SYTM_RAT
ID SYTM_RAT Reviewed; 723 AA.
AC Q68FW7;
DT 31-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT 11-OCT-2004, sequence version 1.
DT 03-AUG-2022, entry version 120.
DE RecName: Full=Threonine--tRNA ligase, mitochondrial;
DE EC=6.1.1.3 {ECO:0000250|UniProtKB:Q9BW92};
DE AltName: Full=Threonyl-tRNA synthetase;
DE Short=ThrRS;
DE AltName: Full=Threonyl-tRNA synthetase-like 1;
DE Flags: Precursor;
GN Name=Tars2; Synonyms=Tarsl1;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Kidney;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
CC -!- FUNCTION: Catalyzes the attachment of threonine to tRNA(Thr) in a two-
CC step reaction: threonine is first activated by ATP to form Thr-AMP and
CC then transferred to the acceptor end of tRNA(Thr). Also edits
CC incorrectly charged tRNA(Thr) via its editing domain.
CC {ECO:0000250|UniProtKB:Q9BW92}.
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:0000250|UniProtKB:Q9BW92};
CC -!- SUBUNIT: Homodimer. {ECO:0000250|UniProtKB:Q9BW92}.
CC -!- SUBCELLULAR LOCATION: Mitochondrion matrix {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the class-II aminoacyl-tRNA synthetase family.
CC {ECO:0000305}.
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DR EMBL; BC079154; AAH79154.1; -; mRNA.
DR RefSeq; NP_001014062.1; NM_001014040.1.
DR RefSeq; XP_008759530.1; XM_008761308.2.
DR AlphaFoldDB; Q68FW7; -.
DR SMR; Q68FW7; -.
DR STRING; 10116.ENSRNOP00000044548; -.
DR iPTMnet; Q68FW7; -.
DR PhosphoSitePlus; Q68FW7; -.
DR jPOST; Q68FW7; -.
DR PaxDb; Q68FW7; -.
DR PRIDE; Q68FW7; -.
DR Ensembl; ENSRNOT00000087052; ENSRNOP00000072886; ENSRNOG00000057194.
DR GeneID; 310672; -.
DR KEGG; rno:310672; -.
DR UCSC; RGD:1308283; rat.
DR CTD; 80222; -.
DR RGD; 1308283; Tars2.
DR eggNOG; KOG1637; Eukaryota.
DR GeneTree; ENSGT00940000161600; -.
DR HOGENOM; CLU_008554_0_3_1; -.
DR InParanoid; Q68FW7; -.
DR OMA; PILEQTC; -.
DR OrthoDB; 813937at2759; -.
DR PhylomeDB; Q68FW7; -.
DR PRO; PR:Q68FW7; -.
DR Proteomes; UP000002494; Chromosome 2.
DR Bgee; ENSRNOG00000057194; Expressed in skeletal muscle tissue and 20 other tissues.
DR Genevisible; Q68FW7; RN.
DR GO; GO:0005759; C:mitochondrial matrix; IEA:UniProtKB-SubCell.
DR GO; GO:0002161; F:aminoacyl-tRNA editing activity; ISS:UniProtKB.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0042803; F:protein homodimerization activity; ISS:UniProtKB.
DR GO; GO:0004829; F:threonine-tRNA ligase activity; ISS:UniProtKB.
DR GO; GO:0006435; P:threonyl-tRNA aminoacylation; IBA:GO_Central.
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 2: Evidence at transcript level;
KW Aminoacyl-tRNA synthetase; ATP-binding; Ligase; Mitochondrion;
KW Nucleotide-binding; Phosphoprotein; Protein biosynthesis;
KW Reference proteome; Transit peptide.
FT TRANSIT 1..?
FT /note="Mitochondrion"
FT /evidence="ECO:0000255"
FT CHAIN ?..723
FT /note="Threonine--tRNA ligase, mitochondrial"
FT /id="PRO_0000254588"
FT DOMAIN 64..126
FT /note="TGS"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01228"
FT MOD_RES 57
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9BW92"
SQ SEQUENCE 723 AA; 81672 MW; 55D41FF833FCE14E CRC64;
MGLCLRWRRL GFPLPGFRRC ELHTVREAPI PTPPHWLAER FGLFEELWTA QVKRLASMTQ
KKARTIKISL PEGQKVDAVA WNTTPYQLAQ QISSTLADTA VAAEVNGELY DLDRPLETDC
HLRFLTFDSP EGKAVFWRSS AHVLGAAAEQ HLGAVLCRGP STESGFYLDF FLGKERTVRS
TELPTLERIC QEIITAAQPF RRLEASRGQL RQLFKDNHFK LHVIEEKVTG TTATVYGCGM
SVDLCQGPHL RHTGQIGALK LLTNSSALWR SSEAPETLQR VSGISFPKAE LLRNWEARRE
EAELRDHRRI GKEQELFFFH ELSPGSCFFL PRGTRIYNAL VAFIRAEYAR RGFSEVKTPT
LFSTKLWEQS GHWEHYRAHM FSLKPPGTDG VDSSQSGHPA RCPKDTLALK PMNCPAHCLM
FAHRPRSWRE LPVRLADFGV LHRAEASGSL GGLTRLWRFQ QDDAHIFCAP SQLEAEIRGC
LDFLRSVYSV LGFSFHLALS TRPPGFLGEP HLWDQAEKVL QQALEEFGEP WNLNPGDGAF
YGPKIDVHLH DALGRPHQCG TIQLDFQLPL RFDLQYKGPA GAPECPVLIH RAVLGSVERL
LGVLAESCGG RWPLWLSPFQ VVVIPVRTEQ EDYARQVQQC LQAAGLVSDL DADCGLTLSR
RVRRAQLAHY NFQFVVGQRE QSQMSVNVRT RDNRQLGERG LAESVQRLLE LQDARVPNAE
ELF
