ID   SYYC_CHICK              Reviewed;         527 AA.
AC   Q5ZJ08;
DT   13-JUN-2006, integrated into UniProtKB/Swiss-Prot.
DT   23-NOV-2004, sequence version 1.
DT   03-AUG-2022, entry version 92.
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; ORFNames=RCJMB04_21p3;
OS   Gallus gallus (Chicken).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC   Coelurosauria; Aves; Neognathae; Galloanserae; Galliformes; Phasianidae;
OC   Phasianinae; Gallus.
OX   NCBI_TaxID=9031;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=CB; TISSUE=Bursa of Fabricius;
RX   PubMed=15642098; DOI=10.1186/gb-2004-6-1-r6;
RA   Caldwell R.B., Kierzek A.M., Arakawa H., Bezzubov Y., Zaim J., Fiedler P.,
RA   Kutter S., Blagodatski A., Kostovska D., Koter M., Plachy J., Carninci P.,
RA   Hayashizaki Y., Buerstedde J.-M.;
RT   "Full-length cDNAs from chicken bursal lymphocytes to facilitate gene
RT   function analysis.";
RL   Genome Biol. 6:R6.1-R6.9(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: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; AJ720626; CAG32285.1; -; mRNA.
DR   RefSeq; NP_001006314.1; NM_001006314.1.
DR   AlphaFoldDB; Q5ZJ08; -.
DR   SMR; Q5ZJ08; -.
DR   STRING; 9031.ENSGALP00000005633; -.
DR   PaxDb; Q5ZJ08; -.
DR   GeneID; 419666; -.
DR   KEGG; gga:419666; -.
DR   CTD; 107271; -.
DR   VEuPathDB; HostDB:geneid_419666; -.
DR   eggNOG; KOG2144; Eukaryota.
DR   eggNOG; KOG2241; Eukaryota.
DR   InParanoid; Q5ZJ08; -.
DR   PhylomeDB; Q5ZJ08; -.
DR   PRO; PR:Q5ZJ08; -.
DR   Proteomes; UP000000539; 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..527
FT                   /note="Tyrosine--tRNA ligase, cytoplasmic"
FT                   /id="PRO_0000239692"
FT   DOMAIN          363..467
FT                   /note="tRNA-binding"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00209"
FT   REGION          337..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   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   527 AA;  59284 MW;  C09BB7DAB8B89D60 CRC64;
     METASGPQEK YQLITRNLQE VLGEDKLMAI LKEREVKIYW GTATTGKPHV AYFVPMSKIA
     DFLKAGCEVT ILFADLHAYL DNMKAPWELL ELRTRYYEHV IKAMLESIGV PLEKLKFIRG
     TDYQLSKEYT LDVYRLSSVV TQHDAKKAGA EVVKQVEHPL LSGLLYPGLQ ALDEEYLKVD
     AQFGGVDQRK IFTFAEKYLP SLGYAKRIHL MNPMVPGLTG SKMSSSEEDS KIDLLDRKED
     VKKKLKKAFC EPGNIENNGV LSFIKHVLFP LKSEFVILRE EKWGGNKTYT AYETLEKDFA
     EQVVHPGDLK NSVEAALNKL LDPIREKFNS PELKKLTNAA YPNPSKAKPA EKGTKNSEPE
     TIVPSRLDIR VGKVVSVEKH PDADSLYVEK IDVGEPEPRT VVSGLVQFVP KEQLQDRLVV
     LLCNLKPQKM RGVESQGMVL CASSVGEPRQ VEPLDPPAEC CAGERVYVEG YEDGEPDDEL
     KPKKKVFEKL QADFRISEDC IAQWKERNFL TKLGSISCKS LKGGSIS