SYT_METMA
ID SYT_METMA Reviewed; 634 AA.
AC Q8PRY4;
DT 29-AUG-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2002, sequence version 1.
DT 03-AUG-2022, entry version 128.
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=MM_3304;
OS Methanosarcina mazei (strain ATCC BAA-159 / DSM 3647 / Goe1 / Go1 / JCM
OS 11833 / OCM 88) (Methanosarcina frisia).
OC Archaea; Euryarchaeota; Stenosarchaea group; Methanomicrobia;
OC Methanosarcinales; Methanosarcinaceae; Methanosarcina.
OX NCBI_TaxID=192952;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-159 / DSM 3647 / Goe1 / Go1 / JCM 11833 / OCM 88;
RX PubMed=12125824;
RA Deppenmeier U., Johann A., Hartsch T., Merkl R., Schmitz R.A.,
RA Martinez-Arias R., Henne A., Wiezer A., Baeumer S., Jacobi C.,
RA Brueggemann H., Lienard T., Christmann A., Boemecke M., Steckel S.,
RA Bhattacharyya A., Lykidis A., Overbeek R., Klenk H.-P., Gunsalus R.P.,
RA Fritz H.-J., Gottschalk G.;
RT "The genome of Methanosarcina mazei: evidence for lateral gene transfer
RT between Bacteria and Archaea.";
RL J. Mol. Microbiol. Biotechnol. 4:453-461(2002).
RN [2]
RP FUNCTION IN AMINOACYLATION AND EDITING, DOMAIN, AND MUTAGENESIS OF
RP 125-CYS--ARG-135.
RX PubMed=15079065; DOI=10.1073/pnas.0401530101;
RA Beebe K., Merriman E., Ribas De Pouplana L., Schimmel P.;
RT "A domain for editing by an archaebacterial tRNA synthetase.";
RL Proc. Natl. Acad. Sci. U.S.A. 101:5958-5963(2004).
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) (Probable). Edits
CC incorrectly charged L-seryl-tRNA(Thr) probably via its editing domain
CC (tested with total bovine tRNA) (PubMed:15079065). Activates L-serine,
CC but does not detectably transfer it to tRNA (tested with total bovine
CC tRNA) (PubMed:15079065). {ECO:0000269|PubMed:15079065}.
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 (approximately residues 1-142) is an
CC archaea-specific tRNA-editing domain that hydrolyzes incorrectly
CC charged L-seryl-tRNA(Thr) (PubMed:15079065). Catalysis of tRNA editing
CC is performed by the charged tRNA itself. {ECO:0000255|HAMAP-
CC Rule:MF_00184, ECO:0000305|PubMed:15079065}.
CC -!- SIMILARITY: Belongs to the class-II aminoacyl-tRNA synthetase family.
CC {ECO:0000255|HAMAP-Rule:MF_00184}.
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DR EMBL; AE008384; AAM33000.1; -; Genomic_DNA.
DR RefSeq; WP_011035193.1; NC_003901.1.
DR AlphaFoldDB; Q8PRY4; -.
DR SMR; Q8PRY4; -.
DR STRING; 192952.MM_3304; -.
DR EnsemblBacteria; AAM33000; AAM33000; MM_3304.
DR GeneID; 44086951; -.
DR KEGG; mma:MM_3304; -.
DR PATRIC; fig|192952.21.peg.3838; -.
DR eggNOG; arCOG00401; Archaea.
DR HOGENOM; CLU_029833_0_0_2; -.
DR OMA; DAHIFML; -.
DR Proteomes; UP000000595; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0002161; F:aminoacyl-tRNA editing activity; IDA:UniProtKB.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0004829; F:threonine-tRNA ligase activity; IDA:UniProtKB.
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; IDA:UniProtKB.
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 1: Evidence at protein level;
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..634
FT /note="Threonine--tRNA ligase"
FT /id="PRO_0000101103"
FT REGION 1..142
FT /note="Editing domain"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00184,
FT ECO:0000305|PubMed:15079065"
FT REGION 214..513
FT /note="Catalytic"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00184"
FT BINDING 306
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00184"
FT BINDING 358
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00184"
FT BINDING 482
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00184"
FT MUTAGEN 125..135
FT /note="CKGHPLSELSR->AAASAAASAAA: Aminoacylates with L-
FT threonine, still misactivates L-serine, no longer edits
FT mischarged L-seryl-tRNA(Thr)."
FT /evidence="ECO:0000269|PubMed:15079065"
SQ SEQUENCE 634 AA; 72765 MW; C8A257D2E0F21C67 CRC64;
MQLLLIHSDY IEYETKKQTP VAEKIEESLK SGRLEEALTA FTAVESVDEA NPEEAIKKAV
SEIEKVAAQV KTNRIMLYPY AHLSSDLSSP KVAVQVLKGM EAALSSRYEV KRAPFGWYKA
FTVSCKGHPL SELSRSIRPE GAAKAEVKTE TCEKEEVVSE ALKAEGTARS YWRILTPDGE
LHEVEGFDLT PYPKLQQFVN YEISKSRAVE RAPPHVELMR RLELADYEPG SDSGNMRYYP
KGRLVKSLLE NYVLDVATEF GAMEVETPLM YDMNHPTLKK YLDRFPARQY SIESDKRHMF
LRFAACFGQF LMNHDMTISY KNLPLRMIEM TRYSFRKEQR GELVGLRRLR AFTMPDMHTL
CEDMDQAVNQ FKEQYDLCIS VLENVGIHIN DYEVAIRFTR DFYEANKDLV VNMAKTVNKP
VLVEMWDTRF FYFVLKFEFN FVDALAKASA LSTVQIDVEN AERYDISYVN ADGKLERPTV
LHCSPSGAIE RCIYALLEKA AMETEEGKVP MLPVWLSPTQ VRIVPISEKH IAFAEEVAKK
LDFRVDVDDR DLSIGKKVRE AGREWVPYVV VIGDKEMEES TINVTIREES GQDKPKKVQM
TPEELNARIK EETSGKPYRK LPLAKYLSAR PKFL
