SYTC_BOVIN
ID SYTC_BOVIN Reviewed; 723 AA.
AC Q3ZBV8;
DT 11-JUL-2006, integrated into UniProtKB/Swiss-Prot.
DT 27-SEP-2005, sequence version 1.
DT 03-AUG-2022, entry version 117.
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 Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Crossbred X Angus; TISSUE=Ileum;
RG NIH - Mammalian Gene Collection (MGC) project;
RL Submitted (AUG-2005) to the EMBL/GenBank/DDBJ databases.
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; BC103082; AAI03083.1; -; mRNA.
DR RefSeq; NP_001029542.1; NM_001034370.2.
DR AlphaFoldDB; Q3ZBV8; -.
DR SMR; Q3ZBV8; -.
DR STRING; 9913.ENSBTAP00000018947; -.
DR PaxDb; Q3ZBV8; -.
DR PeptideAtlas; Q3ZBV8; -.
DR PRIDE; Q3ZBV8; -.
DR Ensembl; ENSBTAT00000018947; ENSBTAP00000018947; ENSBTAG00000014261.
DR GeneID; 510075; -.
DR KEGG; bta:510075; -.
DR CTD; 6897; -.
DR VEuPathDB; HostDB:ENSBTAG00000014261; -.
DR VGNC; VGNC:35605; TARS1.
DR eggNOG; KOG1637; Eukaryota.
DR GeneTree; ENSGT00940000154969; -.
DR HOGENOM; CLU_008554_0_1_1; -.
DR InParanoid; Q3ZBV8; -.
DR OMA; FYYDFAY; -.
DR OrthoDB; 813937at2759; -.
DR TreeFam; TF300858; -.
DR Proteomes; UP000009136; Chromosome 20.
DR Bgee; ENSBTAG00000014261; Expressed in neutrophil and 107 other tissues.
DR GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0042802; F:identical protein binding; IEA:Ensembl.
DR GO; GO:0004829; F:threonine-tRNA ligase activity; ISS:UniProtKB.
DR GO; GO:0008270; F:zinc ion binding; IEA:Ensembl.
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 2: Evidence at transcript level;
KW Acetylation; Aminoacyl-tRNA synthetase; ATP-binding; Cytoplasm; Ligase;
KW Nucleotide-binding; Phosphoprotein; Protein biosynthesis;
KW Reference proteome; Ubl conjugation.
FT CHAIN 1..723
FT /note="Threonine--tRNA ligase 1, cytoplasmic"
FT /id="PRO_0000245024"
FT DOMAIN 79..143
FT /note="TGS"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01228"
FT REGION 1..49
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 17..41
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 39
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P26639"
FT MOD_RES 243
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P26639"
FT MOD_RES 246
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P26639"
FT MOD_RES 298
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:P26639"
FT MOD_RES 453
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P26639"
FT MOD_RES 702
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P26639"
SQ SEQUENCE 723 AA; 83492 MW; 58CC4E5B7BDC4C85 CRC64;
MSEEQASSPS AKMGDEEKPV GAGEEKQKEG SKKKNKEGSG DGGRAELNPW PEYINTRLEM
YNKLKAEHDS ILAEKAEKDS KPIKVTLPDG KQVDAESWKT TPYQIACGIS QGLADNTVIA
KVNKAVWDLD RPLEEDCTLE LLKFEDEEAQ AVYWHSSAHI MGEAMERVYG GCLCYGPPIE
NGFYYDMYLE EGGVSSNDFS SLETLCKKII KEKQAFERLE VKKETLLEMF KYNKFKCRIL
NEKVNTPTTT VYRCGPLIDL CRGPHVRHTG KIKTLKIHKN SSTYWEGKSD METLQRIYGI
SFPDPKMLKE WEKFQEEAKN RDHRKIGRDQ ELYFFHELSP GSCFFLPKGA YIYNTLIEFI
RSEYRKRGFQ EVVTPNIYNS RLWVTSGHWE HYSENMFSFE VEKELFALKP MNCPGHCLMF
DHRPRSWREL PLRVADFGVL HRNELSGALT GLTRVRRFQQ DDAHIFCAME QIEDEIKGCL
DFLRTVYSIF GFSFKLNLST RPEKFLGDIE VWNQAEKQLE NSLNDFGEKW ELNPGDGAFY
GPKIDIQIKD AIGRYHQCAT IQLDFQLPIR FNLTFVSHDG DDKKKPVIIH RAILGSVERM
IAILTENYGG KWPFWLSPRQ VMVVPVGPTC DEYAQKVRQQ FHNAKFMVDI DLDPGCTLNK
KIRNAQLAQY NFILVVGEKE KTSGTVNIRT RDNKVHGERT ISETIERLQQ LKHSRSKQAE
EEF
