Reviewed, UniProtKB/Swiss-Prot Q4PBE6 (HAT1_USTMA)

Names and origin

Protein names

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

Gene names

Name:	HAT1
ORF Names:	UM02567

Organism

Ustilago maydis (Smut fungus) [Complete proteome]

Taxonomic identifier

5270 [NCBI]

Taxonomic lineage

Eukaryota › Fungi › Dikarya › Basidiomycota › Ustilaginomycotina › Ustilaginomycetes › Ustilaginales › Ustilaginaceae › Ustilago

Protein attributes

Sequence length	448 AA.
Sequence status	Complete.
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 + 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 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 – 448	448	Histone acetyltransferase type B catalytic subunit		PRO_0000227727

Sequences

	Sequence		Length	Mass (Da)
	Q4PBE6-1 [UniParc]. Last modified July 19, 2005. Version 1. Checksum: 4BBAE5DC8D52776A	FASTA	448	51,083
	10 20 30 40 50 60 MKDSWSSNST TSTAIRLVGS PYGTDSPFQP TFTYPIYGEA ETIYGYEGLA IKLSVASGSL 70 80 90 100 110 120 VPLLEVTYRA KNEATTAEID DVEGKIKEFL APDFLSTSSP SAMEEFETVV KADKEFRPLG 130 140 150 160 170 180 DKVHSYTRGK VDKGKAKSST ASLASSTLSA SDPNARVFEI YRSTWHTPGF REYHRRMQLF 190 200 210 220 230 240 TLLFIEGASY IQEDETNWEF FTLYEKVSRD DKQTWHFMGY TSLYKFWCWP DSSRIRLSQF 250 260 270 280 290 300 VILPPFQKQG HGGALYTTVY DQIRERANVT ELTVEDPSED FDRLRDGNDL RRLLAPGGFA 310 320 330 340 350 360 DSAKAQNKLH APLDKEWIES QRLQHKLAPR QWSRVLEMVQ LMNLDTTDHE QVKQYRLQVK 370 380 390 400 410 420 ARIYRQNKDI LMQLEKQQQR SKLQETFEGV VEEYGDMVGV DVEDLLDDGP SGTGALYGAD 430 440 EEEDQEQGQG DRHYSNGNGP PRKMARLA

References

[1]

"Insights from the genome of the biotrophic fungal plant pathogen Ustilago maydis." Kaemper J., Kahmann R., Boelker M., Ma L.-J., Brefort T., Saville B.J., Banuett F., Kronstad J.W., Gold S.E., Mueller O., Perlin M.H., Woesten H.A.B., de Vries R., Ruiz-Herrera J., Reynaga-Pena C.G., Snetselaar K., McCann M., Perez-Martin J. , Feldbruegge M., Basse C.W., Steinberg G., Ibeas J.I., Holloman W., Guzman P., Farman M.L., Stajich J.E., Sentandreu R., Gonzalez-Prieto J.M., Kennell J.C., Molina L., Schirawski J., Mendoza-Mendoza A., Greilinger D., Muench K., Roessel N., Scherer M., Vranes M., Ladendorf O., Vincon V., Fuchs U., Sandrock B., Meng S., Ho E.C.H., Cahill M.J., Boyce K.J., Klose J., Klosterman S.J., Deelstra H.J., Ortiz-Castellanos L., Li W., Sanchez-Alonso P., Schreier P.H., Haeuser-Hahn I., Vaupel M., Koopmann E., Friedrich G., Voss H., Schlueter T., Margolis J., Platt D., Swimmer C., Gnirke A., Chen F., Vysotskaia V., Mannhaupt G., Gueldener U., Muensterkoetter M., Haase D., Oesterheld M., Mewes H.-W., Mauceli E.W., DeCaprio D., Wade C.M., Butler J., Young S.K., Jaffe D.B., Calvo S.E., Nusbaum C., Galagan J.E., Birren B.W. Nature 444:97-101(2006) [PubMed: 17080091] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: 521 / FGSC 9021.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AACP01000086 Genomic DNA. Translation: EAK83737.1.
RefSeq	XP_758714.1.
3D structure databases
SMR	Q4PBE6. Positions 3-343.
ModBase	Search...
Protein-protein interaction databases
STRING	Q4PBE6.
Genome annotation databases
GeneID	3630647.
KEGG	uma:UM02567.1.
Phylogenomic databases
eggNOG	fuNOG05412.
HOGENOM	HBG738699.
OMA	VEANECM.
OrthoDB	EOG9CG1RQ.
PhylomeDB	Q4PBE6.
Enzyme and pathway databases
BRENDA	2.3.1.48. 2320.
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_USTMA

Accession

Primary (citable) accession number: Q4PBE6

Entry history

Integrated into UniProtKB/Swiss-Prot:	March 21, 2006
Last sequence update:	July 19, 2005
Last modified:	February 9, 2010
This is version 30 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

FPAP (Fungal Proteome Annotation Project)