ID   SYK_ANAVT               Reviewed;         561 AA.
AC   Q3M8C8;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   25-OCT-2005, sequence version 1.
DT   16-JUN-2009, entry version 29.
DE   RecName: Full=Lysyl-tRNA synthetase;
DE            EC=6.1.1.6;
DE   AltName: Full=Lysine--tRNA ligase;
DE            Short=LysRS;
GN   Name=lysS; OrderedLocusNames=Ava_3150;
OS   Anabaena variabilis (strain ATCC 29413 / PCC 7937).
OC   Bacteria; Cyanobacteria; Nostocales; Nostocaceae; Anabaena.
OX   NCBI_TaxID=240292;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina T.,
RA   Hammon N., Israni S., Pitluck S., Saunders E.H., Schmutz J.,
RA   Larimer F., Land M., Kyrpides N., Mavrommatis K., Richardson P.;
RT   "Complete sequence of Anabaena variabilis ATCC 29413.";
RL   Submitted (SEP-2005) 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.
CC   -!- SIMILARITY: Belongs to the class-II aminoacyl-tRNA synthetase
CC       family.
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DR   EMBL; CP000117; ABA22758.1; -; Genomic_DNA.
DR   RefSeq; YP_323653.1; -.
DR   GeneID; 3680784; -.
DR   GenomeReviews; CP000117_GR; Ava_3150.
DR   KEGG; ava:Ava_3150; -.
DR   NMPDR; fig|240292.3.peg.3155; -.
DR   HOGENOM; Q3M8C8; -.
DR   OMA; Q3M8C8; ITNSASI.
DR   BioCyc; AVAR240292:AVA_3150-MON; -.
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; -; 1.
DR   InterPro; IPR004364; aa-tRNA-synt_II.
DR   InterPro; IPR018150; aa-tRNA-synt_II-like.
DR   InterPro; IPR006195; aa-tRNA-synth_II_cons-reg.
DR   InterPro; IPR002313; Lys-tRNA-synth_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   Gene3D; G3DSA:2.40.50.140; OB_NA_bd_sub; 1.
DR   PANTHER; PTHR22594; aa-tRNA-synt_II; 1.
DR   PANTHER; PTHR22594:SF4; tRNA-synt_lys_2; 1.
DR   Pfam; PF00152; tRNA-synt_2; 1.
DR   Pfam; PF01336; tRNA_anti; 1.
DR   PRINTS; PR00982; TRNASYNTHLYS.
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   CHAIN         1    561       Lysyl-tRNA synthetase.
FT                                /FTId=PRO_1000012838.
FT   METAL       409    409       Magnesium 1 (By similarity).
FT   METAL       416    416       Magnesium 1 (By similarity).
FT   METAL       416    416       Magnesium 2 (By similarity).
SQ   SEQUENCE   561 AA;  63747 MW;  C934A42ECCFA51EE CRC64;
     MSEEDIRAAR LEKVEQLKQL GTNPYAYRWE STHHAAQLQE KFADLTSGEE VDTEVAIAGR
     IMARRVFGKL AFFTLEDETG TIQLYLEKNR IQESMAETDA DAFNHLKQLT DVGDILGAKG
     TIKRTEKGEL SIYVKEYTIL TKSLLPLPDK WHGLTDVAKR YRQRYVDLIV NPEVRQTFRR
     RAQITAGIRR YLEQRDFLEI ETPVLQSETG GADARPFITY HNTLEMELYL RIATELHLKR
     LIVGGFEKVF ELGRVFRNEG ISTRHNPEFT SIEIYQAYAD YNDMMALTEG IITTVAQDVL
     GTLQITYQGE TVDLTPPWRR VTMHDLVKEY TGLDFHSFQT LEEAKSASKN AGIPGVDEAQ
     TIGKILNLAF EEKVEANLIQ PTFVIDYPVE ISPLAKPHRS QPGLVERFEL FIVGRETANS
     FSELTDPIDQ RERLEAQAAK KAAGDLEAQG VDEDFLTALE YGMPPTGGLG IGIDRLVMLL
     TDSASIRDVI AFPLLKPEGS FIKEYRYEST TQTLTMEFDS GSVYEYFKVP LTVKEELDNA
     PSKGQYFHKF IKGKFKYEQL S
//