SYT_THEKO
ID SYT_THEKO Reviewed; 626 AA.
AC Q5JGC8;
DT 30-AUG-2005, integrated into UniProtKB/Swiss-Prot.
DT 15-FEB-2005, sequence version 1.
DT 03-AUG-2022, entry version 107.
DE RecName: Full=Threonine--tRNA ligase {ECO:0000255|HAMAP-Rule:MF_00184};
DE EC=6.1.1.3 {ECO:0000255|HAMAP-Rule:MF_00184};
DE AltName: Full=Threonyl-tRNA synthetase {ECO:0000255|HAMAP-Rule:MF_00184};
DE Short=ThrRS {ECO:0000255|HAMAP-Rule:MF_00184};
GN Name=thrS {ECO:0000255|HAMAP-Rule:MF_00184}; OrderedLocusNames=TK1170;
OS Thermococcus kodakarensis (strain ATCC BAA-918 / JCM 12380 / KOD1)
OS (Pyrococcus kodakaraensis (strain KOD1)).
OC Archaea; Euryarchaeota; Thermococci; Thermococcales; Thermococcaceae;
OC Thermococcus.
OX NCBI_TaxID=69014;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-918 / JCM 12380 / KOD1;
RX PubMed=15710748; DOI=10.1101/gr.3003105;
RA Fukui T., Atomi H., Kanai T., Matsumi R., Fujiwara S., Imanaka T.;
RT "Complete genome sequence of the hyperthermophilic archaeon Thermococcus
RT kodakaraensis KOD1 and comparison with Pyrococcus genomes.";
RL Genome Res. 15:352-363(2005).
CC -!- FUNCTION: Catalyzes the attachment of threonine to tRNA(Thr) in a two-
CC step reaction: L-threonine is first activated by ATP to form Thr-AMP
CC and then transferred to the acceptor end of tRNA(Thr). Also edits
CC incorrectly charged L-seryl-tRNA(Thr). {ECO:0000255|HAMAP-
CC Rule:MF_00184}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + L-threonine + tRNA(Thr) = AMP + diphosphate + H(+) + L-
CC threonyl-tRNA(Thr); Xref=Rhea:RHEA:24624, Rhea:RHEA-COMP:9670,
CC Rhea:RHEA-COMP:9704, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:33019, ChEBI:CHEBI:57926, ChEBI:CHEBI:78442,
CC ChEBI:CHEBI:78534, ChEBI:CHEBI:456215; EC=6.1.1.3;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_00184};
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_00184};
CC Note=Binds 1 zinc ion per subunit. {ECO:0000255|HAMAP-Rule:MF_00184};
CC -!- SUBUNIT: Homodimer. {ECO:0000255|HAMAP-Rule:MF_00184}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00184}.
CC -!- DOMAIN: The N-terminal domain is an archaea-specific tRNA-editing
CC domain that hydrolyzes incorrectly charged L-seryl-tRNA(Thr). Catalysis
CC of tRNA editing is performed by the charged tRNA itself.
CC {ECO:0000255|HAMAP-Rule:MF_00184}.
CC -!- SIMILARITY: Belongs to the class-II aminoacyl-tRNA synthetase family.
CC {ECO:0000255|HAMAP-Rule:MF_00184}.
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DR EMBL; AP006878; BAD85359.1; -; Genomic_DNA.
DR RefSeq; WP_011250121.1; NC_006624.1.
DR AlphaFoldDB; Q5JGC8; -.
DR SMR; Q5JGC8; -.
DR STRING; 69014.TK1170; -.
DR PRIDE; Q5JGC8; -.
DR EnsemblBacteria; BAD85359; BAD85359; TK1170.
DR GeneID; 3235770; -.
DR KEGG; tko:TK1170; -.
DR PATRIC; fig|69014.16.peg.1145; -.
DR eggNOG; arCOG00401; Archaea.
DR HOGENOM; CLU_029833_0_0_2; -.
DR InParanoid; Q5JGC8; -.
DR OMA; DAHIFML; -.
DR OrthoDB; 11656at2157; -.
