ID A0A106L0I2_9BURK Unreviewed; 413 AA.
AC A0A106L0I2;
DT 13-APR-2016, integrated into UniProtKB/TrEMBL.
DT 13-APR-2016, sequence version 1.
DT 27-MAR-2024, entry version 43.
DE RecName: Full=Tyrosine--tRNA ligase {ECO:0000256|HAMAP-Rule:MF_02007};
DE EC=6.1.1.1 {ECO:0000256|HAMAP-Rule:MF_02007};
DE AltName: Full=Tyrosyl-tRNA synthetase {ECO:0000256|HAMAP-Rule:MF_02007};
DE Short=TyrRS {ECO:0000256|HAMAP-Rule:MF_02007};
GN Name=tyrS {ECO:0000256|HAMAP-Rule:MF_02007};
GN ORFNames=DF011_12875 {ECO:0000313|EMBL:RQQ13432.1}, WJ35_08440
GN {ECO:0000313|EMBL:AOJ75096.1}, WJ87_15765
GN {ECO:0000313|EMBL:KVP34308.1}, WK55_07205
GN {ECO:0000313|EMBL:KVT62020.1}, WK57_03280
GN {ECO:0000313|EMBL:KWZ59689.1}, WL29_00025
GN {ECO:0000313|EMBL:KWA79951.1}, WL73_15660
GN {ECO:0000313|EMBL:KWE01752.1}, WM16_20295
GN {ECO:0000313|EMBL:KWK71057.1};
OS Burkholderia ubonensis.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Burkholderiaceae; Burkholderia; Burkholderia cepacia complex.
OX NCBI_TaxID=101571 {ECO:0000313|EMBL:RQQ13432.1, ECO:0000313|Proteomes:UP000274995};
RN [1] {ECO:0000313|Proteomes:UP000060630, ECO:0000313|Proteomes:UP000062998}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MSMB1140WGS {ECO:0000313|EMBL:KVT62020.1,
RC ECO:0000313|Proteomes:UP000067765}, MSMB1795WGS
RC {ECO:0000313|EMBL:KVP34308.1, ECO:0000313|Proteomes:UP000067049},
RC MSMB2087WGS {ECO:0000313|EMBL:KWA79951.1,
RC ECO:0000313|Proteomes:UP000060630}, MSMB2167WGS
RC {ECO:0000313|EMBL:KWE01752.1, ECO:0000313|Proteomes:UP000062998}, and
RC MSMB782WGS {ECO:0000313|EMBL:KWK71057.1,
RC ECO:0000313|Proteomes:UP000065504};
RA Sahl J., Keim P., Wagner D.;
RT "Expanding the genomic diversity of Burkholderia species for the
RT development of highly accurate diagnostics.";
RL Submitted (NOV-2015) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:KWZ59689.1, ECO:0000313|Proteomes:UP000070119}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MSMB1157 {ECO:0000313|EMBL:KWZ59689.1,
RC ECO:0000313|Proteomes:UP000070119};
RA Sahl J., Wagner D., Keim P.;
RL Submitted (NOV-2015) to the EMBL/GenBank/DDBJ databases.
RN [3] {ECO:0000313|EMBL:AOJ75096.1, ECO:0000313|Proteomes:UP000243680}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MSMB0783 {ECO:0000313|EMBL:AOJ75096.1,
RC ECO:0000313|Proteomes:UP000243680};
RA Sahl J., Wagner D., Keim P.;
RT "Diversity of Burkholderia near neighbor genomes.";
RL Submitted (DEC-2015) to the EMBL/GenBank/DDBJ databases.
RN [4] {ECO:0000313|EMBL:RQQ13432.1, ECO:0000313|Proteomes:UP000274995}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Bp8958 {ECO:0000313|EMBL:RQQ13432.1,
RC ECO:0000313|Proteomes:UP000274995};
RA Hall C., Sahl J., Wagner D.;
RT "Comparative analysis of Burkholderia isolates from Puerto Rico.";
RL Submitted (AUG-2018) to the EMBL/GenBank/DDBJ databases.
