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SYY_XANOR
ID   SYY_XANOR               Reviewed;         403 AA.
AC   Q5H5K1; Q5H5K2;
DT   30-MAY-2006, integrated into UniProtKB/Swiss-Prot.
DT   30-MAY-2006, sequence version 2.
DT   03-AUG-2022, entry version 82.
DE   RecName: Full=Tyrosine--tRNA ligase {ECO:0000255|HAMAP-Rule:MF_02007};
DE            EC=6.1.1.1 {ECO:0000255|HAMAP-Rule:MF_02007};
DE   AltName: Full=Tyrosyl-tRNA synthetase {ECO:0000255|HAMAP-Rule:MF_02007};
DE            Short=TyrRS {ECO:0000255|HAMAP-Rule:MF_02007};
GN   Name=tyrS {ECO:0000255|HAMAP-Rule:MF_02007}; OrderedLocusNames=XOO0514;
OS   Xanthomonas oryzae pv. oryzae (strain KACC10331 / KXO85).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Xanthomonadales;
OC   Xanthomonadaceae; Xanthomonas.
OX   NCBI_TaxID=291331;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=KACC10331 / KXO85;
RX   PubMed=15673718; DOI=10.1093/nar/gki206;
RA   Lee B.-M., Park Y.-J., Park D.-S., Kang H.-W., Kim J.-G., Song E.-S.,
RA   Park I.-C., Yoon U.-H., Hahn J.-H., Koo B.-S., Lee G.-B., Kim H.,
RA   Park H.-S., Yoon K.-O., Kim J.-H., Jung C.-H., Koh N.-H., Seo J.-S.,
RA   Go S.-J.;
RT   "The genome sequence of Xanthomonas oryzae pathovar oryzae KACC10331, the
RT   bacterial blight pathogen of rice.";
RL   Nucleic Acids Res. 33:577-586(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_02007}.
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_02007};
CC   -!- SUBUNIT: Homodimer. {ECO:0000255|HAMAP-Rule:MF_02007}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_02007}.
CC   -!- SIMILARITY: Belongs to the class-I aminoacyl-tRNA synthetase family.
CC       TyrS type 2 subfamily. {ECO:0000255|HAMAP-Rule:MF_02007}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AE013598; Type=Frameshift; Evidence={ECO:0000305};
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DR   EMBL; AE013598; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   AlphaFoldDB; Q5H5K1; -.
DR   SMR; Q5H5K1; -.
DR   Proteomes; UP000006735; 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; cd00805; TyrRS_core; 1.
DR   Gene3D; 3.10.290.10; -; 1.
DR   Gene3D; 3.40.50.620; -; 1.
DR   HAMAP; MF_02007; Tyr_tRNA_synth_type2; 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; IPR036986; S4_RNA-bd_sf.
DR   InterPro; IPR002307; Tyr-tRNA-ligase.
DR   InterPro; IPR024088; Tyr-tRNA-ligase_bac-type.
DR   InterPro; IPR024108; Tyr-tRNA-ligase_bac_2.
DR   PANTHER; PTHR11766; PTHR11766; 1.
DR   PANTHER; PTHR11766:SF1; PTHR11766:SF1; 1.
DR   Pfam; PF00579; tRNA-synt_1b; 1.
DR   PRINTS; PR01040; TRNASYNTHTYR.
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..403
FT                   /note="Tyrosine--tRNA ligase"
FT                   /id="PRO_0000236785"
FT   DOMAIN          339..400
FT                   /note="S4 RNA-binding"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_02007"
FT   MOTIF           42..51
FT                   /note="'HIGH' region"
FT   MOTIF           226..230
FT                   /note="'KMSKS' region"
FT   BINDING         229
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_02007"
SQ   SEQUENCE   403 AA;  44470 MW;  E916200641D72B40 CRC64;
     MTTLDESLAL IGRGAEEILK LDQLEARLTS GVPLRVKAGF DPTAPDLHLG HTVLLNKMRQ
     FQQLGHQVIF LIGDFTGMIG DPSGKNATRK PLSREDVLAN ARTYEEQVFK ILDRERTEVR
     FNSEWFGQMS AADMIKLSAQ HTVARMLERD DFAKRFGSQQ PIAIHEFLYP LVQGYDSVAL
     RADVELGGTD QKFNLLMGRG LQEHYGQAPQ IVLTMPLLEG LEGVAKMSKS LGNYIGINEP
     AIDIVTKTMK IGDELTWRWI DLLSLDISVA EAVRLKEQVT SGELHPREVK LRLARELATR
     FHDAATAEQA IAGWHAVVTG QGDTSLLPLQ EVVVPAEGLR IASLLTAAGL TPSNSEATRK
     LKERAVKIDG EVLEDATRVF TQGFEGVIQV GKRNFARVSL VIG
 
 
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