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Database: UniProt
Entry: F7GBQ5_CALJA
LinkDB: F7GBQ5_CALJA
Original site: F7GBQ5_CALJA 
ID   F7GBQ5_CALJA            Unreviewed;       588 AA.
AC   F7GBQ5;
DT   27-JUL-2011, integrated into UniProtKB/TrEMBL.
DT   25-MAY-2022, sequence version 2.
DT   27-MAR-2024, entry version 58.
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|Ensembl:ENSCJAP00000011939.3};
OS   Callithrix jacchus (White-tufted-ear marmoset).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Platyrrhini; Cebidae;
OC   Callitrichinae; Callithrix; Callithrix.
OX   NCBI_TaxID=9483 {ECO:0000313|Ensembl:ENSCJAP00000011939.3, ECO:0000313|Proteomes:UP000008225};
RN   [1] {ECO:0000313|Ensembl:ENSCJAP00000011939.3}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Warren W., Ye L., Minx P., Worley K., Gibbs R., Wilson R.K.;
RL   Submitted (MAR-2009) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|Ensembl:ENSCJAP00000011939.3}
RP   IDENTIFICATION.
RG   Ensembl;
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   AlphaFoldDB; F7GBQ5; -.
DR   Ensembl; ENSCJAT00000012592.4; ENSCJAP00000011939.3; ENSCJAG00000006429.5.
DR   GeneTree; ENSGT00940000161600; -.
DR   Proteomes; UP000008225; Chromosome 18.
DR   Bgee; ENSCJAG00000006429; Expressed in heart and 6 other cell types or tissues.
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   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   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   PRINTS; PR01047; TRNASYNTHTHR.
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};
KW   Reference proteome {ECO:0000313|Proteomes:UP000008225}.
FT   DOMAIN          55..121
FT                   /note="TGS"
FT                   /evidence="ECO:0000259|PROSITE:PS51880"
FT   DOMAIN          205..478
FT                   /note="Aminoacyl-transfer RNA synthetases class-II family
FT                   profile"
FT                   /evidence="ECO:0000259|PROSITE:PS50862"
FT   REGION          247..271
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        253..271
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   588 AA;  66418 MW;  8F09E446C471CAF9 CRC64;
     MGLYQRWQQL RLQGLQAYGL HTAVVSTPPH WLAERLGLFE ELWAAQVKRL ASMAQKEPRT
     IKISLPGGQK VDAVAWNTTP YQLARQISST LADTAVAAQV NGELYDMERP LETDSDLRFL
     TFDSPEGKAV FWHSSTHVLG AAAEQFLGAV LCRGPSTENG FYHDFFLGKE RTIRGSELPV
     LEQICQELTA AAQPFRRLEA SRDQLHRLFK AEYARRGFFE VKTPTLFSTK LWEQSGHWEH
     YQEDMFAVQP PGSDRPASSQ SDHSTRHTTD TLALKPMNCP AHCLMFAHRP RSWRELPLRL
     ADFGALHRAE ASGGLCGLTR LRCFQQDDAH IFCTTDQLEA EIQSCLDFLR SVYAVLGFSF
     RLALSTRPSG FLGDPCLWDQ AEQVLQQALK EFGEPWDLNS GDGAFYGPKI DVHLHDALGR
     PHQCGTIQLD FQLPLRFDLQ YKGQAGALER PVLIHRAVLG SVERLLGVLA ESCRGKWPLW
     LSPFQVVVIP VGTEQEEYAR ETQQSLQAAG LVCDLDADSR LTLSRRIRRA QLAHYNFQFV
     VGQKEQSKST VNIRTRDNRL LGEWSLPEAV QRLVVLQNTR VPNAEEIF
//
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