ID A0A0P1HFZ7_9RHOB Unreviewed; 545 AA.
AC A0A0P1HFZ7;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 24-JAN-2024, entry version 35.
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 ECO:0000313|EMBL:CUH89559.1};
GN ORFNames=PH5382_03506 {ECO:0000313|EMBL:CUH89559.1};
OS Phaeobacter sp. CECT 5382.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC Roseobacteraceae; Phaeobacter.
OX NCBI_TaxID=1712645 {ECO:0000313|EMBL:CUH89559.1, ECO:0000313|Proteomes:UP000050782};
RN [1] {ECO:0000313|EMBL:CUH89559.1, ECO:0000313|Proteomes:UP000050782}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CECT 5382 {ECO:0000313|EMBL:CUH89559.1,
RC ECO:0000313|Proteomes:UP000050782};
RG Swine Surveillance;
RL Submitted (SEP-2015) 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, 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|ARBA:ARBA00004496,
CC 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: Lacks conserved residue(s) required for the propagation of
CC feature annotation. {ECO:0000256|HAMAP-Rule:MF_00177}.
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DR EMBL; CYSG01000023; CUH89559.1; -; Genomic_DNA.
DR RefSeq; WP_058335652.1; NZ_CYSG01000023.1.
DR AlphaFoldDB; A0A0P1HFZ7; -.
DR STRING; 1712645.PH5382_03506; -.
DR OrthoDB; 9803151at2; -.
DR Proteomes; UP000050782; 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; HUPs; 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 NCBIfam; TIGR00467; lysS_arch; 1.
DR PANTHER; PTHR37940; LYSINE--TRNA LIGASE; 1.
DR PANTHER; PTHR37940:SF1; LYSINE--TRNA LIGASE; 1.
DR Pfam; PF01921; tRNA-synt_1f; 1.
DR SUPFAM; SSF48163; An anticodon-binding domain of class I aminoacyl-tRNA synthetases; 1.
DR SUPFAM; SSF52374; Nucleotidylyl transferase; 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};
KW Cytoplasm {ECO:0000256|ARBA:ARBA00022490, 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}; Reference proteome {ECO:0000313|Proteomes:UP000050782}.
FT MOTIF 44..52
FT /note="'HIGH' region"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00177"
FT BINDING 293
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00177"
SQ SEQUENCE 545 AA; 61271 MW; 983C0011A5CDAA0C CRC64;
MFELRDTALK SKAWPFEEAR RVLKRYAKGA PEKGYVLFET GYGPSGLPHI GTFGEVARTT
MIKTAFEVIS DIPTKLICFS DDLDGMRKVP GNVPNPESLT EHLQKPLTSV PDPFGTHESF
GHHNNAMLRR FLDTFGFEYE FYSATEFYGS GQFDEVLKRA VEKYDEIMEV MLASLREERR
QTYSIFLPFH PETGRVLYVP MKKVDAENHT ITFDDEDGKE WTLPVTGGNV KLQWKPDFGA
RWAALEVDFE MYGKDHSTNT PIYDKICRIL GHRAPDHFTY ELFLDANGQK ISKTSGNGIS
IDEWLTYASS ESLSYFMYLK PKTAKRMHFD VIPKAVDEYH QQLRAYATQD LKAQLNNPVW
HIHGGDVPQS DMVVPFSMLL NLASASSAED KATMWGFINK YAPDATPESN PTMDQAAGFA
VAYFNDYVKP TKVFRAPSDQ ERTALQDLAD ALKSPEAALA AIAKKNEIVG KDDTLPEANF
ADEEFLQSVV FAIGKIHGFE PLRDWFTAIY EVLLGASQGP RFGGFIALYG VAETIALIEK
ALAAE
//
