ID A0A0S7EA56_9EURO Unreviewed; 426 AA.
AC A0A0S7EA56;
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=Lysyl-tRNA synthetase {ECO:0000256|ARBA:ARBA00030563};
GN ORFNames=CNMCM8060_006462 {ECO:0000313|EMBL:KAF4176330.1};
OS Aspergillus lentulus.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus.
OX NCBI_TaxID=293939 {ECO:0000313|EMBL:KAF4176330.1, ECO:0000313|Proteomes:UP000713487};
RN [1] {ECO:0000313|EMBL:KAF4176330.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=CNM-CM8060 {ECO:0000313|EMBL:KAF4176330.1};
RA dos Santos R.A.C., Steenwyk J.L., Rivero-Menendez O., Mead M.E.,
RA Silva L.P., Bastos R.W., Alastruey-Izquierdo A., Goldman G.H., Rokas A.;
RT "Genomic and phenotypic heterogeneity of clinical isolates of the human
RT pathogens Aspergillus fumigatus, Aspergillus lentulus and Aspergillus
RT fumigatiaffinis.";
RL bioRxiv 0:0-0(2020).
RN [2] {ECO:0000313|EMBL:KAF4176330.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=CNM-CM8060 {ECO:0000313|EMBL:KAF4176330.1};
RA Santos R.A.C., Steenwyk J.L., Rivero-Menendez O., Mead M.E., Silva L.P.,
RA Bastos R.W., Alastruey-Izquierdo A., Goldman G.H., Rokas A.;
RL Submitted (APR-2020) to the EMBL/GenBank/DDBJ databases.
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:KAF4176330.1}.
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DR EMBL; JAAAPS010000044; KAF4176330.1; -; Genomic_DNA.
DR STRING; 293939.A0A0S7EA56; -.
DR VEuPathDB; FungiDB:TMP_alenIFM54703_8871; -.
DR Proteomes; UP000713487; Unassembled WGS sequence.
DR GO; GO:0005737; C:cytoplasm; IEA:InterPro.
DR GO; GO:0005524; F:ATP binding; IEA:InterPro.
DR GO; GO:0004824; F:lysine-tRNA ligase activity; IEA:InterPro.
DR GO; GO:0006430; P:lysyl-tRNA aminoacylation; IEA:InterPro.
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; IPR018149; Lys-tRNA-synth_II_C.
DR InterPro; IPR012340; NA-bd_OB-fold.
DR PANTHER; PTHR42918:SF5; LYSINE--TRNA LIGASE, MITOCHONDRIAL; 1.
DR PANTHER; PTHR42918; LYSYL-TRNA SYNTHETASE; 1.
DR Pfam; PF00152; tRNA-synt_2; 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;
FT DOMAIN 88..407
FT /note="Aminoacyl-transfer RNA synthetases class-II family
FT profile"
FT /evidence="ECO:0000259|PROSITE:PS50862"
SQ SEQUENCE 426 AA; 47972 MW; 2BB7A12EAF38FF9F CRC64;
MCNIRKLGGV APDAFKRFYR LLRRGDAFSV TGKPHRTGTG ELTVLATELP QLLSPCLHDV
PVNAEEHETS PYPRHVQFLA DQKAADIIRA RSAIIQFLRQ FFLDRSFMEV STPIIGSIAG
GAMARPFQTS ATEFPDRQLS LRIAPELWLK RLVVGGFDKV FEIGPSFRNE GLDKTHNPEF
TTCEFYHAYA NLEDLMSITE NLLSGMAAHI QEFNKNASLK PPEVNFSAPF RRVDFTTGIE
GKIGRRLPDL TTPYALDHVS QLFRDLSLPI PKNPTLPRLL DELCSTYLEP ECINPTFIIN
PPECLSPLSK SFIHPSNQQL VAARAELFID GREIVNTYEE ENSPFEQRRK FEDQVRYNKG
TDEPAEIDES YLEALEWGLP STGGWGCGID RLCMLFTGAK RIGDVLPFGN LRAVTRRHDG
LSRTTD
//
