(data stored in SCRATCH zone)

SWISSPROT: E3J4S3_FRAIE

ID   E3J4S3_FRAIE            Unreviewed;       488 AA.
AC   E3J4S3;
DT   11-JAN-2011, integrated into UniProtKB/TrEMBL.
DT   11-JAN-2011, sequence version 1.
DT   08-MAY-2019, entry version 57.
DE   RecName: Full=Lysine--tRNA ligase {ECO:0000256|HAMAP-Rule:MF_00252};
DE            EC=6.1.1.6 {ECO:0000256|HAMAP-Rule:MF_00252};
DE   AltName: Full=Lysyl-tRNA synthetase {ECO:0000256|HAMAP-Rule:MF_00252};
DE            Short=LysRS {ECO:0000256|HAMAP-Rule:MF_00252};
GN   Name=lysS {ECO:0000256|HAMAP-Rule:MF_00252};
GN   OrderedLocusNames=FraEuI1c_0154 {ECO:0000313|EMBL:ADP78242.1};
OS   Frankia inefficax (strain DSM 45817 / CECT 9037 / EuI1c).
OC   Bacteria; Actinobacteria; Frankiales; Frankiaceae; Frankia.
OX   NCBI_TaxID=298654 {ECO:0000313|EMBL:ADP78242.1, ECO:0000313|Proteomes:UP000002484};
RN   [1] {ECO:0000313|EMBL:ADP78242.1, ECO:0000313|Proteomes:UP000002484}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 45817 / CECT 9037 / EuI1c
RC   {ECO:0000313|Proteomes:UP000002484};
RG   US DOE Joint Genome Institute;
RA   Lucas S., Copeland A., Lapidus A., Cheng J.-F., Bruce D., Goodwin L.,
RA   Pitluck S., Chertkov O., Detter J.C., Han C., Tapia R., Land M.,
RA   Hauser L., Jeffries C., Kyrpides N., Ivanova N., Mikhailova N.,
RA   Beauchemin N., Sen A., Sur S.A., Gtari M., Wall L., Tisa L., Woyke T.;
RT   "Complete sequence of Frankia sp. EuI1c.";
RL   Submitted (OCT-2010) to the EMBL/GenBank/DDBJ databases.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + L-lysine + tRNA(Lys) = AMP + diphosphate + L-lysyl-
CC         tRNA(Lys); Xref=Rhea:RHEA:20792, Rhea:RHEA-COMP:9696, Rhea:RHEA-
CC         COMP:9697, ChEBI:CHEBI:30616, ChEBI:CHEBI:32551,
CC         ChEBI:CHEBI:33019, ChEBI:CHEBI:78442, ChEBI:CHEBI:78529,
CC         ChEBI:CHEBI:456215; EC=6.1.1.6; Evidence={ECO:0000256|HAMAP-
CC         Rule:MF_00252, ECO:0000256|RuleBase:RU000336,
CC         ECO:0000256|SAAS:SAAS01119930};
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000256|HAMAP-
CC         Rule:MF_00252, ECO:0000256|RuleBase:RU000336};
CC       Note=Binds 3 Mg(2+) ions per subunit. {ECO:0000256|HAMAP-
CC       Rule:MF_00252, ECO:0000256|RuleBase:RU000336};
CC   -!- SUBUNIT: Homodimer. {ECO:0000256|HAMAP-Rule:MF_00252}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00252}.
CC   -!- SIMILARITY: Belongs to the class-II aminoacyl-tRNA synthetase
CC       family. {ECO:0000256|HAMAP-Rule:MF_00252,
CC       ECO:0000256|SAAS:SAAS00675054}.
CC   -!- CAUTION: Lacks conserved residue(s) required for the propagation
CC       of feature annotation. {ECO:0000256|HAMAP-Rule:MF_00252}.
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DR   EMBL; CP002299; ADP78242.1; -; Genomic_DNA.
DR   RefSeq; WP_013421365.1; NC_014666.1.
DR   STRING; 298654.FraEuI1c_0154; -.
DR   EnsemblBacteria; ADP78242; ADP78242; FraEuI1c_0154.
