ID A0A0N4WSI9_HAEPC Unreviewed; 1178 AA.
AC A0A0N4WSI9;
DT 09-DEC-2015, integrated into UniProtKB/TrEMBL.
DT 09-DEC-2015, sequence version 1.
DT 27-MAR-2024, entry version 37.
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=HPLM_LOCUS14501 {ECO:0000313|EMBL:VDO53029.1};
OS Haemonchus placei (Barber's pole worm).
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Rhabditina; Rhabditomorpha; Strongyloidea; Trichostrongylidae; Haemonchus.
OX NCBI_TaxID=6290 {ECO:0000313|Proteomes:UP000038042, ECO:0000313|WBParaSite:HPLM_0001450901-mRNA-1};
RN [1] {ECO:0000313|WBParaSite:HPLM_0001450901-mRNA-1}
RP IDENTIFICATION.
RG WormBaseParasite;
RL Submitted (FEB-2017) to UniProtKB.
RN [2] {ECO:0000313|EMBL:VDO53029.1, ECO:0000313|Proteomes:UP000268014}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MHpl1 {ECO:0000313|EMBL:VDO53029.1,
RC ECO:0000313|Proteomes:UP000268014};
RG Pathogen Informatics;
RL Submitted (NOV-2018) to the EMBL/GenBank/DDBJ databases.
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; UZAF01018592; VDO53029.1; -; Genomic_DNA.
DR STRING; 6290.A0A0N4WSI9; -.
DR WBParaSite; HPLM_0001450901-mRNA-1; HPLM_0001450901-mRNA-1; HPLM_0001450901.
DR OMA; GSDHKPG; -.
DR Proteomes; UP000038042; Unplaced.
DR Proteomes; UP000268014; Unassembled WGS sequence.
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:0006424; P:glutamyl-tRNA aminoacylation; IEA:InterPro.
DR CDD; cd00807; GlnRS_core; 1.
DR CDD; cd00936; WEPRS_RNA; 3.
DR Gene3D; 3.40.50.620; HUPs; 1.
DR Gene3D; 1.10.287.10; S15/NS1, RNA-binding; 6.
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; 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 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; PF00458; WHEP-TRS; 5.
DR PRINTS; PR00987; TRNASYNTHGLU.
DR SMART; SM00991; WHEP-TRS; 7.
DR SUPFAM; SSF52374; Nucleotidylyl transferase; 1.
DR SUPFAM; SSF50715; Ribosomal protein L25-like; 1.
DR SUPFAM; SSF47060; S15/NS1 RNA-binding domain; 6.
DR PROSITE; PS00178; AA_TRNA_LIGASE_I; 1.
DR PROSITE; PS51185; WHEP_TRS_2; 5.
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};
KW Reference proteome {ECO:0000313|Proteomes:UP000268014}.
FT DOMAIN 728..798
FT /note="WHEP-TRS"
FT /evidence="ECO:0000259|PROSITE:PS51185"
FT DOMAIN 811..867
FT /note="WHEP-TRS"
FT /evidence="ECO:0000259|PROSITE:PS51185"
FT DOMAIN 883..939
FT /note="WHEP-TRS"
FT /evidence="ECO:0000259|PROSITE:PS51185"
FT DOMAIN 952..1005
FT /note="WHEP-TRS"
FT /evidence="ECO:0000259|PROSITE:PS51185"
FT DOMAIN 1125..1178
FT /note="WHEP-TRS"
FT /evidence="ECO:0000259|PROSITE:PS51185"
FT REGION 857..879
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1053..1080
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1101..1130
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1178 AA; 131180 MW; BFE58D435ED38D3B CRC64;
MVAVKQQPVI NAKQKEVPYA AALAIAFGGY NPCLSIAFNE KEPVGMNMDG SLISNDVTIA
RIVAQSLGLP EFTGSTCFEI AKIDEVLTLC EKVVDGFLVD EEVLSAVQFS KSGTLFEKRV
TVGDVALWSL IIKNPQLQEK FSALLNAIVE DQRFIVAHMM VGKFTNAKIS KPLSKEKQRD
EGKFVELPGA EKGKVVVRFP PEASGYLHIG HAKAALLNQY YQQTFEGQLI MRFDDTNPAK
ENAHFEKVIK EDLAMLNIIP DRWTHSSDYF ELMLQMCEKL LREGKAYVDD TDTETMRKER
EERVESKNRS LSPEANLSLW EEMKKGTERG LQCCVRIKID MQSNNGAMRD PTIYRCKPEE
HVRTGMKYKV YPTYDFACPI VDSVEGVTHA LRTTEYTDRD DQYYFICDAL GLRKPFIWSY
ARLNMTNTVM SKRKLTWFVN EGLVEGWDDP RFPTVRGVMR RGMTVEGLRQ FIIAQGGSRS
VVMMEWDKIW SFNKKVIDPV APRYTALETT AIVPVFISTP VVVQDAEVPL HPKNADVGKK
TIWHSAKLLV EQVDAQEMKS GDTVTFVNWG NIKIVSVNKK NETVSEIHAV LDLANQDYKK
TMKVTWIAEA DIPSAACIPV VAIEYDHIIS KAVVGKEEDW KNFINYESVH YTKMLGEPAL
RSVRKGDIIQ LQRKGFYICD HDYQSKSEFS GTESPLLLIY IPDGHVKEPV NKPKPSSVVA
ASAGKPRDAL ELYKLIEAQG NTVRDLKSKD PKASFQYIYG CYSIFYAEST KLAVQKLLEL
KKQYSEVTGK EYKPGQVPEP SNMVAGSTAN ESLALYMKIE AQGELVRSEK AKDAKSEASK
AAIATLLELK KEYKEKTGQD YKAGQPPATG APSASAPSSA IVEPSNLYAE IEAQGELVRK
EKAKDPKSES AKAAIAKLLD LKKQYKEQTG QDYKPGQQVA SLKSPSIASG GDALSLYSEI
EAQGNLVRQE KAKDAKSATA IAKLLDLKKQ YKEQTGQDYK PGQQVASLKS PSIASGGDAL
SLYSEIEAQG NLEAAKAAIA KLLELKKKYE EVTGYPYKPG QPPAETPSSP QKTASEESAL
YEEIKAQGDL VLELKKKYEE VTGHPYKPGQ PPAETPSSPQ KTAPEESALY EEIKAQGDLV
RQEKQKDAKS DASKAAIQKL LDLKKLYKEK TGQEYKPK
//
