ID A0A2X0MP18_9BASI Unreviewed; 852 AA.
AC A0A2X0MP18;
DT 12-SEP-2018, integrated into UniProtKB/TrEMBL.
DT 12-SEP-2018, sequence version 1.
DT 27-MAR-2024, entry version 21.
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=BZ3500_MVSOF-1268-A1-R1_CHR12-2G03709
GN {ECO:0000313|EMBL:SCZ94134.1};
OS Microbotryum saponariae.
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Pucciniomycotina;
OC Microbotryomycetes; Microbotryales; Microbotryaceae; Microbotryum.
OX NCBI_TaxID=289078 {ECO:0000313|EMBL:SCZ94134.1, ECO:0000313|Proteomes:UP000249723};
RN [1] {ECO:0000313|Proteomes:UP000249723}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Jeantristanb JTB J.-T., Ricardo R.;
RL Submitted (OCT-2016) to the EMBL/GenBank/DDBJ databases.
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 -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
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; FMWP01000052; SCZ94134.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2X0MP18; -.
DR STRING; 289078.A0A2X0MP18; -.
DR Proteomes; UP000249723; Unassembled WGS sequence.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
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 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; IPR020061; Glu_tRNA_lig_a-bdl.
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.
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 Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
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:UP000249723}.
FT DOMAIN 45..186
FT /note="GST C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS50405"
FT REGION 542..564
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 748..810
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 757..783
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 852 AA; 94463 MW; 76C7444AB74D42E8 CRC64;
MAATTTLRLV AQPGKTTPQP FGVLATALAL PSSSSHSVNL EWVHSLPEGA NAVQLVLDGK
ITLGPIEAQQ ALANAFAPEG IYGSDKDESA QITALLLSLP PHPPALPTAL KLLSALERRL
TLRTYLVGHT PTVADYAVWG HLRANPIALG VLAKPGVPHT ARWYAHLTNL DPCQTAVSTI
FQQAKLKAPS ANKADDKKDD GANATFELGL PNAVKGQVVT RLPPEPSGYL HIGHAKAAIL
NQYFARMYEG RFLIRFDDTN PSKEKAEFEE SIIEDLALLG VKADATSYTS DYFDVLQRYC
VQIIKQGNAY ADDTEQEKMR DQRMNGVPSE RRDASVEDNL AHFAEMATGS DEGRRWCIRA
KISVDDPNKA MRDPVIYRCN LLPHHRTGTK YKMYPTYDFC CPIVDSLEGV THALRTNEYR
DRNPQYQWML ATLGLRRVEV WDFGRLAFVY TLLSKRKLKW FVEEGHVRGW DDPRFATVRG
IRRRGMTIEA LTQFMLMQGP SQAFTNLEWD VFWSLNKKVI DPIAPRFTAL EKKDLVKVKI
TGGEGLPTNG PESKSMPKHK KNAEVGEKTT WFDSTIYVEQ VDAITFAQGE EITLMDWGNA
FVRSIQRAGG APEGKVETIE MELNLSGDFK KTKKKITWLA SPSSNDGLRA LTKVTLLDYD
YLIFKKKMEE DDKFEDWLTP QTEFRTEAFA DVNVAGLEKG TIIQFERKGF YIVDKAVKDG
GEEGAELILI PDGKVSTVVS KHEAALNAAA AASKPKGGED KAGKAKKEDK KAKGGEKKQK
KVEAATTTTA TRGLPDLAPE EPKESVLLSD GKEGFEQKVF TKMFKVPSVY GEDGVDAPAT
TKMFAVKPVY QQ
//
