Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

Tyrosine--tRNA ligase

Gene

tyrS

Organism
Thermus thermophilus (strain HB27 / ATCC BAA-163 / DSM 7039)
Status
Reviewed-Annotation score: -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

Miscellaneous

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

Catalytic activityi

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

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Binding sitei235ATP1

GO - Molecular functioni

GO - Biological processi

Keywordsi

Molecular functionAminoacyl-tRNA synthetase, Ligase, RNA-binding
Biological processProtein biosynthesis
LigandATP-binding, Nucleotide-binding

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

Keywords - Cellular componenti

Cytoplasm

Pathology & Biotechi

Chemistry databases

DrugBankiDB03978 Tyrosinal

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00000556651 – 432Tyrosine--tRNA ligaseAdd BLAST432

Interactioni

Subunit structurei

Homodimer.

Protein-protein interaction databases

STRINGi262724.TTC1033

Structurei

Secondary structure

1432
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi8 – 16Combined sources9
Beta strandi20 – 23Combined sources4
Helixi25 – 33Combined sources9
Beta strandi39 – 44Combined sources6
Beta strandi47 – 49Combined sources3
Helixi53 – 67Combined sources15
Beta strandi71 – 76Combined sources6
Helixi80 – 83Combined sources4
Helixi102 – 112Combined sources11
Turni113 – 115Combined sources3
Turni120 – 122Combined sources3
Beta strandi123 – 127Combined sources5
Helixi129 – 132Combined sources4
Helixi137 – 144Combined sources8
Helixi149 – 152Combined sources4
Helixi156 – 163Combined sources8
Helixi170 – 173Combined sources4
Helixi175 – 186Combined sources12
Beta strandi189 – 194Combined sources6
Helixi195 – 197Combined sources3
Helixi198 – 210Combined sources13
Beta strandi217 – 221Combined sources5
Beta strandi229 – 232Combined sources4
Helixi235 – 237Combined sources3
Helixi247 – 255Combined sources9
Helixi259 – 261Combined sources3
Helixi262 – 269Combined sources8
Helixi274 – 283Combined sources10
Helixi285 – 301Combined sources17
Beta strandi302 – 304Combined sources3
Helixi311 – 316Combined sources6
Helixi321 – 323Combined sources3
Helixi333 – 345Combined sources13
Beta strandi356 – 359Combined sources4
Helixi361 – 363Combined sources3
Beta strandi368 – 370Combined sources3
Helixi371 – 377Combined sources7
Beta strandi380 – 383Combined sources4
Helixi384 – 392Combined sources9
Beta strandi396 – 398Combined sources3
Beta strandi409 – 411Combined sources3
Beta strandi416 – 420Combined sources5
Turni421 – 423Combined sources3
Beta strandi424 – 430Combined sources7

3D structure databases

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

Miscellaneous databases

EvolutionaryTraceiP83453

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini369 – 430S4 RNA-bindingUniRule annotationAdd BLAST62

Motif

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Motifi46 – 55"HIGH" region10
Motifi232 – 236"KMSKS" region5

Sequence similaritiesi

Belongs to the class-I aminoacyl-tRNA synthetase family. TyrS type 2 subfamily.UniRule annotation

Phylogenomic databases

eggNOGiENOG4105DA0 Bacteria
COG0162 LUCA
KOiK01866
OMAiVNYMMAK

Family and domain databases

CDDicd00165 S4, 1 hit
cd00805 TyrRS_core, 1 hit
Gene3Di3.10.290.10, 1 hit
3.40.50.620, 1 hit
HAMAPiMF_02007 Tyr_tRNA_synth_type2, 1 hit
InterProiView protein in InterPro
IPR002305 aa-tRNA-synth_Ic
IPR014729 Rossmann-like_a/b/a_fold
IPR002942 S4_RNA-bd
IPR036986 S4_RNA-bd_sf
IPR002307 Tyr-tRNA-ligase
IPR024088 Tyr-tRNA-ligase_bac-type
IPR024108 Tyr-tRNA-ligase_bac_2
PANTHERiPTHR11766 PTHR11766, 2 hits
PTHR11766:SF1 PTHR11766:SF1, 2 hits
PfamiView protein in Pfam
PF00579 tRNA-synt_1b, 1 hit
PRINTSiPR01040 TRNASYNTHTYR
TIGRFAMsiTIGR00234 tyrS, 1 hit
PROSITEiView protein in PROSITE
PS50889 S4, 1 hit

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:TT_C1033

Similar proteinsi

Entry informationi

Entry nameiSYY_THET2
AccessioniPrimary (citable) accession number: P83453
Entry historyiIntegrated into UniProtKB/Swiss-Prot: November 15, 2002
Last sequence update: November 15, 2002
Last modified: March 28, 2018
This is version 105 of the entry and version 1 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome
UniProt is an ELIXIR core data resource
Main funding by: National Institutes of Health