ID A0A1Q5PKK1_9ACTO Unreviewed; 412 AA.
AC A0A1Q5PKK1;
DT 12-APR-2017, integrated into UniProtKB/TrEMBL.
DT 12-APR-2017, sequence version 1.
DT 27-MAR-2024, entry version 29.
DE RecName: Full=Tyrosine--tRNA ligase {ECO:0000256|HAMAP-Rule:MF_02006};
DE EC=6.1.1.1 {ECO:0000256|HAMAP-Rule:MF_02006};
DE AltName: Full=Tyrosyl-tRNA synthetase {ECO:0000256|HAMAP-Rule:MF_02006};
DE Short=TyrRS {ECO:0000256|HAMAP-Rule:MF_02006};
GN Name=tyrS {ECO:0000256|HAMAP-Rule:MF_02006};
GN ORFNames=BSR29_05945 {ECO:0000313|EMBL:OKL47165.1};
OS Boudabousia liubingyangii.
OC Bacteria; Actinomycetota; Actinomycetes; Actinomycetales; Actinomycetaceae;
OC Boudabousia.
OX NCBI_TaxID=1921764 {ECO:0000313|EMBL:OKL47165.1, ECO:0000313|Proteomes:UP000186785};
RN [1] {ECO:0000313|EMBL:OKL47165.1, ECO:0000313|Proteomes:UP000186785}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=VUL4_2 {ECO:0000313|EMBL:OKL47165.1,
RC ECO:0000313|Proteomes:UP000186785};
RA Meng X.;
RT "Actinomyces gypaetusis sp. nov. isolated from the vulture Gypaetus
RT barbatus in Qinghai Tibet Plateau China.";
RL Submitted (NOV-2016) 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_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:0000256|ARBA:ARBA00000069, ECO:0000256|HAMAP-
CC Rule:MF_02006};
CC -!- SUBUNIT: Homodimer. {ECO:0000256|HAMAP-Rule:MF_02006}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_02006}.
CC -!- SIMILARITY: Belongs to the class-I aminoacyl-tRNA synthetase family.
CC TyrS type 1 subfamily. {ECO:0000256|HAMAP-Rule:MF_02006}.
CC -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC feature annotation. {ECO:0000256|HAMAP-Rule:MF_02006}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:OKL47165.1}.
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DR EMBL; MQSV01000004; OKL47165.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1Q5PKK1; -.
DR STRING; 1921764.BSR28_08335; -.
DR Proteomes; UP000186785; 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_02006; Tyr_tRNA_synth_type1; 1.
DR InterPro; IPR002305; aa-tRNA-synth_Ic.
DR InterPro; IPR014729; Rossmann-like_a/b/a_fold.
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 NCBIfam; TIGR00234; tyrS; 1.
DR PANTHER; PTHR11766:SF0; TYROSINE--TRNA LIGASE, MITOCHONDRIAL; 1.
DR PANTHER; PTHR11766; TYROSYL-TRNA SYNTHETASE; 1.
DR Pfam; PF00579; tRNA-synt_1b; 1.
DR PRINTS; PR01040; TRNASYNTHTYR.
DR SUPFAM; SSF55174; Alpha-L RNA-binding motif; 1.
DR SUPFAM; SSF52374; Nucleotidylyl transferase; 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_02006};
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|HAMAP-
KW Rule:MF_02006}; Cytoplasm {ECO:0000256|HAMAP-Rule:MF_02006};
KW Ligase {ECO:0000256|ARBA:ARBA00022598, ECO:0000256|HAMAP-Rule:MF_02006};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|HAMAP-
KW Rule:MF_02006};
KW Protein biosynthesis {ECO:0000256|ARBA:ARBA00022917, ECO:0000256|HAMAP-
KW Rule:MF_02006}; Reference proteome {ECO:0000313|Proteomes:UP000186785};
KW RNA-binding {ECO:0000256|PROSITE-ProRule:PRU00182}.
FT MOTIF 222..226
FT /note="'KMSKS' region"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02006"
FT BINDING 27
FT /ligand="L-tyrosine"
FT /ligand_id="ChEBI:CHEBI:58315"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02006"
FT BINDING 162
FT /ligand="L-tyrosine"
FT /ligand_id="ChEBI:CHEBI:58315"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02006"
FT BINDING 166
FT /ligand="L-tyrosine"
FT /ligand_id="ChEBI:CHEBI:58315"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02006"
FT BINDING 225
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02006"
SQ SEQUENCE 412 AA; 45123 MW; 08A1F205C2DAEF0E CRC64;
MWRGLISQST DLDALREAMD AGPITFYTGY DPTAPSLHHG HLVQLIVMRH LQLAGHRPLA
LVGGATGLIG DPRQSGERTL NEADVVADWA DKLRAQIERF LSFEGDNAAR MVNNYEWTGD
LTAIDLLRGV GKYFRLGTMI AKDTVARRLA SEEGISFTEF SYQLLQANDF RELYKRYGCT
LQTGGNDQWG NLVGGTELIR KSEGASVHVL ATPLITKADG TKFGKSEGGA IWLNPEMLSP
YAFYQFWLNS DDADIERFLK VFTFLSREEI ETVVAQSKEE PWKRLGQRRL AEEVTTLVHG
EEATKKVIAA SEALFSGGDL SALDAQTLID ATSSLPRAEV ELGVTTVIDL LADSGLEKGR
GAARRTVASG GAYLNGVKVE DEEQTISESD LLPGNLVLFR KGRKNLGVGV VK
//
