ID I7GHJ9_MACFA Unreviewed; 246 AA.
AC I7GHJ9;
DT 03-OCT-2012, integrated into UniProtKB/TrEMBL.
DT 03-OCT-2012, sequence version 1.
DT 27-MAR-2024, entry version 29.
DE RecName: Full=Aspartate--tRNA ligase, cytoplasmic {ECO:0000256|ARBA:ARBA00018853};
DE EC=6.1.1.12 {ECO:0000256|ARBA:ARBA00012841};
OS Macaca fascicularis (Crab-eating macaque) (Cynomolgus monkey).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini;
OC Cercopithecidae; Cercopithecinae; Macaca.
OX NCBI_TaxID=9541 {ECO:0000313|EMBL:BAE88209.1};
RN [1] {ECO:0000313|EMBL:BAE88209.1}
RP NUCLEOTIDE SEQUENCE.
RX PubMed=17194215; DOI=10.1371/journal.pbio.0050013;
RA Wang H.-Y., Chien H.-C., Osada N., Hashimoto K., Sugano S., Gojobori T.,
RA Chou C.-K., Tsai S.-F., Wu C.-I., Shen C.-K.J.;
RT "Rate of evolution in brain-expressed genes in humans and other primates.";
RL PLoS Biol. 5:e13-e13(2007).
CC -!- FUNCTION: Catalyzes the specific attachment of an amino acid to its
CC cognate tRNA in a 2 step reaction: the amino acid (AA) is first
CC activated by ATP to form AA-AMP and then transferred to the acceptor
CC end of the tRNA. {ECO:0000256|ARBA:ARBA00003170}.
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; AB171146; BAE88209.1; -; mRNA.
DR AlphaFoldDB; I7GHJ9; -.
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:InterPro.
DR GO; GO:0006422; P:aspartyl-tRNA aminoacylation; IEA:InterPro.
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 PANTHER; PTHR43450:SF1; ASPARTATE--TRNA LIGASE, CYTOPLASMIC; 1.
DR PANTHER; PTHR43450; ASPARTYL-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 PROSITE; PS50862; AA_TRNA_LIGASE_II; 1.
PE 2: Evidence at transcript level;
KW Aminoacyl-tRNA synthetase {ECO:0000313|EMBL:BAE88209.1};
KW Ligase {ECO:0000313|EMBL:BAE88209.1}.
FT DOMAIN 8..246
FT /note="Aminoacyl-transfer RNA synthetases class-II family
FT profile"
FT /evidence="ECO:0000259|PROSITE:PS50862"
SQ SEQUENCE 246 AA; 28528 MW; 9E08116B4CDF9053 CRC64;
MCICADFEKV FCIGPVFRAE DSNTHRHLTE FVGLDIEMAF NYHYHEVMEE IADTMVQIFK
GLQERFQTEI QTVNKQFPCE PFKFLEPTLR LEYCEALAML REAGVEMGDE DDLSTPNEKL
LGHLVKEKYD TDFYILDKYP LAVRPFYTMP DPRNPKQSNS YDMFMRGEEI LSGAQRIHDP
QLLTERTLHH GIDLEKIKAY IDSFRFGAPP HAGGGIGLER VTMLFLGLHN VRQTSMFPRD
PKRLTP
//
