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Q58530

- KAE1B_METJA

UniProt

Q58530 - KAE1B_METJA

Protein

Probable bifunctional tRNA threonylcarbamoyladenosine biosynthesis protein

Gene

MJ1130

Organism
Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440) (Methanococcus jannaschii)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 115 (01 Oct 2014)
      Sequence version 2 (15 Dec 1998)
      Previous versions | rss
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    Functioni

    Required for the formation of a threonylcarbamoyl group on adenosine at position 37 (t6A37) in tRNAs that read codons beginning with adenine. Is a component of the KEOPS complex that is probably involved in the transfer of the threonylcarbamoyl moiety of threonylcarbamoyl-AMP (TC-AMP) to the N6 group of A37. The Kae1 domain likely plays a direct catalytic role in this reaction By similarity. The Bud32 domain probably displays kinase activity that regulates Kae1 function. In vitro, exhibits low ATPase activity, but does not bind DNA and does not have endonuclease activity.1 PublicationUniRule annotation

    Catalytic activityi

    ATP + a protein = ADP + a phosphoprotein.UniRule annotation
    L-threonylcarbamoyladenylate + adenine(37) in tRNA = AMP + N(6)-L-threonylcarbamoyladenine(37) in tRNA.UniRule annotation

    Cofactori

    Binds 1 Fe2+ ion per subunit.UniRule annotation

    Enzyme regulationi

    Activity provided by the Kae1 region seems to be regulated via phosphorylation by the protein kinase Bud32, which is itself activated by Cgi121.1 Publication

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Metal bindingi106 – 1061IronCurated
    Metal bindingi110 – 1101IronCurated
    Metal bindingi127 – 1271IronCurated
    Binding sitei159 – 1591Threonylcarbamoyl-AMPCurated
    Binding sitei172 – 1721Threonylcarbamoyl-AMP; via amide nitrogenUniRule annotation
    Binding sitei176 – 1761Threonylcarbamoyl-AMPCurated
    Binding sitei256 – 2561Threonylcarbamoyl-AMPCurated
    Metal bindingi284 – 2841IronCurated
    Binding sitei360 – 3601ATPUniRule annotation
    Active sitei451 – 4511Proton acceptor; for kinase activityUniRule annotation

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Nucleotide bindingi339 – 3479ATPUniRule annotation

    GO - Molecular functioni

    1. ATP binding Source: UniProtKB-HAMAP
    2. iron ion binding Source: UniProtKB-HAMAP
    3. metalloendopeptidase activity Source: InterPro
    4. protein serine/threonine/tyrosine kinase activity Source: UniProtKB-HAMAP
    5. protein serine/threonine kinase activity Source: UniProtKB-KW
    6. protein tyrosine kinase activity Source: InterPro
    7. transferase activity, transferring acyl groups other than amino-acyl groups Source: UniProtKB-HAMAP
    8. zinc ion binding Source: InterPro

    GO - Biological processi

    1. threonylcarbamoyladenosine biosynthetic process Source: UniProtKB-HAMAP

    Keywords - Molecular functioni

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

    Keywords - Biological processi

    tRNA processing

    Keywords - Ligandi

    ATP-binding, Iron, Metal-binding, Nucleotide-binding

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Probable bifunctional tRNA threonylcarbamoyladenosine biosynthesis proteinUniRule annotation
    Including the following 2 domains:
    tRNA N6-adenosine threonylcarbamoyltransferaseUniRule annotation (EC:2.6.99.4UniRule annotation)
    Alternative name(s):
    N6-L-threonylcarbamoyladenine synthase
    Short name:
    t(6)A synthase
    t(6)A37 threonylcarbamoyladenosine biosynthesis protein Kae1UniRule annotation
    tRNA threonylcarbamoyladenosine biosynthesis protein Kae1UniRule annotation
    Serine/threonine-protein kinase Bud32UniRule annotation (EC:2.7.11.1UniRule annotation)
    Gene namesi
    Ordered Locus Names:MJ1130
    OrganismiMethanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440) (Methanococcus jannaschii)
    Taxonomic identifieri243232 [NCBI]
    Taxonomic lineageiArchaeaEuryarchaeotaMethanococciMethanococcalesMethanocaldococcaceaeMethanocaldococcus
    ProteomesiUP000000805: Chromosome

    Subcellular locationi

    Cytoplasm UniRule annotation

    GO - Cellular componenti

    1. cytoplasm Source: UniProtKB-SubCell

    Keywords - Cellular componenti

    Cytoplasm

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 535535Probable bifunctional tRNA threonylcarbamoyladenosine biosynthesis proteinPRO_0000096979Add
    BLAST

    Interactioni

    Subunit structurei

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

    Protein-protein interaction databases

    STRINGi243232.MJ1130.

