SYTC2_BOVIN
ID SYTC2_BOVIN Reviewed; 724 AA.
AC A6QNM8;
DT 20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT 21-AUG-2007, sequence version 1.
DT 03-AUG-2022, entry version 90.
DE RecName: Full=Threonine--tRNA ligase 2, cytoplasmic;
DE EC=6.1.1.3 {ECO:0000250|UniProtKB:Q8BLY2};
DE AltName: Full=Threonyl-tRNA synthetase;
DE Short=ThrRS;
DE AltName: Full=Threonyl-tRNA synthetase protein 3;
GN Name=TARS3; Synonyms=TARSL2;
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=Hereford; TISSUE=Hypothalamus;
RG NIH - Mammalian Gene Collection (MGC) project;
RL Submitted (JUL-2007) 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:Q8BLY2}.
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:Q8BLY2};
CC -!- SUBUNIT: May be a component of the multisynthetase complex (MSC), a
CC large multi-subunit complex which contains at least eight different
CC aminoacyl-tRNA synthetases plus three auxillary subunits AIMP1, AIMP2
CC and EEF1E1. Interacts with the MSC components EPRS1, AIMP1, AIMP2 and
CC KARS1. {ECO:0000250|UniProtKB:A2RTX5}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q8BLY2}. Nucleus
CC {ECO:0000250|UniProtKB:Q8BLY2}. Note=Primarily cytoplasmic. Also
CC detected at lower levels in the nucleus.
CC {ECO:0000250|UniProtKB:Q8BLY2}.
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; BC148906; AAI48907.1; -; mRNA.
DR RefSeq; NP_001095559.1; NM_001102089.2.
DR AlphaFoldDB; A6QNM8; -.
DR SMR; A6QNM8; -.
DR STRING; 9913.ENSBTAP00000047958; -.
DR PaxDb; A6QNM8; -.
DR PRIDE; A6QNM8; -.
DR Ensembl; ENSBTAT00000052449; ENSBTAP00000047958; ENSBTAG00000007651.
DR GeneID; 525350; -.
DR KEGG; bta:525350; -.
DR CTD; 123283; -.
DR VEuPathDB; HostDB:ENSBTAG00000007651; -.
DR VGNC; VGNC:35606; TARS3.
DR eggNOG; KOG1637; Eukaryota.
DR GeneTree; ENSGT00940000159348; -.
DR HOGENOM; CLU_008554_0_1_1; -.
DR InParanoid; A6QNM8; -.
DR OrthoDB; 813937at2759; -.
DR TreeFam; TF300858; -.
DR Proteomes; UP000009136; Chromosome 21.
DR Bgee; ENSBTAG00000007651; Expressed in occipital lobe and 100 other tissues.
DR ExpressionAtlas; A6QNM8; baseline.
DR GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0004829; F:threonine-tRNA ligase activity; ISS:UniProtKB.
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 InterPro; IPR002314; aa-tRNA-synt_IIb.
DR InterPro; IPR006195; aa-tRNA-synth_II.
DR InterPro; IPR045864; aa-tRNA-synth_II/BPL/LPL.
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; 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; Coiled coil;
KW Cytoplasm; Ligase; Nucleotide-binding; Nucleus; Phosphoprotein;
KW Protein biosynthesis; Reference proteome.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250|UniProtKB:A2RTX5"
FT CHAIN 2..724
FT /note="Threonine--tRNA ligase 2, cytoplasmic"
FT /id="PRO_0000333827"
FT DOMAIN 155..220
FT /note="TGS"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01228"
FT REGION 90..112
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 44..72
FT /evidence="ECO:0000255"
FT MOD_RES 2
FT /note="N-acetylalanine"
FT /evidence="ECO:0000250|UniProtKB:A2RTX5"
FT MOD_RES 451
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:A2RTX5"
SQ SEQUENCE 724 AA; 83076 MW; 6B3307FCC4EE0FD8 CRC64;
MAAEALAAEA VASRLARQEE DIRWLWAEVH RLRDEQLNAP DRCQAEGPCL TREVAQLRAE
NRELRHCLYR LRLCLAEELS HQARLESAAR AEAGRAAAGA QPPPSQSLEE DVKKEIDPDN
EVKNPPNFMK ERLKFFEILK KDHQLLLAIY EKKGDSSNVI TVRVADGRTV KGEAWKTTPY
QVAAEISQEL AETTVVAKVN GELWDLDRPL EGDATVELLT FEDEEARAVY WHSSAHVLGE
ALELHYGGLL CCSPPGDGSF HYDVYLEDRA VSSAELPVLE SMCQAIIKEQ QPFERLEVST
KVLLDLFKYN KFKCRILKEK VATPTTTVYR CGPLVELCKG PHVRHTGTIK VIKIFKNSLA
YWADNPEMEM LQRVYGVSFP DEQRMAAWEE LQEEARARDH RTIGKEQELF FFHDLSPGSC
FFLPRGACIY NTLIDFIREQ HHQRNFTEVL SPNMYSCKLW EASGHWQHYS ENMFTFDIDK
DTFALKPMNC PGHCLMFAHR PRSWREMPIR LADFGVLHRN EPSGALSGLT CVRRFQQDDA
HIFCTVGQLE EEIKGCLQFL QSVYSTFGFS FQLNLSTRPE NFLGKIELWD EAEKQLQNSL
MEFGKPWKIN PGEGAFYGPK IDLEIKDALG RYHQCATIQL DFQLPIRFNL TYVSKDGDDK
KNPVIIHQAI LGSVERMIAI LSENYGGKWP FWLSPRQVMV IPVGPTCEKY ALQWLEKRKR
QIML
