ID   SYY_THET8               Reviewed;         432 AA.
AC   Q5SIH0;
DT   30-MAY-2006, integrated into UniProtKB/Swiss-Prot.
DT   21-DEC-2004, sequence version 1.
DT   03-AUG-2022, entry version 97.
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=TTHA1399;
OS   Thermus thermophilus (strain ATCC 27634 / DSM 579 / HB8).
OC   Bacteria; Deinococcus-Thermus; Deinococci; Thermales; Thermaceae; Thermus.
OX   NCBI_TaxID=300852;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 27634 / DSM 579 / HB8;
RA   Masui R., Kurokawa K., Nakagawa N., Tokunaga F., Koyama Y., Shibata T.,
RA   Oshima T., Yokoyama S., Yasunaga T., Kuramitsu S.;
RT   "Complete genome sequence of Thermus thermophilus HB8.";
RL   Submitted (NOV-2004) 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_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}.
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DR   EMBL; AP008226; BAD71222.1; -; Genomic_DNA.
DR   RefSeq; WP_011173450.1; NC_006461.1.
DR   RefSeq; YP_144665.1; NC_006461.1.
DR   AlphaFoldDB; Q5SIH0; -.
DR   SMR; Q5SIH0; -.
DR   STRING; 300852.55772781; -.
DR   EnsemblBacteria; BAD71222; BAD71222; BAD71222.
DR   GeneID; 3168499; -.
DR   KEGG; ttj:TTHA1399; -.
DR   PATRIC; fig|300852.9.peg.1373; -.
DR   eggNOG; COG0162; Bacteria.
DR   HOGENOM; CLU_024003_5_0_0; -.
DR   OMA; YMMAKDS; -.
DR   PhylomeDB; Q5SIH0; -.
DR   Proteomes; UP000000532; 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_02007; Tyr_tRNA_synth_type2; 1.
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; IPR024108; Tyr-tRNA-ligase_bac_2.
DR   PANTHER; PTHR11766; PTHR11766; 2.
DR   PANTHER; PTHR11766:SF1; PTHR11766:SF1; 2.
DR   Pfam; PF00579; tRNA-synt_1b; 1.
DR   PRINTS; PR01040; TRNASYNTHTYR.
DR   TIGRFAMs; TIGR00234; tyrS; 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..432
FT                   /note="Tyrosine--tRNA ligase"
FT                   /id="PRO_0000236772"
FT   DOMAIN          369..430
FT                   /note="S4 RNA-binding"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_02007"
FT   MOTIF           46..55
FT                   /note="'HIGH' region"
FT   MOTIF           232..236
FT                   /note="'KMSKS' region"
FT   BINDING         235
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_02007"
SQ   SEQUENCE   432 AA;  48718 MW;  71B04B8976B8D91B CRC64;
     MAGTGHTPEE ALALLKRGAE EIVPEEELLA KLKEGRPLTV KLGADPTRPD LHLGHAVVLR
     KMRQFQELGH KVVLIIGDFT GMIGDPSGRS KTRPPLTLEE TRENAKTYVA QAGKILRQEP
     HLFELRYNSE WLEGLTFKEV VRLTSLMTVA QMLEREDFKK RYEAGIPISL HELLYPFAQA
     YDSVAIRADV EMGGTDQRFN LLVGREVQRA YGQSPQVCFL MPLLVGLDGR EKMSKSLDNY
     IGLTEPPEAM FKKLMRVPDP LLPSYFRLLT DLEEEEIEAL LKAGPVPAHR VLARLLTAAY
     ALPQIPPRID RAFYESLGYA WEAFGRDKEA GPEEVRRAEA RYDEVAKGGI PEEIPEVTIP
     ASELKEGRIW VARLFTLAGL TPSNAEARRL IQNRGLRLDG EVLTDPMLQV DLSRPRILQR
     GKDRFVRVRL SD