ID A0A1Q5AXW5_9ACTN Unreviewed; 601 AA.
AC A0A1Q5AXW5;
DT 12-APR-2017, integrated into UniProtKB/TrEMBL.
DT 12-APR-2017, sequence version 1.
DT 24-JAN-2024, entry version 30.
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=A6A27_25730 {ECO:0000313|EMBL:OKI63932.1};
OS Micromonospora sp. CB01531.
OC Bacteria; Actinomycetota; Actinomycetes; Micromonosporales;
OC Micromonosporaceae; Micromonospora.
OX NCBI_TaxID=1718947 {ECO:0000313|EMBL:OKI63932.1, ECO:0000313|Proteomes:UP000186700};
RN [1] {ECO:0000313|EMBL:OKI63932.1, ECO:0000313|Proteomes:UP000186700}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CB01531 {ECO:0000313|EMBL:OKI63932.1,
RC ECO:0000313|Proteomes:UP000186700};
RX PubMed=27999165; DOI=10.1128/mbio.02104-16;
RA Yan X., Ge H., Huang T., Hindra, Yang D., Teng Q., Crnovcic I., Li X.,
RA Rudolf J.D., Lohman J.R., Gansemans Y., Zhu X., Huang Y., Zhao L.X.,
RA Jiang Y., Van Nieuwerburgh F., Rader C., Duan Y., Shen B.;
RT "Strain Prioritization and Genome Mining for Enediyne Natural Products.";
RL MBio 7:e02104-e02116(2016).
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: 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:OKI63932.1}.
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DR EMBL; LWLS01000069; OKI63932.1; -; Genomic_DNA.
DR RefSeq; WP_073835726.1; NZ_LWLS01000069.1.
DR AlphaFoldDB; A0A1Q5AXW5; -.
DR STRING; 1718947.A6A27_25730; -.
DR OrthoDB; 9802326at2; -.
DR Proteomes; UP000186700; 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:UP000186700}.
FT DOMAIN 135..558
FT /note="Aminoacyl-transfer RNA synthetases class-II family
FT profile"
FT /evidence="ECO:0000259|PROSITE:PS50862"
FT REGION 192..195
FT /note="Aspartate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00044"
FT REGION 567..601
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 168
FT /ligand="L-aspartate"
FT /ligand_id="ChEBI:CHEBI:29991"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00044"
FT BINDING 214..216
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00044"
FT BINDING 214
FT /ligand="L-aspartate"
FT /ligand_id="ChEBI:CHEBI:29991"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00044"
FT BINDING 223
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00044"
FT BINDING 443
FT /ligand="L-aspartate"
FT /ligand_id="ChEBI:CHEBI:29991"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00044"
FT BINDING 477
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00044"
FT BINDING 484
FT /ligand="L-aspartate"
FT /ligand_id="ChEBI:CHEBI:29991"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00044"
FT BINDING 529..532
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"
FT SITE 76
FT /note="Important for tRNA non-discrimination"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00044"
SQ SEQUENCE 601 AA; 65535 MW; FBB111527F09131D CRC64;
MIRTHNAGSL RAADAGSTVT LAGWVARRRD HGGVIFVDLR DGSGVVQVVF REEDAHALRN
EFCVKVTGEV TRRPAGNENP DLPTGEVEVT ASELEVLSEA APLPLPVDDQ IEAGDDIRLK
YRYLDLRRSG PARAMRLRSR ANQLARSVLN ERDFLEIETP TLTRSTPEGA RDFLVPVRLQ
PGSWYALPQS PQLFKQLLMV GGMERYYQIA RCYRDEDFRA DRQPEFTQLD IEMSFVTEDD
VIELGEAIVS ALWSDLAGHE ISRPIPRITW HDAMSRYGSD KPDLRYGVEL TELTDYLRGT
EFRVFAGAID AGGYVGAVVM PGGAAQSRKE LDGWQDWAKA RGARGLAYVV LDAETGEARG
PVAKNLSEAH LAGLADAVGA KPGDAVFFAA STNTREAQEL LGAARIEIAK RANLIDETAW
AFCWVVDAPM FERTDEGGWT AVHHPFTSPN ADWVDRFEEA PDRALAYAYD IVCNGNEIGG
GSVRIHRGDV QQRVFDLLGI SPEEAQDKFG FLLEAFKYGP PPHGGIAFGW DRICMLLAGA
DSIREVIAFP KTRGGFDPLT GAPTPITGQQ RAEAGVDAKP KAATGPHAGT AGPVAPVADP
T
//
