(data stored in ACNUC7421 zone)

HOGENOM: ACIS3_1_PE100

ID   ACIS3_1_PE100                        STANDARD;      PRT;   498 AA.
AC   ACIS3_1_PE100; D9PZM1;
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=Lysyl-tRNA synthetase; EC=6.1.1 6;AltName:
DE   Full=Lysine--tRNA ligase; (ACIS3_1.PE100).
GN   Name=lysS; OrderedLocusNames=ASAC_0101;
OS   ACIDILOBUS SACCHAROVORANS 345-15.
OC   Archaea; Crenarchaeota; Thermoprotei; Acidilobales; Acidilobaceae;
OC   Acidilobus.
OX   NCBI_TaxID=666510;
RN   [0]
RP   -.;
RG   -.;
RL   -.;
CC   -!- SEQ. DATA ORIGIN: Translated from the HOGENOM CDS ACIS3_1.PE100.
CC       Acidilobus saccharovorans 345-15 chromosome, complete genome.
CC       sequence.
CC   -!- ANNOTATIONS ORIGIN:D9PZM1_ACIS3
CC   -!- CATALYTIC ACTIVITY: ATP + L-lysine + tRNA(Lys) = AMP + diphosphate
CC       + L-lysyl-tRNA(Lys).
CC   -!- COFACTOR: Binds 3 magnesium ions per subunit (By similarity).
CC   -!- SUBUNIT: Homodimer (By similarity).
CC   -!- SUBCELLULAR LOCATION: Cytoplasm (By similarity).
CC   -!- SIMILARITY: Belongs to the class-II aminoacyl-tRNA synthetase
CC       family.
CC   -!- GENE_FAMILY: HOG000236578 [ FAMILY / ALN / TREE ]
DR   UniProtKB/Swiss-Prot; D9PZM1; -.
DR   EMBL; CP001742; ADL18509.1; -; Genomic_DNA.
DR   RefSeq; YP_003815540.1; NC_014374.1.
DR   GeneID; 9498314; -.
DR   GenomeReviews; CP001742_GR; ASAC_0101.
DR   KEGG; asc:ASAC_0101; -.
DR   OMA; NDEASEM; -.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0005524; F:ATP binding; IEA:HAMAP.
DR   GO; GO:0004824; F:lysine-tRNA ligase activity; IEA:HAMAP.
DR   GO; GO:0000287; F:magnesium ion binding; IEA:HAMAP.
DR   GO; GO:0003676; F:nucleic acid binding; IEA:InterPro.
DR   GO; GO:0006430; P:lysyl-tRNA aminoacylation; IEA:HAMAP.
DR   HAMAP; MF_00252; Lys_tRNA_synth_class2; 1; -.
DR   InterPro; IPR004364; aa-tRNA-synt_II.
DR   InterPro; IPR018150; aa-tRNA-synt_II-like.
DR   InterPro; IPR006195; aa-tRNA-synth_II.
DR   InterPro; IPR002313; Lys-tRNA-synth_II.
DR   InterPro; IPR018149; Lys-tRNA-synth_II_C.
DR   InterPro; IPR012340; NA-bd_OB-fold.
DR   InterPro; IPR016027; NA-bd_OB-fold-like.
DR   InterPro; IPR004365; NA-bd_OB_tRNA-helicase.
DR   Gene3D; G3DSA:2.40.50.140; OB_NA_bd_sub; 1.
DR   PANTHER; PTHR22594; aa-tRNA-synt_II; 1.
DR   Pfam; PF00152; tRNA-synt_2; 1.
DR   Pfam; PF01336; tRNA_anti; 1.
DR   PRINTS; PR00982; TRNASYNTHLYS.
DR   SUPFAM; SSF50249; Nucleic_acid_OB; 1.
DR   TIGRFAMs; TIGR00499; LysS_bact; 1.
DR   PROSITE; PS50862; AA_TRNA_LIGASE_II; 1.
DR   HOGENOMDNA; ACIS3_1.PE100; -.
KW   lysyl-tRNA synthetase (LysS);
KW   Aminoacyl-tRNA synthetase; ATP-binding; Complete proteome; Cytoplasm;
KW   Ligase; Magnesium; Metal-binding; Nucleotide-binding;
KW   Protein biosynthesis.
SQ   SEQUENCE   498 AA;  UNKNOWN MW;  UNKNOWN CRC64;
     MSVEWDKERL KLLEELRSKG VNPYPHKYPI THTIRQIKDL AASRGDRPHE PFLRDISTAG
     RVANIRRHGK ASFVDIFDEG ERLQLYLRVN ELGDRYKEFL YYVGRGDIIG VRGDLFYTMK
     GELSLLVKDY QLLAKALIEP PDWTKLSPEF RYAHRYVDFL YNDQARRAME VRFNTIKEIR
     QYLYSKGFVE VETPVLQPVY GGALAKPFMT HVNALDEDWY LRISLELYLK RFIVGGFDKV
     FEIGKVFRNE DIDVTHNPEF TMMELYWAYA DYNDIMDLTE DMIRTVAAKV LGTTQLRIPM
     PDGSVAEVDV GQRFRRETMF DLLSEALGKN IEEVSDDEMK RMLDQMGLVP RGGVYSRGLM
     VEKLFDKLVT PKLIQPTFVL DYPIETTPLC KPHRSKPGLV ERFELYVAGV ELANAYTELN
     DPVLQDRLFK EEQEMRKRGD LEAHPYDVDF VRALSYGMPP TGGLGVGIDR LVMMFTGVSS
     IKEVLPFPMV SAKLVQGG
//

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