ID SYDND_SULTO Reviewed; 429 AA.
AC Q976I3; F9VMP5;
DT 29-MAR-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-2001, sequence version 1.
DT 27-MAR-2024, entry version 136.
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=STK_02050;
OS Sulfurisphaera tokodaii (strain DSM 16993 / JCM 10545 / NBRC 100140 / 7)
OS (Sulfolobus tokodaii).
OC Archaea; Thermoproteota; Thermoprotei; Sulfolobales; Sulfolobaceae;
OC Sulfurisphaera.
OX NCBI_TaxID=273063;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 16993 / JCM 10545 / NBRC 100140 / 7;
RX PubMed=11572479; DOI=10.1093/dnares/8.4.123;
RA Kawarabayasi Y., Hino Y., Horikawa H., Jin-no K., Takahashi M., Sekine M.,
RA Baba S., Ankai A., Kosugi H., Hosoyama A., Fukui S., Nagai Y.,
RA Nishijima K., Otsuka R., Nakazawa H., Takamiya M., Kato Y., Yoshizawa T.,
RA Tanaka T., Kudoh Y., Yamazaki J., Kushida N., Oguchi A., Aoki K.,
RA Masuda S., Yanagii M., Nishimura M., Yamagishi A., Oshima T., Kikuchi H.;
RT "Complete genome sequence of an aerobic thermoacidophilic Crenarchaeon,
RT Sulfolobus tokodaii strain7.";
RL DNA Res. 8:123-140(2001).
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). Reaction proceeds in two steps: L-aspartate is first
CC activated by ATP to form Asp-AMP and then transferred to the acceptor
CC end of tRNA(Asp/Asn). {ECO:0000255|HAMAP-Rule:MF_02075}.
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};
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 -!- 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; BA000023; BAK54191.1; -; Genomic_DNA.
DR RefSeq; WP_010978146.1; NC_003106.2.
DR PDB; 1WYD; X-ray; 2.30 A; A/B=1-429.
DR PDBsum; 1WYD; -.
DR AlphaFoldDB; Q976I3; -.
DR SMR; Q976I3; -.
DR STRING; 273063.STK_02050; -.
DR GeneID; 1458094; -.
DR KEGG; sto:STK_02050; -.
DR PATRIC; fig|273063.9.peg.252; -.
DR eggNOG; arCOG00406; Archaea.
DR OrthoDB; 5908at2157; -.
DR EvolutionaryTrace; Q976I3; -.
DR Proteomes; UP000001015; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0004815; F:aspartate-tRNA ligase activity; IEA:UniProtKB-UniRule.
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:0003676; F:nucleic acid binding; IEA:InterPro.
DR GO; GO:0006422; P:aspartyl-tRNA aminoacylation; IEA:UniProtKB-UniRule.
DR CDD; cd00776; AsxRS_core; 1.
DR CDD; cd04316; ND_PkAspRS_like_N; 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 1: Evidence at protein level;
KW 3D-structure; Aminoacyl-tRNA synthetase; ATP-binding; Cytoplasm; Ligase;
KW Magnesium; Metal-binding; Nucleotide-binding; Protein biosynthesis;
KW Reference proteome.
