ID A0A0M9A8R0_9HYME Unreviewed; 520 AA.
AC A0A0M9A8R0;
DT 09-DEC-2015, integrated into UniProtKB/TrEMBL.
DT 09-DEC-2015, sequence version 1.
DT 27-MAR-2024, entry version 33.
DE RecName: Full=Aspartate--tRNA ligase, cytoplasmic {ECO:0000256|ARBA:ARBA00018853};
DE EC=6.1.1.12 {ECO:0000256|ARBA:ARBA00012841};
DE AltName: Full=Aspartyl-tRNA synthetase {ECO:0000256|ARBA:ARBA00033155};
DE Flags: Fragment;
GN ORFNames=WN51_02811 {ECO:0000313|EMBL:KOX79545.1};
OS Melipona quadrifasciata.
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Hymenoptera; Apocrita; Aculeata; Apoidea;
OC Anthophila; Apidae; Melipona.
OX NCBI_TaxID=166423 {ECO:0000313|EMBL:KOX79545.1, ECO:0000313|Proteomes:UP000053105};
RN [1] {ECO:0000313|EMBL:KOX79545.1, ECO:0000313|Proteomes:UP000053105}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=0111107301 {ECO:0000313|EMBL:KOX79545.1};
RC TISSUE=Whole body {ECO:0000313|EMBL:KOX79545.1};
RA Pan H., Kapheim K.;
RT "The genome of Melipona quadrifasciata.";
RL Submitted (JUL-2015) to the EMBL/GenBank/DDBJ databases.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + L-aspartate + tRNA(Asp) = AMP + diphosphate + L-
CC aspartyl-tRNA(Asp); Xref=Rhea:RHEA:19649, Rhea:RHEA-COMP:9660,
CC Rhea:RHEA-COMP:9678, ChEBI:CHEBI:29991, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:33019, ChEBI:CHEBI:78442, ChEBI:CHEBI:78516,
CC ChEBI:CHEBI:456215; EC=6.1.1.12;
CC Evidence={ECO:0000256|ARBA:ARBA00000225};
CC -!- SIMILARITY: Belongs to the class-II aminoacyl-tRNA synthetase family.
CC Type 2 subfamily. {ECO:0000256|ARBA:ARBA00005312}.
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DR EMBL; KQ435711; KOX79545.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0M9A8R0; -.
DR STRING; 166423.A0A0M9A8R0; -.
DR OrthoDB; 382728at2759; -.
DR Proteomes; UP000053105; Unassembled WGS sequence.
DR GO; GO:0005737; C:cytoplasm; IEA:InterPro.
DR GO; GO:0004815; F:aspartate-tRNA ligase activity; IEA:UniProtKB-EC.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0003676; F:nucleic acid binding; IEA:InterPro.
DR GO; GO:0006422; P:aspartyl-tRNA aminoacylation; IEA:InterPro.
DR CDD; cd04320; AspRS_cyto_N; 1.
DR CDD; cd00776; AsxRS_core; 1.
DR Gene3D; 2.40.50.140; Nucleic acid-binding proteins; 1.
DR HAMAP; MF_02075; Asp_tRNA_synth_type2; 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; IPR004523; Asp-tRNA_synthase_2.
DR InterPro; IPR002312; Asp/Asn-tRNA-synth_IIb.
DR InterPro; IPR012340; NA-bd_OB-fold.
DR InterPro; IPR004365; NA-bd_OB_tRNA.
DR NCBIfam; TIGR00458; aspS_nondisc; 1.
DR PANTHER; PTHR43450:SF1; ASPARTATE--TRNA LIGASE, CYTOPLASMIC; 1.
DR PANTHER; PTHR43450; ASPARTYL-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 Ligase {ECO:0000313|EMBL:KOX79545.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000053105}.
FT DOMAIN 215..520
FT /note="Aminoacyl-transfer RNA synthetases class-II family
FT profile"
FT /evidence="ECO:0000259|PROSITE:PS50862"
FT REGION 1..41
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:KOX79545.1"
SQ SEQUENCE 520 AA; 58872 MW; FD5C8ED7B87BA2CB CRC64;
SDELSKKSLK KQQKEAEKAA KKAERKAQNQ AQHDKAQEED VSIGKYGDTG LIQSRDKHTE
RKFTDIKSLN PNLKDQTVWI RGRLHTSRAK GKQCFIVLRQ QSYTIQGLAA VNEKVSKQMI
KFLSNITKES IVDIEAIVKC VPSQIESCTQ KDVEVHIEKV FVISAAKPQL PLQIEDASRP
VGEADENALN IKVNQDTRLD NRVLDLRTPA NQAIYKVEAA ICKLFRDILT SKGFIEIHTP
KIISAASEGG ANVFTVSYFK GNAYLAQSPQ LYKQMAIAAD FDKVFTVGAV FRAEDSNTHR
HLTEFVGLDL EMAFKYHYHE VVDTIGQLFV EMFKGLRDNY AAEIEAVRQQ YNVEPFKFLD
PPLKLEFKDA IELLAEVGVT LGREDDLSTP DEKLLGKLVK AKYDTDFYIL DKYPLAVRPF
YTMPDPNNPK VSNSYDMFMR GEEIISGAQR IHDPELLTER AKHHGIDLEK IRSYIDAFKY
GCPPHAGGGI GMERVVMLYL GLDNIRKVSM FPRDPKRITP
//
