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Q8TJS2

- KAE1B_METAC

UniProt

Q8TJS2 - KAE1B_METAC

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Protein

Probable bifunctional tRNA threonylcarbamoyladenosine biosynthesis protein

Gene

MA_3705

Organism
Methanosarcina acetivorans (strain ATCC 35395 / DSM 2834 / JCM 12185 / C2A)
Status
Reviewed - Annotation score: 4 out of 5- Protein inferred from homologyi

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 bindingi113 – 1131IronUniRule annotation
Metal bindingi117 – 1171IronUniRule annotation
Metal bindingi134 – 1341IronUniRule annotation
Binding sitei166 – 1661Threonylcarbamoyl-AMPUniRule annotation
Binding sitei179 – 1791Threonylcarbamoyl-AMP; via amide nitrogenUniRule annotation
Binding sitei183 – 1831Threonylcarbamoyl-AMPUniRule annotation
Binding sitei262 – 2621Threonylcarbamoyl-AMPUniRule annotation
Metal bindingi290 – 2901IronUniRule annotation
Binding sitei377 – 3771ATPUniRule annotation
Active sitei464 – 4641Proton acceptor; for kinase activityUniRule annotation

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi355 – 3639ATPUniRule 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

Enzyme and pathway databases

BioCyciMACE188937:GI2O-3748-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:2.6.99.4UniRule 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:MA_3705
OrganismiMethanosarcina acetivorans (strain ATCC 35395 / DSM 2834 / JCM 12185 / C2A)
Taxonomic identifieri188937 [NCBI]
Taxonomic lineageiArchaeaEuryarchaeotaMethanomicrobiaMethanosarcinalesMethanosarcinaceaeMethanosarcina
ProteomesiUP000002487: 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 – 547547Probable bifunctional tRNA threonylcarbamoyladenosine biosynthesis proteinPRO_0000303654Add
BLAST

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

STRINGi188937.MA3705.

Structurei

3D structure databases

ProteinModelPortaliQ8TJS2.
SMRiQ8TJS2. Positions 5-330.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini340 – 547208Protein kinaseUniRule annotationAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni1 – 329329Kae1Add
BLAST
Regioni134 – 1385Threonylcarbamoyl-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.
InParanoidiQ8TJS2.
KOiK15904.
OMAiRDNAGMI.
PhylomeDBiQ8TJS2.

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.
IPR000719. Prot_kinase_dom.
IPR018934. RIO-like_kinase.
IPR009220. tRNA_threonyl_synthase/kinase.
IPR008266. Tyr_kinase_AS.
[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.
PROSITEiPS50011. PROTEIN_KINASE_DOM. 1 hit.
PS00109. PROTEIN_KINASE_TYR. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q8TJS2-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MKNTFILGIE GTAWNLSAAI VTETEIIAEV TETYKPEVGG IHPREAAQHH
60 70 80 90 100
AKYAASVIKR LLAEAKEKGV EPSDLDGIAF SQGPGLGPCL RTIATAARML
110 120 130 140 150
SLSLDIPLIG VNHCIAHIEI GIWRTPARDP VVLYVSGANS QVISFMEGRY
160 170 180 190 200
RVFGETLDIG LGNALDKFAR RAGLPHPGGP KIEACAKDAK RYIPLPYVIK
210 220 230 240 250
GMDLSFSGLS TASSEALKKA SLEDVCYSYQ ETAFAMVVEV AERALAHTGK
260 270 280 290 300
NEVLLAGGVG ANTRLREMLN EMCEARGAKF YVPEKRFMGD NGTMIAYTGL
310 320 330 340 350
LMYKSGNTLT LEDSRVNPNF RTDDVNVTWI KEEEMKKVPE ISPEAFLRAP
360 370 380 390 400
PGERLDNGAE AVIYLDEGPE GKKVLVKERV PKLYRHKEID ERIRRERNRT
410 420 430 440 450
EARLISEARR AGVPTPIIYD IEEFKLKMQF IEGVPIKYLI TPELSEKVGE
460 470 480 490 500
LVGRLHSSGI VHGDLTTSNL LLAGERLYLI DFGLAYFDKS LEARGVDVHV
510 520 530 540
LFQTFESTHR GHETLVKAFE KGYGSTFIDS KDVLKRVEEI KKRARYA
Length:547
Mass (Da):60,639
Last modified:June 1, 2002 - v1
Checksum:iCE1798004A897139
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AE010299 Genomic DNA. Translation: AAM07060.1.
RefSeqiNP_618580.1. NC_003552.1.
WP_011023612.1. NC_003552.1.

Genome annotation databases

EnsemblBacteriaiAAM07060; AAM07060; MA_3705.
GeneIDi1475598.
KEGGimac:MA3705.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AE010299 Genomic DNA. Translation: AAM07060.1 .
RefSeqi NP_618580.1. NC_003552.1.
WP_011023612.1. NC_003552.1.

3D structure databases

ProteinModelPortali Q8TJS2.
SMRi Q8TJS2. Positions 5-330.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

STRINGi 188937.MA3705.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblBacteriai AAM07060 ; AAM07060 ; MA_3705 .
GeneIDi 1475598.
KEGGi mac:MA3705.

Phylogenomic databases

eggNOGi COG0533.
InParanoidi Q8TJS2.
KOi K15904.
OMAi RDNAGMI.
PhylomeDBi Q8TJS2.

Enzyme and pathway databases

BioCyci MACE188937:GI2O-3748-MONOMER.

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.
IPR000719. Prot_kinase_dom.
IPR018934. RIO-like_kinase.
IPR009220. tRNA_threonyl_synthase/kinase.
IPR008266. Tyr_kinase_AS.
[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.
PROSITEi PS50011. PROTEIN_KINASE_DOM. 1 hit.
PS00109. PROTEIN_KINASE_TYR. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

  1. "The genome of Methanosarcina acetivorans reveals extensive metabolic and physiological diversity."
    Galagan J.E., Nusbaum C., Roy A., Endrizzi M.G., Macdonald P., FitzHugh W., Calvo S., Engels R., Smirnov S., Atnoor D., Brown A., Allen N., Naylor J., Stange-Thomann N., DeArellano K., Johnson R., Linton L., McEwan P.
    , McKernan K., Talamas J., Tirrell A., Ye W., Zimmer A., Barber R.D., Cann I., Graham D.E., Grahame D.A., Guss A.M., Hedderich R., Ingram-Smith C., Kuettner H.C., Krzycki J.A., Leigh J.A., Li W., Liu J., Mukhopadhyay B., Reeve J.N., Smith K., Springer T.A., Umayam L.A., White O., White R.H., de Macario E.C., Ferry J.G., Jarrell K.F., Jing H., Macario A.J.L., Paulsen I.T., Pritchett M., Sowers K.R., Swanson R.V., Zinder S.H., Lander E., Metcalf W.W., Birren B.
    Genome Res. 12:532-542(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: ATCC 35395 / DSM 2834 / JCM 12185 / C2A.

Entry informationi

Entry nameiKAE1B_METAC
AccessioniPrimary (citable) accession number: Q8TJS2
Entry historyi
Integrated into UniProtKB/Swiss-Prot: September 11, 2007
Last sequence update: June 1, 2002
Last modified: October 29, 2014
This is version 90 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

Complete proteome, Multifunctional enzyme, Reference proteome

Documents

  1. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3