SYEM_XENTR
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 03-AUG-2022, entry version 97.
DE RecName: Full=Probable glutamate--tRNA ligase, mitochondrial;
DE EC=6.1.1.17;
DE AltName: Full=Glutamyl-tRNA synthetase;
DE Short=GluRS;
DE Flags: Precursor;
GN Name=ears2;
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: Catalyzes the attachment of glutamate to tRNA(Glu) in a two-
CC step reaction: glutamate is first activated by ATP to form Glu-AMP and
CC then transferred to the acceptor end of tRNA(Glu). {ECO:0000250}.
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 -!- SUBCELLULAR LOCATION: Mitochondrion matrix {ECO:0000250}.
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 PaxDb; Q66JG3; -.
DR DNASU; 493404; -.
DR GeneID; 493404; -.
DR KEGG; xtr:493404; -.
DR CTD; 124454; -.
DR Xenbase; XB-GENE-970848; ears2.
DR eggNOG; KOG1149; Eukaryota.
DR InParanoid; Q66JG3; -.
DR OrthoDB; 879920at2759; -.
DR Proteomes; UP000008143; Chromosome 9.
DR Proteomes; UP000790000; Unplaced.
DR Bgee; ENSXETG00000012433; Expressed in skeletal muscle tissue and 12 other tissues.
DR GO; GO:0005759; C:mitochondrial matrix; IEA:UniProtKB-SubCell.
DR GO; GO:0005739; C:mitochondrion; IBA:GO_Central.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0004818; F:glutamate-tRNA ligase activity; IBA:GO_Central.
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; IBA:GO_Central.
DR CDD; cd00808; GluRS_core; 1.
DR Gene3D; 1.10.10.350; -; 1.
DR Gene3D; 3.40.50.620; -; 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 Pfam; PF19269; Anticodon_2; 1.
DR Pfam; PF00749; tRNA-synt_1c; 1.
DR PRINTS; PR00987; TRNASYNTHGLU.
DR SUPFAM; SSF48163; SSF48163; 1.
DR TIGRFAMs; TIGR00464; gltX_bact; 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="Probable glutamate--tRNA ligase, 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
