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Protein

Threonine--tRNA ligase

Gene

thrS

Organism
Staphylococcus aureus (strain MW2)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Catalyzes the attachment of threonine to tRNA(Thr) in a two-step reaction: L-threonine is first activated by ATP to form Thr-AMP and then transferred to the acceptor end of tRNA(Thr). Also edits incorrectly charged L-seryl-tRNA(Thr).UniRule annotation

Catalytic activityi

ATP + L-threonine + tRNA(Thr) = AMP + diphosphate + L-threonyl-tRNA(Thr).UniRule annotation

Cofactori

Zn2+UniRule annotation1 PublicationNote: Binds 1 zinc ion per subunit.UniRule annotation1 Publication

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Metal bindingi336ZincUniRule annotation1 Publication1
Binding sitei365ATP1 Publication1
Binding sitei365L-threonine1 Publication1
Metal bindingi387Zinc; via tele nitrogenUniRule annotation1 Publication1
Binding sitei468L-threonine1 Publication1
Binding sitei471ATP1 Publication1
Metal bindingi517Zinc; via pros nitrogenUniRule annotation1 Publication1
Binding sitei522ATP1 Publication1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Nucleotide bindingi377 – 378ATP1 Publication2
Nucleotide bindingi485 – 486ATP1 Publication2

GO - Molecular functioni

GO - Biological processi

Keywordsi

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

Enzyme and pathway databases

BRENDAi6.1.1.3. 3352.

Names & Taxonomyi

Protein namesi
Recommended name:
Threonine--tRNA ligaseUniRule annotation (EC:6.1.1.3UniRule annotation)
Alternative name(s):
Threonyl-tRNA synthetaseUniRule annotation
Short name:
ThrRSUniRule annotation
Gene namesi
Name:thrSUniRule annotation
Ordered Locus Names:MW1626
OrganismiStaphylococcus aureus (strain MW2)
Taxonomic identifieri196620 [NCBI]
Taxonomic lineageiBacteriaFirmicutesBacilliBacillalesStaphylococcaceaeStaphylococcus
Proteomesi
  • UP000000418 Componenti: Chromosome

Subcellular locationi

  • Cytoplasm UniRule annotation

GO - Cellular componenti

Keywords - Cellular componenti

Cytoplasm

Pathology & Biotechi

Chemistry databases

DrugBankiDB03355. 5'-O-(N-(L-Threonyl)-Sulfamoyl)Adenosine.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00001010521 – 645Threonine--tRNA ligaseAdd BLAST645

Proteomic databases

PRIDEiQ8NW68.

Interactioni

Subunit structurei

Homodimer.UniRule annotation1 Publication

Structurei

Secondary structure

1645
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi9 – 11Combined sources3
Beta strandi18 – 20Combined sources3
Helixi22 – 27Combined sources6
Helixi31 – 36Combined sources6
Beta strandi39 – 42Combined sources4
Beta strandi45 – 47Combined sources3
Beta strandi58 – 62Combined sources5
Helixi67 – 88Combined sources22
Beta strandi89 – 91Combined sources3
Beta strandi103 – 109Combined sources7
Turni116 – 118Combined sources3
Helixi119 – 131Combined sources13
Beta strandi136 – 140Combined sources5
Turni142 – 144Combined sources3
Helixi145 – 149Combined sources5
Helixi154 – 160Combined sources7
Beta strandi164 – 166Combined sources3
Beta strandi170 – 174Combined sources5
Beta strandi177 – 180Combined sources4
Helixi189 – 191Combined sources3
Beta strandi194 – 204Combined sources11
Beta strandi209 – 211Combined sources3
Beta strandi213 – 224Combined sources12
Helixi225 – 240Combined sources16
Helixi243 – 249Combined sources7
Beta strandi253 – 256Combined sources4
Turni257 – 259Combined sources3
Beta strandi260 – 266Combined sources7
Helixi268 – 287Combined sources20
Beta strandi290 – 292Combined sources3
Beta strandi297 – 300Combined sources4
Helixi302 – 307Combined sources6
Helixi309 – 312Combined sources4
Beta strandi321 – 323Combined sources3
Turni324 – 326Combined sources3
Beta strandi327 – 331Combined sources5
Beta strandi333 – 335Combined sources3
Helixi336 – 344Combined sources9
Helixi350 – 352Combined sources3
Beta strandi355 – 364Combined sources10
Turni369 – 371Combined sources3
Turni374 – 376Combined sources3
Beta strandi379 – 390Combined sources12
Helixi392 – 394Combined sources3
Helixi395 – 412Combined sources18
Beta strandi418 – 424Combined sources7
Beta strandi430 – 434Combined sources5
Helixi437 – 454Combined sources18
Beta strandi461 – 463Combined sources3
Beta strandi471 – 476Combined sources6
Beta strandi484 – 494Combined sources11
Helixi495 – 498Combined sources4
Beta strandi506 – 508Combined sources3
Beta strandi514 – 523Combined sources10
Helixi524 – 535Combined sources12
Turni541 – 543Combined sources3
Beta strandi548 – 554Combined sources7
Helixi555 – 570Combined sources16
Turni571 – 573Combined sources3
Beta strandi576 – 578Combined sources3
Helixi585 – 595Combined sources11
Beta strandi598 – 603Combined sources6
Helixi605 – 609Combined sources5
Beta strandi612 – 617Combined sources6
Beta strandi625 – 627Combined sources3
Helixi628 – 640Combined sources13

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1NYQX-ray3.20A/B1-645[»]
1NYRX-ray2.80A/B1-645[»]
ProteinModelPortaliQ8NW68.
SMRiQ8NW68.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ8NW68.

Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni1 – 62N1 domain1 PublicationAdd BLAST62
Regioni63 – 223N2 domain1 PublicationAdd BLAST161
Regioni242 – 540Catalytic1 PublicationAdd BLAST299
Regioni541 – 645Anticodon recognition1 PublicationAdd BLAST105

Domaini

The protein structure shows 2 N-terminal domains, the central catalytic and C-terminal anticodon recognition domain. Comparison with the E.coli structure shows the N-terminal domains (editing region) are quite flexible with respect to the catalytic domain. The C-terminal domain recognizes the anticodon region of the tRNA while the acceptor arm is sandwiched between the N-terminal domains and the catalytic domain (PubMed:12875846).1 Publication

Sequence similaritiesi

Belongs to the class-II aminoacyl-tRNA synthetase family.UniRule annotation

Phylogenomic databases

HOGENOMiHOG000003879.
KOiK01868.
OMAiFYYDFAY.

Family and domain databases

CDDicd00771. ThrRS_core. 1 hit.
Gene3Di3.10.20.30. 1 hit.
3.40.50.800. 1 hit.
HAMAPiMF_00184. Thr_tRNA_synth. 1 hit.
InterProiView protein in InterPro
IPR002314. aa-tRNA-synt_IIb.
IPR006195. aa-tRNA-synth_II.
IPR004154. Anticodon-bd.
IPR036621. Anticodon-bd_dom_sf.
IPR012675. Beta-grasp_dom_sf.
IPR004095. TGS.
IPR012676. TGS-like.
IPR002320. Thr-tRNA-ligase_IIa.
IPR018163. Thr/Ala-tRNA-synth_IIc_edit.
IPR033728. ThrRS_core.
IPR012947. tRNA_SAD.
PANTHERiPTHR11451. PTHR11451. 1 hit.
PfamiView protein in Pfam
PF03129. HGTP_anticodon. 1 hit.
PF02824. TGS. 1 hit.
PF00587. tRNA-synt_2b. 1 hit.
PF07973. tRNA_SAD. 1 hit.
PRINTSiPR01047. TRNASYNTHTHR.
SMARTiView protein in SMART
SM00863. tRNA_SAD. 1 hit.
SUPFAMiSSF52954. SSF52954. 1 hit.
SSF55186. SSF55186. 1 hit.
SSF81271. SSF81271. 1 hit.
TIGRFAMsiTIGR00418. thrS. 1 hit.
PROSITEiView protein in PROSITE
PS50862. AA_TRNA_LIGASE_II. 1 hit.

Sequencei

Sequence statusi: Complete.

Q8NW68-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MEQINIQFPD GNKKAFDKGT TTEDIAQSIS PGLRKKAVAG KFNGQLVDLT
60 70 80 90 100
KPLETDGSIE IVTPGSEEAL EVLRHSTAHL MAHAIKRLYG NVKFGVGPVI
110 120 130 140 150
EGGFYYDFDI DQNISSDDFE QIEKTMKQIV NENMKIERKV VSRDEAKELF
160 170 180 190 200
SNDEYKLELI DAIPEDENVT LYSQGDFTDL CRGVHVPSTA KIKEFKLLST
210 220 230 240 250
AGAYWRGDSN NKMLQRIYGT AFFDKKELKA HLQMLEERKE RDHRKIGKEL
260 270 280 290 300
ELFTNSQLVG AGLPLWLPNG ATIRREIERY IVDKEVSMGY DHVYTPVLAN
310 320 330 340 350
VDLYKTSGHW DHYQEDMFPP MQLDETESMV LRPMNCPHHM MIYANKPHSY
360 370 380 390 400
RELPIRIAEL GTMHRYEASG AVSGLQRVRG MTLNDSHIFV RPDQIKEEFK
410 420 430 440 450
RVVNMIIDVY KDFGFEDYSF RLSYRDPEDK EKYFDDDDMW NKAENMLKEA
460 470 480 490 500
ADELGLSYEE AIGEAAFYGP KLDVQVKTAM GKEETLSTAQ LDFLLPERFD
510 520 530 540 550
LTYIGQDGEH HRPVVIHRGV VSTMERFVAF LTEETKGAFP TWLAPKQVQI
560 570 580 590 600
IPVNVDLHYD YARQLQDELK SQGVRVSIDD RNEKMGYKIR EAQMQKIPYQ
610 620 630 640
IVVGDKEVEN NQVNVRQYGS QDQETVEKDE FIWNLVDEIR LKKHR
Length:645
Mass (Da):74,460
Last modified:October 1, 2002 - v1
Checksum:i18FF7CFC22892FBA
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
BA000033 Genomic DNA. Translation: BAB95491.1.
RefSeqiWP_000435132.1. NC_003923.1.

Genome annotation databases

EnsemblBacteriaiBAB95491; BAB95491; BAB95491.
GeneIDi31214585.
KEGGisam:MW1626.

Similar proteinsi

Entry informationi

Entry nameiSYT_STAAW
AccessioniPrimary (citable) accession number: Q8NW68
Entry historyiIntegrated into UniProtKB/Swiss-Prot: October 31, 2003
Last sequence update: October 1, 2002
Last modified: November 22, 2017
This is version 110 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

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