ID   SYEM_CHICK              Reviewed;         502 AA.
AC   Q5ZJ66;
DT   31-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT   23-NOV-2004, sequence version 1.
DT   27-MAR-2024, entry version 101.
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=RCJMB04_20f12;
OS   Gallus gallus (Chicken).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC   Coelurosauria; Aves; Neognathae; Galloanserae; Galliformes; Phasianidae;
OC   Phasianinae; Gallus.
OX   NCBI_TaxID=9031;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=CB; TISSUE=Bursa of Fabricius;
RX   PubMed=15642098; DOI=10.1186/gb-2004-6-1-r6;
RA   Caldwell R.B., Kierzek A.M., Arakawa H., Bezzubov Y., Zaim J., Fiedler P.,
RA   Kutter S., Blagodatski A., Kostovska D., Koter M., Plachy J., Carninci P.,
RA   Hayashizaki Y., Buerstedde J.-M.;
RT   "Full-length cDNAs from chicken bursal lymphocytes to facilitate gene
RT   function analysis.";
RL   Genome Biol. 6:R6.1-R6.9(2005).
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; AJ720568; CAG32227.1; -; mRNA.
DR   RefSeq; NP_001026638.1; NM_001031467.1.
DR   AlphaFoldDB; Q5ZJ66; -.
DR   SMR; Q5ZJ66; -.
DR   STRING; 9031.ENSGALP00000009866; -.
DR   PaxDb; 9031-ENSGALP00000009866; -.
DR   GeneID; 427672; -.
DR   KEGG; gga:427672; -.
DR   CTD; 124454; -.
DR   VEuPathDB; HostDB:geneid_427672; -.
DR   eggNOG; KOG1149; Eukaryota.
DR   InParanoid; Q5ZJ66; -.
DR   OMA; ETQMANG; -.
DR   OrthoDB; 5404395at2759; -.
DR   PhylomeDB; Q5ZJ66; -.
DR   PRO; PR:Q5ZJ66; -.
DR   Proteomes; UP000000539; Unassembled WGS sequence.
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..20
FT                   /note="Mitochondrion"
FT                   /evidence="ECO:0000255"
FT   CHAIN           21..502
FT                   /note="Nondiscriminating glutamyl-tRNA synthetase EARS2,
FT                   mitochondrial"
FT                   /id="PRO_0000254563"
FT   MOTIF           24..32
FT                   /note="'HIGH' region"
FT   MOTIF           263..267
FT                   /note="'KMSKS' region"
FT   BINDING         19..21
FT                   /ligand="L-glutamate"
FT                   /ligand_id="ChEBI:CHEBI:29985"
FT                   /evidence="ECO:0000250"
FT   BINDING         29
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250"
FT   BINDING         55
FT                   /ligand="L-glutamate"
FT                   /ligand_id="ChEBI:CHEBI:29985"
FT                   /evidence="ECO:0000250"
FT   BINDING         207..211
FT                   /ligand="L-glutamate"
FT                   /ligand_id="ChEBI:CHEBI:29985"
FT                   /evidence="ECO:0000250"
FT   BINDING         225
FT                   /ligand="L-glutamate"
FT                   /ligand_id="ChEBI:CHEBI:29985"
FT                   /evidence="ECO:0000250"
FT   BINDING         228
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250"
FT   BINDING         263..267
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   502 AA;  56954 MW;  1E84C3BB0E744570 CRC64;
     MAGMLREVCG AAASGLRVRF GPSPTGFLHL GGLRTALYNY VFAKQQRGTF VLRVEDTDQG
     RVVAGAAESI EDMLHWAGIP PDESPRRGGP FGPYQQSLRL DLYRAASEAL LDRGAAYRCF
     CTPQRLELLR KEALRNQQTP RYDNRCRHLT PKEVAEKLAQ GLDWVVRFRL ERGVEPFQDL
     VYGWNKHEVA EVEGDPVILK ADGFPTYHLA NVVDDHHMGI SHVLRGTEWL TSTSKHLLLY
     KAFGWDPPQF GHLPLLLNKD GSKLSKRQGD IFLERFAQEG YLPEALLDMI TNCGSGFAEK
     QMGRTLEELI SQFEIGRITT HSALLDLEKL PEFNRMHLTR HIENEGLRQK LIQELQLLVE
     DVYGDQEVDK EVLEKEYVEQ VLLLRKGHIS HLKDLVSDNY SYLWVRPSVS REQLQMISAE
     VDEIGKLVLG LMTKPAAVWT IEELNKDLRS LQKQTRETKY SSMMKLLRLA LSGQQHGPSV
     AEMMVTLGPR EVCGRISKVL SS
//