SYYC_BOVIN
ID SYYC_BOVIN Reviewed; 528 AA.
AC Q29465; Q9TSJ1;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 4.
DT 03-AUG-2022, entry version 135.
DE RecName: Full=Tyrosine--tRNA ligase, cytoplasmic;
DE EC=6.1.1.1;
DE AltName: Full=Tyrosyl-tRNA synthetase;
DE Short=TyrRS;
DE Contains:
DE RecName: Full=Tyrosine--tRNA ligase, cytoplasmic, N-terminally processed;
GN Name=YARS1; Synonyms=TYRS, YARS;
OS Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Liver;
RA Levanets O.V., Naidenov V.G., Odynets K.A., Woodmaska M.I., Matsuka G.K.H.,
RA Wientjes F.-J., Gassen H.G., Kornelyuk A.I.;
RT "Amino acid sequence of bovine tyrosyl-tRNA synthetase. Possible generation
RT of the isolated cytokine-like C-terminal domain via proteolytic cleavage at
RT the 'PEST'-like sequence.";
RL Submitted (AUG-1998) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 17-212.
RC TISSUE=Liver;
RA Levanets O.V., Naidenov V.G., Woodmaska M.I., Odynets K.A., Matsuka G.H.,
RA Kornelyuk A.I.;
RT "PCR-amplification, cloning and sequencing of nucleotide-binding domain of
RT mammalian tyrosyl-tRNA synthetase.";
RL Biopolim. Kletka 12:66-71(1996).
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 -!- SUBUNIT: Homodimer. {ECO:0000250}.
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; AF087021; AAC82467.1; -; mRNA.
DR EMBL; X96373; CAA65245.1; -; Genomic_DNA.
DR RefSeq; NP_776645.1; NM_174220.2.
DR AlphaFoldDB; Q29465; -.
DR SMR; Q29465; -.
DR STRING; 9913.ENSBTAP00000024051; -.
DR PaxDb; Q29465; -.
DR PeptideAtlas; Q29465; -.
DR PRIDE; Q29465; -.
DR GeneID; 281581; -.
DR KEGG; bta:281581; -.
DR CTD; 8565; -.
DR eggNOG; KOG2144; Eukaryota.
DR eggNOG; KOG2241; Eukaryota.
DR InParanoid; Q29465; -.
DR OrthoDB; 852081at2759; -.
DR Proteomes; UP000009136; Unplaced.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0031090; C:organelle membrane; IEA:UniProt.
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 Acetylation; Aminoacyl-tRNA synthetase; ATP-binding; Cytoplasm; Ligase;
KW Nucleotide-binding; Phosphoprotein; Protein biosynthesis;
KW Reference proteome; RNA-binding; tRNA-binding.
FT CHAIN 1..528
FT /note="Tyrosine--tRNA ligase, cytoplasmic"
FT /id="PRO_0000423284"
FT INIT_MET 1
FT /note="Removed; alternate"
FT /evidence="ECO:0000250|UniProtKB:P54577"
FT CHAIN 2..528
FT /note="Tyrosine--tRNA ligase, cytoplasmic, N-terminally
FT processed"
FT /id="PRO_0000055672"
FT DOMAIN 364..468
FT /note="tRNA-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00209"
FT REGION 338..362
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 44..52
FT /note="'HIGH' region"
FT MOTIF 222..226
FT /note="'KMSKS' region"
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"
FT MOD_RES 1
FT /note="N-acetylmethionine"
FT /evidence="ECO:0000250|UniProtKB:P54577"
FT MOD_RES 2
FT /note="N-acetylglycine; in Tyrosine--tRNA ligase,
FT cytoplasmic, N-terminally processed"
FT /evidence="ECO:0000250|UniProtKB:P54577"
FT MOD_RES 197
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P54577"
FT MOD_RES 205
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P54577"
FT MOD_RES 206
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P54577"
FT MOD_RES 386
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P54577"
FT MOD_RES 474
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P54577"
FT MOD_RES 482
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P54577"
FT MOD_RES 490
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P54577"
FT CONFLICT 21
FT /note="V -> A (in Ref. 2; CAA65245)"
FT /evidence="ECO:0000305"
FT CONFLICT 202
FT /note="L -> P (in Ref. 2; CAA65245)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 528 AA; 59149 MW; 44D16CB9F75EA7C3 CRC64;
MGDSLSPEEK LSLITRNLQE VLGEEKLKEI LKERELKVYW GTATTGKPHV AYFVPMSKIA
DFLKAGCEVT ILFADLHAYL DNMKAPWDVL ELRTSYYENV IKAMLESIGV PLEKLRFIKG
TDYQLSKEYT LDVYRLSSVV TQHDAKKAGA EVVKQVEHPL LSGLLYPGLQ ALDEEYLKVD
AQFGGVDQRK IFTFAEKYLP ALGYSKRIHL MNPMVPGLTG SKMSSSEEES KIDLLDRKED
VKKKLKKAFC EPGNVENNGV LAFIRHVLFP LKSEFVILRD EKWGGNKTYT AYLDLEKDFA
DEVVHPGDLK NSVEVALNKL LDPIREKFNT PALKKLSSAA YPDPSKQKPA VKGPAKNSEP
EEVIPSRLDI RVGKVISVDK HPDADSLYVE KIDVGEAEPR TVVSGLVQFV PKEELQDRLV
VVLCNLKPQK MRGVKSQGML LCASVEGVNR KVEPLDPPAG SAPGERVFVK GYEKGQPDEE
LKPKKKVFEK LQADFKISDE YIAQWKQTNF MTKMGSVSCK SLKGGNIS
