(data stored in ACNUC14830 zone)

HOGENOM: DESB2_1_PE101

ID   DESB2_1_PE101                        STANDARD;      PRT;   471 AA.
AC   DESB2_1_PE101; E1QDG1;
DT   00-JAN-0000 (Rel. 1, Created)
DT   00-JAN-0000 (Rel. 2, Last sequence update)
DT   00-JAN-0000 (Rel. 3, Last annotation update)
DE   RecName: Full=Glutamyl-tRNA synthetase; EC=6.1.1 17;AltName:
DE   Full=Glutamate--tRNA ligase; (DESB2_1.PE101).
GN   Name=gltX; OrderedLocusNames=Deba_0101;
OS   DESULFARCULUS BAARSII DSM 2075.
OC   Bacteria; Proteobacteria; Deltaproteobacteria; Desulfarculales;
OC   Desulfarculaceae; Desulfarculus.
OX   NCBI_TaxID=644282;
RN   [0]
RP   -.;
RG   -.;
RL   -.;
CC   -!- SEQ. DATA ORIGIN: Translated from the HOGENOM CDS DESB2_1.PE101.
CC       Desulfarculus baarsii DSM 2075 chromosome, complete genome.
CC       / IFO 0083) chromosome G, complete sequence.
CC   -!- ANNOTATIONS ORIGIN:E1QDG1_DESB2
CC   -!- FUNCTION: Catalyzes the attachment of glutamate to tRNA(Glu) in a
CC       two-step reaction: glutamate is first activated by ATP to form
CC       Glu-AMP and then transferred to the acceptor end of tRNA(Glu) (By
CC       similarity).
CC   -!- CATALYTIC ACTIVITY: ATP + L-glutamate + tRNA(Glu) = AMP +
CC       diphosphate + L-glutamyl-tRNA(Glu).
CC   -!- SUBUNIT: Monomer (By similarity).
CC   -!- SUBCELLULAR LOCATION: Cytoplasm (By similarity).
CC   -!- SIMILARITY: Belongs to the class-I aminoacyl-tRNA synthetase
CC       family.
CC   -!- GENE_FAMILY: HOG000252722 [ FAMILY / ALN / TREE ]
DR   UniProtKB/Swiss-Prot; E1QDG1; -.
DR   EMBL; CP002085; ADK83480.1; -; Genomic_DNA.
DR   RefSeq; YP_003806074.1; NC_014365.1.
DR   ProteinModelPortal; E1QDG1; -.
DR   GeneID; 9492536; -.
DR   GenomeReviews; CP002085_GR; Deba_0101.
DR   KEGG; dbr:Deba_0101; -.
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:EC.
DR   GO; GO:0006424; P:glutamyl-tRNA aminoacylation; IEA:InterPro.
DR   HAMAP; MF_00022_B; Glu_tRNA_synth_B; 1; -.
DR   InterPro; IPR008925; aa-tRNA-synth_I_codon-bd.
DR   InterPro; IPR020751; aa-tRNA-synth_I_codon-bd_sub2.
DR   InterPro; IPR001412; aa-tRNA-synth_I_CS.
DR   InterPro; IPR004527; Glu-tRNA-synth_Ib_bac/mito.
DR   InterPro; IPR000924; Glu/Gln-tRNA-synth_Ib.
DR   InterPro; IPR020061; Glu/Gln-tRNA-synth_Ib_a-bdl.
DR   InterPro; IPR020058; Glu/Gln-tRNA-synth_Ib_cat-dom.
DR   InterPro; IPR014729; Rossmann-like_a/b/a_fold.
DR   Gene3D; G3DSA:1.10.1160.10; Glu/Gln-tRNA-synth_Ic_a-bdl; 1.
DR   Gene3D; G3DSA:3.40.50.620; Rossmann-like_a/b/a_fold; 2.
DR   Gene3D; G3DSA:1.10.10.350; tRNA_synt_bd; 1.
DR   PANTHER; PTHR10119; Glu_tRNA-synt_1c; 1.
DR   Pfam; PF00749; tRNA-synt_1c; 1.
DR   PRINTS; PR00987; TRNASYNTHGLU.
DR   SUPFAM; SSF48163; tRNA-synt_bind; 1.
DR   TIGRFAMs; TIGR00464; GltX_bact; 1.
DR   PROSITE; PS00178; AA_TRNA_LIGASE_I; 1.
DR   HOGENOMDNA; DESB2_1.PE101; -.
KW   glutamyl-tRNA synthetase;
KW   Aminoacyl-tRNA synthetase; ATP-binding; Complete proteome; Cytoplasm;
KW   Ligase; Nucleotide-binding; Protein biosynthesis.
SQ   SEQUENCE   471 AA;  UNKNOWN MW;  UNKNOWN CRC64;
     MTQNNDNRPK VRTRFPPSPT GALHIGGGRT ALFNWLFARH HGGQFIMRLE DTDLQRSKPE
     HVTSILEAME WLGLDFDEGP YYQTKRFDRY KQVVEQMLQS GAAYWCHCSP ETLQAKREAA
     MASGAKPMYD GCCRGKGLGP APGAVVRFAG PRTGSTTFND MVKGPITFDH AELDDLIIQR
     SDGSPTYHLA VIVDDIDMEV THVIRGDDHV SNTPRQILLI RALGHLEPRY AHIPMILGQD
     KARLSKRHGA TAITDYREMG YLPEAMINAL ARLGWSHGDQ EIFSRQELIE LFDLDSVGRS
     AAVFDLDKLR SLNHKYIQKA DPQRLAQLVQ PFLAKLGLAA YDEAVLRKAI PELVQRTENL
     EQLAQWAQPY LVDQPEMDAK ARQKFLIGPE AAAILRQVRE LVAAGNVDDV AAMNEAFRAL
     AARTGQKLGA LAQPTRVALT GRTASPGIFE VMAILGRQAV LTRLDQAIAG A
//

If you have problems or comments...

PBIL Back to PBIL home page