Histone acetyltransferase GCN5 - Candida glabrata (strain ATCC 2001 / CBS 138 / JCM 3761 / NBRC 0622 / NRRL Y-65) (Yeast)

Preferred order of sections

Names and origin

Protein names

Recommended name:
Histone acetyltransferase GCN5
EC=2.3.1.48

Gene names

Name:	GCN5
Ordered Locus Names:	CAGL0F08283g

Organism

Candida glabrata (strain ATCC 2001 / CBS 138 / JCM 3761 / NBRC 0622 / NRRL Y-65) (Yeast) (Torulopsis glabrata) [Complete proteome]

Taxonomic identifier

284593 [NCBI]

Taxonomic lineage

Eukaryota › Fungi › Dikarya › Ascomycota › Saccharomycotina › Saccharomycetes › Saccharomycetales › Saccharomycetaceae › Nakaseomyces › mitosporic Nakaseomyces

Protein attributes

Sequence length	546 AA.
Sequence status	Complete.
Protein existence	Inferred from homology

General annotation (Comments)

Function	Acetylates histone H2B to form H2BK11ac and H2BK16ac, histone H3 to form H3K14ac, with a lower preference histone H4 to form H4K8ac and H4K16ac, and contributes to H2A.Z acetylation. Acetylation of histones gives a specific tag for epigenetic transcription activation By similarity.
Catalytic activity	Acetyl-CoA + [histone] = CoA + acetyl-[histone].
Subcellular location	Nucleus By similarity.
Sequence similarities	Belongs to the GCN5 family. Contains 1 bromo domain. Contains 1 N-acetyltransferase domain.

Ontologies

Keywords
Biological process	Transcription Transcription regulation
Cellular component	Nucleus
Domain	Bromodomain
Molecular function	Activator Acyltransferase Chromatin regulator Transferase
Technical term	Complete proteome
Gene Ontology (GO)
Biological process	regulation of transcription, DNA-dependent Inferred from electronic annotation. Source: UniProtKB-KW transcription, DNA-dependent Inferred from electronic annotation. Source: UniProtKB-KW
Cellular component	nucleus Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular function	histone acetyltransferase activity Inferred from electronic annotation. Source: EC
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 546

546

Histone acetyltransferase GCN5

PRO_0000211196

Regions

Domain

207 – 362

156

N-acetyltransferase

Domain

451 – 521

71

Bromo

Compositional bias

37 – 208

172

Glu-rich

Compositional bias

45 – 115

71

Asp-rich

Sites

Site

280

1

Important for catalytic activity By similarity

Sequences

Sequence

Length

Mass (Da)

Tools

Q6FTW5 [UniParc].

Last modified July 19, 2004. Version 1.
Checksum: 977FDACF889D0189
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FASTA

546

63,512

        10         20         30         40         50         60 
MVTRRRLHHP EVEQVSKRQK VDKAESKNKK HADVAAERGE QSTEDHEDES QDKKDKKVVG 

        70         80         90        100        110        120 
DNRDEDEEVS PNGQEAAEDN DDRKDKDAKE KDTETNDEGT EKSHTDVNDD DDDVDESKEE 

       130        140        150        160        170        180 
DAAAAVDITK EKKDEQESDN KTEEKKVQEN EEEEEEDENK NDEDVEELGS TEPVDDEKKG 

       190        200        210        220        230        240 
LVKFEFDGVE YKFKERASVI EENEGKIEFR VVSNDNTREN MMVLTGLKNI FQKQLPKMPK 

       250        260        270        280        290        300 
EYIARLVYDR SHLSMAVIRK PLTVVGGITY KPFNKRQFAE IVFCAISSTE QVRGYGAHLM 

       310        320        330        340        350        360 
NHLKDYVRNT SDIRYFLTYA DNYAIGYFKK QGFTKDITLD KKVWMGYIKD YEGGTLMQCS 

       370        380        390        400        410        420 
MLPRIRYLDA AKILLLQEAA LRRKIRTISK SHVVHPGLEC FNDIENIKPI DPMSIPGLKE 

       430        440        450        460        470        480 
AGWTPEMDEL AQRPKRGPHY AAIQNILVEL QNHAAAWPFL RPVNKEEVPD YYEFIKEPMD 

       490        500        510        520        530        540 
LSTMELKLEN NKYEKMEEFI YDARLVCNNC RLYNGENTSY YKYANRLEKF FNNKVKEIPE 


YSHLID

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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.

Souciet J.-L.
Nature 430:35-44(2004) [PubMed: 15229592] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 2001 / CBS 138 / JCM 3761 / NBRC 0622 / NRRL Y-65.

Cross-references

Sequence databases
EMBL GenBank DDBJ	CR380952 Genomic DNA. Translation: CAG59253.1.
RefSeq	XP_446329.1. XM_446329.1.
3D structure databases
ProteinModelPortal	Q6FTW5.
SMR	Q6FTW5. Positions 206-369, 436-545.
ModBase	Search...
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
GeneID	2887572.
GenomeReviews	Gene locus CAGL0F08283g in contig CR380952_GR.
KEGG	cgr:CAGL0F08283g.
Phylogenomic databases
eggNOG	fuNOG05844.
HOGENOM	HBG749648.
OMA	LVYDRSH.
OrthoDB	EOG412QF2.
Family and domain databases
InterPro	IPR000182. AcTrfase_GCN5-related_dom. IPR016181. Acyl_CoA_acyltransferase. IPR001487. Bromodomain. IPR018359. Bromodomain_CS. [Graphical view]
Gene3D	G3DSA:3.40.630.30. Acyl_CoA_acyltransferase. 1 hit. G3DSA:1.20.920.10. Bromodomain. 1 hit.
KO	K06062.
Pfam	PF00583. Acetyltransf_1. 1 hit. PF00439. Bromodomain. 1 hit. [Graphical view]
PRINTS	PR00503. BROMODOMAIN.
SMART	SM00297. BROMO. 1 hit. [Graphical view]
SUPFAM	SSF55729. Acyl_CoA_acyltransferase. 1 hit. SSF47370. Bromodomain. 1 hit.
PROSITE	PS00633. BROMODOMAIN_1. 1 hit. PS50014. BROMODOMAIN_2. 1 hit. PS51186. GNAT. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

GCN5_CANGA

Accession

Primary (citable) accession number: Q6FTW5

Entry history

Integrated into UniProtKB/Swiss-Prot:	February 1, 2005
Last sequence update:	July 19, 2004
Last modified:	December 14, 2011
This is version 58 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Fungal Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families