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Protein

tRNA N6-adenosine threonylcarbamoyltransferase

Gene

kae1

Organism
Pyrococcus abyssi (strain GE5 / Orsay)
Status
Reviewed-Annotation score: Annotation score: 5 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. Kae1 likely plays a direct catalytic role in this reaction, but requires other protein(s) of the complex to fulfill this activity. In vitro, binds tRNA, ssRNA, both single- and double-stranded DNA, and exhibits a low ATPase activity.UniRule annotation4 Publications

Catalytic activityi

L-threonylcarbamoyladenylate + adenine(37) in tRNA = AMP + N(6)-L-threonylcarbamoyladenine(37) in tRNA.UniRule annotation1 Publication

Cofactori

Fe2+UniRule annotation1 PublicationNote: Binds 1 Fe2+ ion per subunit.UniRule annotation1 Publication

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Metal bindingi107IronUniRule annotation1 Publication1
Metal bindingi111IronUniRule annotation1 Publication1
Metal bindingi127IronUniRule annotation1 Publication1
Binding sitei159SubstrateCurated1
Binding sitei172Substrate; via amide nitrogenCurated1
Binding sitei176SubstrateCurated1
Binding sitei257SubstrateCurated1
Metal bindingi285IronUniRule annotation1 Publication1

GO - Molecular functioni

  • metal ion binding Source: UniProtKB-KW
  • N(6)-L-threonylcarbamoyladenine synthase Source: UniProtKB-EC
  • single-stranded RNA binding Source: UniProtKB
  • tRNA binding Source: UniProtKB

GO - Biological processi

  • tRNA threonylcarbamoyladenosine modification Source: UniProtKB
Complete GO annotation...

Keywords - Molecular functioni

Acyltransferase, Transferase

Keywords - Biological processi

tRNA processing

Keywords - Ligandi

Iron, Metal-binding

Enzyme and pathway databases

BRENDAi2.6.99.4. 5242.

Names & Taxonomyi

Protein namesi
Recommended name:
tRNA N6-adenosine threonylcarbamoyltransferaseUniRule annotation (EC:2.3.1.234UniRule annotation1 Publication)
Alternative name(s):
N6-L-threonylcarbamoyladenine synthaseUniRule annotation
Short name:
t(6)A synthaseUniRule annotation
Pa-Kae1
t(6)A37 threonylcarbamoyladenosine biosynthesis protein Kae1UniRule annotation
tRNA threonylcarbamoyladenosine biosynthesis protein Kae1UniRule annotation
Gene namesi
Name:kae1UniRule annotation
Ordered Locus Names:PYRAB17710
ORF Names:PAB1159
OrganismiPyrococcus abyssi (strain GE5 / Orsay)
Taxonomic identifieri272844 [NCBI]
Taxonomic lineageiArchaeaEuryarchaeotaThermococciThermococcalesThermococcaceaePyrococcus
Proteomesi
  • UP000000810 Componenti: Chromosome
  • UP000009139 Componenti: Chromosome

Subcellular locationi

  • Cytoplasm UniRule annotation

GO - Cellular componenti

  • cytoplasm Source: UniProtKB-SubCell
  • EKC/KEOPS complex Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi107H → A: Abolishes iron binding. Reduces the tRNA modification activity of the KEOPS complex by 90%. 1 Publication1
Mutagenesisi127Y → F: Loss of iron, but no change in DNA-binding. 1 Publication1
Mutagenesisi159D → A: Completely impairs the tRNA modification activity of the KEOPS complex. Does not impair ATPase activity of the complex. 1 Publication1

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00000969811 – 324tRNA N6-adenosine threonylcarbamoyltransferaseAdd BLAST324

Interactioni

Subunit structurei

Monomer. Component of the KEOPS complex that consists of Kae1, Bud32, Cgi121 and Pcc1; the whole complex dimerizes.UniRule annotation3 Publications

Protein-protein interaction databases

STRINGi272844.PAB1159.

Structurei

Secondary structure

1324
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi3 – 7Combined sources5
Beta strandi9 – 18Combined sources10
Beta strandi23 – 30Combined sources8
Helixi40 – 62Combined sources23
Turni66 – 68Combined sources3
Beta strandi71 – 79Combined sources9
Helixi81 – 97Combined sources17
Beta strandi102 – 106Combined sources5
Helixi107 – 113Combined sources7
Helixi114 – 118Combined sources5
Beta strandi124 – 128Combined sources5
Beta strandi133 – 139Combined sources7
Beta strandi142 – 152Combined sources11
Helixi154 – 165Combined sources12
Helixi171 – 180Combined sources10
Helixi200 – 212Combined sources13
Helixi217 – 243Combined sources27
Beta strandi246 – 252Combined sources7
Helixi253 – 256Combined sources4
Helixi258 – 271Combined sources14
Beta strandi274 – 276Combined sources3
Helixi280 – 283Combined sources4
Helixi287 – 299Combined sources13
Helixi306 – 309Combined sources4
Helixi317 – 319Combined sources3

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
2IVNX-ray1.65A1-324[»]
2IVOX-ray2.90A/B/C/D1-324[»]
2IVPX-ray2.50A1-324[»]
ProteinModelPortaliQ9UXT7.
SMRiQ9UXT7.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ9UXT7.

Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni127 – 131Substrate bindingCurated5

Sequence similaritiesi

Belongs to the KAE1 / TsaD family.UniRule annotation

Phylogenomic databases

eggNOGiarCOG01183. Archaea.
COG0533. LUCA.
HOGENOMiHOG000109569.
KOiK01409.
OMAiLMIAHAG.

Family and domain databases

HAMAPiMF_01446. Kae1. 1 hit.
InterProiIPR000905. Gcp-like_dom.
IPR022449. Kae1.
IPR017861. KAE1/TsaD.
IPR017860. Peptidase_M22_CS.
[Graphical view]
PfamiPF00814. Peptidase_M22. 1 hit.
[Graphical view]
PRINTSiPR00789. OSIALOPTASE.
TIGRFAMsiTIGR03722. arch_KAE1. 1 hit.
TIGR00329. gcp_kae1. 1 hit.
PROSITEiPS01016. GLYCOPROTEASE. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q9UXT7-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MLALGIEGTA HTLGIGIVSE DKVLANVFDT LTTEKGGIHP KEAAEHHARL
60 70 80 90 100
MKPLLRKALS EAGVSLDDID VIAFSQGPGL GPALRVVATA ARALAVKYRK
110 120 130 140 150
PIVGVNHCIA HVEITKMFGV KDPVGLYVSG GNTQVLALEG GRYRVFGETL
160 170 180 190 200
DIGIGNAIDV FARELGLGFP GGPKVEKLAE KGEKYIELPY AVKGMDLSFS
210 220 230 240 250
GLLTEAIRKY RSGKYRVEDL AYSFQETAFA ALVEVTERAV AHTEKDEVVL
260 270 280 290 300
VGGVAANNRL REMLRIMTED RGIKFFVPPY DLCRDNGAMI AYTGLRMYKA
310 320
GISFRLEETI VKQKFRTDEV EIVW
Length:324
Mass (Da):35,368
Last modified:May 1, 2000 - v1
Checksum:iD0A3E4279EA04C31
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AJ248288 Genomic DNA. Translation: CAB50676.1.
HE613800 Genomic DNA. Translation: CCE71245.1.
PIRiF75029.
RefSeqiWP_010868890.1. NC_000868.1.

Genome annotation databases

EnsemblBacteriaiCAB50676; CAB50676; PAB1159.
GeneIDi1496074.
KEGGipab:PAB1159.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AJ248288 Genomic DNA. Translation: CAB50676.1.
HE613800 Genomic DNA. Translation: CCE71245.1.
PIRiF75029.
RefSeqiWP_010868890.1. NC_000868.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
2IVNX-ray1.65A1-324[»]
2IVOX-ray2.90A/B/C/D1-324[»]
2IVPX-ray2.50A1-324[»]
ProteinModelPortaliQ9UXT7.
SMRiQ9UXT7.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi272844.PAB1159.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiCAB50676; CAB50676; PAB1159.
GeneIDi1496074.
KEGGipab:PAB1159.

Phylogenomic databases

eggNOGiarCOG01183. Archaea.
COG0533. LUCA.
HOGENOMiHOG000109569.
KOiK01409.
OMAiLMIAHAG.

Enzyme and pathway databases

BRENDAi2.6.99.4. 5242.

Miscellaneous databases

EvolutionaryTraceiQ9UXT7.

Family and domain databases

HAMAPiMF_01446. Kae1. 1 hit.
InterProiIPR000905. Gcp-like_dom.
IPR022449. Kae1.
IPR017861. KAE1/TsaD.
IPR017860. Peptidase_M22_CS.
[Graphical view]
PfamiPF00814. Peptidase_M22. 1 hit.
[Graphical view]
PRINTSiPR00789. OSIALOPTASE.
TIGRFAMsiTIGR03722. arch_KAE1. 1 hit.
TIGR00329. gcp_kae1. 1 hit.
PROSITEiPS01016. GLYCOPROTEASE. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiKAE1_PYRAB
AccessioniPrimary (citable) accession number: Q9UXT7
Secondary accession number(s): G8ZKV4
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 2, 2001
Last sequence update: May 1, 2000
Last modified: November 30, 2016
This is version 112 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Miscellaneous

The ATP binding pocket identified in the crystal structure would actually engage the substrate TC-AMP.

Caution

Was originally (PubMed:17766251) thought to have endonuclease activity, but it could not be confirmed with orthologs purified from M.jannaschii (PubMed:18951093) and S. cerevisiae (PubMed:21183954).1 Publication

Keywords - Technical termi

3D-structure, Complete proteome

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. SIMILARITY comments
    Index of protein domains and families

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 one 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.