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Q4X0W8 (HAT1_ASPFU) Reviewed, UniProtKB/Swiss-Prot

Last modified November 13, 2013. Version 56. 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
ORF Names:AFUA_2G12030
OrganismNeosartorya fumigata (strain ATCC MYA-4609 / Af293 / CBS 101355 / FGSC A1100) (Aspergillus fumigatus) [Reference proteome]
Taxonomic identifier330879 [NCBI]
Taxonomic lineageEukaryotaFungiDikaryaAscomycotaPezizomycotinaEurotiomycetesEurotiomycetidaeEurotialesAspergillaceaeAspergillus

Protein attributes

Sequence length570 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: UniProtKB-EC

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 570570Histone acetyltransferase type B catalytic subunit
PRO_0000227717

Sequences

Sequence LengthMass (Da)Tools
Q4X0W8 [UniParc].

Last modified July 5, 2005. Version 1.
Checksum: 1DDCBEFADABA788F

FASTA57065,962
        10         20         30         40         50         60 
MALILERLYL LSSPRNAIIR NTRSEAGREL IFSFGLPSLS LPSCIASQYG KRRRLYFTTQ 

        70         80         90        100        110        120 
LHVNSFLHWT CDANDAVNIT LVQPDEQKLK TVSSFHPQFT YPIFGDDERI FGYKGLIIRL 

       130        140        150        160        170        180 
RFAAHDLRPQ LHISYDEKFK PVEDIAAVDI PKTLKPWIPE DAFVTLPDYE KAVLEDKAAK 

       190        200        210        220        230        240 
DFKPPGKLVH CYVSRNRNFE IWAGSLADPE VRRLLDRAQI FVSLFIEAGT PLATDDPEWT 

       250        260        270        280        290        300 
LQRWTVYFVY EIVKPPTPTA SKYSIVGYAT TYRWWHYRRD RTQVPVVKND PFPSGPEIHP 

       310        320        330        340        350        360 
SQLPSRLRIA QFLILPPHQN SGHGRHLYTA IHSACVQDPS VVELTVEDPN EAFDVLRDSA 

       370        380        390        400        410        420 
DYHILRPEFI KHEVNINPDP YEAHSRNQRP RRVPTAALIP VKLLHDIRTS YKIDSTQFAH 

       430        440        450        460        470        480 
ILEMFLLSQI PLKNRHAGGA NMSRLLIKKH RAEDPNERRY YWWRMLTKQR LYKRSKDILI 

       490        500        510        520        530        540 
QLDLDERIQK LEETVSNVEE GYEVLLKEFS EREEKLKARG VVESPAATVS DDASAGPSGT 

       550        560        570 
SRDQRVKRKF TVEDDEDKVE EEDTAKRTKV 

« Hide

References

[1]"Genomic sequence of the pathogenic and allergenic filamentous fungus Aspergillus fumigatus."
Nierman W.C., Pain A., Anderson M.J., Wortman J.R., Kim H.S., Arroyo J., Berriman M., Abe K., Archer D.B., Bermejo C., Bennett J.W., Bowyer P., Chen D., Collins M., Coulsen R., Davies R., Dyer P.S., Farman M.L. expand/collapse author list , Fedorova N., Fedorova N.D., Feldblyum T.V., Fischer R., Fosker N., Fraser A., Garcia J.L., Garcia M.J., Goble A., Goldman G.H., Gomi K., Griffith-Jones S., Gwilliam R., Haas B.J., Haas H., Harris D.E., Horiuchi H., Huang J., Humphray S., Jimenez J., Keller N., Khouri H., Kitamoto K., Kobayashi T., Konzack S., Kulkarni R., Kumagai T., Lafton A., Latge J.-P., Li W., Lord A., Lu C., Majoros W.H., May G.S., Miller B.L., Mohamoud Y., Molina M., Monod M., Mouyna I., Mulligan S., Murphy L.D., O'Neil S., Paulsen I., Penalva M.A., Pertea M., Price C., Pritchard B.L., Quail M.A., Rabbinowitsch E., Rawlins N., Rajandream M.A., Reichard U., Renauld H., Robson G.D., Rodriguez de Cordoba S., Rodriguez-Pena J.M., Ronning C.M., Rutter S., Salzberg S.L., Sanchez M., Sanchez-Ferrero J.C., Saunders D., Seeger K., Squares R., Squares S., Takeuchi M., Tekaia F., Turner G., Vazquez de Aldana C.R., Weidman J., White O., Woodward J.R., Yu J.-H., Fraser C.M., Galagan J.E., Asai K., Machida M., Hall N., Barrell B.G., Denning D.W.
Nature 438:1151-1156(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC MYA-4609 / Af293 / CBS 101355 / FGSC A1100.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AAHF01000001 Genomic DNA. Translation: EAL93497.1.
RefSeqXP_755535.1. XM_750442.1.

3D structure databases

ProteinModelPortalQ4X0W8.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING5085.CADAFUAP00004796.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblFungiCADAFUAT00004796; CADAFUAP00004796; CADAFUAG00004796.
GeneID3513677.
KEGGafm:AFUA_2G12030.

Phylogenomic databases

eggNOGNOG326277.
HOGENOMHOG000164382.
KOK11303.
OMAHISYDEK.
OrthoDBEOG7HTHSD.

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. SSF55729. 1 hit.
ProtoNetSearch...

Entry information

Entry nameHAT1_ASPFU
AccessionPrimary (citable) accession number: Q4X0W8
Entry history
Integrated into UniProtKB/Swiss-Prot: March 21, 2006
Last sequence update: July 5, 2005
Last modified: November 13, 2013
This is version 56 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