ID A0A160VU13_9EURY Unreviewed; 523 AA.
AC A0A160VU13;
DT 06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT 06-JUL-2016, sequence version 1.
DT 24-JAN-2024, entry version 39.
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=A3L04_01780 {ECO:0000313|EMBL:ASJ15891.1}, CHITON_0352
GN {ECO:0000313|EMBL:CUX77131.1};
OS Thermococcus chitonophagus.
OC Archaea; Euryarchaeota; Thermococci; Thermococcales; Thermococcaceae;
OC Thermococcus.
OX NCBI_TaxID=54262 {ECO:0000313|EMBL:CUX77131.1, ECO:0000313|Proteomes:UP000093069};
RN [1] {ECO:0000313|Proteomes:UP000093069}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Vorgias C.E.;
RL Submitted (JAN-2016) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:CUX77131.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=1 {ECO:0000313|EMBL:CUX77131.1};
RA Oliw E.H.;
RL Submitted (JAN-2016) to the EMBL/GenBank/DDBJ databases.
RN [3] {ECO:0000313|EMBL:ASJ15891.1, ECO:0000313|Proteomes:UP000250189}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=GC74 {ECO:0000313|EMBL:ASJ15891.1,
RC ECO:0000313|Proteomes:UP000250189};
RA Oger P.M.;
RT "Complete genome sequence of Thermococcus chitonophagus type strain GC74.";
RL Submitted (APR-2016) 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; CP015193; ASJ15891.1; -; Genomic_DNA.
DR EMBL; LN999010; CUX77131.1; -; Genomic_DNA.
DR RefSeq; WP_068576177.1; NZ_LN999010.1.
DR AlphaFoldDB; A0A160VU13; -.
DR STRING; 54262.CHITON_0352; -.
DR GeneID; 33321263; -.
DR KEGG; tch:CHITON_0352; -.
DR OrthoDB; 6838at2157; -.
DR Proteomes; UP000093069; Chromosome i.
DR Proteomes; UP000250189; 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 CDD; cd00674; LysRS_core_class_I; 1.
DR Gene3D; 1.10.10.350; -; 1.
DR Gene3D; 1.10.10.770; -; 1.
DR Gene3D; 3.40.50.620; HUPs; 2.
DR Gene3D; 6.10.20.10; Lysine tRNA ligase, stem contact fold domain; 1.
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; IPR001412; aa-tRNA-synth_I_CS.
DR InterPro; IPR008925; aa_tRNA-synth_I_cd-bd_sf.
DR InterPro; IPR002904; Lys-tRNA-ligase.
DR InterPro; IPR042078; Lys-tRNA-ligase_SC_fold.
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.
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}.
FT DOMAIN 442..520
FT /note="Aminoacyl-tRNA synthetase class I anticodon-binding"
FT /evidence="ECO:0000259|Pfam:PF19269"
FT MOTIF 30..38
FT /note="'HIGH' region"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00177"
FT MOTIF 279..283
FT /note="'KMSKS' region"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00177"
SQ SEQUENCE 523 AA; 61371 MW; 19751DB992FE00BA CRC64;
MVHWADHMAE KIIRERGEKE LYVVESGITP SGYVHIGNFR ELFTAYIVGH ALRDRGYKVR
HIHMWDDYDR FRKVPKNVPQ EWKEYLGMPV REVPDPWGCH DSYAEHFMDL FESEVEKLGM
EVDFLYASEL YKKGEYSEEI RKAFENRGKI MAILNKYREI AKQPPLPENW WPAMVYCPEH
RKESEIIEWD GEWKVKFRCP EGHEGWTDIR DGNVKLRWRV DWPMRWAHFG VDFEPAGKDH
LAAGSSYDTG KDIIKKVYGK EAPLTLMYEF VGIKGQKGKM SGSKGNVILL SDLYEVLEPG
LVRFIYARHR PNKEIKIDLG LGLLNLYDEF DKVERIYFGV EKGKGDVEEL KRTYELSMPK
KPERLIAQAP FRFLAVLVQL PHMTEEKIIS TLISQGHVPK ALDYQDLERI KLRIKLAKNW
VEKYAPDDVK FVILDKPPEI EIPEEIREAM LEVAQWLEGR EAFTIDELNN VLYDVAKKRG
IPSKSWFSTL YKVFIGRERG PRLASFLASL DRKFVIRRLR LEA
//
