ID A0A0V1LNW7_9BILA Unreviewed; 558 AA.
AC A0A0V1LNW7;
DT 16-MAR-2016, integrated into UniProtKB/TrEMBL.
DT 16-MAR-2016, sequence version 1.
DT 27-MAR-2024, entry version 23.
DE RecName: Full=Nondiscriminating glutamyl-tRNA synthetase EARS2, mitochondrial {ECO:0000256|ARBA:ARBA00044142};
DE EC=6.1.1.17 {ECO:0000256|ARBA:ARBA00012835};
DE EC=6.1.1.24 {ECO:0000256|ARBA:ARBA00044054};
DE AltName: Full=Glutamate--tRNA(Gln) ligase EARS2, mitochondrial {ECO:0000256|ARBA:ARBA00044313};
DE AltName: Full=Glutamyl-tRNA synthetase {ECO:0000256|ARBA:ARBA00030865};
DE AltName: Full=Mitochondrial glutamyl-tRNA synthetase {ECO:0000256|ARBA:ARBA00044251};
GN Name=EARS2 {ECO:0000313|EMBL:KRZ61068.1};
GN ORFNames=T02_8264 {ECO:0000313|EMBL:KRZ61068.1};
OS Trichinella nativa.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Enoplea; Dorylaimia;
OC Trichinellida; Trichinellidae; Trichinella.
OX NCBI_TaxID=6335 {ECO:0000313|EMBL:KRZ61068.1, ECO:0000313|Proteomes:UP000054721};
RN [1] {ECO:0000313|EMBL:KRZ61068.1, ECO:0000313|Proteomes:UP000054721}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ISS10 {ECO:0000313|EMBL:KRZ61068.1};
RA Korhonen P.K., Edoardo P., Giuseppe L.R., Gasser R.B.;
RT "Evolution of Trichinella species and genotypes.";
RL Submitted (MAY-2015) to the EMBL/GenBank/DDBJ databases.
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:0000256|ARBA:ARBA00043804};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:64613;
CC Evidence={ECO:0000256|ARBA:ARBA00043804};
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:0000256|ARBA:ARBA00043725};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:23541;
CC Evidence={ECO:0000256|ARBA:ARBA00043725};
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:0000256|ARBA:ARBA00043717};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:18398;
CC Evidence={ECO:0000256|ARBA:ARBA00043717};
CC -!- SIMILARITY: Belongs to the class-I aminoacyl-tRNA synthetase family.
CC Glutamate--tRNA ligase type 1 subfamily.
CC {ECO:0000256|ARBA:ARBA00007894}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:KRZ61068.1}.
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DR EMBL; JYDW01000022; KRZ61068.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0V1LNW7; -.
DR STRING; 6335.A0A0V1LNW7; -.
DR Proteomes; UP000054721; Unassembled WGS sequence.
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; 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; 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.
PE 3: Inferred from homology;
KW Aminoacyl-tRNA synthetase {ECO:0000256|ARBA:ARBA00023146,
KW ECO:0000256|RuleBase:RU363037};
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|RuleBase:RU363037};
KW Ligase {ECO:0000256|ARBA:ARBA00022598, ECO:0000256|RuleBase:RU363037};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW ECO:0000256|RuleBase:RU363037};
KW Protein biosynthesis {ECO:0000256|ARBA:ARBA00022917,
KW ECO:0000256|RuleBase:RU363037};
KW Reference proteome {ECO:0000313|Proteomes:UP000054721}.
FT DOMAIN 73..390
FT /note="Glutamyl/glutaminyl-tRNA synthetase class Ib
FT catalytic"
FT /evidence="ECO:0000259|Pfam:PF00749"
FT DOMAIN 425..552
FT /note="Aminoacyl-tRNA synthetase class I anticodon-binding"
FT /evidence="ECO:0000259|Pfam:PF19269"
SQ SEQUENCE 558 AA; 65275 MW; 684325732FD3F114 CRC64;
MHLATFIYIS KDLKLKKHIC FLFMDNSWMA STSSNRSLLE FLMFYCHSVR KSARIRLLLL
CGDAQRRYAS NGVRVRFAPS PTGFLHFGGL RTALFNYFFA KKRDGVFVLR IEDTDRRRIV
NSSVQNLLSV LNYLKITPDE GPANGGPYGP YVQSERIPLY QAAAEQLIAE RKAYRCFCSE
QRISILRKEM ARLNHRKNYD NFCRKLSMEE ANQRMRNGEK FVVRFFQKSR SYSLNDLVYG
KYTTNVSEED GDPVIIKSDQ YPTYHFANVV DDHMMHISHV LRGEEWLTSL SKHLQIYEAF
NWEPPQFGHL PVMLDMDGSK LSKRDLSVHV DHFLASGYHP DALINFVCFA GGGFGDLKNA
DMLYSTKQLI RMFNLNMVQR RRTKLDVQWL KRFNREAIRR QSEDALLEQL LKLINREIPA
EHRIEYDDKY FRSVLRHFRP HIDSLSDLLL SENRYLWSWP NQVDSKLTIT SNQWLLFLDQ
LINQLDALPE DHFMENAVAL NLLNCAKHSQ LQSKKAMQFL RHTLTGADKG LPIAEILVLF
GKTYSLQRLR RIREQSTI
//
