GenomeNet

Database: UniProt
Entry: Q5XHY5
LinkDB: Q5XHY5
Original site: Q5XHY5 
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   24-JAN-2024, entry version 134.
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}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
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.ENSRNOP00000075146; -.
DR   iPTMnet; Q5XHY5; -.
DR   PhosphoSitePlus; Q5XHY5; -.
DR   jPOST; Q5XHY5; -.
DR   PaxDb; 10116-ENSRNOP00000044467; -.
DR   Ensembl; ENSRNOT00000051910.3; ENSRNOP00000044467.2; ENSRNOG00000019023.7.
DR   Ensembl; ENSRNOT00055044476; ENSRNOP00055036383; ENSRNOG00055025622.
DR   Ensembl; ENSRNOT00060036694; ENSRNOP00060030205; ENSRNOG00060020828.
DR   Ensembl; ENSRNOT00065035786; ENSRNOP00065028847; ENSRNOG00065020968.
DR   GeneID; 294810; -.
DR   KEGG; rno:294810; -.
DR   AGR; RGD:1359527; -.
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   OrthoDB; 1119631at2759; -.
DR   PRO; PR:Q5XHY5; -.
DR   Proteomes; UP000002494; Chromosome 2.
DR   Bgee; ENSRNOG00000019023; Expressed in liver and 20 other cell types or 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; cd01667; TGS_ThrRS; 1.
DR   CDD; cd00860; ThrRS_anticodon; 1.
DR   CDD; cd00771; ThrRS_core; 1.
DR   Gene3D; 3.10.20.30; -; 1.
DR   Gene3D; 3.40.50.800; Anticodon-binding domain; 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; IPR047246; ThrRS_anticodon.
DR   InterPro; IPR033728; ThrRS_core.
DR   InterPro; IPR012947; tRNA_SAD.
DR   NCBIfam; TIGR00418; thrS; 1.
DR   PANTHER; PTHR11451:SF36; THREONINE--TRNA LIGASE 1, CYTOPLASMIC; 1.
DR   PANTHER; PTHR11451; THREONINE-TRNA LIGASE; 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; SSF52954; Class II aaRS ABD-related; 1.
DR   SUPFAM; SSF55681; Class II aaRS and biotin synthetases; 1.
DR   SUPFAM; SSF81271; TGS-like; 1.
DR   SUPFAM; SSF55186; ThrRS/AlaRS common domain; 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
//
DBGET integrated database retrieval system