Reviewed, UniProtKB/Swiss-Prot Q6CC99 (HAT1_YARLI)

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:	YALI0C11231g

Organism

Yarrowia lipolytica (Candida lipolytica) [Complete proteome]

Taxonomic identifier

4952 [NCBI]

Taxonomic lineage

Eukaryota › Fungi › Dikarya › Ascomycota › Saccharomycotina › Saccharomycetes › Saccharomycetales › Dipodascaceae › Yarrowia

Protein attributes

Sequence length	451 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 – 451	451	Histone acetyltransferase type B catalytic subunit		PRO_0000227728

Sequences

	Sequence		Length	Mass (Da)
	Q6CC99-1 [UniParc]. Last modified August 16, 2004. Version 1. Checksum: 6D491A9BF98D7133	FASTA	451	52,089
	10 20 30 40 50 60 MDIATEWTTN ANEALTITLE PSKGKGKGKE VSNGSEKSHV FNPIFTYPIY GDVETILGYK 70 80 90 100 110 120 NFELNLKMDA STMLPLVTVK FSDKLEFDGI SFDDPVERLL EFLPEETATD EAEWEEKRVK 130 140 150 160 170 180 ELGDGFKPVG KEFGTFSVNS EKYTVHRSTL LDPETLKLHL RLQIFVPLFI EAGSYIDNED 190 200 210 220 230 240 DRWEIYIVYN AEKEIVGFST VYCYWFYEPS AKESKAPKDA SLEQLQKQPF SPTLRKRISQ 250 260 270 280 290 300 YVILPPFQGK GLGGQLYTLL FSRFYADPNV YEITVEDPSE AFDDLRDRCD LKWLADQGFP 310 320 330 340 350 360 SEVFRMLQTT SAHGEKAGDN RTGRTKVVAG AFWTKWLEEH RLKYKLAHRQ FARCFEMILL 370 380 390 400 410 420 ACLEVSSPTK KRNIKDARLF IKKRVYVRNR EFLEELGGKI EVMSKLQETY ESMEEDYARI 430 440 450 MKPVLGYVKD GLKKRDRNDA GNEEAKRVKV E

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: CLIB 122 / E 150.

Cross-references

Sequence databases
EMBL GenBank DDBJ	CR382129 Genomic DNA. Translation: CAG82023.1.
RefSeq	XP_501713.1.
3D structure databases
SMR	Q6CC99. Positions 5-361.
ModBase	Search...
Protein-protein interaction databases
STRING	Q6CC99.
Genome annotation databases
GeneID	2909147.
GenomeReviews	Gene locus YALI0C11231g in contig CR382129_GR.
KEGG	yli:YALI0C11231g.
Phylogenomic databases
eggNOG	fuNOG05412.
HOGENOM	HBG738699.
OMA	VEANECM.
OrthoDB	EOG9CG1RQ.
PhylomeDB	Q6CC99.
Enzyme and pathway databases
BRENDA	2.3.1.48. 3602.
Family and domain databases
InterPro	IPR016181. Acyl_CoA_acyltransferase. IPR019467. Hat1_N. IPR017380. Hist_AcTrfase_B-typ_cat-su. [Graphical view]
Gene3D	G3DSA:3.40.630.30. Acyl_CoA_acyltransferase. 1 hit.
Pfam	PF10394. Hat1_N. 1 hit. [Graphical view]
PIRSF	PIRSF038084. HAT-B_cat. 1 hit.
ProtoNet	Search...

Entry information

Entry name

HAT1_YARLI

Accession

Primary (citable) accession number: Q6CC99

Entry history

Integrated into UniProtKB/Swiss-Prot:	March 21, 2006
Last sequence update:	August 16, 2004
Last modified:	February 9, 2010
This is version 37 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

FPAP (Fungal Proteome Annotation Project)