ID   SYY_MYCPN               Reviewed;         399 AA.
AC   P75122;
DT   01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1997, sequence version 1.
DT   03-AUG-2022, entry version 122.
DE   RecName: Full=Tyrosine--tRNA ligase {ECO:0000255|HAMAP-Rule:MF_02006};
DE            EC=6.1.1.1 {ECO:0000255|HAMAP-Rule:MF_02006};
DE   AltName: Full=Tyrosyl-tRNA synthetase {ECO:0000255|HAMAP-Rule:MF_02006};
DE            Short=TyrRS {ECO:0000255|HAMAP-Rule:MF_02006};
GN   Name=tyrS {ECO:0000255|HAMAP-Rule:MF_02006}; OrderedLocusNames=MPN_669;
GN   ORFNames=MP173;
OS   Mycoplasma pneumoniae (strain ATCC 29342 / M129) (Mycoplasmoides
OS   pneumoniae).
OC   Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mycoplasma.
OX   NCBI_TaxID=272634;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 29342 / M129;
RX   PubMed=8948633; DOI=10.1093/nar/24.22.4420;
RA   Himmelreich R., Hilbert H., Plagens H., Pirkl E., Li B.-C., Herrmann R.;
RT   "Complete sequence analysis of the genome of the bacterium Mycoplasma
RT   pneumoniae.";
RL   Nucleic Acids Res. 24:4420-4449(1996).
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_02006}.
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_02006};
CC   -!- SUBUNIT: Homodimer. {ECO:0000255|HAMAP-Rule:MF_02006}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_02006}.
CC   -!- SIMILARITY: Belongs to the class-I aminoacyl-tRNA synthetase family.
CC       TyrS type 1 subfamily. {ECO:0000255|HAMAP-Rule:MF_02006}.
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DR   EMBL; U00089; AAB95821.1; -; Genomic_DNA.
DR   PIR; S73499; S73499.
DR   RefSeq; NP_110358.1; NC_000912.1.
DR   RefSeq; WP_010875026.1; NC_000912.1.
DR   AlphaFoldDB; P75122; -.
DR   SMR; P75122; -.
DR   IntAct; P75122; 1.
DR   STRING; 272634.MPN_669; -.
DR   PRIDE; P75122; -.
DR   EnsemblBacteria; AAB95821; AAB95821; MPN_669.
DR   KEGG; mpn:MPN_669; -.
DR   PATRIC; fig|272634.6.peg.734; -.
DR   HOGENOM; CLU_024003_0_3_14; -.
DR   OMA; YMMAKDS; -.
DR   BioCyc; MPNE272634:G1GJ3-1071-MON; -.
DR   Proteomes; UP000000808; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0003723; F:RNA binding; IEA:UniProtKB-KW.
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; cd00165; S4; 1.
DR   CDD; cd00805; TyrRS_core; 1.
DR   Gene3D; 3.10.290.10; -; 1.
DR   Gene3D; 3.40.50.620; -; 1.
DR   HAMAP; MF_02006; Tyr_tRNA_synth_type1; 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; IPR002942; S4_RNA-bd.
DR   InterPro; IPR036986; S4_RNA-bd_sf.
DR   InterPro; IPR002307; Tyr-tRNA-ligase.
DR   InterPro; IPR024088; Tyr-tRNA-ligase_bac-type.
DR   InterPro; IPR024107; Tyr-tRNA-ligase_bac_1.
DR   PANTHER; PTHR11766; PTHR11766; 1.
DR   Pfam; PF01479; S4; 1.
DR   Pfam; PF00579; tRNA-synt_1b; 1.
DR   PRINTS; PR01040; TRNASYNTHTYR.
DR   SMART; SM00363; S4; 1.
DR   TIGRFAMs; TIGR00234; tyrS; 1.
DR   PROSITE; PS00178; AA_TRNA_LIGASE_I; 1.
DR   PROSITE; PS50889; S4; 1.
PE   3: Inferred from homology;
KW   Aminoacyl-tRNA synthetase; ATP-binding; Cytoplasm; Ligase;
KW   Nucleotide-binding; Protein biosynthesis; Reference proteome; RNA-binding.
FT   CHAIN           1..399
FT                   /note="Tyrosine--tRNA ligase"
FT                   /id="PRO_0000055658"
FT   DOMAIN          332..395
FT                   /note="S4 RNA-binding"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_02006"
FT   MOTIF           41..50
FT                   /note="'HIGH' region"
FT   MOTIF           226..230
FT                   /note="'KMSKS' region"
FT   BINDING         36
FT                   /ligand="L-tyrosine"
FT                   /ligand_id="ChEBI:CHEBI:58315"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_02006"
FT   BINDING         166
FT                   /ligand="L-tyrosine"
FT                   /ligand_id="ChEBI:CHEBI:58315"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_02006"
FT   BINDING         170
FT                   /ligand="L-tyrosine"
FT                   /ligand_id="ChEBI:CHEBI:58315"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_02006"
FT   BINDING         229
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_02006"
SQ   SEQUENCE   399 AA;  44650 MW;  50E6B8A3FE3E9A4E CRC64;
     MTKDLLALLK ERGLFVQANF EKELKQLLNQ GSFAFYVGFD PTAPSLHIGN YVLLHVAQIF
     QAMGHIPHVL LGSGTALIGD PTGRMELRQM MSRETIAENT RNIKKQIRRF LGSNVVFCQN
     ETWLKKLNYI EVIRELGPCF SVNKMLATDA FSARWERGLT LMELNYMVLQ AYDFYYLNQK
     YGVQLQIGGS DQWANILAGA DLIRRKTQKQ VYGMTTNLLV KANGEKMGKS ASGALWLDPQ
     KTSPYDFYQY WINLDDASLQ KVFLMLTKLD TKAIETLCNL KGAAIKEAKA KLAFELTDAI
     HGTKAALVAQ AKSARIFAFQ PDTETKTVRA GTRLVDVIVD LGLVVSRSEA RRVIQQGGLT
     INQEKVTDVE MVLQASSQPL VIGKGKKRFV TVQVIANTK