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
//