SYY_PICTO
ID SYY_PICTO Reviewed; 329 AA.
AC Q6L2J1;
DT 13-JUN-2006, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 92.
DE RecName: Full=Tyrosine--tRNA ligase {ECO:0000255|HAMAP-Rule:MF_02009};
DE EC=6.1.1.1 {ECO:0000255|HAMAP-Rule:MF_02009};
DE AltName: Full=Tyrosyl-tRNA synthetase {ECO:0000255|HAMAP-Rule:MF_02009};
DE Short=TyrRS {ECO:0000255|HAMAP-Rule:MF_02009};
GN Name=tyrS {ECO:0000255|HAMAP-Rule:MF_02009}; OrderedLocusNames=PTO0226;
OS Picrophilus torridus (strain ATCC 700027 / DSM 9790 / JCM 10055 / NBRC
OS 100828).
OC Archaea; Candidatus Thermoplasmatota; Thermoplasmata; Thermoplasmatales;
OC Picrophilaceae; Picrophilus.
OX NCBI_TaxID=263820;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700027 / DSM 9790 / JCM 10055 / NBRC 100828;
RX PubMed=15184674; DOI=10.1073/pnas.0401356101;
RA Fuetterer O., Angelov A., Liesegang H., Gottschalk G., Schleper C.,
RA Schepers B., Dock C., Antranikian G., Liebl W.;
RT "Genome sequence of Picrophilus torridus and its implications for life
RT around pH 0.";
RL Proc. Natl. Acad. Sci. U.S.A. 101:9091-9096(2004).
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_02009}.
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_02009};
CC -!- SUBUNIT: Homodimer. {ECO:0000255|HAMAP-Rule:MF_02009}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_02009}.
CC -!- SIMILARITY: Belongs to the class-I aminoacyl-tRNA synthetase family.
CC TyrS type 4 subfamily. {ECO:0000255|HAMAP-Rule:MF_02009}.
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DR EMBL; AE017261; AAT42811.1; -; Genomic_DNA.
DR RefSeq; WP_011177027.1; NC_005877.1.
DR AlphaFoldDB; Q6L2J1; -.
DR SMR; Q6L2J1; -.
DR STRING; 263820.PTO0226; -.
DR EnsemblBacteria; AAT42811; AAT42811; PTO0226.
DR GeneID; 2844152; -.
DR KEGG; pto:PTO0226; -.
DR PATRIC; fig|263820.9.peg.244; -.
DR eggNOG; arCOG01886; Archaea.
DR HOGENOM; CLU_035267_1_1_2; -.
DR OMA; VATWHAW; -.
DR OrthoDB; 59062at2157; -.
DR Proteomes; UP000000438; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0004831; F:tyrosine-tRNA ligase activity; IEA:UniProtKB-EC.
DR GO; GO:0006437; P:tyrosyl-tRNA aminoacylation; IEA:InterPro.
DR Gene3D; 3.40.50.620; -; 1.
DR HAMAP; MF_02009; Tyr_tRNA_synth_type4; 1.
DR InterPro; IPR002305; aa-tRNA-synth_Ic.
DR InterPro; IPR014729; Rossmann-like_a/b/a_fold.
DR InterPro; IPR002307; Tyr-tRNA-ligase.
DR InterPro; IPR023678; Tyr-tRNA-ligase_4.
DR InterPro; IPR023617; Tyr-tRNA-ligase_arc/euk-type.
DR Pfam; PF00579; tRNA-synt_1b; 1.
DR PIRSF; PIRSF006588; TyrRS_arch_euk; 1.
DR PRINTS; PR01040; TRNASYNTHTYR.
DR TIGRFAMs; TIGR00234; tyrS; 1.
DR PROSITE; PS00178; AA_TRNA_LIGASE_I; 1.
PE 3: Inferred from homology;
KW Aminoacyl-tRNA synthetase; ATP-binding; Cytoplasm; Ligase;
KW Nucleotide-binding; Protein biosynthesis; Reference proteome.
FT CHAIN 1..329
FT /note="Tyrosine--tRNA ligase"
FT /id="PRO_0000240264"
FT MOTIF 220..224
FT /note="'KMSKS' region"
FT BINDING 31
FT /ligand="L-tyrosine"
FT /ligand_id="ChEBI:CHEBI:58315"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02009"
FT BINDING 157
FT /ligand="L-tyrosine"
FT /ligand_id="ChEBI:CHEBI:58315"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02009"
FT BINDING 161
FT /ligand="L-tyrosine"
FT /ligand_id="ChEBI:CHEBI:58315"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02009"
FT BINDING 164
FT /ligand="L-tyrosine"
FT /ligand_id="ChEBI:CHEBI:58315"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02009"
FT BINDING 179
FT /ligand="L-tyrosine"
FT /ligand_id="ChEBI:CHEBI:58315"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02009"
FT BINDING 223
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02009"
SQ SEQUENCE 329 AA; 37054 MW; 547787F4EA633426 CRC64;
MDAIDFVKKN TEEIVTMDEA FKALNNNPKG YIGFEPSGNP HLGTCLLLAN KINDMVNAGI
KMTVLLADWH AMVNDKLNGD LNEIRKSGEL FKRAWLAAGL NSNVKFVWAS ELVEKSDYWS
LLLKVAKNAS LLRIRRSLPI MGRSEEDADR DFSKYIYPLM QVTDIFYLDV DFALGGMDQR
HAHMLARDIA ERMNIKKPVS VHTPLLSSLK GSGRMDSFKK MSKSEPDSAI FMTDSNDDIK
RKIKNAYCPM KEVNGNPVID ILKYIIFPYY NDKISIKRPE SKGGPVDVDM DSLTRMYISG
EIHPVDLKNA VGELLCDIIG PVREKLTGD