ID   SYY_PYRAR               Reviewed;         372 AA.
AC   A4WN67;
DT   11-SEP-2007, integrated into UniProtKB/Swiss-Prot.
DT   29-MAY-2007, sequence version 1.
DT   03-AUG-2022, entry version 77.
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=Pars_2290;
OS   Pyrobaculum arsenaticum (strain DSM 13514 / JCM 11321 / PZ6).
OC   Archaea; Crenarchaeota; Thermoprotei; Thermoproteales; Thermoproteaceae;
OC   Pyrobaculum.
OX   NCBI_TaxID=340102;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 700994 / DSM 13514 / JCM 11321 / PZ6;
RG   US DOE Joint Genome Institute;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Glavina del Rio T., Dalin E.,
RA   Tice H., Pitluck S., Chain P., Malfatti S., Shin M., Vergez L., Schmutz J.,
RA   Larimer F., Land M., Hauser L., Kyrpides N., Mikhailova N., Cozen A.E.,
RA   Fitz-Gibbon S.T., House C.H., Saltikov C., Lowe T.M., Richardson P.;
RT   "Complete sequence of Pyrobaculum arsenaticum DSM 13514.";
RL   Submitted (APR-2007) to the EMBL/GenBank/DDBJ databases.
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; CP000660; ABP51834.1; -; Genomic_DNA.
DR   AlphaFoldDB; A4WN67; -.
DR   SMR; A4WN67; -.
DR   STRING; 340102.Pars_2290; -.
DR   EnsemblBacteria; ABP51834; ABP51834; Pars_2290.
DR   KEGG; pas:Pars_2290; -.
DR   HOGENOM; CLU_035267_1_1_2; -.
DR   OMA; YIGFEIS; -.
DR   PhylomeDB; A4WN67; -.
DR   Proteomes; UP000001567; 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; -; 2.
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; 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.
PE   3: Inferred from homology;
KW   Aminoacyl-tRNA synthetase; ATP-binding; Cytoplasm; Ligase;
KW   Nucleotide-binding; Protein biosynthesis.
FT   CHAIN           1..372
FT                   /note="Tyrosine--tRNA ligase"
FT                   /id="PRO_0000303679"
FT   MOTIF           246..250
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         169
FT                   /ligand="L-tyrosine"
FT                   /ligand_id="ChEBI:CHEBI:58315"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_02009"
FT   BINDING         173
FT                   /ligand="L-tyrosine"
FT                   /ligand_id="ChEBI:CHEBI:58315"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_02009"
FT   BINDING         176
FT                   /ligand="L-tyrosine"
FT                   /ligand_id="ChEBI:CHEBI:58315"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_02009"
FT   BINDING         191
FT                   /ligand="L-tyrosine"
FT                   /ligand_id="ChEBI:CHEBI:58315"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_02009"
FT   BINDING         249
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_02009"
SQ   SEQUENCE   372 AA;  42066 MW;  71BDD6C28C7F7296 CRC64;
     MDVESRLSLI LRYPAEEVIT VEELKEILQA GYKLNHYIGF EISGFIHIGT GVVSMSKVVD
     LQKAGVRTQI LLADIHSWLN NKLGGDLETI RRVAVTYYVE TFKKIIEVLG GDPDGTRFVL
     GSDLYHHNDE YWLLLMDITR HLTLSQVRHS LTILGRKMGE SIPLAYLVYP PLQVADVFAL
     GAHIPHGGID QRRAHILARE VAHKIRFYPL EVDGKRVKPV ALHHRLLPAL NISAKPASKE
     ELSELKMSKS IPQSAIFVHD SPEEIKQKIA KAYCPPREVE YNPVLELLRV SAFREERKTP
     FVIRRPAQYG GDVEVWSYQE LEGLYREGKI HPADLKNAAA EALAGLLEPV YKFFQGPGAK
     LLEEMKNITI TR