SYYM_RAT
ID SYYM_RAT Reviewed; 471 AA.
AC Q5I0L3;
DT 03-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT 15-FEB-2005, sequence version 1.
DT 03-AUG-2022, entry version 114.
DE RecName: Full=Tyrosine--tRNA ligase, mitochondrial;
DE EC=6.1.1.1 {ECO:0000250|UniProtKB:Q9Y2Z4};
DE AltName: Full=Tyrosyl-tRNA synthetase;
DE Short=TyrRS;
DE Flags: Precursor;
GN Name=Yars2;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Liver;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
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).
CC {ECO:0000250|UniProtKB:Q9Y2Z4}.
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 Evidence={ECO:0000250|UniProtKB:Q9Y2Z4};
CC -!- SUBUNIT: Homodimer. {ECO:0000250|UniProtKB:Q9Y2Z4}.
CC -!- SUBCELLULAR LOCATION: Mitochondrion matrix
CC {ECO:0000250|UniProtKB:Q9Y2Z4}.
CC -!- SIMILARITY: Belongs to the class-I aminoacyl-tRNA synthetase family.
CC {ECO:0000305}.
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DR EMBL; BC088224; AAH88224.1; -; mRNA.
DR RefSeq; NP_001009627.1; NM_001009627.1.
DR AlphaFoldDB; Q5I0L3; -.
DR SMR; Q5I0L3; -.
DR STRING; 10116.ENSRNOP00000037398; -.
DR iPTMnet; Q5I0L3; -.
DR PhosphoSitePlus; Q5I0L3; -.
DR jPOST; Q5I0L3; -.
DR PaxDb; Q5I0L3; -.
DR PRIDE; Q5I0L3; -.
DR GeneID; 287924; -.
DR KEGG; rno:287924; -.
DR CTD; 51067; -.
DR RGD; 1311696; Yars2.
DR VEuPathDB; HostDB:ENSRNOG00000025252; -.
DR eggNOG; KOG2623; Eukaryota.
DR HOGENOM; CLU_024003_1_0_1; -.
DR InParanoid; Q5I0L3; -.
DR OMA; YMMAKDS; -.
DR OrthoDB; 914272at2759; -.
DR PhylomeDB; Q5I0L3; -.
DR TreeFam; TF105974; -.
DR PRO; PR:Q5I0L3; -.
DR Proteomes; UP000002494; Chromosome 11.
DR Bgee; ENSRNOG00000025252; Expressed in pancreas and 19 other tissues.
DR Genevisible; Q5I0L3; RN.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0005759; C:mitochondrial matrix; IEA:UniProtKB-SubCell.
DR GO; GO:0005739; C:mitochondrion; IBA:GO_Central.
DR GO; GO:0016604; C:nuclear body; IEA:Ensembl.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0042803; F:protein homodimerization activity; ISO:RGD.
DR GO; GO:0000049; F:tRNA binding; ISO:RGD.
DR GO; GO:0072545; F:tyrosine binding; ISO:RGD.
DR GO; GO:0004831; F:tyrosine-tRNA ligase activity; ISO:RGD.
DR GO; GO:0070184; P:mitochondrial tyrosyl-tRNA aminoacylation; ISO:RGD.
DR GO; GO:0043039; P:tRNA aminoacylation; ISO:RGD.
DR CDD; cd00805; TyrRS_core; 1.
DR Gene3D; 3.10.290.10; -; 1.
DR Gene3D; 3.40.50.620; -; 1.
DR InterPro; IPR001412; aa-tRNA-synth_I_CS.
DR InterPro; IPR002305; aa-tRNA-synth_Ic.
DR InterPro; IPR014729; Rossmann-like_a/b/a_fold.
DR InterPro; IPR036986; S4_RNA-bd_sf.
DR InterPro; IPR002307; Tyr-tRNA-ligase.
DR InterPro; IPR024088; Tyr-tRNA-ligase_bac-type.
DR PANTHER; PTHR11766; PTHR11766; 1.
DR Pfam; PF00579; tRNA-synt_1b; 1.
DR PRINTS; PR01040; TRNASYNTHTYR.
DR TIGRFAMs; TIGR00234; tyrS; 1.
DR PROSITE; PS00178; AA_TRNA_LIGASE_I; 1.
PE 2: Evidence at transcript level;
KW Acetylation; Aminoacyl-tRNA synthetase; ATP-binding; Ligase; Mitochondrion;
KW Nucleotide-binding; Protein biosynthesis; Reference proteome;
KW Transit peptide.
FT TRANSIT 1..?
FT /note="Mitochondrion"
FT /evidence="ECO:0000255"
FT CHAIN ?..471
FT /note="Tyrosine--tRNA ligase, mitochondrial"
FT /id="PRO_0000250721"
FT MOTIF 76..85
FT /note="'HIGH' region"
FT MOTIF 275..279
FT /note="'KMSKS' region"
FT BINDING 71
FT /ligand="L-tyrosine"
FT /ligand_id="ChEBI:CHEBI:58315"
FT /evidence="ECO:0000250|UniProtKB:Q9Y2Z4"
FT BINDING 75
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:Q9Y2Z4"
FT BINDING 115
FT /ligand="L-tyrosine"
FT /ligand_id="ChEBI:CHEBI:58315"
FT /evidence="ECO:0000250|UniProtKB:Q9Y2Z4"
FT BINDING 215
FT /ligand="L-tyrosine"
FT /ligand_id="ChEBI:CHEBI:58315"
FT /evidence="ECO:0000250|UniProtKB:Q9Y2Z4"
FT BINDING 219
FT /ligand="L-tyrosine"
FT /ligand_id="ChEBI:CHEBI:58315"
FT /evidence="ECO:0000250|UniProtKB:Q9Y2Z4"
FT BINDING 222
FT /ligand="L-tyrosine"
FT /ligand_id="ChEBI:CHEBI:58315"
FT /evidence="ECO:0000250|UniProtKB:Q9Y2Z4"
FT BINDING 241
FT /ligand="L-tyrosine"
FT /ligand_id="ChEBI:CHEBI:58315"
FT /evidence="ECO:0000250|UniProtKB:Q9Y2Z4"
FT BINDING 268
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:Q9Y2Z4"
FT BINDING 278
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT MOD_RES 349
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q9Y2Z4"
FT MOD_RES 361
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q8BYL4"
SQ SEQUENCE 471 AA; 52628 MW; A9431FD9EA3FBE92 CRC64;
MAAPMLRHLC RVPQSGVWTR GPRAVRPGAR GMLVAPRARG LFKEFFPESG TKTELPELFD
RRRAGSPQTV YCGFDPTGDS LHVGHLLTLL GLFHFQRAGH NVIALVGGST ALLGDPSGRT
KEREALSAEC VRANARALQR GLETLAANHA RLFADGRPWG TFTVLDNAAW FQKQHLMDFL
ATVGGHFRMG TLLSRLSVQS RLKSPEGMSL AEFFYQVLQA YDFYYLFRHY GCRVQLGGSD
QLGNIMSGYE FIHKLTGEDV FGITVPLITS TTGAKLGKSA GNAVWLNREK TSPFELYQFF
IRQQDDSVER YLKLFTFLPL PEIDHIMQLH VKEPEKRIAQ KRLAAEVTKL VHGQEGLDSA
KRCTQALYHS SIEALEVMSD QELKELFKEA SFSELVLDPG TSVIDTCRKA NAIPDGPRGY
RMITEGGVSI NHRQVTNPES VLVIGQHILK NGLSLLKIGK RNFYIIKWLQ L
