SYTC_SULTO
ID SYTC_SULTO Reviewed; 540 AA.
AC Q973C8; F9VNS1;
DT 30-AUG-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-2001, sequence version 1.
DT 03-AUG-2022, entry version 118.
DE RecName: Full=Threonine--tRNA ligase catalytic subunit;
DE EC=6.1.1.3 {ECO:0000255|HAMAP-Rule:MF_00184};
DE AltName: Full=Threonyl-tRNA synthetase catalytic subunit;
DE Short=ThrRS-cat;
GN Name=thrS-cat {ECO:0000305}; Synonyms=thrS; OrderedLocusNames=STK_09660;
OS Sulfurisphaera tokodaii (strain DSM 16993 / JCM 10545 / NBRC 100140 / 7)
OS (Sulfolobus tokodaii).
OC Archaea; Crenarchaeota; Thermoprotei; Sulfolobales; Sulfolobaceae;
OC Sulfurisphaera.
OX NCBI_TaxID=273063;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 16993 / JCM 10545 / NBRC 100140 / 7;
RX PubMed=11572479; DOI=10.1093/dnares/8.4.123;
RA Kawarabayasi Y., Hino Y., Horikawa H., Jin-no K., Takahashi M., Sekine M.,
RA Baba S., Ankai A., Kosugi H., Hosoyama A., Fukui S., Nagai Y.,
RA Nishijima K., Otsuka R., Nakazawa H., Takamiya M., Kato Y., Yoshizawa T.,
RA Tanaka T., Kudoh Y., Yamazaki J., Kushida N., Oguchi A., Aoki K.,
RA Masuda S., Yanagii M., Nishimura M., Yamagishi A., Oshima T., Kikuchi H.;
RT "Complete genome sequence of an aerobic thermoacidophilic Crenarchaeon,
RT Sulfolobus tokodaii strain7.";
RL DNA Res. 8:123-140(2001).
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 activates
CC L-serine and transfers it to tRNA(Thr) but cannot deacylate incorrectly
CC charged amino acid; unlike most archaea the editing function is found
CC in a freestanding protein. {ECO:0000250|UniProtKB:Q97VW8}.
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 (By similarity). Probably interacts with its editing
CC subunit (By similarity). {ECO:0000250|UniProtKB:Q97VW8,
CC ECO:0000250|UniProtKB:Q9YDW0}.
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; BA000023; BAK54429.1; -; Genomic_DNA.
DR RefSeq; WP_010978967.1; NC_003106.2.
DR AlphaFoldDB; Q973C8; -.
DR SMR; Q973C8; -.
DR STRING; 273063.STK_09660; -.
DR EnsemblBacteria; BAK54429; BAK54429; STK_09660.
DR GeneID; 1458938; -.
DR KEGG; sto:STK_09660; -.
DR PATRIC; fig|273063.9.peg.1081; -.
DR eggNOG; arCOG00401; Archaea.
DR OMA; DAHIFML; -.
DR OrthoDB; 11656at2157; -.
DR Proteomes; UP000001015; 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; 3.30.930.10; -; 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; IPR002320; Thr-tRNA-ligase_IIa.
DR InterPro; IPR018163; Thr/Ala-tRNA-synth_IIc_edit.
DR InterPro; IPR033728; ThrRS_core.
DR PANTHER; PTHR11451; PTHR11451; 1.
DR Pfam; PF03129; HGTP_anticodon; 1.
DR Pfam; PF00587; tRNA-synt_2b; 1.
DR PRINTS; PR01047; TRNASYNTHTHR.
DR SUPFAM; SSF55186; SSF55186; 1.
DR SUPFAM; SSF55681; SSF55681; 1.
DR TIGRFAMs; TIGR00418; thrS; 1.
DR PROSITE; PS50862; AA_TRNA_LIGASE_II; 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..540
FT /note="Threonine--tRNA ligase catalytic subunit"
FT /id="PRO_0000101114"
FT REGION 134..428
FT /note="Catalytic"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00184"
FT BINDING 226
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00184"
FT BINDING 277
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00184"
FT BINDING 405
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00184"
SQ SEQUENCE 540 AA; 63111 MW; 8B25418AECA5C4F9 CRC64;
MEEYKGVWLK AGIIYALNLA SNGFKPVEVG LGERDFYVDV ESDTTLTLDE AKKFATYNQY
SYQLKDGYIE FNGNKIKVLG EPSSLEPKYF EILNISVHHP SPNVQYVRIR GVGFEKKEEL
DQYLKWLEEV SEYDHRIIGE RLDLFSFPDE TAPGLALFHY KGQIIRKELM KFMEEINESM
GYQEVFTAEI YRSILWKTSG HYDYYKDKMV LFKMEDEELG LKPMNCPAHI LIYKSKTRSY
KDLPIRFSEF GLVFRWEKRG ELYGLLRVRG FVQDDGHIFL TEDQIKDEVK MLVKKTIDVL
SIFGFKGDDV RINLSTRPDE SIGSDELWEK ATNALVSALN ELGIKYIVKE KEGAFYGPKI
DFDIRDSLGR WWQLSTIQVD FNLPERFKLE YIDKDGSRKR PVMIHRAIYG SIERFMAILL
EHFRGKLPTW LSPVQVRILP ISKDVEDYAL NLLSKLKENK IRVELDMSDE TLSKRIKKAY
DEGVPYMIIV GKKEREEGKV TVRGRNNVEI RGVKFDDFLK ALLEEIRNRD LNQSAINKLK
