ID   A5DWG2_LODEL            Unreviewed;       697 AA.
AC   A5DWG2;
DT   12-JUN-2007, integrated into UniProtKB/TrEMBL.
DT   12-JUN-2007, sequence version 1.
DT   02-SEP-2026, entry version 102.
DE   RecName: Full=Aminoacyl-transfer RNA synthetases class-II family profile domain-containing protein {ECO:0000259|PROSITE:PS50862};
GN   ORFNames=LELG_01698 {ECO:0000313|EMBL:EDK43520.1};
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; Pichiomycetes;
OC   Debaryomycetaceae; Candida/Lodderomyces clade; Lodderomyces.
OX   NCBI_TaxID=379508 {ECO:0000313|EMBL:EDK43520.1, ECO:0000313|Proteomes:UP000001996};
RN   [1] {ECO:0000313|EMBL:EDK43520.1, 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       Type 1 subfamily. {ECO:0000256|ARBA:ARBA00006303}.
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DR   EMBL; CH981525; EDK43520.1; -; Genomic_DNA.
DR   AlphaFoldDB; A5DWG2; -.
DR   FunCoup; A5DWG2; 638.
DR   STRING; 379508.A5DWG2; -.
DR   GeneID; 5233740; -.
DR   KEGG; lel:PVL30_001671; -.
DR   VEuPathDB; FungiDB:LELG_01698; -.
DR   eggNOG; KOG2411; Eukaryota.
DR   HOGENOM; CLU_014330_4_1_1; -.
DR   InParanoid; A5DWG2; -.
DR   OMA; LCGWVDR; -.
DR   OrthoDB; 439710at2759; -.
DR   Proteomes; UP000001996; Unassembled WGS sequence.
DR   GO; GO:0005739; C:mitochondrion; IEA:TreeGrafter.
DR   GO; GO:0004815; F:aspartate-tRNA ligase activity; IEA:TreeGrafter.
DR   GO; GO:0005524; F:ATP binding; IEA:InterPro.
DR   GO; GO:0006422; P:aspartyl-tRNA aminoacylation; IEA:TreeGrafter.
DR   Gene3D; 3.30.930.10; Bira Bifunctional Protein, Domain 2; 1.
DR   Gene3D; 3.30.1360.30; GAD-like domain; 1.
DR   Gene3D; 2.40.50.140; Nucleic acid-binding proteins; 1.
DR   HAMAP; MF_00044; Asp_tRNA_synth_type1; 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; IPR004524; Asp-tRNA-ligase_1.
DR   InterPro; IPR002312; Asp/Asn-tRNA-synth_IIb.
DR   InterPro; IPR004115; GAD-like_sf.
DR   InterPro; IPR012340; NA-bd_OB-fold.
DR   NCBIfam; TIGR00459; aspS_bact; 1.
DR   NCBIfam; NF001750; PRK00476.1; 1.
DR   PANTHER; PTHR22594:SF5; ASPARTATE--TRNA LIGASE, MITOCHONDRIAL; 1.
DR   PANTHER; PTHR22594; ASPARTYL/LYSYL-TRNA SYNTHETASE; 1.
DR   Pfam; PF00152; tRNA-synt_2; 1.
DR   PRINTS; PR01042; TRNASYNTHASP.
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:0000256|ARBA:ARBA00023146};
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW   Ligase {ECO:0000256|ARBA:ARBA00022598};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW   Protein biosynthesis {ECO:0000256|ARBA:ARBA00022917};
KW   Reference proteome {ECO:0000313|Proteomes:UP000001996}.
FT   DOMAIN          197..664
FT                   /note="Aminoacyl-transfer RNA synthetases class-II family
FT                   profile"
FT                   /evidence="ECO:0000259|PROSITE:PS50862"
FT   REGION          117..141
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        120..129
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   697 AA;  80296 MW;  824551441E356E08 CRC64;
     MFYTAFGGCS KRLYSTLPEK ASTLAKFNFP YSTGTIGSIT TQLDKYLNRK DTLITLHGHI
     DRKSRIRPTV GFGFLRDQEG DVIQFIADAD NNEHQLVLEK MKKLTVEDSI SITGYAKPKV
     GKEQGRQEET AMATRSRTED ASKKPKAWEL VVKDLQILNS SNLDASRLEK LKQTDPEDIP
     PQFRYLQLRT KFFQSALRTR SKIAQLVRNT LVNNHDFVEI ETPLLFKSTP EGAREFLVPT
     RTYDQFYALP QSPQQYKQIL MASGFTRYFQ LAKCFRDEDL RADRQPEFTQ VDLEMSYINS
     AEQIMKVVED VVMNIWLKIC NRPTYTLNEK GFLQKLTDID NNKVQFSKLA YPEALLKYGI
     DKPDLRSDIT FITLDEFFIG EENSEFSVVE ACVLRNALDN ENKSSKNKLP KELTSTHNYS
     RRRPYVWAIR NDKDLLWYEK LVEKKFMKKT NHFDEKKLKT ILNLKPGDIL AISTRSKFPY
     ENPTPLGKFR QLAIKEFPGK WQRPIEKESG ELVNDYKFED MVVGSWVVDF PLFNPVEISS
     STEDPYPEYS MNKYESTHHP FTMCKSEDYE LMGSNPLQVR GEHYDLVING VEVGGGSRRI
     HDPALQKYVF EEILQIKHYD QLFGHLLKAL SMGCPPHAGL ALGFDRLCAM VVGSSSIRDV
     IAFPKNQSGK DLVVESPTEV LEKALNEYFI TKKNNNK
//