ID   SYY_THEON               Reviewed;         375 AA.
AC   B6YWK6;
DT   28-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT   20-JAN-2009, sequence version 1.
DT   03-AUG-2022, entry version 82.
DE   RecName: Full=Tyrosine--tRNA ligase {ECO:0000255|HAMAP-Rule:MF_02009};
DE            EC=6.1.1.1 {ECO:0000255|HAMAP-Rule:MF_02009};
DE   AltName: Full=Tyrosyl-tRNA synthetase {ECO:0000255|HAMAP-Rule:MF_02009};
DE            Short=TyrRS {ECO:0000255|HAMAP-Rule:MF_02009};
GN   Name=tyrS {ECO:0000255|HAMAP-Rule:MF_02009}; OrderedLocusNames=TON_0981;
OS   Thermococcus onnurineus (strain NA1).
OC   Archaea; Euryarchaeota; Thermococci; Thermococcales; Thermococcaceae;
OC   Thermococcus.
OX   NCBI_TaxID=523850;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NA1;
RX   PubMed=18790866; DOI=10.1128/jb.00746-08;
RA   Lee H.S., Kang S.G., Bae S.S., Lim J.K., Cho Y., Kim Y.J., Jeon J.H.,
RA   Cha S.-S., Kwon K.K., Kim H.-T., Park C.-J., Lee H.-W., Kim S.I., Chun J.,
RA   Colwell R.R., Kim S.-J., Lee J.-H.;
RT   "The complete genome sequence of Thermococcus onnurineus NA1 reveals a
RT   mixed heterotrophic and carboxydotrophic metabolism.";
RL   J. Bacteriol. 190:7491-7499(2008).
CC   -!- FUNCTION: Catalyzes the attachment of tyrosine to tRNA(Tyr) in a two-
CC       step reaction: tyrosine is first activated by ATP to form Tyr-AMP and
CC       then transferred to the acceptor end of tRNA(Tyr). {ECO:0000255|HAMAP-
CC       Rule:MF_02009}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + L-tyrosine + tRNA(Tyr) = AMP + diphosphate + H(+) + L-
CC         tyrosyl-tRNA(Tyr); Xref=Rhea:RHEA:10220, Rhea:RHEA-COMP:9706,
CC         Rhea:RHEA-COMP:9707, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616,
CC         ChEBI:CHEBI:33019, ChEBI:CHEBI:58315, ChEBI:CHEBI:78442,
CC         ChEBI:CHEBI:78536, ChEBI:CHEBI:456215; EC=6.1.1.1;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_02009};
CC   -!- SUBUNIT: Homodimer. {ECO:0000255|HAMAP-Rule:MF_02009}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_02009}.
CC   -!- SIMILARITY: Belongs to the class-I aminoacyl-tRNA synthetase family.
CC       TyrS type 4 subfamily. {ECO:0000255|HAMAP-Rule:MF_02009}.
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DR   EMBL; CP000855; ACJ16469.1; -; Genomic_DNA.
DR   RefSeq; WP_012571941.1; NC_011529.1.
DR   AlphaFoldDB; B6YWK6; -.
DR   SMR; B6YWK6; -.
DR   STRING; 523850.TON_0981; -.
DR   EnsemblBacteria; ACJ16469; ACJ16469; TON_0981.
DR   GeneID; 7017285; -.
DR   KEGG; ton:TON_0981; -.
DR   PATRIC; fig|523850.10.peg.989; -.
DR   eggNOG; arCOG01886; Archaea.
DR   HOGENOM; CLU_035267_1_1_2; -.
DR   OMA; YIGFEIS; -.
DR   OrthoDB; 59062at2157; -.
DR   Proteomes; UP000002727; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0004831; F:tyrosine-tRNA ligase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0006437; P:tyrosyl-tRNA aminoacylation; IEA:UniProtKB-UniRule.
DR   Gene3D; 3.40.50.620; -; 1.
DR   HAMAP; MF_02009; Tyr_tRNA_synth_type4; 1.
DR   InterPro; IPR002305; aa-tRNA-synth_Ic.
DR   InterPro; IPR014729; Rossmann-like_a/b/a_fold.
DR   InterPro; IPR002307; Tyr-tRNA-ligase.
DR   InterPro; IPR023678; Tyr-tRNA-ligase_4.
DR   InterPro; IPR023617; Tyr-tRNA-ligase_arc/euk-type.
DR   Pfam; PF00579; tRNA-synt_1b; 1.
DR   PIRSF; PIRSF006588; TyrRS_arch_euk; 1.
DR   TIGRFAMs; TIGR00234; tyrS; 1.
PE   3: Inferred from homology;
KW   Aminoacyl-tRNA synthetase; ATP-binding; Cytoplasm; Ligase;
KW   Nucleotide-binding; Protein biosynthesis.
FT   CHAIN           1..375
FT                   /note="Tyrosine--tRNA ligase"
FT                   /id="PRO_1000189476"
FT   MOTIF           251..255
FT                   /note="'KMSKS' region"
FT   BINDING         37
FT                   /ligand="L-tyrosine"
FT                   /ligand_id="ChEBI:CHEBI:58315"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_02009"
FT   BINDING         168
FT                   /ligand="L-tyrosine"
FT                   /ligand_id="ChEBI:CHEBI:58315"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_02009"
FT   BINDING         172
FT                   /ligand="L-tyrosine"
FT                   /ligand_id="ChEBI:CHEBI:58315"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_02009"
FT   BINDING         175
FT                   /ligand="L-tyrosine"
FT                   /ligand_id="ChEBI:CHEBI:58315"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_02009"
FT   BINDING         190
FT                   /ligand="L-tyrosine"
FT                   /ligand_id="ChEBI:CHEBI:58315"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_02009"
FT   BINDING         254
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_02009"
SQ   SEQUENCE   375 AA;  43133 MW;  F3E0B4905B1C4F6E CRC64;
     MDIGRKIELI TKRPTEELLT VENLRHLLEI GAPMQHYIGF EISGYIHLGT GLMAGAKIAD
     LQKAGIKTRI FLADWHSWIN DKLGGDLEII QKVALTYFKE GMKQSIKVMG GDPDKVEFVL
     ASEILEKGDY WQTVIDISKN VTLARMMRSI TIMGRQMGEA IDFAKLIYPA MQVADIFYQG
     VTIAHAGMDQ RKAHVIAIEV AQKLKYHAIE HNGEKLKPVA LHHHLLLGLQ EPPVWPIESE
     EQYKELKTQM KMSKSKPYSA VFIHDTPEEI KQKLRKAFCP AREVKYNPVL DWAEYIIFRE
     EPTEFTIHRP AKFGGDVTYT TFEELKRDFA EGKLHPLDLK NAVAEYLIEL LKPVRDYFEK
     HPEPLELMRE IKITR