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Database: UniProt
Entry: W9VLQ9_9GAMM
LinkDB: W9VLQ9_9GAMM
Original site: W9VLQ9_9GAMM 
ID   W9VLQ9_9GAMM            Unreviewed;       587 AA.
AC   W9VLQ9;
DT   14-MAY-2014, integrated into UniProtKB/TrEMBL.
DT   14-MAY-2014, sequence version 1.
DT   24-JAN-2024, entry version 49.
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:EXJ11465.1};
GN   ORFNames=D791_01597 {ECO:0000313|EMBL:EXJ11465.1};
OS   Nitrincola nitratireducens.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Oceanospirillales;
OC   Oceanospirillaceae; Nitrincola.
OX   NCBI_TaxID=1229521 {ECO:0000313|EMBL:EXJ11465.1, ECO:0000313|Proteomes:UP000019464};
RN   [1] {ECO:0000313|Proteomes:UP000019464}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=AK23 {ECO:0000313|Proteomes:UP000019464};
RA   Singh A., Pinnaka A.K., Vaidya B.;
RL   Submitted (NOV-2012) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:EXJ11465.1, ECO:0000313|Proteomes:UP000019464}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=AK23 {ECO:0000313|EMBL:EXJ11465.1,
RC   ECO:0000313|Proteomes:UP000019464};
RX   PubMed=26481633; DOI=10.1016/j.syapm.2015.09.002;
RA   Singh A., Vaidya B., Tanuku N.R., Pinnaka A.K.;
RT   "Nitrincola nitratireducens sp. nov. isolated from a haloalkaline crater
RT   lake.";
RL   Syst. Appl. Microbiol. 38:555-562(2015).
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:EXJ11465.1}.
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DR   EMBL; AONB01000006; EXJ11465.1; -; Genomic_DNA.
DR   RefSeq; WP_036509741.1; NZ_AONB01000006.1.
DR   AlphaFoldDB; W9VLQ9; -.
DR   STRING; 1229521.D791_01597; -.
DR   PATRIC; fig|1229521.3.peg.1621; -.
DR   OrthoDB; 9802326at2; -.
DR   Proteomes; UP000019464; 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}.
FT   DOMAIN          140..555
FT                   /note="Aminoacyl-transfer RNA synthetases class-II family
FT                   profile"
FT                   /evidence="ECO:0000259|PROSITE:PS50862"
FT   REGION          197..200
FT                   /note="Aspartate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00044"
FT   BINDING         173
FT                   /ligand="L-aspartate"
FT                   /ligand_id="ChEBI:CHEBI:29991"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00044"
FT   BINDING         219..221
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00044"
FT   BINDING         219
FT                   /ligand="L-aspartate"
FT                   /ligand_id="ChEBI:CHEBI:29991"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00044"
FT   BINDING         228
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00044"
FT   BINDING         449
FT                   /ligand="L-aspartate"
FT                   /ligand_id="ChEBI:CHEBI:29991"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00044"
FT   BINDING         482
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00044"
FT   BINDING         489
FT                   /ligand="L-aspartate"
FT                   /ligand_id="ChEBI:CHEBI:29991"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00044"
FT   BINDING         534..537
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00044"
FT   SITE            30
FT                   /note="Important for tRNA non-discrimination"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00044"
FT   SITE            81
FT                   /note="Important for tRNA non-discrimination"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00044"
SQ   SEQUENCE   587 AA;  66007 MW;  82C400B39115E5FF CRC64;
     MRSHYCGDLR KEHIGQDITL MGWVHRRRDH GGVIFLDVRD REGITQVVFD PDRHESFKLA
     DSVRNEYVIE LRGSVRARPA GTENKDMPTG DIEVLGKELR ILNKSDTPPF QLDEHQQVGE
     DVRLRNRFID LRRPEIQRKL RFRSQITHYI RNYLENNGFI DIETPILTRA TPEGARDYLV
     PSRTHEGHFF ALPQSPQLFK QLLMVSGFDR YYQIAKCFRD EDLRADRQPE FTQIDIETSF
     LSEDEIIAIT ETMIRGLFSE LLNVELGDFP HMPYSEAMQR YGSDKPDLRF PMELVDVADL
     VAAVDFKVFA APAQDPNGRV AALNVPGGAE LTRKQIDDYT KFVSIYGAKG LAWIKVNDLA
     QGAEGLQSPI VKFLGEDVAL KIMERVGAKN GDLVFFGADK AKVVNEALGA LRLKVGEDLK
     MHQCEWAPLW VVDFPMFEDD GKGGLTALHH PFTSPNCTPA ELIEQPEGKL SRAYDMVLNG
     TELGGGSVRI HDQEMQRAVF KVLGITDEEA EEKFGFLLNA LRYGAPPHGG LAFGLDRLVM
     LMTGSSSIRE VIAFPKTQSA ACLLTDAPGE VSAAQLRELN IKVRKAP
//
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