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

Threonine--tRNA ligase

Gene

thrS

Organism
Shigella flexneri
Status
Reviewed-Annotation score: -Protein inferred from homologyi

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 annotationNote: Binds 1 zinc ion per subunit.UniRule annotation

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Metal bindingi334ZincUniRule annotation1
Metal bindingi385Zinc; via tele nitrogenUniRule annotation1
Metal bindingi511Zinc; via pros nitrogenUniRule annotation1

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

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:SF1512, S1630
OrganismiShigella flexneri
Taxonomic identifieri623 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacteralesEnterobacteriaceaeShigella
Proteomesi
  • UP000002673 Componenti: Chromosome
  • UP000001006 Componenti: Chromosome

Subcellular locationi

  • Cytoplasm UniRule annotation

GO - Cellular componenti

Keywords - Cellular componenti

Cytoplasm

Pathology & Biotechi

Chemistry databases

DrugBankiDB03869 5'-O-(N-(L-Seryl)-Sulfamoyl)Adenosine
DB03355 5'-O-(N-(L-Threonyl)-Sulfamoyl)Adenosine
DB04024 N'-L-Seryl-3'-Amino-(3'-Deoxy)-Adenosine

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00001010451 – 642Threonine--tRNA ligaseAdd BLAST642

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei286N6-acetyllysineUniRule annotation1

Keywords - PTMi

Acetylation

Interactioni

Subunit structurei

Homodimer.UniRule annotation

Structurei

3D structure databases

ProteinModelPortaliP0A8M5
SMRiP0A8M5
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni243 – 534CatalyticUniRule annotationAdd BLAST292

Sequence similaritiesi

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

Phylogenomic databases

eggNOGiENOG4105C22 Bacteria
COG0441 LUCA
HOGENOMiHOG000003880
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
SUPFAMiSSF55186 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.

P0A8M5-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MPVITLPDGS QRHYDHAVSP MDVALDIGPG LAKACIAGRV NGELVDACDL
60 70 80 90 100
IENDAQLSII TAKDEEGLEI IRHSCAHLLG HAIKQLWPHT KMAIGPVIDN
110 120 130 140 150
GFYYDVDLDR TLTQEDVEAL EKRMHELAEK NYDVIKKKVS WHEARETFAN
160 170 180 190 200
RGESYKVSIL DENIAHDDKP GLYFHEEYVD MCRGPHVPNM RFCHHFKLMK
210 220 230 240 250
TAGAYWRGDS NNKMLQRIYG TAWADKKALN AYLQRLEEAA KRDHRKIGKQ
260 270 280 290 300
LDLYHMQEEA PGMVFWHNDG WTIFRELEVF VRSKLKEYQY QEVKGPFMMD
310 320 330 340 350
RVLWEKTGHW DNYKDAMFTT SSENREYCIK PMNCPGHVQI FNQGLKSYRD
360 370 380 390 400
LPLRMAEFGS CHRNEPSGSL HGLMRVRGFT QDDAHIFCTE EQIRDEVNGC
410 420 430 440 450
IRLVYDMYST FGFEKIVVKL STRPEKRIGS DEMWDRAEAD LAVALEENNI
460 470 480 490 500
PFEYQLGEGA FYGPKIEFTL YDCLDRAWQC GTVQLDFSLP SRLSASYVGE
510 520 530 540 550
DNERKVPVMI HRAILGSMER FIGILTEEFA GFFPTWLAPV QVVIMNITDS
560 570 580 590 600
QSEYVNELTQ KLSNAGIRVK ADLRNEKIGF KIREHTLRRV PYMLVCGDKE
610 620 630 640
VESGKVAVRT RRGKDLGSMD VNEVIEKLQQ EIRSRSLKQL EE
Length:642
Mass (Da):74,014
Last modified:June 7, 2005 - v1
Checksum:i38D8913B19CDAB7B
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AE005674 Genomic DNA Translation: AAN43102.1
AE014073 Genomic DNA Translation: AAP16992.1
RefSeqiNP_707395.1, NC_004337.2
WP_001144202.1, NZ_NIYR01000095.1

Genome annotation databases

EnsemblBacteriaiAAN43102; AAN43102; SF1512
AAP16992; AAP16992; S1630
GeneIDi1023405
KEGGisfl:SF1512
sfx:S1630
PATRICifig|198214.7.peg.1788

Similar proteinsi

Entry informationi

Entry nameiSYT_SHIFL
AccessioniPrimary (citable) accession number: P0A8M5
Secondary accession number(s): P00955, P78166, P78241
Entry historyiIntegrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: June 7, 2005
Last modified: May 23, 2018
This is version 103 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

Complete proteome, Reference proteome

Documents

  1. Aminoacyl-tRNA synthetases
    List of aminoacyl-tRNA synthetase entries
  2. SIMILARITY comments
    Index of protein domains and families

Cookie policy

We would like to use anonymized google analytics cookies to gather statistics on how uniprot.org is used in aggregate. Learn more

UniProt is an ELIXIR core data resource
Main funding by: National Institutes of Health