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Q9UYB9

- BUD32_PYRAB

UniProt

Q9UYB9 - BUD32_PYRAB

Protein

KEOPS complex subunit Bud32

Gene

bud32

Organism
Pyrococcus abyssi (strain GE5 / Orsay)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 98 (01 Oct 2014)
      Sequence version 1 (01 May 2000)
      Previous versions | rss
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    Functioni

    Component of the KEOPS complex that is required for the formation of a threonylcarbamoyl group on adenosine at position 37 (t6A37) in tRNAs that read codons beginning with adenine. The complex is probably involved in the transfer of the threonylcarbamoyl moiety of threonylcarbamoyl-AMP (TC-AMP) to the N6 group of A37. Bud32 has ATPase activity in the context of the KEOPS complex and likely plays a supporting role to the catalytic subunit Kae1.2 Publications

    Catalytic activityi

    ATP + a protein = ADP + a phosphoprotein.1 Publication

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Binding sitei27 – 271ATPPROSITE-ProRule annotation
    Active sitei127 – 1271Proton acceptorPROSITE-ProRule annotation

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Nucleotide bindingi4 – 129ATPPROSITE-ProRule annotation

    GO - Molecular functioni

    1. ATPase activity Source: UniProtKB
    2. ATP binding Source: InterPro
    3. protein serine/threonine kinase activity Source: InterPro
    4. protein tyrosine kinase activity Source: InterPro

    GO - Biological processi

    1. ATP catabolic process Source: GOC
    2. threonylcarbamoyladenosine biosynthetic process Source: UniProtKB

    Keywords - Molecular functioni

    Hydrolase, Kinase, Serine/threonine-protein kinase, Transferase

    Keywords - Biological processi

    tRNA processing

    Keywords - Ligandi

    ATP-binding, Nucleotide-binding

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    KEOPS complex subunit Bud32 (EC:3.6.-.-)
    Alternative name(s):
    Atypical serine/threonine protein kinase Bud32 (EC:2.7.11.1)
    Gene namesi
    Name:bud32
    Ordered Locus Names:PAB1047, PYRAB15890
    OrganismiPyrococcus abyssi (strain GE5 / Orsay)
    Taxonomic identifieri272844 [NCBI]
    Taxonomic lineageiArchaeaEuryarchaeotaThermococciThermococcalesThermococcaceaePyrococcus
    ProteomesiUP000000810: Chromosome

    Subcellular locationi

    Cytoplasm By similarity

    GO - Cellular componenti

    1. EKC/KEOPS complex Source: UniProtKB

    Keywords - Cellular componenti

    Cytoplasm

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi127 – 1271D → R: Completely abolishes ATPase activity of the KEOPS complex and completely impairs the tRNA modification activity of the complex. 1 Publication

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 220220KEOPS complex subunit Bud32PRO_0000430322Add
    BLAST

    Interactioni

    Subunit structurei

    Component of the KEOPS complex that consists of Kae1, Bud32, Cgi121 and Pcc1; the whole complex dimerizes.2 Publications

    Protein-protein interaction databases

    STRINGi272844.PAB1047.

    Structurei

    3D structure databases

    ProteinModelPortaliQ9UYB9.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini1 – 220220Protein kinasePROSITE-ProRule annotationAdd
    BLAST

    Sequence similaritiesi

    Contains 1 protein kinase domain.PROSITE-ProRule annotation

    Phylogenomic databases

    eggNOGiCOG3642.
    HOGENOMiHOG000226425.
    KOiK07174.
    OMAiPPLEQLN.

    Family and domain databases

    InterProiIPR022495. Bud32.
    IPR011009. Kinase-like_dom.
    IPR000719. Prot_kinase_dom.
    IPR018934. RIO-like_kinase.
    IPR008266. Tyr_kinase_AS.
    [Graphical view]
    PANTHERiPTHR12209. PTHR12209. 1 hit.
    PfamiPF01163. RIO1. 1 hit.
    [Graphical view]
    SUPFAMiSSF56112. SSF56112. 1 hit.
    TIGRFAMsiTIGR03724. arch_bud32. 1 hit.
    PROSITEiPS50011. PROTEIN_KINASE_DOM. 1 hit.
    PS00109. PROTEIN_KINASE_TYR. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    Q9UYB9-1 [UniParc]FASTAAdd to Basket

