ID A0A372G6U1_9ACTN Unreviewed; 586 AA. AC A0A372G6U1; DT 07-NOV-2018, integrated into UniProtKB/TrEMBL. DT 07-NOV-2018, sequence version 1. DT 08-MAY-2019, entry version 6. 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. 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 RT Leucetta chagosensis."; RL Submitted (AUG-2018) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Aspartyl-tRNA synthetase with relaxed tRNA specificity CC since it is able to aspartylate not only its cognate tRNA(Asp) but CC also tRNA(Asn). Reaction proceeds in two steps: L-aspartate is CC first activated by ATP to form Asp-AMP and then transferred to the CC acceptor 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 ECO:0000256|SAAS:SAAS00385220}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00044, CC ECO:0000256|SAAS:SAAS00385180}. CC -!- SIMILARITY: Belongs to the class-II aminoacyl-tRNA synthetase CC family. Type 1 subfamily. {ECO:0000256|HAMAP-Rule:MF_00044, CC ECO:0000256|SAAS:SAAS01090900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {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 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; 3.30.1360.30; -; 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; 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 TIGRFAMs; TIGR00459; aspS_bact; 1. DR PROSITE; PS50862; AA_TRNA_LIGASE_II; 1. PE 3: Inferred from homology; KW Aminoacyl-tRNA synthetase {ECO:0000256|HAMAP-Rule:MF_00044, KW ECO:0000256|SAAS:SAAS00462052}; KW ATP-binding {ECO:0000256|HAMAP-Rule:MF_00044, KW ECO:0000256|SAAS:SAAS00461969}; KW Complete proteome {ECO:0000313|Proteomes:UP000262882}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00044, KW ECO:0000256|SAAS:SAAS00461954}; KW Ligase {ECO:0000256|HAMAP-Rule:MF_00044, KW ECO:0000256|SAAS:SAAS00462038, ECO:0000313|EMBL:RFS81108.1}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00044, KW ECO:0000256|SAAS:SAAS00089651}; KW Protein biosynthesis {ECO:0000256|HAMAP-Rule:MF_00044, KW ECO:0000256|SAAS:SAAS00462033}; KW Reference proteome {ECO:0000313|Proteomes:UP000262882}. FT DOMAIN 148 549 AA_TRNA_LIGASE_II. {ECO:0000259|PROSITE: FT PS50862}. FT NP_BIND 215 217 ATP. {ECO:0000256|HAMAP-Rule:MF_00044}. FT NP_BIND 528 531 ATP. {ECO:0000256|HAMAP-Rule:MF_00044}. FT REGION 193 196 Aspartate. {ECO:0000256|HAMAP-Rule: FT MF_00044}. FT BINDING 169 169 Aspartate. {ECO:0000256|HAMAP-Rule: FT MF_00044}. FT BINDING 215 215 Aspartate. {ECO:0000256|HAMAP-Rule: FT MF_00044}. FT BINDING 224 224 ATP. {ECO:0000256|HAMAP-Rule:MF_00044}. FT BINDING 442 442 Aspartate. {ECO:0000256|HAMAP-Rule: FT MF_00044}. FT BINDING 476 476 ATP. {ECO:0000256|HAMAP-Rule:MF_00044}. FT BINDING 483 483 Aspartate. {ECO:0000256|HAMAP-Rule: FT MF_00044}. FT SITE 31 31 Important for tRNA non-discrimination. FT {ECO:0000256|HAMAP-Rule:MF_00044}. FT SITE 77 77 Important for tRNA non-discrimination. FT {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 //