ID A0A1V4AH60_9BACT Unreviewed; 619 AA. AC A0A1V4AH60; DT 07-JUN-2017, integrated into UniProtKB/TrEMBL. DT 07-JUN-2017, sequence version 1. DT 03-AUG-2022, entry version 21. DE RecName: Full=Threonine--tRNA ligase {ECO:0000256|HAMAP-Rule:MF_00184}; DE EC=6.1.1.3 {ECO:0000256|HAMAP-Rule:MF_00184}; DE AltName: Full=Threonyl-tRNA synthetase {ECO:0000256|HAMAP-Rule:MF_00184}; DE Short=ThrRS {ECO:0000256|HAMAP-Rule:MF_00184}; GN Name=thrS {ECO:0000256|HAMAP-Rule:MF_00184}; GN ORFNames=B0D78_11010 {ECO:0000313|EMBL:OON86935.1}; OS Pyramidobacter sp. C12-8. OC Bacteria; Synergistetes; Synergistia; Synergistales; Synergistaceae; OC Pyramidobacter; unclassified Pyramidobacter. OX NCBI_TaxID=1943580 {ECO:0000313|EMBL:OON86935.1, ECO:0000313|Proteomes:UP000190264}; RN [1] {ECO:0000313|EMBL:OON86935.1, ECO:0000313|Proteomes:UP000190264} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=C12-8 {ECO:0000313|EMBL:OON86935.1, RC ECO:0000313|Proteomes:UP000190264}; RA Kang S.; RT "Fluoroacetate degrading rumen bacteria."; RL Submitted (JAN-2017) to the EMBL/GenBank/DDBJ databases. 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:0000256|ARBA:ARBA00000070, ECO:0000256|HAMAP- CC Rule:MF_00184}; CC -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|HAMAP-Rule:MF_00184}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|HAMAP-Rule:MF_00184}; CC -!- SUBUNIT: Homodimer. {ECO:0000256|HAMAP-Rule:MF_00184}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00184}. CC -!- SIMILARITY: Belongs to the class-II aminoacyl-tRNA synthetase family. CC {ECO:0000256|HAMAP-Rule:MF_00184}. CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ CC whole genome shotgun (WGS) entry which is preliminary data. CC {ECO:0000313|EMBL:OON86935.1}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; MUHX01000035; OON86935.1; -; Genomic_DNA. DR STRING; 1943580.B0D78_11010; -. DR EnsemblBacteria; OON86935; OON86935; B0D78_11010. DR Proteomes; UP000190264; Unassembled WGS sequence. 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 {ECO:0000256|ARBA:ARBA00023146, KW ECO:0000256|HAMAP-Rule:MF_00184}; KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|HAMAP- KW Rule:MF_00184}; Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00184}; KW Ligase {ECO:0000256|ARBA:ARBA00022598, ECO:0000256|HAMAP-Rule:MF_00184}; KW Metal-binding {ECO:0000256|HAMAP-Rule:MF_00184}; KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|HAMAP- KW Rule:MF_00184}; KW Protein biosynthesis {ECO:0000256|ARBA:ARBA00022917, ECO:0000256|HAMAP- KW Rule:MF_00184}; KW RNA-binding {ECO:0000256|ARBA:ARBA00022884, ECO:0000256|HAMAP- KW Rule:MF_00184}; KW tRNA-binding {ECO:0000256|ARBA:ARBA00022555, ECO:0000256|HAMAP- KW Rule:MF_00184}; Zinc {ECO:0000256|HAMAP-Rule:MF_00184}. FT DOMAIN 1..37 FT /note="TGS" FT /evidence="ECO:0000259|PROSITE:PS51880" FT DOMAIN 241..508 FT /note="AA_TRNA_LIGASE_II" FT /evidence="ECO:0000259|PROSITE:PS50862" FT REGION 217..508 FT /note="Catalytic" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00184" FT BINDING 308 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_note="catalytic" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00184" FT BINDING 359 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_note="catalytic" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00184" FT BINDING 485 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_note="catalytic" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00184" SQ SEQUENCE 619 AA; 71484 MW; F609256ACB25EE70 CRC64; MLANWKLNKG AVAAFVDGEE KDLDVVVDHD AEVKPITPET EEGIEIVRHS TAHLLAEAVM NLYPAAKVAI GPTIKDGFYY DIEFPETVSE EILPALEKEM RRIAKRSIPL RRERVGVADA IKLFKERNDP YKVEILEGVG DETVNLYWQD DYVDLCRGPH VPNTRFLKHF KLLSMAGAYW RGDEHNIMLT RIYGTAFNTQ EELDAYITRM EEARRRDHRK LGRELDLFSL HNEGVGFPFF HPKGMVVMNK LMSFWRRLHF LNGYSEARTP QILNRDLWLQ SGHWDHYREN MYFTTIDDIP HAIKPMNCPG GIIIYKTSKH SYRELPIRMG ELGVVHRHEL SGALHGLMRV RCFTQDDAHH FCTPEQIKDE VKLIMKLEDY VYTHVFGFKY HVELSTRPEN SMGSDELWEI AENALRETLE ETGTPYVLNP GDGAFYGPKI DFHLEDCIGR TWQCGTIQLD FTMPEKFDMT YVGADGKEHR PVMLHRTILG SIERFMGILI ENYAGAFPYW LAPVQVKLLA VSDDHLSYAR EVAEKLQDLN VRVEIDRRDE KLGRKIRDAQ MEKVPYMLVI GDKEVEARTV AVRDRAKGDL GSMDFAAFTG LLAEQYDPEK ENFRVRLGQ //