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Database: UniProt
Entry: A0A2B7Y9E5_9EURO
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ID   A0A2B7Y9E5_9EURO        Unreviewed;       708 AA.
AC   A0A2B7Y9E5;
DT   20-DEC-2017, integrated into UniProtKB/TrEMBL.
DT   20-DEC-2017, sequence version 1.
DT   27-MAR-2024, entry version 18.
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=AJ79_00765 {ECO:0000313|EMBL:PGH18136.1};
OS   Helicocarpus griseus UAMH5409.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Onygenales; Ajellomycetaceae; Helicocarpus.
OX   NCBI_TaxID=1447875 {ECO:0000313|EMBL:PGH18136.1, ECO:0000313|Proteomes:UP000223968};
RN   [1] {ECO:0000313|EMBL:PGH18136.1, ECO:0000313|Proteomes:UP000223968}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=UAMH5409 {ECO:0000313|EMBL:PGH18136.1,
RC   ECO:0000313|Proteomes:UP000223968};
RA   Munoz J.F., Mcewen J.G., Clay O.K., Cuomo C.A.;
RT   "Comparative genomics in systemic dimorphic fungi from Ajellomycetaceae.";
RL   Submitted (OCT-2017) 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}.
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:PGH18136.1}.
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DR   EMBL; PDNB01000006; PGH18136.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A2B7Y9E5; -.
DR   STRING; 1447875.A0A2B7Y9E5; -.
DR   OrthoDB; 934at2759; -.
DR   Proteomes; UP000223968; Unassembled WGS sequence.
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; 3.40.50.620; 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; 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   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:UP000223968}.
FT   DOMAIN          48..186
FT                   /note="GST C-terminal"
FT                   /evidence="ECO:0000259|PROSITE:PS50405"
SQ   SEQUENCE   708 AA;  80222 MW;  A0AF7F00DF4E4F2C CRC64;
     MAHLTVAAKA NNAFILPTLL AVNYVKQSLP GTDITPIFED VESIGTQKAK LELKTEDGKT
     IYDDDVLKHL ENIYEPLQAG NKEQVDEWVK RSTALRPLDF KSLDQPMKEL DAHLTLRSYI
     VGYSLTLADL AVWGTLRGNR IAVSTIRKAA SNTSRWFAFI EASYPWVNIA VTELSANAVK
     RKAAASAAGA SYNIGLQNTE NGVVTRFPPE PSGYLHIGHA KAALLNDYFA HEQYKGTLIC
     RFDDTNPSKE NQEFEDAIKY DLSLLGIYPD KTSFSSDYFQ EMYEYCIQII KDGKAYADDT
     QKEVMQDERF NGIESKRRNE SVEDNLARFA EMKTGSEEGQ RWCIRAKISV DDVNKALRDP
     VIYRCNLQPH HRTGSTWKIY PTYDFCVPIL DSLEGVTHAL RTTEYGDRNA QYFWMQEALG
     IRKVDIWDFS RVNFIRAVLS KRKLTKFVDD GLVWGWDDPR MPTIRGIRRR GMTVPALREF
     ILKQGPSRNV VNLDWTLFWA TNRKYIDPVA PRHTAVDKQD AVPANVQGIE DVQVADKPKH
     GKNAELGSKK VVYSNQILLD QADAATFRQD EEITLMNWGN AIVRKITNDP TTGKVTGLDL
     ELHLAGDVKK TDKKVTWLAK KGQDLVPVEL VDFDYIISKD KIEKDEDVMD FLTPKTEFRS
     EGFADCNVAN LAQGDIIQFE RKGYFRLDRA FKDGKAAVFF NIPTGKTG
//
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