ID A0A1I8NNB4_STOCA Unreviewed; 761 AA.
AC A0A1I8NNB4;
DT 18-JAN-2017, integrated into UniProtKB/TrEMBL.
DT 18-JAN-2017, sequence version 1.
DT 27-MAR-2024, entry version 31.
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=106093899 {ECO:0000313|EnsemblMetazoa:SCAU000581-PB};
OS Stomoxys calcitrans (Stable fly) (Conops calcitrans).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Muscoidea;
OC Muscidae; Stomoxys.
OX NCBI_TaxID=35570 {ECO:0000313|EnsemblMetazoa:SCAU000581-PB, ECO:0000313|Proteomes:UP000095300};
RN [1] {ECO:0000313|EnsemblMetazoa:SCAU000581-PB}
RP IDENTIFICATION.
RC STRAIN=USDA {ECO:0000313|EnsemblMetazoa:SCAU000581-PB};
RG EnsemblMetazoa;
RL Submitted (MAY-2020) 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_013116518.1; XM_013261064.1.
DR AlphaFoldDB; A0A1I8NNB4; -.
DR STRING; 35570.A0A1I8NNB4; -.
DR EnsemblMetazoa; SCAU000581-RB; SCAU000581-PB; SCAU000581.
DR GeneID; 106093899; -.
DR KEGG; scac:106093899; -.
DR VEuPathDB; VectorBase:SCAU000581; -.
DR OrthoDB; 1119631at2759; -.
DR Proteomes; UP000095300; Unassembled WGS sequence.
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: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 121..183
FT /note="TGS"
FT /evidence="ECO:0000259|PROSITE:PS51880"
FT DOMAIN 389..664
FT /note="Aminoacyl-transfer RNA synthetases class-II family
FT profile"
FT /evidence="ECO:0000259|PROSITE:PS50862"
SQ SEQUENCE 761 AA; 87388 MW; EBFEB3C161953F81 CRC64;
MNRFVQVLKL KEKKSIRLRS LTTCQNLRVL LSNVVGLSSP AKESTERRLP DLYKVNCGTL
IRNFATLSSK MKKEKQKNVA VDGGKKVKEL NPWPDYIEER NKLWEKCKAE YLAEVAAKPR
NPIKITLPDG KQVDGTSWET TPYEVAKGIS QGLADNTVIS KVNGEVWDLD RVLEGDCTLH
LLKFDDPDAQ AVFWHSSAHI MGEAMERIYG GHLCYGPPIA EGFYYDMHLD GEGISTNDYP
VMEGLVKQIV KEKQPFERLV MKKSDLLEMF KYNEFKVRIL NEKVQTDTTT VYKCGPLIDL
CRGPHVRHTG KVKALKVTKN SSTYWEGKAD AETLQRVYGI SFPDPKQLKE WEKLQEEAAK
RDHRKIGKEQ ELFFFHELSP GSCFFLPRGA HIYNTLMNFI KSEYRKRGFQ EVVTPNIYNS
KLWVTSGHWQ HYAENMFSFE AEKETFALKP MNCPGHCLMF DVRNRSWREL PLRMADFGVL
HRNELSGALT GLTRVRRFQQ DDAHIFCAPD QIKSEMKGCL DFLRHVYTIF GFSFNLVLST
RPEKYLGELE QWNDAEKALA ESLDEFGMPW KENPGDGAFY GPKIDITIMD ALKRAHQCAT
IQLDFQLPIR FNLNYIADDG EKKRPVIIHR AILGSVERMI AILTENYAGK WPFWLSPRQA
MVVPVGPQFD EYAQSVREQL HSAGFMVEAD CDAGDTMNKK IRNAQLAQFN FILVVGEKER
SSNTVNVRTR DNKVHGEVSV SDLLTKLQKI RDDFVTNEDN F
//
