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Database: UniProt
Entry: A0A120E7F9_9BASI
LinkDB: A0A120E7F9_9BASI
Original site: A0A120E7F9_9BASI 
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
//
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