SYTC2_XENTR
ID SYTC2_XENTR Reviewed; 814 AA.
AC Q0V9S0;
DT 20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT 05-SEP-2006, sequence version 1.
DT 03-AUG-2022, entry version 100.
DE RecName: Full=Threonine--tRNA ligase 2, cytoplasmic;
DE EC=6.1.1.3 {ECO:0000250|UniProtKB:Q8BLY2};
DE AltName: Full=Threonyl-tRNA synthetase;
DE Short=ThrRS;
DE AltName: Full=Threonyl-tRNA synthetase protein 3;
GN Name=tars3; Synonyms=tarsl2;
OS Xenopus tropicalis (Western clawed frog) (Silurana tropicalis).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Silurana.
OX NCBI_TaxID=8364;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Testis;
RG NIH - Xenopus Gene Collection (XGC) project;
RL Submitted (AUG-2006) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Catalyzes the attachment of threonine to tRNA(Thr) in a two-
CC step reaction: threonine is first activated by ATP to form Thr-AMP and
CC then transferred to the acceptor end of tRNA(Thr). Also edits
CC incorrectly charged tRNA(Thr) via its editing domain, at the post-
CC transfer stage. {ECO:0000250|UniProtKB:Q8BLY2}.
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:0000250|UniProtKB:Q8BLY2};
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q8BLY2}. Nucleus
CC {ECO:0000250|UniProtKB:Q8BLY2}. Note=Primarily cytoplasmic. Also
CC detected at lower levels in the nucleus.
CC {ECO:0000250|UniProtKB:Q8BLY2}.
CC -!- SIMILARITY: Belongs to the class-II aminoacyl-tRNA synthetase family.
CC {ECO:0000305}.
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DR EMBL; BC121417; AAI21418.1; -; mRNA.
DR RefSeq; NP_001096223.1; NM_001102753.1.
DR AlphaFoldDB; Q0V9S0; -.
DR SMR; Q0V9S0; -.
DR STRING; 8364.ENSXETP00000054472; -.
DR PaxDb; Q0V9S0; -.
DR PRIDE; Q0V9S0; -.
DR DNASU; 100124774; -.
DR Ensembl; ENSXETT00000043847; ENSXETP00000043847; ENSXETG00000020313.
DR GeneID; 100124774; -.
DR KEGG; xtr:100124774; -.
DR CTD; 123283; -.
DR Xenbase; XB-GENE-5954362; tars3.
DR eggNOG; KOG1637; Eukaryota.
DR HOGENOM; CLU_008554_0_2_1; -.
DR InParanoid; Q0V9S0; -.
DR OMA; IWDEAEK; -.
DR OrthoDB; 813937at2759; -.
DR PhylomeDB; Q0V9S0; -.
DR TreeFam; TF300858; -.
DR Proteomes; UP000008143; Chromosome 3.
DR Proteomes; UP000790000; Unplaced.
DR Bgee; ENSXETG00000020313; Expressed in testis and 13 other tissues.
DR ExpressionAtlas; Q0V9S0; baseline.
DR GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0004829; F:threonine-tRNA ligase activity; ISS:UniProtKB.
DR GO; GO:0006435; P:threonyl-tRNA aminoacylation; ISS:UniProtKB.
DR CDD; cd00771; ThrRS_core; 1.
DR Gene3D; 3.10.20.30; -; 1.
DR Gene3D; 3.30.930.10; -; 1.
DR Gene3D; 3.40.50.800; -; 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; IPR033728; ThrRS_core.
DR InterPro; IPR012947; tRNA_SAD.
DR PANTHER; PTHR11451; PTHR11451; 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; SSF55186; SSF55186; 1.
DR SUPFAM; SSF55681; SSF55681; 1.
DR SUPFAM; SSF81271; SSF81271; 1.
DR TIGRFAMs; TIGR00418; thrS; 1.
DR PROSITE; PS50862; AA_TRNA_LIGASE_II; 1.
DR PROSITE; PS51880; TGS; 1.
PE 2: Evidence at transcript level;
KW Aminoacyl-tRNA synthetase; ATP-binding; Coiled coil; Cytoplasm; Ligase;
KW Nucleotide-binding; Nucleus; Protein biosynthesis; Reference proteome.
FT CHAIN 1..814
FT /note="Threonine--tRNA ligase 2, cytoplasmic"
FT /id="PRO_0000333830"
FT DOMAIN 172..234
FT /note="TGS"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01228"
FT REGION 62..142
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 2..72
FT /evidence="ECO:0000255"
FT MOTIF 798..804
FT /note="Nuclear localization signal"
FT /evidence="ECO:0000250|UniProtKB:Q8BLY2"
FT COMPBIAS 118..136
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 814 AA; 93328 MW; 97A63139DAEE7562 CRC64;
MAAHIAQRLT VQEQEIRRLN EEIGRLLELG LQGSVEHSPN PVLEQLRAEN EKLKYRISHL
QRSLREEQER ARPGQYGEPG LKDAAPVEEP KQQNNKAKEK GQATKGENSV GGKPSACEGN
KKNEKKAGKE VDGHKQEGPC APGFIKDRLA LYETLKNEHD ALLAARAAHQ SKPIKITLAD
GKQVDGESWK TTPYQVAIGI SKGLADNVVI AKVNNELWDL DRPLEQDSNV ELLKFDSEEA
QAVYWHSSAH ILGETMENFY GGCLCYGPPI ENGFYYDMYL DGRGVSSNEF PSLENMCKAI
IKEKQPFERL EVSKDLLLEM FKYNKFKCRI LNEKVDTPTT TVYRCGPLID LCRGPHVRHT
GKIKTLKIYK NSSTYWEGRA DMETLQRIYG ISFPDSKLMK EWEQFQEEAK NRDHRKIGRD
QELFFFHDLS PGSCFFLPRG AHIYNTLTDF IKGEYQIRNF TEVASPNIYN SKLWEMSGHW
QHYSENMFSF EVEKETFALK PMNCPGHCLM FGHRPRSWRE LPLRFADFGV LHRNELSGTL
SGLTRVRRFQ QDDAHIFCTM DQIQEEMNGC LQFLQSVYKV FGFTFQLHLS TRPENYLGEI
EIWNEAEKQL ESSLNQFGEP WKLNPGDGAF YGPKIDIKIK DAIGRYHQCA TIQLDFQLPI
RFNLTYVSKD GDDKKRPVII HRAILGSVER MIAILCENYG GKWPFWLSPR QVMVIPVGPS
CDEYAQQVCK DVFEAGFMAE VDLDHSCTLN KKIRNAQLAQ CNFILVVGEK EKTDSAVNVR
TRDNKVHGEI LLTSAIEKLK TLKKLRSKNA EEEF
