ID U1PIM1_9EURY Unreviewed; 577 AA.
AC U1PIM1;
DT 13-NOV-2013, integrated into UniProtKB/TrEMBL.
DT 13-NOV-2013, sequence version 1.
DT 27-MAR-2024, entry version 48.
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 ORFNames=J07HX64_01704 {ECO:0000313|EMBL:ERH09939.1};
OS halophilic archaeon J07HX64.
OC Archaea; Euryarchaeota; Stenosarchaea group; Halobacteria; Halobacteriales.
OX NCBI_TaxID=1085028 {ECO:0000313|EMBL:ERH09939.1};
RN [1] {ECO:0000313|EMBL:ERH09939.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=23637883;
RA Podell S., Ugalde J.A., Narasingarao P., Banfield J.F., Heidelberg K.B.,
RA Allen E.E.;
RT "Assembly-driven community genomics of a hypersaline microbial ecosystem.";
RL PLoS ONE 8:E61692-E61692(2013).
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}.
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DR EMBL; KE356579; ERH09939.1; -; Genomic_DNA.
DR AlphaFoldDB; U1PIM1; -.
DR STRING; 1085028.J07HX64_01704; -.
DR HOGENOM; CLU_001882_1_3_2; -.
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}.
FT DOMAIN 107..415
FT /note="Glutamyl/glutaminyl-tRNA synthetase class Ib
FT catalytic"
FT /evidence="ECO:0000259|Pfam:PF00749"
FT DOMAIN 434..496
FT /note="Glutamyl/glutaminyl-tRNA synthetase class Ib anti-
FT codon binding"
FT /evidence="ECO:0000259|Pfam:PF03950"
FT DOMAIN 514..563
FT /note="tRNA synthetases class I (E and Q) anti-codon
FT binding"
FT /evidence="ECO:0000259|Pfam:PF20974"
FT REGION 66..106
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 429..458
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 113..123
FT /note="'HIGH' region"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02076"
FT COMPBIAS 66..81
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 82..99
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 577 AA; 63749 MW; 25F98931E7291038 CRC64;
MDDDIRERVE RRAEIDALYN AVKHDSEAQV GAILGPLMSE NPEFRQYGDE IAGAVGPVVG
RVNEMSSDER RTRLEELAPE RVTELEAEEE TDETTLPDLP DADPGDVRMR VAPNPNGPWH
IGHARMAAVV GRYAERYDGS FICRFDDTDP ETKRPDLDAY DAILDAIGYL GFEPDDVVVA
SDRLETYYEH GRRLIDAGGA YTCSCPGAAF SEQKNAGEAC PHRGKNTEQV HEEFGRMIEG
GYDAGEMVLR VRTDIEHPNP ALRDWVAFRM VDTPHPRPVA AGYRCWPMLD FQSGVDDHLT
GVTHIIRGID LQDSAKRQAF VYDYFGWEYP EVVHWGHVEV DAYDVPMSTS SIQEQIETGE
LDGWDDPRAP TVASLRRRGI RGEALVAAMS ELGMSTTNVD LAMSSVYAEN RERIDADADR
AFLVRDTASN GDGAVERPVE GGPDTGTPPV HPEFEGRGRR EIPATGGVLV ESEDLPPAGE
RVWLKGLGCV RHTGGVFEHA DEPLSVTRNE GVDIVHWVPA DDNVPVRLRT PEGDVSGYAE
PGVDTCEPDD LLQFERVGFA RVDSPGTDPV VAYFAHR
//
