ID   SYYC_XENLA              Reviewed;         528 AA.
AC   Q7ZX51;
DT   13-JUN-2006, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2003, sequence version 1.
DT   03-AUG-2022, entry version 82.
DE   RecName: Full=Tyrosine--tRNA ligase, cytoplasmic;
DE            EC=6.1.1.1;
DE   AltName: Full=Tyrosyl-tRNA synthetase;
DE            Short=TyrRS;
GN   Name=yars1; Synonyms=yars;
OS   Xenopus laevis (African clawed frog).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC   Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Xenopus.
OX   NCBI_TaxID=8355;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Embryo;
RG   NIH - Xenopus Gene Collection (XGC) project;
RL   Submitted (JAN-2003) 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:0000250}.
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   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the class-I aminoacyl-tRNA synthetase family.
CC       {ECO:0000305}.
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DR   EMBL; BC045236; AAH45236.1; -; mRNA.
DR   RefSeq; NP_001080746.1; NM_001087277.1.
DR   AlphaFoldDB; Q7ZX51; -.
DR   SMR; Q7ZX51; -.
DR   DNASU; 380438; -.
DR   GeneID; 380438; -.
DR   KEGG; xla:380438; -.
DR   CTD; 380438; -.
DR   Xenbase; XB-GENE-491612; yars1.S.
DR   OrthoDB; 852081at2759; -.
DR   Proteomes; UP000186698; Chromosome 2S.
DR   Bgee; 380438; Expressed in stomach and 19 other tissues.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0000049; F:tRNA binding; IEA:UniProtKB-KW.
DR   GO; GO:0004831; F:tyrosine-tRNA ligase activity; IEA:UniProtKB-EC.
DR   GO; GO:0006437; P:tyrosyl-tRNA aminoacylation; IEA:InterPro.
DR   CDD; cd00805; TyrRS_core; 1.
DR   Gene3D; 2.40.50.140; -; 1.
DR   Gene3D; 3.40.50.620; -; 1.
DR   InterPro; IPR002305; aa-tRNA-synth_Ic.
DR   InterPro; IPR012340; NA-bd_OB-fold.
DR   InterPro; IPR014729; Rossmann-like_a/b/a_fold.
DR   InterPro; IPR002547; tRNA-bd_dom.
DR   InterPro; IPR002307; Tyr-tRNA-ligase.
DR   Pfam; PF00579; tRNA-synt_1b; 1.
DR   Pfam; PF01588; tRNA_bind; 1.
DR   PRINTS; PR01040; TRNASYNTHTYR.
DR   SUPFAM; SSF50249; SSF50249; 1.
DR   TIGRFAMs; TIGR00234; tyrS; 1.
DR   PROSITE; PS50886; TRBD; 1.
PE   2: Evidence at transcript level;
KW   Aminoacyl-tRNA synthetase; ATP-binding; Cytoplasm; Ligase;
KW   Nucleotide-binding; Protein biosynthesis; Reference proteome; RNA-binding;
KW   tRNA-binding.
FT   CHAIN           1..528
FT                   /note="Tyrosine--tRNA ligase, cytoplasmic"
FT                   /id="PRO_0000239694"
FT   DOMAIN          364..468
FT                   /note="tRNA-binding"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00209"
FT   REGION          332..362
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOTIF           44..52
FT                   /note="'HIGH' region"
FT                   /evidence="ECO:0000250"
FT   MOTIF           222..226
FT                   /note="'KMSKS' region"
FT                   /evidence="ECO:0000250"
FT   COMPBIAS        342..362
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         39
FT                   /ligand="L-tyrosine"
FT                   /ligand_id="ChEBI:CHEBI:58315"
FT                   /evidence="ECO:0000250"
FT   BINDING         166
FT                   /ligand="L-tyrosine"
FT                   /ligand_id="ChEBI:CHEBI:58315"
FT                   /evidence="ECO:0000250"
FT   BINDING         170
FT                   /ligand="L-tyrosine"
FT                   /ligand_id="ChEBI:CHEBI:58315"
FT                   /evidence="ECO:0000250"
FT   BINDING         173
FT                   /ligand="L-tyrosine"
FT                   /ligand_id="ChEBI:CHEBI:58315"
FT                   /evidence="ECO:0000250"
FT   BINDING         188
FT                   /ligand="L-tyrosine"
FT                   /ligand_id="ChEBI:CHEBI:58315"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   528 AA;  58874 MW;  556EDF9DDA652275 CRC64;
     MGDSLTLEGK AQLITRNLQE LLGEDKMKEI LKERPLRIYW GTATTGKPHV AYFVPMSKIA
     DFLKAGCEVT ILFADLHAYL DNMKAPWDLL ELRTRYYEQV IQAMLQSIGV PLERLRFIRG
     TEFQLSKEYT LDVYRLSSVV TQHDAKKAGA EVVKQVEHPL LSGLLYPGLQ ALDEEYLKVD
     AQFGGVDQRK IFTFAEKYLP ALGYAKRIHL MNPMVPGLTG AKMSSSEEES KIDLLDSPAD
     VKKKLKKAFC EPGNVENNGV LSFVRHVLFP LKSEFVVLRD EKFGGNKTYT DFETLEKDFA
     EELVHPGDLK ASVEKALNKL LHPIREKFNS PEMKKLSNDA YPDASKQKSV PKGSTKNSGT
     EEIDPSLLDL RVGKILSVSQ HPDADSLYVE SVDVGEANPR CVVSGLVQYV PSDQLLGRSV
     VLLCNLKPQK MRGIESQGML LCASTEGEQK QVEPLDPPSG SAPGERIYIE GYENGEPEGE
     LKPKKKVFEK LQVDFRISDD LCAQWKGKNF LTKLGSVTCK TLRGGSIG