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Database: UniProt
Entry: A0A1N7C1Z6_9EURY
LinkDB: A0A1N7C1Z6_9EURY
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ID   A0A1N7C1Z6_9EURY        Unreviewed;       434 AA.
AC   A0A1N7C1Z6;
DT   15-MAR-2017, integrated into UniProtKB/TrEMBL.
DT   15-MAR-2017, sequence version 1.
DT   24-JAN-2024, entry version 29.
DE   RecName: Full=Aspartate--tRNA(Asp/Asn) ligase {ECO:0000256|HAMAP-Rule:MF_02075};
DE            EC=6.1.1.23 {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};
DE   AltName: Full=Non-discriminating aspartyl-tRNA synthetase {ECO:0000256|HAMAP-Rule:MF_02075};
DE            Short=ND-AspRS {ECO:0000256|HAMAP-Rule:MF_02075};
GN   Name=aspS {ECO:0000256|HAMAP-Rule:MF_02075};
GN   ORFNames=BB347_08750 {ECO:0000313|EMBL:APX96695.1}, SAMN05421809_1469
GN   {ECO:0000313|EMBL:SIR57474.1};
OS   Natronorubrum daqingense.
OC   Archaea; Euryarchaeota; Stenosarchaea group; Halobacteria; Natrialbales;
OC   Natrialbaceae; Natronorubrum.
OX   NCBI_TaxID=588898 {ECO:0000313|EMBL:SIR57474.1, ECO:0000313|Proteomes:UP000185687};
RN   [1] {ECO:0000313|EMBL:APX96695.1, ECO:0000313|Proteomes:UP000187321}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=JX313 {ECO:0000313|EMBL:APX96695.1,
RC   ECO:0000313|Proteomes:UP000187321};
RA   Shuang W.;
RT   "Complete genome sequence of Haloterrigena daqingensis type strain
RT   (JX313T).";
RL   Submitted (JAN-2017) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:SIR57474.1, ECO:0000313|Proteomes:UP000185687}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CGMCC 1.8909 {ECO:0000313|EMBL:SIR57474.1,
RC   ECO:0000313|Proteomes:UP000185687};
RA   Mah S.A., Swanson W.J., Moy G.W., Vacquier V.D.;
RL   Submitted (JAN-2017) to the EMBL/GenBank/DDBJ databases.
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:0000256|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: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}.
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DR   EMBL; CP019327; APX96695.1; -; Genomic_DNA.
DR   EMBL; FTNP01000002; SIR57474.1; -; Genomic_DNA.
DR   RefSeq; WP_076580620.1; NZ_FTNP01000002.1.
DR   AlphaFoldDB; A0A1N7C1Z6; -.
DR   STRING; 588898.BB347_08750; -.
DR   GeneID; 30956027; -.
DR   KEGG; hda:BB347_08750; -.
DR   OrthoDB; 5908at2157; -.
DR   Proteomes; UP000185687; Unassembled WGS sequence.
DR   Proteomes; UP000187321; 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   3: Inferred from homology;
KW   Aminoacyl-tRNA synthetase {ECO:0000256|ARBA:ARBA00023146,
KW   ECO:0000256|HAMAP-Rule:MF_02075};
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|HAMAP-
KW   Rule:MF_02075}; Cytoplasm {ECO:0000256|HAMAP-Rule:MF_02075};
KW   Ligase {ECO:0000256|ARBA:ARBA00022598, ECO:0000256|HAMAP-Rule:MF_02075};
KW   Magnesium {ECO:0000256|HAMAP-Rule:MF_02075};
KW   Metal-binding {ECO:0000256|HAMAP-Rule:MF_02075};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|HAMAP-
KW   Rule:MF_02075}; Protein biosynthesis {ECO:0000256|HAMAP-Rule:MF_02075};
KW   Reference proteome {ECO:0000313|Proteomes:UP000185687}.
FT   DOMAIN          134..434
FT                   /note="Aminoacyl-transfer RNA synthetases class-II family
FT                   profile"
FT                   /evidence="ECO:0000259|PROSITE:PS50862"
FT   REGION          189..192
FT                   /note="Aspartate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_02075"
FT   BINDING         167
FT                   /ligand="L-aspartate"
FT                   /ligand_id="ChEBI:CHEBI:29991"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_02075"
FT   BINDING         211..213
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_02075"
FT   BINDING         211
FT                   /ligand="L-aspartate"
FT                   /ligand_id="ChEBI:CHEBI:29991"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_02075"
FT   BINDING         219..221
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_02075"
FT   BINDING         357
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_02075"
FT   BINDING         357
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_02075"
FT   BINDING         357
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="3"
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         360
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_02075"
FT   BINDING         364
FT                   /ligand="L-aspartate"
FT                   /ligand_id="ChEBI:CHEBI:29991"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_02075"
FT   BINDING         405..408
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_02075"
FT   SITE            82
FT                   /note="Important for tRNA non-discrimination"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_02075"
SQ   SEQUENCE   434 AA;  48604 MW;  CEFB56B073BC8BFE CRC64;
     MQDRIHTADA EPGDDATVAG WVHEIRDLGG IAFLILRDSS GKIQIKFEKD EMDEELVETG
     LSVSRESVVK VSGAVEEEPR APTGVEVTPE ELEVVAPAEP ELPLDPSGKV DAELSTRLDN
     RTLDLRKDEV QAVFEIRAEI LRAVREQFRA FDCTEINTPK IVATGTEGGT ELFPITYFGE
     EAFMNQSPQL FKQLIAGSNV ERVFEIGPIF RAEEHNTPRH LNEATSIDFE GAFCDQNDAM
     DVVEGVVTAA YEAIVENCQD ELEALGLAAE FEVPDEAFPR LSYEEAIERI NATGELDEQL
     VWGDDLPTEG EKALGDDVGG HYFITDWPSE IKPFYIKDHD DDEQLSTGFD LMHPRMELVS
     GGQREHRHEK LIEGFEQQGL DPEQFEYYTK MFKYGMPPHA GFGLGGERLV MTILGLDNIR
     EAVLFPRDRQ RLSP
//
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