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Q5AZR6 (HAT1_EMENI) Reviewed, UniProtKB/Swiss-Prot

Last modified April 3, 2013. Version 49. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | Third-party data text xml rdf/xml gff fasta
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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 (strain FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139) (Aspergillus nidulans) [Reference proteome]
Taxonomic identifier227321 [NCBI]
Taxonomic lineageEukaryota › Fungi › Dikarya › Ascomycota › Pezizomycotina › Eurotiomycetes › Eurotiomycetidae › Eurotiales › Trichocomaceae › Emericella ›

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
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

nucleus

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular_functionhistone acetyltransferase activity

Inferred from electronic annotation. Source: EC

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 [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

References

« Hide 'large scale' references
[1]"Sequencing of Aspergillus nidulans and comparative analysis with A. fumigatus and A. oryzae."
Galagan J.E., Calvo S.E., Cuomo C., Ma L.-J., Wortman J.R., Batzoglou S., Lee S.-I., Bastuerkmen M., Spevak C.C., Clutterbuck J., Kapitonov V., Jurka J., Scazzocchio C., Farman M.L., Butler J., Purcell S., Harris S., Braus G.H. expand/collapse author list , Draht O., Busch S., D'Enfert C., Bouchier C., Goldman G.H., Bell-Pedersen D., Griffiths-Jones S., Doonan J.H., Yu J., Vienken K., Pain A., Freitag M., Selker E.U., Archer D.B., Penalva M.A., Oakley B.R., Momany M., Tanaka T., Kumagai T., Asai K., Machida M., Nierman W.C., Denning D.W., Caddick M.X., Hynes M., Paoletti M., Fischer R., Miller B.L., Dyer P.S., Sachs M.S., Osmani S.A., Birren B.W.
Nature 438:1105-1115(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139.
[2]"The 2008 update of the Aspergillus nidulans genome annotation: a community effort."
Wortman J.R., Gilsenan J.M., Joardar V., Deegan J., Clutterbuck J., Andersen M.R., Archer D., Bencina M., Braus G., Coutinho P., von Dohren H., Doonan J., Driessen A.J., Durek P., Espeso E., Fekete E., Flipphi M., Estrada C.G. expand/collapse author list , Geysens S., Goldman G., de Groot P.W., Hansen K., Harris S.D., Heinekamp T., Helmstaedt K., Henrissat B., Hofmann G., Homan T., Horio T., Horiuchi H., James S., Jones M., Karaffa L., Karanyi Z., Kato M., Keller N., Kelly D.E., Kiel J.A., Kim J.M., van der Klei I.J., Klis F.M., Kovalchuk A., Krasevec N., Kubicek C.P., Liu B., Maccabe A., Meyer V., Mirabito P., Miskei M., Mos M., Mullins J., Nelson D.R., Nielsen J., Oakley B.R., Osmani S.A., Pakula T., Paszewski A., Paulsen I., Pilsyk S., Pocsi I., Punt P.J., Ram A.F., Ren Q., Robellet X., Robson G., Seiboth B., van Solingen P., Specht T., Sun J., Taheri-Talesh N., Takeshita N., Ussery D., vanKuyk P.A., Visser H., van de Vondervoort P.J., de Vries R.P., Walton J., Xiang X., Xiong Y., Zeng A.P., Brandt B.W., Cornell M.J., van den Hondel C.A., Visser J., Oliver S.G., Turner G.
Fungal Genet. Biol. 46:S2-13(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: GENOME REANNOTATION.
Strain: FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		AACD01000105 Genomic DNA. Translation: EAA58000.1.
BN001301 Genomic DNA. Translation: CBF69944.1.
RefSeqXP_663818.1. XM_658726.1.

3D structure databases

ProteinModelPortalQ5AZR6.
ModBaseSearch...

Protein-protein interaction databases

STRING162425.CADANIAP00006788.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblFungiCADANIAT00006788; CADANIAP00006788; CADANIAG00006788.
GeneID2870802.
KEGGani:AN6214.2.

Phylogenomic databases

eggNOGNOG326277.
HOGENOMHOG000164382.
KOK11303.
OMAWEVLIYL.
OrthoDBEOG4WHCV7.

Family and domain databases

Gene3D3.40.630.30. 1 hit.
3.90.360.10. 1 hit.
InterProIPR016181. Acyl_CoA_acyltransferase.
IPR019467. Hat1_N.
IPR017380. Hist_AcTrfase_B-typ_cat-su.
[Graphical view]
PANTHERPTHR12046. PTHR12046. 1 hit.
PfamPF10394. Hat1_N. 1 hit.
[Graphical view]
PIRSFPIRSF038084. HAT-B_cat. 1 hit.
SUPFAMSSF55729. Acyl_CoA_acyltransferase. 1 hit.
ProtoNetSearch...

Entry information

Entry nameHAT1_EMENI
AccessionPrimary (citable) accession number: Q5AZR6
Secondary accession number(s): C8V1T7
Entry history
Integrated into UniProtKB/Swiss-Prot: March 21, 2006
Last sequence update: April 26, 2005
Last modified: April 3, 2013
This is version 49 of the entry and version 1 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

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