Skip Header

Contribute Send feedback
Read comments (0) or add your own

Reviewed, UniProtKB/Swiss-Prot Q5AZR6 (HAT1_EMENI)

Last modified February 9, 2010. Version 29. 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
ORF Names: AN6214
OrganismEmericella nidulans (Aspergillus nidulans) [Complete proteome]
Taxonomic identifier162425 [NCBI]
Taxonomic lineageEukaryotaFungiDikaryaAscomycotaPezizomycotinaEurotiomycetesEurotiomycetidaeEurotialesTrichocomaceaeEmericella

Protein attributes

Sequence length496 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 – 496496Histone acetyltransferase type B catalytic subunit
PRO_0000227722

Sequences

Sequence LengthMass (Da)Tools
Q5AZR6-1 [UniParc].

Last modified April 26, 2005. Version 1.
Checksum: 92441200489692C4

FASTA49657,779
        10         20         30         40         50         60 
MSAEGEWSCD ANDAVQITIV HPDQQKPKTL SSFHPQFTYP IFGEEERIFG YKGLIIRLRF 

        70         80         90        100        110        120 
AAHNLRPHVH VSYDEKFTAV DDAEPVDIIG ALKEFLPEEA FSSLPEFESA VQEEDAKEFV 

       130        140        150        160        170        180 
PPGKLSHSYS IRGRNYEIWA ASLADPQVQL LLNRFQIMVS FYIEAGTPLS TDDPEWTLDR 

       190        200        210        220        230        240 
WTVYFVLTAA RYEKVEPPTP TASSYSIVGY ATTYRWWFYK RDRSENPMPR DGPFPPPELV 

       250        260        270        280        290        300 
RPGELPSRLR IAQFLILPPH QGTGHGVNLY NTIHKTCLDD PTIMELTVED PNESFDVLRD 

       310        320        330        340        350        360 
SADYHILRPE FLKHNIQINP DPWSDFSKKT KRVPTSSLLP LKTLNEIRTA YKIEPTQFAH 

       370        380        390        400        410        420 
IQEMFLLGQI PLKNRRKGGA NMARLLVKKY RDDDPNNRRY YWWRMLTKQR LYKRSRDVLI 

       430        440        450        460        470        480 
QLKMSERHKA LEDTVTNVED GYEQLFGFFN EREERLRAQQ EEAETSNNRD QRTKRKFTVE 

       490 
DEDDEDESAA AKRPKA 

« Hide

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AACD01000105 Genomic DNA. Translation: EAA58000.1.
RefSeqXP_663818.1.

3D structure databases

SMRQ5AZR6. Positions 5-369.
ModBaseSearch...

Genome annotation databases

GeneID2870802.
KEGGani:AN6214.2.

Phylogenomic databases

PhylomeDBQ5AZR6.

Enzyme and pathway databases

BRENDA2.3.1.48. 3859.

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_EMENI
AccessionPrimary (citable) accession number: Q5AZR6
Entry history
Integrated into UniProtKB/Swiss-Prot: March 21, 2006
Last sequence update: April 26, 2005
Last modified: February 9, 2010
This is version 29 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