ID A0A158Q904_9BILA Unreviewed; 1363 AA.
AC A0A158Q904;
DT 08-JUN-2016, integrated into UniProtKB/TrEMBL.
DT 08-JUN-2016, sequence version 1.
DT 27-MAR-2024, entry version 28.
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};
OS Elaeophora elaphi.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Spirurina; Spiruromorpha; Filarioidea; Onchocercidae; Elaeophora.
OX NCBI_TaxID=1147741 {ECO:0000313|Proteomes:UP000050640, ECO:0000313|WBParaSite:EEL_0000927401-mRNA-1};
RN [1] {ECO:0000313|WBParaSite:EEL_0000927401-mRNA-1}
RP IDENTIFICATION.
RG WormBaseParasite;
RL Submitted (APR-2016) to UniProtKB.
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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR STRING; 1147741.A0A158Q904; -.
DR WBParaSite; EEL_0000927401-mRNA-1; EEL_0000927401-mRNA-1; EEL_0000927401.
DR Proteomes; UP000050640; Unplaced.
DR GO; GO:0017101; C:aminoacyl-tRNA synthetase multienzyme complex; IEA:UniProt.
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:0004827; F:proline-tRNA ligase activity; IEA:InterPro.
DR GO; GO:0006424; P:glutamyl-tRNA aminoacylation; IEA:InterPro.
DR GO; GO:0006433; P:prolyl-tRNA aminoacylation; IEA:InterPro.
DR CDD; cd00807; GlnRS_core; 1.
DR CDD; cd00778; ProRS_core_arch_euk; 1.
DR CDD; cd00936; WEPRS_RNA; 2.
DR Gene3D; 1.20.1050.130; -; 1.
DR Gene3D; 3.40.50.620; HUPs; 1.
DR Gene3D; 1.10.287.10; S15/NS1, RNA-binding; 4.
DR HAMAP; MF_02076; Glu_tRNA_synth_type2; 1.
DR InterPro; IPR002314; aa-tRNA-synt_IIb.
DR InterPro; IPR001412; aa-tRNA-synth_I_CS.
DR InterPro; IPR006195; aa-tRNA-synth_II.
DR InterPro; IPR045864; aa-tRNA-synth_II/BPL/LPL.
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; IPR036282; Glutathione-S-Trfase_C_sf.
DR InterPro; IPR004499; Pro-tRNA-ligase_IIa_arc-type.
DR InterPro; IPR033721; ProRS_core_arch_euk.
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 InterPro; IPR009068; uS15_NS1_RNA-bd_sf.
DR InterPro; IPR000738; WHEP-TRS_dom.
DR NCBIfam; TIGR00463; gltX_arch; 1.
DR NCBIfam; TIGR00408; proS_fam_I; 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 Pfam; PF00587; tRNA-synt_2b; 1.
DR Pfam; PF00458; WHEP-TRS; 4.
DR PRINTS; PR00987; TRNASYNTHGLU.
DR SMART; SM00991; WHEP-TRS; 4.
DR SUPFAM; SSF55681; Class II aaRS and biotin synthetases; 1.
DR SUPFAM; SSF47616; GST C-terminal domain-like; 1.
DR SUPFAM; SSF52374; Nucleotidylyl transferase; 1.
DR SUPFAM; SSF50715; Ribosomal protein L25-like; 1.
DR SUPFAM; SSF47060; S15/NS1 RNA-binding domain; 4.
DR PROSITE; PS00178; AA_TRNA_LIGASE_I; 1.
DR PROSITE; PS50862; AA_TRNA_LIGASE_II; 1.
DR PROSITE; PS51185; WHEP_TRS_2; 4.
PE 3: Inferred from homology;
KW Aminoacyl-tRNA synthetase {ECO:0000256|ARBA:ARBA00023146};
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
KW Ligase {ECO:0000256|ARBA:ARBA00022598};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Protein biosynthesis {ECO:0000256|ARBA:ARBA00022917}.
