ID A0A0D2G8L8_9EURO Unreviewed; 558 AA.
AC A0A0D2G8L8;
DT 29-APR-2015, integrated into UniProtKB/TrEMBL.
DT 29-APR-2015, sequence version 1.
DT 27-MAR-2024, entry version 35.
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=PV04_04216 {ECO:0000313|EMBL:KIW68259.1};
OS Phialophora macrospora.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Chaetothyriomycetidae; Chaetothyriales; Herpotrichiellaceae; Phialophora.
OX NCBI_TaxID=1851006 {ECO:0000313|EMBL:KIW68259.1, ECO:0000313|Proteomes:UP000054266};
RN [1] {ECO:0000313|EMBL:KIW68259.1, ECO:0000313|Proteomes:UP000054266}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 27337 {ECO:0000313|EMBL:KIW68259.1,
RC ECO:0000313|Proteomes:UP000054266};
RG The Broad Institute Genomics Platform;
RA Cuomo C., de Hoog S., Gorbushina A., Stielow B., Teixiera M.,
RA Abouelleil A., Chapman S.B., Priest M., Young S.K., Wortman J., Nusbaum C.,
RA Birren B.;
RT "The Genome Sequence of Capronia semiimmersa CBS27337.";
RL Submitted (JAN-2015) 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; KN846958; KIW68259.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0D2G8L8; -.
DR STRING; 5601.A0A0D2G8L8; -.
DR HOGENOM; CLU_001882_1_2_1; -.
DR OrthoDB; 934at2759; -.
DR Proteomes; UP000054266; 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 Gene3D; 3.40.50.620; HUPs; 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 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; 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 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}.
FT DOMAIN 34..341
FT /note="Glutamyl/glutaminyl-tRNA synthetase class Ib
FT catalytic"
FT /evidence="ECO:0000259|Pfam:PF00749"
FT DOMAIN 344..424
FT /note="Glutamyl/glutaminyl-tRNA synthetase class Ib anti-
FT codon binding"
FT /evidence="ECO:0000259|Pfam:PF03950"
FT DOMAIN 464..539
FT /note="tRNA synthetases class I (E and Q) anti-codon
FT binding"
FT /evidence="ECO:0000259|Pfam:PF20974"
FT REGION 1..23
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..22
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 558 AA; 63360 MW; B8D5B83608C52E2B CRC64;
MADKPPKVKD ASGPKGKKAP KVKQMELPNA AAGVVTRFPP EPSGYLHIGH SKAALLNDYF
AHIQYPGGKL ILRFDDTNTE KENAEFQDAI REDVALLGIQ PDVVSYTSDY FDQIDEYCVK
IIQAGKAYAD DTPGDVMSAQ RMAREPSVHR DDSIEDNLAR YEDMKKGTEE GKRWCIRAKI
SYANDNASLR DPVIFRCPKS QTPHHRTGDK YKAYPTYQFA CPVVDALEGV THALRTTEYN
DQDAQYKWIL KALELRPVFI WTFSKIQFVR TLMSKRKLTK LVNAGIVSGW DDPRFPTVRG
IRRRGMTVEG LRDFMVSQGP SKNVVNMDWH TIWTMNKKVI DLRAARYTAI DSNHVVCKIT
NLPQDGPYEE TKPKHAKYDL GDKKVVYSQN ILIEQDDART FAKDEEITLM NWGNAYVRDI
EYSNSTASSA TPDGVADGVS NLGNVSSMTL ELHLDGDFKA TKKKITWLSK DQDLVPIELV
DFDHLLAKDK LTEEDESHWE DFLTKQSEFK TEAVADVNVW DVNVDDVLQF DRKGYYRCDK
APTKEARGIF FKIPSGKE
//
