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Protein

Tyrosine--tRNA ligase

Gene

tyrS

Organism
Thermus thermophilus (strain HB27 / ATCC BAA-163 / DSM 7039)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Experimental evidence at protein leveli

Functioni

Catalyzes the attachment of tyrosine to tRNA(Tyr) in a two-step reaction: tyrosine is first activated by ATP to form Tyr-AMP and then transferred to the acceptor end of tRNA(Tyr).UniRule annotation

Catalytic activityi

ATP + L-tyrosine + tRNA(Tyr) = AMP + diphosphate + L-tyrosyl-tRNA(Tyr).UniRule annotation

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei235 – 2351ATP

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Aminoacyl-tRNA synthetase, Ligase

Keywords - Biological processi

Protein biosynthesis

Keywords - Ligandi

ATP-binding, Nucleotide-binding, RNA-binding

Enzyme and pathway databases

BioCyciTTHE262724:GCAT-1045-MONOMER.

Names & Taxonomyi

Protein namesi
Recommended name:
Tyrosine--tRNA ligaseUniRule annotation (EC:6.1.1.1UniRule annotation)
Alternative name(s):
Tyrosyl-tRNA synthetaseUniRule annotation
Short name:
TyrRSUniRule annotation
Gene namesi
Name:tyrSUniRule annotation
Ordered Locus Names:TT_C1033
OrganismiThermus thermophilus (strain HB27 / ATCC BAA-163 / DSM 7039)
Taxonomic identifieri262724 [NCBI]
Taxonomic lineageiBacteriaDeinococcus-ThermusDeinococciThermalesThermaceaeThermus
Proteomesi
  • UP000000592 Componenti: Chromosome

Subcellular locationi

  • Cytoplasm UniRule annotation

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 432432Tyrosine--tRNA ligasePRO_0000055665Add
BLAST

Interactioni

Subunit structurei

Homodimer.

Protein-protein interaction databases

STRINGi262724.TTC1033.

Structurei

Secondary structure

1
432
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi8 – 169Combined sources
Beta strandi20 – 234Combined sources
Helixi25 – 339Combined sources
Beta strandi39 – 446Combined sources
Beta strandi47 – 493Combined sources
Helixi53 – 6715Combined sources
Beta strandi71 – 766Combined sources
Helixi80 – 834Combined sources
Helixi102 – 11211Combined sources
Turni113 – 1153Combined sources
Turni120 – 1223Combined sources
Beta strandi123 – 1275Combined sources
Helixi129 – 1324Combined sources
Helixi137 – 1448Combined sources
Helixi149 – 1524Combined sources
Helixi156 – 1638Combined sources
Helixi170 – 1734Combined sources
Helixi175 – 18612Combined sources
Beta strandi189 – 1946Combined sources
Helixi195 – 1973Combined sources
Helixi198 – 21013Combined sources
Beta strandi217 – 2215Combined sources
Beta strandi229 – 2324Combined sources
Helixi235 – 2373Combined sources
Helixi247 – 2559Combined sources
Helixi259 – 2613Combined sources
Helixi262 – 2698Combined sources
Helixi274 – 28310Combined sources
Helixi285 – 30117Combined sources
Beta strandi302 – 3043Combined sources
Helixi311 – 3166Combined sources
Helixi321 – 3233Combined sources
Helixi333 – 34513Combined sources
Beta strandi356 – 3594Combined sources
Helixi361 – 3633Combined sources
Beta strandi368 – 3703Combined sources
Helixi371 – 3777Combined sources
Beta strandi380 – 3834Combined sources
Helixi384 – 3929Combined sources
Beta strandi396 – 3983Combined sources
Beta strandi409 – 4113Combined sources
Beta strandi416 – 4205Combined sources
Turni421 – 4233Combined sources
Beta strandi424 – 4307Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1H3EX-ray2.90A1-432[»]
1H3FX-ray2.00A/B1-432[»]
ProteinModelPortaliP83453.
SMRiP83453. Positions 6-432.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP83453.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini369 – 43062S4 RNA-bindingUniRule annotationAdd
BLAST

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi46 – 5510"HIGH" region
Motifi232 – 2365"KMSKS" region

Sequence similaritiesi

Belongs to the class-I aminoacyl-tRNA synthetase family. TyrS type 2 subfamily.UniRule annotation
Contains 1 S4 RNA-binding domain.UniRule annotation

Phylogenomic databases

eggNOGiENOG4105DA0. Bacteria.
COG0162. LUCA.
KOiK01866.
OMAiRIAMQKP.
OrthoDBiEOG6B09VR.

