SYT_CENSY
ID SYT_CENSY Reviewed; 615 AA.
AC A0RU76;
DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT 09-JAN-2007, sequence version 1.
DT 03-AUG-2022, entry version 79.
DE RecName: Full=Threonine--tRNA ligase;
DE EC=6.1.1.3;
DE AltName: Full=Threonyl-tRNA synthetase;
DE Short=ThrRS;
GN Name=thrS; OrderedLocusNames=CENSYa_0251;
OS Cenarchaeum symbiosum (strain A).
OC Archaea; Thaumarchaeota; Cenarchaeales; Cenarchaeaceae; Cenarchaeum.
OX NCBI_TaxID=414004;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=A;
RX PubMed=17114289; DOI=10.1073/pnas.0608549103;
RA Hallam S.J., Konstantinidis K.T., Putnam N., Schleper C., Watanabe Y.,
RA Sugahara J., Preston C., de la Torre J., Richardson P.M., DeLong E.F.;
RT "Genomic analysis of the uncultivated marine crenarchaeote Cenarchaeum
RT symbiosum.";
RL Proc. Natl. Acad. Sci. U.S.A. 103:18296-18301(2006).
CC -!- FUNCTION: Catalyzes the attachment of threonine to tRNA(Thr) in a two-
CC step reaction: L-threonine is first activated by ATP to form Thr-AMP
CC and then transferred to the acceptor end of tRNA(Thr). Also edits
CC incorrectly charged L-seryl-tRNA(Thr). {ECO:0000250|UniProtKB:Q9UZ14}.
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:0000250|UniProtKB:Q9UZ14};
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000250|UniProtKB:Q9UZ14};
CC Note=Binds 1 zinc ion per subunit. {ECO:0000250|UniProtKB:Q9UZ14};
CC -!- SUBUNIT: Homodimer. {ECO:0000250|UniProtKB:Q9UZ14}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q9UZ14}.
CC -!- DOMAIN: The N-terminal domain is an archaea-specific tRNA-editing
CC domain that hydrolyzes incorrectly charged L-seryl-tRNA(Thr). Catalysis
CC of tRNA editing is performed by the charged tRNA itself.
CC {ECO:0000250|UniProtKB:Q9UZ14}.
CC -!- SIMILARITY: Belongs to the class-II aminoacyl-tRNA synthetase family.
CC {ECO:0000305}.
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DR EMBL; DP000238; ABK76893.1; -; Genomic_DNA.
DR AlphaFoldDB; A0RU76; -.
DR SMR; A0RU76; -.
DR STRING; 414004.CENSYa_0251; -.
DR EnsemblBacteria; ABK76893; ABK76893; CENSYa_0251.
DR KEGG; csy:CENSYa_0251; -.
DR PATRIC; fig|414004.10.peg.218; -.
DR HOGENOM; CLU_029833_0_0_2; -.
DR OMA; DAHIFML; -.
DR Proteomes; UP000000758; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0002161; F:aminoacyl-tRNA editing activity; IEA:UniProt.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0004829; F:threonine-tRNA ligase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0000049; F:tRNA binding; IEA:UniProtKB-KW.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0006435; P:threonyl-tRNA aminoacylation; IEA:UniProtKB-UniRule.
DR Gene3D; 3.30.930.10; -; 1.
DR Gene3D; 3.40.50.800; -; 1.
DR Gene3D; 3.50.80.10; -; 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; IPR023509; DTD-like_sf.
DR InterPro; IPR002320; Thr-tRNA-ligase_IIa.
DR InterPro; IPR015011; Threonyl-tRNA_syn_edit_dom_arc.
DR PANTHER; PTHR11451; PTHR11451; 1.
DR Pfam; PF03129; HGTP_anticodon; 1.
DR Pfam; PF00587; tRNA-synt_2b; 1.
DR Pfam; PF08915; tRNA-Thr_ED; 1.
DR PRINTS; PR01047; TRNASYNTHTHR.
DR SUPFAM; SSF55681; SSF55681; 1.
DR TIGRFAMs; TIGR00418; thrS; 1.
DR PROSITE; PS50862; AA_TRNA_LIGASE_II; 1.
PE 3: Inferred from homology;
KW Aminoacyl-tRNA synthetase; ATP-binding; Cytoplasm; Ligase; Metal-binding;
KW Nucleotide-binding; Protein biosynthesis; Reference proteome; RNA-binding;
KW tRNA-binding; Zinc.
FT CHAIN 1..615
FT /note="Threonine--tRNA ligase"
FT /id="PRO_1000020364"
FT REGION 1..132
FT /note="Editing domain"
FT /evidence="ECO:0000250|UniProtKB:Q9UZ14"
FT REGION 196..495
FT /note="Catalytic"
FT /evidence="ECO:0000250|UniProtKB:Q9UZ14"
FT BINDING 288
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250|UniProtKB:Q9UZ14"
FT BINDING 340
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250|UniProtKB:Q9UZ14"
FT BINDING 464
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250|UniProtKB:Q9UZ14"
SQ SEQUENCE 615 AA; 68543 MW; 641D0C62C6CA4CAF CRC64;
MRILQLHCDR IEYSPVKKEI AAAEEPATGG KLEDAVLAFV AVEKGDGPGE AARAAAELRQ
ALGRIGCKKL LIYPYAHLSS TLAAPSIALG LISEMEAALH DLEVSRAPFG WTKSYTISVK
GHPLAEGFKV ITGDARGTGA PKALESESSM KSTWHVLTPD GNMTDASEFD FAGCPKLKAL
ARYEASKKRG TDEPPPHVAL MKRMGIADYE PASDAGNMKF FPNGRLIKSL IERYVTERVV
EYGGYEVETP IMYDSNHPSM VSYFNRFPAR QYSIDSEGKS LFLRFAACFG QFLMAGDYQL
SYKNLPFRLY ELTRYSFRRE QSGELVGLRR LRAFTMPDCH AFCTDMAQAV REAGVRFELS
RDVIGQLGLD AADYEMAIRL TEEFYAENGG AVREMVRRHG RPVLVEMWKE RFFYFVLKWE
FNYIDGAGKA SALSTDQIDV ENGKRYGIEF VDENNGRQHP VILHNSPSGA IERVIYTLLE
KAAADSARGT KPELPLWLSP VQARIIPVGE ELVRNATELA KEMAGHGIRA DVDDRNESMG
KRIREAEKEW VRYILVVGEK EAASGRLSVR DRRTGKSTEM GLDDLVEAVR EQTAGKPSAG
LNSPFYLSKR PQVML
