HAT1_CANAL
ID HAT1_CANAL Reviewed; 413 AA.
AC Q59VF4; A0A1D8PDC8;
DT 21-MAR-2006, integrated into UniProtKB/Swiss-Prot.
DT 26-APR-2005, sequence version 1.
DT 03-AUG-2022, entry version 96.
DE RecName: Full=Histone acetyltransferase type B catalytic subunit;
DE EC=2.3.1.48 {ECO:0000250|UniProtKB:Q12341};
GN Name=HAT1; OrderedLocusNames=CAALFM_C104670WA;
GN ORFNames=CaO19.779, CaO19.8401;
OS Candida albicans (strain SC5314 / ATCC MYA-2876) (Yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Debaryomycetaceae; Candida/Lodderomyces clade; Candida.
OX NCBI_TaxID=237561;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SC5314 / ATCC MYA-2876;
RX PubMed=15123810; DOI=10.1073/pnas.0401648101;
RA Jones T., Federspiel N.A., Chibana H., Dungan J., Kalman S., Magee B.B.,
RA Newport G., Thorstenson Y.R., Agabian N., Magee P.T., Davis R.W.,
RA Scherer S.;
RT "The diploid genome sequence of Candida albicans.";
RL Proc. Natl. Acad. Sci. U.S.A. 101:7329-7334(2004).
RN [2]
RP GENOME REANNOTATION.
RC STRAIN=SC5314 / ATCC MYA-2876;
RX PubMed=17419877; DOI=10.1186/gb-2007-8-4-r52;
RA van het Hoog M., Rast T.J., Martchenko M., Grindle S., Dignard D.,
RA Hogues H., Cuomo C., Berriman M., Scherer S., Magee B.B., Whiteway M.,
RA Chibana H., Nantel A., Magee P.T.;
RT "Assembly of the Candida albicans genome into sixteen supercontigs aligned
RT on the eight chromosomes.";
RL Genome Biol. 8:RESEARCH52.1-RESEARCH52.12(2007).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND GENOME REANNOTATION.
RC STRAIN=SC5314 / ATCC MYA-2876;
RX PubMed=24025428; DOI=10.1186/gb-2013-14-9-r97;
RA Muzzey D., Schwartz K., Weissman J.S., Sherlock G.;
RT "Assembly of a phased diploid Candida albicans genome facilitates allele-
RT specific measurements and provides a simple model for repeat and indel
RT structure.";
RL Genome Biol. 14:RESEARCH97.1-RESEARCH97.14(2013).
CC -!- FUNCTION: Catalytic component of the histone acetylase B (HAT-B)
CC complex. Acetylates 'Lys-14' of histone H4 which is required for
CC telomeric silencing. Has intrinsic substrate specificity that modifies
CC lysine in recognition sequence GXGKXG. Involved in DNA double-strand
CC break repair. {ECO:0000250|UniProtKB:Q12341}.
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:0000250|UniProtKB:Q12341};
CC -!- SUBUNIT: Component of the HAT-B complex composed of at least HAT1 and
CC HAT2. The HAT-B complex binds to histone H4 tail (By similarity).
CC {ECO:0000250, ECO:0000250|UniProtKB:Q12341}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Nucleus {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the HAT1 family. {ECO:0000305}.
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DR EMBL; CP017623; AOW26141.1; -; Genomic_DNA.
DR RefSeq; XP_713589.1; XM_708496.2.
DR AlphaFoldDB; Q59VF4; -.
DR SMR; Q59VF4; -.
DR STRING; 237561.Q59VF4; -.
DR GeneID; 3644770; -.
DR KEGG; cal:CAALFM_C104670WA; -.
DR CGD; CAL0000199484; HAT1.
DR VEuPathDB; FungiDB:C1_04670W_A; -.
DR eggNOG; KOG2696; Eukaryota.
DR HOGENOM; CLU_036024_2_1_1; -.
DR InParanoid; Q59VF4; -.
DR OMA; YFINLDE; -.
DR OrthoDB; 708105at2759; -.
DR PHI-base; PHI:5282; -.
DR PRO; PR:Q59VF4; -.
DR Proteomes; UP000000559; Chromosome 1.
DR GO; GO:0000781; C:chromosome, telomeric region; IEA:GOC.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0000123; C:histone acetyltransferase complex; IEA:EnsemblFungi.
