ID   SYY_SHIBS               Reviewed;         424 AA.
AC   Q320Z4;
DT   16-MAY-2006, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 3.
DT   03-AUG-2022, entry version 99.
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=SBO_1497;
OS   Shigella boydii serotype 4 (strain Sb227).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Shigella.
OX   NCBI_TaxID=300268;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Sb227;
RX   PubMed=16275786; DOI=10.1093/nar/gki954;
RA   Yang F., Yang J., Zhang X., Chen L., Jiang Y., Yan Y., Tang X., Wang J.,
RA   Xiong Z., Dong J., Xue Y., Zhu Y., Xu X., Sun L., Chen S., Nie H., Peng J.,
RA   Xu J., Wang Y., Yuan Z., Wen Y., Yao Z., Shen Y., Qiang B., Hou Y., Yu J.,
RA   Jin Q.;
RT   "Genome dynamics and diversity of Shigella species, the etiologic agents of
RT   bacillary dysentery.";
RL   Nucleic Acids Res. 33:6445-6458(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_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; CP000036; ABB66114.1; -; Genomic_DNA.
DR   RefSeq; WP_011379201.1; NC_007613.1.
DR   AlphaFoldDB; Q320Z4; -.
DR   SMR; Q320Z4; -.
DR   EnsemblBacteria; ABB66114; ABB66114; SBO_1497.
DR   KEGG; sbo:SBO_1497; -.
DR   HOGENOM; CLU_024003_0_3_6; -.
DR   OMA; YHSSVQA; -.
DR   Proteomes; UP000007067; 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   Acetylation; Aminoacyl-tRNA synthetase; ATP-binding; Cytoplasm; Ligase;
KW   Nucleotide-binding; Protein biosynthesis; RNA-binding.
FT   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0000250"
FT   CHAIN           2..424
FT                   /note="Tyrosine--tRNA ligase"
FT                   /id="PRO_0000234766"
FT   DOMAIN          357..414
FT                   /note="S4 RNA-binding"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_02006"
FT   MOTIF           42..51
FT                   /note="'HIGH' region"
FT   MOTIF           235..239
FT                   /note="'KMSKS' region"
FT   BINDING         37
FT                   /ligand="L-tyrosine"
FT                   /ligand_id="ChEBI:CHEBI:58315"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_02006"
FT   BINDING         175
FT                   /ligand="L-tyrosine"
FT                   /ligand_id="ChEBI:CHEBI:58315"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_02006"
FT   BINDING         179
FT                   /ligand="L-tyrosine"
FT                   /ligand_id="ChEBI:CHEBI:58315"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_02006"
FT   BINDING         238
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_02006"
FT   MOD_RES         144
FT                   /note="N6-acetyllysine"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_02006"
SQ   SEQUENCE   424 AA;  47860 MW;  E0FBB81ED28F0B3A CRC64;
     MASSNLIKQL QERGLVAQVT DEEALAERLA QGPIALYCGF DPTADSLHLG HLVPLLCLKR
     FQQAGHKPVA LVGGATGLIG DPSFKAAERK LNTEETVQEW VDKIRKQVAP FLDFDCGENS
     AIAANNYDWF GNMNVLTFLR DIGKHFSVNQ MINKEAVKQR LNREDEGMSI TEFSYNLQQG
     YDWTCLNTHY YVELQIGGSD QRWNITSEID LTRRLHQNHV LGLTVPLITK ADGTKFGKTE
     GGAVWLDPKK TSPYKFYQFW INTADADVYR FLKFFTFMSI EEINALEEED KNSGKAPRAQ
     YVLAEQVTRL VHGEEGLQAA KRITECLFSG SLSALSEADF EQLAQDGVPM VEMEKGADLM
     QALVDSELQP SRGQARKTIA SNAITINGEK QSDPEYFFKE EDRLFGRFTL LRRGKKNYCL
     ICWK