SYY_STAAE
ID SYY_STAAE Reviewed; 420 AA.
AC A6QHR2;
DT 20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT 21-AUG-2007, sequence version 1.
DT 03-AUG-2022, entry version 96.
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=NWMN_1622;
OS Staphylococcus aureus (strain Newman).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcaceae;
OC Staphylococcus.
OX NCBI_TaxID=426430;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Newman;
RX PubMed=17951380; DOI=10.1128/jb.01000-07;
RA Baba T., Bae T., Schneewind O., Takeuchi F., Hiramatsu K.;
RT "Genome sequence of Staphylococcus aureus strain Newman and comparative
RT analysis of staphylococcal genomes: polymorphism and evolution of two major
RT pathogenicity islands.";
RL J. Bacteriol. 190:300-310(2008).
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; AP009351; BAF67894.1; -; Genomic_DNA.
DR RefSeq; WP_000186029.1; NZ_CP023390.1.
DR PDB; 1JII; X-ray; 3.20 A; A=1-420.
DR PDB; 1JIJ; X-ray; 3.20 A; A=1-420.
DR PDB; 1JIK; X-ray; 2.80 A; A=1-420.
DR PDB; 1JIL; X-ray; 2.20 A; A=1-420.
DR PDBsum; 1JII; -.
DR PDBsum; 1JIJ; -.
DR PDBsum; 1JIK; -.
DR PDBsum; 1JIL; -.
DR AlphaFoldDB; A6QHR2; -.
DR SMR; A6QHR2; -.
DR EnsemblBacteria; BAF67894; BAF67894; NWMN_1622.
DR KEGG; sae:NWMN_1622; -.
DR HOGENOM; CLU_024003_0_3_9; -.
DR OMA; YMMAKDS; -.
DR BRENDA; 6.1.1.1; 3352.
DR EvolutionaryTrace; A6QHR2; -.
DR Proteomes; UP000006386; 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 DisProt; DP02035; -.
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; 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; IPR024107; Tyr-tRNA-ligase_bac_1.
DR PANTHER; PTHR11766; PTHR11766; 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 1: Evidence at protein level;
KW 3D-structure; Aminoacyl-tRNA synthetase; ATP-binding; Cytoplasm; Ligase;
KW Nucleotide-binding; Protein biosynthesis; RNA-binding.
FT CHAIN 1..420
FT /note="Tyrosine--tRNA ligase"
FT /id="PRO_1000088630"
FT DOMAIN 353..420
FT /note="S4 RNA-binding"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02006"
FT MOTIF 41..50
FT /note="'HIGH' region"
FT MOTIF 231..235
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 170
FT /ligand="L-tyrosine"
FT /ligand_id="ChEBI:CHEBI:58315"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02006"
FT BINDING 174
FT /ligand="L-tyrosine"
FT /ligand_id="ChEBI:CHEBI:58315"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02006"
FT BINDING 234
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02006"
FT HELIX 4..11
FT /evidence="ECO:0007829|PDB:1JIL"
FT STRAND 16..20
FT /evidence="ECO:0007829|PDB:1JII"
FT HELIX 21..30
FT /evidence="ECO:0007829|PDB:1JIL"
FT STRAND 34..39
FT /evidence="ECO:0007829|PDB:1JIL"
FT STRAND 42..45
FT /evidence="ECO:0007829|PDB:1JIL"
FT HELIX 48..62
FT /evidence="ECO:0007829|PDB:1JIL"
FT STRAND 66..71
FT /evidence="ECO:0007829|PDB:1JIL"
FT HELIX 75..77
FT /evidence="ECO:0007829|PDB:1JIL"
FT HELIX 93..110
FT /evidence="ECO:0007829|PDB:1JIL"
FT STRAND 114..118
FT /evidence="ECO:0007829|PDB:1JIL"
FT STRAND 120..123
FT /evidence="ECO:0007829|PDB:1JIL"
FT HELIX 125..128
FT /evidence="ECO:0007829|PDB:1JIL"
FT HELIX 133..139
FT /evidence="ECO:0007829|PDB:1JIL"
FT HELIX 141..143
FT /evidence="ECO:0007829|PDB:1JIL"
FT HELIX 146..150
FT /evidence="ECO:0007829|PDB:1JIL"
FT HELIX 153..155
FT /evidence="ECO:0007829|PDB:1JIL"
FT HELIX 156..159
FT /evidence="ECO:0007829|PDB:1JIL"
FT TURN 160..162
FT /evidence="ECO:0007829|PDB:1JIL"
FT HELIX 165..185
FT /evidence="ECO:0007829|PDB:1JIL"
FT STRAND 187..193
FT /evidence="ECO:0007829|PDB:1JIL"
FT HELIX 194..196
FT /evidence="ECO:0007829|PDB:1JIL"
FT HELIX 197..211
FT /evidence="ECO:0007829|PDB:1JIL"
FT STRAND 217..221
FT /evidence="ECO:0007829|PDB:1JIL"
FT STRAND 227..229
FT /evidence="ECO:0007829|PDB:1JIJ"
FT STRAND 236..239
FT /evidence="ECO:0007829|PDB:1JIL"
FT STRAND 241..243
FT /evidence="ECO:0007829|PDB:1JIL"
FT TURN 244..246
FT /evidence="ECO:0007829|PDB:1JIL"
FT HELIX 249..257
FT /evidence="ECO:0007829|PDB:1JIL"
FT HELIX 261..271
FT /evidence="ECO:0007829|PDB:1JIL"
FT HELIX 276..288
FT /evidence="ECO:0007829|PDB:1JIL"
FT HELIX 290..292
FT /evidence="ECO:0007829|PDB:1JIL"
FT HELIX 294..308
FT /evidence="ECO:0007829|PDB:1JIL"
FT HELIX 310..323
FT /evidence="ECO:0007829|PDB:1JIL"
SQ SEQUENCE 420 AA; 47598 MW; B6916EA4BE4B21B2 CRC64;
MTNVLIEDLK WRGLIYQQTD EQGIEDLLNK EQVTLYCGAD PTADSLHIGH LLPFLTLRRF
QEHGHRPIVL IGGGTGMIGD PSGKSEERVL QTEEQVDKNI EGISKQMHNI FEFGTDHGAV
LVNNRDWLGQ ISLISFLRDY GKHVGVNYML GKDSIQSRLE HGISYTEFTY TILQAIDFGH
LNRELNCKIQ VGGSDQWGNI TSGIELMRRM YGQTDAYGLT IPLVTKSDGK KFGKSESGAV
WLDAEKTSPY EFYQFWINQS DEDVIKFLKY FTFLGKEEID RLEQSKNEAP HLREAQKTLA
EEVTKFIHGE DALNDAIRIS QALFSGDLKS LSAKELKDGF KDVPQVTLSN DTTNIVEVLI
ETGISPSKRQ AREDVNNGAI YINGERQQDV NYALAPEDKI DGEFTIIRRG KKKYFMVNYQ
