Ronholm J., Shapiro N.,
RA Woyke T., Grigoriev I.V., Labutti K.M., Greer C., Whyte L., Bakermans C.;
RT "Draft genome of eurypsychrophile Rhodotorula sp. JG1b isolated from
RT permafrost in the hyper-arid Upper Elevation McMurdo Dry Valleys,
RT Antarctica.";
RL Submitted (DEC-2015) to the EMBL/GenBank/DDBJ databases.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(2E)-butenoyl-CoA + L-lysyl-[protein] = CoA + H(+) + N(6)-
CC (2E)-butenoyl-L-lysyl-[protein]; Xref=Rhea:RHEA:53908, Rhea:RHEA-
CC COMP:9752, Rhea:RHEA-COMP:13707, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:29969, ChEBI:CHEBI:57287, ChEBI:CHEBI:57332,
CC ChEBI:CHEBI:137954; Evidence={ECO:0000256|ARBA:ARBA00029286};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:53909;
CC Evidence={ECO:0000256|ARBA:ARBA00029286};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=2-hydroxyisobutanoyl-CoA + L-lysyl-[protein] = CoA + H(+) +
CC N(6)-(2-hydroxyisobutanoyl)-L-lysyl-[protein]; Xref=Rhea:RHEA:24180,
CC Rhea:RHEA-COMP:9752, Rhea:RHEA-COMP:15921, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:29969, ChEBI:CHEBI:57287, ChEBI:CHEBI:131780,
CC ChEBI:CHEBI:144968; Evidence={ECO:0000256|ARBA:ARBA00029298};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:24181;
CC Evidence={ECO:0000256|ARBA:ARBA00029298};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=acetyl-CoA + L-lysyl-[histone] = CoA + H(+) + N(6)-acetyl-L-
CC lysyl-[histone]; Xref=Rhea:RHEA:21992, Rhea:RHEA-COMP:9845,
CC Rhea:RHEA-COMP:11338, 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|ARBA:ARBA00024456};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:21993;
CC Evidence={ECO:0000256|ARBA:ARBA00024456};
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 -!- 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;
CC Evidence={ECO:0000256|ARBA:ARBA00029280};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:45949;
CC Evidence={ECO:0000256|ARBA:ARBA00029280};
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; KQ954483; KWU44014.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A120E7F9; -.
DR STRING; 1305733.A0A120E7F9; -.
DR OrthoDB; 118560at2759; -.
DR Proteomes; UP000062823; Unassembled WGS sequence.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0004402; F:histone acetyltransferase activity; IEA:UniProtKB-EC.
DR GO; GO:0106226; F:peptide 2-hydroxyisobutyryltransferase activity; IEA:RHEA.
DR GO; GO:0140064; F:peptide crotonyltransferase activity; IEA:RHEA.
DR GO; GO:0006355; P:regulation of DNA-templated transcription; IEA:InterPro.
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:SF161; HISTONE ACETYLTRANSFERASE KAT5; 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 Activator {ECO:0000256|ARBA:ARBA00023159};
KW DNA damage {ECO:0000256|ARBA:ARBA00022763};
KW DNA repair {ECO:0000256|ARBA:ARBA00023204};
KW Nucleus {ECO:0000256|RuleBase:RU361211};
KW Reference proteome {ECO:0000313|Proteomes:UP000062823};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 291..562
FT /note="MYST-type HAT"
FT /evidence="ECO:0000259|PROSITE:PS51726"
FT REGION 1..26
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 66..107
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 139..186
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 200..266
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 153..180
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 217..237
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 467
FT /note="Proton donor/acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR602717-51"
SQ SEQUENCE 574 AA; 65094 MW; B9C314FBDFFAE51A CRC64;
MLTSCLPTVN RPAEPPPKPV ISPPNTLTLS QIITGCKVYV ERTIHPERPD ETEVRKAEVL
SIRERKLGRA ERKERKARLR AAQDDQEAAE AQRKQLEEEE EKARSGGDRL EYYCHYVEFN
KRLDEWVPAS KILLSREVEW PVPPAPPAAP GSTRKNSRES STVPPASPSP AGSSVNGASS
EAKKAADAGN LLRKAAIRAA HEASVSNKRK AVDAELGTPD EDEDEDAEGE PDTDGDSEMV
DAQTGADGSV QPELADGSTD DGGEVPTFSK AREIEKLRTQ GSMTQSHSEV SRVKNLDRIQ
IGRHIVEAWY FSPYPVEYAH TPILYVCEFC LSFFASEKQI ERHRKKCTLK HPPGNEIYRD
DYVCFFEIDG RKQKTWCRNL CLLCKAFLDH KTLYYDVDPF MYYVMCSRDE YGLHFVGFFS
KEKESAENYN VACILTMPQF QRMGYGKLLI EFSYELSKKE QKLGSPEKPL SDLGLLSYRA
YWAETIVDLL INTKEDISID EIANKTAITH ADIMHTCQVL QLLKFHKGQH HLVVSPAVLE
QHERVKSKSR HMIDPSKLIW RPPVFTRQEL RFGY
//