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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: Annotation score: 4 out of 5-Experimental evidence at protein leveli

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

Fe2+UniRule annotationNote: 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
Complete GO annotation...

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:2.3.1.234UniRule 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 Componenti: Chromosome

Subcellular locationi

Cytoplasm UniRule annotation

GO - Cellular componenti

  1. cytoplasm Source: UniProtKB-SubCell
Complete GO annotation...

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 – 76Combined sources
Beta strandi9 – 2113Combined sources
Beta strandi25 – 306Combined sources
Helixi40 – 6223Combined sources
Helixi66 – 683Combined sources
Beta strandi71 – 755Combined sources
Beta strandi77 – 793Combined sources
Helixi81 – 9818Combined sources
Beta strandi103 – 1053Combined sources
Helixi107 – 11913Combined sources
Beta strandi125 – 1328Combined sources
Beta strandi134 – 1396Combined sources
Beta strandi141 – 15212Combined sources
Helixi155 – 1639Combined sources
Turni164 – 1674Combined sources
Helixi172 – 1776Combined sources
Helixi178 – 1825Combined sources
Helixi201 – 21212Combined sources
Helixi217 – 24327Combined sources
Beta strandi246 – 2538Combined sources
Helixi254 – 2563Combined sources
Helixi258 – 27114Combined sources
Beta strandi273 – 2753Combined sources
Turni280 – 2834Combined sources
Helixi288 – 29912Combined sources
Helixi306 – 3083Combined sources
Helixi317 – 3193Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
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_dom.
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

        10         20         30         40         50
MIVLGLEGTA HTISCGIIDE SRILAMESSM YRPKTGGIRP LDAAVHHSEV
60 70 80 90 100
IDTVISRALE KAKISIHDID LIGFSMGPGL APSLRVTATA ARTISVLTGK
110 120 130 140 150
PIIGVNHPLG HIEIGRRVTG AIDPVMLYVS GGNTQVIAHV NGRYRVLGET
160 170 180 190 200
LDIGIGNMID KFAREAGIPF PGGPEIEKLA MKGTKLLDLP YSVKGMDTAF
210 220 230 240 250
SGILTAALQY LKTGQAIEDI SYSIQETAFA MLVEVLERAL YVSGKDEILM
260 270 280 290 300
AGGVALNRRL RDMVTNMARE AGIRSYLTDR EYCMDNGIMI AQAALLMYKS
310 320 330 340 350
GVRMSVEETA VNPRFRIDEV DAPWITDASR KDYGKAGAES RIEEVSFHGR
360 370 380 390 400
PAIRKVRISK SYRNSDLDKK IRYERMRNEF TILRKLKEAG VNSPVVYDFD
410 420 430 440 450
PFSMSITMQK IPGRMMSAEL NEGRTDFLNE LGIMIAKMHR AGIAHGDLTV
460 470 480 490 500
NNIIVNDSVF IIDPSMGKVN AEIEDMAVDI YALEDSIKGL GLDSGSVIGQ
510 520
MLKSYRNNFN LADDVLETVS AIRRRHRYV
Length:529
Mass (Da):58,202
Last modified:March 1, 2001 - v1
Checksum:i9C878F334EE056D3
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AL445064 Genomic DNA. Translation: CAC11469.1.
RefSeqiNP_393804.1. NC_002578.1.
WP_010900753.1. NC_002578.1.

Genome annotation databases

GeneIDi1455944.
KEGGitac:Ta0324.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AL445064 Genomic DNA. Translation: CAC11469.1.
RefSeqiNP_393804.1. NC_002578.1.
WP_010900753.1. NC_002578.1.

3D structure databases

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

Protein-protein interaction databases

STRINGi273075.Ta0324.

Proteomic databases

PRIDEiQ9HLA5.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

GeneIDi1455944.
KEGGitac:Ta0324.

Phylogenomic databases

eggNOGiCOG0533.
HOGENOMiHOG000109569.
KOiK15904.
OMAiRDNAGMI.

Miscellaneous databases

EvolutionaryTraceiQ9HLA5.

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_dom.
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.
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  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(1999) [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: April 1, 2015
This is version 100 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

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.