ID   A0A372G6U1_9ACTN        Unreviewed;       586 AA.
AC   A0A372G6U1;
DT   07-NOV-2018, integrated into UniProtKB/TrEMBL.
DT   07-NOV-2018, sequence version 1.
DT   31-JUL-2019, entry version 8.
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}.
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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   REGION      559    586       Disordered. {ECO:0000256|SAM:MobiDB-
FT                                lite}.
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
//