ID SYEM_XENTR Reviewed; 516 AA.
AC Q66JG3;
DT 31-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT 11-OCT-2004, sequence version 1.
DT 27-MAR-2024, entry version 104.
DE RecName: Full=Nondiscriminating glutamyl-tRNA synthetase EARS2, mitochondrial {ECO:0000250|UniProtKB:Q5JPH6};
DE EC=6.1.1.24 {ECO:0000250|UniProtKB:Q5JPH6};
DE AltName: Full=Glutamate--tRNA(Gln) ligase EARS2, mitochondrial;
DE EC=6.1.1.17 {ECO:0000250|UniProtKB:Q5JPH6};
DE AltName: Full=Glutamyl-tRNA synthetase;
DE Short=GluRS;
DE AltName: Full=Mitochondrial glutamyl-tRNA synthetase;
DE Short=mtGluRS;
DE Flags: Precursor;
GN Name=ears2 {ECO:0000250|UniProtKB:Q5JPH6};
OS Xenopus tropicalis (Western clawed frog) (Silurana tropicalis).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Silurana.
OX NCBI_TaxID=8364;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Embryo;
RG NIH - Xenopus Gene Collection (XGC) project;
RL Submitted (AUG-2004) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Non-discriminating glutamyl-tRNA synthetase that catalyzes
CC aminoacylation of both mitochondrial tRNA(Glu) and tRNA(Gln) and
CC participates in RNA aminoacylation for mitochondrial protein
CC translation. Attachs glutamate to tRNA(Glu) or tRNA(Gln) in a two-step
CC reaction: glutamate is first activated by ATP to form Glu-AMP and then
CC transferred to the acceptor end of tRNA(Glu) or tRNA(Gln).
CC {ECO:0000250|UniProtKB:Q5JPH6}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + L-glutamate + tRNA(Glx) = AMP + diphosphate + L-
CC glutamyl-tRNA(Glx); Xref=Rhea:RHEA:18397, Rhea:RHEA-COMP:9713,
CC Rhea:RHEA-COMP:9716, ChEBI:CHEBI:29985, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:33019, ChEBI:CHEBI:78442, ChEBI:CHEBI:78520,
CC ChEBI:CHEBI:456215; EC=6.1.1.24;
CC Evidence={ECO:0000250|UniProtKB:Q5JPH6};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:18398;
CC Evidence={ECO:0000250|UniProtKB:Q5JPH6};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + L-glutamate + tRNA(Glu) = AMP + diphosphate + L-
CC glutamyl-tRNA(Glu); Xref=Rhea:RHEA:23540, Rhea:RHEA-COMP:9663,
CC Rhea:RHEA-COMP:9680, ChEBI:CHEBI:29985, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:33019, ChEBI:CHEBI:78442, ChEBI:CHEBI:78520,
CC ChEBI:CHEBI:456215; EC=6.1.1.17;
CC Evidence={ECO:0000250|UniProtKB:Q5JPH6};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:23541;
CC Evidence={ECO:0000250|UniProtKB:Q5JPH6};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + L-glutamate + tRNA(Gln) = AMP + diphosphate + L-
CC glutamyl-tRNA(Gln); Xref=Rhea:RHEA:64612, Rhea:RHEA-COMP:9662,
CC Rhea:RHEA-COMP:9684, ChEBI:CHEBI:29985, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:33019, ChEBI:CHEBI:78442, ChEBI:CHEBI:78520,
CC ChEBI:CHEBI:456215; Evidence={ECO:0000250|UniProtKB:Q5JPH6};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:64613;
CC Evidence={ECO:0000250|UniProtKB:Q5JPH6};
CC -!- SUBCELLULAR LOCATION: Mitochondrion matrix
CC {ECO:0000250|UniProtKB:Q5JPH6}.
CC -!- SIMILARITY: Belongs to the class-I aminoacyl-tRNA synthetase family.
CC Glutamate--tRNA ligase type 1 subfamily. {ECO:0000305}.
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DR EMBL; BC080925; AAH80925.1; -; mRNA.
DR RefSeq; NP_001008042.1; NM_001008041.1.
DR AlphaFoldDB; Q66JG3; -.
DR SMR; Q66JG3; -.
DR STRING; 8364.ENSXETP00000040409; -.
DR PaxDb; 8364-ENSXETP00000027183; -.
DR DNASU; 493404; -.
DR Ensembl; ENSXETT00000027183; ENSXETP00000027183; ENSXETG00000012433.
DR Ensembl; ENSXETT00000087519; ENSXETP00000086446; ENSXETG00000012433.
DR GeneID; 493404; -.
DR KEGG; xtr:493404; -.
DR AGR; Xenbase:XB-GENE-970848; -.
DR CTD; 124454; -.
DR Xenbase; XB-GENE-970848; ears2.
DR eggNOG; KOG1149; Eukaryota.
DR InParanoid; Q66JG3; -.
DR OMA; EAFKWVG; -.
