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Database: UniProt
Entry: A0A151SRX7_CAJCA
LinkDB: A0A151SRX7_CAJCA
Original site: A0A151SRX7_CAJCA 
ID   A0A151SRX7_CAJCA        Unreviewed;       727 AA.
AC   A0A151SRX7;
DT   08-JUN-2016, integrated into UniProtKB/TrEMBL.
DT   08-JUN-2016, sequence version 1.
DT   27-MAR-2024, entry version 27.
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=KK1_003859 {ECO:0000313|EMBL:KYP57594.1};
OS   Cajanus cajan (Pigeon pea) (Cajanus indicus).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   rosids; fabids; Fabales; Fabaceae; Papilionoideae; 50 kb inversion clade;
OC   NPAAA clade; indigoferoid/millettioid clade; Phaseoleae; Cajanus.
OX   NCBI_TaxID=3821 {ECO:0000313|EMBL:KYP57594.1, ECO:0000313|Proteomes:UP000075243};
RN   [1] {ECO:0000313|EMBL:KYP57594.1, ECO:0000313|Proteomes:UP000075243}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. Asha {ECO:0000313|Proteomes:UP000075243};
RX   PubMed=22057054; DOI=10.1038/nbt.2022;
RA   Varshney R.K., Chen W., Li Y., Bharti A.K., Saxena R.K., Schlueter J.A.,
RA   Donoghue M.T., Azam S., Fan G., Whaley A.M., Farmer A.D., Sheridan J.,
RA   Iwata A., Tuteja R., Penmetsa R.V., Wu W., Upadhyaya H.D., Yang S.P.,
RA   Shah T., Saxena K.B., Michael T., McCombie W.R., Yang B., Zhang G.,
RA   Yang H., Wang J., Spillane C., Cook D.R., May G.D., Xu X., Jackson S.A.;
RT   "Draft genome sequence of pigeonpea (Cajanus cajan), an orphan legume crop
RT   of resource-poor farmers.";
RL   Nat. Biotechnol. 30:83-89(2012).
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   -!- 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; CM003613; KYP57594.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A151SRX7; -.
DR   STRING; 3821.A0A151SRX7; -.
DR   OMA; CPVVDSH; -.
DR   OrthoDB; 2733051at2759; -.
DR   Proteomes; UP000075243; Chromosome 11.
DR   GO; GO:0005737; C:cytoplasm; 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:0006424; P:glutamyl-tRNA aminoacylation; IEA:InterPro.
DR   GO; GO:0009791; P:post-embryonic development; IEA:UniProt.
DR   GO; GO:0048608; P:reproductive structure development; IEA:UniProt.
DR   CDD; cd10289; GST_C_AaRS_like; 1.
DR   Gene3D; 1.20.1050.130; -; 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; IPR036282; Glutathione-S-Trfase_C_sf.
DR   InterPro; IPR004046; GST_C.
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; PF00043; GST_C; 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   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:UP000075243}.
FT   DOMAIN          98..153
FT                   /note="Glutathione S-transferase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00043"
FT   DOMAIN          221..525
FT                   /note="Glutamyl/glutaminyl-tRNA synthetase class Ib
FT                   catalytic"
FT                   /evidence="ECO:0000259|Pfam:PF00749"
FT   DOMAIN          528..615
FT                   /note="Glutamyl/glutaminyl-tRNA synthetase class Ib anti-
FT                   codon binding"
FT                   /evidence="ECO:0000259|Pfam:PF03950"
FT   DOMAIN          632..705
FT                   /note="tRNA synthetases class I (E and Q) anti-codon
FT                   binding"
FT                   /evidence="ECO:0000259|Pfam:PF20974"
SQ   SEQUENCE   727 AA;  82193 MW;  B6FBD5CB1B39EA7E CRC64;
     MDIQTFAFAA SSPPLPVIAT AKLAGISPSI DTSLPPDSSP TFIFSDGLEL HGAHVLLRYI
     GRAANFYGQN AFESSQADEW LEYATILSSG PAFENGCKYI DEYLEKRTFL VGYSLSIADL
     AIWAGLAGSG KRWESLRKSK KYPNLARWFN SIVTEHGTAL NEVTSAYVGK KGLGEPTVTK
     SKDQSVITDK VKNVDGHVSG NNKGGSKPSA EIDLPDAEVG KVRLRFAPEP SGYLHIGHSK
     AALLNKYFAE RYQGQVIVRF DDTNPAKESN EFVDNLVKDI ETLGIKYEQI TYTSDYFPEL
     MELAEKLIHQ GKAYVDDTPR EQMQKERMDG IESKCRNNSV EENIKLWKEM IAGTERGLQC
     CVRGKLDMQD PNKSLRDPVY YRCNPMPHHR IGSKYKVYPT YDFACPYVDA REGITHALRS
     SEYHDRNAQY YRIQEDMGVR KVLIYEFSRL NMVYTLLSKR KLLWFVQNGK VDGWDDARFP
     TVQGIVRRGL KIEALIQFIV EQGASKNLNL MEWDKLWTIN KKIIDPVCPR HTAVIADRRV
     LLTLTDGPEK LFVRIIPRHK KYEAAGVKAT SYTKSIWIDH ADAESISAGE EVTLMDWGNA
     IVKEIVKDQD GNITGLCGVL HLEGSVKTTK LKLTWLPNIN ELVSLTLVEF DYLITKKKLE
     EGEDFIDVVN PCTKKEISAY GDSNMRNLQR GDILQLERKG YFRCDVPFVR FSQPIVLFAI
     PDGRQQT
//
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