(data stored in SCRATCH3701 zone)

SWISSPROT: SYT_RICTY

ID   SYT_RICTY               Reviewed;         635 AA.
AC   Q68XE8;
DT   30-AUG-2005, integrated into UniProtKB/Swiss-Prot.
DT   11-OCT-2004, sequence version 1.
DT   11-DEC-2019, entry version 93.
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=RT0212;
OS   Rickettsia typhi (strain ATCC VR-144 / Wilmington).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Rickettsiales;
OC   Rickettsiaceae; Rickettsieae; Rickettsia; typhus group.
OX   NCBI_TaxID=257363;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC VR-144 / Wilmington;
RX   PubMed=15317790; DOI=10.1128/jb.186.17.5842-5855.2004;
RA   McLeod M.P., Qin X., Karpathy S.E., Gioia J., Highlander S.K., Fox G.E.,
RA   McNeill T.Z., Jiang H., Muzny D., Jacob L.S., Hawes A.C., Sodergren E.,
RA   Gill R., Hume J., Morgan M., Fan G., Amin A.G., Gibbs R.A., Hong C.,
RA   Yu X.-J., Walker D.H., Weinstock G.M.;
RT   "Complete genome sequence of Rickettsia typhi and comparison with sequences
RT   of other Rickettsiae.";
RL   J. Bacteriol. 186:5842-5855(2004).
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}.
DR   EMBL; AE017197; AAU03694.1; -; Genomic_DNA.
DR   RefSeq; WP_011190680.1; NC_006142.1.
DR   SMR; Q68XE8; -.
DR   STRING; 257363.RT0212; -.
DR   EnsemblBacteria; AAU03694; AAU03694; RT0212.
DR   KEGG; rty:RT0212; -.
DR   eggNOG; ENOG4105C22; Bacteria.
DR   eggNOG; COG0441; LUCA.
DR   HOGENOM; HOG000003880; -.
DR   KO; K01868; -.
DR   OMA; FYYDFAY; -.
DR   OrthoDB; 900765at2; -.
DR   BioCyc; RTYP257363:G1G0L-217-MONOMER; -.
DR   Proteomes; UP000000604; 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; 3.40.50.800; -; 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; 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; 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;
DR   PRODOM; Q68XE8.
DR   SWISS-2DPAGE; Q68XE8.
KW   Aminoacyl-tRNA synthetase; ATP-binding; Cytoplasm; Ligase; Metal-binding;
KW   Nucleotide-binding; Protein biosynthesis; RNA-binding; tRNA-binding; Zinc.
FT   CHAIN           1..635
FT                   /note="Threonine--tRNA ligase"
FT                   /id="PRO_0000101039"
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   METAL           333
FT                   /note="Zinc"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00184"
FT   METAL           384
FT                   /note="Zinc; via tele nitrogen"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00184"
FT   METAL           510
FT                   /note="Zinc; via pros nitrogen"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00184"
SQ   SEQUENCE   635 AA;  72799 MW;  9B0F9A0E3AA3239D CRC64;
     MINISFPDGS VKQFAQNITA FEIANAISMS LAKAAMVVEI NGEFKDLSTV IEHDCKLRIL
     TAKDYECLEI IRHDAAHLTA AAVKELFPET QVAIGPAIEN GYYYDFARDK PFSRDDLATI
     EAKMQELVKK NEKITRELWD RDKAIEFFLS IGEHYKAKII ASIPAGEQIT LYRQGNFIDL
     CRGPHAPSTG FVKYFKLMKV AGAYWRGNSR NEMLQRIYGT AWATKEQLDN YLFMLEEAEK
     RDHRKIGKEL DLFHFQEEAQ GMVFWHDKGW SIYNTIEQYI RKKNRKNGYI EVKTPVLVDK
     SLWEASGHWA KFRCDMFTLE TDDKILALKP MNCPCHVQIF KQGIKSYRDL PLRMSEFGLC
     HRNEASGALH GLMRVRSLVQ DDAHIFCAEE QITDETVRFC KLLTEVYKDF GFTDIKVKFS
     DRPEIRAGND EVWDKAEHAL KTAVEKVGFI YTLNPGDGAF YGPKLEFVLT DAIGRQWQCG
     TLQMDFVLPE RLDANYIAAS GEKKRPVMLH RAILGSLERF IGILIEEYAG KFPIWLAPVQ
     VAIATITNDL NDYALEVQKT LIDNNIRTDI NISPDKINYK IREFSNQKIP MIAVIGKKEQ
     ANKQVTIRKF GTTGQEILSI EQLIAMIKKE NSNYL
//

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