ID A0A340XQG5_LIPVE Unreviewed; 718 AA.
AC A0A340XQG5;
DT 10-OCT-2018, integrated into UniProtKB/TrEMBL.
DT 10-OCT-2018, sequence version 1.
DT 27-MAR-2024, entry version 25.
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_007463571.1};
OS Lipotes vexillifer (Yangtze river dolphin).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Whippomorpha; Cetacea; Odontoceti;
OC Lipotidae; Lipotes.
OX NCBI_TaxID=118797 {ECO:0000313|Proteomes:UP000265300, ECO:0000313|RefSeq:XP_007463571.1};
RN [1] {ECO:0000313|RefSeq:XP_007463571.1}
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_007463571.1; XM_007463509.1.
DR AlphaFoldDB; A0A340XQG5; -.
DR STRING; 118797.A0A340XQG5; -.
DR GeneID; 103089189; -.
DR KEGG; lve:103089189; -.
DR CTD; 80222; -.
DR InParanoid; A0A340XQG5; -.
DR OrthoDB; 1119631at2759; -.
DR Proteomes; UP000265300; 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_007463571.1};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Protein biosynthesis {ECO:0000256|ARBA:ARBA00022917};
KW Reference proteome {ECO:0000313|Proteomes:UP000265300}.
FT DOMAIN 59..121
FT /note="TGS"
FT /evidence="ECO:0000259|PROSITE:PS51880"
FT DOMAIN 328..608
FT /note="Aminoacyl-transfer RNA synthetases class-II family
FT profile"
FT /evidence="ECO:0000259|PROSITE:PS50862"
FT REGION 379..401
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 383..401
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 718 AA; 80851 MW; 6B600E272DA992D5 CRC64;
MGLYQRWRRL RIPGLQACGL HMAAVPTPPH WLVERLGLFE ELWTAQVKRL ASMAQKEHRT
IKISLPGGQI VDAVAWNTTP YQLAQQISSK LADTAVAAQV NGEPYDLERP LETDSDLRFL
TFDSAEGKAV FWHSSTHVLG AAAEQLLGAV LCQGPSTGCG FYHDFFLGKE RTIKGSELPV
LERICQELAA AAQPFRRLEA SQDQLRQLFK DNPFKLHLIE EKVTGPTATV YGCGMLVDLC
RGPHLRHTGQ IGGLKLLSNS SSLWRFSGTP ETLQRVSGIS FPTAEELRAW EEWREEAELR
DHRRIGKEQE LFFFHELSPG SCFFLPRGTR VYNVLVAFIR AEYTRRGFSE VKTPTLFSTK
LWELSGHWEH YREDMFALQP PGSDSHAGSQ SDHSTSHPTG TLALKPMNCP AHCLMFAHRP
RSWRELPLRL ADFGALHRAE ASGSLGGLTR LRRFQQDDAH IFCAPDQLEA EIRGCLDFLR
SVYTVLGFSF RLALSTRPSG FLGEPCLWDQ AEQVLQQALE EFGEPWDLNP GDGAFYGPKI
DVHLHDALGR PHQCGTIQLD FQLPLRFDLQ YKGQAGALER PVLIHRAVLG SVERMLGVLA
ENCGGKWPLW LSPFQVVVIP VGTEQEEYAR EAQRSLQAAG LVGDLDTDSG LTLGRRIRRA
QLAHYNFQFV VGQKEQSKRT VNIRTRDNRR LGERDLAEAV QRLLELQNTR VPNAEEIF
//