DR GO; GO:0005634; C:nucleus; IDA:CGD.
DR GO; GO:0003682; F:chromatin binding; IEA:EnsemblFungi.
DR GO; GO:0010485; F:H4 histone acetyltransferase activity; IBA:GO_Central.
DR GO; GO:0042393; F:histone binding; IEA:EnsemblFungi.
DR GO; GO:0006974; P:cellular response to DNA damage stimulus; IMP:CGD.
DR GO; GO:0034614; P:cellular response to reactive oxygen species; IMP:CGD.
DR GO; GO:0006281; P:DNA repair; IMP:CGD.
DR GO; GO:0016573; P:histone acetylation; IDA:CGD.
DR GO; GO:0043967; P:histone H4 acetylation; IBA:GO_Central.
DR GO; GO:2000221; P:negative regulation of pseudohyphal growth; IMP:CGD.
DR GO; GO:0036166; P:phenotypic switching; IMP:CGD.
DR GO; GO:0031509; P:subtelomeric heterochromatin assembly; IEA:EnsemblFungi.
DR Gene3D; 1.10.10.390; -; 1.
DR Gene3D; 3.90.360.10; -; 1.
DR InterPro; IPR016181; Acyl_CoA_acyltransferase.
DR InterPro; IPR000182; GNAT_dom.
DR InterPro; IPR019467; Hat1_N.
DR InterPro; IPR037113; Hat1_N_sf.
DR InterPro; IPR017380; Hist_AcTrfase_B-typ_cat-su.
DR InterPro; IPR013523; Hist_AcTrfase_HAT1_C.
DR PANTHER; PTHR12046; PTHR12046; 1.
DR Pfam; PF00583; Acetyltransf_1; 1.
DR Pfam; PF10394; Hat1_N; 1.
DR PIRSF; PIRSF038084; HAT-B_cat; 1.
DR SUPFAM; SSF55729; SSF55729; 1.
PE 3: Inferred from homology;
KW Acyltransferase; Chromatin regulator; Cytoplasm; DNA damage; DNA repair;
KW Nucleus; Reference proteome; Transferase.
FT CHAIN 1..413
FT /note="Histone acetyltransferase type B catalytic subunit"
FT /id="PRO_0000227719"
FT REGION 51..53
FT /note="Interaction with histone H4 N-terminus"
FT /evidence="ECO:0000250|UniProtKB:Q12341"
FT REGION 209..211
FT /note="Interaction with histone H4 N-terminus"
FT /evidence="ECO:0000250|UniProtKB:Q12341"
FT ACT_SITE 269
FT /note="Proton donor/acceptor"
FT /evidence="ECO:0000250|UniProtKB:Q12341"
FT BINDING 234..236
FT /ligand="acetyl-CoA"
FT /ligand_id="ChEBI:CHEBI:57288"
FT /evidence="ECO:0000250|UniProtKB:Q12341"
FT BINDING 241..247
FT /ligand="acetyl-CoA"
FT /ligand_id="ChEBI:CHEBI:57288"
FT /evidence="ECO:0000250|UniProtKB:Q12341"
FT SITE 182
FT /note="Interaction with histone H4 N-terminus"
FT /evidence="ECO:0000250|UniProtKB:O14929"
SQ SEQUENCE 413 AA; 48355 MW; 94B7ACA991EA8747 CRC64;
MSSAKEQSSV TAALQPEQWT TSSNEALKLF VTNPEAALNF QPTFTYPIFG DAETIYGYKD
LDIFLCFDHY TFKPFLNIKY SAKLTDDPEI IDIKKTIDEF LPKSTIFKDE VKWVDSIKEE
KDNGYKIPGK LIDSFSENDK EYDIYKIDLK SDNGYELHQR LQILVLLFIE AGSFIDAKDE
LWNLYVLYEK DNKSTSNNEP SIVGFTTAYN YWKYPGAKKF DSTEQESRIK ISQFIILPIY
QGQGLGQLFY SHLFDKWLAQ DDIIEVVVED PNESFDDLRD RADLKRLNTS EQFDFKAVTP
KVDKEWVEKT RRALKLEKRQ FARLLEIILL YKLKHGYPGI TKRDVRLFIK KRLYDKNKEG
LATLDDNTKK DKLQTAYQAL EDDYYRILGD LKLNIKREND EEETDTVSKK QKV
