SYDND_HALSA
ID SYDND_HALSA Reviewed; 436 AA.
AC O07683; Q9HS07;
DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT 01-JUL-1997, sequence version 1.
DT 03-AUG-2022, entry version 144.
DE RecName: Full=Aspartate--tRNA(Asp/Asn) ligase {ECO:0000255|HAMAP-Rule:MF_02075};
DE EC=6.1.1.23 {ECO:0000255|HAMAP-Rule:MF_02075};
DE AltName: Full=Aspartyl-tRNA synthetase {ECO:0000255|HAMAP-Rule:MF_02075};
DE Short=AspRS {ECO:0000255|HAMAP-Rule:MF_02075};
DE AltName: Full=Non-discriminating aspartyl-tRNA synthetase {ECO:0000255|HAMAP-Rule:MF_02075};
DE Short=ND-AspRS {ECO:0000255|HAMAP-Rule:MF_02075};
GN Name=aspS {ECO:0000255|HAMAP-Rule:MF_02075}; OrderedLocusNames=VNG_0461G;
OS Halobacterium salinarum (strain ATCC 700922 / JCM 11081 / NRC-1)
OS (Halobacterium halobium).
OC Archaea; Euryarchaeota; Stenosarchaea group; Halobacteria; Halobacteriales;
OC Halobacteriaceae; Halobacterium.
OX NCBI_TaxID=64091;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA Ihara H., Shinoda H., Ishigami M.;
RT "Aspartyl-tRNA synthetase from Halobacterium salinarium.";
RL Submitted (JUN-1997) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700922 / JCM 11081 / NRC-1;
RX PubMed=11016950; DOI=10.1073/pnas.190337797;
RA Ng W.V., Kennedy S.P., Mahairas G.G., Berquist B., Pan M., Shukla H.D.,
RA Lasky S.R., Baliga N.S., Thorsson V., Sbrogna J., Swartzell S., Weir D.,
RA Hall J., Dahl T.A., Welti R., Goo Y.A., Leithauser B., Keller K., Cruz R.,
RA Danson M.J., Hough D.W., Maddocks D.G., Jablonski P.E., Krebs M.P.,
RA Angevine C.M., Dale H., Isenbarger T.A., Peck R.F., Pohlschroder M.,
RA Spudich J.L., Jung K.-H., Alam M., Freitas T., Hou S., Daniels C.J.,
RA Dennis P.P., Omer A.D., Ebhardt H., Lowe T.M., Liang P., Riley M., Hood L.,
RA DasSarma S.;
RT "Genome sequence of Halobacterium species NRC-1.";
RL Proc. Natl. Acad. Sci. U.S.A. 97:12176-12181(2000).
RN [3]
RP FUNCTION AS A NON-DISCRIMINATING ASPRS, CATALYTIC ACTIVITY, SUBSTRATE
RP SPECIFICITY, MUTAGENESIS OF HIS-26 AND PRO-84, AND DISCRIMINATION SITES.
RX PubMed=17114946; DOI=10.4161/rna.3.3.3116;
RA Cardoso A.M., Polycarpo C., Martins O.B., Soll D.;
RT "A non-discriminating aspartyl-tRNA synthetase from Halobacterium
RT salinarum.";
RL RNA Biol. 3:110-114(2006).
CC -!- FUNCTION: Aspartyl-tRNA synthetase with relaxed tRNA specificity since
CC it is able to aspartylate not only its cognate tRNA(Asp) but also
CC tRNA(Asn). This indicates that it is not able to differentiate between
CC base C36 in the tRNA(Asp) anticodon (GUC) from base U36 in the
CC tRNA(Asn) (anticodon GUU). Reaction proceeds in two steps: L-aspartate
CC is first activated by ATP to form Asp-AMP and then transferred to the
CC acceptor end of tRNA(Asp/Asn). {ECO:0000269|PubMed:17114946}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + L-aspartate + tRNA(Asx) = AMP + diphosphate + L-
CC aspartyl-tRNA(Asx); Xref=Rhea:RHEA:18349, Rhea:RHEA-COMP:9710,
CC Rhea:RHEA-COMP:9711, ChEBI:CHEBI:29991, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:33019, ChEBI:CHEBI:78442, ChEBI:CHEBI:78516,
CC ChEBI:CHEBI:456215; EC=6.1.1.23; Evidence={ECO:0000255|HAMAP-
CC Rule:MF_02075, ECO:0000269|PubMed:17114946};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_02075};
CC Note=Binds 3 Mg(2+) cations per subunit. The strongest magnesium site
CC (Mg1) is bound to the beta- and gamma-phosphates of ATP and four water
CC molecules complete its coordination sphere. {ECO:0000255|HAMAP-
CC Rule:MF_02075};
CC -!- SUBUNIT: Homodimer. {ECO:0000255|HAMAP-Rule:MF_02075}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_02075}.
