ID   SYY_SYNAS               Reviewed;         428 AA.
AC   Q2LR98;
DT   16-MAY-2006, integrated into UniProtKB/Swiss-Prot.
DT   21-FEB-2006, sequence version 1.
DT   03-AUG-2022, entry version 89.
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=SYNAS_07330;
GN   ORFNames=SYN_02977;
OS   Syntrophus aciditrophicus (strain SB).
OC   Bacteria; Proteobacteria; Deltaproteobacteria; Syntrophales; Syntrophaceae;
OC   Syntrophus.
OX   NCBI_TaxID=56780;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SB;
RX   PubMed=17442750; DOI=10.1073/pnas.0610456104;
RA   McInerney M.J., Rohlin L., Mouttaki H., Kim U., Krupp R.S.,
RA   Rios-Hernandez L., Sieber J., Struchtemeyer C.G., Bhattacharyya A.,
RA   Campbell J.W., Gunsalus R.P.;
RT   "The genome of Syntrophus aciditrophicus: life at the thermodynamic limit
RT   of microbial growth.";
RL   Proc. Natl. Acad. Sci. U.S.A. 104:7600-7605(2007).
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; CP000252; ABC76612.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q2LR98; -.
DR   SMR; Q2LR98; -.
DR   STRING; 56780.SYN_02977; -.
DR   EnsemblBacteria; ABC76612; ABC76612; SYN_02977.
DR   KEGG; sat:SYN_02977; -.
DR   eggNOG; COG0162; Bacteria.
DR   HOGENOM; CLU_024003_0_3_7; -.
DR   OMA; YHSSVQA; -.
DR   Proteomes; UP000001933; 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; 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; 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..428
FT                   /note="Tyrosine--tRNA ligase"
FT                   /id="PRO_0000234801"
FT   DOMAIN          361..427
FT                   /note="S4 RNA-binding"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_02006"
FT   MOTIF           41..50
FT                   /note="'HIGH' region"
FT   MOTIF           229..233
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         169
FT                   /ligand="L-tyrosine"
FT                   /ligand_id="ChEBI:CHEBI:58315"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_02006"
FT   BINDING         173
FT                   /ligand="L-tyrosine"
FT                   /ligand_id="ChEBI:CHEBI:58315"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_02006"
FT   BINDING         232
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_02006"
SQ   SEQUENCE   428 AA;  48282 MW;  4168FF7E157264BB CRC64;
     MILKNVYDVF MERGFIEQVT DENAVRKALE APLACYIGFD PTARSLHIGS LVPIMALIHL
     QRHGHTSIAL VGGGTALIGD PSGKTEMRQI LTREKIELNA TCMRRQFARY LSFEDKKAMM
     INNADWLTKL NYISFLRDIG RHFSVNKMLA AESYKMRLEK GLNFIEFNYM LLQAYDFLYL
     FQNHNCVMQM GGNDQWGNML AGVDLIRRVE GKVAHSMTFP LLTTATGQKM GKTEKGAVWL
     DRELTSPYEY YQYWINTGDI DVGKFLALFT FLPMEEIHQV KSLSDKELNM AKAILAFEAT
     KITHGEDAAL AAWNASAVAF GVKLIDTSLM PSSTIPRGQL SQDASAIPFI KKSWNELAKG
     IPAYEIMHEC GLCSSKSEAR RLIAQGGGYV NENPIFAFDE LITTEHLDRS GQIKLRKGKK
     KYMIIKVE