ID   SYY_SULIM               Reviewed;         361 AA.
AC   C3MYZ9;
DT   22-SEP-2009, integrated into UniProtKB/Swiss-Prot.
DT   16-JUN-2009, sequence version 1.
DT   03-AUG-2022, entry version 61.
DE   RecName: Full=Tyrosine--tRNA ligase {ECO:0000255|HAMAP-Rule:MF_02009};
DE            EC=6.1.1.1 {ECO:0000255|HAMAP-Rule:MF_02009};
DE   AltName: Full=Tyrosyl-tRNA synthetase {ECO:0000255|HAMAP-Rule:MF_02009};
DE            Short=TyrRS {ECO:0000255|HAMAP-Rule:MF_02009};
GN   Name=tyrS {ECO:0000255|HAMAP-Rule:MF_02009}; OrderedLocusNames=M1425_2042;
OS   Sulfolobus islandicus (strain M.14.25 / Kamchatka #1).
OC   Archaea; Crenarchaeota; Thermoprotei; Sulfolobales; Sulfolobaceae;
OC   Sulfolobus.
OX   NCBI_TaxID=427317;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=M.14.25 / Kamchatka #1;
RX   PubMed=19435847; DOI=10.1073/pnas.0808945106;
RA   Reno M.L., Held N.L., Fields C.J., Burke P.V., Whitaker R.J.;
RT   "Biogeography of the Sulfolobus islandicus pan-genome.";
RL   Proc. Natl. Acad. Sci. U.S.A. 106:8605-8610(2009).
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_02009}.
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_02009};
CC   -!- SUBUNIT: Homodimer. {ECO:0000255|HAMAP-Rule:MF_02009}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_02009}.
CC   -!- SIMILARITY: Belongs to the class-I aminoacyl-tRNA synthetase family.
CC       TyrS type 4 subfamily. {ECO:0000255|HAMAP-Rule:MF_02009}.
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DR   EMBL; CP001400; ACP38783.1; -; Genomic_DNA.
DR   RefSeq; WP_012712009.1; NC_012588.1.
DR   AlphaFoldDB; C3MYZ9; -.
DR   SMR; C3MYZ9; -.
DR   EnsemblBacteria; ACP38783; ACP38783; M1425_2042.
DR   GeneID; 7795994; -.
DR   GeneID; 7939377; -.
DR   KEGG; sia:M1425_2042; -.
DR   HOGENOM; CLU_035267_1_1_2; -.
DR   OMA; YIGFEIS; -.
DR   Proteomes; UP000001350; 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   CDD; cd00805; TyrRS_core; 1.
DR   Gene3D; 3.40.50.620; -; 1.
DR   HAMAP; MF_02009; Tyr_tRNA_synth_type4; 1.
DR   InterPro; IPR002305; aa-tRNA-synth_Ic.
DR   InterPro; IPR014729; Rossmann-like_a/b/a_fold.
DR   InterPro; IPR002307; Tyr-tRNA-ligase.
DR   InterPro; IPR023678; Tyr-tRNA-ligase_4.
DR   InterPro; IPR023617; Tyr-tRNA-ligase_arc/euk-type.
DR   Pfam; PF00579; tRNA-synt_1b; 2.
DR   PIRSF; PIRSF006588; TyrRS_arch_euk; 1.
DR   PRINTS; PR01040; TRNASYNTHTYR.
DR   TIGRFAMs; TIGR00234; tyrS; 1.
PE   3: Inferred from homology;
KW   Aminoacyl-tRNA synthetase; ATP-binding; Cytoplasm; Ligase;
KW   Nucleotide-binding; Protein biosynthesis.
FT   CHAIN           1..361
FT                   /note="Tyrosine--tRNA ligase"
FT                   /id="PRO_1000216403"
FT   MOTIF           236..240
FT                   /note="'KMSKS' region"
FT   BINDING         36
FT                   /ligand="L-tyrosine"
FT                   /ligand_id="ChEBI:CHEBI:58315"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_02009"
FT   BINDING         162
FT                   /ligand="L-tyrosine"
FT                   /ligand_id="ChEBI:CHEBI:58315"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_02009"
FT   BINDING         166
FT                   /ligand="L-tyrosine"
FT                   /ligand_id="ChEBI:CHEBI:58315"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_02009"
FT   BINDING         169
FT                   /ligand="L-tyrosine"
FT                   /ligand_id="ChEBI:CHEBI:58315"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_02009"
FT   BINDING         184
FT                   /ligand="L-tyrosine"
FT                   /ligand_id="ChEBI:CHEBI:58315"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_02009"
FT   BINDING         239
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_02009"
SQ   SEQUENCE   361 AA;  41296 MW;  EFD6ABA9EA7C15F5 CRC64;
     MSIDQRLQLI TRNAAEIITI DELRKKLESE EKLKGYIGFE PSGLFHIGWL IWTQKVKDLV
     EAGVNMTLLR ATWHAWINDK LGGDLSLIKM AADYTVEVIK NYGVDTTKLN IVDADDMVKE
     KDYWALVIKV AKNSSLARIK RALTIMGRRA EEAEIDASKL IYPAMQVSDI FYLDLDIALG
     GTDQRKAHML ARDVAEKMGK KKIVSIHTPL LVGLQGGQRM SITEGMEEDD IQAEIKMSKS
     KPESAIFVSD SREDVERKIM GAYCPKGVAE NNPILQILKY IIFPRYNFVK IERDIRYGGD
     VEFKDYEELE RAYIEGKIHP MDLKKATARR LNEILEPIRK SLERKPEFEE MIQKISKSVT
     R