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Reviewed, UniProtKB/Swiss-Prot Q750F5 (HAT1_ASHGO)

Last modified February 9, 2010. Version 43. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

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 (Yeast) (Eremothecium gossypii) [Complete proteome]
Taxonomic identifier33169 [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
Gene Ontology (GO)
   Biological processDNA 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 componentcytoplasm

Inferred from electronic annotation. Source: UniProtKB-SubCell

nucleus

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular functionhistone acetyltransferase activity

Inferred from electronic annotation. Source: EC

protein binding

Inferred from electronic annotation. Source: InterPro

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
Q750F5-1 [UniParc].

Last modified July 5, 2004. Version 1.
Checksum: E687AE0E8545E618

FASTA39145,190
        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 EIILLYDNSP NFEIQVKARL YQKNHEVLTG MDSDTRKAKL QEAFTSLKED 

       370        380        390 
YARILQKVPN RRRVLPSDEE NAGESKRHKK E 

« Hide

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: 15001715] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 10895 / CBS 109.51 / FGSC 9923 / NRRL Y-1056.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AE016820 Genomic DNA. Translation: AAS54489.1.
RefSeqNP_986665.1.

3D structure databases

SMRQ750F5. Positions 5-319.
ModBaseSearch...

Protein-protein interaction databases

STRINGQ750F5.

Genome annotation databases

GeneID4622964.
GenomeReviewsGene locus AGL001W in contig AE016820_GR.
KEGGago:AGOS_AGL001W.
NMPDRfig|33169.1.peg.4310.

Organism-specific databases

AGDAGL001W.

Phylogenomic databases

eggNOGfuNOG05412.
HOGENOMHBG738699.
OMAFESHISA.
OrthoDBEOG9CG1RQ.

Enzyme and pathway databases

BRENDA2.3.1.48. 279361.

Family and domain databases

InterProIPR016181. Acyl_CoA_acyltransferase.
IPR019467. Hat1_N.
IPR017380. Hist_AcTrfase_B-typ_cat-su.
[Graphical view]
Gene3DG3DSA:3.40.630.30. Acyl_CoA_acyltransferase. 1 hit.
PfamPF10394. Hat1_N. 1 hit.
[Graphical view]
PIRSFPIRSF038084. HAT-B_cat. 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: July 5, 2004
Last modified: February 9, 2010
This is version 43 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectFPAP (Fungal Proteome Annotation Project)

Relevant documents

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents