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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: -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 (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.UniRule annotation1 Publication

Catalytic activityi

ATP + a protein = ADP + a phosphoprotein.UniRule annotation
L-threonylcarbamoyladenylate + adenine(37) in tRNA = AMP + N6-L-threonylcarbamoyladenine(37) in tRNA.UniRule annotation

Cofactori

Fe2+UniRule annotationNote: 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)DescriptionActionsGraphical viewLength
Metal bindingi106IronCurated1
Metal bindingi110IronCurated1
Metal bindingi127IronCurated1
Binding sitei159Threonylcarbamoyl-AMPCurated1
Binding sitei172Threonylcarbamoyl-AMP; via amide nitrogenUniRule annotation1
Binding sitei176Threonylcarbamoyl-AMPCurated1
Binding sitei256Threonylcarbamoyl-AMPCurated1
Metal bindingi284IronCurated1
Binding sitei360ATPUniRule annotation1
Active sitei451Proton acceptor; for kinase activityUniRule annotation1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Nucleotide bindingi339 – 347ATPUniRule annotation9

GO - Molecular functioni

GO - Biological processi

Keywordsi

Molecular functionAcyltransferase, Kinase, Multifunctional enzyme, Serine/threonine-protein kinase, Transferase
Biological processtRNA processing
LigandATP-binding, Iron, Metal-binding, Nucleotide-binding

Enzyme and pathway databases

BioCyciMJAN243232:G1GKE-1225-MONOMER

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:MJ1130
OrganismiMethanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440) (Methanococcus jannaschii)
Taxonomic identifieri243232 [NCBI]
Taxonomic lineageiArchaeaEuryarchaeotaMethanococciMethanococcalesMethanocaldococcaceaeMethanocaldococcus
Proteomesi
  • UP000000805 Componenti: Chromosome

Subcellular locationi

  • Cytoplasm UniRule annotation

GO - Cellular componenti

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00000969791 – 535Probable bifunctional tRNA threonylcarbamoyladenosine biosynthesis proteinAdd BLAST535

Interactioni

Subunit structurei

Component of the KEOPS complex that consists of Kae1, Bud32, Cgi121 and Pcc1; the whole complex dimerizes.UniRule annotation2 Publications

Protein-protein interaction databases

STRINGi243232.MJ_1130

Structurei

Secondary structure

1535
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi2 – 7Combined sources6
Beta strandi9 – 19Combined sources11
Beta strandi20 – 22Combined sources3
Beta strandi24 – 31Combined sources8
Beta strandi37 – 40Combined sources4
Helixi44 – 62Combined sources19
Helixi65 – 67Combined sources3
Beta strandi70 – 78Combined sources9
Helixi80 – 97Combined sources18
Beta strandi101 – 105Combined sources5
Helixi106 – 117Combined sources12
Beta strandi124 – 128Combined sources5
Beta strandi133 – 139Combined sources7
Beta strandi142 – 152Combined sources11
Helixi154 – 164Combined sources11
Helixi172 – 180Combined sources9
Helixi200 – 211Combined sources12
Helixi216 – 242Combined sources27
Beta strandi245 – 251Combined sources7
Helixi252 – 255Combined sources4
Helixi257 – 269Combined sources13
Beta strandi273 – 275Combined sources3
Helixi279 – 282Combined sources4
Helixi286 – 298Combined sources13
Helixi305 – 307Combined sources3
Helixi316 – 318Combined sources3
Beta strandi345 – 351Combined sources7
Beta strandi356 – 362Combined sources7
Helixi370 – 390Combined sources21
Helixi391 – 394Combined sources4
Beta strandi401 – 405Combined sources5
Turni406 – 409Combined sources4
Beta strandi410 – 414Combined sources5
Beta strandi418 – 420Combined sources3
Helixi421 – 424Combined sources4
Helixi430 – 444Combined sources15
Beta strandi456 – 465Combined sources10
Helixi477 – 494Combined sources18
Helixi496 – 498Combined sources3
Helixi499 – 513Combined sources15
Helixi517 – 528Combined sources12

