ID M3B0G8_PSEFD Unreviewed; 469 AA.
AC M3B0G8;
DT 01-MAY-2013, integrated into UniProtKB/TrEMBL.
DT 01-MAY-2013, sequence version 1.
DT 27-MAR-2024, entry version 51.
DE RecName: Full=Lysyl-tRNA synthetase {ECO:0000256|ARBA:ARBA00030563};
GN ORFNames=MYCFIDRAFT_153654 {ECO:0000313|EMBL:EME82937.1};
OS Pseudocercospora fijiensis (strain CIRAD86) (Black leaf streak disease
OS fungus) (Mycosphaerella fijiensis).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC Dothideomycetidae; Mycosphaerellales; Mycosphaerellaceae; Pseudocercospora.
OX NCBI_TaxID=383855 {ECO:0000313|EMBL:EME82937.1, ECO:0000313|Proteomes:UP000016932};
RN [1] {ECO:0000313|EMBL:EME82937.1, ECO:0000313|Proteomes:UP000016932}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CIRAD86 {ECO:0000313|EMBL:EME82937.1,
RC ECO:0000313|Proteomes:UP000016932};
RX PubMed=23236275; DOI=10.1371/journal.ppat.1003037;
RA Ohm R.A., Feau N., Henrissat B., Schoch C.L., Horwitz B.A., Barry K.W.,
RA Condon B.J., Copeland A.C., Dhillon B., Glaser F., Hesse C.N., Kosti I.,
RA LaButti K., Lindquist E.A., Lucas S., Salamov A.A., Bradshaw R.E.,
RA Ciuffetti L., Hamelin R.C., Kema G.H.J., Lawrence C., Scott J.A.,
RA Spatafora J.W., Turgeon B.G., de Wit P.J.G.M., Zhong S., Goodwin S.B.,
RA Grigoriev I.V.;
RT "Diverse lifestyles and strategies of plant pathogenesis encoded in the
RT genomes of eighteen Dothideomycetes fungi.";
RL PLoS Pathog. 8:E1003037-E1003037(2012).
CC -!- SIMILARITY: Belongs to the class-II aminoacyl-tRNA synthetase family.
CC {ECO:0000256|ARBA:ARBA00008226}.
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DR EMBL; KB446558; EME82937.1; -; Genomic_DNA.
DR RefSeq; XP_007926315.1; XM_007928124.1.
DR AlphaFoldDB; M3B0G8; -.
DR STRING; 383855.M3B0G8; -.
DR GeneID; 19331702; -.
DR KEGG; pfj:MYCFIDRAFT_153654; -.
DR eggNOG; KOG1885; Eukaryota.
DR HOGENOM; CLU_008255_6_0_1; -.
DR OrthoDB; 648039at2759; -.
DR Proteomes; UP000016932; 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:InterPro.
DR GO; GO:0003676; F:nucleic acid binding; IEA:InterPro.
DR GO; GO:0006430; P:lysyl-tRNA aminoacylation; IEA:InterPro.
DR CDD; cd04322; LysRS_N; 1.
DR Gene3D; 2.40.50.140; Nucleic acid-binding proteins; 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; 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 PANTHER; PTHR42918:SF5; LYSINE--TRNA LIGASE, MITOCHONDRIAL; 1.
DR PANTHER; PTHR42918; LYSYL-TRNA SYNTHETASE; 1.
DR Pfam; PF00152; tRNA-synt_2; 1.
DR Pfam; PF01336; tRNA_anti-codon; 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 Reference proteome {ECO:0000313|Proteomes:UP000016932}.
FT DOMAIN 122..445
FT /note="Aminoacyl-transfer RNA synthetases class-II family
FT profile"
FT /evidence="ECO:0000259|PROSITE:PS50862"
SQ SEQUENCE 469 AA; 52459 MW; 494A8A608450E5AE CRC64;
MLVGKISSLR TAGSKLLFMD LVTDTGTVQV VCKLPHLQQH HSATTSESWK AFTKTARKGD
YYSVVGHKHV TERGELSLLA SELPRLLSPS LHQVPEAYEH PEARARNRHV DMIVNAEAIQ
TLQMRHEIEA AIQAFFNERE FVKVTTPLLS ATAGGAAARP FETVATELSD ETLQLRIAPE
LWLKRLVVGG MPKVYELGPA FRNEGVDATH NPEFNICEFY EAYASLDQLM ATTERLLCEL
DAYIESLRKL GKFSALSLPA IRPKYTEIAG SISEVQPFQR VEFIPTLEKK LGSKLGHLET
DDAYSHIAGL FSEKNIPKPV NPTLPRLLDA LAAEYLEPLS KEEPIFITHH PACMSPLSKH
FKCPNTGQTV AARAELFIGG CEYANMYEEE NSPFEQRRKF EEQLQQRSRD AEAMQLDEDY
LRCLEWGLPP TGGWGCGVDR LVMLFSGRER MSDVLAFGSL RTVVGLGKK
//
