ID A0A168KFL1_CORDF Unreviewed; 621 AA.
AC A0A168KFL1;
DT 06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT 06-JUL-2016, sequence version 1.
DT 27-MAR-2024, entry version 32.
DE RecName: Full=Lysyl-tRNA synthetase {ECO:0000256|ARBA:ARBA00030563};
GN ORFNames=LEL_01169 {ECO:0000313|EMBL:OAA81624.1};
OS Akanthomyces lecanii RCEF 1005.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Hypocreales; Cordycipitaceae; Akanthomyces;
OC Cordyceps confragosa.
OX NCBI_TaxID=1081108 {ECO:0000313|EMBL:OAA81624.1, ECO:0000313|Proteomes:UP000076881};
RN [1] {ECO:0000313|EMBL:OAA81624.1, ECO:0000313|Proteomes:UP000076881}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=RCEF 1005 {ECO:0000313|EMBL:OAA81624.1,
RC ECO:0000313|Proteomes:UP000076881};
RX PubMed=27071652; DOI=10.1093/gbe/evw082;
RA Shang Y., Xiao G., Zheng P., Cen K., Zhan S., Wang C.;
RT "Divergent and convergent evolution of fungal pathogenicity.";
RL Genome Biol. Evol. 8:1374-1387(2016).
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:OAA81624.1}.
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DR EMBL; AZHF01000001; OAA81624.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A168KFL1; -.
DR STRING; 1081108.A0A168KFL1; -.
DR OrthoDB; 648039at2759; -.
DR Proteomes; UP000076881; 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 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 PANTHER; PTHR42918:SF5; LYSINE--TRNA LIGASE, MITOCHONDRIAL; 1.
DR PANTHER; PTHR42918; LYSYL-TRNA SYNTHETASE; 1.
DR Pfam; PF00152; tRNA-synt_2; 2.
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 Aminoacyl-tRNA synthetase {ECO:0000313|EMBL:OAA81624.1};
KW Ligase {ECO:0000313|EMBL:OAA81624.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000076881}.
FT DOMAIN 216..621
FT /note="Aminoacyl-transfer RNA synthetases class-II family
FT profile"
FT /evidence="ECO:0000259|PROSITE:PS50862"
FT REGION 1..66
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 501..520
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..23
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 34..48
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 621 AA; 69768 MW; AF8BDD8DFE0B70C5 CRC64;
MRSIALSRQN VQTFASVPDA KNGTSIPSEP CDEAEHASPF KQQRRSDLGK DQASGSPLYP
ESYPRIEPSE ARMAVPEFLE SEENELSQPL INLVGRVRAK RVVGKNLVFL DIVNEFQKVQ
IVVNKSKCVE PLDNICTHNS KKFHLFRSLI QVGDHISVNG VRDHTPAGLL TLAAREIPEL
LSPTMEQIPE VLTDSKTKMQ DRHVDMLVNK ETVDVLRLRS EITKHMRDHF HSKRFLEFQT
PILAENAGGA IARPFVTRAT EFKDKDLALR VAPELWLKRL VVGGVDRVFE IGPAFRNEGV
DATHNPEFTM CEFYSAYSSL PDLIKETEEL LTSLAKHTQK LIQTQLTSLP PIDLQKFKRP
FKQVEFVPAL EEATGVRFPK LSAEDALPEL LALMKLAGID IPGDIPTSLP RLLDRLAAMY
IEPKSFEEPL FITNHPACMS PLAKSFLCPK TYQLVSARAE LFVGGRELAN MYEEENDPKE
QQRKLTTHRN LVNTEDGEVG INAPVEKSND NEAPKDEETL EDEVEMEELR MEEEETDQEV
FDNHMKRPEE EDEWATSPLD RSYIKALDYG LPPTGGWGCG VERLVMLFSG ANRISDCLSF
GTIRNVVGLS SDAAKKEGGK P
//
