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   03-AUG-2022, entry version 81.
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; 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: 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; BC122204; AAI22205.1; -; mRNA.
DR   RefSeq; NP_001038907.1; NM_001045442.1.
DR   AlphaFoldDB; Q0P499; -.
DR   SMR; Q0P499; -.
DR   GeneID; 751732; -.
DR   KEGG; dre:751732; -.
DR   CTD; 124454; -.
DR   ZFIN; ZDB-GENE-060825-214; ears2.
DR   InParanoid; Q0P499; -.
DR   OrthoDB; 879920at2759; -.
DR   PhylomeDB; Q0P499; -.
DR   PRO; PR:Q0P499; -.
DR   Proteomes; UP000000437; Genome assembly.
DR   Proteomes; UP000814640; Unplaced.
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..22
FT                   /note="Mitochondrion"
FT                   /evidence="ECO:0000255"
FT   CHAIN           23..503
FT                   /note="Probable glutamate--tRNA ligase, 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