ID A0A1H5WQJ8_9EURY Unreviewed; 331 AA.
AC A0A1H5WQJ8;
DT 18-JAN-2017, integrated into UniProtKB/TrEMBL.
DT 18-JAN-2017, sequence version 1.
DT 24-JAN-2024, entry version 28.
DE RecName: Full=Tyrosine--tRNA ligase {ECO:0000256|HAMAP-Rule:MF_02008};
DE EC=6.1.1.1 {ECO:0000256|HAMAP-Rule:MF_02008};
DE AltName: Full=Tyrosyl-tRNA synthetase {ECO:0000256|HAMAP-Rule:MF_02008};
DE Short=TyrRS {ECO:0000256|HAMAP-Rule:MF_02008};
GN Name=tyrS {ECO:0000256|HAMAP-Rule:MF_02008};
GN ORFNames=DV707_01000 {ECO:0000313|EMBL:QCC46367.1}, SAMN04488133_1361
GN {ECO:0000313|EMBL:SEG01704.1};
OS Halobellus limi.
OC Archaea; Euryarchaeota; Stenosarchaea group; Halobacteria; Haloferacales;
OC Haloferacaceae; Halobellus.
OX NCBI_TaxID=699433 {ECO:0000313|EMBL:SEG01704.1, ECO:0000313|Proteomes:UP000236740};
RN [1] {ECO:0000313|EMBL:SEG01704.1, ECO:0000313|Proteomes:UP000236740}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CGMCC 1.10331 {ECO:0000313|EMBL:SEG01704.1,
RC ECO:0000313|Proteomes:UP000236740};
RA de Groot N.N.;
RL Submitted (OCT-2016) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:QCC46367.1, ECO:0000313|Proteomes:UP000296733}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CGMCC 1.10331 {ECO:0000313|EMBL:QCC46367.1,
RC ECO:0000313|Proteomes:UP000296733};
RX PubMed=30975999; DOI=.1038/s41467-019-09390-9;
RA Xiong L., Liu S., Chen S., Xiao Y., Zhu B., Gao Y., Zhang Y., Chen B.,
RA Luo J., Deng Z., Chen X., Wang L., Chen S.;
RT "A new type of DNA phosphorothioation-based antiviral system in archaea.";
RL Nat. Commun. 10:1688-1688(2019).
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_02008}.
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_02008};
CC -!- SUBUNIT: Homodimer. {ECO:0000256|HAMAP-Rule:MF_02008}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_02008}.
CC -!- SIMILARITY: Belongs to the class-I aminoacyl-tRNA synthetase family.
CC TyrS type 3 subfamily. {ECO:0000256|HAMAP-Rule:MF_02008}.
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DR EMBL; CP031311; QCC46367.1; -; Genomic_DNA.
DR EMBL; FNVN01000001; SEG01704.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1H5WQJ8; -.
DR KEGG; hlm:DV707_01000; -.
DR OrthoDB; 8389at2157; -.
DR Proteomes; UP000236740; Unassembled WGS sequence.
DR Proteomes; UP000296733; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0004831; F:tyrosine-tRNA ligase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0006437; P:tyrosyl-tRNA aminoacylation; IEA:UniProtKB-UniRule.
DR Gene3D; 3.40.50.620; HUPs; 1.
DR Gene3D; 1.10.240.10; Tyrosyl-Transfer RNA Synthetase; 1.
DR HAMAP; MF_02008; Tyr_tRNA_synth_type3; 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; IPR002307; Tyr-tRNA-ligase.
DR InterPro; IPR023684; Tyr-tRNA-ligase_3.
DR InterPro; IPR023617; Tyr-tRNA-ligase_arc/euk-type.
DR NCBIfam; TIGR00234; tyrS; 1.
DR PANTHER; PTHR46264:SF4; TYROSINE--TRNA LIGASE, CYTOPLASMIC; 1.
DR PANTHER; PTHR46264; TYROSINE-TRNA LIGASE; 1.
DR Pfam; PF00579; tRNA-synt_1b; 1.
DR PIRSF; PIRSF006588; TyrRS_arch_euk; 1.
DR PRINTS; PR01040; TRNASYNTHTYR.
DR SUPFAM; SSF52374; Nucleotidylyl transferase; 1.
DR PROSITE; PS00178; AA_TRNA_LIGASE_I; 1.
PE 3: Inferred from homology;
KW Aminoacyl-tRNA synthetase {ECO:0000256|ARBA:ARBA00023146,
KW ECO:0000256|HAMAP-Rule:MF_02008};
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|HAMAP-
KW Rule:MF_02008}; Cytoplasm {ECO:0000256|HAMAP-Rule:MF_02008};
KW Ligase {ECO:0000256|ARBA:ARBA00022598, ECO:0000256|HAMAP-Rule:MF_02008};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|HAMAP-
KW Rule:MF_02008};
KW Protein biosynthesis {ECO:0000256|ARBA:ARBA00022917, ECO:0000256|HAMAP-
KW Rule:MF_02008}; Reference proteome {ECO:0000313|Proteomes:UP000236740}.
FT MOTIF 38..46
FT /note="'HIGH' region"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02008"
FT MOTIF 212..216
FT /note="'KMSKS' region"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02008"
FT BINDING 33
FT /ligand="L-tyrosine"
FT /ligand_id="ChEBI:CHEBI:58315"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02008"
FT BINDING 154
FT /ligand="L-tyrosine"
FT /ligand_id="ChEBI:CHEBI:58315"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02008"
FT BINDING 158
FT /ligand="L-tyrosine"
FT /ligand_id="ChEBI:CHEBI:58315"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02008"
FT BINDING 161
FT /ligand="L-tyrosine"
FT /ligand_id="ChEBI:CHEBI:58315"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02008"
FT BINDING 176
FT /ligand="L-tyrosine"
FT /ligand_id="ChEBI:CHEBI:58315"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02008"
FT BINDING 215
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02008"
SQ SEQUENCE 331 AA; 36395 MW; AB87BEC4F6247803 CRC64;
MDAYDLITRN VSEVVTEEEV RALAESPDGK RAYVGYEPSG VLHIGHMLTA NKLIELQEAG
FEVVVLLADV HAYLNGKGTF AEIRETATRM QEQFVAYGLE ESQTEFVLGS EFQLDEEYVL
DLHALELETS LSRASRAMAE IAGGDTATVA QAVYPLMQAL DIVYLDVDVA IGGMEQRKVH
MLARDTLPSI DADSPTCLHT PLIADLTTGV GKMSSSEGLS ISMEDSESEI EAKVEKAYCP
PTADPDPTDE GEERENPVLQ IFEYHVFPRF GEVVVERPEK YGGDLTYGSY EALEADLESG
ELHPADAKGA LATYLNDLIE PGREKIRQQR D
//
