SYDM_RAT
ID SYDM_RAT Reviewed; 652 AA.
AC Q3KRD0;
DT 03-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT 08-NOV-2005, sequence version 1.
DT 03-AUG-2022, entry version 123.
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 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 [LARGE SCALE MRNA].
RC TISSUE=Prostate;
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).
RN [2]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-218, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=16641100; DOI=10.1073/pnas.0600895103;
RA Hoffert J.D., Pisitkun T., Wang G., Shen R.-F., Knepper M.A.;
RT "Quantitative phosphoproteomics of vasopressin-sensitive renal cells:
RT regulation of aquaporin-2 phosphorylation at two sites.";
RL Proc. Natl. Acad. Sci. U.S.A. 103:7159-7164(2006).
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; BC105774; AAI05775.1; -; mRNA.
DR RefSeq; NP_001029315.1; NM_001034143.1.
DR AlphaFoldDB; Q3KRD0; -.
DR SMR; Q3KRD0; -.
DR IntAct; Q3KRD0; 1.
DR STRING; 10116.ENSRNOP00000003828; -.
DR iPTMnet; Q3KRD0; -.
DR PhosphoSitePlus; Q3KRD0; -.
DR PaxDb; Q3KRD0; -.
DR PRIDE; Q3KRD0; -.
DR Ensembl; ENSRNOT00000003828; ENSRNOP00000003828; ENSRNOG00000002813.
DR GeneID; 304919; -.
DR KEGG; rno:304919; -.
DR UCSC; RGD:1308286; rat.
DR CTD; 55157; -.
DR RGD; 1308286; Dars2.
DR eggNOG; KOG2411; Eukaryota.
DR GeneTree; ENSGT01030000234618; -.
DR HOGENOM; CLU_014330_3_1_1; -.
DR InParanoid; Q3KRD0; -.
DR OMA; YQLDVEM; -.
DR OrthoDB; 697974at2759; -.
DR PhylomeDB; Q3KRD0; -.
DR TreeFam; TF314827; -.
DR PRO; PR:Q3KRD0; -.
DR Proteomes; UP000002494; Chromosome 13.
DR Bgee; ENSRNOG00000002813; Expressed in heart and 19 other tissues.
DR Genevisible; Q3KRD0; RN.
DR GO; GO:0005759; C:mitochondrial matrix; IEA:UniProtKB-SubCell.
DR GO; GO:0005739; C:mitochondrion; IBA:GO_Central.
DR GO; GO:0005654; C:nucleoplasm; IEA:Ensembl.
DR GO; GO:0004815; F:aspartate-tRNA ligase activity; ISS:UniProtKB.
DR GO; GO:0050560; F:aspartate-tRNA(Asn) ligase activity; ISO:RGD.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0003676; F:nucleic acid binding; IEA:InterPro.
DR GO; GO:0042803; F:protein homodimerization activity; ISO:RGD.
DR GO; GO:0006422; P:aspartyl-tRNA aminoacylation; IBA:GO_Central.
DR GO; GO:0070145; P:mitochondrial asparaginyl-tRNA aminoacylation; ISS:UniProtKB.
DR GO; GO:0043039; P:tRNA aminoacylation; ISO:RGD.
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 1: Evidence at protein level;
KW Aminoacyl-tRNA synthetase; ATP-binding; Ligase; Mitochondrion;
KW Nucleotide-binding; Phosphoprotein; Protein biosynthesis;
KW Reference proteome; Transit peptide.
FT TRANSIT 1..46
FT /note="Mitochondrion"
FT /evidence="ECO:0000255"
FT CHAIN 47..652
FT /note="Aspartate--tRNA ligase, mitochondrial"
FT /id="PRO_0000250738"
FT REGION 243..246
FT /note="Aspartate"
FT /evidence="ECO:0000250"
FT BINDING 265..267
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT BINDING 265
FT /ligand="L-aspartate"
FT /ligand_id="ChEBI:CHEBI:29991"
FT /evidence="ECO:0000250"
FT BINDING 534
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT BINDING 541
FT /ligand="L-aspartate"
FT /ligand_id="ChEBI:CHEBI:29991"
FT /evidence="ECO:0000250"
FT BINDING 583..586
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT MOD_RES 218
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:16641100"
FT MOD_RES 241
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q6PI48"
SQ SEQUENCE 652 AA; 73953 MW; 6CB570CC05F30086 CRC64;
MYLGSWLNRL GRGLSRPIGK TKQPIWGSLS RSLTLSSQRV PEFSSFVART NTCGELRSSH
LGQEVTLCGW IQYRRQNTFL VLRDCHGLVQ ILIPQDESAA SVRRTLCEAP VESVVRVSGT
VIARPLGQEN PKMPTGEIEI KAKTAELLNA CKKLPFEIKD FVKKTEALRL QYRYLDLRSS
QMQHNLRLRS QMVMKMREYL CTLHGFVDIE TPTLFKRTPG GAKEFLVPSR EPGRFYSLPQ
SPQQFKQLLM VGGLDRYFQV ARCYRDEGSR PDRQPEFTQI DIEMSFVDQT GIQHLVEGLL
HYSWPEDKDP LVAPFPSMTF AEALATYGTD KPDTRFGMKI VDISDVFRNT EIRFLQDALA
KPQGTVKAIC VHEGAKYLRK EDIEFIRKFA AHHFSQEVLP IFLNARKNWS SPFAKFITEE
ERLELTRLME IQEDDMVLLT AGQHEKACSL LGKLRLECAD LLETRGLALR DPALFSFLWV
LDFPLFLAKE ESPTELESAH HPFTAPHPGD IHLLYTEPEK VRGQHYDLVL NGNEIGGGSI
RIHDAQLQRY ILETLLKEDV KLLSHLLQAL DYGAPPHGGI ALGLDRLVCL VTGAPSIRDV
IAFPKSYRGH DLMSNAPDTV SPEDLKPYHI HVSWPTDSEE RASATPSKYL SS
