SYDC_RAT
ID SYDC_RAT Reviewed; 501 AA.
AC P15178;
DT 01-APR-1990, integrated into UniProtKB/Swiss-Prot.
DT 01-APR-1990, sequence version 1.
DT 03-AUG-2022, entry version 173.
DE RecName: Full=Aspartate--tRNA ligase, cytoplasmic;
DE EC=6.1.1.12 {ECO:0000269|PubMed:2642907};
DE AltName: Full=Aspartyl-tRNA synthetase;
DE Short=AspRS;
GN Name=Dars1; Synonyms=Dars, Drs1;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, CATALYTIC ACTIVITY, AND SUBUNIT.
RC TISSUE=Liver;
RX PubMed=2642907; DOI=10.1016/s0021-9258(19)85019-6;
RA Mirande M., Waller J.-P.;
RT "Molecular cloning and primary structure of cDNA encoding the catalytic
RT domain of rat liver aspartyl-tRNA synthetase.";
RL J. Biol. Chem. 264:842-847(1989).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC TISSUE=Liver;
RX PubMed=8973367; DOI=10.1016/s0378-1119(96)00455-6;
RA Lazard M., Agou F., Cavarelli J., Latreille M.T., Moras D., Mirande M.;
RT "Genomic organization of the rat aspartyl-tRNA synthetase gene family: a
RT single active gene and several retropseudogenes.";
RL Gene 180:197-205(1996).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Lung;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
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:0000269|PubMed:2642907}.
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:0000269|PubMed:2642907};
CC -!- SUBUNIT: Homodimer (PubMed:2642907). Part of a multisubunit complex
CC that groups tRNA ligases for Arg (RARS1), Asp (DARS1), Gln (QARS1), Ile
CC (IARS1), Leu (LARS1), Lys (KARS1), Met (MARS1) the bifunctional ligase
CC for Glu and Pro (EPRS1) and the auxiliary subunits AIMP1/p43, AIMP2/p38
CC and EEF1E1/p18 (By similarity). {ECO:0000250|UniProtKB:P14868,
CC ECO:0000269|PubMed:2642907}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm.
CC -!- SIMILARITY: Belongs to the class-II aminoacyl-tRNA synthetase family.
CC Type 2 subfamily. {ECO:0000305}.
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DR EMBL; J04487; AAA40789.1; -; mRNA.
DR EMBL; U30812; AAC52981.1; -; Genomic_DNA.
DR EMBL; U30485; AAC52981.1; JOINED; Genomic_DNA.
DR EMBL; U30800; AAC52981.1; JOINED; Genomic_DNA.
DR EMBL; U30801; AAC52981.1; JOINED; Genomic_DNA.
DR EMBL; U30802; AAC52981.1; JOINED; Genomic_DNA.
DR EMBL; U30803; AAC52981.1; JOINED; Genomic_DNA.
DR EMBL; U30804; AAC52981.1; JOINED; Genomic_DNA.
DR EMBL; U30805; AAC52981.1; JOINED; Genomic_DNA.
DR EMBL; U30806; AAC52981.1; JOINED; Genomic_DNA.
DR EMBL; U30807; AAC52981.1; JOINED; Genomic_DNA.
DR EMBL; U30808; AAC52981.1; JOINED; Genomic_DNA.
DR EMBL; U30809; AAC52981.1; JOINED; Genomic_DNA.
DR EMBL; U30810; AAC52981.1; JOINED; Genomic_DNA.
DR EMBL; U30811; AAC52981.1; JOINED; Genomic_DNA.
DR EMBL; BC072534; AAH72534.1; -; mRNA.
DR PIR; A32197; SYRTDT.
DR RefSeq; NP_446251.1; NM_053799.3.
DR AlphaFoldDB; P15178; -.
DR SMR; P15178; -.
DR BioGRID; 250460; 6.
DR IntAct; P15178; 4.
DR MINT; P15178; -.
DR STRING; 10116.ENSRNOP00000005127; -.
DR iPTMnet; P15178; -.
DR PhosphoSitePlus; P15178; -.
DR jPOST; P15178; -.
DR PaxDb; P15178; -.
DR PRIDE; P15178; -.
DR Ensembl; ENSRNOT00000005127; ENSRNOP00000005127; ENSRNOG00000003743.
DR GeneID; 116483; -.
DR KEGG; rno:116483; -.
DR UCSC; RGD:621167; rat.
DR CTD; 1615; -.
DR RGD; 621167; Dars.
DR eggNOG; KOG0556; Eukaryota.
DR GeneTree; ENSGT01030000234618; -.
DR HOGENOM; CLU_004553_2_1_1; -.
DR InParanoid; P15178; -.
DR OMA; WVHEIRD; -.
DR OrthoDB; 677307at2759; -.
DR PhylomeDB; P15178; -.
DR TreeFam; TF105676; -.
DR PRO; PR:P15178; -.
DR Proteomes; UP000002494; Chromosome 13.
DR Bgee; ENSRNOG00000003743; Expressed in quadriceps femoris and 20 other tissues.
DR ExpressionAtlas; P15178; baseline and differential.
DR Genevisible; P15178; RN.
DR GO; GO:0017101; C:aminoacyl-tRNA synthetase multienzyme complex; ISS:UniProtKB.
DR GO; GO:0005737; C:cytoplasm; ISO:RGD.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0045202; C:synapse; ISO:RGD.
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 1: Evidence at protein 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_0000111012"
FT REGION 251..254
FT /note="Aspartate"
FT /evidence="ECO:0000250"
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"
SQ SEQUENCE 501 AA; 57126 MW; D3D389B39D7327E2 CRC64;
MPSANASRKG QEKPREIVDA AEDYAKERYG VSSMIQSQEK PDRVLVRVKD LTVQKADEVV
WVRARVHTSR AKGKQCFLVL RQQQFNVQAL VAVGDHASKQ MVKFAANINK ESIIDVEGIV
RKVNQKIGSC TQQDVELHVQ KIYVISLAEP RLPLQLDDAI RPEVEGEEDG RATVNQDTRL
DNRIIDLRTS TSQAIFHLQS GICHLFRETL INKGFVEIQT PKIISAASEG GANVFTVSYF
KSNAYLAQSP QLYKQMCICA DFEKVFCIGP VFRAEDSNTH RHLTEFVGLD IEMAFNYHYH
EVVEEIADTL VQIFKGLQER FQTEIQTVNK QFPCEPFKFL EPTLRLEYCE ALAMLREAGV
EMDDEEDLST PNEKLLGRLV KEKYDTDFYV LDKYPLAVRP FYTMPDPRNP KQSNSYDMFM
RGEEILSGAQ RIHDPQLLTE RALHHGIDLE KIKAYIDSFR FGAPPHAGGG IGLERVTMLF
LGLHNVRQTS MFPRDPKRLT P
