GenomeNet

Database: UniProt
Entry: A0A0K0DUH3_STRER
LinkDB: A0A0K0DUH3_STRER
Original site: A0A0K0DUH3_STRER 
ID   A0A0K0DUH3_STRER        Unreviewed;       701 AA.
AC   A0A0K0DUH3;
DT   14-OCT-2015, integrated into UniProtKB/TrEMBL.
DT   14-OCT-2015, sequence version 1.
DT   27-MAR-2024, entry version 27.
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   Strongyloides stercoralis (Threadworm).
OC   Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC   Tylenchina; Panagrolaimomorpha; Strongyloidoidea; Strongyloididae;
OC   Strongyloides.
OX   NCBI_TaxID=6248 {ECO:0000313|WBParaSite:SSTP_0000088600.1};
RN   [1] {ECO:0000313|WBParaSite:SSTP_0000088600.1}
RP   IDENTIFICATION.
RG   WormBaseParasite;
RL   Submitted (AUG-2015) 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}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   AlphaFoldDB; A0A0K0DUH3; -.
DR   STRING; 6248.A0A0K0DUH3; -.
DR   WBParaSite; SSTP_0000088600.1; SSTP_0000088600.1; SSTP_0000088600.
DR   Proteomes; UP000035681; 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};
KW   Reference proteome {ECO:0000313|Proteomes:UP000035681}.
FT   DOMAIN          54..116
FT                   /note="TGS"
FT                   /evidence="ECO:0000259|PROSITE:PS51880"
FT   DOMAIN          318..587
FT                   /note="Aminoacyl-transfer RNA synthetases class-II family
FT                   profile"
FT                   /evidence="ECO:0000259|PROSITE:PS50862"
SQ   SEQUENCE   701 AA;  81120 MW;  512F3B9A7AE503BC CRC64;
     MTVENKENSS IQTIKVSKDK CELNPWPDYI QERNVMFDRL LAEYKAEIAA KPTEKITITL
     PDGKTFEGES WRTTPLNIAE KIAKSLAENA VIAKVNDELW DLDRPFEGNA NLKILKFDED
     EGKAVFWHSS AHILGECMER CCGGHLCYGP PIQEGFYYDM YQENKTVSIE DFPKLESVAK
     CVVKDKQPFE RLEMKKEDLL EMFKYNKFKV RILNEKINTP TTTVYRCGSL IDLCRGPHVR
     NTGKIKAFHI TKTSASYWEG KADAESLQRV YGISFPDTKQ LKEWKTLQEE AAKRDHRKIG
     TDQELFFFHH LSPGSCFWYP KGTFIYNTLT NFIKKEYRKR GFTEVITPNI YNSKLWEQSG
     HWQHYSDDMF QIDVEKEKFA LKPMNCPGHC LMFDQKPRTH NELPFRFADF GVLHRNEASG
     ALTGLTRVRR FQQDDAHIFC RPDQIKSEIA GCLAFLKYVY EEIFGFTFSL NLSTRPETGY
     LGDLDTWNKA EDKLKEALDA SGEKWKLNPG DGAFYGPKID ITIQDALKRN HQCATIQLDF
     QLPERFDLTY IDEKGEKCRP VMIHRAILGS VERMTAILTE SFGGKWPFWL SPRQIKIITV
     HESMKEYAAG VTKKLFDAGF EVDYDPDSSD TMNKQIRNAQ LAQFNFILVI GEKEMNNGTA
     NVRTRDNQVR GEIKIDDLIN IFNRLKNNYT RDAESAEEFK C
//
DBGET integrated database retrieval system