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SYT_RICPR
ID   SYT_RICPR               Reviewed;         635 AA.
AC   O05947;
DT   01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT   01-JUL-1997, sequence version 1.
DT   03-AUG-2022, entry version 128.
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=RP221;
OS   Rickettsia prowazekii (strain Madrid E).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Rickettsiales;
OC   Rickettsiaceae; Rickettsieae; Rickettsia; typhus group.
OX   NCBI_TaxID=272947;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=Madrid E;
RX   PubMed=9274032; DOI=10.1099/00221287-143-8-2783;
RA   Andersson J.O., Andersson S.G.E.;
RT   "Genomic rearrangements during evolution of the obligate intracellular
RT   parasite Rickettsia prowazekii as inferred from an analysis of 52015 bp
RT   nucleotide sequence.";
RL   Microbiology 143:2783-2795(1997).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Madrid E;
RX   PubMed=9823893; DOI=10.1038/24094;
RA   Andersson S.G.E., Zomorodipour A., Andersson J.O., Sicheritz-Ponten T.,
RA   Alsmark U.C.M., Podowski R.M., Naeslund A.K., Eriksson A.-S., Winkler H.H.,
RA   Kurland C.G.;
RT   "The genome sequence of Rickettsia prowazekii and the origin of
RT   mitochondria.";
RL   Nature 396:133-140(1998).
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; Y11780; CAA72469.1; -; Genomic_DNA.
DR   EMBL; AJ235270; CAA14684.1; -; Genomic_DNA.
DR   PIR; E71733; E71733.
DR   RefSeq; NP_220607.1; NC_000963.1.
DR   RefSeq; WP_004598574.1; NC_000963.1.
DR   AlphaFoldDB; O05947; -.
DR   SMR; O05947; -.
DR   STRING; 272947.RP221; -.
DR   EnsemblBacteria; CAA14684; CAA14684; CAA14684.
DR   GeneID; 57569349; -.
DR   KEGG; rpr:RP221; -.
DR   PATRIC; fig|272947.5.peg.229; -.
DR   eggNOG; COG0441; Bacteria.
DR   HOGENOM; CLU_008554_0_1_5; -.
DR   OMA; FYYDFAY; -.
DR   Proteomes; UP000002480; 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; 3.10.20.30; -; 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; IPR012675; Beta-grasp_dom_sf.
DR   InterPro; IPR004095; TGS.
DR   InterPro; IPR012676; TGS-like.
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; PF02824; TGS; 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   SUPFAM; SSF81271; SSF81271; 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..635
FT                   /note="Threonine--tRNA ligase"
FT                   /id="PRO_0000101038"
FT   DOMAIN          1..61
FT                   /note="TGS"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01228"
FT   REGION          242..533
FT                   /note="Catalytic"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00184"
FT   BINDING         333
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00184"
FT   BINDING         384
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00184"
FT   BINDING         510
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00184"
SQ   SEQUENCE   635 AA;  72677 MW;  B000D1514AF729D5 CRC64;
     MINISFPDGS VKQFAQNITA FEIVNAISMS LAKAAIVVEI NGELKDLSTV IENDCKLRIL
     TAQDYECLEI IRHDAAHLTA EAVKELFPET QVTIGPAIEN GYYYDFARDK PFSIDDLANI
     EAKMQELSKK NEKITRELWD RDKAVEFFLS IGEHYKAKII ASIPEGEPIT LYRQGNFIDL
     CRGPHSPSTG FVKHFKLMKV AGAYWRGNSR NEMLQRIYGT AWATKEQLDN YLFMLEEAEK
     RDHRKIGKEL DLFHFQEEAQ GMVFWHDKGW SIYNTIEQYI RKKIRKNGYI EVKTPVLVDK
     SLWEASGHWA KFRCDMFTLE TDDKTLALKP MNCPCHVQIF KQGIKSYRDL PLRMSEFGLC
     HRNEASGALH GLMRVRSLVQ DDAHIFCAEE QITDETVRFC KLLTEVYKDF GFTDIKVKFS
     DRSEICAGND EVWDKAENAL KTAIEKAGFI YTLNPGEAAF YGPKIEFVLT DAIGRQWQCG
     TLQMDFVLPE RLDANYIAAS GEKKRPVMLH RAILGSLERF IGILIEEYAG KFPIWLAPVQ
     VAIATITNDL NDYALEVQKT LIDNGVRTDI NISPDKINYK IREFSNQKIP IIAVIGKQEQ
     ANKQVTIRKL GTIEQEILSI EQLIAMIKKE NSNYL
 
 
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