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Q4PBE6

- HAT1_USTMA

UniProt

Q4PBE6 - HAT1_USTMA

Protein

Histone acetyltransferase type B catalytic subunit

Gene

HAT1

Organism
Ustilago maydis (strain 521 / FGSC 9021) (Corn smut fungus)
Status
Reviewed - Annotation score: 2 out of 5- Protein inferred from homologyi
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    • History
      Entry version 54 (01 Oct 2014)
      Sequence version 1 (19 Jul 2005)
      Previous versions | rss
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    Functioni

    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.By similarity

    Catalytic activityi

    Acetyl-CoA + [histone] = CoA + acetyl-[histone].

    GO - Molecular functioni

    1. histone acetyltransferase activity Source: UniProtKB-EC

    GO - Biological processi

    1. chromatin silencing at telomere Source: InterPro
    2. DNA repair Source: UniProtKB-KW

    Keywords - Molecular functioni

    Acyltransferase, Chromatin regulator, Transferase

    Keywords - Biological processi

    DNA damage, DNA repair

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Histone acetyltransferase type B catalytic subunit (EC:2.3.1.48)
    Gene namesi
    Name:HAT1
    ORF Names:UM02567
    OrganismiUstilago maydis (strain 521 / FGSC 9021) (Corn smut fungus)
    Taxonomic identifieri237631 [NCBI]
    Taxonomic lineageiEukaryotaFungiDikaryaBasidiomycotaUstilaginomycotinaUstilaginomycetesUstilaginalesUstilaginaceaeUstilago
    ProteomesiUP000000561: Unassembled WGS sequence

    Subcellular locationi

    Cytoplasm By similarity. Nucleus By similarity

    GO - Cellular componenti

    1. cytoplasm Source: UniProtKB-SubCell
    2. histone acetyltransferase complex Source: InterPro

    Keywords - Cellular componenti

    Cytoplasm, Nucleus

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 448448Histone acetyltransferase type B catalytic subunitPRO_0000227727Add
    BLAST

    Interactioni

    Subunit structurei

    Component of the HAT-B complex composed of at least HAT1 and HAT2. The HAT-B complex binds to histone H4 tail By similarity.By similarity

    Protein-protein interaction databases

    STRINGi5270.UM02567.1.

    Structurei

    3D structure databases

    ProteinModelPortaliQ4PBE6.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the HAT1 family.Curated

    Phylogenomic databases

    eggNOGiNOG326277.
    HOGENOMiHOG000074728.
    KOiK11303.
    OMAiHISYDEK.
    OrthoDBiEOG7HTHSD.

    Family and domain databases

    Gene3Di1.10.10.390. 1 hit.
    3.40.630.30. 1 hit.
    3.90.360.10. 1 hit.
    InterProiIPR016181. Acyl_CoA_acyltransferase.
    IPR019467. Hat1_N.
    IPR017380. Hist_AcTrfase_B-typ_cat-su.
    IPR013523. Hist_AcTrfase_HAT1_C.
    [Graphical view]
    PANTHERiPTHR12046. PTHR12046. 1 hit.
    PfamiPF10394. Hat1_N. 1 hit.
    [Graphical view]
    PIRSFiPIRSF038084. HAT-B_cat. 1 hit.
    SUPFAMiSSF55729. SSF55729. 1 hit.

    Sequencei

    Sequence statusi: Complete.

    Q4PBE6-1 [UniParc]FASTAAdd to Basket

    « Hide

    MKDSWSSNST TSTAIRLVGS PYGTDSPFQP TFTYPIYGEA ETIYGYEGLA    50
    IKLSVASGSL VPLLEVTYRA KNEATTAEID DVEGKIKEFL APDFLSTSSP 100
    SAMEEFETVV KADKEFRPLG DKVHSYTRGK VDKGKAKSST ASLASSTLSA 150
    SDPNARVFEI YRSTWHTPGF REYHRRMQLF TLLFIEGASY IQEDETNWEF 200
    FTLYEKVSRD DKQTWHFMGY TSLYKFWCWP DSSRIRLSQF VILPPFQKQG 250
    HGGALYTTVY DQIRERANVT ELTVEDPSED FDRLRDGNDL RRLLAPGGFA 300
    DSAKAQNKLH APLDKEWIES QRLQHKLAPR QWSRVLEMVQ LMNLDTTDHE 350
    QVKQYRLQVK ARIYRQNKDI LMQLEKQQQR SKLQETFEGV VEEYGDMVGV 400
    DVEDLLDDGP SGTGALYGAD EEEDQEQGQG DRHYSNGNGP PRKMARLA 448
    Length:448
    Mass (Da):51,083
    Last modified:July 19, 2005 - v1
    Checksum:i4BBAE5DC8D52776A
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AACP01000086 Genomic DNA. Translation: EAK83737.1.
    RefSeqiXP_758714.1. XM_753621.1.

    Genome annotation databases

    EnsemblFungiiUM02567T0; UM02567P0; UM02567.
    GeneIDi3630647.
    KEGGiuma:UM02567.1.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AACP01000086 Genomic DNA. Translation: EAK83737.1 .
    RefSeqi XP_758714.1. XM_753621.1.

    3D structure databases

    ProteinModelPortali Q4PBE6.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    STRINGi 5270.UM02567.1.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblFungii UM02567T0 ; UM02567P0 ; UM02567 .
    GeneIDi 3630647.
    KEGGi uma:UM02567.1.

    Phylogenomic databases

    eggNOGi NOG326277.
    HOGENOMi HOG000074728.
    KOi K11303.
    OMAi HISYDEK.
    OrthoDBi EOG7HTHSD.

    Family and domain databases

    Gene3Di 1.10.10.390. 1 hit.
    3.40.630.30. 1 hit.
    3.90.360.10. 1 hit.
    InterProi IPR016181. Acyl_CoA_acyltransferase.
    IPR019467. Hat1_N.
    IPR017380. Hist_AcTrfase_B-typ_cat-su.
    IPR013523. Hist_AcTrfase_HAT1_C.
    [Graphical view ]
    PANTHERi PTHR12046. PTHR12046. 1 hit.
    Pfami PF10394. Hat1_N. 1 hit.
    [Graphical view ]
    PIRSFi PIRSF038084. HAT-B_cat. 1 hit.
    SUPFAMi SSF55729. SSF55729. 1 hit.
    ProtoNeti Search...

    Publicationsi

    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] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: 521 / FGSC 9021.

    Entry informationi

    Entry nameiHAT1_USTMA
    AccessioniPrimary (citable) accession number: Q4PBE6
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: March 21, 2006
    Last sequence update: July 19, 2005
    Last modified: October 1, 2014
    This is version 54 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programFungal Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    Complete proteome, Reference proteome

    Documents

    1. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3