ID A0A0V1D2B6_TRIBR Unreviewed; 591 AA.
AC A0A0V1D2B6;
DT 16-MAR-2016, integrated into UniProtKB/TrEMBL.
DT 16-MAR-2016, sequence version 1.
DT 27-MAR-2024, entry version 32.
DE RecName: Full=Lysine--tRNA ligase {ECO:0000256|ARBA:ARBA00015745, ECO:0000256|RuleBase:RU003748};
DE EC=6.1.1.6 {ECO:0000256|ARBA:ARBA00013166, ECO:0000256|RuleBase:RU003748};
DE AltName: Full=Lysyl-tRNA synthetase {ECO:0000256|ARBA:ARBA00030563, ECO:0000256|RuleBase:RU003748};
GN Name=Kars {ECO:0000313|EMBL:KRY55658.1};
GN ORFNames=T03_16932 {ECO:0000313|EMBL:KRY55658.1};
OS Trichinella britovi (Parasitic roundworm).
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Enoplea; Dorylaimia;
OC Trichinellida; Trichinellidae; Trichinella.
OX NCBI_TaxID=45882 {ECO:0000313|EMBL:KRY55658.1, ECO:0000313|Proteomes:UP000054653};
RN [1] {ECO:0000313|EMBL:KRY55658.1, ECO:0000313|Proteomes:UP000054653}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ISS120 {ECO:0000313|EMBL:KRY55658.1};
RA Korhonen P.K., Edoardo P., Giuseppe L.R., Gasser R.B.;
RT "Evolution of Trichinella species and genotypes.";
RL Submitted (JAN-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,
CC ECO:0000256|RuleBase:RU003748};
CC -!- SIMILARITY: Belongs to the class-II aminoacyl-tRNA synthetase family.
CC {ECO:0000256|ARBA:ARBA00008226}.
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:KRY55658.1}.
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DR EMBL; JYDI01000052; KRY55658.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0V1D2B6; -.
DR Proteomes; UP000054653; Unassembled WGS sequence.
DR GO; GO:0005737; C:cytoplasm; IEA:InterPro.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0004824; F:lysine-tRNA ligase activity; IEA:UniProtKB-EC.
DR GO; GO:0003676; F:nucleic acid binding; IEA:InterPro.
DR GO; GO:0006430; P:lysyl-tRNA aminoacylation; IEA:InterPro.
DR CDD; cd00775; LysRS_core; 1.
DR CDD; cd04322; LysRS_N; 1.
DR Gene3D; 2.40.50.140; Nucleic acid-binding proteins; 1.
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; IPR045864; aa-tRNA-synth_II/BPL/LPL.
DR InterPro; IPR002313; Lys-tRNA-ligase_II.
DR InterPro; IPR034762; Lys-tRNA-ligase_II_bac/euk.
DR InterPro; IPR044136; Lys-tRNA-ligase_II_N.
DR InterPro; IPR018149; Lys-tRNA-synth_II_C.
DR InterPro; IPR012340; NA-bd_OB-fold.
DR InterPro; IPR004365; NA-bd_OB_tRNA.
DR NCBIfam; TIGR00499; lysS_bact; 1.
DR PANTHER; PTHR42918:SF9; LYSINE--TRNA LIGASE; 1.
DR PANTHER; PTHR42918; LYSYL-TRNA SYNTHETASE; 1.
DR Pfam; PF00152; tRNA-synt_2; 1.
DR Pfam; PF01336; tRNA_anti-codon; 1.
DR PIRSF; PIRSF039101; LysRS2; 1.
DR PRINTS; PR00982; TRNASYNTHLYS.
DR SUPFAM; SSF55681; Class II aaRS and biotin synthetases; 1.
DR SUPFAM; SSF50249; Nucleic acid-binding proteins; 1.
DR PROSITE; PS50862; AA_TRNA_LIGASE_II; 1.
PE 3: Inferred from homology;
KW Ligase {ECO:0000313|EMBL:KRY55658.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000054653}.
FT DOMAIN 255..580
FT /note="Aminoacyl-transfer RNA synthetases class-II family
FT profile"
FT /evidence="ECO:0000259|PROSITE:PS50862"
SQ SEQUENCE 591 AA; 68032 MW; 34D364773C1D15B4 CRC64;
MSSLVLFRHC FLRLSSISIP NNVCFSSKSI RALKRQLKLE KKLKEKAEKA EISAAHGALG
TVEKDKKDLK KTDDAVDATE YYCLRLAAIK QLRENGFEPY PHKFEVTISL TDFIEKYNSV
KCEEVLNETV CVAGRIHSKR EAGQKLIFYD LRAEGTRLQI MANGKFYKTG EAEFLRINES
VRRGDIVGCT GHPSRTKKGE LSIIPTELVL LTPCLRMLPH LHYGLKNQET RYRMRYLDLI
INNNVRNIFI RRAQILNYIR KYLDSIGFLE VETPMMNMIP GGATAKPFVT HHNELDRDLY
MRVAPELYLK MLIVGGIDRV YEIGRNFRNE SIDLTHNPEF TMCEFYMAYA DYNDLMKITE
DLLSGMVKHL FGSYLVTYHP NGPEGEAVTI DFTPPYRKIS MYFELEKKLN VKLPPPSELV
KEENRRFFDD LCLKHEVECP PPRTTARLLD KLVGEFIEID CITPTFIIDH PQIMSPLAKW
HRAIPGLTER FELFVMTREL CNAYTELNDP VVQRERFEEQ AANKAAGDEE AQPIDEVFCN
ALEHGLPPTA GWGMGIDRLT MLLTDQNNIK EVLLFPAMKP DETREKLNDT V
//
