ID   A0A0K0EIG6_STRER        Unreviewed;       587 AA.
AC   A0A0K0EIG6;
DT   14-OCT-2015, integrated into UniProtKB/TrEMBL.
DT   14-OCT-2015, sequence version 1.
DT   27-MAR-2024, entry version 37.
DE   SubName: Full=AA_TRNA_LIGASE_II domain-containing protein {ECO:0000313|WBParaSite:SSTP_0000927100.1};
OS   Strongyloides stercoralis (Threadworm).
OC   Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC   Tylenchina; Panagrolaimomorpha; Strongyloidoidea; Strongyloididae;
OC   Strongyloides.
OX   NCBI_TaxID=6248 {ECO:0000313|WBParaSite:SSTP_0000927100.1};
RN   [1] {ECO:0000313|WBParaSite:SSTP_0000927100.1}
RP   IDENTIFICATION.
RG   WormBaseParasite;
RL   Submitted (AUG-2015) to UniProtKB.
CC   -!- SIMILARITY: Belongs to the class-II aminoacyl-tRNA synthetase family.
CC       Type 1 subfamily. {ECO:0000256|ARBA:ARBA00006303}.
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DR   AlphaFoldDB; A0A0K0EIG6; -.
DR   STRING; 6248.A0A0K0EIG6; -.
DR   WBParaSite; SSTP_0000927100.1; SSTP_0000927100.1; SSTP_0000927100.
DR   Proteomes; UP000035681; Unassembled WGS sequence.
DR   GO; GO:0005737; C:cytoplasm; IEA:InterPro.
DR   GO; GO:0004812; F:aminoacyl-tRNA ligase activity; IEA:UniProtKB-KW.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0003676; F:nucleic acid binding; IEA:InterPro.
DR   GO; GO:0006418; P:tRNA aminoacylation for protein translation; IEA:InterPro.
DR   CDD; cd04317; EcAspRS_like_N; 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; IPR047089; Asp-tRNA-ligase_1_N.
DR   InterPro; IPR002312; Asp/Asn-tRNA-synth_IIb.
DR   InterPro; IPR004115; GAD-like_sf.
DR   InterPro; IPR012340; NA-bd_OB-fold.
DR   InterPro; IPR004365; NA-bd_OB_tRNA.
DR   NCBIfam; TIGR00459; aspS_bact; 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   Pfam; PF01336; tRNA_anti-codon; 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:UP000035681}.
FT   DOMAIN          151..555
FT                   /note="Aminoacyl-transfer RNA synthetases class-II family
FT                   profile"
FT                   /evidence="ECO:0000259|PROSITE:PS50862"
SQ   SEQUENCE   587 AA;  67731 MW;  B4ECE7B0FF411C7A CRC64;
     MLHSFKRLSS AINRYTLRSH NCGELRSKDE GKIVSLYGWV AYKRMNKFVV LKDAYGMTQL
     RIDEKNDKLQ EVLKNITSES CISVVGVVEN RGNDINKLMN TGEIEVCVQD LNVLNHAPKI
     VPIHLKTENH DQTKLMYRYL DIRSQYMQNN LRLRSYVTNE IRKFLTEHAS FVEIETPTLF
     RKTPGGAKEF IVPAGGLYKG KFYSLPQSPQ QFKQLLMVGS IDKYFQIARC YRDEGAKQDR
     QPEFTQIDIE LSYTNQEMII ELIEDMIISS WPKSMEELKP EKKFKQFSYD YVMENYGSDK
     PDLRIPWIIN DISYLLKDIF KCEFVQCFIA RDCFSHISTS EKNKWKKIME INESCQSFEF
     FKMTKNKWIK DKIKEILVKK FEIKEDDVFV VSWGNNEKFV KWTLGQLRNH IGEAAGLRKG
     GKFEILWVVD FPLFEEDGGK YVSSHHPFTA PKEVDLKNLI NMKDLLSIKA LHYDLVINGI
     EVGGGSIRIH DASLQKHVLE NILKEPSAEL DYFVKALEYG APPHGGFALG LDRYIALLIG
     NGDSNTSIKD VIAFPKSKSG RCLMSDSPAT PDDDTLRRYG IMTVKDN
//