Reviewed, UniProtKB/Swiss-Prot Q6BSQ1 (HAT1_DEBHA)

Names and origin

Protein names

Recommended name:
    Histone acetyltransferase type B catalytic subunit
    EC=2.3.1.48

Gene names

Name:	HAT1
Ordered Locus Names:	DEHA2D07062g

Organism

Debaryomyces hansenii (Yeast) (Torulaspora hansenii) [Complete proteome]

Taxonomic identifier

4959 [NCBI]

Taxonomic lineage

Eukaryota › Fungi › Dikarya › Ascomycota › Saccharomycotina › Saccharomycetes › Saccharomycetales › Saccharomycetaceae › Debaryomyces

Protein attributes

Sequence length	409 AA.
Sequence status	Complete.
Protein existence	Inferred from homology.

General annotation (Comments)

Function	Catalytic component of the histone acetylase B (HAT-B) complex. Acetylates 'Lys-12' of histone H4 which is required for telomeric silencing. Has intrinsic substrate specificity that modifies lysine in recognition sequence GXGKXG. Involved in DNA double-strand break repair By similarity.
Catalytic activity	Acetyl-CoA + [histone] = CoA + acetyl-[histone].
Subunit structure	Component of the HAT-B complex composed of at least HAT1 and HAT2. The HAT-B complex binds to histone H4 tail By similarity.
Subcellular location	Cytoplasm By similarity. Nucleus By similarity.
Sequence similarities	Belongs to the HAT1 family.

Ontologies

Keywords
Biological process	DNA damage DNA repair
Cellular component	Cytoplasm Nucleus
Molecular function	Acyltransferase Chromatin regulator Transferase
Technical term	Complete proteome
Gene Ontology (GO)
Biological process	DNA repair Inferred from electronic annotation. Source: UniProtKB-KW chromatin silencing at telomere Inferred from electronic annotation. Source: InterPro histone acetylation Inferred from electronic annotation. Source: InterPro
Cellular component	cytoplasm Inferred from electronic annotation. Source: UniProtKB-SubCell nucleus Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular function	histone acetyltransferase activity Inferred from electronic annotation. Source: EC protein binding Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 409	409	Histone acetyltransferase type B catalytic subunit		PRO_0000227723

Sequences

	Sequence		Length	Mass (Da)
	Q6BSQ1-1 [UniParc]. Last modified December 16, 2008. Version 2. Checksum: 2A9794B7363E08C2	FASTA	409	47,711
	10 20 30 40 50 60 MSDNSPITSI TAASLQPELW TSSSNDALQI YITDSDGTAL NFHPNFTYPI FGDSEQIFGY 70 80 90 100 110 120 RDLVIFLCFD HCTFYPFLNV KYSDKLNDDT LEDPREKLLS YLPESTIFKD EVKWVDSINK 130 140 150 160 170 180 EKEGFEIPGE LVGNIFTHGD DKFGIYKLDL KNAQGLELHK RLQILVLLFI EAGSYIDHQD 190 200 210 220 230 240 ELWDIYVMYK VTDEKTPSII GFCTAYNYWK YGGFEKFDSN QQEVRKKISQ FIVLPMYQGL 250 260 270 280 290 300 KLGGRFYNKL YEYWMQDPRV IEVVVEDPSE SFDDLRDRCD LTRLCQNTIK VASVDLPLIN 310 320 330 340 350 360 TEWATKLRQE QKLEKRQFSR LLEMILIYQL EHNLTNITKK QVRLFIKKRL YEKNKEILDG 370 380 390 400 LDEPTRLDKL QTAYASLESD YKRILSGLSL HKRALDSTEG SSKKSKPNV

References

[1]

"Genome evolution in yeasts." Dujon B., Sherman D., Fischer G., Durrens P., Casaregola S., Lafontaine I., de Montigny J., Marck C., Neuveglise C., Talla E., Goffard N., Frangeul L., Aigle M., Anthouard V., Babour A., Barbe V., Barnay S., Blanchin S. , Beckerich J.-M., Beyne E., Bleykasten C., Boisrame A., Boyer J., Cattolico L., Confanioleri F., de Daruvar A., Despons L., Fabre E., Fairhead C., Ferry-Dumazet H., Groppi A., Hantraye F., Hennequin C., Jauniaux N., Joyet P., Kachouri R., Kerrest A., Koszul R., Lemaire M., Lesur I., Ma L., Muller H., Nicaud J.-M., Nikolski M., Oztas S., Ozier-Kalogeropoulos O., Pellenz S., Potier S., Richard G.-F., Straub M.-L., Suleau A., Swennen D., Tekaia F., Wesolowski-Louvel M., Westhof E., Wirth B., Zeniou-Meyer M., Zivanovic Y., Bolotin-Fukuhara M., Thierry A., Bouchier C., Caudron B., Scarpelli C., Gaillardin C., Weissenbach J., Wincker P., Souciet J.-L. Nature 430:35-44(2004) [PubMed: 15229592] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 36239 / CBS 767 / IFO 0083 / IGC 2968 / JCM 1990.

Cross-references

Sequence databases
EMBL GenBank DDBJ	CR382136 Genomic DNA. Translation: CAG86913.2.
RefSeq	XP_458769.1.
3D structure databases
ModBase	Search...
Protein-protein interaction databases
STRING	Q6BSQ1.
Genome annotation databases
GeneID	2901027.
GenomeReviews	Gene locus DEHA2D07062g in contig CR382136_GR.
KEGG	dha:DEHA0D07799g.
Phylogenomic databases
eggNOG	fuNOG05412.
HOGENOM	HBG738699.
OMA	FMESFLR.
OrthoDB	EOG9CG1RQ.
Enzyme and pathway databases
BRENDA	2.3.1.48. 74267.
Family and domain databases
InterPro	IPR016181. Acyl_CoA_acyltransferase. IPR019467. Hat1_N. IPR017380. Hist_AcTrfase_B-typ_cat-su. [Graphical view]
Pfam	PF10394. Hat1_N. 1 hit. [Graphical view]
PIRSF	PIRSF038084. HAT-B_cat. 1 hit.
ProtoNet	Search...

Entry information

Entry name

HAT1_DEBHA

Accession

Primary (citable) accession number: Q6BSQ1

Entry history

Integrated into UniProtKB/Swiss-Prot:	March 21, 2006
Last sequence update:	December 16, 2008
Last modified:	February 9, 2010
This is version 37 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

FPAP (Fungal Proteome Annotation Project)