SYTC_RAT
ID SYTC_RAT Reviewed; 695 AA.
AC Q5XHY5;
DT 15-FEB-2005, integrated into UniProtKB/Swiss-Prot.
DT 23-NOV-2004, sequence version 1.
DT 03-AUG-2022, entry version 127.
DE RecName: Full=Threonine--tRNA ligase 1, cytoplasmic;
DE EC=6.1.1.3 {ECO:0000250|UniProtKB:Q9D0R2};
DE AltName: Full=Threonine--tRNA ligase, cytoplasmic;
DE AltName: Full=Threonyl-tRNA synthetase;
DE Short=ThrRS;
DE AltName: Full=Threonyl-tRNA synthetase 1;
GN Name=Tars1; Synonyms=Tars;
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=Testis;
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).
RN [2]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-270, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22673903; DOI=10.1038/ncomms1871;
RA Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., Lundby C.,
RA Olsen J.V.;
RT "Quantitative maps of protein phosphorylation sites across 14 different rat
RT organs and tissues.";
RL Nat. Commun. 3:876-876(2012).
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, at the post-
CC transfer stage. {ECO:0000250|UniProtKB:Q9D0R2}.
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:Q9D0R2};
CC -!- SUBUNIT: Homodimer. {ECO:0000250|UniProtKB:P26639}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q9D0R2}.
CC -!- PTM: ISGylated. {ECO:0000250|UniProtKB:P26639}.
CC -!- SIMILARITY: Belongs to the class-II aminoacyl-tRNA synthetase family.
CC {ECO:0000305}.
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DR EMBL; BC083914; AAH83914.1; -; mRNA.
DR RefSeq; NP_001006977.1; NM_001006976.1.
DR AlphaFoldDB; Q5XHY5; -.
DR SMR; Q5XHY5; -.
DR BioGRID; 254808; 1.
DR STRING; 10116.ENSRNOP00000044467; -.
DR iPTMnet; Q5XHY5; -.
DR PhosphoSitePlus; Q5XHY5; -.
DR jPOST; Q5XHY5; -.
DR PaxDb; Q5XHY5; -.
DR PRIDE; Q5XHY5; -.
DR Ensembl; ENSRNOT00000051910; ENSRNOP00000044467; ENSRNOG00000019023.
DR GeneID; 294810; -.
DR KEGG; rno:294810; -.
DR CTD; 6897; -.
DR RGD; 1359527; Tars1.
DR eggNOG; KOG1637; Eukaryota.
DR GeneTree; ENSGT00940000154969; -.
DR HOGENOM; CLU_008554_0_1_1; -.
DR InParanoid; Q5XHY5; -.
DR PRO; PR:Q5XHY5; -.
DR Proteomes; UP000002494; Chromosome 2.
DR Bgee; ENSRNOG00000019023; Expressed in liver and 20 other tissues.
DR ExpressionAtlas; Q5XHY5; baseline and differential.
DR Genevisible; Q5XHY5; RN.
DR GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR GO; GO:0005524; F:ATP binding; ISO:RGD.
DR GO; GO:0042802; F:identical protein binding; ISO:RGD.
DR GO; GO:0004829; F:threonine-tRNA ligase activity; ISS:UniProtKB.
DR GO; GO:0008270; F:zinc ion binding; ISO:RGD.
DR GO; GO:0006435; P:threonyl-tRNA aminoacylation; ISS:UniProtKB.
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 Acetylation; Aminoacyl-tRNA synthetase; ATP-binding; Cytoplasm; Ligase;
KW Nucleotide-binding; Phosphoprotein; Protein biosynthesis;
KW Reference proteome; Ubl conjugation.
FT CHAIN 1..695
FT /note="Threonine--tRNA ligase 1, cytoplasmic"
FT /id="PRO_0000101121"
FT DOMAIN 51..115
FT /note="TGS"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01228"
FT REGION 1..21
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 215
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P26639"
FT MOD_RES 218
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P26639"
FT MOD_RES 270
FT /note="Phosphotyrosine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 425
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P26639"
SQ SEQUENCE 695 AA; 80576 MW; B282CF7F5F47363A CRC64;
MSEEKASSPS GKMDGEKPLN PWPEYINTRL DMYHKLKAEH DSILAEKAAK DSKPIKVTLP
DGKQVDAESW KTTPYQIACG ISQGLADNTV VAKVNKVVWD LDRPLETDCT LELLKFEDEE
AQAVYWHSSA HIMGEAMERV YGGCLCYGPP IENGFYYDMY LEEGGVSSND FSSLETLCKK
IIKEKQTFER LEVKKETLLE MFKYNKFKCR ILNEKVNTPT TTVYRCGPLI DLCRGPHVRH
TGKIKTLKIH KNSSTYWEGK ADMETLQRIY GISFPDPKLL KEWEKFQEEA KNRDHRKIGR
DQELYFFHEL SPGSCFFLPK GAYIYNTLME FIRSEYRKRG FQEVVTPNIF NSRLWMTSGH
WQHYSENMFS FEVEKEQFAL KPMNCPGHCL MFDHRPRSWR ELPLRLADFG VLHRNELSGA
LTGLTRVRRF QQDDAHIFCA MEQIEDEIKG CLDFLRTVYS VFGFSFKLNL STRPEKFLGD
IEIWNQAEKQ LENSLNEFGE KWELNPGDGA FYGPKIDIQI KDAIGRYHQC ATIQLDFQLP
IRFNLTYVSH DGDDKKRPVI VHRAILGSVE RMIAILTENY GGKWPFWLSP RQVMVVPVGP
TCDEYAQKVR QEFHDAKFMV DIDLDPGCTL NKKIRNAQLA QYNFILVVGE KEKASGTVNI
RTRDNKVHGE RTVGETVERL QQLKQLRSKQ AEEEF
