SYT_PARMW
ID SYT_PARMW Reviewed; 611 AA.
AC Q7U662;
DT 30-AUG-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2003, sequence version 1.
DT 03-AUG-2022, entry version 114.
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=SYNW1478;
OS Parasynechococcus marenigrum (strain WH8102).
OC Bacteria; Cyanobacteria; Synechococcales; Prochlorococcaceae;
OC Parasynechococcus; Parasynechococcus marenigrum.
OX NCBI_TaxID=84588;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=WH8102;
RX PubMed=12917641; DOI=10.1038/nature01943;
RA Palenik B., Brahamsha B., Larimer F.W., Land M.L., Hauser L., Chain P.,
RA Lamerdin J.E., Regala W., Allen E.E., McCarren J., Paulsen I.T.,
RA Dufresne A., Partensky F., Webb E.A., Waterbury J.;
RT "The genome of a motile marine Synechococcus.";
RL Nature 424:1037-1042(2003).
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 -!- SIMILARITY: Belongs to the class-II aminoacyl-tRNA synthetase family.
CC {ECO:0000255|HAMAP-Rule:MF_00184}.
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DR EMBL; BX569693; CAE07993.1; -; Genomic_DNA.
DR RefSeq; WP_011128342.1; NC_005070.1.
DR AlphaFoldDB; Q7U662; -.
DR SMR; Q7U662; -.
DR STRING; 84588.SYNW1478; -.
DR EnsemblBacteria; CAE07993; CAE07993; SYNW1478.
DR KEGG; syw:SYNW1478; -.
DR eggNOG; COG0441; Bacteria.
DR HOGENOM; CLU_008554_0_1_3; -.
DR OMA; DAHIFML; -.
DR OrthoDB; 900765at2; -.
DR Proteomes; UP000001422; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
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:0006435; P:threonyl-tRNA aminoacylation; IEA:UniProtKB-UniRule.
DR CDD; cd00771; ThrRS_core; 1.
DR Gene3D; 3.30.930.10; -; 1.
DR Gene3D; 3.40.50.800; -; 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; IPR002320; Thr-tRNA-ligase_IIa.
DR InterPro; IPR018163; Thr/Ala-tRNA-synth_IIc_edit.
DR InterPro; IPR033728; ThrRS_core.
DR InterPro; IPR012947; tRNA_SAD.
DR PANTHER; PTHR11451; PTHR11451; 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; SSF55186; SSF55186; 1.
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..611
FT /note="Threonine--tRNA ligase"
FT /id="PRO_0000101071"
FT REGION 1..25
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 209..502
FT /note="Catalytic"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00184"
FT BINDING 302
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00184"
FT BINDING 353
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00184"
FT BINDING 479
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00184"
SQ SEQUENCE 611 AA; 69160 MW; FEE3507F015B3AA6 CRC64;
MAGPDRKPVS SAAATTPAPS APVVLPKTSE SSQLLKIRHS MSHVMAMAVQ QLFPKARVTI
GPWTESGFYY DFDNPDPFTE ADLKAIKKGM IKIINKKVPL ERVEVTRAEA ETKIKAQNEP
YKLEILEGLQ DPITLYTLGE DWWDLCAGPH VEHTGQLNAK AFELESVAGA YWRGDETKAQ
LHRIYGTAWE TPEQLAEHKR RKEEALRRDH RRIGKDLDLF SIEDEAGAGL VFWHPRGARM
RLLIEEFWRQ AHFEGGYELL YTPHVADISL WKTSGHLDFY AESMFGPMEV DEREYQLKPM
NCPFHVLTYA SKLRSYRELP IRWAELGTVY RYERPGVMHG LMRVRGFTQD DAHVFCLPEQ
ISDEILKILD LTERILSTFD FNTYEINLST RPEKSIGDDA VWDLATKGLI EALERKGWKY
KIDEGGGAFY GPKIDLKIED AIGRMWQCST IQLDFNLPER FKLDYVAADG SKQRPIMIHR
AIFGSLERFF GIMTENYAGD YPFWLAPEQV RLLPVTDEVQ PYAESLLDQL TQAGVRATID
RSGDRLGKLI RTGEQMKIPV LAVIGAKEAE QNAVSLRSRR DGDLGVAAVA DLLRAAESAN
SQRAAGLGLN G
