ID A0A2G5IA01_CERBT Unreviewed; 636 AA.
AC A0A2G5IA01;
DT 31-JAN-2018, integrated into UniProtKB/TrEMBL.
DT 31-JAN-2018, sequence version 1.
DT 27-MAR-2024, entry version 29.
DE RecName: Full=Lysine--tRNA ligase {ECO:0000256|ARBA:ARBA00013166, 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 ORFNames=CB0940_01775 {ECO:0000313|EMBL:PIB01532.1};
OS Cercospora beticola (Sugarbeet leaf spot fungus).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC Dothideomycetidae; Mycosphaerellales; Mycosphaerellaceae; Cercospora.
OX NCBI_TaxID=122368 {ECO:0000313|EMBL:PIB01532.1, ECO:0000313|Proteomes:UP000230605};
RN [1] {ECO:0000313|EMBL:PIB01532.1, ECO:0000313|Proteomes:UP000230605}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=09-40 {ECO:0000313|EMBL:PIB01532.1,
RC ECO:0000313|Proteomes:UP000230605};
RA De Jonge R., Ebert M.K., Suttle J.C., Jurick Ii W.M., Secor G.A.,
RA Thomma B.P., Van De Peer Y., Bolton M.D.;
RT "The cercosporin biosynthetic gene cluster was horizontally transferred to
RT several fungal lineages and shown to be expanded in Cercospora beticola
RT based on microsynteny with recipient genomes.";
RL Submitted (OCT-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:PIB01532.1}.
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DR EMBL; LKMD01000100; PIB01532.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2G5IA01; -.
DR OrthoDB; 648039at2759; -.
DR Proteomes; UP000230605; Chromosome 1.
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:PIB01532.1}.
FT DOMAIN 284..606
FT /note="Aminoacyl-transfer RNA synthetases class-II family
FT profile"
FT /evidence="ECO:0000259|PROSITE:PS50862"
FT REGION 1..102
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 16..47
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 54..77
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 636 AA; 71433 MW; 9944A455D9AF174A CRC64;
MAAQQAADAV KDAVNTVTEK VSSLTTGAGS NDNGTDNANT GGTTPNLVLD EVTGEKVSKS
ELKKRIKARE KEAKKAAAPP KQAPASSKKK VGGAQDDEAQ LNPNQYFEIR SRAVKRMKET
SSPNPYPHKF HVTYDLRDFE KDFGHLKKGD VLKDKAISVG VRIYNIRTSG ENLRFYEVAV
NGAEIQIMAQ NLESTSATPF AEQHDILRRG DIIGVTGYPG RTSPKREDNP GELSIFAQEV
TLLAPCLHQI PSEHYGFRDQ ESRYRNRHLD MIMNKSTVDT FIARSKIVRY VRNYFDNNGF
YELETPILLK SAGGATAKPF FTHHNDLNMT LALRIATELP LKQLVIGGIH RVYELGRQFR
NEGIDLTHNP EFTTCEYYEA FADVYDVMER TEELVEGMVK FVTGGLQTKF TTVDGEVYDV
NWAKPWKRIE MIPALEEACG EKFPPGDQLH TAETNEFLRR MLKKTGLECT PPLTNARMID
KMVGEFIEEK CINPTFITGH PQVMSPLAKY HRANAGLCER FEAFVCKKEI VNAYTELNDP
FDQRLRFEEQ ANQKAQGDDE AQPLDEGFLN ALEYGLPPTG GWGMGIDRMV MFLTNNYSIK
EVLTFPFMKD EIQAPKPKAA EVVDVEPVPV EGITHK
//
