ID A5E5W3_LODEL Unreviewed; 547 AA.
AC A5E5W3;
DT 12-JUN-2007, integrated into UniProtKB/TrEMBL.
DT 12-JUN-2007, sequence version 1.
DT 27-MAR-2024, entry version 100.
DE RecName: Full=Lysyl-tRNA synthetase {ECO:0000256|ARBA:ARBA00030563};
GN ORFNames=LELG_05002 {ECO:0000313|EMBL:EDK46821.1};
OS Lodderomyces elongisporus (strain ATCC 11503 / CBS 2605 / JCM 1781 / NBRC
OS 1676 / NRRL YB-4239) (Yeast) (Saccharomyces elongisporus).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Debaryomycetaceae; Candida/Lodderomyces clade;
OC Lodderomyces.
OX NCBI_TaxID=379508 {ECO:0000313|EMBL:EDK46821.1, ECO:0000313|Proteomes:UP000001996};
RN [1] {ECO:0000313|EMBL:EDK46821.1, ECO:0000313|Proteomes:UP000001996}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 11503 / BCRC 21390 / CBS 2605 / JCM 1781 / NBRC 1676 /
RC NRRL YB-4239 {ECO:0000313|Proteomes:UP000001996};
RX PubMed=19465905; DOI=10.1038/nature08064;
RA Butler G., Rasmussen M.D., Lin M.F., Santos M.A., Sakthikumar S.,
RA Munro C.A., Rheinbay E., Grabherr M., Forche A., Reedy J.L., Agrafioti I.,
RA Arnaud M.B., Bates S., Brown A.J., Brunke S., Costanzo M.C.,
RA Fitzpatrick D.A., de Groot P.W., Harris D., Hoyer L.L., Hube B., Klis F.M.,
RA Kodira C., Lennard N., Logue M.E., Martin R., Neiman A.M., Nikolaou E.,
RA Quail M.A., Quinn J., Santos M.C., Schmitzberger F.F., Sherlock G.,
RA Shah P., Silverstein K.A., Skrzypek M.S., Soll D., Staggs R.,
RA Stansfield I., Stumpf M.P., Sudbery P.E., Srikantha T., Zeng Q., Berman J.,
RA Berriman M., Heitman J., Gow N.A., Lorenz M.C., Birren B.W., Kellis M.,
RA Cuomo C.A.;
RT "Evolution of pathogenicity and sexual reproduction in eight Candida
RT genomes.";
RL Nature 459:657-662(2009).
CC -!- SIMILARITY: Belongs to the class-II aminoacyl-tRNA synthetase family.
CC {ECO:0000256|ARBA:ARBA00008226}.
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DR EMBL; CH981531; EDK46821.1; -; Genomic_DNA.
DR RefSeq; XP_001523586.1; XM_001523536.1.
DR AlphaFoldDB; A5E5W3; -.
DR STRING; 379508.A5E5W3; -.
DR GeneID; 5230830; -.
DR KEGG; lel:LELG_05002; -.
DR VEuPathDB; FungiDB:LELG_05002; -.
DR eggNOG; KOG1885; Eukaryota.
DR HOGENOM; CLU_008255_6_0_1; -.
DR InParanoid; A5E5W3; -.
DR OMA; MQERHVD; -.
DR OrthoDB; 648039at2759; -.
DR Proteomes; UP000001996; 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:UP000001996}.
FT DOMAIN 221..537
FT /note="Aminoacyl-transfer RNA synthetases class-II family
FT profile"
FT /evidence="ECO:0000259|PROSITE:PS50862"
SQ SEQUENCE 547 AA; 62562 MW; 7FEAEF489A73BBED CRC64;
MLRCLNPSLR SSFRRLYCNN VGIKLLSTAS VARQMTKENL TAERRKAIIQ SEPYFESSCY
PSIADARQQY PDATLLRISD FRNRFETTDF SNYEYNRTSE CYNIEGRISG IRKFGKAMFF
FDLVQDNCKL QVLISNSLVV LEKSEFDRVH SWFKEGDYVS CHGFASRTKT GELTLKVNTP
VRMLSPCLIQ LPDKLIDKGI INQNRVMNYL VNPKSANPII VKSQVIQAIR QFFINKGFLE
MQTPILSSLG TGANAQPFLT KFKDDHVQLR VAPELWLKKM VIAGFEKIFE IGNNFRNEGI
DQSHNPEFTS CEFYQSFTSL EELMNITEEL LKQIFHKFKV PLGGTEQTKV SLKSIKFPKY
DFLPTLEEIT GKKINDLSLD SLLTLYKELG ITVPSNPNPI SLVNNLSETY LESLSVTKHY
NVPVIIYNQP EILSPLAKSK TDGHNGIPVS LRFELFINGK EYVNAYEEEN NPKIQLAKFQ
QQKANKQKYG DNEMLIPDWE YVKTMEMGLP PTGGWGIGID RLAMYVSGAE RIDEVLPFGN
LRDVLKQ
//