DR PhylomeDB; Q5JGC8; -.
DR Proteomes; UP000000536; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0002161; F:aminoacyl-tRNA editing activity; IEA:UniProt.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0004829; F:threonine-tRNA ligase activity; IBA:GO_Central.
DR GO; GO:0000049; F:tRNA binding; IEA:UniProtKB-KW.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0006435; P:threonyl-tRNA aminoacylation; IBA:GO_Central.
DR Gene3D; 3.30.930.10; -; 1.
DR Gene3D; 3.40.50.800; -; 1.
DR Gene3D; 3.50.80.10; -; 1.
DR HAMAP; MF_00184; Thr_tRNA_synth; 1.
DR InterPro; IPR002314; aa-tRNA-synt_IIb.
DR InterPro; IPR006195; aa-tRNA-synth_II.
DR InterPro; IPR045864; aa-tRNA-synth_II/BPL/LPL.
DR InterPro; IPR004154; Anticodon-bd.
DR InterPro; IPR036621; Anticodon-bd_dom_sf.
DR InterPro; IPR023509; DTD-like_sf.
DR InterPro; IPR002320; Thr-tRNA-ligase_IIa.
DR InterPro; IPR015011; Threonyl-tRNA_syn_edit_dom_arc.
DR PANTHER; PTHR11451; PTHR11451; 1.
DR Pfam; PF03129; HGTP_anticodon; 1.
DR Pfam; PF00587; tRNA-synt_2b; 1.
DR Pfam; PF08915; tRNA-Thr_ED; 1.
DR PRINTS; PR01047; TRNASYNTHTHR.
DR SUPFAM; SSF55681; SSF55681; 1.
DR TIGRFAMs; TIGR00418; thrS; 1.
DR PROSITE; PS50862; AA_TRNA_LIGASE_II; 1.
PE 3: Inferred from homology;
KW Aminoacyl-tRNA synthetase; ATP-binding; Cytoplasm; Ligase; Metal-binding;
KW Nucleotide-binding; Protein biosynthesis; Reference proteome; RNA-binding;
KW tRNA-binding; Zinc.
FT CHAIN 1..626
FT /note="Threonine--tRNA ligase"
FT /id="PRO_0000101111"
FT REGION 1..145
FT /note="Editing domain"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00184"
FT REGION 207..506
FT /note="Catalytic"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00184"
FT BINDING 299
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00184"
FT BINDING 351
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00184"
FT BINDING 475
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00184"
SQ SEQUENCE 626 AA; 73296 MW; 8B0D5176D50E0FC5 CRC64;
MRMLLIHSDY LEYEVKDKAL KNPEPISDEQ KTGRLDEVLA VFISVEKVDE TNPDEVVEKA
VKEIEDVASQ IKAERIFVYP FAHLSSELAK PDVALEVLRK IEEKLREKGY EVKRAPFGYY
KAFKLSCKGH PLAELSRTIV PEKAVSKEER NIALEKEEKE LKSYWYILTP EGELIDVDKF
DFTGHENLKK FVNYEIAKNR VADREPPHVR LMLEQELVDY EPGSDAGNLR YYPKGRLIKS
LLEQYVTEKV IEYGAMEVET PIMYDFEHPA LEKYLNRFPA RQYVVKSGDK KFFLRFAACF
GQFLIKKDAT ISYRNLPLRM YELTRYSFRR EKSGELSGLR RLRAFTMPDM HTVARDLKQA
MDEFKKQYKL SMEVLKGVGL TPEDYEVAIR FTRDFWEQNR DFIVELAKII GKPVLIEMWD
QRFFYFILKF EFNFVDNLDK AAALSTVQID VENAERFGIK YYDEEGKERT PLILHCSPSG
AIERVMYAIL EKQAKLQEKG IKPMYPLWLS PIQVRVIPVS DEVMDYALYV AGKLEGAKIR
VDVDDTGDRL NKKIRKAEKE WIPYIIVVGR NEKEQNTVTV RRRSDGRQVE MQLEDLIREI
KGQTEGFPYK PRPLPLLLSR RPKFRG
