ID A0A1Y4GN45_9BACT Unreviewed; 595 AA.
AC A0A1Y4GN45;
DT 30-AUG-2017, integrated into UniProtKB/TrEMBL.
DT 30-AUG-2017, sequence version 1.
DT 24-JAN-2024, entry version 28.
DE RecName: Full=Aspartate--tRNA(Asp/Asn) ligase {ECO:0000256|HAMAP-Rule:MF_00044};
DE EC=6.1.1.23 {ECO:0000256|HAMAP-Rule:MF_00044};
DE AltName: Full=Aspartyl-tRNA synthetase {ECO:0000256|HAMAP-Rule:MF_00044};
DE Short=AspRS {ECO:0000256|HAMAP-Rule:MF_00044};
DE AltName: Full=Non-discriminating aspartyl-tRNA synthetase {ECO:0000256|HAMAP-Rule:MF_00044};
DE Short=ND-AspRS {ECO:0000256|HAMAP-Rule:MF_00044};
GN Name=aspS {ECO:0000256|HAMAP-Rule:MF_00044};
GN ORFNames=B5F39_05725 {ECO:0000313|EMBL:OUO93681.1};
OS Cloacibacillus sp. An23.
OC Bacteria; Synergistota; Synergistia; Synergistales; Synergistaceae;
OC Cloacibacillus.
OX NCBI_TaxID=1965591 {ECO:0000313|EMBL:OUO93681.1, ECO:0000313|Proteomes:UP000196418};
RN [1] {ECO:0000313|Proteomes:UP000196418}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=An23 {ECO:0000313|Proteomes:UP000196418};
RA Medvecky M., Cejkova D., Polansky O., Karasova D., Kubasova T., Cizek A.,
RA Rychlik I.;
RT "Function of individual gut microbiota members based on whole genome
RT sequencing of pure cultures obtained from chicken caecum.";
RL Submitted (APR-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_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:0000256|HAMAP-
CC Rule:MF_00044};
CC -!- SUBUNIT: Homodimer. {ECO:0000256|HAMAP-Rule:MF_00044}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00044}.
CC -!- SIMILARITY: Belongs to the class-II aminoacyl-tRNA synthetase family.
CC Type 1 subfamily. {ECO:0000256|ARBA:ARBA00006303, ECO:0000256|HAMAP-
CC Rule:MF_00044}.
CC -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC feature annotation. {ECO:0000256|HAMAP-Rule:MF_00044}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:OUO93681.1}.
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DR EMBL; NFJQ01000005; OUO93681.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1Y4GN45; -.
DR OrthoDB; 9802326at2; -.
DR Proteomes; UP000196418; Unassembled WGS sequence.
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 CDD; cd00777; AspRS_core; 1.
DR CDD; cd04317; EcAspRS_like_N; 1.
DR Gene3D; 3.30.1360.30; GAD-like domain; 1.
DR Gene3D; 2.40.50.140; Nucleic acid-binding proteins; 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; IPR047089; Asp-tRNA-ligase_1_N.
DR InterPro; IPR002312; Asp/Asn-tRNA-synth_IIb.
DR InterPro; IPR047090; AspRS_core.
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 NCBIfam; TIGR00459; aspS_bact; 1.
DR PANTHER; PTHR22594:SF5; ASPARTATE--TRNA LIGASE, MITOCHONDRIAL; 1.
DR PANTHER; PTHR22594; ASPARTYL/LYSYL-TRNA SYNTHETASE; 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; SSF55681; Class II aaRS and biotin synthetases; 1.
DR SUPFAM; SSF55261; GAD domain-like; 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_00044};
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|HAMAP-
KW Rule:MF_00044}; Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00044};
KW Ligase {ECO:0000256|ARBA:ARBA00022598, ECO:0000256|HAMAP-Rule:MF_00044};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|HAMAP-
KW Rule:MF_00044};
KW Protein biosynthesis {ECO:0000256|ARBA:ARBA00022917, ECO:0000256|HAMAP-
KW Rule:MF_00044}; Reference proteome {ECO:0000313|Proteomes:UP000196418}.
FT DOMAIN 156..562
FT /note="Aminoacyl-transfer RNA synthetases class-II family
FT profile"
FT /evidence="ECO:0000259|PROSITE:PS50862"
FT REGION 207..210
FT /note="Aspartate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00044"
FT BINDING 183
FT /ligand="L-aspartate"
FT /ligand_id="ChEBI:CHEBI:29991"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00044"
FT BINDING 229..231
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00044"
FT BINDING 229
FT /ligand="L-aspartate"
FT /ligand_id="ChEBI:CHEBI:29991"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00044"
FT BINDING 238
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00044"
FT BINDING 455
FT /ligand="L-aspartate"
FT /ligand_id="ChEBI:CHEBI:29991"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00044"
FT BINDING 489
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00044"
FT BINDING 496
FT /ligand="L-aspartate"
FT /ligand_id="ChEBI:CHEBI:29991"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00044"
FT BINDING 541..544
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00044"
FT SITE 91
FT /note="Important for tRNA non-discrimination"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00044"
SQ SEQUENCE 595 AA; 67408 MW; 16420EAA63EED198 CRC64;
MERYFDASWR RTMYCGTPRL EDAGKKAVLN GWLRCRRDLG GIIFIELWDK TGVTQIVFNP
ELNADAHERA GALRSEYVLA VKGTLRKRPE GTENPELATG EVELMVEDFI VLAPSKLPPF
ELDNADEVNE DLRMKYRYLD IRRDSMQKNL KTRHDVTRYT RNYFADNGFI EIETPMLTKS
TPEGARDYLV PSRVNPGCFY ALPQSPQLFK QLLMVGGCDR YMQIAKCFRD EDLRADRQPE
FTQLDLEMSF ITEEDIMTLV ENYLAGLFKE INGVEVKTPF LRMTWDEAMN KYGIDKPDMR
IPMEMVSLEE VFRDGENPFA QLVANGGTIK GLRLPGGATL SRKELSELEG RAKSLGAKGM
ANFLVKEGEL KGPLVKFLSE EQLAKLRELS AIENGDALFI MADESWRKAC EILGQIRLEL
GRARGMVEAG FRFLWVTEFP LFEWDDESGR YTAVHHPFTA PMDEDVEHLL TEPGKVRSRA
YDVVLNGTEL GGGSIRIHNP EMQQLAFRAL NFTPEAAKER FGFLLEGLSY GTPPHGGLAI
GLDRLVMLMT GSKSIRDVMA FPKNQKAQCP MTEAPSEVEP KQLEELSIKV VEPLA
//
