ID   SYEM_MACFA              Reviewed;         506 AA.
AC   Q4R4F1;
DT   31-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT   19-JUL-2005, sequence version 1.
DT   03-AUG-2022, entry version 74.
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=QtsA-10185;
OS   Macaca fascicularis (Crab-eating macaque) (Cynomolgus monkey).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini;
OC   Cercopithecidae; Cercopithecinae; Macaca.
OX   NCBI_TaxID=9541;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Testis;
RG   International consortium for macaque cDNA sequencing and analysis;
RT   "DNA sequences of macaque genes expressed in brain or testis and its
RT   evolutionary implications.";
RL   Submitted (JUN-2005) 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; AB178963; BAE02014.1; -; mRNA.
DR   RefSeq; NP_001270434.1; NM_001283505.1.
DR   AlphaFoldDB; Q4R4F1; -.
DR   SMR; Q4R4F1; -.
DR   STRING; 9541.XP_005591523.1; -.
DR   GeneID; 101926460; -.
DR   CTD; 124454; -.
DR   eggNOG; KOG1149; Eukaryota.
DR   Proteomes; UP000233100; Unplaced.
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: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; 3.40.50.620; -; 1.
DR   HAMAP; MF_00022; Glu_tRNA_synth_type1; 1.
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; 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   Acetylation; Aminoacyl-tRNA synthetase; ATP-binding; Ligase; Mitochondrion;
KW   Nucleotide-binding; Protein biosynthesis; Reference proteome; RNA-binding;
KW   Transit peptide.
FT   TRANSIT         1..41
FT                   /note="Mitochondrion"
FT                   /evidence="ECO:0000255"
FT   CHAIN           42..506
FT                   /note="Probable glutamate--tRNA ligase, mitochondrial"
FT                   /id="PRO_0000254561"
FT   MOTIF           45..53
FT                   /note="'HIGH' region"
FT   MOTIF           284..288
FT                   /note="'KMSKS' region"
FT   BINDING         40..42
FT                   /ligand="L-glutamate"
FT                   /ligand_id="ChEBI:CHEBI:29985"
FT                   /evidence="ECO:0000250"
FT   BINDING         50
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250"
FT   BINDING         76
FT                   /ligand="L-glutamate"
FT                   /ligand_id="ChEBI:CHEBI:29985"
FT                   /evidence="ECO:0000250"
FT   BINDING         228..232
FT                   /ligand="L-glutamate"
FT                   /ligand_id="ChEBI:CHEBI:29985"
FT                   /evidence="ECO:0000250"
FT   BINDING         246
FT                   /ligand="L-glutamate"
FT                   /ligand_id="ChEBI:CHEBI:29985"
FT                   /evidence="ECO:0000250"
FT   BINDING         249
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250"
FT   BINDING         284..288
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250"
FT   MOD_RES         256
FT                   /note="N6-succinyllysine"
FT                   /evidence="ECO:0000250|UniProtKB:Q9CXJ1"
FT   MOD_RES         486
FT                   /note="N6-acetyllysine"
FT                   /evidence="ECO:0000250|UniProtKB:Q5JPH6"
SQ   SEQUENCE   506 AA;  56865 MW;  314400085FF645F6 CRC64;
     MAALLRRLLQ RGRPLAASGR RVGRREARLG TGPGVAVRVR FAPSPTGFLH LGGLRTALYN
     YIFAKKYQGS FILRLEDTDQ TRFVPGAAEN IENMLEWAGI PPDESPRRGG PAGPYQQSQR
     LELYAQATEA LLKTGAAYPC FCSPQRLELL KKEALRNHQM PRYDNRCRNM SQEQVAQKLA
     KDPKPAIRFR LEQAAPAFED LVYGWNRHDV ASVEGDPVIM KSDGFPTYHL ACVVDDHHMG
     ISHVLRGSEW LISTAKHLLL YQALGWHPPH FAHLPLLLNR DGSKLSKRQG DIFLEHFAAE
     GFLPDSLLDI ITNCGSGFAE NQMGRTLPEL ITQFNLTRVT CHSALLDLEK LPEFNRLHLQ
     RLVNNESQRC QLVEKLQALV EEAFGSQLQN RDVLNPIYME RILLLRQGHI CRLQDLVSPV
     YSYLWTRPSV GRAQLDAISE EVDVIAKRVL GLLERSGMSL TQDMLSGELK KLSEGLEGTK
     HSNVMKLLRV ALSGQQALSS MFKVQG