ID   SYWM_BOVIN              Reviewed;         360 AA.
AC   Q3T099;
DT   31-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT   11-OCT-2005, sequence version 1.
DT   03-AUG-2022, entry version 102.
DE   RecName: Full=Tryptophan--tRNA ligase, mitochondrial;
DE            EC=6.1.1.2;
DE   AltName: Full=(Mt)TrpRS;
DE   AltName: Full=Tryptophanyl-tRNA synthetase;
DE            Short=TrpRS;
DE   Flags: Precursor;
GN   Name=WARS2;
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 [LARGE SCALE MRNA].
RC   STRAIN=Crossbred X Angus; TISSUE=Ileum;
RG   NIH - Mammalian Gene Collection (MGC) project;
RL   Submitted (AUG-2005) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Mitochondrial aminoacyl-tRNA synthetase that activate and
CC       transfer the amino acids to their corresponding tRNAs during the
CC       translation of mitochondrial genes and protein synthesis.
CC       {ECO:0000250|UniProtKB:Q9UGM6}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + L-tryptophan + tRNA(Trp) = AMP + diphosphate + H(+) + L-
CC         tryptophanyl-tRNA(Trp); Xref=Rhea:RHEA:24080, Rhea:RHEA-COMP:9671,
CC         Rhea:RHEA-COMP:9705, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616,
CC         ChEBI:CHEBI:33019, ChEBI:CHEBI:57912, ChEBI:CHEBI:78442,
CC         ChEBI:CHEBI:78535, ChEBI:CHEBI:456215; EC=6.1.1.2;
CC   -!- SUBCELLULAR LOCATION: Mitochondrion matrix
CC       {ECO:0000250|UniProtKB:Q9UGM6}.
CC   -!- SIMILARITY: Belongs to the class-I aminoacyl-tRNA synthetase family.
CC       {ECO:0000305}.
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DR   EMBL; BC102487; AAI02488.1; -; mRNA.
DR   RefSeq; NP_001029754.1; NM_001034582.2.
DR   AlphaFoldDB; Q3T099; -.
DR   SMR; Q3T099; -.
DR   STRING; 9913.ENSBTAP00000006675; -.
DR   PaxDb; Q3T099; -.
DR   PRIDE; Q3T099; -.
DR   Ensembl; ENSBTAT00000081338; ENSBTAP00000072936; ENSBTAG00000005064.
DR   GeneID; 532903; -.
DR   KEGG; bta:532903; -.
DR   CTD; 10352; -.
DR   VEuPathDB; HostDB:ENSBTAG00000005064; -.
DR   VGNC; VGNC:36864; WARS2.
DR   eggNOG; KOG2713; Eukaryota.
DR   GeneTree; ENSGT00940000153724; -.
DR   HOGENOM; CLU_029244_1_5_1; -.
DR   InParanoid; Q3T099; -.
DR   OMA; GWGQFKP; -.
DR   OrthoDB; 1298726at2759; -.
DR   TreeFam; TF314321; -.
DR   Proteomes; UP000009136; Chromosome 3.
DR   Bgee; ENSBTAG00000005064; Expressed in oocyte and 106 other tissues.
DR   ExpressionAtlas; Q3T099; baseline and differential.
DR   GO; GO:0005759; C:mitochondrial matrix; ISS:UniProtKB.
DR   GO; GO:0005739; C:mitochondrion; IBA:GO_Central.
DR   GO; GO:0005654; C:nucleoplasm; IEA:Ensembl.
DR   GO; GO:0005886; C:plasma membrane; IEA:Ensembl.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0004830; F:tryptophan-tRNA ligase activity; IBA:GO_Central.
DR   GO; GO:0070183; P:mitochondrial tryptophanyl-tRNA aminoacylation; IBA:GO_Central.
DR   GO; GO:0006436; P:tryptophanyl-tRNA aminoacylation; IBA:GO_Central.
DR   GO; GO:0001570; P:vasculogenesis; IEA:Ensembl.
DR   CDD; cd00806; TrpRS_core; 1.
DR   Gene3D; 3.40.50.620; -; 1.
DR   HAMAP; MF_00140_B; Trp_tRNA_synth_B; 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; IPR002306; Trp-tRNA-ligase.
DR   InterPro; IPR024109; Trp-tRNA-ligase_bac-type.
DR   Pfam; PF00579; tRNA-synt_1b; 1.
DR   PRINTS; PR01039; TRNASYNTHTRP.
DR   TIGRFAMs; TIGR00233; trpS; 1.
DR   PROSITE; PS00178; AA_TRNA_LIGASE_I; 1.
PE   2: Evidence at transcript level;
KW   Aminoacyl-tRNA synthetase; ATP-binding; Ligase; Mitochondrion;
KW   Nucleotide-binding; Protein biosynthesis; Reference proteome;
KW   Transit peptide.
FT   TRANSIT         1..18
FT                   /note="Mitochondrion"
FT                   /evidence="ECO:0000250"
FT   CHAIN           19..360
FT                   /note="Tryptophan--tRNA ligase, mitochondrial"
FT                   /id="PRO_0000254589"
FT   BINDING         42
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250|UniProtKB:Q9UGM6"
FT   BINDING         48..51
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250|UniProtKB:Q9UGM6"
FT   BINDING         167
FT                   /ligand="L-tryptophan"
FT                   /ligand_id="ChEBI:CHEBI:57912"
FT                   /evidence="ECO:0000250|UniProtKB:Q9UGM6"
FT   BINDING         179..181
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250|UniProtKB:Q9UGM6"
FT   BINDING         217
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250|UniProtKB:Q9UGM6"
FT   BINDING         226..230
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250|UniProtKB:Q9UGM6"
SQ   SEQUENCE   360 AA;  40205 MW;  B7B3116B6619C952 CRC64;
     MALRSMRKAR ECWNFIRALH QGPDAAPVPQ KDAVKRIFSG IQPTGIPHLG NYLGAIESWV
     RLQDEHDSVL YSIVDLHSIT VPQDPTILRQ SILDMTAALL ACGINPEKSI LFQQSQVSEH
     TQLSWILTCM VRLPRLQHLH QWKAKTAKEK HNGTVGLLTY PVLQAADILL YKSTHVPVGE
     DQVQHMELVQ DLAQSFNKKY GEFFPVPKSI LTSMKKVKSL RDPSAKMSKS DPDKLATVRI
     TDSPEEIVQK FRKAMTDFTS EVTYEPASRG GVSNLVAIHA AVAGLPVEEV VRRSAGMDTA
     RYKLVVADAV IEKFAPIKSE IEKLKMNKDH LEKVLQVGSA RAKELAYPVC QEVKKLVGFL