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Database: UniProt
Entry: A0A420W9X6_9BACT
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ID   A0A420W9X6_9BACT        Unreviewed;       406 AA.
AC   A0A420W9X6;
DT   08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT   08-MAY-2019, sequence version 1.
DT   13-SEP-2023, entry version 16.
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=C7457_0999 {ECO:0000313|EMBL:RKQ64107.1};
OS   Thermovibrio guaymasensis.
OC   Bacteria; Aquificota; Aquificae; Desulfurobacteriales;
OC   Desulfurobacteriaceae; Thermovibrio.
OX   NCBI_TaxID=240167 {ECO:0000313|EMBL:RKQ64107.1, ECO:0000313|Proteomes:UP000280881};
RN   [1] {ECO:0000313|EMBL:RKQ64107.1, ECO:0000313|Proteomes:UP000280881}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 15521 {ECO:0000313|EMBL:RKQ64107.1,
RC   ECO:0000313|Proteomes:UP000280881};
RA   Goeker M.;
RT   "Genomic Encyclopedia of Type Strains, Phase IV (KMG-IV): sequencing the
RT   most valuable type-strain genomes for metagenomic binning, comparative
RT   biology and taxonomic classification.";
RL   Submitted (OCT-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}.
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:RKQ64107.1}.
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DR   EMBL; RBIE01000001; RKQ64107.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A420W9X6; -.
DR   OrthoDB; 9804243at2; -.
DR   Proteomes; UP000280881; 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; 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 {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};
KW   Cytoplasm {ECO:0000256|ARBA:ARBA00022490, 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|HAMAP-Rule:MF_02007,
KW   ECO:0000256|RuleBase:RU363036};
KW   RNA-binding {ECO:0000256|PROSITE-ProRule:PRU00182}.
FT   DOMAIN          337..400
FT                   /note="RNA-binding S4"
FT                   /evidence="ECO:0000259|SMART:SM00363"
FT   MOTIF           41..50
FT                   /note="'HIGH' region"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_02007"
FT   MOTIF           225..229
FT                   /note="'KMSKS' region"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_02007"
FT   BINDING         228
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_02007"
SQ   SEQUENCE   406 AA;  46710 MW;  A87ABF4D9269D18D CRC64;
     MTPEEQLKVI KRGTAEIIGE EELLEKLKSG RKLRVKAGFD PTAPDLHLGH TVLLWKLRDF
     QELGHEVYFL IGDFTAMIGD PTGKSETRPP LTREEVLKNA ETYAQQVFKI LDPEKTVVVF
     NSEWLGSMTA ADLIKLSSKY TVARMLERDD FEKRFKEGRP IHIHEFIYPL LQGYDSVVLK
     ADVELGGTDQ KFNLLMGRHL QREYGLEEQA CIMMPILEGL DGVQKMSKSL GNYIGILEPP
     EEQFGKVMRI SDDLMWRYYR LVTRVPEEEI EEMERAVKEG RLHPMEAKKR LAETIVKTFH
     GEEAAKRARE HFERVFSRRE LPENIPEPEI TVPENPVWLP RLLKEAGLVK STSEGRRQIR
     GGGVRVDGEK VLDENAKIDV LSKEIILQVG KRRFARVKPE KVKVEK
//
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