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
//