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Database: UniProt
Entry: A0A0U1KLT1_9BACI
LinkDB: A0A0U1KLT1_9BACI
Original site: A0A0U1KLT1_9BACI 
ID   A0A0U1KLT1_9BACI        Unreviewed;       592 AA.
AC   A0A0U1KLT1;
DT   17-FEB-2016, integrated into UniProtKB/TrEMBL.
DT   17-FEB-2016, sequence version 1.
DT   24-JAN-2024, entry version 41.
DE   RecName: Full=Aspartate--tRNA ligase {ECO:0000256|HAMAP-Rule:MF_00044};
DE            EC=6.1.1.12 {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};
GN   Name=aspS {ECO:0000256|HAMAP-Rule:MF_00044,
GN   ECO:0000313|EMBL:CQR46940.1};
GN   ORFNames=BN1058_01226 {ECO:0000313|EMBL:CQR46940.1};
OS   Paraliobacillus sp. PM-2.
OC   Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Paraliobacillus.
OX   NCBI_TaxID=1462524 {ECO:0000313|EMBL:CQR46940.1, ECO:0000313|Proteomes:UP000199066};
RN   [1] {ECO:0000313|EMBL:CQR46940.1, ECO:0000313|Proteomes:UP000199066}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=PM-2 {ECO:0000313|EMBL:CQR46940.1,
RC   ECO:0000313|Proteomes:UP000199066};
RA   Murphy D.;
RL   Submitted (MAR-2015) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Catalyzes the attachment of L-aspartate to tRNA(Asp) in a
CC       two-step reaction: L-aspartate is first activated by ATP to form Asp-
CC       AMP and then transferred to the acceptor end of tRNA(Asp).
CC       {ECO:0000256|HAMAP-Rule:MF_00044}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + L-aspartate + tRNA(Asp) = AMP + diphosphate + L-
CC         aspartyl-tRNA(Asp); Xref=Rhea:RHEA:19649, Rhea:RHEA-COMP:9660,
CC         Rhea:RHEA-COMP:9678, ChEBI:CHEBI:29991, ChEBI:CHEBI:30616,
CC         ChEBI:CHEBI:33019, ChEBI:CHEBI:78442, ChEBI:CHEBI:78516,
CC         ChEBI:CHEBI:456215; EC=6.1.1.12; 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: Lacks conserved residue(s) required for the propagation of
CC       feature annotation. {ECO:0000256|HAMAP-Rule:MF_00044}.
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DR   EMBL; CTEI01000001; CQR46940.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0U1KLT1; -.
DR   STRING; 1462524.BN1058_01226; -.
DR   OrthoDB; 9802326at2; -.
DR   Proteomes; UP000199066; 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:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0003676; F:nucleic acid binding; IEA:InterPro.
DR   GO; GO:0016740; F:transferase activity; IEA:UniProt.
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};
KW   Cytoplasm {ECO:0000256|ARBA:ARBA00022490, 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:UP000199066}.
FT   DOMAIN          143..557
FT                   /note="Aminoacyl-transfer RNA synthetases class-II family
FT                   profile"
FT                   /evidence="ECO:0000259|PROSITE:PS50862"
FT   REGION          200..203
FT                   /note="Aspartate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00044"
FT   BINDING         176
FT                   /ligand="L-aspartate"
FT                   /ligand_id="ChEBI:CHEBI:29991"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00044"
FT   BINDING         222..224
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00044"
FT   BINDING         222
FT                   /ligand="L-aspartate"
FT                   /ligand_id="ChEBI:CHEBI:29991"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00044"
FT   BINDING         231
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00044"
FT   BINDING         450
FT                   /ligand="L-aspartate"
FT                   /ligand_id="ChEBI:CHEBI:29991"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00044"
FT   BINDING         484
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00044"
FT   BINDING         491
FT                   /ligand="L-aspartate"
FT                   /ligand_id="ChEBI:CHEBI:29991"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00044"
FT   BINDING         536..539
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00044"
SQ   SEQUENCE   592 AA;  67383 MW;  34F9EBDAD73FBE92 CRC64;
     MQQSRELAGK VRKDDVGKTI CLKGWVQKRR DLGGLIFIDL RDRSGIVQIV FNPTVSEPAL
     AIAETIRSEY VIEVTGQVVE RSNDTVNEKM ATGKVEVVVE GINVLNEAKN PPFSIYEDKD
     ITEELRLKHR YLDLRRQSMQ QTFQLRHQAT QVIRQFLNEE GYLEMETPML TKSTPEGARD
     YLVPSRVHPG HFYALPQSPQ LFKQLIMVAG FERYYQFARC FRDEDLRADR QPEFTQIDIE
     TSFMSSDEII EMTERMMKKT MKEVKGIELA LPFPRLRYEE AMARYGSDKP DTRFDMELID
     VSEIVKDSGF KVFNSTVKSG GKVNAINVKG HATTYSRKDI DKLTEFVNVY GAKGLAWLKV
     ESEGLKGPIA KFFTEEEQRA IAKTLQAETN DLLLFVADKQ SIVYDSLGAL RLKLGKELNL
     IDESQFNFLW VTDWPLLEYD DEAGRYFAAH HPFTMPAYED IDKLSANPEQ VKAQAYDLVL
     NGFELGGGSL RIYKKELQDK MFEILGFSKE EAEEQFSFLL QALEYGTPPH GGIALGFDRL
     VMLLAGKSNL RDTILFPKTA SAMDPLTEAP GTVSDDQLDE LSLVLQNQTD TK
//
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