ID   SYT_ALHEH               Reviewed;         641 AA.
AC   Q0AAL5;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   17-OCT-2006, sequence version 1.
DT   16-JUN-2009, entry version 24.
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=Mlg_0768;
OS   Alkalilimnicola ehrlichei (strain MLHE-1).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Chromatiales;
OC   Ectothiorhodospiraceae; Alkalilimnicola.
OX   NCBI_TaxID=187272;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA   Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H.,
RA   Pitluck S., Sims D., Brettin T., Bruce D., Han C., Tapia R., Gilna P.,
RA   Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N.,
RA   Mikhailova N., Oremland R.S., Hoeft S.E., Switzer-Blum J., Kulp T.,
RA   King G., Tabita R., Witte B., Santini J.M., Basu P., Hollibaugh J.T.,
RA   Xie G., Stolz J.F., Richardson P.;
RT   "Complete sequence of Alkalilimnicola ehrilichei MLHE-1.";
RL   Submitted (AUG-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.
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DR   EMBL; CP000453; ABI56122.1; -; Genomic_DNA.
DR   RefSeq; YP_741612.1; -.
DR   GeneID; 4268582; -.
DR   GenomeReviews; CP000453_GR; Mlg_0768.
DR   KEGG; aeh:Mlg_0768; -.
DR   NMPDR; fig|187272.6.peg.737; -.
DR   HOGENOM; Q0AAL5; -.
DR   OMA; Q0AAL5; QDEAPGM.
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    641       Threonyl-tRNA synthetase.
FT                                /FTId=PRO_1000020335.
FT   REGION      242    533       Catalytic.
FT   METAL       333    333       Zinc; catalytic (By similarity).
FT   METAL       384    384       Zinc; catalytic (By similarity).
FT   METAL       510    510       Zinc; catalytic (By similarity).
SQ   SEQUENCE   641 AA;  73783 MW;  0024C284EDA6ADA7 CRC64;
     MPAITLPDGS RREFDHPVTV RDVAESIGKG LARAALAGRV DGRLVDLSHR IDDDVQLEIV
     TDRDPDGVDM IRHSTAHLMA QAVKELFPEA QVTIGPVIEN GFYYDFAYKR PFTEDDLKAI
     EKKMEELARQ DFEVHREVWD RDEAIRFFLE QGEQYKAEII EDLPEHETIS VYKQGDFLDL
     CRGPHVPNTG KLKAFKLQKV AGAYWRGKSD NEMLQRIYGT AWPDKKQLKA YLHRLAEAEK
     RDHRRIGRAQ NLFHLQEEAP GMAFWHPKGW QIYLEVQEYI RRLTRGHGYQ EIHTPQLVDR
     SLWEKSGHWD KFQDNMFITE SESRDYAVKP MNCPCHVQVY NQGLKSYRDL PLRLAEFGSC
     HRNEPSGTLH GLMRVRNFVQ DDAHIFCTED QIQQEVADFI DLVFKAYNDF GFDDVIIALS
     TRPDERVGED ALWDKAEHAL EEALNRAGLE WQLQPGEGAF YGPKIEFTLK DCLGRTWQLG
     TIQVDFSMPG RLGATYVAED GSKKVPVMLH RAILGSLERF IGILIEHYAG ALPPWLAPVQ
     AVVLNITDRQ GEYARRIEKR FRERGLRVDA DLRNEKIGFK IREHTLQKVP YMLVVGDKEV
     ENNTVAVRTR EGQDLGSMAV DDFLQRLESE IARLGRSNSE D
//