ID   SYY_METBF               Reviewed;         317 AA.
AC   Q46BQ5;
DT   13-JUN-2006, integrated into UniProtKB/Swiss-Prot.
DT   13-SEP-2005, sequence version 1.
DT   03-AUG-2022, entry version 112.
DE   RecName: Full=Tyrosine--tRNA ligase {ECO:0000255|HAMAP-Rule:MF_02008};
DE            EC=6.1.1.1 {ECO:0000255|HAMAP-Rule:MF_02008};
DE   AltName: Full=Tyrosyl-tRNA synthetase {ECO:0000255|HAMAP-Rule:MF_02008};
DE            Short=TyrRS {ECO:0000255|HAMAP-Rule:MF_02008};
GN   Name=tyrS {ECO:0000255|HAMAP-Rule:MF_02008}; OrderedLocusNames=Mbar_A1745;
OS   Methanosarcina barkeri (strain Fusaro / DSM 804).
OC   Archaea; Euryarchaeota; Stenosarchaea group; Methanomicrobia;
OC   Methanosarcinales; Methanosarcinaceae; Methanosarcina.
OX   NCBI_TaxID=269797;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Fusaro / DSM 804;
RX   PubMed=16980466; DOI=10.1128/jb.00810-06;
RA   Maeder D.L., Anderson I., Brettin T.S., Bruce D.C., Gilna P., Han C.S.,
RA   Lapidus A., Metcalf W.W., Saunders E., Tapia R., Sowers K.R.;
RT   "The Methanosarcina barkeri genome: comparative analysis with
RT   Methanosarcina acetivorans and Methanosarcina mazei reveals extensive
RT   rearrangement within methanosarcinal genomes.";
RL   J. Bacteriol. 188:7922-7931(2006).
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_02008}.
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_02008};
CC   -!- SUBUNIT: Homodimer. {ECO:0000255|HAMAP-Rule:MF_02008}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_02008}.
CC   -!- SIMILARITY: Belongs to the class-I aminoacyl-tRNA synthetase family.
CC       TyrS type 3 subfamily. {ECO:0000255|HAMAP-Rule:MF_02008}.
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DR   EMBL; CP000099; AAZ70687.1; -; Genomic_DNA.
DR   RefSeq; WP_011306733.1; NC_007355.1.
DR   AlphaFoldDB; Q46BQ5; -.
DR   SMR; Q46BQ5; -.
DR   STRING; 269797.Mbar_A1745; -.
DR   PRIDE; Q46BQ5; -.
DR   EnsemblBacteria; AAZ70687; AAZ70687; Mbar_A1745.
DR   GeneID; 3625790; -.
DR   KEGG; mba:Mbar_A1745; -.
DR   eggNOG; arCOG01886; Archaea.
DR   HOGENOM; CLU_035267_0_1_2; -.
DR   OMA; YIGFEIS; -.
DR   OrthoDB; 59062at2157; -.
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   CDD; cd00805; TyrRS_core; 1.
DR   Gene3D; 3.40.50.620; -; 1.
DR   HAMAP; MF_02008; Tyr_tRNA_synth_type3; 1.
DR   InterPro; IPR001412; aa-tRNA-synth_I_CS.
DR   InterPro; IPR002305; aa-tRNA-synth_Ic.
DR   InterPro; IPR014729; Rossmann-like_a/b/a_fold.
DR   InterPro; IPR002307; Tyr-tRNA-ligase.
DR   InterPro; IPR023684; Tyr-tRNA-ligase_3.
DR   InterPro; IPR023617; Tyr-tRNA-ligase_arc/euk-type.
DR   Pfam; PF00579; tRNA-synt_1b; 1.
DR   PIRSF; PIRSF006588; TyrRS_arch_euk; 1.
DR   PRINTS; PR01040; TRNASYNTHTYR.
DR   TIGRFAMs; TIGR00234; tyrS; 1.
DR   PROSITE; PS00178; AA_TRNA_LIGASE_I; 1.
PE   3: Inferred from homology;
KW   Aminoacyl-tRNA synthetase; ATP-binding; Cytoplasm; Ligase;
KW   Nucleotide-binding; Protein biosynthesis.
FT   CHAIN           1..317
FT                   /note="Tyrosine--tRNA ligase"
FT                   /id="PRO_0000240257"
FT   MOTIF           38..46
FT                   /note="'HIGH' region"
FT   MOTIF           211..215
FT                   /note="'KMSKS' region"
FT   BINDING         33
FT                   /ligand="L-tyrosine"
FT                   /ligand_id="ChEBI:CHEBI:58315"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_02008"
FT   BINDING         155
FT                   /ligand="L-tyrosine"
FT                   /ligand_id="ChEBI:CHEBI:58315"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_02008"
FT   BINDING         159
FT                   /ligand="L-tyrosine"
FT                   /ligand_id="ChEBI:CHEBI:58315"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_02008"
FT   BINDING         162
FT                   /ligand="L-tyrosine"
FT                   /ligand_id="ChEBI:CHEBI:58315"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_02008"
FT   BINDING         177
FT                   /ligand="L-tyrosine"
FT                   /ligand_id="ChEBI:CHEBI:58315"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_02008"
FT   BINDING         214
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_02008"
SQ   SEQUENCE   317 AA;  36110 MW;  72B284D8BC84D981 CRC64;
     MDRLDLIKRN VQEIVTEGEL EELLNKKKAP RAYVGYEPSG KIHMGHVLTV NKLIDLQKAG
     FEITVLLADV HAYLNRKGTL EEVRKIADYN KRCFIALGLD KEKTNFVYGS DYQLGAEYML
     NVLKLSRSVT LNRARRSMDE VGRAMDDPTV SQMVYPLMQA IDIAMLGVDI AVGGIDQRKI
     HMLARENLKN LGFETPICIH TPILLGLDGT KMASSKENFI SVDDTEEEIY RKLKKAYCKI
     GDTEENPILA LFRYHIFPRY ETIVIERPEK FGGNITYTSY EEMENAFVAE SVHPMDLKNS
     AAKYINEILD PVRKVLL