ID   A0A424NMZ4_9FLAO        Unreviewed;       521 AA.
AC   A0A424NMZ4;
DT   08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT   08-MAY-2019, sequence version 1.
DT   03-AUG-2022, entry version 10.
DE   RecName: Full=Lysine--tRNA ligase {ECO:0000256|HAMAP-Rule:MF_00177};
DE            EC=6.1.1.6 {ECO:0000256|HAMAP-Rule:MF_00177};
DE   AltName: Full=Lysyl-tRNA synthetase {ECO:0000256|HAMAP-Rule:MF_00177};
DE            Short=LysRS {ECO:0000256|HAMAP-Rule:MF_00177};
GN   Name=lysS {ECO:0000256|HAMAP-Rule:MF_00177};
GN   ORFNames=CBD95_005050 {ECO:0000313|EMBL:RPG56091.1};
OS   Flavobacteriales bacterium TMED235.
OC   Bacteria; Bacteroidetes; Flavobacteriia; Flavobacteriales.
OX   NCBI_TaxID=1986726 {ECO:0000313|EMBL:RPG56091.1, ECO:0000313|Proteomes:UP000196715};
RN   [1] {ECO:0000313|EMBL:RPG56091.1, ECO:0000313|Proteomes:UP000196715}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=TMED235 {ECO:0000313|EMBL:RPG56091.1};
RX   PubMed=28713657; DOI=10.7717/peerj.3558;
RA   Tully B.J., Sachdeva R., Graham E.D., Heidelberg J.F.;
RT   "290 metagenome-assembled genomes from the Mediterranean Sea: a resource
RT   for marine microbiology.";
RL   PeerJ 5:e3558-e3558(2017).
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, ChEBI:CHEBI:33019,
CC         ChEBI:CHEBI:78442, ChEBI:CHEBI:78529, ChEBI:CHEBI:456215; EC=6.1.1.6;
CC         Evidence={ECO:0000256|ARBA:ARBA00000204, ECO:0000256|HAMAP-
CC         Rule:MF_00177};
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00177}.
CC   -!- SIMILARITY: Belongs to the class-I aminoacyl-tRNA synthetase family.
CC       {ECO:0000256|ARBA:ARBA00005594, ECO:0000256|HAMAP-Rule:MF_00177}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:RPG56091.1}.
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DR   EMBL; NHKG02000077; RPG56091.1; -; Genomic_DNA.
DR   Proteomes; UP000196715; Unassembled WGS sequence.
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:0000049; F:tRNA binding; IEA:InterPro.
DR   GO; GO:0006430; P:lysyl-tRNA aminoacylation; IEA:UniProtKB-UniRule.
DR   Gene3D; 1.10.10.350; -; 1.
DR   Gene3D; 3.40.50.620; -; 2.
DR   HAMAP; MF_00177; Lys_tRNA_synth_class1; 1.
DR   InterPro; IPR020751; aa-tRNA-synth_I_codon-bd_sub2.
DR   InterPro; IPR001412; aa-tRNA-synth_I_CS.
DR   InterPro; IPR008925; aa_tRNA-synth_I_cd-bd_sf.
DR   InterPro; IPR002904; Lys-tRNA-ligase.
DR   InterPro; IPR014729; Rossmann-like_a/b/a_fold.
DR   PANTHER; PTHR37940; PTHR37940; 1.
DR   Pfam; PF01921; tRNA-synt_1f; 1.
DR   SUPFAM; SSF48163; SSF48163; 1.
DR   TIGRFAMs; TIGR00467; lysS_arch; 1.
DR   PROSITE; PS00178; AA_TRNA_LIGASE_I; 1.
PE   3: Inferred from homology;
KW   Aminoacyl-tRNA synthetase {ECO:0000256|ARBA:ARBA00023146,
KW   ECO:0000256|HAMAP-Rule:MF_00177};
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|HAMAP-
KW   Rule:MF_00177}; Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00177};
KW   Ligase {ECO:0000256|ARBA:ARBA00022598, ECO:0000256|HAMAP-Rule:MF_00177};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|HAMAP-
KW   Rule:MF_00177};
KW   Protein biosynthesis {ECO:0000256|ARBA:ARBA00022917, ECO:0000256|HAMAP-
KW   Rule:MF_00177}.
FT   MOTIF           44..52
FT                   /note="'HIGH' region"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00177"
FT   MOTIF           289..293
FT                   /note="'KMSKS' region"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00177"
FT   BINDING         292
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00177"
SQ   SEQUENCE   521 AA;  60585 MW;  0FD31FB592644C57 CRC64;
     MVIDKLNIEK TNAWPFVEAK KILKQRKKNI EKKGKIILQT GYGPSGLPHI GTFGEVARTT
     MVVNALNHIT DIPKEIITFS DDMDGLRKIP ENIPNKNILE KHLHKPLTVI PDPFKKFNSF
     GEHNNEMLKK FLNEFNFKYN FKSSSNLYKS GAFNEPLKII LKNYQGIMNI ILPTLGKERQ
     KTYSPFLPIC PDTGVVLEIP IKEIDEKNSK IIFDNNGKEL EKSILDGNCK LQWKVDWAMR
     WYSLDVDFEM YGKDLIESAI LSTKIIKLLG KTNPEGFAYE LFLDEKGEKI SKSKGNGITI
     DEWLNFASPE SLSLFMYQNP KRAKKLYNDV VPKAVDEYLE CIEKEKNQNE IQKLLNPAWH
     VHNGNVPKEK IIMSFSMLLN LVQTSNANSK ELLWKFVKKY KSEINEKEYP IFDNLLEYAI
     KYFNQIVKQN KKFKNPSDQE RRALNSLIEV LENCNDKMEP EEIQTKIYSV GKENGYEKNL
     RDWFKLIYEV IFGDENGPRM GYFISFFGVQ ETKKLIIEKL K
//