SYT_ARTS2
ID SYT_ARTS2 Reviewed; 669 AA.
AC A0JXC7;
DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT 12-DEC-2006, sequence version 1.
DT 03-AUG-2022, entry version 95.
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=Arth_2317;
OS Arthrobacter sp. (strain FB24).
OC Bacteria; Actinobacteria; Micrococcales; Micrococcaceae; Arthrobacter.
OX NCBI_TaxID=290399;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=FB24;
RX PubMed=24501649; DOI=10.4056/sigs.4438185;
RA Nakatsu C.H., Barabote R., Thompson S., Bruce D., Detter C., Brettin T.,
RA Han C., Beasley F., Chen W., Konopka A., Xie G.;
RT "Complete genome sequence of Arthrobacter sp. strain FB24.";
RL Stand. Genomic Sci. 9:106-116(2013).
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; CP000454; ABK03697.1; -; Genomic_DNA.
DR RefSeq; WP_011692161.1; NC_008541.1.
DR AlphaFoldDB; A0JXC7; -.
DR SMR; A0JXC7; -.
DR STRING; 290399.Arth_2317; -.
DR EnsemblBacteria; ABK03697; ABK03697; Arth_2317.
DR KEGG; art:Arth_2317; -.
DR eggNOG; COG0441; Bacteria.
DR HOGENOM; CLU_008554_3_1_11; -.
DR OMA; FYYDFAY; -.
DR OrthoDB; 900765at2; -.
DR Proteomes; UP000000754; 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; IPR004095; TGS.
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.
DR PROSITE; PS51880; TGS; 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..669
FT /note="Threonine--tRNA ligase"
FT /id="PRO_1000020338"
FT DOMAIN 3..60
FT /note="TGS"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01228"
FT REGION 260..566
FT /note="Catalytic"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00184"
FT BINDING 365
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00184"
FT BINDING 416
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00184"
FT BINDING 543
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00184"
SQ SEQUENCE 669 AA; 74930 MW; 21BE16FDEBC45439 CRC64;
MSDAQQITLI VDGEETKVTT GTTGAELFFE RRDVVVARVN GELKDLDQPL PEGADIEGVT
IDSPDGLNVL RHSTAHVMAQ AVQQLRPDAK LGIGPYITDG FYFDFDVAEP FTPEDLKALE
KMMLKIINQN QKFVRRVVSE DEAREAMKNE PYKLELLGKK NNAADAGEGV NVEVGAGDIT
IYDNVDRKSG DSVWCDLCRG PHLPNTKLIS NAFALTRSSA AYWLGNQNNQ QLQRIYGTAW
PTKDALKAYQ ERIAEAERRD HRKLGAELDL FSFPDELGSG LPVFHPKGGI IRKAMEDYSR
QRHVDAGYDF VYTPHITKGH LYEVSGHLDW YKEGMFPAMH IDAELNEDGT VRKPGQDYYL
KPMNCPMHNL IFRSRGRSYR ELPLRLFEFG SVYRYEKSGV VHGLTRVRGM TQDDAHIYCT
REQMKDELTT TLNFVLGLLK DYGLDDFYLE LSTKNEDKFV GDDATWDEAT RTLAEVAEAS
GLELIPDPGG AAFYGPKISV QAKDALGRTW QMSTIQLDFN LPERFELEFQ AADGTRQRPV
MIHRALFGSV ERFMGVLTEH YAGAFPAWLA PVQVVGIPVA EAFNDYMFDV VDQLKAVGIR
AEVDISSDRF PKKIRTASKD KIPFVLIAGG EDAEAGAVSF RFRDGSQDNG VPVAEAVQRI
VEAVRNRTS
