GenomeNet

Database: UniProt
Entry: A0A1S6FHV9_9SPHN
LinkDB: A0A1S6FHV9_9SPHN
Original site: A0A1S6FHV9_9SPHN 
ID   A0A1S6FHV9_9SPHN        Unreviewed;       612 AA.
AC   A0A1S6FHV9;
DT   10-MAY-2017, integrated into UniProtKB/TrEMBL.
DT   10-MAY-2017, sequence version 1.
DT   24-JAN-2024, entry version 29.
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=BXU08_04830 {ECO:0000313|EMBL:AQR73090.1};
OS   Sphingomonas sp. LM7.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Sphingomonadales;
OC   Sphingomonadaceae; Sphingomonas.
OX   NCBI_TaxID=1938607 {ECO:0000313|EMBL:AQR73090.1, ECO:0000313|Proteomes:UP000189383};
RN   [1] {ECO:0000313|EMBL:AQR73090.1, ECO:0000313|Proteomes:UP000189383}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=LM7 {ECO:0000313|EMBL:AQR73090.1,
RC   ECO:0000313|Proteomes:UP000189383};
RA   Hentchel K., Vargas G., Fiebig A., Chen S.L., Coleman M., Crosson S.;
RT   "Genome sequences of bacteria isolated from the littoral zone of southern
RT   Lake Michigan.";
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_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   ---------------------------------------------------------------------------
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; CP019511; AQR73090.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1S6FHV9; -.
DR   STRING; 1938607.BXU08_04830; -.
DR   KEGG; splm:BXU08_04830; -.
DR   OrthoDB; 9802326at2; -.
DR   Proteomes; UP000189383; 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   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:UP000189383}.
FT   DOMAIN          144..562
FT                   /note="Aminoacyl-transfer RNA synthetases class-II family
FT                   profile"
FT                   /evidence="ECO:0000259|PROSITE:PS50862"
FT   REGION          199..202
FT                   /note="Aspartate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00044"
FT   BINDING         175
FT                   /ligand="L-aspartate"
FT                   /ligand_id="ChEBI:CHEBI:29991"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00044"
FT   BINDING         221..223
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00044"
FT   BINDING         221
FT                   /ligand="L-aspartate"
FT                   /ligand_id="ChEBI:CHEBI:29991"
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            33
FT                   /note="Important for tRNA non-discrimination"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00044"
SQ   SEQUENCE   612 AA;  67784 MW;  1D2985EC5D909CB8 CRC64;
     MHAYRSHTCA QLRAANVGEE VRLSGWVHRT REHANVLFVD LRDHYGVTQI VVETTSDLYP
     IVDGCGAESV LTFTGKVAAR SPETLNPKLA TGEIEIYPSD VKVQSAAERL PLPVFGDAEY
     PEEIRLKNRF LDLRRERLHK NIVLRSNVIS SLRQRMISHG FTEFQTPILT ASSPEGARDY
     LVPSRVHPGK FYALPQAPQM FKQLLMVAGF DRYFQIAPCF RDEDARADRS PGEFYQLDFE
     MSFVTQDDVF AAIEPVLHGV FEEFADFDGK GRSVSPLPFK RIPYRESMLK YGSDKPDLRN
     PLLVHDVGDF FKGSGFGRFA SMVEEGNVVR AIAAPNTHEK SRKFFDEMNS WAQSEGFPGL
     GYATQKDGVF GGPIANNHGQ DGMKAIADAM GLGPNDGIFF AAGAEGKAAK LAGLARTRVG
     EQLELIDKSR FEFCWIVDFP MFEADEDTGK IDFSHNPFSM PQGELEALET MDPLDILAFQ
     YDIVCNGVEL SSGAIRNHKP EIMYKAFEIA GYTQADVDTN FAGMINAFKF GAPPHGGSAP
     GVDRIVMLLA DEPNIREVIV FPMTQKAEDL MMQAPSFVSE KQLKELNIRL APQVAADLSK
     KSIDGAVDPA AG
//
DBGET integrated database retrieval system