ID A0A1V3L2I7_9PAST Unreviewed; 467 AA.
AC A0A1V3L2I7;
DT 07-JUN-2017, integrated into UniProtKB/TrEMBL.
DT 07-JUN-2017, sequence version 1.
DT 27-MAR-2024, entry version 30.
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=BKG88_01540 {ECO:0000313|EMBL:OOF87426.1}, BKG93_08420
GN {ECO:0000313|EMBL:OOF84184.1};
OS Rodentibacter ratti.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Pasteurellales;
OC Pasteurellaceae; Rodentibacter.
OX NCBI_TaxID=1906745 {ECO:0000313|EMBL:OOF84184.1, ECO:0000313|Proteomes:UP000189549};
RN [1] {ECO:0000313|Proteomes:UP000189353, ECO:0000313|Proteomes:UP000189549}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Ppn157 {ECO:0000313|EMBL:OOF84184.1,
RC ECO:0000313|Proteomes:UP000189549}, and Ppn158
RC {ECO:0000313|EMBL:OOF87426.1, ECO:0000313|Proteomes:UP000189353};
RA Christensen H.;
RT "Rodentibacter gen. nov. and new species.";
RL Submitted (OCT-2016) to the EMBL/GenBank/DDBJ databases.
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}.
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:OOF84184.1}.
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DR EMBL; MLAH01000051; OOF84184.1; -; Genomic_DNA.
DR EMBL; MLAI01000009; OOF87426.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1V3L2I7; -.
DR STRING; 1906745.BKG94_06425; -.
DR OrthoDB; 9762036at2; -.
DR Proteomes; UP000189353; Unassembled WGS sequence.
DR Proteomes; UP000189549; Unassembled WGS sequence.
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}.
FT DOMAIN 145..457
FT /note="Aminoacyl-transfer RNA synthetases class-II family
FT profile"
FT /evidence="ECO:0000259|PROSITE:PS50862"
SQ SEQUENCE 467 AA; 52824 MW; D88090E17F26DC9F CRC64;
MSKIASIVDV LQGKVSIGET VTVRGWVRTR RDSKAGLSFL AVYDGSCFDP IQAIINNDIE
NYENEILRLT TGCSVVVTGK VVESPAEGQA VELQAEKVEV AGFVEDPDSY PMAAKRHSIE
YLREVAHLRP RTNIIGAVAR VRHCLAQAIH RFFHEQGFYW VATPLITASD TEGAGEMFRV
STLDLENLPR DEKGAVDFSQ DFFGKESFLT VSGQLNGETY ACALSKIYTF GPTFRAENSN
TTRHLAEFWM VEPEVAFATL EDNAKLAEDM LKYVFRAVLA ERKDDLSFFE KHVDKDVITR
LENFVNSDFA QIDYTDAIEV LLKSGKKFEF PVSWGIDLSS EHERYLAEEY FKSPVVVKNY
PKDIKAFYMR LNDDGKTVAA MDVLAPGIGE IIGGSQREER LEVLDKRMEE MGLNPQDYYW
YRDLRKYGTV PHSGFGLGFE RLIVYVTGVQ NIRDVIPFPR TPRNANF
//
