ID A0A0S1SM81_9BACT Unreviewed; 533 AA.
AC A0A0S1SM81; A0A0S1SFR3; A0A0S1SJI1; A0A0S1SRY6; A0A0S1STD4;
DT 17-FEB-2016, integrated into UniProtKB/TrEMBL.
DT 17-FEB-2016, sequence version 1.
DT 27-MAR-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 ORFNames=PeribacterD1_0003 {ECO:0000313|EMBL:ALM12708.1};
OS Candidatus Peribacter riflensis.
OC Bacteria; Candidatus Peregrinibacteria; Candidatus Peribacteria;
OC Candidatus Peribacterales; Candidatus Peribacteraceae; Peribacter.
OX NCBI_TaxID=1735162 {ECO:0000313|EMBL:ALM12708.1, ECO:0000313|Proteomes:UP000069135};
RN [1] {ECO:0000313|Proteomes:UP000069135}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Anantharaman K., Brown C.T., Burstein D., Castelle C.J., Probst A.J.,
RA Thomas B.C., Williams K.H., Banfield J.F.;
RT "Analysis of five complete genome sequences for members of the class
RT Peribacteria in the recently recognized Peregrinibacteria bacterial
RT phylum.";
RL Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:ALM12708.1, ECO:0000313|Proteomes:UP000069135}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=RIFOXYD1_FULL_PER-ii_59_16 {ECO:0000313|EMBL:ALM12708.1};
RX PubMed=26844018;
RA Anantharaman K., Brown C.T., Burstein D., Castelle C.J., Probst A.J.,
RA Thomas B.C., Williams K.H., Banfield J.F.;
RT "Analysis of five complete genome sequences for members of the class
RT Peribacteria in the recently recognized Peregrinibacteria bacterial
RT phylum.";
RL PeerJ 4:E1607-E1607(2016).
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; CP013065; ALM12708.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0S1SM81; -.
DR STRING; 1735162.PeribacterB2_0003; -.
DR KEGG; prf:PeribacterA2_0003; -.
DR Proteomes; UP000069135; 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: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; 1.10.10.770; -; 1.
DR Gene3D; 3.40.50.620; HUPs; 2.
DR HAMAP; MF_00177; Lys_tRNA_synth_class1; 1.
DR InterPro; IPR045462; aa-tRNA-synth_I_cd-bd.
DR InterPro; IPR020751; aa-tRNA-synth_I_codon-bd_sub2.
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; PF19269; Anticodon_2; 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.
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}.
FT DOMAIN 434..529
FT /note="Aminoacyl-tRNA synthetase class I anticodon-binding"
FT /evidence="ECO:0000259|Pfam:PF19269"
SQ SEQUENCE 533 AA; 60222 MW; E2438018051ED201 CRC64;
MQWVDSIVGE IEQRFAAEIK AGKPLILRDE KTLSGRVHVG SLRGIVIHGV LAQVLKEKGV
ACDFLFELND FDPMDELPAT LTNREEFRQY MGQPLFTVPS PDPKKAPNYP LVFGNELQEV
VKGLQIPITY YPLAPLYKEG KFNEVIRDAL DHATEIRTIY RAVSGSLKPE DWYPLQVICE
QCGKVGTTQV TGWDGKLVTY ACKPDLVKWA KGCGHSGTVS PFDGHAKLPW KVEWPAKWKV
MNVKIEGAGK DHSAAGGSRD IGRRICEEIF HYPEPLNIPY EFFNIAGKKM SASKGLGASA
KEVSDLLPPK ILKLLMIRKQ PNQPIDFDPE GVTIPQLFDE HDRLADYAFG RQEKPEPDFA
RTFTLTQTDF PKKPADLWHM RFTLVAFIVQ MPHLALPEEA EKAKGSALTE AEKSNLQERA
DYAKRWLKAL APAQFRFTFV QDADFAPEEL PALSAAQKQA FTMIHRQLKE TPWTGEEVHK
VLHAVKTELN MPPKEIFAPL YQLFFKRDDG PQMGWLLSTL PKEEVLKRIG LYS
//