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
2VWBX-ray3.05A/B1-535[»]
3EN9X-ray2.67A/B1-535[»]
3ENHX-ray3.60A/B1-535[»]
5JMVX-ray3.39A/B/C1-335[»]
ProteinModelPortaliQ58530
SMRiQ58530
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ58530

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini333 – 535Protein kinaseUniRule annotationAdd BLAST203

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni1 – 323Kae1Add BLAST323
Regioni127 – 131Threonylcarbamoyl-AMP bindingCurated5

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

Phylogenomic databases

eggNOGiarCOG01183 Archaea
arCOG01185 Archaea
COG0533 LUCA
COG3642 LUCA
InParanoidiQ58530
KOiK15904
OMAiGETMDTG
OrthoDBiPOG093Z05SV
PhylomeDBiQ58530

Family and domain databases

HAMAPiMF_01446 Kae1, 1 hit
MF_01447 Kae1_Bud32_arch, 1 hit
InterProiView protein in InterPro
IPR022495 Bud32
IPR000905 Gcp-like_dom
IPR034680 Kae1/OSGEP
IPR017861 KAE1/TsaD
IPR022449 Kae1_arc
IPR011009 Kinase-like_dom_sf
IPR017860 Peptidase_M22_CS
IPR000719 Prot_kinase_dom
IPR009220 tRNA_threonyl_synthase/kinase
IPR008266 Tyr_kinase_AS
PANTHERiPTHR11735 PTHR11735, 1 hit
PTHR11735:SF14 PTHR11735:SF14, 1 hit
PfamiView protein in Pfam
PF00814 Peptidase_M22, 1 hit
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
PROSITEiView protein in PROSITE
PS01016 GLYCOPROTEASE, 1 hit
PS50011 PROTEIN_KINASE_DOM, 1 hit
PS00109 PROTEIN_KINASE_TYR, 1 hit

Sequencei

Sequence statusi: Complete.

Q58530-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MICLGLEGTA EKTGVGIVTS DGEVLFNKTI MYKPPKQGIN PREAADHHAE
60 70 80 90 100
TFPKLIKEAF EVVDKNEIDL IAFSQGPGLG PSLRVTATVA RTLSLTLKKP
110 120 130 140 150
IIGVNHCIAH IEIGKLTTEA EDPLTLYVSG GNTQVIAYVS KKYRVFGETL
160 170 180 190 200
DIAVGNCLDQ FARYVNLPHP GGPYIEELAR KGKKLVDLPY TVKGMDIAFS
210 220 230 240 250
GLLTAAMRAY DAGERLEDIC YSLQEYAFSM LTEITERALA HTNKGEVMLV
260 270 280 290 300
GGVAANNRLR EMLKAMCEGQ NVDFYVPPKE FCGDNGAMIA WLGLLMHKNG
310 320 330 340 350
RWMSLDETKI IPNYRTDMVE VNWIKEIKGK KRKIPEHLIG KGAEADIKRD
360 370 380 390 400
SYLDFDVIIK ERVKKGYRDE RLDENIRKSR TAREARYLAL VKDFGIPAPY
410 420 430 440 450
IFDVDLDNKR IMMSYINGKL AKDVIEDNLD IAYKIGEIVG KLHKNDVIHN
460 470 480 490 500
DLTTSNFIFD KDLYIIDFGL GKISNLDEDK AVDLIVFKKA VLSTHHEKFD
510 520 530
EIWERFLEGY KSVYDRWEII LELMKDVERR ARYVE
Length:535
Mass (Da):60,570
Last modified:December 15, 1998 - v2
Checksum:iB18EEFACE8E5A99F
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
L77117 Genomic DNA Translation: AAB99132.1
RefSeqiWP_010870641.1, NC_000909.1

Genome annotation databases

EnsemblBacteriaiAAB99132; AAB99132; MJ_1130
GeneIDi1452026
KEGGimja:MJ_1130

Similar proteinsi

Entry informationi

Entry nameiKAE1B_METJA
AccessioniPrimary (citable) accession number: Q58530
Entry historyiIntegrated into UniProtKB/Swiss-Prot: July 15, 1998
Last sequence update: December 15, 1998
Last modified: May 23, 2018
This is version 137 of the entry and version 2 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

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