Reviewed, UniProtKB/Swiss-Prot Q4X0W8 (HAT1_ASPFU)

Names and origin

Protein names

Recommended name:
    Histone acetyltransferase type B catalytic subunit
    EC=2.3.1.48

Gene names

Name:	hat1
ORF Names:	AFUA_2G12030

Organism

Aspergillus fumigatus (Sartorya fumigata) [Complete proteome]

Taxonomic identifier

5085 [NCBI]

Taxonomic lineage

Eukaryota › Fungi › Dikarya › Ascomycota › Pezizomycotina › Eurotiomycetes › Eurotiomycetidae › Eurotiales › Trichocomaceae › mitosporic Trichocomaceae › Aspergillus

Protein attributes

Sequence length	570 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Inferred 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 + acetylhistone.
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 process	DNA damage DNA repair
Cellular component	Cytoplasm Nucleus
Molecular function	Acyltransferase Chromatin regulator Transferase
Technical term	Complete proteome
Gene Ontology (GO)
Biological process	DNA 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 component	cytoplasm Inferred from electronic annotation. Source: UniProtKB-SubCell nucleus Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular function	histone acetyltransferase activity Inferred from electronic annotation. Source: EC protein binding Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 570	570	Histone acetyltransferase type B catalytic subunit		PRO_0000227717

Sequences

	Sequence		Length	Mass (Da)
	Q4X0W8-1 [UniParc]. Last modified July 5, 2005. Version 1. Checksum: 1DDCBEFADABA788F	FASTA	570	65,962
	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

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. , 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: 16372009] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: Af293 / CBS 101355 / FGSC A1100.

Cross-references

Sequence databases
EMBLGenBankDDBJ	AAHF01000001 Genomic DNA. Translation: EAL93497.1.
RefSeq	XP_755535.1.
3D structure databases
ModBase	Search...
Genome annotation databases
GeneID	3513677.
GenomeReviews	Gene locus hat1 in contig CM000170_GR.
KEGG	afm:AFUA_2G12030.
Enzyme and pathway databases
BRENDA	2.3.1.48. 18841.
Family and domain databases
InterPro	IPR016181. Acyl_CoA_acyltransferase. IPR019467. Hat1_N. IPR017380. Hist_AcTrfase_B-typ_cat-su. [Graphical view]
Gene3D	G3DSA:3.40.630.30. Acyl_CoA_acyltransferase. 1 hit.
Pfam	PF10394. Hat1_N. 1 hit. [Graphical view]
PIRSF	PIRSF038084. HAT-B_cat. 1 hit.
ProtoNet	Search...

Entry information

Entry name

HAT1_ASPFU

Accession

Primary (citable) accession number: Q4X0W8

Entry history

Integrated into UniProtKB/Swiss-Prot:	March 21, 2006
Last sequence update:	July 5, 2005
Last modified:	September 22, 2009
This is version 28 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

FPAP (Fungal Proteome Annotation Project)