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Database: UniProt
Entry: A0A2Y9QF97_TRIMA
LinkDB: A0A2Y9QF97_TRIMA
Original site: A0A2Y9QF97_TRIMA 
ID   A0A2Y9QF97_TRIMA        Unreviewed;       715 AA.
AC   A0A2Y9QF97;
DT   12-SEP-2018, integrated into UniProtKB/TrEMBL.
DT   12-SEP-2018, sequence version 1.
DT   27-MAR-2024, entry version 21.
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=LOC101352238 {ECO:0000313|RefSeq:XP_023580367.1};
OS   Trichechus manatus latirostris (Florida manatee).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Afrotheria; Sirenia; Trichechidae; Trichechus.
OX   NCBI_TaxID=127582 {ECO:0000313|Proteomes:UP000248480, ECO:0000313|RefSeq:XP_023580367.1};
RN   [1] {ECO:0000313|RefSeq:XP_023580367.1}
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_023580367.1; XM_023724599.1.
DR   AlphaFoldDB; A0A2Y9QF97; -.
DR   STRING; 127582.A0A2Y9QF97; -.
DR   InParanoid; A0A2Y9QF97; -.
DR   OrthoDB; 1119631at2759; -.
DR   Proteomes; UP000248480; 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: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_023580367.1};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW   Protein biosynthesis {ECO:0000256|ARBA:ARBA00022917};
KW   Reference proteome {ECO:0000313|Proteomes:UP000248480}.
FT   DOMAIN          58..124
FT                   /note="TGS"
FT                   /evidence="ECO:0000259|PROSITE:PS51880"
FT   DOMAIN          331..605
FT                   /note="Aminoacyl-transfer RNA synthetases class-II family
FT                   profile"
FT                   /evidence="ECO:0000259|PROSITE:PS50862"
SQ   SEQUENCE   715 AA;  80066 MW;  BF55F08260C1FAB5 CRC64;
     MGLFQTWLRL RLPELHACGL RTVHEAAVPT PPHWLLERLG LFEELWAAQV KRSASKAQEE
     QRTIKVSLPG GQKVDAVAWN TTPYQLAGQI SSALADTAVV AEVNGEPYDL DRPLETDSSI
     RFLTFDSPEG KAVFWHSSAH VLGAAAEQLL GAVLCRGPST ECGFYHDFFL GKERTVQGSE
     LPVLERICRE LAAAAQPFRR LEASRGQLRQ LFKDNPFKLR LIEEKVTGPT ATVYGCGTSV
     DLCRGPHLRH TGQIGGLKLL TNSSSLWRSS GAPETLQRVS GISFPSAEGL WAWAAWREEA
     ELRDHRRIGK EQELFFFHEL SPGSCFFLPR GTRVYHALMA FIRAEYTRRG FSEVKTPMLF
     STKLWEQSGH WEHYREDMFA LQPPGPDRPA SSPSDHPTLA LKPMNCPAHC LMFAHRPRSW
     RELPLRLADF GALHRAEASG GLGGLTRLRC FQQDDAHIFC APDQLEAEIR GCLDFLRSVY
     SVLGFSFRLA LSTRPPGFLG ESRLWDQAEH VLQQALKAFG EPWDLRPGDG AFYGPKIDVH
     LQDALGRPHQ CGTIQLDFQL PLRFGLRYRG QAGALERPVL IHRAVLGSVE RMLAVLAESC
     GGKWPLWLSP FQVVVIPVGP EQEGYAREVQ QSLQAAGLVG DLDADSGLSL SRRVRRAQLA
     HYNFQFVVGQ KEQSRRTVNI RTRDNRRLGE RSLTEAVGRL LELQNTRVSN AEEML
//
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