    « Hide

    MKLIKQGAEA KIYLAEFSEL YFDYPIKVIV KERIKKRYRI PEIDLKLRKE    50
    RTIREARILR RAKEFGVNVP YVFEVDTKNM IIVMEYIEGE RLKELLEKLP 100
    MEERLKVCRE VGRQIGKLHE AGIVHGDLTT SNMILREGKV YFIDFGLAEF 150
    DDTIEAQGVD LHLLKRAMES THYKWFERGF EEVLKGYIEI RGEDKGREIR 200
    EKIREIELRG RYRERSWITQ 220
    Length:220
    Mass (Da):26,343
    Last modified:May 1, 2000 - v1
    Checksum:iA37A9382419FEF75
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AJ248288 Genomic DNA. Translation: CAB50493.1.
    HE613800 Genomic DNA. Translation: CCE71048.1.
    PIRiG75006.
    RefSeqiNP_127263.1. NC_000868.1.

    Genome annotation databases

    EnsemblBacteriaiCAB50493; CAB50493; PAB1047.
    GeneIDi1495877.
    KEGGipab:PAB1047.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AJ248288 Genomic DNA. Translation: CAB50493.1 .
    HE613800 Genomic DNA. Translation: CCE71048.1 .
    PIRi G75006.
    RefSeqi NP_127263.1. NC_000868.1.

    3D structure databases

    ProteinModelPortali Q9UYB9.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    STRINGi 272844.PAB1047.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblBacteriai CAB50493 ; CAB50493 ; PAB1047 .
    GeneIDi 1495877.
    KEGGi pab:PAB1047.

    Phylogenomic databases

    eggNOGi COG3642.
    HOGENOMi HOG000226425.
    KOi K07174.
    OMAi PPLEQLN.

    Family and domain databases

    InterProi IPR022495. Bud32.
    IPR011009. Kinase-like_dom.
    IPR000719. Prot_kinase_dom.
    IPR018934. RIO-like_kinase.
    IPR008266. Tyr_kinase_AS.
    [Graphical view ]
    PANTHERi PTHR12209. PTHR12209. 1 hit.
    Pfami PF01163. RIO1. 1 hit.
    [Graphical view ]
    SUPFAMi SSF56112. SSF56112. 1 hit.
    TIGRFAMsi TIGR03724. arch_bud32. 1 hit.
    PROSITEi PS50011. PROTEIN_KINASE_DOM. 1 hit.
    PS00109. PROTEIN_KINASE_TYR. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: GE5 / Orsay.
    2. "Re-annotation of two hyperthermophilic archaea Pyrococcus abyssi GE5 and Pyrococcus furiosus DSM 3638."
      Gao J., Wang J.
      Curr. Microbiol. 64:118-129(2012) [PubMed] [Europe PMC] [Abstract]
      Cited for: GENOME REANNOTATION.
      Strain: GE5 / Orsay.
    3. "In vitro biosynthesis of a universal t6A tRNA modification in Archaea and Eukarya."
      Perrochia L., Crozat E., Hecker A., Zhang W., Bareille J., Collinet B., van Tilbeurgh H., Forterre P., Basta T.
      Nucleic Acids Res. 41:1953-1964(2013) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION IN T(6)A TRNA MODIFICATION, SUBUNIT.
    4. "Functional assignment of KEOPS/EKC complex subunits in the biosynthesis of the universal t6A tRNA modification."
      Perrochia L., Guetta D., Hecker A., Forterre P., Basta T.
      Nucleic Acids Res. 41:9484-9499(2013) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION IN THE KEOPS COMPLEX, CATALYTIC ACTIVITY, SUBUNIT, MUTAGENESIS OF ASP-127.

    Entry informationi

    Entry nameiBUD32_PYRAB
    AccessioniPrimary (citable) accession number: Q9UYB9
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: October 1, 2014
    Last sequence update: May 1, 2000
    Last modified: October 1, 2014
    This is version 98 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programProkaryotic Protein Annotation Program

    Miscellaneousi

    Miscellaneous

    This protein is considered an atypical serine/threonine kinase, because it lacks the conventional structural elements necessary for the substrate recognition as well as a lysine residue that in all other serine/threonine kinases participates in the catalytic event By similarity. Bud32 has protein kinase activity in vitro, but in the context of the KEOPS complex, the catalytic subunit Kae1 switches the activity of Bud32 from kinase into ATPase (PubMed:23945934).By similarity1 Publication

    Keywords - Technical termi

    Complete proteome

    Documents

    1. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3