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Q9HLA5

- KAE1B_THEAC

UniProt

Q9HLA5 - KAE1B_THEAC

Protein

Probable bifunctional tRNA threonylcarbamoyladenosine biosynthesis protein

Gene

Ta0324

Organism
Thermoplasma acidophilum (strain ATCC 25905 / DSM 1728 / JCM 9062 / NBRC 15155 / AMRC-C165)
Status
Reviewed - Annotation score: 4 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 95 (01 Oct 2014)
      Sequence version 1 (01 Mar 2001)
      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. The Bud32 domain probably displays kinase activity that regulates Kae1 function.UniRule 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

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Metal bindingi107 – 1071IronUniRule annotation
    Metal bindingi111 – 1111IronUniRule annotation
    Metal bindingi128 – 1281IronUniRule annotation
    Binding sitei160 – 1601Threonylcarbamoyl-AMPUniRule annotation
    Binding sitei173 – 1731Threonylcarbamoyl-AMP; via amide nitrogenUniRule annotation
    Binding sitei177 – 1771Threonylcarbamoyl-AMPUniRule annotation
    Binding sitei257 – 2571Threonylcarbamoyl-AMPUniRule annotation
    Metal bindingi285 – 2851IronUniRule annotation
    Binding sitei355 – 3551ATPUniRule annotation
    Active sitei447 – 4471Proton acceptor; for kinase activityUniRule annotation

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Nucleotide bindingi335 – 3428ATPUniRule 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. transferase activity, transferring acyl groups other than amino-acyl groups Source: UniProtKB-HAMAP
    7. 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:Ta0324
    OrganismiThermoplasma acidophilum (strain ATCC 25905 / DSM 1728 / JCM 9062 / NBRC 15155 / AMRC-C165)
    Taxonomic identifieri273075 [NCBI]
    Taxonomic lineageiArchaeaEuryarchaeotaThermoplasmataThermoplasmatalesThermoplasmataceaeThermoplasma
    ProteomesiUP000001024: 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 – 529529Probable bifunctional tRNA threonylcarbamoyladenosine biosynthesis proteinPRO_0000303661Add
    BLAST

    Proteomic databases

    PRIDEiQ9HLA5.

    Interactioni

    Subunit structurei

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

    Protein-protein interaction databases

    STRINGi273075.Ta0324.

    Structurei

    Secondary structure

    1
    529
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi2 – 76
    Beta strandi9 – 2113
    Beta strandi25 – 306
    Helixi40 – 6223
    Helixi66 – 683
    Beta strandi71 – 755
    Beta strandi77 – 793
    Helixi81 – 9818
    Beta strandi103 – 1053
    Helixi107 – 11913
    Beta strandi125 – 1328
    Beta strandi134 – 1396
    Beta strandi141 – 15212
    Helixi155 – 1639
    Turni164 – 1674
    Helixi172 – 1776
    Helixi178 – 1825
    Helixi201 – 21212
    Helixi217 – 24327
    Beta strandi246 – 2538
    Helixi254 – 2563
    Helixi258 – 27114
    Beta strandi273 – 2753
    Turni280 – 2834
    Helixi288 – 29912
    Helixi306 – 3083
    Helixi317 – 3193

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    3ENOX-ray3.02A/B1-329[»]
    ProteinModelPortaliQ9HLA5.
    SMRiQ9HLA5. Positions 1-325.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiQ9HLA5.

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini329 – 529201Protein kinaseUniRule annotationAdd
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni1 – 324324Kae1Add
    BLAST
    Regioni128 – 1325Threonylcarbamoyl-AMP bindingUniRule annotation

    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.
    HOGENOMiHOG000109569.
    KOiK15904.
    OMAiRDNAGMI.

    Family and domain databases

    HAMAPiMF_01447. Kae1_Bud32_arch.
    InterProiIPR022495. Bud32.
    IPR000905. Gcp-like_dom.
    IPR022449. Kae1.
    IPR017861. KAE1/YgjD.
    IPR011009. Kinase-like_dom.
    IPR018934. RIO-like_kinase.
    IPR009220. tRNA_threonyl_synthase/kinase.
    [Graphical view]
    PfamiPF00814. Peptidase_M22. 1 hit.
    PF01163. RIO1. 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.

