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   16-JUN-2009, entry version 64.
DE   RecName: Full=Tyrosyl-tRNA synthetase, cytoplasmic;
DE            EC=6.1.1.1;
DE   AltName: Full=Tyrosyl--tRNA ligase;
DE            Short=TyrRS;
GN   Name=YARS; Synonyms=TYRS;
OS   Bos taurus (Bovine).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Laurasiatheria; Cetartiodactyla; Ruminantia;
OC   Pecora; Bovidae; 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.,
RA   Matsuka G.K.H., Wientjes F.-J., Gassen H.G., Kornelyuk A.I.;
RT   "Amino acid sequence of bovine tyrosyl-tRNA synthetase. Possible
RT   generation of the isolated cytokine-like C-terminal domain via
RT   proteolytic cleavage at 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.,
RA   Matsuka G.H., Kornelyuk A.I.;
RT   "PCR-amplification, cloning and sequencing of nucleotide-binding
RT   domain of mammalian tyrosyl-tRNA synthetase.";
RL   Biopolim. Kletka 12:66-71(1996).
CC   -!- FUNCTION: Catalyzes the attachment of tyrosine to tRNA(Tyr) in a
CC       two-step reaction: tyrosine is first activated by ATP to form Tyr-
CC       AMP and then transferred to the acceptor end of tRNA(Tyr) (By
CC       similarity).
CC   -!- CATALYTIC ACTIVITY: ATP + L-tyrosine + tRNA(Tyr) = AMP +
CC       diphosphate + L-tyrosyl-tRNA(Tyr).
CC   -!- SUBUNIT: Homodimer (By similarity).
CC   -!- SUBCELLULAR LOCATION: Cytoplasm (By similarity).
CC   -!- SIMILARITY: Belongs to the class-I aminoacyl-tRNA synthetase
CC       family.
CC   -!- SIMILARITY: Contains 1 tRNA-binding domain.
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DR   EMBL; AF087021; AAC82467.1; -; mRNA.
DR   EMBL; X96373; CAA65245.1; -; Genomic_DNA.
DR   IPI; IPI00687540; -.
DR   RefSeq; NP_776645.1; -.
DR   UniGene; Bt.4535; -.
DR   HSSP; P54577; 1N3L.
DR   SMR; Q29465; 5-341, 6-342, 359-527, 360-528.
DR   Ensembl; ENSBTAG00000018065; Bos taurus.
DR   GeneID; 281581; -.
DR   KEGG; bta:281581; -.
DR   HOVERGEN; Q29465; -.
DR   BRENDA; 6.1.1.1; 251.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0005515; F:protein binding; ISS:AgBase.
DR   GO; GO:0000049; F:tRNA binding; IEA:UniProtKB-KW.
DR   GO; GO:0004831; F:tyrosine-tRNA ligase activity; IEA:EC.
DR   GO; GO:0006437; P:tyrosyl-tRNA aminoacylation; IEA:InterPro.
DR   InterPro; IPR001412; aa-tRNA-synth_I_CS.
DR   InterPro; IPR002305; aa-tRNA-synth_Ib.
DR   InterPro; IPR012340; NA-bd_OB-fold.
DR   InterPro; IPR014729; Rossmann-like_a/b/a_fold.
DR   InterPro; IPR002547; tRNA_bd.
DR   InterPro; IPR015624; Tyr-tRNA-synth_Ib_arc/euk.
DR   InterPro; IPR002307; Tyr-tRNA-synth_Ib_bac/mito.
DR   Gene3D; G3DSA:2.40.50.140; OB_NA_bd_sub; 1.
DR   Gene3D; G3DSA:3.40.50.620; Rossmann-like_a/b/a_fold; 1.
DR   PANTHER; PTHR11946:SF8; Tyr-tRNA_synth; 1.
DR   Pfam; PF00579; tRNA-synt_1b; 1.
DR   Pfam; PF01588; tRNA_bind; 1.
DR   PRINTS; PR01040; TRNASYNTHTYR.
DR   TIGRFAMs; TIGR00234; tyrS; 1.
DR   PROSITE; PS00178; AA_TRNA_LIGASE_I; FALSE_NEG.
DR   PROSITE; PS50886; TRBD; 1.
PE   2: Evidence at transcript level;
KW   Acetylation; Aminoacyl-tRNA synthetase; ATP-binding; Cytoplasm;
KW   Ligase; Nucleotide-binding; Protein biosynthesis; RNA-binding;
KW   tRNA-binding.
FT   INIT_MET      1      1       Removed (By similarity).
FT   CHAIN         2    528       Tyrosyl-tRNA synthetase, cytoplasmic.
FT                                /FTId=PRO_0000055672.
FT   DOMAIN      364    468       tRNA-binding.
FT   MOTIF        44     52       "HIGH" region.
FT   MOTIF       222    226       "KMSKS" region.
FT   BINDING      39     39       Tyrosine (By similarity).
FT   BINDING     166    166       Tyrosine (By similarity).
FT   BINDING     170    170       Tyrosine (By similarity).
FT   BINDING     173    173       Tyrosine (By similarity).
FT   BINDING     188    188       Tyrosine (By similarity).
FT   MOD_RES       2      2       N-acetylglycine (By similarity).
FT   CONFLICT     21     21       V -> A (in Ref. 2; CAA65245).
FT   CONFLICT    202    202       L -> P (in Ref. 2; CAA65245).
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
//