ID W5Q6N0_SHEEP Unreviewed; 535 AA.
AC W5Q6N0;
DT 16-APR-2014, integrated into UniProtKB/TrEMBL.
DT 16-APR-2014, sequence version 1.
DT 27-MAR-2024, entry version 53.
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|Ensembl:ENSOARP00000018371.1};
OS Ovis aries (Sheep).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Caprinae; Ovis.
OX NCBI_TaxID=9940 {ECO:0000313|Ensembl:ENSOARP00000018371.1, ECO:0000313|Proteomes:UP000002356};
RN [1] {ECO:0000313|Ensembl:ENSOARP00000018371.1, ECO:0000313|Proteomes:UP000002356}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Texel {ECO:0000313|Ensembl:ENSOARP00000018371.1,
RC ECO:0000313|Proteomes:UP000002356};
RX PubMed=20809919; DOI=10.1111/j.1365-2052.2010.02100.x;
RA Archibald A.L., Cockett N.E., Dalrymple B.P., Faraut T., Kijas J.W.,
RA Maddox J.F., McEwan J.C., Hutton Oddy V., Raadsma H.W., Wade C., Wang J.,
RA Wang W., Xun X.;
RT "The sheep genome reference sequence: a work in progress.";
RL Anim. Genet. 41:449-453(2010).
RN [2] {ECO:0000313|Ensembl:ENSOARP00000018371.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (NOV-2023) to UniProtKB.
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}.
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DR EMBL; AMGL01068857; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR RefSeq; XP_004021249.2; XM_004021200.3.
DR AlphaFoldDB; W5Q6N0; -.
DR SMR; W5Q6N0; -.
DR STRING; 9940.ENSOARP00000018371; -.
DR PaxDb; 9940-ENSOARP00000018371; -.
DR Ensembl; ENSOART00000018633.1; ENSOARP00000018371.1; ENSOARG00000017122.1.
DR GeneID; 101117387; -.
DR KEGG; oas:101117387; -.
DR CTD; 124454; -.
DR eggNOG; KOG1149; Eukaryota.
DR HOGENOM; CLU_015768_6_3_1; -.
DR OMA; EAFKWVG; -.
DR OrthoDB; 5404395at2759; -.
DR Proteomes; UP000002356; Chromosome 24.
DR Bgee; ENSOARG00000017122; Expressed in epididymis and 54 other cell types or tissues.
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; 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 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:UP000002356};
KW RNA-binding {ECO:0000256|ARBA:ARBA00022884}.
FT DOMAIN 49..363
FT /note="Glutamyl/glutaminyl-tRNA synthetase class Ib
FT catalytic"
FT /evidence="ECO:0000259|Pfam:PF00749"
FT DOMAIN 399..533
FT /note="Aminoacyl-tRNA synthetase class I anticodon-binding"
FT /evidence="ECO:0000259|Pfam:PF19269"
SQ SEQUENCE 535 AA; 59218 MW; E8A4AEDBEECEDE2F CRC64;
MHGGPRVPMP PHMAVFLKRL LHPGRSPAAL GRLMGRREAS LGTDPGAAVR VRFAPSPTGF
LHLGGLRTAL YNYIFAKKHQ GSFILRLEDT DQTRLVPGAA ENIEDMLEWA GVPPDESPRR
GGPAGPYLQS QRLALYAQAA EALLKSGAAY LCFCSPQRLE LLKKEALRNR QTPRYDNRCR
SLSQAQVAQK LATDPKPAIR FRLDGEAPAF QDLVYGWNRH EVASVEGDPV ILKSDGFPTY
HLASVVDDHH MGISHVLRGS EWLVSTSKHL LLYQALGWQP PHFAHLPLLL NKDGSKLSKR
QGDIFLEHFA ATGFLPDALL DIITNCGSGF AENQMGRTLP ELIAQFDLSR VTCHSALLDL
EKLPEFNRLH LRRLVGDETQ RCQLVGQLQA LVEEAFGNQL QDREVLDPAY VERIILLRQG
HICRLQDLVS PAYSYLWTRP AVGRAQLGAI SEKVDIIAKR VLGLLEGPGT NLTQDVLNGE
LKKLSDGLEG IKHSNVMKLL RVALSGQQQG PPVAEMMVSL GPKEVRERIQ KVLCS
//
