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Database: UniProt
Entry: A0A3Q0DEA0_MESAU
LinkDB: A0A3Q0DEA0_MESAU
Original site: A0A3Q0DEA0_MESAU 
ID   A0A3Q0DEA0_MESAU        Unreviewed;       723 AA.
AC   A0A3Q0DEA0;
DT   13-FEB-2019, integrated into UniProtKB/TrEMBL.
DT   13-FEB-2019, sequence version 1.
DT   27-MAR-2024, entry version 22.
DE   RecName: Full=threonine--tRNA ligase {ECO:0000256|ARBA:ARBA00013163};
DE            EC=6.1.1.3 {ECO:0000256|ARBA:ARBA00013163};
DE   AltName: Full=Threonyl-tRNA synthetase {ECO:0000256|ARBA:ARBA00031900};
GN   Name=Tars2 {ECO:0000313|RefSeq:XP_021091101.1};
OS   Mesocricetus auratus (Golden hamster).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea;
OC   Cricetidae; Cricetinae; Mesocricetus.
OX   NCBI_TaxID=10036 {ECO:0000313|Proteomes:UP000189706, ECO:0000313|RefSeq:XP_021091101.1};
RN   [1] {ECO:0000313|RefSeq:XP_021091101.1}
RP   IDENTIFICATION.
RG   RefSeq;
RL   Submitted (NOV-2023) to UniProtKB.
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:0000256|ARBA:ARBA00000070};
CC   -!- SIMILARITY: Belongs to the class-II aminoacyl-tRNA synthetase family.
CC       {ECO:0000256|ARBA:ARBA00008226}.
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DR   RefSeq; XP_005084321.1; XM_005084264.2.
DR   RefSeq; XP_021091101.1; XM_021235442.1.
DR   AlphaFoldDB; A0A3Q0DEA0; -.
DR   STRING; 10036.ENSMAUP00000006188; -.
DR   KEGG; maua:101825871; -.
DR   OrthoDB; 1119631at2759; -.
DR   Proteomes; UP000189706; Unplaced.
DR   GO; GO:0005737; C:cytoplasm; IEA:InterPro.
DR   GO; GO:0002161; F:aminoacyl-tRNA editing activity; IEA:Ensembl.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0042803; F:protein homodimerization activity; IEA:Ensembl.
DR   GO; GO:0004829; F:threonine-tRNA ligase activity; IEA:UniProtKB-EC.
DR   GO; GO:0006435; P:threonyl-tRNA aminoacylation; IEA:InterPro.
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:SF27; THREONINE--TRNA LIGASE, MITOCHONDRIAL; 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   3: Inferred from homology;
KW   Aminoacyl-tRNA synthetase {ECO:0000256|ARBA:ARBA00023146};
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW   Ligase {ECO:0000256|ARBA:ARBA00022598, ECO:0000313|RefSeq:XP_021091101.1};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW   Protein biosynthesis {ECO:0000256|ARBA:ARBA00022917};
KW   Reference proteome {ECO:0000313|Proteomes:UP000189706}.
FT   DOMAIN          64..126
FT                   /note="TGS"
FT                   /evidence="ECO:0000259|PROSITE:PS51880"
FT   DOMAIN          333..625
FT                   /note="Aminoacyl-transfer RNA synthetases class-II family
FT                   profile"
FT                   /evidence="ECO:0000259|PROSITE:PS50862"
SQ   SEQUENCE   723 AA;  81664 MW;  8331303285E0CF11 CRC64;
     MGVCLRWRGL GLPLPGFRRC ELHTVHEASV PTPPHWLAER FGLFEELWAA QVKRLARVTQ
     KNTRAIKISL PEGQKVDAVA WNTTPYQLAQ QISSTLADTA VAAEVNGELY DLERPLETDC
     HLRFLTFDSP EGKSVLWHSS AHVLGAAAEQ QMGAVLCRGP STESGFYHDF FLGKERTVRS
     SELPVLERIC QEIIAAAQPF RRLEVSRDQL RQLFKDNHFK LHLIEEKVTG PTATVYGCGM
     SVDLCRGPHL RHTGQIGVLK LLTNSSASWR SPAAPETLQR VSGISFPSTE LLRAWEEQRE
     VALLRDHRRI GKEQELFFFH ELSPGSCFFL PRGTRVYNAL VTFIRAEYAH RGFSEVKTPT
     LFSTKLWEQS GHWEHYRADM FSLKPPGTNG PDISQSDPRA RCPKDTLALK PMNCPAHCLM
     FAHRPRSWRE LPVRLADFGV LHRAEASGSL GGLTRLWRFQ QDDAHIFCAP NQLEAEIRDC
     LDFLRSVYAV LGFSFHLALS TRPSGFLGEP HLWDQAEQVL QQALEEFGEP WDLNPGDGAF
     YGPKIDVHLH DALGRPHQCG TIQLDFQLPL RFNLQYKGQL GALEHPVLIH RAVLGSVERM
     LGVLAESCGG KWPLWLSPLQ VVVIPVGAEQ EEYARQVQQC LQAAGLVSDL DADSGLTLSR
     RVRRAQLAYY NFQFVVGQRE QNRRTVNVRT RENRQLGERG LAEAVQRLLE LQNARVPNAE
     EMF
//
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