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Q58530

- KAE1B_METJA

UniProt

Q58530 - KAE1B_METJA

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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: 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. 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

Fe2+UniRule annotationNote: Binds 1 Fe(2+) 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. 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:2.6.99.4UniRule 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-HAMAP
Complete GO annotation...

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 – 76Combined sources
Beta strandi9 – 1911Combined sources
Beta strandi24 – 318Combined sources
Beta strandi37 – 404Combined sources
Helixi44 – 6219Combined sources
Helixi65 – 673Combined sources
Beta strandi70 – 789Combined sources
Helixi80 – 9718Combined sources
Beta strandi101 – 1055Combined sources
Helixi106 – 11712Combined sources
Beta strandi124 – 1285Combined sources
Beta strandi133 – 1397Combined sources
Beta strandi142 – 15211Combined sources
Helixi154 – 16411Combined sources
Helixi172 – 1809Combined sources
Helixi200 – 21112Combined sources
Helixi216 – 24227Combined sources
Beta strandi245 – 2517Combined sources
Helixi252 – 2554Combined sources
Helixi257 – 26913Combined sources
Beta strandi273 – 2753Combined sources
Helixi279 – 2824Combined sources
Helixi286 – 29813Combined sources
Helixi305 – 3073Combined sources
Beta strandi345 – 3517Combined sources
Beta strandi356 – 3627Combined sources
Helixi370 – 39021Combined sources
Helixi391 – 3944Combined sources
Beta strandi401 – 4055Combined sources
Turni406 – 4094Combined sources
Beta strandi410 – 4145Combined sources
Beta strandi418 – 4203Combined sources
Helixi421 – 4244Combined sources
Helixi430 – 44415Combined sources
Beta strandi456 – 46510Combined sources
Helixi477 – 49418Combined sources
Helixi496 – 4983Combined sources
Helixi499 – 51315Combined sources
Helixi517 – 52812Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
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.
InParanoidiQ58530.
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

« 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.
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:
EMBLi
GenBanki
DDBJi
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:
PDBei
RCSB PDBi
PDBji
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.
InParanoidi Q58530.
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

« Hide 'large scale' publications
  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: November 26, 2014
This is version 117 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