ID   SYY_DEHM1               Reviewed;         396 AA.
AC   Q3Z8V6;
DT   30-MAY-2006, integrated into UniProtKB/Swiss-Prot.
DT   27-SEP-2005, 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=DET0601;
OS   Dehalococcoides mccartyi (strain ATCC BAA-2266 / KCTC 15142 / 195)
OS   (Dehalococcoides ethenogenes (strain 195)).
OC   Bacteria; Chloroflexi; Dehalococcoidia; Dehalococcoidales;
OC   Dehalococcoidaceae; Dehalococcoides.
OX   NCBI_TaxID=243164;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-2266 / KCTC 15142 / 195;
RX   PubMed=15637277; DOI=10.1126/science.1102226;
RA   Seshadri R., Adrian L., Fouts D.E., Eisen J.A., Phillippy A.M., Methe B.A.,
RA   Ward N.L., Nelson W.C., DeBoy R.T., Khouri H.M., Kolonay J.F., Dodson R.J.,
RA   Daugherty S.C., Brinkac L.M., Sullivan S.A., Madupu R., Nelson K.E.,
RA   Kang K.H., Impraim M., Tran K., Robinson J.M., Forberger H.A., Fraser C.M.,
RA   Zinder S.H., Heidelberg J.F.;
RT   "Genome sequence of the PCE-dechlorinating bacterium Dehalococcoides
RT   ethenogenes.";
RL   Science 307:105-108(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}.
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DR   EMBL; CP000027; AAW40099.1; -; Genomic_DNA.
DR   RefSeq; WP_010936376.1; NC_002936.3.
DR   AlphaFoldDB; Q3Z8V6; -.
DR   SMR; Q3Z8V6; -.
DR   STRING; 243164.DET0601; -.
DR   EnsemblBacteria; AAW40099; AAW40099; DET0601.
DR   KEGG; det:DET0601; -.
DR   PATRIC; fig|243164.10.peg.579; -.
DR   eggNOG; COG0162; Bacteria.
DR   HOGENOM; CLU_024003_5_0_0; -.
DR   OMA; YMMAKDS; -.
DR   OrthoDB; 402899at2; -.
DR   Proteomes; UP000008289; 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; 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; IPR024108; Tyr-tRNA-ligase_bac_2.
DR   PANTHER; PTHR11766; PTHR11766; 1.
DR   PANTHER; PTHR11766:SF1; PTHR11766:SF1; 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..396
FT                   /note="Tyrosine--tRNA ligase"
FT                   /id="PRO_0000236713"
FT   DOMAIN          338..396
FT                   /note="S4 RNA-binding"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_02007"
FT   MOTIF           43..52
FT                   /note="'HIGH' region"
FT   MOTIF           227..231
FT                   /note="'KMSKS' region"
FT   BINDING         230
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_02007"
SQ   SEQUENCE   396 AA;  44240 MW;  4A2EDD530CE50428 CRC64;
     MNQAENRIDQ ILKRGVAEVI VEEDFKKLLL SGKKLRLKEG FDPSSPDIHL GHMVALRKLR
     QLQDLGHQVV LIVGDWTAQI GDPSGASVTR PMLSAEQVKA NAKTYLEQFF KIVDKDKTEV
     RWQSEWYANF KLEDVVRLSS KFTVAQMLAR DDFAKRYAAG KPISVTELLY PMLQAYDSVM
     VKSDVEFGGT DQKFNLLVGR ELQEMLGQKP QQVLMVPILV GTDGVHKMSK SLGNYIGVAE
     EPTEIFGKCM SIPDELILQY FELVTDIPAT EIADFKNQMA NGLVNPMVLK KRLARELITQ
     LYSAAAAEEA DAQFTRVVQR GEIPEDMPEC RLENGESICV IDFIIKADLA KSKSEARRLL
     EQGGVEINSA KISDPGTTVK CGDIIKAGKR RYSKAV