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:0000256|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:0000256|ARBA:ARBA00000069, ECO:0000256|HAMAP-
CC Rule:MF_02007};
CC -!- SUBUNIT: Homodimer. {ECO:0000256|HAMAP-Rule:MF_02007}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_02007}.
CC -!- SIMILARITY: Belongs to the class-I aminoacyl-tRNA synthetase family.
CC TyrS type 2 subfamily. {ECO:0000256|HAMAP-Rule:MF_02007}.
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DR EMBL; CP013420; AOJ75096.1; -; Genomic_DNA.
DR EMBL; LPBA01000079; KVP34308.1; -; Genomic_DNA.
DR EMBL; LPDQ01000042; KVT62020.1; -; Genomic_DNA.
DR EMBL; LPHD01000111; KWA79951.1; -; Genomic_DNA.
DR EMBL; LPIX01000061; KWE01752.1; -; Genomic_DNA.
DR EMBL; LPLU01000104; KWK71057.1; -; Genomic_DNA.
DR EMBL; LNJU01000001; KWZ59689.1; -; Genomic_DNA.
DR EMBL; QTOC01000008; RQQ13432.1; -; Genomic_DNA.
DR RefSeq; WP_010091358.1; NZ_QTOD01000012.1.
DR STRING; 101571.WJ32_03645; -.
DR OrthoDB; 9804243at2; -.
DR Proteomes; UP000060630; Unassembled WGS sequence.
DR Proteomes; UP000062998; Unassembled WGS sequence.
DR Proteomes; UP000065504; Unassembled WGS sequence.
DR Proteomes; UP000067049; Unassembled WGS sequence.
DR Proteomes; UP000067765; Unassembled WGS sequence.
DR Proteomes; UP000070119; Chromosome 1.
DR Proteomes; UP000243680; Chromosome 1.
DR Proteomes; UP000274995; Unassembled WGS sequence.
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; PF13275; S4_2; 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 {ECO:0000256|ARBA:ARBA00023146,
KW ECO:0000256|HAMAP-Rule:MF_02007};
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|HAMAP-
KW Rule:MF_02007}; Cytoplasm {ECO:0000256|HAMAP-Rule:MF_02007};
KW Ligase {ECO:0000256|ARBA:ARBA00022598, ECO:0000256|HAMAP-Rule:MF_02007};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|HAMAP-
KW Rule:MF_02007};
KW Protein biosynthesis {ECO:0000256|ARBA:ARBA00022917, ECO:0000256|HAMAP-
KW Rule:MF_02007}; RNA-binding {ECO:0000256|PROSITE-ProRule:PRU00182}.
FT DOMAIN 351..412
FT /note="RNA-binding S4"
FT /evidence="ECO:0000259|SMART:SM00363"
FT MOTIF 59..68
FT /note="'HIGH' region"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02007"
FT MOTIF 243..247
FT /note="'KMSKS' region"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02007"
FT BINDING 246
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02007"
SQ SEQUENCE 413 AA; 45888 MW; 2BA7275B8E9840DE CRC64;
MSTEPSSKPV FPITDEVRHA LAVTKRGVDE LLIEEEFAQK LARSAATGKP LRIKLGLDPT
APDIHIGHTV VLNKMRQLQD LGHTVIFLIG DFTSLIGDPS GRNATRPPLT REQIEANAKT
YFEQAALVLD RDKTEIRYNS EWSMPLGADG MIKLASRYTV ARILEREDFT KRFQSGVPIS
IHEFLYPLMQ GYDSVALNAD LELGGTDQKF NLLVGRELQK QYGQEQQCIL TMPLLEGLDG
VEKMSKSKGN YVGISEKPND MFGKLMSISD TLMWRYFELL SFRSMDEIVG FRREIETGRN
PRDFKVLLAQ EIVARFHSQA DAERALEDFN HRAKGGVPDD IPSVTLAGAP LAIGQLLKQA
GLVPSTSEAL RNIEQGGVKI DGTAITDKGL KIEAGEYVVQ VGKRRFARVT LTA
//