    Structurei

    Secondary structure

    1
    535
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi2 – 76
    Beta strandi9 – 1911
    Beta strandi24 – 318
    Beta strandi37 – 404
    Helixi44 – 6219
    Helixi65 – 673
    Beta strandi70 – 789
    Helixi80 – 9718
    Beta strandi101 – 1055
    Helixi106 – 11712
    Beta strandi124 – 1285
    Beta strandi133 – 1397
    Beta strandi142 – 15211
    Helixi154 – 16411
    Helixi172 – 1809
    Helixi200 – 21112
    Helixi216 – 24227
    Beta strandi245 – 2517
    Helixi252 – 2554
    Helixi257 – 26913
    Beta strandi273 – 2753
    Helixi279 – 2824
    Helixi286 – 29813
    Helixi305 – 3073
    Beta strandi345 – 3517
    Beta strandi356 – 3627
    Helixi370 – 39021
    Helixi391 – 3944
    Beta strandi401 – 4055
    Turni406 – 4094
    Beta strandi410 – 4145
    Beta strandi418 – 4203
    Helixi421 – 4244
    Helixi430 – 44415
    Beta strandi456 – 46510
    Helixi477 – 49418
    Helixi496 – 4983
    Helixi499 – 51315
    Helixi517 – 52812

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    2VWBX-ray3.05A/B1-535[»]
    3EN9X-ray2.67A/B1-535[»]
    3ENHX-ray3.60A/B1-535[»]
    ProteinModelPortaliQ58530.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiQ58530.

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini333 – 535203Protein kinaseUniRule annotationAdd
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni1 – 323323Kae1Add
    BLAST
    Regioni127 – 1315Threonylcarbamoyl-AMP bindingCurated

    Sequence similaritiesi

    In the N-terminal section; belongs to the KAE1 / TsaD family.UniRule annotation
    In the C-terminal section; belongs to the protein kinase superfamily. Tyr protein kinase family. BUD32 subfamily.UniRule annotation
    Contains 1 protein kinase domain.UniRule annotation

    Phylogenomic databases

    eggNOGiCOG0533.
    KOiK15904.
    OMAiRDNAGMI.
    PhylomeDBiQ58530.

    Family and domain databases

    HAMAPiMF_01446. Kae1_arch.
    MF_01447. Kae1_Bud32_arch.
    InterProiIPR022495. Bud32.
    IPR000905. Gcp-like_dom.
    IPR022449. Kae1.
    IPR017861. KAE1/YgjD.
    IPR011009. Kinase-like_dom.
    IPR017860. Peptidase_M22_CS.
    IPR000719. Prot_kinase_dom.
    IPR009220. tRNA_threonyl_synthase/kinase.
    IPR008266. Tyr_kinase_AS.
    [Graphical view]
    PfamiPF00814. Peptidase_M22. 1 hit.
    PF00069. Pkinase. 1 hit.
    [Graphical view]
    PIRSFiPIRSF036401. Gcp_STYKS. 1 hit.
    PRINTSiPR00789. OSIALOPTASE.
    SUPFAMiSSF56112. SSF56112. 1 hit.
    TIGRFAMsiTIGR03724. arch_bud32. 1 hit.
    TIGR03722. arch_KAE1. 1 hit.
    TIGR00329. gcp_kae1. 1 hit.
    PROSITEiPS01016. GLYCOPROTEASE. 1 hit.
    PS50011. PROTEIN_KINASE_DOM. 1 hit.
    PS00109. PROTEIN_KINASE_TYR. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    Q58530-1 [UniParc]FASTAAdd to Basket

