ID M0CUP2_9EURY Unreviewed; 581 AA.
AC M0CUP2;
DT 03-APR-2013, integrated into UniProtKB/TrEMBL.
DT 03-APR-2013, sequence version 1.
DT 27-MAR-2024, entry version 49.
DE RecName: Full=Glutamate--tRNA ligase {ECO:0000256|HAMAP-Rule:MF_02076};
DE EC=6.1.1.17 {ECO:0000256|HAMAP-Rule:MF_02076};
DE AltName: Full=Glutamyl-tRNA synthetase {ECO:0000256|HAMAP-Rule:MF_02076};
DE Short=GluRS {ECO:0000256|HAMAP-Rule:MF_02076};
GN Name=gltX {ECO:0000256|HAMAP-Rule:MF_02076,
GN ECO:0000313|EMBL:ELZ25594.1};
GN ORFNames=C475_10338 {ECO:0000313|EMBL:ELZ25594.1};
OS Halosimplex carlsbadense 2-9-1.
OC Archaea; Euryarchaeota; Stenosarchaea group; Halobacteria; Halobacteriales;
OC Haloarculaceae; Halosimplex.
OX NCBI_TaxID=797114 {ECO:0000313|EMBL:ELZ25594.1, ECO:0000313|Proteomes:UP000011626};
RN [1] {ECO:0000313|EMBL:ELZ25594.1, ECO:0000313|Proteomes:UP000011626}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=2-9-1 {ECO:0000313|EMBL:ELZ25594.1,
RC ECO:0000313|Proteomes:UP000011626};
RX PubMed=25393412; DOI=10.1371/journal.pgen.1004784;
RA Becker E.A., Seitzer P.M., Tritt A., Larsen D., Krusor M., Yao A.I., Wu D.,
RA Madern D., Eisen J.A., Darling A.E., Facciotti M.T.;
RT "Phylogenetically driven sequencing of extremely halophilic archaea reveals
RT strategies for static and dynamic osmo-response.";
RL PLoS Genet. 10:E1004784-E1004784(2014).
CC -!- FUNCTION: Catalyzes the attachment of glutamate to tRNA(Glu) in a two-
CC step reaction: glutamate is first activated by ATP to form Glu-AMP and
CC then transferred to the acceptor end of tRNA(Glu). {ECO:0000256|HAMAP-
CC Rule:MF_02076}.
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; Evidence={ECO:0000256|HAMAP-
CC Rule:MF_02076};
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_02076}.
CC -!- SIMILARITY: Belongs to the class-I aminoacyl-tRNA synthetase family.
CC Glutamate--tRNA ligase type 2 subfamily. {ECO:0000256|HAMAP-
CC Rule:MF_02076}.
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:ELZ25594.1}.
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DR EMBL; AOIU01000024; ELZ25594.1; -; Genomic_DNA.
DR RefSeq; WP_006883742.1; NZ_AOIU01000024.1.
DR AlphaFoldDB; M0CUP2; -.
DR STRING; 797114.C475_10338; -.
DR PATRIC; fig|797114.5.peg.2102; -.
DR eggNOG; arCOG04302; Archaea.
DR OrthoDB; 10470at2157; -.
DR Proteomes; UP000011626; Unassembled WGS sequence.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0004818; F:glutamate-tRNA ligase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0006424; P:glutamyl-tRNA aminoacylation; IEA:UniProtKB-UniRule.
DR Gene3D; 2.40.240.100; -; 1.
DR Gene3D; 3.40.50.620; HUPs; 1.
DR HAMAP; MF_02076; Glu_tRNA_synth_type2; 1.
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; 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:SF4; GLUTAMINE--TRNA LIGASE; 1.
DR PANTHER; PTHR43097; GLUTAMINE-TRNA LIGASE; 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; SSF52374; Nucleotidylyl transferase; 1.
DR SUPFAM; SSF50715; Ribosomal protein L25-like; 1.
PE 3: Inferred from homology;
KW Aminoacyl-tRNA synthetase {ECO:0000256|ARBA:ARBA00023146,
KW ECO:0000256|HAMAP-Rule:MF_02076};
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|HAMAP-
KW Rule:MF_02076}; Cytoplasm {ECO:0000256|HAMAP-Rule:MF_02076};
KW Ligase {ECO:0000256|ARBA:ARBA00022598, ECO:0000256|HAMAP-Rule:MF_02076};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|HAMAP-
KW Rule:MF_02076};
KW Protein biosynthesis {ECO:0000256|ARBA:ARBA00022917, ECO:0000256|HAMAP-
KW Rule:MF_02076}; Reference proteome {ECO:0000313|Proteomes:UP000011626}.
FT DOMAIN 107..415
FT /note="Glutamyl/glutaminyl-tRNA synthetase class Ib
FT catalytic"
FT /evidence="ECO:0000259|Pfam:PF00749"
FT DOMAIN 421..500
FT /note="Glutamyl/glutaminyl-tRNA synthetase class Ib anti-
FT codon binding"
FT /evidence="ECO:0000259|Pfam:PF03950"
FT DOMAIN 516..563
FT /note="tRNA synthetases class I (E and Q) anti-codon
FT binding"
FT /evidence="ECO:0000259|Pfam:PF20974"
FT REGION 427..461
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 114..124
FT /note="'HIGH' region"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02076"
SQ SEQUENCE 581 AA; 64874 MW; 604AA7D048890FE2 CRC64;
MDEDVREQAE EAAEVDALFN ALKHDSDAQV GAIMGPLMGQ NPEFREYGDE MAGVVAPVVQ
RVNGMDAAGK RERLEALAPE RVEELEAEDE EDDQVLPDLP NVSEYDEVRM RLAPNPNGPW
HLGSARMPAV IGTYKEMYDG WMLCRFDDTD PETKRPDLDA YDEIVEAVDY LGFEPDEVIK
ASDRVDIYYD HARELIDLGG AYTCSCPGEE FSELKNSAEP CPHRDKDTET VHEEFDAMVD
GEYDSGEMVL RVKTDIEHKN PALRDFVAFR MIDTPHPREA AADYRCWPML DFQSGIDDHL
TGITHIIRGI DLQDSAKRQA FVYDYFGWEY PEVVHWGHVQ IDAYDVPMST STIIEQIEAG
ELTGWDDPRA PTIASLRRRG IRGEAIVDAM VELGTSSSNV DLAMSSIYAT NRDLIDEETD
RAFFVRSEGP GTDGSVELPV SGGPEEGEPL VHPNHEDRGR RSIPVEDGVV VETADLPAAG
ERVWLKGYGC VRYEDDELVA TGDDLDVVRE GDVDVIHWVP AEGPRLRLRT MDGDVTGVAE
PGVRDYEVDD LVQFERVGFA RLDSVPSRGT DDPAVAYYTH P
//
