ID   A0A3B3DIE8_ORYME        Unreviewed;       724 AA.
AC   A0A3B3DIE8;
DT   05-DEC-2018, integrated into UniProtKB/TrEMBL.
DT   05-DEC-2018, sequence version 1.
DT   27-MAR-2024, entry version 28.
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};
OS   Oryzias melastigma (Marine medaka).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC   Ovalentaria; Atherinomorphae; Beloniformes; Adrianichthyidae; Oryziinae;
OC   Oryzias.
OX   NCBI_TaxID=30732 {ECO:0000313|Ensembl:ENSOMEP00000029888.1, ECO:0000313|Proteomes:UP000261560};
RN   [1] {ECO:0000313|Ensembl:ENSOMEP00000029888.1}
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (SEP-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   AlphaFoldDB; A0A3B3DIE8; -.
DR   STRING; 30732.ENSOMEP00000029888; -.
DR   PaxDb; 30732-ENSOMEP00000029888; -.
DR   Ensembl; ENSOMET00000020041.1; ENSOMEP00000029888.1; ENSOMEG00000013835.1.
DR   GeneTree; ENSGT00940000154969; -.
DR   OMA; WYADGMY; -.
DR   OrthoDB; 1119631at2759; -.
DR   Proteomes; UP000261560; Unplaced.
DR   GO; GO:0005737; C:cytoplasm; IEA:InterPro.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
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:SF54; THREONINE--TRNA LIGASE; 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};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW   Protein biosynthesis {ECO:0000256|ARBA:ARBA00022917}.
FT   DOMAIN          81..143
FT                   /note="TGS"
FT                   /evidence="ECO:0000259|PROSITE:PS51880"
FT   DOMAIN          353..626
FT                   /note="Aminoacyl-transfer RNA synthetases class-II family
FT                   profile"
FT                   /evidence="ECO:0000259|PROSITE:PS50862"
FT   REGION          1..52
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        21..39
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   724 AA;  83249 MW;  871F497D1C0432DF CRC64;
     MADQTVVEKM SEMQVDAGKK GGAGNEKKDG KKKAKNTAGD SAGRSELSPP PQYIDERLSL
     YAKLKAEHDA LIAERATKDS RPIKVTLPDG KVLEAESWKT TPYQLACGIS QGLADNTVIA
     KVNNSVWDLD RPLEDNCSLQ LLKFDDEEAQ AVYWHSSAHI LGEAMEKVYG GCLCYGPPIE
     SGFYYDMFLD NNEGVSSNDF PCLENLCKKI IKEKQPFERL EIKKETLLEM FKYNKFKCRI
     LNEKVTTPTT TVYRCGPLID LCRGPHVRHT GKIKALKIHK NSSTYWEGKA DMETLQRIYG
     ISFPDPKMLK EWEKFQEEAK NRDHRKLGRE QDLFFFHELS PGSCFFLPKG AFIYNTLIEF
     IRSEYRNRGF QEVVTPNIYN SKLWVTSGHW QHYSENMFSF EVEKEIFALK PMNCPGHCLM
     FDHRPRSWRE LPLRMADFGV LHRNELSGAL TGLTRVRRFQ QDDAHIFCSM DQIEEEIKGC
     LHFLRTVYDV FGFTFKLNLS TRPEKFLGEP EMWDQAEKQL ENSLNEFGEK WVLNPGDGAF
     YGPKIDIQIK DAIGRYHQCA TIQLDFQLPI RFNLAYVSHD GDDKKRPVII HRAILGSVER
     MIAILTENYG GKWPLWLSPR QVMLVPVGPT CEEYAEKVKQ EFHINGFMAD VDLDPGCTLN
     KKIRNAQLAQ YNFILVVGEK EKTSNTVNVR TRDNKVHGEC SVEECIQRLT RLKASRSRNA
     EEEF
//