ID   SYYC_XENTR              Reviewed;         528 AA.
AC   Q6DIJ1;
DT   13-JUN-2006, integrated into UniProtKB/Swiss-Prot.
DT   16-AUG-2004, sequence version 1.
DT   03-AUG-2022, entry version 96.
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 tropicalis (Western clawed frog) (Silurana tropicalis).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC   Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Silurana.
OX   NCBI_TaxID=8364;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Embryo;
RG   NIH - Xenopus Gene Collection (XGC) project;
RL   Submitted (JUN-2004) 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; BC075547; AAH75547.1; -; mRNA.
DR   RefSeq; NP_001004987.1; NM_001004987.1.
DR   AlphaFoldDB; Q6DIJ1; -.
DR   SMR; Q6DIJ1; -.
DR   STRING; 8364.ENSXETP00000057912; -.
DR   PaxDb; Q6DIJ1; -.
DR   DNASU; 448444; -.
DR   GeneID; 448444; -.
DR   KEGG; xtr:448444; -.
DR   CTD; 8565; -.
DR   Xenbase; XB-GENE-491608; yars1.
DR   eggNOG; KOG2144; Eukaryota.
DR   eggNOG; KOG2241; Eukaryota.
DR   InParanoid; Q6DIJ1; -.
DR   OrthoDB; 852081at2759; -.
DR   Proteomes; UP000008143; Chromosome 2.
DR   Proteomes; UP000790000; Unplaced.
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; IBA:GO_Central.
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_0000239695"
FT   DOMAIN          364..468
FT                   /note="tRNA-binding"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00209"
FT   REGION          335..364
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..361
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;  58958 MW;  982F25E6AE4AB9E5 CRC64;
     MGDGLTPEGK AQLITRNLQE VLGEDKMKEI LKERPLRIYW GTATTGKPHV AYFVPMSKIA
     DFLKAGCEVT ILFADLHAYL DNMKAPWDLL ELRTRYYEQV IQAMLQSIGV PLERLRFIRG
     TEFQLSKEYT LDVYRLSSVV TQHDAKKAGA EVVKQVEHPL LSGLLYPGLQ ALDEEYLKVD
     AQFGGVDQRK IFTFAEKYLP ALGYAKRIHL MNPMVPGLTG AKMSSSEEES KIDLLDSPAD
     VKKKLKKAFC EPGNIENNGV LSFVRHVLFP LKSEFVVLRD EKFGGNKTYT DFETLEKDFT
     EQLVHPGDLK ASVEKALNKL LDPIREKFNS PEMKKLSNDA YPGASKQKTV PKGSTKNSGP
     EEIDPSLLDL RVGKILSVRQ HPDADSLYVE SVDVGEENPR CVVSGLVQYV PSDQLLGRSV
     VLLCNLKPQK MRGIESQGML LCASTEGEQK QVEPLDPPTG SAPGERIYIE GYENGEPEGE
     LKPKKKVFEK LQVDFRISDD LCAQWKGKNF LTKLGSVTCK TLRGGSIS