SYDND_MAGSA
ID SYDND_MAGSA Reviewed; 876 AA.
AC Q2W3D5;
DT 16-MAY-2006, integrated into UniProtKB/Swiss-Prot.
DT 10-JAN-2006, sequence version 1.
DT 03-AUG-2022, entry version 105.
DE RecName: Full=Aspartate--tRNA(Asp/Asn) ligase;
DE EC=6.1.1.23;
DE AltName: Full=Aspartyl-tRNA synthetase;
DE Short=AspRS;
DE AltName: Full=Non-discriminating aspartyl-tRNA synthetase;
DE Short=ND-AspRS;
GN Name=aspS; OrderedLocusNames=amb2837;
OS Magnetospirillum magneticum (strain AMB-1 / ATCC 700264).
OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhodospirillales;
OC Rhodospirillaceae; Magnetospirillum.
OX NCBI_TaxID=342108;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AMB-1 / ATCC 700264;
RX PubMed=16303747; DOI=10.1093/dnares/dsi002;
RA Matsunaga T., Okamura Y., Fukuda Y., Wahyudi A.T., Murase Y., Takeyama H.;
RT "Complete genome sequence of the facultative anaerobic magnetotactic
RT bacterium Magnetospirillum sp. strain AMB-1.";
RL DNA Res. 12:157-166(2005).
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_00044}.
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_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; AP007255; BAE51640.1; -; Genomic_DNA.
DR AlphaFoldDB; Q2W3D5; -.
DR SMR; Q2W3D5; -.
DR STRING; 342108.amb2837; -.
DR EnsemblBacteria; BAE51640; BAE51640; amb2837.
DR KEGG; mag:amb2837; -.
DR HOGENOM; CLU_328120_0_0_5; -.
DR OMA; DWPLLEW; -.
DR Proteomes; UP000007058; 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:0003676; F:nucleic acid binding; IEA:InterPro.
DR GO; GO:0006422; P:aspartyl-tRNA aminoacylation; IEA:UniProtKB-UniRule.
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 3: Inferred from homology;
KW Aminoacyl-tRNA synthetase; ATP-binding; Cytoplasm; Ligase;
KW Nucleotide-binding; Protein biosynthesis; Reference proteome.
FT CHAIN 1..876
FT /note="Aspartate--tRNA(Asp/Asn) ligase"
FT /id="PRO_0000235533"
FT REGION 1..278
FT /note="Unknown"
FT REGION 279..876
FT /note="Aspartyl-tRNA synthetase"
FT REGION 477..480
FT /note="Aspartate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00044"
FT BINDING 453
FT /ligand="L-aspartate"
FT /ligand_id="ChEBI:CHEBI:29991"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00044"
FT BINDING 499..501
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00044"
FT BINDING 499
FT /ligand="L-aspartate"
FT /ligand_id="ChEBI:CHEBI:29991"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00044"
FT BINDING 729
FT /ligand="L-aspartate"
FT /ligand_id="ChEBI:CHEBI:29991"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00044"
FT BINDING 763
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00044"
FT BINDING 770
FT /ligand="L-aspartate"
FT /ligand_id="ChEBI:CHEBI:29991"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00044"
FT BINDING 815..818
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00044"
FT SITE 311
FT /note="Important for tRNA non-discrimination"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00044"
SQ SEQUENCE 876 AA; 97040 MW; 0352C2B2DEEF5B74 CRC64;
MAATDTPWRP FRQAGALRRP MIDPAFVQGH PAYPDAFAQF FAGHGRYGHF AERVGNRNSR
NGWRRRALAP GPAVGAEIVA RHHEAAAQAG QGGDAARHQH RVDRLGQHHV RAAFEQVGRH
FRLRGRSEHD RHRKGIVGAD SPAHPPHQIA RLLHAEIRVH HQKVDHFRPE VVFGIVAVVK
AQQIPASQHA KGAGDDITAA EVEIAQQGAH TWGVVGHGLP SWQERTTFWP PAFRSPSDRS
ATSEFVAGLV NIGLSRLDKI WPGMPSSRFG FKRAYEGFMH VYRSHTCGQL KAADAGIQAR
LSGWVHRKRD HGNLLFVDLR DHYGITQCVI DVSSPVFAAL DKARPESVIT VTGKVVKRSA
ETINPRLPTG EIELQVAEVE IQSIADVLPI QVAGDQEYPE DMRLRYRFLD LRREDVHANM
MLRSRVIAYL RQAMIGQGFT EFQTPILTAS SPEGARDYLV PSRIHPGKFY ALPQAPQQFK
QLLMVAGFDK YFQIAPCFRD EAGRADRSPG EFYQLDFEMS YVTQDDVFAA IEPVLEGVFK
EFGKGRAVTP APFPRITYAD SMLKYGSDKP DLRNPIIIAD VTEPFRGSGF GLFAKLVDKG
AVVRAIPAPG AAGQPRSWFD KLNDWARENG AGGLGYIQFA ADGPKGPIAK NLEPARVEAI
KAAANLKDGD AVFFACDKAL PAAKFAGLVR TKIGNELDLL EKDVFKFCWT VDFPMYEINE
ETGLVEFSHN PFSMPQGGMD ALLNQDPLTI NAYQYDIVCN GVELSSGAIR NHRPDIMYKA
FEIAGYSAAH VEEHFGGMLN AFKFGAPPHG GSAPGVDRIV MLLADQPNIR EIILFPMNQQ
AQDLLMQAPA EIAMERLREL HIKVDLPKPK KEVKEG
