ID A0A0M0JW28_9EUKA Unreviewed; 911 AA.
AC A0A0M0JW28;
DT 11-NOV-2015, integrated into UniProtKB/TrEMBL.
DT 11-NOV-2015, sequence version 1.
DT 27-MAR-2024, entry version 30.
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=Ctob_013363 {ECO:0000313|EMBL:KOO30477.1};
OS Chrysochromulina tobinii.
OC Eukaryota; Haptista; Haptophyta; Prymnesiophyceae; Prymnesiales;
OC Chrysochromulinaceae; Chrysochromulina.
OX NCBI_TaxID=1460289 {ECO:0000313|EMBL:KOO30477.1, ECO:0000313|Proteomes:UP000037460};
RN [1] {ECO:0000313|Proteomes:UP000037460}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=CCMP291 {ECO:0000313|Proteomes:UP000037460};
RX PubMed=26397803; DOI=10.1371/journal.pgen.1005469;
RA Hovde B.T., Deodato C.R., Hunsperger H.M., Ryken S.A., Yost W., Jha R.K.,
RA Patterson J., Monnat R.J. Jr., Barlow S.B., Starkenburg S.R.,
RA Cattolico R.A.;
RT "Genome Sequence and Transcriptome Analyses of Chrysochromulina tobin:
RT Metabolic Tools for Enhanced Algal Fitness in the Prominent Order
RT Prymnesiales (Haptophyceae).";
RL PLoS Genet. 11:e1005469-e1005469(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 -!- 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:KOO30477.1}.
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DR EMBL; JWZX01002218; KOO30477.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0M0JW28; -.
DR OrthoDB; 2733051at2759; -.
DR Proteomes; UP000037460; 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; cd10289; GST_C_AaRS_like; 1.
DR Gene3D; 1.20.1050.130; -; 1.
DR Gene3D; 3.40.50.620; HUPs; 1.
DR Gene3D; 1.10.287.10; S15/NS1, RNA-binding; 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; 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 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; 1.
DR PRINTS; PR00987; TRNASYNTHGLU.
DR SMART; SM00991; WHEP-TRS; 1.
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};
KW Reference proteome {ECO:0000313|Proteomes:UP000037460}.
FT DOMAIN 15..80
FT /note="WHEP-TRS"
FT /evidence="ECO:0000259|SMART:SM00991"
FT REGION 73..168
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 82..151
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 911 AA; 100282 MW; F52080501C25C278 CRC64;
MSVQHVETAA SWEEWERLVT EIGNVVKDLK TAGNADKDTV DSAVAELLHR KEQFKAALEA
AITAAPDEAT AEMLKAKIPA APKPNKQDKK KASKAEDDGA EKDAKSDAAK KQEEEKMAAR
ARKKAAEEAK KQGGGDAPLA KEVKAEEGAS PAKKEASAPA PTAGKRPALE TVTSAAATVS
GGAEKKVVLN RTTELWFGKD APPLFALLAS RLAKREVVIK RVDPKQLPPG STAYLLLPLG
AGSFSGEMVI ARYFARLGPS VDAPSQLYGA PGDAASATTV DQWISHAETL ESATGPMVAE
ALGALNTHLT MRTVIAGHAV TIGDGAVWLA LKRNAAAAKA SSHGFPHVRR WLKFMETHPA
CVAIAQDFLG AQKDGAGSLD LALKDAVMGE VVTRFPPEPS GHLHIGHVKA ALLNSHFAER
YQGKMLLRFD DTNPSKEKEE YEEAIRHDLA RLEIVPAAVS HTSDWFGDIK DIATEMIKAG
LAYCDPSPQE EQQKNRFERK ENVHRSASVE ENLRWWDEMQ KGSEEGLTCC LRAKIDMKSD
NGAMRDPTIF RCNLTPHAQT KDKYKAYPTY DMACPIVDWL EGVTHTLRDS QYADRDAQYR
WFLEALAPYL TARRARGPIN FQPFSRVNFV RTLLSKRKLQ WLIDQKQAEG WDDPRFPTVA
GVLRRGLTVA GLKTFILAMG ASKNTNLMEW DKIWAINKAV VDPVATRYTA LLADGLVPFE
LAGAPAEPFA QTLFRHPKDE SLGKKTRLFA STVMLQAEDA ITLEADEEVT LMSWGNAIVR
HVEMGADGKV VRVRGELHIA GDVKKTKKKL TWLASTPDNL VDVELIDLDF MLNKDKIEEE
DDIKEIFNPN TVLPYMAKGE AAMRTIKKGE TIQVERRGFY ICDEPYVRAS EPIKFFFVPD
GKSFFGVPLK K
//