DR OrthoDB; 5404395at2759; -.
DR Proteomes; UP000008143; Chromosome 9.
DR Bgee; ENSXETG00000012433; Expressed in skeletal muscle tissue and 12 other cell types or tissues.
DR GO; GO:0005759; C:mitochondrial matrix; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0004818; F:glutamate-tRNA ligase activity; IEA:UniProtKB-EC.
DR GO; GO:0050561; F:glutamate-tRNA(Gln) ligase activity; IEA:RHEA.
DR GO; GO:0000049; F:tRNA binding; IEA:InterPro.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0006424; P:glutamyl-tRNA aminoacylation; IEA:InterPro.
DR CDD; cd00808; GluRS_core; 1.
DR Gene3D; 1.10.10.350; -; 1.
DR Gene3D; 3.40.50.620; HUPs; 1.
DR HAMAP; MF_00022; Glu_tRNA_synth_type1; 1.
DR InterPro; IPR045462; aa-tRNA-synth_I_cd-bd.
DR InterPro; IPR020751; aa-tRNA-synth_I_codon-bd_sub2.
DR InterPro; IPR001412; aa-tRNA-synth_I_CS.
DR InterPro; IPR008925; aa_tRNA-synth_I_cd-bd_sf.
DR InterPro; IPR004527; Glu-tRNA-ligase_bac/mito.
DR InterPro; IPR000924; Glu/Gln-tRNA-synth.
DR InterPro; IPR020058; Glu/Gln-tRNA-synth_Ib_cat-dom.
DR InterPro; IPR033910; GluRS_core.
DR InterPro; IPR014729; Rossmann-like_a/b/a_fold.
DR NCBIfam; TIGR00464; gltX_bact; 1.
DR PANTHER; PTHR43311; GLUTAMATE--TRNA LIGASE; 1.
DR PANTHER; PTHR43311:SF2; GLUTAMATE--TRNA LIGASE, MITOCHONDRIAL-RELATED; 1.
DR Pfam; PF19269; Anticodon_2; 1.
DR Pfam; PF00749; tRNA-synt_1c; 1.
DR PRINTS; PR00987; TRNASYNTHGLU.
DR SUPFAM; SSF48163; An anticodon-binding domain of class I aminoacyl-tRNA synthetases; 1.
DR SUPFAM; SSF52374; Nucleotidylyl transferase; 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; RNA-binding;
KW Transit peptide.
FT TRANSIT 1..39
FT /note="Mitochondrion"
FT /evidence="ECO:0000255"
FT CHAIN 40..516
FT /note="Nondiscriminating glutamyl-tRNA synthetase EARS2,
FT mitochondrial"
FT /id="PRO_0000254565"
FT MOTIF 43..51
FT /note="'HIGH' region"
FT MOTIF 282..286
FT /note="'KMSKS' region"
FT BINDING 38..40
FT /ligand="L-glutamate"
FT /ligand_id="ChEBI:CHEBI:29985"
FT /evidence="ECO:0000250"
FT BINDING 48
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT BINDING 74
FT /ligand="L-glutamate"
FT /ligand_id="ChEBI:CHEBI:29985"
FT /evidence="ECO:0000250"
FT BINDING 226..230
FT /ligand="L-glutamate"
FT /ligand_id="ChEBI:CHEBI:29985"
FT /evidence="ECO:0000250"
FT BINDING 244
FT /ligand="L-glutamate"
FT /ligand_id="ChEBI:CHEBI:29985"
FT /evidence="ECO:0000250"
FT BINDING 247
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT BINDING 282..286
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
SQ SEQUENCE 516 AA; 58607 MW; EB54FFDEBE953600 CRC64;
MRPAFIRGKW LSRTLELATG LGRRTCSSRE SGREVRVRFA PSPTGFLHLG GLRTALYNYL
FAKKHGGAFI LRLEDTDRSR LVPGAAESIE DMLEWAGIPP DESPRHGGPC GPYEQSKRLD
LYHVAAQALL DSGAAYRCFC TPQRLELLKR EAMRNRQTPR YDNRCRHLTP KQVEEKLSRN
SPFVIRFFLQ EGAQPFQDLV YGWTQHDVAS VEGDPVILKG DGFPTYHLAN VVDDHHMCVS
HVLRGAEWLI STAKHLLLYQ ALGWQPPQFA HLPLLLNKDG SKLSKRQGDI FIQHYVHSGY
LSDALLDLIT NCGSGFTENQ MGRTVDTLIQ QYELGKTSTH SALLDLDKLP EFNRIHLTRW
IEGTETRVQL VGQLQVLLKD TYKDLELDEK HIERILLLRK GHLCRLTDLL SPEYSYLWVR
PSVTREQLQC LTSEASKVKN LVVRLLQEND SGFTLETLNG ELRKQLKQVK DTKYSSAMKL
LRVALSGQEH GPSVAEMLLS LGRQESIVRL QNALPD
//
