ID SYY_BURP1 Reviewed; 413 AA.
AC Q3JNS0;
DT 30-MAY-2006, integrated into UniProtKB/Swiss-Prot.
DT 30-MAY-2006, sequence version 2.
DT 13-SEP-2023, entry version 88.
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};
GN OrderedLocusNames=BURPS1710b_3412;
OS Burkholderia pseudomallei (strain 1710b).
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Burkholderiaceae; Burkholderia; pseudomallei group.
OX NCBI_TaxID=320372;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=1710b;
RX PubMed=20333227; DOI=10.1093/gbe/evq003;
RA Losada L., Ronning C.M., DeShazer D., Woods D., Fedorova N., Kim H.S.,
RA Shabalina S.A., Pearson T.R., Brinkac L., Tan P., Nandi T., Crabtree J.,
RA Badger J., Beckstrom-Sternberg S., Saqib M., Schutzer S.E., Keim P.,
RA Nierman W.C.;
RT "Continuing evolution of Burkholderia mallei through genome reduction and
RT large-scale rearrangements.";
RL Genome Biol. Evol. 2:102-116(2010).
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}.
CC -!- SEQUENCE CAUTION:
CC Sequence=ABA49713.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; CP000124; ABA49713.1; ALT_INIT; Genomic_DNA.
DR RefSeq; WP_004527727.1; NC_007434.1.
DR AlphaFoldDB; Q3JNS0; -.
DR SMR; Q3JNS0; -.
DR EnsemblBacteria; ABA49713; ABA49713; BURPS1710b_3412.
DR KEGG; bpm:BURPS1710b_3412; -.
DR HOGENOM; CLU_024003_5_0_4; -.
DR Proteomes; UP000002700; Chromosome I.
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; 3.40.50.620; HUPs; 1.
DR Gene3D; 3.10.290.10; RNA-binding S4 domain; 1.
DR Gene3D; 1.10.240.10; Tyrosyl-Transfer RNA Synthetase; 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 NCBIfam; TIGR00234; tyrS; 1.
DR PANTHER; PTHR11766:SF1; TYROSINE--TRNA LIGASE; 1.
DR PANTHER; PTHR11766; TYROSYL-TRNA SYNTHETASE; 1.
DR Pfam; PF01479; S4; 1.
DR Pfam; PF00579; tRNA-synt_1b; 1.
DR PRINTS; PR01040; TRNASYNTHTYR.
DR SMART; SM00363; S4; 1.
DR SUPFAM; SSF55174; Alpha-L RNA-binding motif; 1.
DR SUPFAM; SSF52374; Nucleotidylyl transferase; 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..413
FT /note="Tyrosine--tRNA ligase"
FT /id="PRO_0000236702"
FT DOMAIN 351..411
FT /note="S4 RNA-binding"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02007"
FT MOTIF 59..68
FT /note="'HIGH' region"
FT MOTIF 243..247
FT /note="'KMSKS' region"
FT BINDING 246
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02007"
SQ SEQUENCE 413 AA; 45660 MW; 498C85462F3F5D6F CRC64;
MSTDPTSKPA FPITDEVRHA LAVTKRGVDE LLIEEEFAQK LAKSAATDKP LRIKLGLDPT
APDIHLGHTV VLNKMRQLQD LGHTVIFLIG DFTSLIGDPS GRNATRPPLT REQIESNAKT
YFEQAALVLD RAKTEIRYNS EWSMPLGADG MIKLASRYTV ARMLEREDFT KRFQGGIPIS
IHEFLYPLMQ GYDSVALNAD LELGGTDQKF NLLVGRELQK QYGQEQQCIL TMPLLEGLDG
VEKMSKSKGN YVGISEKPTD MFGKLMSISD VLMWRYFELL SFRSLDEIAR FRGEAEGGRN
PRDFKVMLAQ EIVARFHSQA DAERALEDFN HRAKGGVPDD IPAVTLAGAP LAIGQLLKQA
GLVPSTSEAL RNIEQGGVKI DGATVSDKAL KVDAGEFVVQ VGKRRFARVT LTA
//
