ID A0A0L1KUS0_9EUGL Unreviewed; 980 AA.
AC A0A0L1KUS0;
DT 11-NOV-2015, integrated into UniProtKB/TrEMBL.
DT 11-NOV-2015, sequence version 1.
DT 27-MAR-2024, entry version 30.
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=XU18_1996 {ECO:0000313|EMBL:KNH07464.1};
OS Perkinsela sp. CCAP 1560/4.
OC Eukaryota; Discoba; Euglenozoa; Kinetoplastea; Prokinetoplastina;
OC Ichthyobodonidae; Perkinsela.
OX NCBI_TaxID=1314962 {ECO:0000313|EMBL:KNH07464.1, ECO:0000313|Proteomes:UP000036983};
RN [1] {ECO:0000313|EMBL:KNH07464.1, ECO:0000313|Proteomes:UP000036983}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CCAP 1560/4 {ECO:0000313|EMBL:KNH07464.1};
RA Tanifuji G., David V., Flegontov P., Gerasimov E., Hashimi H.,
RA Logacheva M., Maruyama S., Onodera N., Gray M., Archibald J., Curtis B.,
RA Cenci U., Lukes J.;
RT "Draft genomes of Paramoeba pemaquidensis and its kinetoplastid
RT endosymbiont Perkinsela sp. CCAP 1560/4.";
RL Submitted (JUN-2015) 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:KNH07464.1}.
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DR EMBL; LFNC01000115; KNH07464.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0L1KUS0; -.
DR EnsemblProtists; KNH07464; KNH07464; XU18_1996.
DR OrthoDB; 1119631at2759; -.
DR Proteomes; UP000036983; Unassembled WGS sequence.
DR GO; GO:0005737; C:cytoplasm; IEA:InterPro.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion 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; cd00860; ThrRS_anticodon; 1.
DR CDD; cd00771; ThrRS_core; 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; 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:SF44; THREONINE--TRNA LIGASE, CHLOROPLASTIC_MITOCHONDRIAL 2; 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 ECO:0000313|EMBL:KNH07464.1}; ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW Ligase {ECO:0000256|ARBA:ARBA00022598};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Protein biosynthesis {ECO:0000256|ARBA:ARBA00022917};
KW Reference proteome {ECO:0000313|Proteomes:UP000036983};
KW Zinc {ECO:0000256|ARBA:ARBA00022833}.
FT DOMAIN 401..834
FT /note="Aminoacyl-transfer RNA synthetases class-II family
FT profile"
FT /evidence="ECO:0000259|PROSITE:PS50862"
SQ SEQUENCE 980 AA; 110069 MW; BD35458427819AC2 CRC64;
MSTQTSKSEQ LPPYWAPRSA MFEDLYSKQM DRFRSLRKPI VVHRVKRILS VSDEVRDVQC
TGHFTRPIDI LPVACANPAE ADTHRSRLVA HSEESTPQRV SSTIGNKVVV VARINGDTLW
DLTRPLEASI ESLEFIYWCD AASASEDAGA SQSDVDELDE DTQNLARHVF WHSSAHMLGY
AMEKILEPCQ LHHGPALDAV FSRKAVSEEE KAPMQSTESI ARTPEDRAAF LRTMCAQYGK
ADKIVTGGGF FYEASVSQAI KEGVDFNRLQ KQIGSIQREN HPFQRLVVTQ SEAQLLFADN
PLKQKWIAKS AETEGESCVF TAYRCGEFID LCRGPHVIST GVVRKVILTK VGGVQAAHTD
SASTKESTTA CLQRVYGISF PTNALAKVFS EHIERASTQL DHKNVGIAQN LFHTAVDMAC
PGSAFFLPHG TRIYNALLSF LRKEYAKRGY EEVITANIYD QKLWMTSGHW DKYRENLFLI
ASEKTSDAAS TADESSKKEL VSSMALKPMN CPGHCVLYSL SAHSYKSLPL RYAEFGVLHR
NEVRGALRGL TRVTRFVQDD AHIFCTPYQL HGEIGRNLSF LGFVYEKVLG FTDYKLMLST
KPSDKMYIGD DDIWQLAESK LQSALNSFCF AHVARAVGVL RGQSSPVEHD GHWPVFGSRR
EGEIQGDSMQ AFWQSYGFET TEYTGTEDNI QNVIALRRAI RDQLKSAAES SGEIESPIAR
FVKDLVADAR AVELLKALFE TKLWVLNEGE GAFYGPKIDV EVCDSMGRSH QLGTTQLDFN
LPQRFDLKYA EKAKDSASQS DVNRPIMVHR AILGSIERCV GILTEHYDGG KSWPLWMSPR
QIMVVPISKH HFEYAAKVQR VLKFPELFHS QEAFVSAASD EADIDLNRCA LDDGEFADSP
GFYCDVDLTD NKLDKKIRNA QQSYYNFILV VGREEAENGC VNVRSRENKQ LGMKTVGEVI
QKLHKLRKEF WRSQSVPGWE
//
