SYDND_NOSP7
ID SYDND_NOSP7 Reviewed; 595 AA.
AC B2J116;
DT 24-MAR-2009, integrated into UniProtKB/Swiss-Prot.
DT 10-JUN-2008, sequence version 1.
DT 03-AUG-2022, entry version 78.
DE RecName: Full=Aspartate--tRNA(Asp/Asn) ligase {ECO:0000255|HAMAP-Rule:MF_00044};
DE EC=6.1.1.23 {ECO:0000255|HAMAP-Rule:MF_00044};
DE AltName: Full=Aspartyl-tRNA synthetase {ECO:0000255|HAMAP-Rule:MF_00044};
DE Short=AspRS {ECO:0000255|HAMAP-Rule:MF_00044};
DE AltName: Full=Non-discriminating aspartyl-tRNA synthetase {ECO:0000255|HAMAP-Rule:MF_00044};
DE Short=ND-AspRS {ECO:0000255|HAMAP-Rule:MF_00044};
GN Name=aspS {ECO:0000255|HAMAP-Rule:MF_00044}; OrderedLocusNames=Npun_F3458;
OS Nostoc punctiforme (strain ATCC 29133 / PCC 73102).
OC Bacteria; Cyanobacteria; Nostocales; Nostocaceae; Nostoc.
OX NCBI_TaxID=63737;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 29133 / PCC 73102;
RG US DOE Joint Genome Institute;
RA Copeland A., Lucas S., Lapidus A., Glavina del Rio T., Dalin E., Tice H.,
RA Pitluck S., Chain P., Malfatti S., Shin M., Vergez L., Schmutz J.,
RA Larimer F., Land M., Hauser L., Kyrpides N., Kim E., Meeks J.C., Elhai J.,
RA Campbell E.L., Thiel T., Longmire J., Potts M., Atlas R.;
RT "Complete sequence of chromosome of Nostoc punctiforme ATCC 29133.";
RL Submitted (APR-2008) 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: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; CP001037; ACC81867.1; -; Genomic_DNA.
DR RefSeq; WP_012409841.1; NC_010628.1.
DR AlphaFoldDB; B2J116; -.
DR SMR; B2J116; -.
DR STRING; 63737.Npun_F3458; -.
DR EnsemblBacteria; ACC81867; ACC81867; Npun_F3458.
DR KEGG; npu:Npun_F3458; -.
DR eggNOG; COG0173; Bacteria.
DR HOGENOM; CLU_014330_3_2_3; -.
DR OMA; YQLDVEM; -.
DR OrthoDB; 226836at2; -.
DR PhylomeDB; B2J116; -.
DR Proteomes; UP000001191; 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..595
FT /note="Aspartate--tRNA(Asp/Asn) ligase"
FT /id="PRO_1000091019"
FT REGION 202..205
FT /note="Aspartate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00044"
FT BINDING 178
FT /ligand="L-aspartate"
FT /ligand_id="ChEBI:CHEBI:29991"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00044"
FT BINDING 224..226
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00044"
FT BINDING 224
FT /ligand="L-aspartate"
FT /ligand_id="ChEBI:CHEBI:29991"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00044"
FT BINDING 233
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00044"
FT BINDING 458
FT /ligand="L-aspartate"
FT /ligand_id="ChEBI:CHEBI:29991"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00044"
FT BINDING 488
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00044"
FT BINDING 495
FT /ligand="L-aspartate"
FT /ligand_id="ChEBI:CHEBI:29991"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00044"
FT BINDING 540..543
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00044"
FT SITE 30
FT /note="Important for tRNA non-discrimination"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00044"
SQ SEQUENCE 595 AA; 67664 MW; B42B64837DB0FEFE CRC64;
MRTHYCGELR KEHIGETVTF YGWVDRRRDH GGVVFLDLRD RSGIVQIVSD PQRTPDSYEQ
ANALRNEYVV EITGRVTQRP EESLNTRIPT GEVEIYADKI KLLNAVGKQL PFQVSVADTE
TVREDLRLKY RYLDLRRERM AQNLQLRHQI VKAMRRYLED LEGFIEVETP ILTRSTPEGA
RDYVLPSRVN PGEWYALPQS PQLFKQLLMV SGLDRYYQIA RCFRDEDLRA DRQPEFTQLD
MEMSFMSQEE IIELNESLVC HIFKTVKGIE LQRPFLRLTY AEGMERYGSD KPDTRYGLEL
VDVSDIVKDS GFKVFRDTVT NGGIVKILPI PNGNDVISNV RIKPGGDLFK EASEAGAKGL
AYIRVRDDGE IDTIGAIKDN LSEEQKQEIL RRTGAKAGHL LLFGAGEAAT VNKTLDRLRQ
AIAREFNLID PDKINLLWIT DFPMFEWNAD EKRLEALHHP FTAPHPDDLS DLKTARAQAY
DLVLNGVEVG GGSLRIYQRE IQQQVFEAIG LSPEEAQSKF GFLLEAFEYG TPPHGGIAYG
LDRLVMLLAG EESIRDVIAF PKTQQARCLL TDAPSSVDAK QLKELHVAST YKPKS
