SYT_METBF
ID SYT_METBF Reviewed; 635 AA.
AC Q467V2;
DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT 13-SEP-2005, sequence version 1.
DT 03-AUG-2022, entry version 121.
DE RecName: Full=Threonine--tRNA ligase {ECO:0000255|HAMAP-Rule:MF_00184};
DE EC=6.1.1.3 {ECO:0000255|HAMAP-Rule:MF_00184};
DE AltName: Full=Threonyl-tRNA synthetase {ECO:0000255|HAMAP-Rule:MF_00184};
DE Short=ThrRS {ECO:0000255|HAMAP-Rule:MF_00184};
GN Name=thrS {ECO:0000255|HAMAP-Rule:MF_00184}; OrderedLocusNames=Mbar_A2945;
OS Methanosarcina barkeri (strain Fusaro / DSM 804).
OC Archaea; Euryarchaeota; Stenosarchaea group; Methanomicrobia;
OC Methanosarcinales; Methanosarcinaceae; Methanosarcina.
OX NCBI_TaxID=269797;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Fusaro / DSM 804;
RX PubMed=16980466; DOI=10.1128/jb.00810-06;
RA Maeder D.L., Anderson I., Brettin T.S., Bruce D.C., Gilna P., Han C.S.,
RA Lapidus A., Metcalf W.W., Saunders E., Tapia R., Sowers K.R.;
RT "The Methanosarcina barkeri genome: comparative analysis with
RT Methanosarcina acetivorans and Methanosarcina mazei reveals extensive
RT rearrangement within methanosarcinal genomes.";
RL J. Bacteriol. 188:7922-7931(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:0000255|HAMAP-
CC Rule:MF_00184}.
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:0000255|HAMAP-Rule:MF_00184};
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_00184};
CC Note=Binds 1 zinc ion per subunit. {ECO:0000255|HAMAP-Rule:MF_00184};
CC -!- SUBUNIT: Homodimer. {ECO:0000255|HAMAP-Rule:MF_00184}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00184}.
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:0000255|HAMAP-Rule:MF_00184}.
CC -!- SIMILARITY: Belongs to the class-II aminoacyl-tRNA synthetase family.
CC {ECO:0000255|HAMAP-Rule:MF_00184}.
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DR EMBL; CP000099; AAZ71840.1; -; Genomic_DNA.
DR RefSeq; WP_011307881.1; NC_007355.1.
DR AlphaFoldDB; Q467V2; -.
DR SMR; Q467V2; -.
DR STRING; 269797.Mbar_A2945; -.
DR PRIDE; Q467V2; -.
DR EnsemblBacteria; AAZ71840; AAZ71840; Mbar_A2945.
DR GeneID; 3626144; -.
DR KEGG; mba:Mbar_A2945; -.
DR eggNOG; arCOG00401; Archaea.
DR HOGENOM; CLU_029833_0_0_2; -.
DR OMA; DAHIFML; -.
DR OrthoDB; 11656at2157; -.
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 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; 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; RNA-binding; tRNA-binding; Zinc.
FT CHAIN 1..635
FT /note="Threonine--tRNA ligase"
FT /id="PRO_1000020426"
FT REGION 1..144
FT /note="Editing domain"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00184"
FT REGION 215..514
FT /note="Catalytic"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00184"
FT BINDING 307
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00184"
FT BINDING 359
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00184"
FT BINDING 483
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00184"
SQ SEQUENCE 635 AA; 73105 MW; 163E72F138EC7425 CRC64;
MQLLLIHSDY IEYETKKQTP VAEKIEESLK SCRLEEALTA FMAVESVDEA NPEETIEKTV
FEIEKVATQV KTDRIMLYPY AHLSSDLSSP KVAVKVFKGI ETALSGKYEV KRAPFGWYKA
FSISCKGHPL SELSRSIRPE GTQRAAGKVE AGKEKEEVVS EALKAEDTAK SYWRILTPDG
ELREIENFDL TPYPKLQQFV DYEISKSRAV ERAPPHVELM RRLELADYEP GSDSGNMRYY
PKGRLIKALL ENYVLDVATD FGAMEVETPI MYDMNHPTLK KYLDRFPARQ YSIESDKRQM
FLRFAACFGQ FLMNHDMTIS YRNLPLRMIE MTRYSFRKEQ RGELVGLRRL RAFTMPDMHS
LCEDMDQAVD QFKKQYDLCI DVLENIGIHI KDYEVAIRFT KDFYESNKEL IVNMARTVNK
PVLVEMWDTR FFYFVLKFEF NFVDALAKAS ALSTVQIDVE NAERYDISYV NADGKLERPT
VLHCSPSGAI ERCIYALLEK AAMETEEGKV PMLPVWLSPT QVRIVPISEK HVAFAEEVSQ
KLDCRVDIDD RDLSIGKKVR EAGREWVPYV VVIGDKEIED GTINVTIRAE SEQKKPKKVQ
ITPEELNDRI KGEIAGKPYR KLPLSKHLSG RPKFV
