ID   SYY_NATPD               Reviewed;         345 AA.
AC   Q3IQU8;
DT   13-JUN-2006, integrated into UniProtKB/Swiss-Prot.
DT   08-NOV-2005, sequence version 1.
DT   03-AUG-2022, entry version 98.
DE   RecName: Full=Tyrosine--tRNA ligase {ECO:0000255|HAMAP-Rule:MF_02008};
DE            EC=6.1.1.1 {ECO:0000255|HAMAP-Rule:MF_02008};
DE   AltName: Full=Tyrosyl-tRNA synthetase {ECO:0000255|HAMAP-Rule:MF_02008};
DE            Short=TyrRS {ECO:0000255|HAMAP-Rule:MF_02008};
GN   Name=tyrS {ECO:0000255|HAMAP-Rule:MF_02008}; OrderedLocusNames=NP_2810A;
OS   Natronomonas pharaonis (strain ATCC 35678 / DSM 2160 / CIP 103997 / JCM
OS   8858 / NBRC 14720 / NCIMB 2260 / Gabara) (Halobacterium pharaonis).
OC   Archaea; Euryarchaeota; Stenosarchaea group; Halobacteria; Halobacteriales;
OC   Haloarculaceae; Natronomonas.
OX   NCBI_TaxID=348780;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 35678 / DSM 2160 / CIP 103997 / JCM 8858 / NBRC 14720 / NCIMB
RC   2260 / Gabara;
RX   PubMed=16169924; DOI=10.1101/gr.3952905;
RA   Falb M., Pfeiffer F., Palm P., Rodewald K., Hickmann V., Tittor J.,
RA   Oesterhelt D.;
RT   "Living with two extremes: conclusions from the genome sequence of
RT   Natronomonas pharaonis.";
RL   Genome Res. 15:1336-1343(2005).
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_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:0000255|HAMAP-Rule:MF_02008};
CC   -!- SUBUNIT: Homodimer. {ECO:0000255|HAMAP-Rule:MF_02008}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_02008}.
CC   -!- SIMILARITY: Belongs to the class-I aminoacyl-tRNA synthetase family.
CC       TyrS type 3 subfamily. {ECO:0000255|HAMAP-Rule:MF_02008}.
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DR   EMBL; CR936257; CAI49496.1; -; Genomic_DNA.
DR   RefSeq; WP_011323121.1; NC_007426.1.
DR   AlphaFoldDB; Q3IQU8; -.
DR   SMR; Q3IQU8; -.
DR   STRING; 348780.NP_2810A; -.
DR   PRIDE; Q3IQU8; -.
DR   EnsemblBacteria; CAI49496; CAI49496; NP_2810A.
DR   GeneID; 3703432; -.
DR   KEGG; nph:NP_2810A; -.
DR   eggNOG; arCOG01886; Archaea.
DR   HOGENOM; CLU_035267_0_1_2; -.
DR   OMA; YIGFEIS; -.
DR   OrthoDB; 59062at2157; -.
DR   Proteomes; UP000002698; 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; -; 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   Pfam; PF00579; tRNA-synt_1b; 1.
DR   PIRSF; PIRSF006588; TyrRS_arch_euk; 1.
DR   PRINTS; PR01040; TRNASYNTHTYR.
DR   TIGRFAMs; TIGR00234; tyrS; 1.
DR   PROSITE; PS00178; AA_TRNA_LIGASE_I; 1.
PE   3: Inferred from homology;
KW   Aminoacyl-tRNA synthetase; ATP-binding; Cytoplasm; Ligase;
KW   Nucleotide-binding; Protein biosynthesis; Reference proteome.
FT   CHAIN           1..345
FT                   /note="Tyrosine--tRNA ligase"
FT                   /id="PRO_0000240261"
FT   MOTIF           41..49
FT                   /note="'HIGH' region"
FT   BINDING         36
FT                   /ligand="L-tyrosine"
FT                   /ligand_id="ChEBI:CHEBI:58315"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_02008"
FT   BINDING         163
FT                   /ligand="L-tyrosine"
FT                   /ligand_id="ChEBI:CHEBI:58315"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_02008"
FT   BINDING         167
FT                   /ligand="L-tyrosine"
FT                   /ligand_id="ChEBI:CHEBI:58315"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_02008"
FT   BINDING         170
FT                   /ligand="L-tyrosine"
FT                   /ligand_id="ChEBI:CHEBI:58315"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_02008"
FT   BINDING         185
FT                   /ligand="L-tyrosine"
FT                   /ligand_id="ChEBI:CHEBI:58315"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_02008"
SQ   SEQUENCE   345 AA;  37891 MW;  AD9478B4F28339D8 CRC64;
     MDTVERTDLV ARFTEEVIER DEIETLFEEQ DEPTAYIGYA PTGEMHIGHF TTMRKLADFI
     DAGLDVTVLV ADLHAHLDDA KSPFELLEAR SEYYERAIEG MIAAAGADPD GISFIRGTDF
     QLDEPYTLDL YRLLADTTLS RAQRAGSEVV RQSENPSLGS LVYTLMQALD VAALDADIAY
     GGIDQRGIYM LAREQLPDHG YDKPACVFAP LLSGLSGGKM SASEAGSKIN LTDDGEAIDE
     KIGGAYCPAG ETEENGVLEY LEYLVFPVFD QRDTSFVVER PEKYGGDLEY GTYDELEADF
     VSGELHPADL KPAAAAAIDE VVAPVRELLL EDPELLASAY PERYE