SYY_THEMA
ID SYY_THEMA Reviewed; 401 AA.
AC Q9WYU8;
DT 30-MAY-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1999, sequence version 1.
DT 03-AUG-2022, entry version 119.
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=TM_0478;
OS Thermotoga maritima (strain ATCC 43589 / DSM 3109 / JCM 10099 / NBRC 100826
OS / MSB8).
OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga.
OX NCBI_TaxID=243274;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 43589 / DSM 3109 / JCM 10099 / NBRC 100826 / MSB8;
RX PubMed=10360571; DOI=10.1038/20601;
RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., Haft D.H.,
RA Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., McDonald L.A.,
RA Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., Stewart A.M.,
RA Cotton M.D., Pratt M.S., Phillips C.A., Richardson D.L., Heidelberg J.F.,
RA Sutton G.G., Fleischmann R.D., Eisen J.A., White O., Salzberg S.L.,
RA Smith H.O., Venter J.C., Fraser C.M.;
RT "Evidence for lateral gene transfer between Archaea and Bacteria from
RT genome sequence of Thermotoga maritima.";
RL Nature 399:323-329(1999).
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; AE000512; AAD35566.1; -; Genomic_DNA.
DR PIR; F72372; F72372.
DR RefSeq; NP_228288.1; NC_000853.1.
DR RefSeq; WP_004081488.1; NZ_CP011107.1.
DR AlphaFoldDB; Q9WYU8; -.
DR SMR; Q9WYU8; -.
DR STRING; 243274.THEMA_02295; -.
DR EnsemblBacteria; AAD35566; AAD35566; TM_0478.
DR KEGG; tma:TM0478; -.
DR eggNOG; COG0162; Bacteria.
DR InParanoid; Q9WYU8; -.
DR OMA; YMMAKDS; -.
DR OrthoDB; 402899at2; -.
DR Proteomes; UP000008183; Chromosome.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
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; IBA:GO_Central.
DR GO; GO:0043039; P:tRNA aminoacylation; IBA:GO_Central.
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; 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; 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..401
FT /note="Tyrosine--tRNA ligase"
FT /id="PRO_0000236771"
FT DOMAIN 334..395
FT /note="S4 RNA-binding"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02007"
FT MOTIF 41..50
FT /note="'HIGH' region"
FT MOTIF 225..229
FT /note="'KMSKS' region"
FT BINDING 228
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02007"
SQ SEQUENCE 401 AA; 46186 MW; A65F7638A239B210 CRC64;
MTPEEQVKIL KRNVVDLISE EELLDRIKRK GKLRVKLGVD PSRPDLHLGH AVVLRKLREF
QDLGHTVVLI IGDFTARIGD PSGRNETRPM LTKEEVLENA KTYQEQAFKI LDPKRTELRF
NGEWLDRMTF ADVIILASKY TVARMLERDD FAKRFKEGIP IAISEFLYPL AQAYDSVAIQ
SDVELGGTDQ LFNLLVGRKI QEEYGQEPQI VMTMPIIEGT DGKLKMSKSY GNYIAFNDPP
EEMYGKLMSI PDELIIKYMR LLTDIPEERI EEYERKMKEK TINPRDVKMV LAYEITRFFH
GEENAKKAQE HFVKVFQKKE IPDEMPVVEI SQEKNIVDLL VEIGAASSKS EAKRLVSQGG
VYIDGERIED IKFTVEPDGE RVLRVGKRKF YRISGGETKK L
