SYDM_BOVIN
ID SYDM_BOVIN Reviewed; 651 AA.
AC A6QPU5;
DT 08-APR-2008, integrated into UniProtKB/Swiss-Prot.
DT 21-AUG-2007, sequence version 1.
DT 03-AUG-2022, entry version 90.
DE RecName: Full=Aspartate--tRNA ligase, mitochondrial;
DE EC=6.1.1.12 {ECO:0000250|UniProtKB:Q6PI48};
DE AltName: Full=Aspartyl-tRNA synthetase;
DE Short=AspRS;
DE Flags: Precursor;
GN Name=DARS2;
OS Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Hereford; TISSUE=Thymus;
RG NIH - Mammalian Gene Collection (MGC) project;
RL Submitted (JUL-2007) 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:0000250|UniProtKB:Q6PI48};
CC -!- SUBUNIT: Homodimer. {ECO:0000250|UniProtKB:Q6PI48}.
CC -!- SUBCELLULAR LOCATION: Mitochondrion matrix
CC {ECO:0000250|UniProtKB:Q6PI48}.
CC -!- SIMILARITY: Belongs to the class-II aminoacyl-tRNA synthetase family.
CC Type 1 subfamily. {ECO:0000305}.
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DR EMBL; BC149492; AAI49493.1; -; mRNA.
DR RefSeq; NP_001095692.1; NM_001102222.1.
DR AlphaFoldDB; A6QPU5; -.
DR SMR; A6QPU5; -.
DR STRING; 9913.ENSBTAP00000005704; -.
DR PaxDb; A6QPU5; -.
DR PRIDE; A6QPU5; -.
DR GeneID; 538772; -.
DR KEGG; bta:538772; -.
DR CTD; 55157; -.
DR eggNOG; KOG2411; Eukaryota.
DR InParanoid; A6QPU5; -.
DR OrthoDB; 697974at2759; -.
DR Proteomes; UP000009136; Unplaced.
DR GO; GO:0005759; C:mitochondrial matrix; IEA:UniProtKB-SubCell.
DR GO; GO:0005739; C:mitochondrion; IBA:GO_Central.
DR GO; GO:0031090; C:organelle membrane; IEA:UniProt.
DR GO; GO:0004815; F:aspartate-tRNA ligase activity; ISS:UniProtKB.
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; IBA:GO_Central.
DR GO; GO:0070145; P:mitochondrial asparaginyl-tRNA aminoacylation; ISS:UniProtKB.
DR Gene3D; 2.40.50.140; -; 1.
DR Gene3D; 3.30.1360.30; -; 1.
DR Gene3D; 3.30.930.10; -; 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; IPR002312; Asp/Asn-tRNA-synth_IIb.
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 PANTHER; PTHR22594:SF5; PTHR22594:SF5; 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; SSF50249; SSF50249; 1.
DR SUPFAM; SSF55261; SSF55261; 1.
DR SUPFAM; SSF55681; SSF55681; 1.
DR TIGRFAMs; TIGR00459; aspS_bact; 1.
DR PROSITE; PS50862; AA_TRNA_LIGASE_II; 1.
PE 2: Evidence at transcript level;
KW Acetylation; Aminoacyl-tRNA synthetase; ATP-binding; Ligase; Mitochondrion;
KW Nucleotide-binding; Phosphoprotein; Protein biosynthesis;
KW Reference proteome; Transit peptide.
FT TRANSIT 1..44
FT /note="Mitochondrion"
FT /evidence="ECO:0000255"
FT CHAIN 45..651
FT /note="Aspartate--tRNA ligase, mitochondrial"
FT /id="PRO_0000327860"
FT REGION 241..244
FT /note="Aspartate"
FT /evidence="ECO:0000250"
FT BINDING 263..265
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT BINDING 263
FT /ligand="L-aspartate"
FT /ligand_id="ChEBI:CHEBI:29991"
FT /evidence="ECO:0000250"
FT BINDING 532
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT BINDING 539
FT /ligand="L-aspartate"
FT /ligand_id="ChEBI:CHEBI:29991"
FT /evidence="ECO:0000250"
FT BINDING 581..584
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT MOD_RES 216
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q3KRD0"
FT MOD_RES 239
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q6PI48"
FT MOD_RES 379
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q6PI48"
SQ SEQUENCE 651 AA; 73688 MW; BF9790C9E0C877C7 CRC64;
MFCWLSRLCG ELSTPTRRTT QLIWSSAARS MVLSSQRIPE LSSFVARTNT CGELRSSHLG
QEVTLCGWIQ FRRQNIFLVL RDFHGLVQVV IPQDESAASV KKILCEAPME SVVQVSGTVI
SRPPGQKNPK MPTGEIEIKV KTAKLLNSCK KLPFEIKDFM KKTETLRLQY RYLDLRSVQM
QYNLRLRSQM VMKMREYLCN LHGFVDVETP TLFKRTPGGA KEFVIPSREP GKFYSLPQSP
QQFKQLLMVG GLDRYFQVAR CYRDEGSRPD RQPEFTQIDI EMSFVDQTGV QSLIEGLLQY
SWPSDKDPLV VPFPSMPFAE ALASYGTDKP DTRFGMKIVD ISDMFRNTEV GFLQDALSKP
QGTVKAICIR KGAKYLKRKD IESIRKFAAD HFNEEVLPIF LKTNENWNSP VAKFIMEEQG
LGLVKLLETQ EEDVVLLTAG EHKKACSLMG KLRLECADLL EARGVVLRDP ALFSFLWVVD
FPLFLPKEEN PQELESAHHP FTAPHPSDIH LLYTEPHKVR SQHYDLVLNG NEIGGGSIRI
HNSELQHCVL DTVLKEDVKL LSHLLQALDY GAPPHGGIAL GLDRLMCLVT GAPSIRDVIA
FPKSFRGHDL MSNAPDSIPP EELKPYHIQV SWPMDAETEK SSSNHPCRSE S
