ID A0A367LBD1_9HYPO Unreviewed; 1003 AA.
AC A0A367LBD1;
DT 07-NOV-2018, integrated into UniProtKB/TrEMBL.
DT 07-NOV-2018, sequence version 1.
DT 27-MAR-2024, entry version 19.
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=L249_7619 {ECO:0000313|EMBL:RCI11733.1};
OS Ophiocordyceps polyrhachis-furcata BCC 54312.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Hypocreales; Ophiocordycipitaceae; Ophiocordyceps.
OX NCBI_TaxID=1330021 {ECO:0000313|EMBL:RCI11733.1, ECO:0000313|Proteomes:UP000253664};
RN [1] {ECO:0000313|EMBL:RCI11733.1, ECO:0000313|Proteomes:UP000253664}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BCC 54312 {ECO:0000313|EMBL:RCI11733.1,
RC ECO:0000313|Proteomes:UP000253664};
RX PubMed=26511477; DOI=10.1186/s12864-015-2101-4;
RA Wichadakul D., Kobmoo N., Ingsriswang S., Tangphatsornruang S.,
RA Chantasingh D., Luangsa-ard J.J., Eurwilaichitr L.;
RT "Insights from the genome of Ophiocordyceps polyrhachis-furcata to
RT pathogenicity and host specificity in insect fungi.";
RL BMC Genomics 16:881-881(2015).
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 Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-pass membrane protein
CC {ECO:0000256|ARBA:ARBA00004141}.
CC -!- SIMILARITY: Belongs to the arsenical resistance-3 (ACR3) (TC 2.A.59)
CC family. {ECO:0000256|ARBA:ARBA00010110}.
CC -!- SIMILARITY: Belongs to the class-I aminoacyl-tRNA synthetase family.
CC Glutamate--tRNA ligase type 2 subfamily.
CC {ECO:0000256|ARBA:ARBA00008927}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:RCI11733.1}.
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DR EMBL; LKCN02000010; RCI11733.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A367LBD1; -.
DR STRING; 1330021.A0A367LBD1; -.
DR Proteomes; UP000253664; Unassembled WGS sequence.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0015297; F:antiporter activity; 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:0015103; F:inorganic anion transmembrane transporter activity; IEA:InterPro.
DR GO; GO:0006424; P:glutamyl-tRNA aminoacylation; IEA:InterPro.
DR Gene3D; 1.20.1050.10; -; 1.
DR Gene3D; 1.20.1530.20; -; 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; IPR004706; Arsenical-R_Acr3.
DR InterPro; IPR002657; BilAc:Na_symport/Acr3.
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; IPR038770; Na+/solute_symporter_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; TIGR00832; acr3; 1.
DR NCBIfam; TIGR00463; gltX_arch; 1.
DR PANTHER; PTHR43097:SF5; GLUTAMATE--TRNA LIGASE; 1.
DR PANTHER; PTHR43097; GLUTAMINE-TRNA LIGASE; 1.
DR Pfam; PF01758; SBF; 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.
DR PROSITE; PS00178; AA_TRNA_LIGASE_I; 1.
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}; Membrane {ECO:0000256|SAM:Phobius};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Protein biosynthesis {ECO:0000256|ARBA:ARBA00022917};
KW Reference proteome {ECO:0000313|Proteomes:UP000253664};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 670..688
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 700..719
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 739..763
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 772..788
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 800..821
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 833..857
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 877..896
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 908..929
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 970..991
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 115..420
FT /note="Glutamyl/glutaminyl-tRNA synthetase class Ib
FT catalytic"
FT /evidence="ECO:0000259|Pfam:PF00749"
FT DOMAIN 424..502
FT /note="Glutamyl/glutaminyl-tRNA synthetase class Ib anti-
FT codon binding"
FT /evidence="ECO:0000259|Pfam:PF03950"
FT DOMAIN 532..606
FT /note="tRNA synthetases class I (E and Q) anti-codon
FT binding"
FT /evidence="ECO:0000259|Pfam:PF20974"
FT REGION 626..655
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 626..648
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1003 AA; 112440 MW; E4E85D67D0D89D76 CRC64;
MKDAELEKLW TKLSGDFRSI EPHLRDLDKH LTLRSHLTGY SLGDVETKTW QTLRANKVAM
GSIRKNGLPN LTRWFTFIEQ SNPQIHEASK SADAAAKKPG GANYNLALQD TDKGVVTRFL
PEPSGYLHIG HAKAALLSDY FGHVAYKGKM RLRLDDTNPS KESEEFQDAI VEDLALMGIK
ADSLTYTSDY FDYLYDMCRK LISMGKAYAD DTGLETMRAQ RMDGIPSKRR DRSVDENLRI
FEEMKKGSDE GLVNCIRAKI SADDPNKALR DPVIYRCNVK DAHHRTGRKW NMYPMYDFAC
PVVDSHEGVT HALRSTEYTD RNPQYQWFLD TLGLRQVHMW DFSRINLIKT FLSKRKLAKL
VESGKVWGWD DPRMPTIRGV RRRGMTVPAL RDFILRQGPS RNVVVMDWTS FWNTNKKEID
PVVPRHTALL AKDMVKAKLT GSDVPSGVVV EQRPKHPKNA SVGTKDLVLS SEIYLDQVDA
KSFAVGEEVT LMGWGNAIVR DPPASSSSER DAVKTMTLEL NLKGDFKATE KKVTWLSAQG
LDLVPAELWD FDYLITKDKL EEEDKVEDFL NPVTATMEEA RCDGGVGLLK ADDIIQLERR
GFYRVDKGLK DWKGDEAGII MTREAKQDPS PIEEADATEH RRQQQHHGHD LPCPPSKSAF
RELGLLDRFL ALWILLAMLV GIVVGNFAAG AERVLQQGRF IGVSIPIAVG LLVMMYPILC
NVRFESLHLV LRQKRLWRQL GFSLVINWLI APFFMLALAS AFLPDQPGLR KGLMLVGLGR
CIAMVLIWNE LAGGDGEYCA VLVAVNSLLQ LLLFAPMAIF LIGVVRHDDG VRLLTYSVVA
SSVGVFLGIP LAAAVATRLS VRKLAGERWF DDVFMRWLSP WSLIGLLYTV VVLFAAQGRH
VVHQIVSVVR VAAPLVVYFM AIFFGALWAT RRLGFGYRLG CAQSFTAASN NFELAIAVAV
ATFGPDGDEA LASSVGPLIE VPVLLTLVYL VRGIGRRWDW REG
//
