ID   A0A183VPQ7_TRIRE        Unreviewed;       643 AA.
AC   A0A183VPQ7;
DT   07-SEP-2016, integrated into UniProtKB/TrEMBL.
DT   07-SEP-2016, 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};
OS   Trichobilharzia regenti (Nasal bird schistosome).
OC   Eukaryota; Metazoa; Spiralia; Lophotrochozoa; Platyhelminthes; Trematoda;
OC   Digenea; Strigeidida; Schistosomatoidea; Schistosomatidae; Trichobilharzia.
OX   NCBI_TaxID=157069 {ECO:0000313|WBParaSite:TRE_0000246501-mRNA-1};
RN   [1] {ECO:0000313|WBParaSite:TRE_0000246501-mRNA-1}
RP   IDENTIFICATION.
RG   WormBaseParasite;
RL   Submitted (JUN-2016) 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; A0A183VPQ7; -.
DR   STRING; 157069.A0A183VPQ7; -.
DR   WBParaSite; TRE_0000246501-mRNA-1; TRE_0000246501-mRNA-1; TRE_0000246501.
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   InterPro; IPR012947; tRNA_SAD.
DR   PANTHER; PTHR11451:SF46; 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          19..81
FT                   /note="TGS"
FT                   /evidence="ECO:0000259|PROSITE:PS51880"
FT   DOMAIN          288..533
FT                   /note="Aminoacyl-transfer RNA synthetases class-II family
FT                   profile"
FT                   /evidence="ECO:0000259|PROSITE:PS50862"
SQ   SEQUENCE   643 AA;  74843 MW;  A6F89092F0F85AD1 CRC64;
     LWNKLKKEYD DFIASQPRSP IQITLPDGTI VDGKAWETTP MEVAKNISKT LAEHAVIAKV
     NGELWDLLRP FEKSSSLEVY NFDHKDGEYV FWHSSAHVLG EALERCYGGH LCYGPPVEEG
     FYYDMWLPNQ QQSGLRPEDL HVVENLCHNI CKENQPFERL EMKKEDLLKM FAYNQFKCRI
     IRDKIDTPTT TVYRCGPLID LCRGPHVRHT GCIKALTVTK SSCSYWEGRV DAEALQRVYG
     ISFPDPKRLK EWKHMQEEAA KRDHRKLGVE QKLFFFHELS PGSCFFLPAG AHIYNTLVSF
     IRSEYWKRGF QEVITPNIYN SALWEQSGHW QHYSEHLFKI EVEKQTFGLK PMNCPGHCLM
     YAKEIRSHRE LPLRFADFDD AHIFCREDQI KDEIKNCLDF LRYVYGVFGF SFELYLSTRP
     EKFMGEIEMW NRAEKQLKES MDEVGMKWQL NPGDGAFYGP KIDITIMDAL RRRHQCATIQ
     LDFQMPVRFN LTYKIHCTDK VNVHRPVIIH RAILGSVERI IAILTESYAG KWPFWLSPRQ
     VLVVPVVSAC DEYAIEVKNR LHDAGFTTSI DTDPGRTLNK KIRNGQLLQN NFILVVGEKE
     VTNGTVNVRT RDNKVHGEHP VEHVIERFRQ LAASRTLEAE QEF
//