    Sequencei

    Sequence statusi: Complete.

    Q9HLA5-1 [UniParc]FASTAAdd to Basket

    « Hide

    MIVLGLEGTA HTISCGIIDE SRILAMESSM YRPKTGGIRP LDAAVHHSEV    50
    IDTVISRALE KAKISIHDID LIGFSMGPGL APSLRVTATA ARTISVLTGK 100
    PIIGVNHPLG HIEIGRRVTG AIDPVMLYVS GGNTQVIAHV NGRYRVLGET 150
    LDIGIGNMID KFAREAGIPF PGGPEIEKLA MKGTKLLDLP YSVKGMDTAF 200
    SGILTAALQY LKTGQAIEDI SYSIQETAFA MLVEVLERAL YVSGKDEILM 250
    AGGVALNRRL RDMVTNMARE AGIRSYLTDR EYCMDNGIMI AQAALLMYKS 300
    GVRMSVEETA VNPRFRIDEV DAPWITDASR KDYGKAGAES RIEEVSFHGR 350
    PAIRKVRISK SYRNSDLDKK IRYERMRNEF TILRKLKEAG VNSPVVYDFD 400
    PFSMSITMQK IPGRMMSAEL NEGRTDFLNE LGIMIAKMHR AGIAHGDLTV 450
    NNIIVNDSVF IIDPSMGKVN AEIEDMAVDI YALEDSIKGL GLDSGSVIGQ 500
    MLKSYRNNFN LADDVLETVS AIRRRHRYV 529
    Length:529
    Mass (Da):58,202
    Last modified:March 1, 2001 - v1
    Checksum:i9C878F334EE056D3
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AL445064 Genomic DNA. Translation: CAC11469.1.
    RefSeqiNP_393804.1. NC_002578.1.
    WP_010900753.1. NC_002578.1.

    Genome annotation databases

    EnsemblBacteriaiCAC11469; CAC11469; CAC11469.
    GeneIDi1455944.
    KEGGitac:Ta0324.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AL445064 Genomic DNA. Translation: CAC11469.1 .
    RefSeqi NP_393804.1. NC_002578.1.
    WP_010900753.1. NC_002578.1.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    3ENO X-ray 3.02 A/B 1-329 [» ]
    ProteinModelPortali Q9HLA5.
    SMRi Q9HLA5. Positions 1-325.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    STRINGi 273075.Ta0324.

    Proteomic databases

    PRIDEi Q9HLA5.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblBacteriai CAC11469 ; CAC11469 ; CAC11469 .
    GeneIDi 1455944.
    KEGGi tac:Ta0324.

    Phylogenomic databases

    eggNOGi COG0533.
    HOGENOMi HOG000109569.
    KOi K15904.
    OMAi RDNAGMI.

    Miscellaneous databases

    EvolutionaryTracei Q9HLA5.

    Family and domain databases

    HAMAPi MF_01447. Kae1_Bud32_arch.
    InterProi IPR022495. Bud32.
    IPR000905. Gcp-like_dom.
    IPR022449. Kae1.
    IPR017861. KAE1/YgjD.
    IPR011009. Kinase-like_dom.
    IPR018934. RIO-like_kinase.
    IPR009220. tRNA_threonyl_synthase/kinase.
    [Graphical view ]
    Pfami PF00814. Peptidase_M22. 1 hit.
    PF01163. RIO1. 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.
    ProtoNeti Search...

    Publicationsi

    1. "The genome sequence of the thermoacidophilic scavenger Thermoplasma acidophilum."
      Ruepp A., Graml W., Santos-Martinez M.-L., Koretke K.K., Volker C., Mewes H.-W., Frishman D., Stocker S., Lupas A.N., Baumeister W.
      Nature 407:508-513(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: ATCC 25905 / DSM 1728 / JCM 9062 / NBRC 15155 / AMRC-C165.
    2. Cited for: X-RAY CRYSTALLOGRAPHY (3.02 ANGSTROMS) OF 1-329.

    Entry informationi

    Entry nameiKAE1B_THEAC
    AccessioniPrimary (citable) accession number: Q9HLA5
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: September 11, 2007
    Last sequence update: March 1, 2001
    Last modified: October 1, 2014
    This is version 95 of the entry and version 1 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. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    2. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3