FT CHAIN 1..429
FT /note="Aspartate--tRNA(Asp/Asn) ligase"
FT /id="PRO_0000111007"
FT REGION 189..192
FT /note="Aspartate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02075"
FT BINDING 167
FT /ligand="L-aspartate"
FT /ligand_id="ChEBI:CHEBI:29991"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02075"
FT BINDING 210..212
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02075"
FT BINDING 210
FT /ligand="L-aspartate"
FT /ligand_id="ChEBI:CHEBI:29991"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02075"
FT BINDING 352
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02075"
FT BINDING 352
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02075"
FT BINDING 352
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="3"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02075"
FT BINDING 355
FT /ligand="L-aspartate"
FT /ligand_id="ChEBI:CHEBI:29991"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02075"
FT BINDING 355
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="L-aspartate"
FT /ligand_id="ChEBI:CHEBI:29991"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02075"
FT BINDING 400..403
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02075"
FT SITE 82
FT /note="Important for tRNA non-discrimination"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02075"
FT TURN 7..9
FT /evidence="ECO:0007829|PDB:1WYD"
FT HELIX 12..14
FT /evidence="ECO:0007829|PDB:1WYD"
FT STRAND 18..31
FT /evidence="ECO:0007829|PDB:1WYD"
FT STRAND 34..41
FT /evidence="ECO:0007829|PDB:1WYD"
FT STRAND 44..50
FT /evidence="ECO:0007829|PDB:1WYD"
FT HELIX 57..60
FT /evidence="ECO:0007829|PDB:1WYD"
FT STRAND 68..77
FT /evidence="ECO:0007829|PDB:1WYD"
FT STRAND 79..81
FT /evidence="ECO:0007829|PDB:1WYD"
FT HELIX 82..84
FT /evidence="ECO:0007829|PDB:1WYD"
FT STRAND 85..96
FT /evidence="ECO:0007829|PDB:1WYD"
FT STRAND 106..108
FT /evidence="ECO:0007829|PDB:1WYD"
FT HELIX 114..119
FT /evidence="ECO:0007829|PDB:1WYD"
FT HELIX 121..125
FT /evidence="ECO:0007829|PDB:1WYD"
FT HELIX 128..150
FT /evidence="ECO:0007829|PDB:1WYD"
FT STRAND 160..164
FT /evidence="ECO:0007829|PDB:1WYD"
FT STRAND 174..177
FT /evidence="ECO:0007829|PDB:1WYD"
FT STRAND 180..184
FT /evidence="ECO:0007829|PDB:1WYD"
FT HELIX 189..199
FT /evidence="ECO:0007829|PDB:1WYD"
FT STRAND 200..209
FT /evidence="ECO:0007829|PDB:1WYD"
FT STRAND 216..218
FT /evidence="ECO:0007829|PDB:1WYD"
FT STRAND 221..231
FT /evidence="ECO:0007829|PDB:1WYD"
FT HELIX 235..256
FT /evidence="ECO:0007829|PDB:1WYD"
FT HELIX 258..264
FT /evidence="ECO:0007829|PDB:1WYD"
FT STRAND 276..279
FT /evidence="ECO:0007829|PDB:1WYD"
FT HELIX 280..289
FT /evidence="ECO:0007829|PDB:1WYD"
FT HELIX 302..312
FT /evidence="ECO:0007829|PDB:1WYD"
FT STRAND 315..320
FT /evidence="ECO:0007829|PDB:1WYD"
FT HELIX 324..326
FT /evidence="ECO:0007829|PDB:1WYD"
FT STRAND 340..348
FT /evidence="ECO:0007829|PDB:1WYD"
FT STRAND 351..359
FT /evidence="ECO:0007829|PDB:1WYD"
FT HELIX 363..372
FT /evidence="ECO:0007829|PDB:1WYD"
FT HELIX 377..380
FT /evidence="ECO:0007829|PDB:1WYD"
FT HELIX 381..384
FT /evidence="ECO:0007829|PDB:1WYD"
FT HELIX 385..388
FT /evidence="ECO:0007829|PDB:1WYD"
FT STRAND 394..400
FT /evidence="ECO:0007829|PDB:1WYD"
FT HELIX 401..409
FT /evidence="ECO:0007829|PDB:1WYD"
FT HELIX 414..416
FT /evidence="ECO:0007829|PDB:1WYD"
FT STRAND 418..420
FT /evidence="ECO:0007829|PDB:1WYD"
SQ SEQUENCE 429 AA; 49074 MW; 5BABA8F4D9437D69 CRC64;
MYRSHFIADV TPEYDGKEVI WAGWVHLLRD LGGKKFIILR DKTGLGQVVV DKNSSAFGIS
QELTQESVIQ VRGIVKADKR APRGIELHAE EITLLSKAKA PLPLDVSGKV KADIDTRLRE
RVLDLRRQEM QAVIKIQSLA LKAFRETLYK EGFIEIFTPK IIASATEGGA QLFPVIYFGK
EAFLAQSPQL YKELMAGVVE RVFEVAPAWR AEESDTPFHL AEFISMDVEM AFADYNDVMQ
LLEKILHNIV KTIKEEGKEE LKILNYEPPE VKIPIKRLKY TEAIEILRSK GYNIKFGDDI
GTPELRILNE ELKEDLYFIV DWPSDARPFY TKSKSENPEL SESFDLIYKF LEIVSGSTRN
HKREVLEEAL KKKGLKPESF EFFLKWFDYG MPPHAGFGMG LARLMVMLTG IQSVKEIVPF
PRDKKRLTP
//
