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Database: UniProt
Entry: A0A0U4WEK2_9GAMM
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ID   A0A0U4WEK2_9GAMM        Unreviewed;       466 AA.
AC   A0A0U4WEK2;
DT   16-MAR-2016, integrated into UniProtKB/TrEMBL.
DT   16-MAR-2016, sequence version 1.
DT   27-MAR-2024, entry version 35.
DE   RecName: Full=Asparagine--tRNA ligase {ECO:0000256|HAMAP-Rule:MF_00534};
DE            EC=6.1.1.22 {ECO:0000256|HAMAP-Rule:MF_00534};
DE   AltName: Full=Asparaginyl-tRNA synthetase {ECO:0000256|HAMAP-Rule:MF_00534};
DE            Short=AsnRS {ECO:0000256|HAMAP-Rule:MF_00534};
GN   Name=asnS {ECO:0000256|HAMAP-Rule:MF_00534};
GN   ORFNames=ATY27_15060 {ECO:0000313|EMBL:ALZ76948.1};
OS   Rheinheimera sp. F8.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Chromatiales; Chromatiaceae;
OC   Rheinheimera.
OX   NCBI_TaxID=1763998 {ECO:0000313|EMBL:ALZ76948.1, ECO:0000313|Proteomes:UP000059499};
RN   [1] {ECO:0000313|Proteomes:UP000059499}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=F8 {ECO:0000313|Proteomes:UP000059499};
RA   Schuster A.K., Szewzyk U.;
RT   "Draft genome sequence of Rheinheimera sp. F8, a biofilm-forming strain
RT   which produces large amounts of extracellular DNA.";
RL   Submitted (DEC-2015) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:ALZ76948.1, ECO:0000313|Proteomes:UP000059499}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=F8 {ECO:0000313|EMBL:ALZ76948.1,
RC   ECO:0000313|Proteomes:UP000059499};
RX   PubMed=26966195;
RA   Schuster A.K., Szewzyk U.;
RT   "Draft Genome Sequence of Rheinheimera sp. F8, a Biofilm-Forming Strain
RT   Which Produces Large Amounts of Extracellular DNA.";
RL   Genome Announc. 4:0-0(2016).
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + L-asparagine + tRNA(Asn) = AMP + diphosphate + H(+) + L-
CC         asparaginyl-tRNA(Asn); Xref=Rhea:RHEA:11180, Rhea:RHEA-COMP:9659,
CC         Rhea:RHEA-COMP:9674, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616,
CC         ChEBI:CHEBI:33019, ChEBI:CHEBI:58048, ChEBI:CHEBI:78442,
CC         ChEBI:CHEBI:78515, ChEBI:CHEBI:456215; EC=6.1.1.22;
CC         Evidence={ECO:0000256|HAMAP-Rule:MF_00534};
CC   -!- SUBUNIT: Homodimer. {ECO:0000256|HAMAP-Rule:MF_00534}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00534}.
CC   -!- SIMILARITY: Belongs to the class-II aminoacyl-tRNA synthetase family.
CC       {ECO:0000256|HAMAP-Rule:MF_00534}.
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DR   EMBL; CP013656; ALZ76948.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0U4WEK2; -.
DR   Proteomes; UP000059499; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0004816; F:asparagine-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:0006421; P:asparaginyl-tRNA aminoacylation; IEA:UniProtKB-UniRule.
DR   CDD; cd00776; AsxRS_core; 1.
DR   CDD; cd04318; EcAsnRS_like_N; 1.
DR   Gene3D; 2.40.50.140; Nucleic acid-binding proteins; 1.
DR   HAMAP; MF_00534; Asn_tRNA_synth; 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; IPR004522; Asn-tRNA-ligase.
DR   InterPro; IPR002312; Asp/Asn-tRNA-synth_IIb.
DR   InterPro; IPR012340; NA-bd_OB-fold.
DR   InterPro; IPR004365; NA-bd_OB_tRNA.
DR   NCBIfam; TIGR00457; asnS; 1.
DR   PANTHER; PTHR22594:SF34; ASPARAGINE--TRNA LIGASE, MITOCHONDRIAL-RELATED; 1.
DR   PANTHER; PTHR22594; ASPARTYL/LYSYL-TRNA SYNTHETASE; 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; 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_00534};
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|HAMAP-
KW   Rule:MF_00534}; Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00534};
KW   Ligase {ECO:0000256|ARBA:ARBA00022598, ECO:0000256|HAMAP-Rule:MF_00534};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|HAMAP-
KW   Rule:MF_00534};
KW   Protein biosynthesis {ECO:0000256|ARBA:ARBA00022917, ECO:0000256|HAMAP-
KW   Rule:MF_00534}; Reference proteome {ECO:0000313|Proteomes:UP000059499}.
FT   DOMAIN          144..458
FT                   /note="Aminoacyl-transfer RNA synthetases class-II family
FT                   profile"
FT                   /evidence="ECO:0000259|PROSITE:PS50862"
SQ   SEQUENCE   466 AA;  52353 MW;  8267EA4A2085B5F2 CRC64;
     MTHAVIKDVL AGQYAAGATI TVKGWIRTRR DSKAGISFLA VHDGSCFDAL QAVAPADLNN
     YETEIKRLTT ACSVIVTGTV VKSEGQGQSY EIQASHVEVL GWVENPDTYP MAPKRHSMEY
     LREQAHLRAR TNMVGAITRV RHCLAQAIHR FFHERGFYWI STPIITGADA EGAGEMFRVS
     TLDLENLPRD DKGHIDYKQD FFGKETFLTV SGQLNVETYA CALSNVYTFG PTFRAENSNT
     TRHLAEFWMI EPEVAFAELK DVAQLAEDML KYVFKAVLAE RADDMAFFAE RVDDKAISRL
     QQIVESSFVR MDYTDAITIL QNCGKKFDYA VEWGVDLQSE HERYLAEVHV GAPVILQNYP
     KDIKAFYMRM NEDGKTVAAM DILAPGIGEI IGGSQREERL EQLDARMDAM GLNKEDYSWY
     RDLRRYGTVP HAGFGLGFER LVSYVTGVGN VRDVIAFPRT PGNADF
//
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