ID F1MTX7_BOVIN Unreviewed; 501 AA.
AC F1MTX7;
DT 03-MAY-2011, integrated into UniProtKB/TrEMBL.
DT 03-MAY-2011, sequence version 1.
DT 27-MAR-2024, entry version 86.
DE RecName: Full=Aspartate--tRNA ligase, cytoplasmic {ECO:0000256|ARBA:ARBA00018853};
DE EC=6.1.1.12 {ECO:0000256|ARBA:ARBA00012841};
DE AltName: Full=Aspartyl-tRNA synthetase {ECO:0000256|ARBA:ARBA00033155};
GN Name=DARS1 {ECO:0000313|Ensembl:ENSBTAP00000013123.2,
GN ECO:0000313|VGNC:VGNC:27881};
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 {ECO:0000313|Ensembl:ENSBTAP00000013123.2, ECO:0000313|Proteomes:UP000009136};
RN [1] {ECO:0000313|Ensembl:ENSBTAP00000013123.2, ECO:0000313|Proteomes:UP000009136}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Hereford {ECO:0000313|Ensembl:ENSBTAP00000013123.2,
RC ECO:0000313|Proteomes:UP000009136};
RA Rosen B.D., Bickhart D.M., Koren S., Schnabel R.D., Hall R., Zimin A.,
RA Dreischer C., Schultheiss S., Schroeder S.G., Elsik C.G., Couldrey C.,
RA Liu G.E., Van Tassell C.P., Phillippy A.M., Smith T.P.L., Medrano J.F.;
RT "ARS-UCD1.2.";
RL Submitted (MAR-2018) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSBTAP00000013123.2}
RP IDENTIFICATION.
RC STRAIN=Hereford {ECO:0000313|Ensembl:ENSBTAP00000013123.2};
RG Ensembl;
RL Submitted (NOV-2023) to UniProtKB.
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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR AlphaFoldDB; F1MTX7; -.
DR SMR; F1MTX7; -.
DR Ensembl; ENSBTAT00000013123.3; ENSBTAP00000013123.2; ENSBTAG00000009949.4.
DR VEuPathDB; HostDB:ENSBTAG00000009949; -.
DR VGNC; VGNC:27881; DARS1.
DR GeneTree; ENSGT01030000234618; -.
DR HOGENOM; CLU_004553_2_1_1; -.
DR OMA; WVHEIRD; -.
DR TreeFam; TF105676; -.
DR Proteomes; UP000009136; Chromosome 2.
DR Bgee; ENSBTAG00000009949; Expressed in choroid plexus and 108 other cell types or tissues.
DR ExpressionAtlas; F1MTX7; baseline.
DR GO; GO:0005737; C:cytoplasm; IEA:InterPro.
DR GO; GO:0031090; C:organelle membrane; IEA:UniProt.
DR GO; GO:0004815; F:aspartate-tRNA ligase activity; IEA:UniProtKB-EC.
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; IEA:InterPro.
DR CDD; cd04320; AspRS_cyto_N; 1.
DR CDD; cd00776; AsxRS_core; 1.
DR Gene3D; 2.40.50.140; Nucleic acid-binding proteins; 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 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 Pfam; PF01336; tRNA_anti-codon; 1.
DR PRINTS; PR01042; TRNASYNTHASP.
DR SUPFAM; SSF55681; Class II aaRS and biotin synthetases; 1.
DR SUPFAM; SSF50249; Nucleic acid-binding proteins; 1.
DR PROSITE; PS50862; AA_TRNA_LIGASE_II; 1.
PE 3: Inferred from homology;
KW Acetylation {ECO:0000256|ARBA:ARBA00022990};
KW Reference proteome {ECO:0000313|Proteomes:UP000009136}.
FT DOMAIN 196..501
FT /note="Aminoacyl-transfer RNA synthetases class-II family
FT profile"
FT /evidence="ECO:0000259|PROSITE:PS50862"
SQ SEQUENCE 501 AA; 57052 MW; A71600F58AA7AEB5 CRC64;
MPSANASRRS QEKPREIMDA AEDYAKERYG VSSMIQSQEK PDRVLVRISD LTVQKAGEVV
WVRARVHTSR AKGKQCFLVL RQQQFNVQAL VAVGDHASKQ MVKFAANINK ESIVDVEGVV
RKVNQKIGSC TQQDVELHVQ KIYVISSAEP RLPLQLDDAV RPEVEGEEDG RATVNQDTRL
DNRVIDLRTS TSQAIFRLQS GICHLFRETL TNKGFVEIQT PKIISAASEG GANVFTVSYF
KNNAYLAQSP QLYKQMCICA DFEKVFCIGP VFRAEDSNTH RHLTEFVGLD IEMAFNYHYH
EVVEEIADTL VQIFKGLQKR FQTEIQTVNK QFPCEPFKFL EPTLRLEYCE ALAMLREAGI
EMGDEEDLST PNEKLLGRLV KEKYDTDFYI LDKYPLAVRP FYTMPDPRNP KQSNSYDMFM
RGEEILSGAQ RIHDPQLLTE RALHHGIDLE KIKAYIDSFR FGAPPHAGGG IGLERVTMLF
LGLHNVRQTS MFPRDPKRLT P
//
