ID A0A372G6U1_9ACTN Unreviewed; 586 AA. AC A0A372G6U1; DT 07-NOV-2018, integrated into UniProtKB/TrEMBL. DT 07-NOV-2018, sequence version 1. DT 25-MAY-2022, entry version 16. 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=D0T12_33640 {ECO:0000313|EMBL:RFS81108.1}; OS Actinomadura sp. LHW52907. OC Bacteria; Actinobacteria; Streptosporangiales; Thermomonosporaceae; OC Actinomadura; unclassified Actinomadura. OX NCBI_TaxID=2303421 {ECO:0000313|EMBL:RFS81108.1, ECO:0000313|Proteomes:UP000262882}; RN [1] {ECO:0000313|EMBL:RFS81108.1, ECO:0000313|Proteomes:UP000262882} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=LHW52907 {ECO:0000313|EMBL:RFS81108.1, RC ECO:0000313|Proteomes:UP000262882}; RA Li L., Lin H.W.; RT "Actinomadura spongicola sp. nov., isolated from marine sponge Leucetta RT chagosensis."; RL Submitted (AUG-2018) 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: 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:RFS81108.1}. 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; QVNQ01000016; RFS81108.1; -; Genomic_DNA. DR EnsemblBacteria; RFS81108; RFS81108; D0T12_33640. DR Proteomes; UP000262882; 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 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 {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:UP000262882}. FT DOMAIN 148..549 FT /note="AA_TRNA_LIGASE_II" FT /evidence="ECO:0000259|PROSITE:PS50862" FT NP_BIND 215..217 FT /note="ATP" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00044" FT NP_BIND 528..531 FT /note="ATP" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00044" FT REGION 193..196 FT /note="Aspartate" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00044" FT REGION 559..586 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT BINDING 169 FT /note="Aspartate" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00044" FT BINDING 215 FT /note="Aspartate" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00044" FT BINDING 224 FT /note="ATP" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00044" FT BINDING 442 FT /note="Aspartate" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00044" FT BINDING 476 FT /note="ATP" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00044" FT BINDING 483 FT /note="Aspartate" 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 77 FT /note="Important for tRNA non-discrimination" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00044" SQ SEQUENCE 586 AA; 65085 MW; 36F9A99F0DA99CE6 CRC64; MIRSHEAGTL RREHAGRQVT LAGWVGRRRD HGGVTFIDLR DASGVAQVVF REEDTAHDLR SEFCVKVVGE VRVRPEGNEN PELPTGDVEV AATDIEVLSD AAPLPFPIEG DVNVNEEIRL KYRYLDLRRD AVARAMRIRS EASFLTHEVM REHGFVNVET PTLTRSTPEG ARDFLVPVRL QPGHWYALPQ SPQLFKQLLM VGGLERYYQI ARCYRDEDFR ADRQPEFTQI DIEMSFCDQA DVQTVGEDLV ARLWKEIAGY EIPRPIPHIT YADAMARYGS DKPDLRFGVE LTDMTEYFAQ TSFRVFQAPY VGAVVMPGGA SQTRRELDAW QDWAKARGAR GLAYVLVQDD GTLGGPVAKN LSDTEKSGLA AKVGASPGDA VFFGAGRRHA TQELLGAARL EIGRRRDLID ETAWEFVWVV DAPIFEPVED DRGEQVGWTS VHHPFTAPKP EFADTFQDDP GGALANAYDL VLNGTEIGGG SIRIHRAEMQ QRVFDVLGLS KEEAESKFGF LLEAFKFGPP PHGGIAFGWD RIVMLLARQD SIRDVIAFPK AASGYDPLTA APTPITPQQR AEAGVDVIPE DEPAES //