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Database: UniProt
Entry: A0A087GKE7_ARAAL
LinkDB: A0A087GKE7_ARAAL
Original site: A0A087GKE7_ARAAL 
ID   A0A087GKE7_ARAAL        Unreviewed;       731 AA.
AC   A0A087GKE7;
DT   29-OCT-2014, integrated into UniProtKB/TrEMBL.
DT   29-OCT-2014, sequence version 1.
DT   27-MAR-2024, entry version 37.
DE   RecName: Full=GST C-terminal domain-containing protein {ECO:0000259|PROSITE:PS50405};
GN   OrderedLocusNames=AALP_Aa7g249900 {ECO:0000313|EMBL:KFK30349.1};
OS   Arabis alpina (Alpine rock-cress).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   rosids; malvids; Brassicales; Brassicaceae; Arabideae; Arabis.
OX   NCBI_TaxID=50452 {ECO:0000313|EMBL:KFK30349.1, ECO:0000313|Proteomes:UP000029120};
RN   [1] {ECO:0000313|Proteomes:UP000029120}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. Pajares {ECO:0000313|Proteomes:UP000029120};
RX   PubMed=27246759; DOI=10.1038/nplants.2014.23;
RA   Willing E.M., Rawat V., Mandakova T., Maumus F., James G.V.,
RA   Nordstroem K.J., Becker C., Warthmann N., Chica C., Szarzynska B.,
RA   Zytnicki M., Albani M.C., Kiefer C., Bergonzi S., Castaings L.,
RA   Mateos J.L., Berns M.C., Bujdoso N., Piofczyk T., de Lorenzo L.,
RA   Barrero-Sicilia C., Mateos I., Piednoel M., Hagmann J., Chen-Min-Tao R.,
RA   Iglesias-Fernandez R., Schuster S.C., Alonso-Blanco C., Roudier F.,
RA   Carbonero P., Paz-Ares J., Davis S.J., Pecinka A., Quesneville H.,
RA   Colot V., Lysak M.A., Weigel D., Coupland G., Schneeberger K.;
RT   "Genome expansion of Arabis alpina linked with retrotransposition and
RT   reduced symmetric DNA methylation.";
RL   Nat. Plants 1:14023-14023(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   -!- 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; CM002875; KFK30349.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A087GKE7; -.
DR   EnsemblPlants; KFK30349; KFK30349; AALP_AA7G249900.
DR   Gramene; KFK30349; KFK30349; AALP_AA7G249900.
DR   eggNOG; KOG1147; Eukaryota.
DR   OMA; YLVENAC; -.
DR   OrthoDB; 2733051at2759; -.
DR   Proteomes; UP000029120; Chromosome 7.
DR   GO; GO:0005737; C:cytoplasm; IEA:InterPro.
DR   GO; GO:0004812; F:aminoacyl-tRNA ligase activity; IEA:UniProtKB-KW.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0009791; P:post-embryonic development; IEA:UniProt.
DR   GO; GO:0048608; P:reproductive structure development; IEA:UniProt.
DR   GO; GO:0006418; P:tRNA aminoacylation for protein translation; IEA:InterPro.
DR   CDD; cd10289; GST_C_AaRS_like; 1.
DR   Gene3D; 1.20.1050.130; -; 1.
DR   Gene3D; 3.40.50.620; HUPs; 2.
DR   InterPro; IPR001412; aa-tRNA-synth_I_CS.
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; IPR010987; Glutathione-S-Trfase_C-like.
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   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; 2.
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   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:UP000029120}.
FT   DOMAIN          1..123
FT                   /note="GST C-terminal"
FT                   /evidence="ECO:0000259|PROSITE:PS50405"
SQ   SEQUENCE   731 AA;  82842 MW;  237D1DF6A7A97BB2 CRC64;
     MQQTVAASIQ QAMTGLINED NPFVDEWLDY ASVFSSGSEF GNACNLIDKY LESRTFLVGH
     SISIADVSLW SALAVTGQRW DSLRKSKKYP SLVRWFNSIL DEYSEVLATY VVKTDAEDKG
     KPLIDLPGAD FGKVRFRFAP EPSGYLHIGH AKAALLNKYF VDRYKGELIL RFDDTNPARE
     NNEFVDSLIK DVGTLGIKYK KVTYTSDYFP DLMKMAEKLM REGKAYVDDT PTEQMKEERK
     NGITHALRSS EYHDRNAQYS RVQDDMGMQR VQIYEFSRLN LVYTLLSKRK LLWFVNEGLV
     DGWDDPRFPT VQGIVRRGLK IEALIQFILE QGASKNLNLM EWDKIWSINK KIIDPVCPRH
     TAVIENRRVL LTLTNGPDEP FVRIIPKHKK FEGAGEKATT FTKRIWIEGG DASAISIDEE
     VTLMDWGNAI VKEIVKDSQG HVTALSGVLN LQGSVKTTKL KLTWLPDTNE LVNLTLIDFD
     YLITKKKLKE DEKVRAVVNP HTKKETLALG DSNMRNLKRE DVIQLERKGY FRSVVAVDLI
     SSVRVQLKLD SVYTEYSAQY LVENACPKKR QGTDLKLTVK DCLEFALKEG IPKAEDWPHL
     GSEVKPPSSY KPALVSMKGE VIEAENMEEA WDLSRYQPVA AKLHLFSPHI DLVGDGIYGG
     PSGEEAGYVG LRDVIIVDEQ MIQGKAIARF QFVKVAMGMM FVLAFPDDDD SRNVKLTFLL
     VDFVVPRLSS N
//
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