SYY_DECAR
ID SYY_DECAR Reviewed; 424 AA.
AC Q47B76;
DT 16-MAY-2006, integrated into UniProtKB/Swiss-Prot.
DT 13-SEP-2005, sequence version 1.
DT 03-AUG-2022, entry version 94.
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=Daro_3175;
OS Dechloromonas aromatica (strain RCB).
OC Bacteria; Proteobacteria; Betaproteobacteria; Rhodocyclales; Azonexaceae;
OC Dechloromonas.
OX NCBI_TaxID=159087;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=RCB;
RX PubMed=19650930; DOI=10.1186/1471-2164-10-351;
RA Salinero K.K., Keller K., Feil W.S., Feil H., Trong S., Di Bartolo G.,
RA Lapidus A.;
RT "Metabolic analysis of the soil microbe Dechloromonas aromatica str. RCB:
RT indications of a surprisingly complex life-style and cryptic anaerobic
RT pathways for aromatic degradation.";
RL BMC Genomics 10:351-351(2009).
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; CP000089; AAZ47905.1; -; Genomic_DNA.
DR RefSeq; WP_011288901.1; NC_007298.1.
DR AlphaFoldDB; Q47B76; -.
DR SMR; Q47B76; -.
DR STRING; 159087.Daro_3175; -.
DR EnsemblBacteria; AAZ47905; AAZ47905; Daro_3175.
DR KEGG; dar:Daro_3175; -.
DR eggNOG; COG0162; Bacteria.
DR HOGENOM; CLU_024003_0_3_4; -.
DR OMA; YMMAKDS; -.
DR OrthoDB; 402899at2; -.
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; 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 3: Inferred from homology;
KW Aminoacyl-tRNA synthetase; ATP-binding; Cytoplasm; Ligase;
KW Nucleotide-binding; Protein biosynthesis; RNA-binding.
FT CHAIN 1..424
FT /note="Tyrosine--tRNA ligase"
FT /id="PRO_0000234704"
FT DOMAIN 357..414
FT /note="S4 RNA-binding"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02006"
FT MOTIF 42..51
FT /note="'HIGH' region"
FT MOTIF 234..238
FT /note="'KMSKS' region"
FT BINDING 37
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 178
FT /ligand="L-tyrosine"
FT /ligand_id="ChEBI:CHEBI:58315"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02006"
FT BINDING 237
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02006"
SQ SEQUENCE 424 AA; 46711 MW; A2E449E862E7DB72 CRC64;
MYQSPLIQDL HDRGLIAQIT DAAALDKLLT EESVTLYCGF DPTADSLHLG HLVPVLILKR
FQEAGHKPIA LVGGATGMIG DPSFKATERK LNTPDVIASW VGKIRGQVEP FLKFDGANAA
IMANNYDWFG GMNCLEFMRD IGKHFSVNAM IKKESVQQRL TREDQGISYT EFSYSLLQGY
DFAELNKRYG CVLQIGGSDQ WGNIVAGTDL TRRLHQKHVF GLTLPLITKA DGTKFGKTES
GAIWLDPKKT SPYAFYQFWL NTSDADVYKF MNFFTFLPVA RIAEIEAADK ASGTKPEAQR
ILAEEATRLV HGEVALMAAR RITECLFSGQ LADLTENDLE QLAQDGMPGV QLEKSNTGLI
DALVASGLAK SKSEARTFIQ SGSVAINGNK AEALDHAIGG DELLYGRFTI LRRGKKNYGL
ISWQ
