SYWM_CAEEL
ID SYWM_CAEEL Reviewed; 360 AA.
AC C0HKD6; P46579; Q5TYM1; Q7Z259;
DT 25-OCT-2017, integrated into UniProtKB/Swiss-Prot.
DT 25-OCT-2017, sequence version 1.
DT 03-AUG-2022, entry version 24.
DE RecName: Full=Tryptophan--tRNA ligase, mitochondrial;
DE EC=6.1.1.2 {ECO:0000250|UniProtKB:P00953};
DE AltName: Full=Tryptophanyl-tRNA synthetase;
DE Short=TrpRS;
DE Flags: Precursor;
GN Name=wars-2 {ECO:0000312|WormBase:C34E10.4b};
GN Synonyms=wrs-2 {ECO:0000312|WormBase:C34E10.4b};
GN ORFNames=C34E10.4 {ECO:0000312|WormBase:C34E10.4b};
OS Caenorhabditis elegans.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC Caenorhabditis.
OX NCBI_TaxID=6239;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Bristol N2;
RX PubMed=9851916; DOI=10.1126/science.282.5396.2012;
RG The C. elegans sequencing consortium;
RT "Genome sequence of the nematode C. elegans: a platform for investigating
RT biology.";
RL Science 282:2012-2018(1998).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RA Ohtsuki T.;
RT "C. elegans mitochondrial aminoacyl-tRNA synthetases.";
RL Submitted (NOV-2002) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Catalyzes the attachment of tryptophan to tRNA(Trp).
CC {ECO:0000250|UniProtKB:P00953}.
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 Evidence={ECO:0000250|UniProtKB:P00953};
CC -!- SUBCELLULAR LOCATION: Mitochondrion matrix
CC {ECO:0000250|UniProtKB:Q9UGM6}.
CC -!- MISCELLANEOUS: Complex locus in which transcription results in the
CC production of one large primary transcript that gives rise to two
CC functionally distinct proteins, wars-2 and prx-10.
CC -!- SIMILARITY: Belongs to the class-I aminoacyl-tRNA synthetase family.
CC {ECO:0000305}.
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DR EMBL; BX284603; CCD66648.1; -; Genomic_DNA.
DR EMBL; AB096634; BAC76734.1; -; mRNA.
DR PIR; T15761; T15761.
DR RefSeq; NP_001021201.1; NM_001026030.3.
DR AlphaFoldDB; C0HKD6; -.
DR SMR; C0HKD6; -.
DR STRING; 6239.C34E10.4b; -.
DR EnsemblMetazoa; C34E10.4b.1; C34E10.4b.1; WBGene00006946.
DR EnsemblMetazoa; C34E10.4b.2; C34E10.4b.2; WBGene00006946.
DR EnsemblMetazoa; C34E10.4b.3; C34E10.4b.3; WBGene00006946.
DR EnsemblMetazoa; C34E10.4b.4; C34E10.4b.4; WBGene00006946.
DR EnsemblMetazoa; C34E10.4b.5; C34E10.4b.5; WBGene00006946.
DR EnsemblMetazoa; C34E10.4b.6; C34E10.4b.6; WBGene00006946.
DR GeneID; 175719; -.
DR CTD; 175719; -.
DR WormBase; C34E10.4b; CE37710; WBGene00006946; wars-2.
DR eggNOG; KOG2713; Eukaryota.
DR OMA; GWGQFKP; -.
DR OrthoDB; 1175089at2759; -.
DR Proteomes; UP000001940; Chromosome III.
DR Bgee; WBGene00006946; Expressed in germ line (C elegans) and 4 other tissues.
DR ExpressionAtlas; C0HKD6; baseline and differential.
DR GO; GO:0005759; C:mitochondrial matrix; IBA:GO_Central.
DR GO; GO:0005739; C:mitochondrion; IBA:GO_Central.
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 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; IPR002306; Trp-tRNA-ligase.
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..?
FT /note="Mitochondrion"
FT /evidence="ECO:0000255"
FT CHAIN ?..360
FT /note="Tryptophan--tRNA ligase, mitochondrial"
FT /id="PRO_0000441751"
FT REGION 220..241
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 39..47
FT /note="'HIGH' region"
FT /evidence="ECO:0000305"
FT MOTIF 229..233
FT /note="'KMSKS' region"
FT /evidence="ECO:0000305"
FT COMPBIAS 220..235
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 38
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:Q9UGM6"
FT BINDING 44..47
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:Q9UGM6"
FT BINDING 168
FT /ligand="L-tryptophan"
FT /ligand_id="ChEBI:CHEBI:57912"
FT /evidence="ECO:0000250|UniProtKB:Q9UGM6"
FT BINDING 180..182
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:Q9UGM6"
FT BINDING 229..233
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:Q9UGM6"
SQ SEQUENCE 360 AA; 40474 MW; E73230D906FA1E7A CRC64;
MIFSGKFTSH LLNYGFKPNN LRLLSTSTHP TIYFTGIQPT GIPHLGNFFG SIEPWTELQN
SVDKNILMML SVVDQHAISL GPLPANELRQ NTHQMTASLI ACGVDPNRTL LFRQSDVPQI
AQISWILGSL QTTSKLARLP QYKEKKERFK KGDIPVGLLT YPLLQAADVL TFKATTVPVG
EDQSQHLNLL GGLAYAFNKT YETEIFPIPK QLTRESHARI RSLREPEKKM SKSSGGPRSR
IEITDSRSTI IEKCQKAQSD NAGKVTYDKE NRLAVSNLLD LYSAVTKTQT SEIDFSNWTT
LDLKMNLAEA VDKRLAPIRQ KFEELQNTGE VDKVLTENGE KAREIAEKNL EEIRRTIGFL