Family and domain databases

Gene3Di3.10.290.10. 1 hit.
3.40.50.620. 1 hit.
HAMAPiMF_02007. Tyr_tRNA_synth_type2.
InterProiIPR002305. aa-tRNA-synth_Ic.
IPR014729. Rossmann-like_a/b/a_fold.
IPR002942. S4_RNA-bd.
IPR002307. Tyr-tRNA-ligase.
IPR024088. Tyr-tRNA-ligase_bac-type.
IPR024108. Tyr-tRNA-ligase_bac_2.
[Graphical view]
PANTHERiPTHR11766. PTHR11766. 2 hits.
PfamiPF00579. tRNA-synt_1b. 1 hit.
[Graphical view]
PRINTSiPR01040. TRNASYNTHTYR.
TIGRFAMsiTIGR00234. tyrS. 1 hit.
PROSITEiPS50889. S4. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P83453-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MAGTGHTPEE ALALLKRGAE EIVPEEELLA KLKEGRPLTV KLGADPTRPD
60 70 80 90 100
LHLGHAVVLR KMRQFQELGH KVVLIIGDFT GMIGDPSGRS KTRPPLTLEE
110 120 130 140 150
TRENAKTYVA QAGKILRQEP HLFELRYNSE WLEGLTFKEV VRLTSLMTVA
160 170 180 190 200
QMLEREDFKK RYEAGIPISL HELLYPFAQA YDSVAIRADV EMGGTDQRFN
210 220 230 240 250
LLVGREVQRA YGQSPQVCFL MPLLVGLDGR EKMSKSLDNY IGLTEPPEAM
260 270 280 290 300
FKKLMRVPDP LLPSYFRLLT DLEEEEIEAL LKAGPVPAHR VLARLLTAAY
310 320 330 340 350
ALPQIPPRID RAFYESLGYA WEAFGRDKEA GPEEVRRAEA RYDEVAKGGI
360 370 380 390 400
PEEIPEVTIP ASELKEGRIW VARLFTLAGL TPSNAEARRL IQNRGLRLDG
410 420 430
EVLTDPMLQV DLSRPRILQR GKDRFVRVRL SD
Length:432
Mass (Da):48,718
Last modified:November 15, 2002 - v1
Checksum:i71B04B8976B8D91B
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AE017221 Genomic DNA. Translation: AAS81375.1.
RefSeqiWP_011173450.1. NC_005835.1.

Genome annotation databases

EnsemblBacteriaiAAS81375; AAS81375; TT_C1033.
KEGGitth:TTC1033.
PATRICi23952467. VBITheThe54392_1024.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AE017221 Genomic DNA. Translation: AAS81375.1.
RefSeqiWP_011173450.1. NC_005835.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1H3EX-ray2.90A1-432[»]
1H3FX-ray2.00A/B1-432[»]
ProteinModelPortaliP83453.
SMRiP83453. Positions 6-432.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi262724.TTC1033.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAS81375; AAS81375; TT_C1033.
KEGGitth:TTC1033.
PATRICi23952467. VBITheThe54392_1024.

Phylogenomic databases

eggNOGiENOG4105DA0. Bacteria.
COG0162. LUCA.
KOiK01866.
OMAiRIAMQKP.
OrthoDBiEOG6B09VR.

Enzyme and pathway databases

BioCyciTTHE262724:GCAT-1045-MONOMER.

Miscellaneous databases

EvolutionaryTraceiP83453.

Family and domain databases

Gene3Di3.10.290.10. 1 hit.
3.40.50.620. 1 hit.
HAMAPiMF_02007. Tyr_tRNA_synth_type2.
InterProiIPR002305. aa-tRNA-synth_Ic.
IPR014729. Rossmann-like_a/b/a_fold.
IPR002942. S4_RNA-bd.
IPR002307. Tyr-tRNA-ligase.
IPR024088. Tyr-tRNA-ligase_bac-type.
IPR024108. Tyr-tRNA-ligase_bac_2.
[Graphical view]
PANTHERiPTHR11766. PTHR11766. 2 hits.
PfamiPF00579. tRNA-synt_1b. 1 hit.
[Graphical view]
PRINTSiPR01040. TRNASYNTHTYR.
TIGRFAMsiTIGR00234. tyrS. 1 hit.
PROSITEiPS50889. S4. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: HB27 / ATCC BAA-163 / DSM 7039.
  2. "Class I tyrosyl-tRNA synthetase has a class II mode of cognate tRNA recognition."
    Yaremchuk A., Kriklivyi I., Tukalo M., Cusack S.
    EMBO J. 21:3829-3840(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS).

Entry informationi

Entry nameiSYY_THET2
AccessioniPrimary (citable) accession number: P83453
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 15, 2002
Last sequence update: November 15, 2002
Last modified: May 11, 2016
This is version 94 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Miscellaneous

Although this protein is a class I aminoacyl-tRNA synthetase, it displays a class II mode of tRNA recognition.

Keywords - Technical termi

3D-structure, Complete proteome

Documents

  1. Aminoacyl-tRNA synthetases
    List of aminoacyl-tRNA synthetase entries
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. 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.