(data stored in SCRATCH zone)

HOGENOM: FLAJ1_1_PE1001

ID   FLAJ1_1_PE1001                       STANDARD;      PRT;   501 AA.
AC   FLAJ1_1_PE1001; A5FL73;
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; Short=GluRS; (FLAJ1_1.PE1001).
GN   Name=gltX; OrderedLocusNames=Fjoh_1006;
OS   FLAVOBACTERIUM JOHNSONIAE UW101.
OC   Bacteria; Bacteroidetes; Flavobacteria; Flavobacteriales;
OC   Flavobacteriaceae; Flavobacterium.
OX   NCBI_TaxID=376686;
RN   [0]
RP   -.;
RG   -.;
RL   -.;
CC   -!- SEQ. DATA ORIGIN: Translated from the HOGENOM CDS FLAJ1_1.PE1001.
CC       Flavobacterium johnsoniae UW101, complete genome.
CC       annotated by Ensembl
CC   -!- ANNOTATIONS ORIGIN:SYE_FLAJ1
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.
CC   -!- SIMILARITY: Belongs to the class-I aminoacyl-tRNA synthetase
CC       family.
CC   -!- GENE_FAMILY: HOG000252720 [ FAMILY / ALN / TREE ]
DR   UniProtKB/Swiss-Prot; A5FL73; -.
DR   EMBL; CP000685; ABQ04039.1; -; Genomic_DNA.
DR   RefSeq; YP_001193358.1; NC_009441.1.
DR   ProteinModelPortal; A5FL73; -.
DR   STRING; A5FL73; -.
DR   GeneID; 5090597; -.
DR   GenomeReviews; CP000685_GR; Fjoh_1006.
DR   KEGG; fjo:Fjoh_1006; -.
DR   eggNOG; COG0008; -.
DR   OMA; MAHIPLI; -.
DR   ProtClustDB; PRK01406; -.
DR   BioCyc; FJOH376686:FJOH_1006-MON; -.
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; FLAJ1_1.PE1001; -.
KW   Aminoacyl-tRNA synthetase; ATP-binding; Complete proteome; Cytoplasm;
KW   Ligase; Nucleotide-binding; Protein biosynthesis.
SQ   SEQUENCE   501 AA;  UNKNOWN MW;  UNKNOWN CRC64;
     MSKQVRVRFA PSPTGPLHIG GVRTALFNYL FAKKHNGVFY LRIEDTDQTR FVPGAEAYIM
     EALEWLGISP EETVGKNEKF GPYRQSDRKD LYQKYADQLI NSGWAYYAFD TPEALDAHRK
     QHEAEGKTFI YNHHNREKLD TSLVISAEET AKRIANGEHY VIRFKTPVDE TLHLKDIIRG
     DVKFETNLLD DKVLFKSDGM PTYHLANIVD DHLMETSHVI RGEEWLPSMP LHVLLYRAFG
     WDAPEFAHLP LILKPVGNGK LSKRDGDKLG FPVFPLEWKT EEGVSSGYRE KGFFPEAVVN
     FLALLGWNDG TDKELFSLEE LVEAFDLNRV HKAGAKFDPE KNKWFNHQYL IKQNDADLAK
     SFSTILEEKG FSTPLEVTTR IVSLIKERAH FVSEFWDLTD FFFQAPSSYD EKASKNWKEE
     TPALMKELIS VLENIEDFTS ANIETIVKEW LTKNEIGMGK VMQPFRLSLV GALKGPHLFD
     IVEIIGKEET VSRIQKAISA L
//

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