ID W6K2L8_9MICO Unreviewed; 611 AA.
AC W6K2L8;
DT 16-APR-2014, integrated into UniProtKB/TrEMBL.
DT 16-APR-2014, sequence version 1.
DT 24-JAN-2024, entry version 51.
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 ECO:0000313|EMBL:CCH75396.1};
GN ORFNames=BN11_680002 {ECO:0000313|EMBL:CCH75396.1};
OS Tetrasphaera australiensis Ben110.
OC Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Intrasporangiaceae;
OC Tetrasphaera.
OX NCBI_TaxID=1193182 {ECO:0000313|EMBL:CCH75396.1, ECO:0000313|Proteomes:UP000035763};
RN [1] {ECO:0000313|EMBL:CCH75396.1, ECO:0000313|Proteomes:UP000035763}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Ben110 {ECO:0000313|EMBL:CCH75396.1,
RC ECO:0000313|Proteomes:UP000035763};
RX PubMed=23178666; DOI=10.1038/ismej.2012.136;
RA Kristiansen R., Nguyen H.T.T., Saunders A.M., Nielsen J.L., Wimmer R.,
RA Le V.Q., McIlroy S.J., Petrovski S., Seviour R.J., Calteau A.,
RA Nielsen K.L., Nielsen P.H.;
RT "A metabolic model for members of the genus Tetrasphaera involved in
RT enhanced biological phosphorus removal.";
RL ISME J. 7:543-554(2013).
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:CCH75396.1}.
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DR EMBL; CAJA01000494; CCH75396.1; -; Genomic_DNA.
DR RefSeq; WP_048695850.1; NZ_HG764815.1.
DR AlphaFoldDB; W6K2L8; -.
DR STRING; 1193182.BN11_680002; -.
DR OrthoDB; 9802326at2; -.
DR Proteomes; UP000035763; 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:UP000035763}.
FT DOMAIN 142..560
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 REGION 564..611
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
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 230
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00044"
FT BINDING 453
FT /ligand="L-aspartate"
FT /ligand_id="ChEBI:CHEBI:29991"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00044"
FT BINDING 487
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00044"
FT BINDING 494
FT /ligand="L-aspartate"
FT /ligand_id="ChEBI:CHEBI:29991"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00044"
FT BINDING 539..542
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00044"
FT SITE 31
FT /note="Important for tRNA non-discrimination"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00044"
SQ SEQUENCE 611 AA; 66328 MW; 4B2FD66AD3F72B47 CRC64;
MLRTHHAGAL RAEQIDQTVT LTGWVAKRRD HGGVAFIDLR DASGVVQVVA RDEVLTGAAH
DLRNEFCVKV TGTVIARGEH NVNPDLPTGE IEVVASAIEV LSPSDVLPFQ IDERVTVGEE
ARLKHRYLDL RRPGTHSAGH ALRLRSRVNA AARKVLGERD FVEIETPTLT RSTPEGARDF
LVPARLAPGS WYALPQSPQL FKQLLMVAGM ERYYQIARCY RDEDFRADRQ PEFTQLDIEM
SFVTQDDIIE LGEALAKEIW SLIGVELETP FLRMPYAEAM ARFGTDKPDL RFGQELTDCT
DFFADTTFRV FQAPYVGAVV MPGGASQPRK TLDAWQEFAK QRGAKGLAYV LVQEDGSLTG
PVAKNLSEAE TGRLAGHVGA EPGDCILFAA GEAKPSRSLL GATRLEIGKR CGLIDEDAWS
LLWVLDAPLF EPASEAVAAG DVAVGGGAWT AVHHAFTSPQ EQFLDTLESD PGSALAYAYD
MVCNGNEIGG GSIRIHRRDI QERVFAIMGL TPEQAQEKFG FLLDAFKFGA PPHGGIAFGW
DRIVMLLGGY DSIRDVIAFP KSGGGYDPLT DAPAPITPEQ RKEAGIDAKP SDANPREAGP
GEAASGPAPQ A
//
