ID M7XIT2_RHOT1 Unreviewed; 834 AA.
AC M7XIT2;
DT 29-MAY-2013, integrated into UniProtKB/TrEMBL.
DT 29-MAY-2013, sequence version 1.
DT 27-MAR-2024, entry version 44.
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=RHTO_03621 {ECO:0000313|EMBL:EMS20088.1};
OS Rhodotorula toruloides (strain NP11) (Yeast) (Rhodosporidium toruloides).
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Pucciniomycotina;
OC Microbotryomycetes; Sporidiobolales; Sporidiobolaceae; Rhodotorula.
OX NCBI_TaxID=1130832 {ECO:0000313|EMBL:EMS20088.1, ECO:0000313|Proteomes:UP000016926};
RN [1] {ECO:0000313|EMBL:EMS20088.1, ECO:0000313|Proteomes:UP000016926}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NP11 {ECO:0000313|EMBL:EMS20088.1,
RC ECO:0000313|Proteomes:UP000016926};
RX PubMed=23047670; DOI=10.1038/ncomms2112;
RA Zhu Z., Zhang S., Liu H., Shen H., Lin X., Yang F., Zhou Y.J., Jin G.,
RA Ye M., Zou H., Zou H., Zhao Z.K.;
RT "A multi-omic map of the lipid-producing yeast Rhodosporidium toruloides.";
RL Nat. Commun. 3:1112-1112(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; KB722663; EMS20088.1; -; Genomic_DNA.
DR RefSeq; XP_016271207.1; XM_016417291.1.
DR AlphaFoldDB; M7XIT2; -.
DR GeneID; 27367634; -.
DR eggNOG; KOG1147; Eukaryota.
DR HOGENOM; CLU_001882_1_2_1; -.
DR OrthoDB; 934at2759; -.
DR Proteomes; UP000016926; Unassembled WGS sequence.
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; cd00807; GlnRS_core; 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; 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; 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 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}.
FT DOMAIN 50..186
FT /note="GST C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS50405"
FT REGION 738..770
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 754..768
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 834 AA; 92492 MW; 00F4EC5C4A2A4407 CRC64;
MASAATPILR LQAKSSPIPL GLCAFAYSLP PAQIQLEWVH SLPKEANGAN CQVEINGKSV
FGTVDCFKAL GDAFAAQGAL GKDNKESTEI LSLLLLAPPF PPSFPTATSF LSTLEQRLTL
RTYLTGSSHP TVADYHLWAA VKTNVIAIGL LPKALHTQRW FNHLSALPPC AKALVDVPAQ
SKVKPAPAAD KKDEKKKEEK ANATFELGLP GAQKGKVVTR LPPEPSGYLH IGHAKAAVLN
QYFARMYDGK FLVRFDDTNP SKEKAEFEQS IVEDLALLGI KADATSYTSD YFDQLQQYAI
QLIKDGKAYA DDTEQEVMRD QRMNGVASAR RDLSPEESLA KFAEMATGSD EGKRWCIRAK
MSVDDPNKAL RDPVIYRVND LPHHRTGSKY KIYPTYDFAC PVVDSIEGVT HALRTNEYRD
RNPQYQWMLD AVGLRKVNVW DFGRLAFVYT LLSKRKLKWF VENGYVSGWD DPRFPTVRGI
RRRGMTVEAI TQFMLQQGPS QAFLNLEWDV IWNLNKKVID PVAPRFVALE KENLVPVKIV
GGEGKPAEGQ VESKVVPKHK KNPEVGEKTT FYTDTIYVEQ ADAASFAQDE ELTLMDWGNA
FVRKISRSSD SGPVTSLEME LNLAGDFKKT KKKVTWLASP KAPSSPEDLT QVSLLDYDYL
ITKKKLEEDD NVEDLINPTT EYRTDAVADH NVASLAQGTI IQFERKGFYI VDRAFDASNP
SQRVELILIP DGRASSVALK HQAPSAPAKD ASKASKTPSK DKQAAMKAKK GAEAISLPEL
APAEAVEVVL KSDGSRGYDI PVKTKMYKVD SPHGHEAYET PTTTSMYEMR PINE
//
