Skip Header

You are using a version of Internet Explorer that may not display all features of this website. Please upgrade to a modern browser.
Contribute Send feedback
Read comments (?) or add your own

Q750F5 (HAT1_ASHGO) Reviewed, UniProtKB/Swiss-Prot

Last modified December 11, 2013. Version 69. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Histone acetyltransferase type B catalytic subunit

EC=2.3.1.48
Gene names
Name:HAT1
Ordered Locus Names:AGL001W
OrganismAshbya gossypii (strain ATCC 10895 / CBS 109.51 / FGSC 9923 / NRRL Y-1056) (Yeast) (Eremothecium gossypii) [Reference proteome]
Taxonomic identifier284811 [NCBI]
Taxonomic lineageEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeEremothecium

Protein attributes

Sequence length391 AA.
Sequence statusComplete.
Protein existenceInferred 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 processDNA damage
DNA repair
   Cellular componentCytoplasm
Nucleus
   Molecular functionAcyltransferase
Chromatin regulator
Transferase
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processDNA repair

Inferred from electronic annotation. Source: UniProtKB-KW

chromatin silencing at telomere

Inferred from electronic annotation. Source: InterPro

   Cellular_componentcytoplasm

Inferred from electronic annotation. Source: UniProtKB-SubCell

histone acetyltransferase complex

Inferred from electronic annotation. Source: InterPro

   Molecular_functionhistone acetyltransferase activity

Inferred from electronic annotation. Source: UniProtKB-EC

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 391391Histone acetyltransferase type B catalytic subunit
PRO_0000227716

Sequences

Sequence LengthMass (Da)Tools
Q750F5 [UniParc].

Last modified January 9, 2013. Version 2.
Checksum: FC2A69642885E61D

FASTA39145,208
        10         20         30         40         50         60 
MAEELKPELW TTSSNSALKL SLVNDENAVQ FSPIFTYPIF GQAEQLFGYQ DLNILLAFDS 

        70         80         90        100        110        120 
VTFKPFLNIK YTKKLERGLD DVEGSILKFL PEGDVILKDE VEWVDAFNGE REKFALPNSE 

       130        140        150        160        170        180 
SKVAEYTSGG ESFAIFKVHL SDPNIRQLHR RMQIFTLLFI EAASYIDEDD SAWDIFMTFN 

       190        200        210        220        230        240 
TSTRQCIGYT TTYKHWRYIN GQEFDSSEKT TKRAKISQFI IFPPYQSKSH GSHLYSAAID 

       250        260        270        280        290        300 
VWSKEEKISE VTVEDPNEAF DDLRDRCDFM RLSGSGLSSS IPEDVPIPRT WLTEQARKYK 

       310        320        330        340        350        360 
LSLVQFTRLV EMILLYDNSP NFEIQVKARL YQKNHEVLTG MDSDTRKAKL QEAFTSLKED 

       370        380        390 
YARILQKVPN RRRVLPSDEE NAGESKRHKK E 

« Hide

References

« Hide 'large scale' references
[1]"The Ashbya gossypii genome as a tool for mapping the ancient Saccharomyces cerevisiae genome."
Dietrich F.S., Voegeli S., Brachat S., Lerch A., Gates K., Steiner S., Mohr C., Poehlmann R., Luedi P., Choi S., Wing R.A., Flavier A., Gaffney T.D., Philippsen P.
Science 304:304-307(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 10895 / CBS 109.51 / FGSC 9923 / NRRL Y-1056.
[2]"Genomes of Ashbya fungi isolated from insects reveal four mating-type loci, numerous translocations, lack of transposons, and distinct gene duplications."
Dietrich F.S., Voegeli S., Kuo S., Philippsen P.
G3 (Bethesda) 3:1225-1239(2013) [PubMed] [Europe PMC] [Abstract]
Cited for: GENOME REANNOTATION, SEQUENCE REVISION TO 312.
Strain: ATCC 10895 / CBS 109.51 / FGSC 9923 / NRRL Y-1056.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AE016820 Genomic DNA. Translation: AAS54489.2.
RefSeqNP_986665.2. NM_211727.2.

3D structure databases

ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING33169.AGOS_AGL001W.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID4622964.
KEGGago:AGOS_AGL001W.

Phylogenomic databases

eggNOGNOG326277.
HOGENOMHOG000074728.
KOK11303.
OrthoDBEOG7HTHSD.

Family and domain databases

Gene3D1.10.10.390. 1 hit.
3.40.630.30. 1 hit.
3.90.360.10. 1 hit.
InterProIPR016181. Acyl_CoA_acyltransferase.
IPR019467. Hat1_N.
IPR017380. Hist_AcTrfase_B-typ_cat-su.
IPR013523. Hist_AcTrfase_HAT1_C.
[Graphical view]
PANTHERPTHR12046. PTHR12046. 1 hit.
PfamPF10394. Hat1_N. 1 hit.
[Graphical view]
PIRSFPIRSF038084. HAT-B_cat. 1 hit.
SUPFAMSSF55729. SSF55729. 1 hit.
ProtoNetSearch...

Entry information

Entry nameHAT1_ASHGO
AccessionPrimary (citable) accession number: Q750F5
Entry history
Integrated into UniProtKB/Swiss-Prot: March 21, 2006
Last sequence update: January 9, 2013
Last modified: December 11, 2013
This is version 69 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families