CC -!- MISCELLANEOUS: The misacylated aspartate-tRNA(Asn) is not used in
CC protein synthesis until it is converted by GatCAB into asparaginyl-
CC tRNA(Asn).
CC -!- SIMILARITY: Belongs to the class-II aminoacyl-tRNA synthetase family.
CC Type 2 subfamily. {ECO:0000255|HAMAP-Rule:MF_02075}.
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DR EMBL; D82887; BAA20527.1; -; Genomic_DNA.
DR EMBL; AE004437; AAG19001.1; -; Genomic_DNA.
DR PIR; E84204; E84204.
DR PIR; T48900; T48900.
DR RefSeq; WP_010902296.1; NC_002607.1.
DR AlphaFoldDB; O07683; -.
DR SMR; O07683; -.
DR STRING; 64091.VNG_0461G; -.
DR PaxDb; O07683; -.
DR EnsemblBacteria; AAG19001; AAG19001; VNG_0461G.
DR GeneID; 5953682; -.
DR GeneID; 62886114; -.
DR KEGG; hal:VNG_0461G; -.
DR PATRIC; fig|64091.14.peg.346; -.
DR HOGENOM; CLU_004553_2_1_2; -.
DR InParanoid; O07683; -.
DR OMA; WVHEIRD; -.
DR OrthoDB; 24288at2157; -.
DR PhylomeDB; O07683; -.
DR BRENDA; 6.1.1.23; 2552.
DR Proteomes; UP000000554; Chromosome.
DR GO; GO:0017101; C:aminoacyl-tRNA synthetase multienzyme complex; IBA:GO_Central.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0004815; F:aspartate-tRNA ligase activity; IBA:GO_Central.
DR GO; GO:0050560; F:aspartate-tRNA(Asn) ligase activity; IEA:UniProtKB-EC.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-UniRule.
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 Aminoacyl-tRNA synthetase; ATP-binding; Cytoplasm; Ligase; Magnesium;
KW Metal-binding; Nucleotide-binding; Protein biosynthesis;
KW Reference proteome.
FT CHAIN 1..436
FT /note="Aspartate--tRNA(Asp/Asn) ligase"
FT /id="PRO_0000110992"
FT REGION 191..194
FT /note="Aspartate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02075"
FT BINDING 169
FT /ligand="L-aspartate"
FT /ligand_id="ChEBI:CHEBI:29991"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02075"
FT BINDING 213..215
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02075"
FT BINDING 213
FT /ligand="L-aspartate"
FT /ligand_id="ChEBI:CHEBI:29991"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02075"
FT BINDING 221..223
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02075"
FT BINDING 359
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02075"
FT BINDING 359
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02075"
FT BINDING 359
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="3"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02075"
FT BINDING 362
FT /ligand="L-aspartate"
FT /ligand_id="ChEBI:CHEBI:29991"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02075"
FT BINDING 362
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02075"
FT BINDING 366
FT /ligand="L-aspartate"
FT /ligand_id="ChEBI:CHEBI:29991"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02075"
FT BINDING 407..410
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02075"
FT SITE 26
FT /note="Important for tRNA non-discrimination"
FT SITE 84
FT /note="Important for tRNA non-discrimination"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02075"
FT MUTAGEN 26
FT /note="H->A,Q: Enhances enzyme specificity for tRNA(Asp)
FT over tRNA(Asn), by decreasing the ability to form Asp-
FT tRNA(Asn)."
FT /evidence="ECO:0000269|PubMed:17114946"
FT MUTAGEN 84
FT /note="P->A,K: Enhances enzyme specificity for tRNA(Asp)
FT over tRNA(Asn), by decreasing the ability to form Asp-
FT tRNA(Asn)."
FT /evidence="ECO:0000269|PubMed:17114946"
SQ SEQUENCE 436 AA; 49038 MW; 47A417B8CD6B1C09 CRC64;
MLERTYIEDV TPDDDGEDTT IAGHVHELRD LGGILFVIVR DATGRLQVVA KEDDTPDLFE
TAEGLSSEDV VQVTGTLEAS DQAPGGVELA PTELTVVSEA TDVPSIEISK DVDADLSTRL
DERHLDVRKP STKAVFSLRS KAMGAMTDWF YDNRFEEVDT PELSTAGAEG GADLFPVVYY
DKEAYLSQSP QLYKQILVAS GVDRLFEVGH AFRAEDFGTS RHVSEIAMFD VELGYVEDHH
DVMDVQEESL RHTIRHVVEH AQRELDELGS DLSVPEADFP RITFEEAREI LADEYDHVPE
DDNDLDTKGE RLLGEYFEEQ GHPAVFVVGY PDEKFYYRQD VDGDDVASRK FDLLYRGQEL
SSGGQREHDI ERLTAKMREQ GVEPENFEFY LDAFRYGVPP HGGYGLGIDR LIQQLAGLDN
IKEAILFPRD PDRLEP
