SYD_DEIRA
ID SYD_DEIRA Reviewed; 577 AA.
AC Q9RUN7;
DT 19-OCT-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 03-AUG-2022, entry version 142.
DE RecName: Full=Aspartate--tRNA(Asp) ligase;
DE EC=6.1.1.12;
DE AltName: Full=Aspartyl-tRNA synthetase 1;
DE Short=AspRS1;
DE AltName: Full=Discriminating aspartyl-tRNA synthetase;
DE Short=D-AspRS;
GN Name=aspS1; OrderedLocusNames=DR_1347;
OS Deinococcus radiodurans (strain ATCC 13939 / DSM 20539 / JCM 16871 / LMG
OS 4051 / NBRC 15346 / NCIMB 9279 / R1 / VKM B-1422).
OC Bacteria; Deinococcus-Thermus; Deinococci; Deinococcales; Deinococcaceae;
OC Deinococcus.
OX NCBI_TaxID=243230;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 13939 / DSM 20539 / JCM 16871 / LMG 4051 / NBRC 15346 / NCIMB
RC 9279 / R1 / VKM B-1422;
RX PubMed=10567266; DOI=10.1126/science.286.5444.1571;
RA White O., Eisen J.A., Heidelberg J.F., Hickey E.K., Peterson J.D.,
RA Dodson R.J., Haft D.H., Gwinn M.L., Nelson W.C., Richardson D.L.,
RA Moffat K.S., Qin H., Jiang L., Pamphile W., Crosby M., Shen M.,
RA Vamathevan J.J., Lam P., McDonald L.A., Utterback T.R., Zalewski C.,
RA Makarova K.S., Aravind L., Daly M.J., Minton K.W., Fleischmann R.D.,
RA Ketchum K.A., Nelson K.E., Salzberg S.L., Smith H.O., Venter J.C.,
RA Fraser C.M.;
RT "Genome sequence of the radioresistant bacterium Deinococcus radiodurans
RT R1.";
RL Science 286:1571-1577(1999).
RN [2]
RP FUNCTION AS A DISCRIMINATING ASPRS, AND GENE NAME.
RX PubMed=9789001; DOI=10.1073/pnas.95.22.12838;
RA Curnow A.W., Tumbula D.L., Pelaschier J.T., Min B., Soll D.;
RT "Glutamyl-tRNA(Gln) amidotransferase in Deinococcus radiodurans may be
RT confined to asparagine biosynthesis.";
RL Proc. Natl. Acad. Sci. U.S.A. 95:12838-12843(1998).
CC -!- FUNCTION: Catalyzes the attachment of L-aspartate to tRNA(Asp) in a
CC two-step reaction: L-aspartate is first activated by ATP to form Asp-
CC AMP and then transferred to the acceptor end of tRNA(Asp). Is specific
CC for tRNA(Asp) since it cannot aspartylate tRNA(Asn).
CC {ECO:0000269|PubMed:9789001}.
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; Evidence={ECO:0000255|HAMAP-
CC Rule:MF_00044};
CC -!- SUBUNIT: Homodimer. {ECO:0000255|HAMAP-Rule:MF_00044}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00044}.
CC -!- SIMILARITY: Belongs to the class-II aminoacyl-tRNA synthetase family.
CC Type 1 subfamily. {ECO:0000255|HAMAP-Rule:MF_00044}.
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DR EMBL; AE000513; AAF10918.1; -; Genomic_DNA.
DR PIR; D75406; D75406.
DR RefSeq; NP_295070.1; NC_001263.1.
DR RefSeq; WP_010887988.1; NZ_CP015081.1.
DR AlphaFoldDB; Q9RUN7; -.
DR SMR; Q9RUN7; -.
DR STRING; 243230.DR_1347; -.
DR PRIDE; Q9RUN7; -.
DR EnsemblBacteria; AAF10918; AAF10918; DR_1347.
DR KEGG; dra:DR_1347; -.
DR PATRIC; fig|243230.17.peg.1544; -.
DR eggNOG; COG0173; Bacteria.
DR HOGENOM; CLU_014330_3_2_0; -.
DR InParanoid; Q9RUN7; -.
DR OMA; YQLDVEM; -.
DR OrthoDB; 226836at2; -.
DR BioCyc; MetaCyc:MON-14053; -.
DR Proteomes; UP000002524; Chromosome I.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0004815; F:aspartate-tRNA ligase activity; IBA:GO_Central.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0003676; F:nucleic acid binding; IEA:InterPro.
DR GO; GO:0006422; P:aspartyl-tRNA aminoacylation; IBA:GO_Central.
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; Cytoplasm; Ligase;
KW Nucleotide-binding; Protein biosynthesis; Reference proteome.
FT CHAIN 1..577
FT /note="Aspartate--tRNA(Asp) ligase"
FT /id="PRO_0000110865"
FT REGION 196..199
FT /note="Aspartate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00044"
FT BINDING 172
FT /ligand="L-aspartate"
FT /ligand_id="ChEBI:CHEBI:29991"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00044"
FT BINDING 218..220
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00044"
FT BINDING 218
FT /ligand="L-aspartate"
FT /ligand_id="ChEBI:CHEBI:29991"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00044"
FT BINDING 227
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00044"
FT BINDING 438
FT /ligand="L-aspartate"
FT /ligand_id="ChEBI:CHEBI:29991"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00044"
FT BINDING 473
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00044"
FT BINDING 480
FT /ligand="L-aspartate"
FT /ligand_id="ChEBI:CHEBI:29991"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00044"
FT BINDING 525..528
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00044"
SQ SEQUENCE 577 AA; 64232 MW; 73AC3B9EA50C3ADB CRC64;
MMKRTSLIGQ LGQAQQQQTV TLQGWVSRRR DLGGLIFLEL RDRSGTVQVQ VEPDSPAFAE
ADRLRAEYVA EIEGTFQPRP ESQRKGGLAD FEVIASRVKV LNAAKTPPFE LDKGESVAED
IRLKYRYLDL RRPEMQRALM LRSKAVTAVT EFLDAEGFIQ VETPMLTKST PEGARDFLVP
SRLNPGEFYA LPQSPQLFKQ LLMIAGFDRY YQLARCFRDE DLRADRQPDF TQLDMEMSFV
EQDDVLEVQE RLLAHVFRRV LDVELPLPFP RMSYFDAMDR YGSDKPDLRF DSAFTDVTGL
FRGGEFAAFA SAPSVKVLVA PELTRKQIDE LERVAKQNGA GGLAWLRRDG EGFTGGISKF
VGGIAPQLIE QTGVAQGGTL LFAAGEWKKA VTALGAVRLA LRDLFDLAAG GPQFHVSWVV
DFPQLEFDED SQSWTYMHHP FTAPHPGDVA LFGTERQGEM RAQAYDLVMN GFEIGGGSVR
IHDPEVQAKM FQAIGFSEEA AREKFGFFLD ALEYGTPPHG GIAWGFDRLL MLMSGAGSIR
EVIAFPKNNR GADLMAQAPS PVEDAQLAEV GVQVRGE