FT DOMAIN 781..837
FT /note="WHEP-TRS"
FT /evidence="ECO:0000259|PROSITE:PS51185"
FT DOMAIN 841..897
FT /note="WHEP-TRS"
FT /evidence="ECO:0000259|PROSITE:PS51185"
FT DOMAIN 911..967
FT /note="WHEP-TRS"
FT /evidence="ECO:0000259|PROSITE:PS51185"
FT DOMAIN 982..1038
FT /note="WHEP-TRS"
FT /evidence="ECO:0000259|PROSITE:PS51185"
FT DOMAIN 1109..1350
FT /note="Aminoacyl-transfer RNA synthetases class-II family
FT profile"
FT /evidence="ECO:0000259|PROSITE:PS50862"
FT REGION 745..775
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1363 AA; 155308 MW; 2AE32EB6E50C81B6 CRC64;
MVVTDTSVES AERRTVTFSI SRRNPAYGTI LALSATGFSI EKSVIFTDEM LNEMILDGIK
YTNDASIARF IVRSSDKAGD LFGRDVIEQA EVDCWVTMVE QYLQHGDLKD FMKSAEEKLE
TSLYLCLNRR TLADIMLWTV IAADANAQQQ KPFSSFFENI LHDPLFADAH NAIGKFQIGT
LEKLQKRKME SKTITTAKRQ DEATKIVEGK KVKDQVKDEG KFIELPGAKK GKVVVRFPPE
ASGYLHIGHA KAALLNQYYQ QTFEGKLIMR FDDTNPAKEN AHFEQVILED LKMLQVKPDR
WTHTSDHFDL ILEMCERLLQ EGKAYVDDTD AELMKKEREE RKESRCRNNT PEQNLALWEE
MKKATIKGQR CCVRIKIDMQ SNNGAMRDPT IYRCRTETHI RTGNKYKVYP TYDFACPIVD
SIEGVTHALR TTEYTDRDEQ YYFICDVLGL RKPYIWSYAR LNMTNTVMSK RKLTWLVDEH
HVEGWDDPRL PTVRGIMRRG LTVEGLKQFI VAQGGSRAVV MMEWDKIWSF NKKVIDPVAP
RYTALDCTEN LVQVMVMDNL TEESKEVSLH PKNVEVGTKT IWYSKKLLVE GLDAREMKIG
DSVTFINLGN VKICHILKDG DKIIEIGAKL DLENKDYKKT LKVTWIADTK LGPKVPVKII
EYSHVISKAI IGKDEDWKQF VNYDSVKYLD FVGEPAMKEI CKGDIIQLQR KGYYICDSAY
TSKSEYSGCE VPIILILIPD GSNKPVKSTH TTTEKNSSNI ELGRTNSDVQ INGNASTNEK
DVLKLSQQIK EQGDLVRSLK AADPKGEKTK EAIAVLLSLK KAYQKLSAED NKANKLPSLD
SANDLYQSIE EQGNLVRSLK AANPKSDETK AAISKLLDLK KRYKESTGSE YKPKSAVSSQ
EQRQLTMERR SIDELYKQIE EQGNIVRALK ASNPKSEEAK AAVAKLLDMK QKYMEIAGKE
YKPGTVAVTS SNNKVESDNT KCKETFAKEI AQQGDLVRSL KAEDSKSREV KDAIAELLKL
KKQYKDEFGE EYGARTSNTN ASIPKKEEVE FEMAGASMKT VEMVRQTKLG LDVKKEENLA
EWYSQIIIKA DMIEYYDVSG CYILRPWSFA IWEVIKKWFD TEIKKLGVRN CYFPMFVSHN
ALQKEKEHIA DFAPEVAWVT RAGNSELSEP IAIRPTSETV IYPSYAKWIQ SYRDLPILLN
QWCNVVRWEF KHPTPFLRTR EFLWQEGHTA FQTKQEAEKE VFTILDLYTK VYTDLLAIPV
TKGRKSEKEK FAGGDFTTTV EAYVPINGRG IQGATSHHLG QNFSKMFDIS FEDPETGKKT
FAWQNSWGMT TRTIGAMIMI HSDNDGLVLP PRVAPVQVSI LLN
//