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    MICLGLEGTA EKTGVGIVTS DGEVLFNKTI MYKPPKQGIN PREAADHHAE    50
    TFPKLIKEAF EVVDKNEIDL IAFSQGPGLG PSLRVTATVA RTLSLTLKKP 100
    IIGVNHCIAH IEIGKLTTEA EDPLTLYVSG GNTQVIAYVS KKYRVFGETL 150
    DIAVGNCLDQ FARYVNLPHP GGPYIEELAR KGKKLVDLPY TVKGMDIAFS 200
    GLLTAAMRAY DAGERLEDIC YSLQEYAFSM LTEITERALA HTNKGEVMLV 250
    GGVAANNRLR EMLKAMCEGQ NVDFYVPPKE FCGDNGAMIA WLGLLMHKNG 300
    RWMSLDETKI IPNYRTDMVE VNWIKEIKGK KRKIPEHLIG KGAEADIKRD 350
    SYLDFDVIIK ERVKKGYRDE RLDENIRKSR TAREARYLAL VKDFGIPAPY 400
    IFDVDLDNKR IMMSYINGKL AKDVIEDNLD IAYKIGEIVG KLHKNDVIHN 450
    DLTTSNFIFD KDLYIIDFGL GKISNLDEDK AVDLIVFKKA VLSTHHEKFD 500
    EIWERFLEGY KSVYDRWEII LELMKDVERR ARYVE 535
    Length:535
    Mass (Da):60,570
    Last modified:December 15, 1998 - v2
    Checksum:iB18EEFACE8E5A99F
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    L77117 Genomic DNA. Translation: AAB99132.1.
    RefSeqiNP_248122.1. NC_000909.1.
    WP_010870641.1. NC_000909.1.

    Genome annotation databases

    EnsemblBacteriaiAAB99132; AAB99132; MJ_1130.
    GeneIDi1452026.
    KEGGimja:MJ_1130.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    L77117 Genomic DNA. Translation: AAB99132.1 .
    RefSeqi NP_248122.1. NC_000909.1.
    WP_010870641.1. NC_000909.1.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    2VWB X-ray 3.05 A/B 1-535 [» ]
    3EN9 X-ray 2.67 A/B 1-535 [» ]
    3ENH X-ray 3.60 A/B 1-535 [» ]
    ProteinModelPortali Q58530.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    STRINGi 243232.MJ1130.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblBacteriai AAB99132 ; AAB99132 ; MJ_1130 .
    GeneIDi 1452026.
    KEGGi mja:MJ_1130.

    Phylogenomic databases

    eggNOGi COG0533.
    KOi K15904.
    OMAi RDNAGMI.
    PhylomeDBi Q58530.

    Miscellaneous databases

    EvolutionaryTracei Q58530.

    Family and domain databases

    HAMAPi MF_01446. Kae1_arch.
    MF_01447. Kae1_Bud32_arch.
    InterProi IPR022495. Bud32.
    IPR000905. Gcp-like_dom.
    IPR022449. Kae1.
    IPR017861. KAE1/YgjD.
    IPR011009. Kinase-like_dom.
    IPR017860. Peptidase_M22_CS.
    IPR000719. Prot_kinase_dom.
    IPR009220. tRNA_threonyl_synthase/kinase.
    IPR008266. Tyr_kinase_AS.
    [Graphical view ]
    Pfami PF00814. Peptidase_M22. 1 hit.
    PF00069. Pkinase. 1 hit.
    [Graphical view ]
    PIRSFi PIRSF036401. Gcp_STYKS. 1 hit.
    PRINTSi PR00789. OSIALOPTASE.
    SUPFAMi SSF56112. SSF56112. 1 hit.
    TIGRFAMsi TIGR03724. arch_bud32. 1 hit.
    TIGR03722. arch_KAE1. 1 hit.
    TIGR00329. gcp_kae1. 1 hit.
    PROSITEi PS01016. GLYCOPROTEASE. 1 hit.
    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: ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440.
    2. "Structure of the archaeal Kae1/Bud32 fusion protein MJ1130: a model for the eukaryotic EKC/KEOPS subcomplex."
      Hecker A., Lopreiato R., Graille M., Collinet B., Forterre P., Libri D., van Tilbeurgh H.
      EMBO J. 27:2340-2351(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (3.05 ANGSTROMS) IN COMPLEX WITH AN ATP ANALOG.
    3. Cited for: X-RAY CRYSTALLOGRAPHY (2.67 ANGSTROMS) IN COMPLEXES WITH MAGNESIUM AND CGI121, FUNCTION, SUBUNIT, ENZYME REGULATION.

    Entry informationi

    Entry nameiKAE1B_METJA
    AccessioniPrimary (citable) accession number: Q58530
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: July 15, 1998
    Last sequence update: December 15, 1998
    Last modified: October 1, 2014
    This is version 115 of the entry and version 2 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programProkaryotic Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    3D-structure, Complete proteome, Multifunctional enzyme, Reference proteome

    Documents

    1. Methanococcus jannaschii
      Methanococcus jannaschii: entries and gene names
    2. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    3. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3