ID G4RPV9_THETK Unreviewed; 430 AA.
AC G4RPV9;
DT 14-DEC-2011, integrated into UniProtKB/TrEMBL.
DT 14-DEC-2011, sequence version 1.
DT 27-MAR-2024, entry version 66.
DE RecName: Full=Aspartate--tRNA ligase {ECO:0000256|HAMAP-Rule:MF_02075};
DE EC=6.1.1.12 {ECO:0000256|HAMAP-Rule:MF_02075};
DE AltName: Full=Aspartyl-tRNA synthetase {ECO:0000256|HAMAP-Rule:MF_02075};
DE Short=AspRS {ECO:0000256|HAMAP-Rule:MF_02075};
GN Name=aspS {ECO:0000256|HAMAP-Rule:MF_02075,
GN ECO:0000313|EMBL:CCC81604.1};
GN OrderedLocusNames=TTX_0953 {ECO:0000313|EMBL:CCC81604.1};
OS Thermoproteus tenax (strain ATCC 35583 / DSM 2078 / JCM 9277 / NBRC 100435
OS / Kra 1).
OC Archaea; Thermoproteota; Thermoprotei; Thermoproteales; Thermoproteaceae;
OC Thermoproteus.
OX NCBI_TaxID=768679 {ECO:0000313|EMBL:CCC81604.1, ECO:0000313|Proteomes:UP000002654};
RN [1] {ECO:0000313|EMBL:CCC81604.1, ECO:0000313|Proteomes:UP000002654}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 35583 / DSM 2078 / JCM 9277 / NBRC 100435 / Kra 1
RC {ECO:0000313|Proteomes:UP000002654};
RX PubMed=22003381; DOI=10.1371/journal.pone.0024222;
RA Siebers B., Zaparty M., Raddatz G., Tjaden B., Albers S.V., Bell S.D.,
RA Blombach F., Kletzin A., Kyrpides N., Lanz C., Plagens A., Rampp M.,
RA Rosinus A., von Jan M., Makarova K.S., Klenk H.P., Schuster S.C.,
RA Hensel R.;
RT "The complete genome sequence of Thermoproteus tenax: a physiologically
RT versatile member of the Crenarchaeota.";
RL PLoS ONE 6:E24222-E24222(2011).
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).
CC {ECO:0000256|HAMAP-Rule:MF_02075}.
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:0000256|HAMAP-
CC Rule:MF_02075};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000256|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:0000256|HAMAP-
CC Rule:MF_02075};
CC -!- SUBUNIT: Homodimer. {ECO:0000256|HAMAP-Rule:MF_02075}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_02075}.
CC -!- SIMILARITY: Belongs to the class-II aminoacyl-tRNA synthetase family.
CC Type 2 subfamily. {ECO:0000256|ARBA:ARBA00005312, ECO:0000256|HAMAP-
CC Rule:MF_02075}.
CC -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC feature annotation. {ECO:0000256|HAMAP-Rule:MF_02075}.
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 EMBL; FN869859; CCC81604.1; -; Genomic_DNA.
DR RefSeq; WP_014126860.1; NC_016070.1.
DR AlphaFoldDB; G4RPV9; -.
DR STRING; 768679.TTX_0953; -.
DR PaxDb; 768679-TTX_0953; -.
DR GeneID; 11261846; -.
DR KEGG; ttn:TTX_0953; -.
DR PATRIC; fig|768679.9.peg.962; -.
DR eggNOG; arCOG00406; Archaea.
DR HOGENOM; CLU_004553_2_1_2; -.
DR OrthoDB; 5908at2157; -.
DR Proteomes; UP000002654; 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: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 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 Aminoacyl-tRNA synthetase {ECO:0000256|HAMAP-Rule:MF_02075};
KW ATP-binding {ECO:0000256|HAMAP-Rule:MF_02075};
KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_02075};
KW Ligase {ECO:0000256|HAMAP-Rule:MF_02075, ECO:0000313|EMBL:CCC81604.1};
KW Magnesium {ECO:0000256|HAMAP-Rule:MF_02075};
KW Metal-binding {ECO:0000256|HAMAP-Rule:MF_02075};
KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_02075};
KW Protein biosynthesis {ECO:0000256|HAMAP-Rule:MF_02075};
KW Reference proteome {ECO:0000313|Proteomes:UP000002654}.
FT DOMAIN 136..430
FT /note="Aminoacyl-transfer RNA synthetases class-II family
FT profile"
FT /evidence="ECO:0000259|PROSITE:PS50862"
FT REGION 191..194
FT /note="Aspartate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02075"
FT BINDING 169
FT /ligand="L-aspartate"
FT /ligand_id="ChEBI:CHEBI:29991"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02075"
FT BINDING 212..214
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02075"
FT BINDING 212
FT /ligand="L-aspartate"
FT /ligand_id="ChEBI:CHEBI:29991"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02075"
FT BINDING 353
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02075"
FT BINDING 353
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02075"
FT BINDING 353
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="3"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02075"
FT BINDING 356
FT /ligand="L-aspartate"
FT /ligand_id="ChEBI:CHEBI:29991"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02075"
FT BINDING 356
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02075"
FT BINDING 360
FT /ligand="L-aspartate"
FT /ligand_id="ChEBI:CHEBI:29991"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02075"
FT BINDING 401..404
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02075"
SQ SEQUENCE 430 AA; 49277 MW; C10F27D611C48364 CRC64;
MPQKTHFTSE ITPDLDGREV ALAGWVWEIR DLGKVKFVIL RDRDGMIQLT FKPGKTPESL
LELVSSLNKE DVIAVRGIVA ASKIARAGVE VFPQELSILA KAKPLPVDIW NNTSDLPTRL
KYRAVDLKNP RNLAIFTLAS EILRAIRDTL YRHKFIEVFT PKIISTSTEG GAELFTVLYF
ERVAYLAQSP QLYKEQLTAS LERVFEIAPA YRAERHNTDY HLNEFISIDG EAAFMNYRDI
MDVLEDLMRS VVSVVKSRED RLKRWGLRPA LEDVSGIPRV EYEEALAKLR SLGYDVKWGD
DLNVEMQRAL MKYYGPLYFI TDFPADLRPF YTKRSEEDPK KSESYDLILN GIEIVSGATR
VHTREVLEAE MRRRSLDPSA FEGHLSVFDW GMPPHAGFGL GFNRLLMALL GLENVREAVL
YPRDRYRLEP
//
