ID B9WJK9_CANDC Unreviewed; 724 AA.
AC B9WJK9;
DT 24-MAR-2009, integrated into UniProtKB/TrEMBL.
DT 24-MAR-2009, sequence version 1.
DT 27-MAR-2024, entry version 82.
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 OrderedLocusNames=Cd36_70040 {ECO:0000313|CGD:CAL0000169543};
GN ORFNames=CD36_70040 {ECO:0000313|EMBL:CAX40556.1};
OS Candida dubliniensis (strain CD36 / ATCC MYA-646 / CBS 7987 / NCPF 3949 /
OS NRRL Y-17841) (Yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Debaryomycetaceae; Candida/Lodderomyces clade; Candida.
OX NCBI_TaxID=573826 {ECO:0000313|EMBL:CAX40556.1, ECO:0000313|Proteomes:UP000002605};
RN [1] {ECO:0000313|EMBL:CAX40556.1, ECO:0000313|Proteomes:UP000002605}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CD36 / ATCC MYA-646 / CBS 7987 / NCPF 3949 / NRRL Y-17841
RC {ECO:0000313|Proteomes:UP000002605};
RX PubMed=19745113; DOI=10.1101/gr.097501.109;
RA Jackson A.P., Gamble J.A., Yeomans T., Moran G.P., Saunders D., Harris D.,
RA Aslett M., Barrell J.F., Butler G., Citiulo F., Coleman D.C.,
RA de Groot P.W.J., Goodwin T.J., Quail M.A., McQuillan J., Munro C.A.,
RA Pain A., Poulter R.T., Rajandream M.A., Renauld H., Spiering M.J.,
RA Tivey A., Gow N.A.R., Barrell B., Sullivan D.J., Berriman M.;
RT "Comparative genomics of the fungal pathogens Candida dubliniensis and
RT Candida albicans.";
RL Genome Res. 19:2231-2244(2009).
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; FM992694; CAX40556.1; -; Genomic_DNA.
DR RefSeq; XP_002421224.1; XM_002421179.1.
DR AlphaFoldDB; B9WJK9; -.
DR GeneID; 8049117; -.
DR KEGG; cdu:CD36_70040; -.
DR CGD; CAL0000169543; Cd36_70040.
DR VEuPathDB; FungiDB:CD36_70040; -.
DR eggNOG; KOG1147; Eukaryota.
DR HOGENOM; CLU_001882_1_2_1; -.
DR OrthoDB; 934at2759; -.
DR Proteomes; UP000002605; Chromosome 7.
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; 3.40.30.70; -; 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; IPR041103; GluRS_N.
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; PF18466; GluRS_N; 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.
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 23..75
FT /note="Glutamate--tRNA ligase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF18466"
FT DOMAIN 215..520
FT /note="Glutamyl/glutaminyl-tRNA synthetase class Ib
FT catalytic"
FT /evidence="ECO:0000259|Pfam:PF00749"
FT DOMAIN 523..613
FT /note="Glutamyl/glutaminyl-tRNA synthetase class Ib anti-
FT codon binding"
FT /evidence="ECO:0000259|Pfam:PF03950"
FT DOMAIN 625..698
FT /note="tRNA synthetases class I (E and Q) anti-codon
FT binding"
FT /evidence="ECO:0000259|Pfam:PF20974"
SQ SEQUENCE 724 AA; 82344 MW; AA035A8180021E47 CRC64;
MSFSLSVAGK APNVPYPVLI AVQFINSSDV DVSIPIEFVD DKTVDSKESI KLVTPGGETF
IDQLDALDYL SQTLPELLPE RSKSQEWIKF ALTKLYVKNF KELAVDLEKL DHHLNFRSFI
VGYQYSLADI AIWGVLRANA LMGSVIKNGV YANISRWYNL LADDKRFEGS VELMTKSLAE
LRKAAKSAKT AAAGGKKEAH KASFEIDLPG AEMGKVVTRF PPEPSGYLHI GHAKAAVLNE
YFAHKFNGKL IIRFDDTNPT KEKVEFQDSI IEDLELLGIK GDQVTYSSDY FQTMYDLAVK
MIKDGNAYCD DTPVDTMREQ RMVGDASARR ERSVEENLRI FTEEMKNGTE EGLKNCLRAK
IDYKAPNKAL RDPVIYRCNL TPHHRTGTEW KMYPIYDFCV PVVDSIEGVT HALRTNEYRD
RNPQYEWMQK ALGLRPVAIW DFGRVNFVRT LLSKRKLQWF VDKNYVSNWD DPRFPTVRGV
RRRGMTVEGL RNFIISQGPS RNIINLEWSV IWAMNKKIID PVAPRFTAVD AKNVVPVRLL
NGPKEPYTES KPKHKKNPEV GNKDVIFAAQ VLIDQEDADL SEGEEVTFMD WGNIIVSKVN
KEGDVVKSVE ANLHLEGDFR KTSKKITWLA DTKDKVEIDM VDFDHLITKD KLDENDNFED
FITPETEFHT KGFADLNVGK LKAGDIIQFE RKGYFRVDKP YDGKPAVLFT IPDGKAVSRY
GAKK
//
