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Database: UniProt
Entry: S8EEW8_9LAMI
LinkDB: S8EEW8_9LAMI
Original site: S8EEW8_9LAMI 
ID   S8EEW8_9LAMI            Unreviewed;       667 AA.
AC   S8EEW8;
DT   16-OCT-2013, integrated into UniProtKB/TrEMBL.
DT   16-OCT-2013, sequence version 1.
DT   13-SEP-2023, entry version 43.
DE   RecName: Full=Aminoacyl-transfer RNA synthetases class-II family profile domain-containing protein {ECO:0000259|PROSITE:PS50862};
DE   Flags: Fragment;
GN   ORFNames=M569_03647 {ECO:0000313|EMBL:EPS71107.1};
OS   Genlisea aurea.
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   asterids; lamiids; Lamiales; Lentibulariaceae; Genlisea.
OX   NCBI_TaxID=192259 {ECO:0000313|EMBL:EPS71107.1, ECO:0000313|Proteomes:UP000015453};
RN   [1] {ECO:0000313|EMBL:EPS71107.1, ECO:0000313|Proteomes:UP000015453}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=23855885;
RA   Leushkin E.V., Sutormin R.A., Nabieva E.R., Penin A.A., Kondrashov A.S.,
RA   Logacheva M.D.;
RT   "The miniature genome of a carnivorous plant Genlisea aurea contains a low
RT   number of genes and short non-coding sequences.";
RL   BMC Genomics 14:476-476(2013).
CC   -!- SIMILARITY: Belongs to the class-II aminoacyl-tRNA synthetase family.
CC       Type 1 subfamily. {ECO:0000256|ARBA:ARBA00006303}.
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:EPS71107.1}.
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DR   EMBL; AUSU01001401; EPS71107.1; -; Genomic_DNA.
DR   AlphaFoldDB; S8EEW8; -.
DR   OrthoDB; 1046261at2759; -.
DR   Proteomes; UP000015453; 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; cd00777; AspRS_core; 1.
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; IPR047090; AspRS_core.
DR   InterPro; IPR004115; GAD-like_sf.
DR   InterPro; IPR029351; GAD_dom.
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; PF02938; GAD; 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; SSF55261; GAD domain-like; 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:UP000015453}.
FT   DOMAIN          227..641
FT                   /note="Aminoacyl-transfer RNA synthetases class-II family
FT                   profile"
FT                   /evidence="ECO:0000259|PROSITE:PS50862"
FT   NON_TER         667
FT                   /evidence="ECO:0000313|EMBL:EPS71107.1"
SQ   SEQUENCE   667 AA;  74131 MW;  001BC7BA63AAF898 CRC64;
     MALLLRSLPA AAASVARVNF SPLSVPLIVL NRRCSIIRRR AFSATGASAS SPETLPAAAP
     KVPLSSSSDA KLRALEWVSR TALCGELSSL DVGRRVRLCG WVALCRVHGG LTFLSLRDHT
     GIVQVTTLPD EFPDAHSIVN ELRVEYVVAV DGVVRPRPVE AVNEKMATGS IEVLAEHVQI
     LNDVKLKLPF LVTTADDAKD STKEEIRLRY RCLDLRRHQM NSNIMFRHRM IKLLRRYLED
     VHGFVEIETP ILSKSTPEGA RDYLVPSRIQ RGTFYALPQS PQIFKQMLMV SGFDRYYQIA
     RCFRDEDLRA DRQPEFTQLD IEMAFVPLED MLKLNEDMIR KVVFLELKGA ELPNPFPRLT
     YAEAMRRYGS DRPDTRFGLE LKDVSEIFRK SSFKLFADTL SIGGIVKALC VPSGAKHYSN
     SSLKKGDVFN EAVKSGAKGL PFLKVLDNGE LEGIPALVSS LSAEERNHFL KQLSASSGDL
     ILFAVGNQKS VNKTLDRLRL HTANELGLID PSSHSILWVT DFPMFEWNDT EGRLEALHHP
     FTAPNPDDMD DLAAARALSY DMVFNGVEIG GGSLRIYKRD VQERVLELVG ISPQQGETKF
     GYLLEALEMG APPHGGIAYG VDRLAMLLAG AKSIRDVIAF PKTTAAQCLL TRTPSEVEQS
     QLEDLSI
//
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