SYT_THET8
ID SYT_THET8 Reviewed; 659 AA.
AC P56881; Q5SH55;
DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT 30-MAY-2000, sequence version 1.
DT 03-AUG-2022, entry version 132.
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=TTHA1875;
OS Thermus thermophilus (strain ATCC 27634 / DSM 579 / HB8).
OC Bacteria; Deinococcus-Thermus; Deinococci; Thermales; Thermaceae; Thermus.
OX NCBI_TaxID=300852;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=10632708; DOI=10.1046/j.1432-1327.2000.01011.x;
RA Cura V., Moras D., Kern D.;
RT "Sequence analysis and modular organization of threonyl-tRNA synthetase
RT from Thermus thermophilus and its interrelation with threonyl-tRNA
RT synthetases of other origins.";
RL Eur. J. Biochem. 267:379-393(2000).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 27634 / DSM 579 / HB8;
RA Masui R., Kurokawa K., Nakagawa N., Tokunaga F., Koyama Y., Shibata T.,
RA Oshima T., Yokoyama S., Yasunaga T., Kuramitsu S.;
RT "Complete genome sequence of Thermus thermophilus HB8.";
RL Submitted (NOV-2004) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP PROTEIN SEQUENCE OF 1-45, AND CHARACTERIZATION.
RX PubMed=8031907; DOI=10.1016/0300-9084(94)90065-5;
RA Zheltonosova J., Melnikova E., Garber M., Reinbolt J., Kern D.,
RA Ehresmann C., Ehresmann B.;
RT "Threonyl-tRNA synthetase from Thermus thermophilus: purification and some
RT structural and kinetic properties.";
RL Biochimie 76:71-77(1994).
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 C-terminal domain recognizes the anticodon bases.
CC -!- SIMILARITY: Belongs to the class-II aminoacyl-tRNA synthetase family.
CC {ECO:0000255|HAMAP-Rule:MF_00184}.
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DR EMBL; AJ250953; CAB65483.1; -; Genomic_DNA.
DR EMBL; AP008226; BAD71698.1; -; Genomic_DNA.
DR RefSeq; WP_011228977.1; NC_006461.1.
DR RefSeq; YP_145141.1; NC_006461.1.
DR AlphaFoldDB; P56881; -.
DR SMR; P56881; -.
DR STRING; 300852.55773257; -.
DR EnsemblBacteria; BAD71698; BAD71698; BAD71698.
DR GeneID; 3168147; -.
DR KEGG; ttj:TTHA1875; -.
DR PATRIC; fig|300852.9.peg.1842; -.
DR eggNOG; COG0441; Bacteria.
DR HOGENOM; CLU_008554_0_1_0; -.
DR OMA; FYYDFAY; -.
DR PhylomeDB; P56881; -.
DR Proteomes; UP000000532; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0004829; F:threonine-tRNA ligase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0000049; F:tRNA binding; IEA:UniProtKB-KW.
DR GO; GO:0006435; P:threonyl-tRNA aminoacylation; IEA:UniProtKB-UniRule.
DR CDD; cd00771; ThrRS_core; 1.
DR Gene3D; 3.10.20.30; -; 1.
DR Gene3D; 3.30.930.10; -; 1.
DR Gene3D; 3.40.50.800; -; 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; IPR012675; Beta-grasp_dom_sf.
DR InterPro; IPR004095; TGS.
DR InterPro; IPR012676; TGS-like.
DR InterPro; IPR002320; Thr-tRNA-ligase_IIa.
DR InterPro; IPR018163; Thr/Ala-tRNA-synth_IIc_edit.
DR InterPro; IPR033728; ThrRS_core.
DR InterPro; IPR012947; tRNA_SAD.
DR PANTHER; PTHR11451; PTHR11451; 1.
DR Pfam; PF03129; HGTP_anticodon; 1.
DR Pfam; PF02824; TGS; 1.
DR Pfam; PF00587; tRNA-synt_2b; 1.
DR Pfam; PF07973; tRNA_SAD; 1.
DR PRINTS; PR01047; TRNASYNTHTHR.
DR SMART; SM00863; tRNA_SAD; 1.
DR SUPFAM; SSF55186; SSF55186; 1.
DR SUPFAM; SSF55681; SSF55681; 1.
DR SUPFAM; SSF81271; SSF81271; 1.
DR TIGRFAMs; TIGR00418; thrS; 1.
DR PROSITE; PS50862; AA_TRNA_LIGASE_II; 1.
DR PROSITE; PS51880; TGS; 1.
PE 1: Evidence at protein level;
KW Aminoacyl-tRNA synthetase; ATP-binding; Cytoplasm;
KW Direct protein sequencing; Ligase; Metal-binding; Nucleotide-binding;
KW Protein biosynthesis; Reference proteome; RNA-binding; tRNA-binding; Zinc.
FT CHAIN 1..659
FT /note="Threonine--tRNA ligase"
FT /id="PRO_0000101075"
FT DOMAIN 1..60
FT /note="TGS"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01228"
FT REGION 234..548
FT /note="Catalytic"
FT REGION 252..552
FT /note="Catalytic"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00184"
FT BINDING 349
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00184"
FT BINDING 400
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00184"
FT BINDING 529
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00184"
FT CONFLICT 42
FT /note="E -> T (in Ref. 3; AA sequence)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 659 AA; 75537 MW; 1993A1BEF1151FF4 CRC64;
MTVYLPDGKP LELPEGATAK DVARALGEGW ERRAVGAIVD GELYDLLKPL PQGAKVRLLT
EKDPEFQTLF RHTLAHVLAQ AVKEFFREKG YDPESVRLGV GPVIEKGFYY DIEAPEPLSD
EDLPAIEAKM REILKRDLPL RRFVLSREEA LARYRGKDPY KTELVLEIPE GEEISFYQQG
DEAYGFTDLC RGPHVPSTGR IPPHFKLTHV AGAYWRGDEN RPMLQRVYGV AFRTAEELKE
YLWQLEEAKK RDHRRLGREL ELFLIDPLVG KGLVLWLPKG NVVREELMAF MREEQVRRGY
QLVTTPHIGS LELYKTSGHY PYYAESQFPP ISFKERGEEE EYLLKPMNCP HHIRIYAYRK
RSYRELPLRL AEFGTVYRYE KAGELLGLTR VRGFTQDDAH IFCTPEEVKG EFLGVLDLVL
KVFATLGLKD YRARIGVRDP KSDKYVGDEA KWALAERQIE EAAAEAGLRY TVEEGDAAFY
GPKLDFVVKD ALGREWQLGT IQVDYNLPER FGLTYVGKDG EEHRPVMLHR APFGSLERFI
GILIEHFAGD FPLWLAPVQA VVVPVSEKQE DYAREVAGRL KEAGLRAEAD TRPERMQARI
RDAEVQKVPY ILVVGEREKA EGAVSVRRRK KGNLGTMPLA AFLEGALREY RERRLEPVF
