ID C1BA80_RHOOB Unreviewed; 503 AA.
AC C1BA80;
DT 26-MAY-2009, integrated into UniProtKB/TrEMBL.
DT 26-MAY-2009, sequence version 1.
DT 01-MAY-2013, entry version 36.
DE RecName: Full=Lysine--tRNA ligase;
DE EC=6.1.1.6;
DE AltName: Full=Lysyl-tRNA synthetase;
GN Name=lysS; OrderedLocusNames=ROP_43360;
OS Rhodococcus opacus (strain B4).
OC Bacteria; Actinobacteria; Actinobacteridae; Actinomycetales;
OC Corynebacterineae; Nocardiaceae; Rhodococcus.
OX NCBI_TaxID=632772;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=B4;
RA Takarada H., Sekine M., Hosoyama A., Yamada R., Fujisawa T., Omata S.,
RA Shimizu A., Tsukatani N., Tanikawa S., Fujita N., Harayama S.;
RT "Comparison of the complete genome sequences of Rhodococcus
RT erythropolis PR4 and Rhodococcus opacus B4.";
RL Submitted (MAR-2009) to the EMBL/GenBank/DDBJ databases.
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.
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DR EMBL; AP011115; BAH52583.1; -; Genomic_DNA.
DR RefSeq; YP_002781528.1; NC_012522.1.
DR STRING; 632772.ROP_43360; -.
DR EnsemblBacteria; BAH52583; BAH52583; ROP_43360.
DR GeneID; 7743056; -.
DR KEGG; rop:ROP_43360; -.
DR PATRIC; 23225991; VBIRhoOpa21106_4373.
DR eggNOG; COG1190; -.
DR HOGENOM; HOG000236578; -.
DR KO; K04567; -.
DR OMA; EHKLEQP; -.
DR ProtClustDB; PRK00484; -.
DR BioCyc; ROPA632772:GH0Q-6738-MONOMER; -.
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 Gene3D; 2.40.50.140; -; 1.
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-ligase_II.
DR InterPro; IPR018149; Lys-tRNA-synth_II_C.
DR InterPro; IPR012340; NA-bd_OB-fold.
DR InterPro; IPR004365; NA-bd_OB_tRNA-helicase.
DR PANTHER; PTHR22594; PTHR22594; 1.
DR PANTHER; PTHR22594:SF4; PTHR22594:SF4; 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.
PE 3: Inferred from homology;
KW Aminoacyl-tRNA synthetase; ATP-binding; Complete proteome; Cytoplasm;
KW Ligase; Magnesium; Metal-binding; Nucleotide-binding;
KW Protein biosynthesis.
FT METAL 413 413 Magnesium 1 (By similarity).
FT METAL 420 420 Magnesium 1 (By similarity).
FT METAL 420 420 Magnesium 2 (By similarity).
SQ SEQUENCE 503 AA; 55904 MW; 969BD270714761F0 CRC64;
MSEVAAQPVD DTPEQLRIRQ EKRERILAEG REAYPVSVAR THSLAEIRAK YPELEPDTAT
GDQVGIVGRV IFVRNTGKLC FATLQEGDGT QLQAMISLAA VGEDALASWK ADVDLGDFVF
VHGEVISSRR GELSVMADSW QIASKSLRPL PVAHKEMNEE SRVRQRYADL IVRPEARDNA
RKRVSVVREL RNALERRGFL EVETPMLQTV AGGAAARPFI THSNALDIDL YLRIAPELFL
KRCVVGGIEK VFEINRNFRN EGVDSTHSPE FAMLETYEAY GTYDDSAVMI RELVQEVAQA
AFGSQVVTLA DGTEYDLSGE WKTLEMYPSL SQAIGVDVTP DTTVEELLAL AEKVGLEVPK
DKGYGHGKLV EELWEHQCGD QLFEPTFVRD FPVETSPLTR DHRSKAGVTE KWDLYIRGFE
LATGYSELVD PVIQRERFVD QARLASAGDD EAMALDEEFL AAMEQGMPPT TGTGMGIDRL
LMALTGLGIR ETILFPIVRP SSR
//
