ID A0A1Y1JES3_PLAGO Unreviewed; 921 AA.
AC A0A1Y1JES3;
DT 30-AUG-2017, integrated into UniProtKB/TrEMBL.
DT 30-AUG-2017, sequence version 1.
DT 27-MAR-2024, entry version 24.
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 ORFNames=PGO_092290 {ECO:0000313|EMBL:GAW81029.1};
OS Plasmodium gonderi.
OC Eukaryota; Sar; Alveolata; Apicomplexa; Aconoidasida; Haemosporida;
OC Plasmodiidae; Plasmodium; Plasmodium (Plasmodium).
OX NCBI_TaxID=77519 {ECO:0000313|EMBL:GAW81029.1, ECO:0000313|Proteomes:UP000195521};
RN [1] {ECO:0000313|Proteomes:UP000195521}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 30045 {ECO:0000313|Proteomes:UP000195521};
RA Arisue N., Honma H., Kawai S., Tougan T., Tanabe K., Horii T.;
RT "Plasmodium gonderi genome.";
RL Submitted (APR-2017) to the EMBL/GenBank/DDBJ databases.
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 -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:GAW81029.1}.
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DR EMBL; BDQF01000010; GAW81029.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1Y1JES3; -.
DR EnsemblProtists; GAW81029; GAW81029; PGO_092290.
DR OMA; WYADGMY; -.
DR OrthoDB; 1119631at2759; -.
DR Proteomes; UP000195521; 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; 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; 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; SSF55186; ThrRS/AlaRS common domain; 1.
DR PROSITE; PS50862; AA_TRNA_LIGASE_II; 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, ECO:0000313|EMBL:GAW81029.1};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Protein biosynthesis {ECO:0000256|ARBA:ARBA00022917};
KW Reference proteome {ECO:0000313|Proteomes:UP000195521}.
FT DOMAIN 485..808
FT /note="Aminoacyl-transfer RNA synthetases class-II family
FT profile"
FT /evidence="ECO:0000259|PROSITE:PS50862"
FT REGION 228..251
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 722..772
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 921 AA; 107062 MW; E0D04ACFA7E4E3FD CRC64;
MRRGVLSFCL LLTNTCNNIN TIYPSLFIPA LGKIKNRVSH LSNVSVAKSC ITKNSDITRN
NRITKKNLIT RNTFCMIKRS LYLDNLKKVN NICKKKKNIF LFNKLFSKKM ASTTSCVHNN
FDDMEKLKKN FVQKENPDFI YERLEIFKKL KEKKKHEKEL LLKNSESIER NINVELLDGS
IKHGEYNITT PFHIASSISK RLAEDSIVAR VTYLEKVDLE LCDIEEEEEV ASGKSGEAEK
PGEEKKSEEK KSNCKLDGTT LLWDMNVPLL GNCKIEFLNM ENEGAKKIFW HSSAHILGSS
LEKLFGGYLT IGPALKEGFY YDIFLGDFAI SNEHYKRIED EFNKLVKENA EFEKLICTKE
EVMELFKYNP FKLELIKSKI PDNKKTSVYK CGNFIDLCLG PHLKNTGKAK AFKVLKNSAA
YWLGNKNNDS LQRVYGITFP KKTELNDYLK FLEEAKKRDH RNVGKKLNFF FFDKYTSPGS
CFWLPHGAKI YNKLIDFVRR EYRIRKYEEV ITPNVFSCDL WKTSGHYQNY KDCMFIFNVE
NKEWGMKPMN CPGHCTMFKQ LNASYRSLPI RLADFGVLHR NEITGSLSGL TRVRRFQQDD
SHIFCTFDQI KQEVLSTLHF IFFIYDLFGF KYELYLSTRP NKFIGSISTW DFAEQALKDA
LNSANIKWKL NEGDGAFYGP KIDILLKDSI HRTHQCGTIQ LDFQLPIRFN LQYKNRDFGA
MEEEEKEAEK KEDEAEKKED KAENKEGEAE KKEGEAEKKD VEAEKKEDSA TDQLKRGFDR
PVIIHRAILG SVERFVAILI EHTAGKLPFW LSPRQAIVLP VSDKFNEYAN YVYDTLNNHF
FDVEIDTSLN TLNKKIREAQ LNQFNFILVV GEKELTTNTV TVRNRDDQNN HEVYSIEELI
AHFNKLLNVN SKMFNQVKPF K
//
