ID A3LWB3_PICST Unreviewed; 720 AA.
AC A3LWB3;
DT 03-APR-2007, integrated into UniProtKB/TrEMBL.
DT 03-APR-2007, sequence version 1.
DT 27-MAR-2024, entry version 98.
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 Name=SYE1 {ECO:0000313|EMBL:ABN66938.1};
GN ORFNames=PICST_89978 {ECO:0000313|EMBL:ABN66938.1};
OS Scheffersomyces stipitis (strain ATCC 58785 / CBS 6054 / NBRC 10063 / NRRL
OS Y-11545) (Yeast) (Pichia stipitis).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Debaryomycetaceae; Scheffersomyces.
OX NCBI_TaxID=322104 {ECO:0000313|EMBL:ABN66938.1, ECO:0000313|Proteomes:UP000002258};
RN [1] {ECO:0000313|EMBL:ABN66938.1, ECO:0000313|Proteomes:UP000002258}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 58785 / CBS 6054 / NBRC 10063 / NRRL Y-11545
RC {ECO:0000313|Proteomes:UP000002258};
RX PubMed=17334359; DOI=10.1038/nbt1290;
RA Jeffries T.W., Grigoriev I.V., Grimwood J., Laplaza J.M., Aerts A.,
RA Salamov A., Schmutz J., Lindquist E., Dehal P., Shapiro H., Jin Y.S.,
RA Passoth V., Richardson P.M.;
RT "Genome sequence of the lignocellulose-bioconverting and xylose-fermenting
RT yeast Pichia stipitis.";
RL Nat. Biotechnol. 25:319-326(2007).
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; CP000499; ABN66938.1; -; Genomic_DNA.
DR RefSeq; XP_001384967.1; XM_001384930.1.
DR AlphaFoldDB; A3LWB3; -.
DR STRING; 322104.A3LWB3; -.
DR GeneID; 4839615; -.
DR KEGG; pic:PICST_89978; -.
DR eggNOG; KOG1147; Eukaryota.
DR HOGENOM; CLU_001882_1_2_1; -.
DR InParanoid; A3LWB3; -.
DR OMA; FIHIPDG; -.
DR OrthoDB; 934at2759; -.
DR Proteomes; UP000002258; Chromosome 5.
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 CDD; cd10306; GST_C_GluRS_N; 1.
DR Gene3D; 1.20.1050.10; -; 1.
DR Gene3D; 3.40.30.70; -; 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; IPR041103; GluRS_N.
DR InterPro; IPR036282; Glutathione-S-Trfase_C_sf.
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; PF18466; GluRS_N; 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.
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:UP000002258}.
FT DOMAIN 23..75
FT /note="Glutamate--tRNA ligase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF18466"
FT DOMAIN 211..516
FT /note="Glutamyl/glutaminyl-tRNA synthetase class Ib
FT catalytic"
FT /evidence="ECO:0000259|Pfam:PF00749"
FT DOMAIN 519..609
FT /note="Glutamyl/glutaminyl-tRNA synthetase class Ib anti-
FT codon binding"
FT /evidence="ECO:0000259|Pfam:PF03950"
FT DOMAIN 621..694
FT /note="tRNA synthetases class I (E and Q) anti-codon
FT binding"
FT /evidence="ECO:0000259|Pfam:PF20974"
SQ SEQUENCE 720 AA; 81764 MW; 5313FA2412871B18 CRC64;
MSLTLSIAAK APFVAYPALI AANFVNTSDV DSSILIEFID EKSVEGSDSS VKLVSAGKTV
TDQVEILSIL AEQFPSVLTA ELGNVWSKFA VDKLYVKNFK ELAVDLEKLD AHLNFKSFIS
GYSYTTADIA VWGVLRANAL MGSVIKNGVY TNVSRWYSLL ADDSRFESVV EFMIKSVNDL
RKSAKTAKNG GKKETHKANF EIDLPGAEMG KVVTRFPPEP SGYLHIGHAK AAILNEYFAH
NYKGQLVIRF DDTNPTKEKE EFQDSIIEDL ALLGVKGEKV TFSSDYFDTM YDLAIKLIKD
GNAYCDDTPL EKMREERMVG EASARRNRSV EENLHIFTEE MKNGTEEGLK NCLRAKIDYT
APNKALRDPV MYRCNLTPHH RTGTQWKMYP IYDFCVPVVD SIEGITHALR TNEYRDRNPQ
YQWIQKALGL RPVEIWDFGR VNFVRTLLSK RKLQWFVDKG HVANWDDPRF PTIRGVRRRG
MTIEGLRNFI ISQGPSKNII NMDWSTIWAM NKKVIDPVAP RFTAVYAENA VPVKLLNVPA
EAYTEEKPKH KKNPEVGNKP VVYFNELLID QADADLVEGE EITFMDWGNV IVSKVNKEGD
VVKSIEANLH LEGDFRKTSK KITWLANTSD KVDVDLVDFD HLITKDKLEE EDNFEDFLTP
ETEFHTKAFA DLNIRKLKTG DIIQFERKGY YRVDQPYKEG KPAVLFTIPD GKAVSKYGKK
//
