ID SYT_ANADE Reviewed; 650 AA. AC Q2IJC0; DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot. DT 07-MAR-2006, sequence version 1. DT 16-JUN-2009, entry version 28. DE RecName: Full=Threonyl-tRNA synthetase; DE EC=6.1.1.3; DE AltName: Full=Threonine--tRNA ligase; DE Short=ThrRS; GN Name=thrS; OrderedLocusNames=Adeh_1982; OS Anaeromyxobacter dehalogenans (strain 2CP-C). OC Bacteria; Proteobacteria; Deltaproteobacteria; Myxococcales; OC Cystobacterineae; Myxococcaceae; Anaeromyxobacter. OX NCBI_TaxID=290397; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina T., RA Hammon N., Israni S., Pitluck S., Brettin T., Bruce D., Han C., RA Tapia R., Gilna P., Kiss H., Schmutz J., Larimer F., Land M., RA Kyrpides N., Anderson I., Sanford R.A., Ritalahti K.M., Thomas H.S., RA Kirby J.R., Zhulin I.B., Loeffler F.E., Richardson P.; RT "Complete sequence of Anaeromyxobacter dehalogenans 2CP-C."; RL Submitted (JAN-2006) to the EMBL/GenBank/DDBJ databases. CC -!- CATALYTIC ACTIVITY: ATP + L-threonine + tRNA(Thr) = AMP + CC diphosphate + L-threonyl-tRNA(Thr). CC -!- COFACTOR: Binds 1 zinc ion per subunit (By similarity). CC -!- SUBUNIT: Homodimer (By similarity). CC -!- SUBCELLULAR LOCATION: Cytoplasm. CC -!- SIMILARITY: Belongs to the class-II aminoacyl-tRNA synthetase CC family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP000251; ABC81753.1; -; Genomic_DNA. DR RefSeq; YP_465190.1; -. DR GeneID; 3887205; -. DR GenomeReviews; CP000251_GR; Adeh_1982. DR KEGG; ade:Adeh_1982; -. DR HOGENOM; Q2IJC0; -. DR OMA; Q2IJC0; NTKIAIG. DR BioCyc; ADEH290397:ADEH_1982-MON; -. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005524; F:ATP binding; IEA:HAMAP. DR GO; GO:0004829; F:threonine-tRNA ligase activity; IEA:HAMAP. DR GO; GO:0008270; F:zinc ion binding; IEA:UniProtKB-KW. DR GO; GO:0006435; P:threonyl-tRNA aminoacylation; IEA:HAMAP. DR HAMAP; MF_00184; -; 1. DR InterPro; IPR002314; aa-tRNA-synt_IIb_cons-reg. DR InterPro; IPR006195; aa-tRNA-synth_II_cons-reg. DR InterPro; IPR004154; Anticodon_bd. DR InterPro; IPR012675; b-grasp_ferredoxin-like. DR InterPro; IPR004095; TGS. DR InterPro; IPR002320; Thr-tRNA-synth_IIa. DR InterPro; IPR018158; Thr-tRNA-synth_IIa_cons-reg. DR InterPro; IPR012947; tRNA_SAD. DR Gene3D; G3DSA:3.40.50.800; Anticodon_bd; 1. DR Gene3D; G3DSA:3.10.20.30; Ferredoxin_fold; 1. DR Pfam; PF03129; HGTP_anticodon; 1. DR Pfam; PF02824; TGS; 1. DR Pfam; PF00587; tRNA-synt_2b; 1. DR Pfam; PF07973; tRNA_SAD; 1. DR PRINTS; PR01047; TRNASYNTHTHR. DR TIGRFAMs; TIGR00418; thrS; 1. DR PROSITE; PS50862; AA_TRNA_LIGASE_II; 1. PE 3: Inferred from homology; KW Aminoacyl-tRNA synthetase; ATP-binding; Complete proteome; Cytoplasm; KW Ligase; Metal-binding; Nucleotide-binding; Protein biosynthesis; Zinc. FT CHAIN 1 650 Threonyl-tRNA synthetase. FT /FTId=PRO_1000020336. FT REGION 248 548 Catalytic. FT METAL 349 349 Zinc; catalytic (By similarity). FT METAL 400 400 Zinc; catalytic (By similarity). FT METAL 525 525 Zinc; catalytic (By similarity). SQ SEQUENCE 650 AA; 72874 MW; 8D12CC9FDCAECD33 CRC64; MSDLVKVTLP DGSQKEAPRG TPVIDFVKGQ IGAGLAKAAY FAKLDGAPVD LSRALDRDAR LEIVTTRSPE ALEVARHDAA HVMASVVQKL YPGTQVTIGP AIEDGFYYDF ARETPFTPED LEKIEKATNE AIKADLPFVR SEISMEAALA LFEGMGERYK VEIVKDIAAK GAKTLTLYKH GDWVDFCLGP HGPSTGRIGV VKLLNVAGAY WRGDAKNAML QRIYGTAFFD KKELDAHLAK LEEVKKRDHR RLGPQLGLFT FHEYAPGAPF WLPAGTVLYN VLEDAMRRLV LKNGYQEVKT PLLFNKRLWE TSGHWGKYRE NMFLVVDSES DPALALEDRC SFSLKPMNCP SHHLIYRMDK RSYRELPVRY FTTDALHRNE ASGSLGGLTR VRQFEQDDAH IYLREEQVTD EVLRIFELMK VVYGAFGLGF EATFSTRPEQ RIGDDALWDR AEALLRKSLD ATGLKWTLNP GDGAFYGPKI DMLVTDSLGR RWQTCTIQLD YAAPERFDLT FVGEDNKEHR PVVIHRAIYG SFERFIAILT EHYAGAFPAW LAPVQARVVT VSDRFDAWAR EAAAALQARG WRVEVDGSSD KLGAKIRNAQ LAKIPFTLVV GEKEVEARGV SPRRHGGEDL KTMPLETFAE LMAREATAPF //