HAT1_CRYNJ
ID HAT1_CRYNJ Reviewed; 416 AA.
AC P0CO06; Q55ZG3; Q5KNS9;
DT 28-JUN-2011, integrated into UniProtKB/Swiss-Prot.
DT 28-JUN-2011, sequence version 1.
DT 03-AUG-2022, entry version 50.
DE RecName: Full=Histone acetyltransferase type B catalytic subunit;
DE EC=2.3.1.48 {ECO:0000250|UniProtKB:Q12341};
GN Name=HAT1; OrderedLocusNames=CNA05430;
OS Cryptococcus neoformans var. neoformans serotype D (strain JEC21 / ATCC
OS MYA-565) (Filobasidiella neoformans).
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Tremellomycetes;
OC Tremellales; Cryptococcaceae; Cryptococcus;
OC Cryptococcus neoformans species complex.
OX NCBI_TaxID=214684;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JEC21 / ATCC MYA-565;
RX PubMed=15653466; DOI=10.1126/science.1103773;
RA Loftus B.J., Fung E., Roncaglia P., Rowley D., Amedeo P., Bruno D.,
RA Vamathevan J., Miranda M., Anderson I.J., Fraser J.A., Allen J.E.,
RA Bosdet I.E., Brent M.R., Chiu R., Doering T.L., Donlin M.J., D'Souza C.A.,
RA Fox D.S., Grinberg V., Fu J., Fukushima M., Haas B.J., Huang J.C.,
RA Janbon G., Jones S.J.M., Koo H.L., Krzywinski M.I., Kwon-Chung K.J.,
RA Lengeler K.B., Maiti R., Marra M.A., Marra R.E., Mathewson C.A.,
RA Mitchell T.G., Pertea M., Riggs F.R., Salzberg S.L., Schein J.E.,
RA Shvartsbeyn A., Shin H., Shumway M., Specht C.A., Suh B.B., Tenney A.,
RA Utterback T.R., Wickes B.L., Wortman J.R., Wye N.H., Kronstad J.W.,
RA Lodge J.K., Heitman J., Davis R.W., Fraser C.M., Hyman R.W.;
RT "The genome of the basidiomycetous yeast and human pathogen Cryptococcus
RT neoformans.";
RL Science 307:1321-1324(2005).
CC -!- FUNCTION: Catalytic component of the histone acetylase B (HAT-B)
CC complex. Acetylates 'Lys-12' 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 (By similarity). {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|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; AE017341; AAW41043.1; -; Genomic_DNA.
DR RefSeq; XP_566862.1; XM_566862.1.
DR AlphaFoldDB; P0CO06; -.
DR SMR; P0CO06; -.
DR STRING; 5207.AAW41043; -.
DR PaxDb; P0CO06; -.
DR EnsemblFungi; AAW41043; AAW41043; CNA05430.
DR GeneID; 3253290; -.
DR KEGG; cne:CNA05430; -.
DR VEuPathDB; FungiDB:CNA05430; -.
DR eggNOG; KOG2696; Eukaryota.
DR HOGENOM; CLU_036024_2_1_1; -.
DR InParanoid; P0CO06; -.
DR OMA; YFINLDE; -.
DR OrthoDB; 708105at2759; -.
DR Proteomes; UP000002149; Chromosome 1.
DR GO; GO:0000781; C:chromosome, telomeric region; IEA:GOC.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0010485; F:H4 histone acetyltransferase activity; IBA:GO_Central.
DR GO; GO:0042393; F:histone binding; IEA:InterPro.
DR GO; GO:0006281; P:DNA repair; IEA:UniProtKB-KW.
DR GO; GO:0043967; P:histone H4 acetylation; IBA:GO_Central.
DR GO; GO:0031509; P:subtelomeric heterochromatin assembly; IEA:InterPro.
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..416
FT /note="Histone acetyltransferase type B catalytic subunit"
FT /id="PRO_0000227721"
FT REGION 52..54
FT /note="Interaction with histone H4 N-terminus"
FT /evidence="ECO:0000250|UniProtKB:Q12341"
FT REGION 235..237
FT /note="Interaction with histone H4 N-terminus"
FT /evidence="ECO:0000250|UniProtKB:Q12341"
FT ACT_SITE 286
FT /note="Proton donor/acceptor"
FT /evidence="ECO:0000250|UniProtKB:Q12341"
FT BINDING 251..253
FT /ligand="acetyl-CoA"
FT /ligand_id="ChEBI:CHEBI:57288"
FT /evidence="ECO:0000250|UniProtKB:Q12341"
FT BINDING 258..264
FT /ligand="acetyl-CoA"
FT /ligand_id="ChEBI:CHEBI:57288"
FT /evidence="ECO:0000250|UniProtKB:Q12341"
FT SITE 207
FT /note="Interaction with histone H4 N-terminus"
FT /evidence="ECO:0000250|UniProtKB:O14929"
SQ SEQUENCE 416 AA; 48537 MW; E039F0594EE21C60 CRC64;
MAETLEEWIS DSNQVLNLQM VRTPEDASLL QYEEQQNIDV FNPAFTYPIF GDNEKIFGYK
GLDIKLHFAS GSLRQYLDIS YDAKLASSTT PPDEIEGALY KFIPPDYTKS EVEFQKRVAG
DAETFKPLGE KIGSYAHPSA GRKGKGQGDS GMAAGKAIED NEDVVEYEMY KATWSTPGFR
EYHRRMQIFV LLFIEGGSYV HEDEDAWEFI VLYERRTRPD SGIFTYHFVG YVSVYPFWCY
PDRVRLRLSQ FVILPPYQHQ GHGSKLYNML FRHMLDRSEV AELTIEDPAE AFEDLRDRND
LRFLVKEGIV KDPMLYVDVG KGKRGSRVEW ELAIRRKYKI AQRQFDRLLE MLLFRQLDKG
NPDKVKAYRL HVKARLYRFN YEMLSQMTVE ERKEALAKTY ESVVEDYKRI LGMTFG
