ID   SYEM_DANRE              Reviewed;         503 AA.
AC   Q0P499;
DT   31-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT   19-SEP-2006, sequence version 1.
DT   27-MAR-2024, entry version 87.
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}; ORFNames=zgc:153247;
OS   Danio rerio (Zebrafish) (Brachydanio rerio).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Cypriniformes;
OC   Danionidae; Danioninae; Danio.
OX   NCBI_TaxID=7955;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Testis;
RG   NIH - Zebrafish Gene Collection (ZGC) project;
RL   Submitted (AUG-2006) 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; BC122204; AAI22205.1; -; mRNA.
DR   RefSeq; NP_001038907.1; NM_001045442.1.
DR   AlphaFoldDB; Q0P499; -.
DR   SMR; Q0P499; -.
DR   STRING; 7955.ENSDARP00000132607; -.
DR   GeneID; 751732; -.
DR   KEGG; dre:751732; -.
DR   AGR; ZFIN:ZDB-GENE-060825-214; -.
DR   CTD; 124454; -.
DR   ZFIN; ZDB-GENE-060825-214; ears2.
DR   InParanoid; Q0P499; -.
DR   OrthoDB; 5404395at2759; -.
DR   PhylomeDB; Q0P499; -.
DR   PRO; PR:Q0P499; -.
DR   Proteomes; UP000000437; Chromosome 1.
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: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; IBA:GO_Central.
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..22
FT                   /note="Mitochondrion"
FT                   /evidence="ECO:0000255"
FT   CHAIN           23..503
FT                   /note="Nondiscriminating glutamyl-tRNA synthetase EARS2,
FT                   mitochondrial"
FT                   /id="PRO_0000254564"
FT   MOTIF           26..34
FT                   /note="'HIGH' region"
FT   MOTIF           265..269
FT                   /note="'KMSKS' region"
FT   BINDING         21..23
FT                   /ligand="L-glutamate"
FT                   /ligand_id="ChEBI:CHEBI:29985"
FT                   /evidence="ECO:0000250"
FT   BINDING         31
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250"
FT   BINDING         57
FT                   /ligand="L-glutamate"
FT                   /ligand_id="ChEBI:CHEBI:29985"
FT                   /evidence="ECO:0000250"
FT   BINDING         209..213
FT                   /ligand="L-glutamate"
FT                   /ligand_id="ChEBI:CHEBI:29985"
FT                   /evidence="ECO:0000250"
FT   BINDING         227
FT                   /ligand="L-glutamate"
FT                   /ligand_id="ChEBI:CHEBI:29985"
FT                   /evidence="ECO:0000250"
FT   BINDING         230
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250"
FT   BINDING         265..269
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   503 AA;  57023 MW;  B5E856B44B303AD7 CRC64;
     MKILRGVSRQ MCTSRPEVRV RFAPSPTGFL HLGGLRTALY NFLFSRQRRG VFILRLEDTD
     QKRLVPGAAE HIEDMLEWAG IPPDESSRRG GDYGPYVQSE RLHLYTEAAS SLLNTGHAYY
     CFCSNQRLEL LKKEAQRSGH APRYDNRCRR LQPQQVEQKL AAGVPAVVRF KLHTGTEEFQ
     DLVFGWTGHA VGAVEGDPVI LKADGYPTYH LASVVDDHHM RISHVLRGCE WLISSAKHLQ
     LYRALRWTPP TYAHLPLLLN RDGSKLSKRQ GDIFLQSFRD RGVLPETLLD LVTHAGSGFS
     DNRMGRRLDE LIRDFNISKI TTHSALLDLD KLEEFSRLHL QRRIEDPQQC VWLCEELKQM
     VKHTHSSEIS AAAVLEPEYI ERVLQLRKGH ISSLQDLLSS THSYLWVRPR VSQTQLQSES
     AHAKDIATAV MQMVLAGGSL VSMERLSSEL KQISSRTNST HSSVMKVLRL LLSAQQRGPS
     VAEMMLSLGE QEVCVRLQKA LEL
//