ID J4C2Z3_THEOR Unreviewed; 730 AA.
AC J4C2Z3;
DT 31-OCT-2012, integrated into UniProtKB/TrEMBL.
DT 31-OCT-2012, sequence version 1.
DT 27-MAR-2024, entry version 43.
DE RecName: Full=glutamate--tRNA ligase {ECO:0000256|ARBA:ARBA00012835};
DE EC=6.1.1.17 {ECO:0000256|ARBA:ARBA00012835};
DE AltName: Full=Glutamyl-tRNA synthetase {ECO:0000256|ARBA:ARBA00030865};
GN ORFNames=TOT_010001344 {ECO:0000313|EMBL:BAM39541.1};
OS Theileria orientalis strain Shintoku.
OC Eukaryota; Sar; Alveolata; Apicomplexa; Aconoidasida; Piroplasmida;
OC Theileriidae; Theileria.
OX NCBI_TaxID=869250 {ECO:0000313|EMBL:BAM39541.1, ECO:0000313|Proteomes:UP000003786};
RN [1] {ECO:0000313|EMBL:BAM39541.1, ECO:0000313|Proteomes:UP000003786}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Shintoku {ECO:0000313|EMBL:BAM39541.1,
RC ECO:0000313|Proteomes:UP000003786};
RX PubMed=22951932;
RA Hayashida K., Hara Y., Abe T., Yamasaki C., Toyoda A., Kosuge T.,
RA Suzuki Y., Sato Y., Kawashima S., Katayama T., Wakaguri H., Inoue N.,
RA Homma K., Tada-Umezaki M., Yagi Y., Fujii Y., Habara T., Kanehisa M.,
RA Watanabe H., Ito K., Gojobori T., Sugawara H., Imanishi T., Weir W.,
RA Gardner M., Pain A., Shiels B., Hattori M., Nene V., Sugimoto C.;
RT "Comparative genome analysis of three eukaryotic parasites with differing
RT abilities to transform leukocytes reveals key mediators of Theileria-
RT induced leukocyte transformation.";
RL MBio 3:e00204-e00212(2012).
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:ARBA00001818};
CC -!- SIMILARITY: Belongs to the class-I aminoacyl-tRNA synthetase family.
CC Glutamate--tRNA ligase type 2 subfamily.
CC {ECO:0000256|ARBA:ARBA00008927}.
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DR EMBL; AP011946; BAM39541.1; -; Genomic_DNA.
DR RefSeq; XP_009689842.1; XM_009691547.1.
DR AlphaFoldDB; J4C2Z3; -.
DR STRING; 869250.J4C2Z3; -.
DR EnsemblProtists; BAM39541; BAM39541; TOT_010001344.
DR GeneID; 20714143; -.
DR KEGG; tot:TOT_010001344; -.
DR VEuPathDB; PiroplasmaDB:TOT_010001344; -.
DR eggNOG; KOG1147; Eukaryota.
DR OrthoDB; 934at2759; -.
DR Proteomes; UP000003786; Chromosome 1.
DR GO; GO:0005737; C:cytoplasm; IEA:InterPro.
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:0006424; P:glutamyl-tRNA aminoacylation; IEA:InterPro.
DR CDD; cd10289; GST_C_AaRS_like; 1.
DR Gene3D; 1.20.1050.130; -; 1.
DR Gene3D; 3.40.50.620; HUPs; 1.
DR HAMAP; MF_02076; Glu_tRNA_synth_type2; 1.
DR InterPro; IPR001412; aa-tRNA-synth_I_CS.
DR InterPro; IPR004526; Glu-tRNA-synth_arc/euk.
DR InterPro; IPR000924; Glu/Gln-tRNA-synth.
DR InterPro; IPR020058; Glu/Gln-tRNA-synth_Ib_cat-dom.
DR InterPro; IPR020059; Glu/Gln-tRNA-synth_Ib_codon-bd.
DR InterPro; IPR010987; Glutathione-S-Trfase_C-like.
DR InterPro; IPR036282; Glutathione-S-Trfase_C_sf.
DR InterPro; IPR004046; GST_C.
DR InterPro; IPR020056; Rbsml_bL25/Gln-tRNA_synth_N.
DR InterPro; IPR011035; Ribosomal_bL25/Gln-tRNA_synth.
DR InterPro; IPR014729; Rossmann-like_a/b/a_fold.
DR InterPro; IPR049437; tRNA-synt_1c_C2.
DR NCBIfam; TIGR00463; gltX_arch; 1.
DR PANTHER; PTHR43097:SF5; GLUTAMATE--TRNA LIGASE; 1.
DR PANTHER; PTHR43097; GLUTAMINE-TRNA LIGASE; 1.
DR Pfam; PF00043; GST_C; 1.
DR Pfam; PF00749; tRNA-synt_1c; 1.
DR Pfam; PF03950; tRNA-synt_1c_C; 1.
DR Pfam; PF20974; tRNA-synt_1c_C2; 1.
DR PRINTS; PR00987; TRNASYNTHGLU.
DR SUPFAM; SSF47616; GST C-terminal domain-like; 1.
DR SUPFAM; SSF52374; Nucleotidylyl transferase; 1.
DR SUPFAM; SSF50715; Ribosomal protein L25-like; 1.
DR PROSITE; PS00178; AA_TRNA_LIGASE_I; 1.
DR PROSITE; PS50405; GST_CTER; 1.
DR PROSITE; PS51257; PROKAR_LIPOPROTEIN; 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:UP000003786}.
FT DOMAIN 61..194
FT /note="GST C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS50405"
SQ SEQUENCE 730 AA; 84769 MW; 7387FF21C9DFEFC0 CRC64;
MKASNPCSLV VNYSVQNPPY GAVILSCISK YLQKSESSPV EFNLDNKLQN NEFSLNGNNL
NEVELAKKLT TLLPYCDKLL DVPEYSELDY WLKVLLLERE KHLETKKAFF ENVEYFEQMN
NHLAHRTYLI GYRLSLSDVV HFSFLRSNCN VNSLKNKYPH LVRWYNFISN VPVGTYECLK
KYDAPARVQY KKPFTKQEQQ DNSYKGVLKG AEEGCVVTRF PPEPSGYLHI GHAKAAMLNY
YFAQKYKGRM LVRFDDTNPS KEKDEYVDSI MEDLKSLNIK YDELSYTSDY FDVFQEYAVK
LIKKGVVYCD DTDVETMRKQ RGEGIESEAR NNTIEKNLEL FEEMIKGTPV GVKNCVRAKM
DMKNKNKCLR DPVFYRCVTN VPHHRTGDKY KAYPTYEFAC PIVDSLQGVT HSLRTNEYSD
RIPLYYWVLE MCELKHVEIY EFSRMNFIRT TLSKRKLRWF VENKYVNGWD DPRMPTVKGI
LRRGLKVQSL FEFILDQGPS KSVNLMEWDK LWAKNKQIID PVAPRYVAVA SNCVVMTVKN
YEEPEQKKRP LHPKNADLGE TDLAFGDKVI VEKEDFDLIE ENEEVTLMKW GNAYVNKEKR
ELTLNLKGDF KLTKKKIHWL PVSETLVECE LVEYGHLLKV DKVDAELLVD DDSMKEFLEP
VTEWVTKAVG EIGLANLEKG KGSLQNQMCT GTVLQLERKS YYIVDETTQS GKLVLVQIPD
GKVAKTKQKK
//