DR   KEGG; fri:FraEuI1c_0154; -.
DR   eggNOG; ENOG4105CRK; Bacteria.
DR   eggNOG; COG1190; LUCA.
DR   HOGENOM; HOG000236578; -.
DR   KO; K04567; -.
DR   OMA; EIFGEKC; -.
DR   OrthoDB; 63621at2; -.
DR   BioCyc; FSP298654:G1GOT-157-MONOMER; -.
DR   Proteomes; UP000002484; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0004824; F:lysine-tRNA ligase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0003676; F:nucleic acid binding; IEA:InterPro.
DR   GO; GO:0006430; P:lysyl-tRNA aminoacylation; IEA:UniProtKB-UniRule.
DR   HAMAP; MF_00252; Lys_tRNA_synth_class2; 1.
DR   InterPro; IPR004364; aa-tRNA-synt_II.
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.
DR   Pfam; PF00152; tRNA-synt_2; 1.
DR   Pfam; PF01336; tRNA_anti-codon; 1.
DR   PRINTS; PR00982; TRNASYNTHLYS.
DR   SUPFAM; SSF50249; SSF50249; 1.
DR   TIGRFAMs; TIGR00499; lysS_bact; 1.
DR   PROSITE; PS50862; AA_TRNA_LIGASE_II; 1.
PE   3: Inferred from homology;
DR   PRODOM; E3J4S3.
DR   SWISS-2DPAGE; E3J4S3.
KW   Aminoacyl-tRNA synthetase {ECO:0000256|HAMAP-Rule:MF_00252,
KW   ECO:0000256|SAAS:SAAS00222048, ECO:0000313|EMBL:ADP78242.1};
KW   ATP-binding {ECO:0000256|HAMAP-Rule:MF_00252,
KW   ECO:0000256|SAAS:SAAS00675071};
KW   Complete proteome {ECO:0000313|Proteomes:UP000002484};
KW   Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00252};
KW   Ligase {ECO:0000256|HAMAP-Rule:MF_00252,
KW   ECO:0000256|SAAS:SAAS00675072};
KW   Magnesium {ECO:0000256|HAMAP-Rule:MF_00252,
KW   ECO:0000256|RuleBase:RU000336};
KW   Metal-binding {ECO:0000256|HAMAP-Rule:MF_00252,
KW   ECO:0000256|RuleBase:RU000336};
KW   Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00252,
KW   ECO:0000256|SAAS:SAAS00675044};
KW   Protein biosynthesis {ECO:0000256|HAMAP-Rule:MF_00252,
KW   ECO:0000256|SAAS:SAAS00470543};
KW   Reference proteome {ECO:0000313|Proteomes:UP000002484}.
FT   DOMAIN      153    467       AA_TRNA_LIGASE_II. {ECO:0000259|PROSITE:
FT                                PS50862}.
FT   METAL       390    390       Magnesium 1. {ECO:0000256|HAMAP-Rule:
FT                                MF_00252}.
FT   METAL       390    390       Magnesium 2. {ECO:0000256|HAMAP-Rule:
FT                                MF_00252}.
SQ   SEQUENCE   488 AA;  54777 MW;  4711789CF8E2CB1C CRC64;
     MTADEPTVDG AARLPRSGYQ TDLTSADVQA APDGTPARVA GRLMLWRRMG GLVFGTIQDR
     AGRVQISLNR NELGEETYKE WHSSVKVGDF VGVTGVVFTT RKGERTVGAT DFAVLNKAVR
     ALPDKWHGIA DVETRYRRRY LDLLANPASR ERFQTRSRVI SRIRRFLDDA DFLEVETPVL
     TEAASGAAAR PFITRHNALG EDFYLRISPE TYLKRVVAGS FDRVYEIGRN FRNEGIDPSH
     LQEFTMLEWY AAYWDYRDNM RFVRELILAI LDDVIGSRTV TYEGTKLDFG ADWPVIDYRD
     AVESRTGVDL RVVRDFETLK TKCADLGLDV SKAASYAALV DLLYKKTVRP ELVQPCFLVG
     HPVELVPLAR RSDDDPTRLD MFQVVANGWE LVKAYSELVD PVDQRERLEE QADLRAAGDD
     ETMMLEEDFI EAMEYGMPPM SGLGLGIDRF IALITDAPTL RDVVLFPSMR GAKGPESTEP
     AQAAGPES
//

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