SYDC_BOVIN
ID SYDC_BOVIN Reviewed; 501 AA.
AC Q3SYZ4;
DT 11-JUL-2006, integrated into UniProtKB/Swiss-Prot.
DT 11-OCT-2005, sequence version 1.
DT 03-AUG-2022, entry version 98.
DE RecName: Full=Aspartate--tRNA ligase, cytoplasmic;
DE EC=6.1.1.12 {ECO:0000250|UniProtKB:P15178};
DE AltName: Full=Aspartyl-tRNA synthetase;
DE Short=AspRS;
GN Name=DARS1; Synonyms=DARS;
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=Crossbred X Angus; TISSUE=Ileum;
RG NIH - Mammalian Gene Collection (MGC) project;
RL Submitted (AUG-2005) 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:0000250|UniProtKB:P15178}.
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:P15178};
CC -!- SUBUNIT: Homodimer. Part of a multisubunit complex that groups tRNA
CC ligases for Arg (RARS1), Asp (DARS1), Gln (QARS1), Ile (IARS1), Leu
CC (LARS1), Lys (KARS1), Met (MARS1) the bifunctional ligase for Glu and
CC Pro (EPRS1) and the auxiliary subunits AIMP1/p43, AIMP2/p38 and
CC EEF1E1/p18. {ECO:0000250|UniProtKB:P14868}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the class-II aminoacyl-tRNA synthetase family.
CC Type 2 subfamily. {ECO:0000305}.
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DR EMBL; BC103319; AAI03320.1; -; mRNA.
DR RefSeq; NP_001030257.1; NM_001035085.1.
DR AlphaFoldDB; Q3SYZ4; -.
DR SMR; Q3SYZ4; -.
DR STRING; 9913.ENSBTAP00000013123; -.
DR PaxDb; Q3SYZ4; -.
DR PeptideAtlas; Q3SYZ4; -.
DR PRIDE; Q3SYZ4; -.
DR GeneID; 510162; -.
DR KEGG; bta:510162; -.
DR CTD; 1615; -.
DR eggNOG; KOG0556; Eukaryota.
DR InParanoid; Q3SYZ4; -.
DR OrthoDB; 677307at2759; -.
DR Proteomes; UP000009136; Unplaced.
DR GO; GO:0017101; C:aminoacyl-tRNA synthetase multienzyme complex; ISS:UniProtKB.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0031090; C:organelle membrane; IEA:UniProt.
DR GO; GO:0004815; F:aspartate-tRNA ligase activity; IBA:GO_Central.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0003723; F:RNA binding; IBA:GO_Central.
DR GO; GO:0006422; P:aspartyl-tRNA aminoacylation; IBA:GO_Central.
DR Gene3D; 2.40.50.140; -; 1.
DR Gene3D; 3.30.930.10; -; 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 PANTHER; PTHR43450; PTHR43450; 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; SSF55681; SSF55681; 1.
DR TIGRFAMs; TIGR00458; aspS_nondisc; 1.
DR PROSITE; PS50862; AA_TRNA_LIGASE_II; 1.
PE 2: Evidence at transcript level;
KW Acetylation; Aminoacyl-tRNA synthetase; ATP-binding; Cytoplasm; Ligase;
KW Nucleotide-binding; Phosphoprotein; Protein biosynthesis;
KW Reference proteome.
FT CHAIN 1..501
FT /note="Aspartate--tRNA ligase, cytoplasmic"
FT /id="PRO_0000245022"
FT REGION 251..254
FT /note="Aspartate"
FT /evidence="ECO:0000250"
FT REGION 411..415
FT /note="Binding site for the 3'-end of tRNA"
FT /evidence="ECO:0000255"
FT BINDING 229
FT /ligand="L-aspartate"
FT /ligand_id="ChEBI:CHEBI:29991"
FT /evidence="ECO:0000250"
FT BINDING 273..275
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT BINDING 273
FT /ligand="L-aspartate"
FT /ligand_id="ChEBI:CHEBI:29991"
FT /evidence="ECO:0000250"
FT BINDING 281..283
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT BINDING 424
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT BINDING 427
FT /ligand="L-aspartate"
FT /ligand_id="ChEBI:CHEBI:29991"
FT /evidence="ECO:0000250"
FT BINDING 431
FT /ligand="L-aspartate"
FT /ligand_id="ChEBI:CHEBI:29991"
FT /evidence="ECO:0000250"
FT BINDING 472..475
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT MOD_RES 52
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P14868"
FT MOD_RES 74
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P14868"
FT MOD_RES 249
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P14868"
FT MOD_RES 374
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P14868"
FT MOD_RES 500
FT /note="Phosphothreonine; by PKA"
FT /evidence="ECO:0000255"
SQ SEQUENCE 501 AA; 57036 MW; A8E00861B2C3E607 CRC64;
MPSANASRRS QEKPREIMDA AEDYAKERYG VSSMIQSQEK PDRVLVRISD LTVQKAGEVV
WVRARVHTSR AKGKQCFLVL RQQQFNVQAL VAVGDHASKQ MVKFAANINK ESIVDVEGVV
RKVNQKIGSC TQQDVELHVQ KIYVISSAEP RLPLQLDDAV RPEVEGEEEG RATVNQDTRL
DNRVIDLRTS TSQAIFRLQS GICHPFRETL TNKGFVEIQT PKIISAASEG GANVFTVSYF
KNNAYLAQSP QLYKQMCICA DFEKVFCIGP VFRAEDSNTH RHLTEFVGLD IEMAFNYHYH
EVVEEIADTL VQIFKGLQKR FQTEIQTVNK QFPCEPFKFL EPTLRLEYCE ALAMLREAGI
EMGDEEDLST PNEKLLGRLV KEKYDTDFYI LDKYPLAVRP FYTMPDPRNP KQSNSYDMFM
RGEEILSGAQ RIHDPQLVTE RALHHGIDLE KIKAYIDSFR FGAPPHAGGG IGLERVTMLF
LGLHNVRQTS MFPRDPKRLT P
