ID   SYY_THEKO               Reviewed;         375 AA.
AC   Q5JF63;
DT   13-JUN-2006, integrated into UniProtKB/Swiss-Prot.
DT   15-FEB-2005, sequence version 1.
DT   03-AUG-2022, entry version 98.
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=TK0568;
OS   Thermococcus kodakarensis (strain ATCC BAA-918 / JCM 12380 / KOD1)
OS   (Pyrococcus kodakaraensis (strain KOD1)).
OC   Archaea; Euryarchaeota; Thermococci; Thermococcales; Thermococcaceae;
OC   Thermococcus.
OX   NCBI_TaxID=69014;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-918 / JCM 12380 / KOD1;
RX   PubMed=15710748; DOI=10.1101/gr.3003105;
RA   Fukui T., Atomi H., Kanai T., Matsumi R., Fujiwara S., Imanaka T.;
RT   "Complete genome sequence of the hyperthermophilic archaeon Thermococcus
RT   kodakaraensis KOD1 and comparison with Pyrococcus genomes.";
RL   Genome Res. 15:352-363(2005).
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; AP006878; BAD84757.1; -; Genomic_DNA.
DR   RefSeq; WP_011249523.1; NC_006624.1.
DR   AlphaFoldDB; Q5JF63; -.
DR   SMR; Q5JF63; -.
DR   IntAct; Q5JF63; 1.
DR   MINT; Q5JF63; -.
DR   STRING; 69014.TK0568; -.
DR   EnsemblBacteria; BAD84757; BAD84757; TK0568.
DR   GeneID; 3234446; -.
DR   KEGG; tko:TK0568; -.
DR   PATRIC; fig|69014.16.peg.555; -.
DR   eggNOG; arCOG01886; Archaea.
DR   HOGENOM; CLU_035267_1_1_2; -.
DR   InParanoid; Q5JF63; -.
DR   OMA; YIGFEIS; -.
DR   OrthoDB; 59062at2157; -.
DR   PhylomeDB; Q5JF63; -.
DR   Proteomes; UP000000536; 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; Reference proteome.
FT   CHAIN           1..375
FT                   /note="Tyrosine--tRNA ligase"
FT                   /id="PRO_0000240270"
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;  43187 MW;  C3A91D6A6CED2BD0 CRC64;
     MDIERKIELI KKKPTEELLT EENLRHLLEV GAPLQHYIGF EISGYIHLGT GLMAGAKIAD
     LQKAGVKTRI FLADWHSWIN DKLGGDLEVI QKVALTYFKE GMKQSIKVMG GDPDKVEFVL
     ASEILDKGDY WQTVIDISKN VTLARMLRSI TIMGRQMGEA IDFAKLIYPA MQVADIFYQG
     VTIAHAGMDQ RKAHVIAIEV AQKLKYHPLE WKGEKLKPVA LHHHLLLGLQ EPPVWPIESE
     EQFKELKTQM KMSKSKPYSA VFIHDSPEEI KQKLRKAFCP AREVKYNPVL DWAEYIIFRE
     EPTEFTIHRP AKFGGDVTYT TFEELKKDFA EGKLHPLDLK NAVAEYLIEL LKPVREYFEK
     HPEPLELMRE IKITR