ID A0A087VJX5_BALRE Unreviewed; 313 AA.
AC A0A087VJX5;
DT 29-OCT-2014, integrated into UniProtKB/TrEMBL.
DT 29-OCT-2014, sequence version 1.
DT 27-MAR-2024, entry version 32.
DE RecName: Full=Aspartate--tRNA ligase, cytoplasmic {ECO:0000256|ARBA:ARBA00018853};
DE EC=6.1.1.12 {ECO:0000256|ARBA:ARBA00012841};
DE Flags: Fragment;
GN ORFNames=N312_07158 {ECO:0000313|EMBL:KFO12917.1};
OS Balearica regulorum gibbericeps (East African grey crowned-crane).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Gruiformes; Gruidae; Balearica.
OX NCBI_TaxID=100784 {ECO:0000313|EMBL:KFO12917.1, ECO:0000313|Proteomes:UP000053309};
RN [1] {ECO:0000313|EMBL:KFO12917.1, ECO:0000313|Proteomes:UP000053309}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BGI_N312 {ECO:0000313|EMBL:KFO12917.1};
RA Zhang G., Li C.;
RT "Genome evolution of avian class.";
RL Submitted (APR-2014) to the EMBL/GenBank/DDBJ databases.
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; KL496104; KFO12917.1; -; Genomic_DNA.
DR RefSeq; XP_010304864.1; XM_010306562.1.
DR AlphaFoldDB; A0A087VJX5; -.
DR GeneID; 104638704; -.
DR KEGG; breg:104638704; -.
DR CTD; 1615; -.
DR OrthoDB; 382728at2759; -.
DR Proteomes; UP000053309; 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:InterPro.
DR GO; GO:0006422; P:aspartyl-tRNA aminoacylation; IEA:InterPro.
DR CDD; cd00776; AsxRS_core; 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 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 PRINTS; PR01042; TRNASYNTHASP.
DR SUPFAM; SSF55681; Class II aaRS and biotin synthetases; 1.
DR PROSITE; PS50862; AA_TRNA_LIGASE_II; 1.
PE 3: Inferred from homology;
KW Ligase {ECO:0000313|EMBL:KFO12917.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000053309}.
FT DOMAIN 10..313
FT /note="Aminoacyl-transfer RNA synthetases class-II family
FT profile"
FT /evidence="ECO:0000259|PROSITE:PS50862"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:KFO12917.1"
FT NON_TER 313
FT /evidence="ECO:0000313|EMBL:KFO12917.1"
SQ SEQUENCE 313 AA; 35829 MW; AA3F28B9D36B879F CRC64;
TSTSQAIFCL QSGICQLFRE TLIRKGFVEI QTPKIISAAS EGGANVFTVS YFKSSAYLAQ
SPQLYKQMCI CADFEKVFCI GPVFRAEDSN THRHLTEFVG LDIEMAFNYH YHEVVDEIAD
TLVQIFKGLQ ERFQTEIQTV NKQFPCEPFK FLEPTLRLEY REAVAMLREA GVEMGDEEDL
STPNEKLLGR LVKEKYDTDF YILDKYPLAV RPFYTMPDPV NPKNSNSYDM FMRGEEILSG
AQRIHDPQLL TERARHHGID LEKIKAYIDS FRFGAPPHAG GGIGLERVTM LYLGLHNVRQ
TSMFPRDPKR LTP
//