ID F4GY48_CELFA Unreviewed; 511 AA.
AC F4GY48;
DT 28-JUN-2011, integrated into UniProtKB/TrEMBL.
DT 28-JUN-2011, sequence version 1.
DT 03-APR-2013, entry version 14.
DE RecName: Full=Lysine--tRNA ligase;
DE EC=6.1.1.6;
DE AltName: Full=Lysyl-tRNA synthetase;
GN Name=lysS; OrderedLocusNames=Celf_0576;
OS Cellulomonas fimi (strain ATCC 484 / DSM 20113 / JCM 1341 / NBRC 15513
OS / NCIMB 8980 / NCTC 7547).
OC Bacteria; Actinobacteria; Actinobacteridae; Actinomycetales;
OC Micrococcineae; Cellulomonadaceae; Cellulomonas.
OX NCBI_TaxID=590998;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 484 / DSM 20113 / JCM 1341 / NBRC 15513 / NCIMB 8980 /
RC NCTC 7547;
RG US DOE Joint Genome Institute;
RA Lucas S., Han J., Lapidus A., Cheng J.-F., Goodwin L., Pitluck S.,
RA Peters L., Chertkov O., Detter J.C., Han C., Tapia R., Land M.,
RA Hauser L., Kyrpides N., Ivanova N., Ovchinnikova G., Pagani I.,
RA Mead D., Brumm P., Woyke T.;
RT "Complete sequence of Cellulomonas fimi ATCC 484.";
RL Submitted (APR-2011) 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; CP002666; AEE44716.1; -; Genomic_DNA.
DR RefSeq; YP_004452103.1; NC_015514.1.
DR EnsemblBacteria; AEE44716; AEE44716; Celf_0576.
DR GeneID; 10591340; -.
DR KEGG; cfi:Celf_0576; -.
DR PATRIC; 54612016; VBICelFim18861_0573.
DR KO; K04567; -.
DR BioCyc; CFIM590998:GJFK-580-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 422 422 Magnesium 1 (By similarity).
FT METAL 429 429 Magnesium 1 (By similarity).
FT METAL 429 429 Magnesium 2 (By similarity).
SQ SEQUENCE 511 AA; 56709 MW; C352FFBA2FE78409 CRC64;
MTAAPDETIA PAPSAPADDT PEQIQVRRAK RERLLAEGTD AYPVGLPRTH TIAQVRAEHP
DLEPGTETQD EVGVAGRVVF LRNTGKLCFA MLQDGEGNRL QAMLSLREVG EERLAAFKTD
VDLGDHVFVH GRVVASRTGE LSVFADAWAM AAKAIRPLPN VYEGAELSEE ARVRQRYVDL
IVNQRSRDMV RTRAAVLRSV RDNLHRRGFL EVETPMLQVR PEGAAARQFE THMNAFDIPL
FLRIAPELFL KRAAVGGVER VFEINRNFRN EGVDATHSPE FAMLEAYEAY GDYDTIAELT
QDLVQTAARD AFGSTTVTLA DGSEYDLGGE WERLPMYDSL SAALGEEITH DTTDEVLLAL
LDKAGVELAP GQRNHGKMVE ELWEHHVGHH LTAPTFVRDF PVETSPLVRD HRHKAGLVEK
WDLYVRGMEL ATGYSELVDP VIQRQRFEAQ ALLAARGDDD AMRIDEDFLT AMEFAMPPSG
GMGMGIDRLL IALTGLGIRE TILFPLVKPQ A
//
