UniProt: D4KB39

Database: UniProt
Entry: D4KB39_9FIRM

LinkDB:  D4KB39_9FIRM 
Original site:  D4KB39_9FIRM

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Ontology (6)   
   GO (6)   
Chemical reaction (1)   
   KEGG ENZYME (1)   
Gene (1)   
   KEGG GENES (1)   
DNA sequence (1)   
   EMBL (1)   
Protein domain (10)   
   InterPro (7)   
   Pfam (2)   
   PROSITE (1)   
All databases (19)   

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ID   D4KB39_9FIRM            Unreviewed;       462 AA.
AC   D4KB39;
DT   18-MAY-2010, integrated into UniProtKB/TrEMBL.
DT   18-MAY-2010, sequence version 1.
DT   24-JAN-2024, entry version 70.
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=FPR_18140 {ECO:0000313|EMBL:CBL02052.1};
OS   Faecalibacterium prausnitzii SL3/3.
OC   Bacteria; Bacillota; Clostridia; Eubacteriales; Oscillospiraceae;
OC   Faecalibacterium.
OX   NCBI_TaxID=657322 {ECO:0000313|EMBL:CBL02052.1, ECO:0000313|Proteomes:UP000007059};
RN   [1] {ECO:0000313|EMBL:CBL02052.1, ECO:0000313|Proteomes:UP000007059}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SL3/3 {ECO:0000313|EMBL:CBL02052.1,
RC   ECO:0000313|Proteomes:UP000007059};
RG   metaHIT consortium -- http://www.metahit.eu/;
RA   Pajon A., Turner K., Parkhill J., Duncan S., Flint H.;
RT   "The genome sequence of Faecalibacterium prausnitzii SL3/3.";
RL   Submitted (MAR-2010) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:CBL02052.1, ECO:0000313|Proteomes:UP000007059}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SL3/3 {ECO:0000313|EMBL:CBL02052.1,
RC   ECO:0000313|Proteomes:UP000007059};
RA   Pajon A.;
RL   Submitted (MAR-2010) 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}.
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DR   EMBL; FP929046; CBL02052.1; -; Genomic_DNA.
DR   AlphaFoldDB; D4KB39; -.
DR   KEGG; fpa:FPR_18140; -.
DR   PATRIC; fig|657322.3.peg.1728; -.
DR   eggNOG; COG0017; Bacteria.
DR   HOGENOM; CLU_004553_2_0_9; -.
DR   Proteomes; UP000007059; 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:0016740; F:transferase activity; IEA:UniProt.
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};
KW   Cytoplasm {ECO:0000256|ARBA:ARBA00022490, 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          105..454
FT                   /note="Aminoacyl-transfer RNA synthetases class-II family
FT                   profile"
FT                   /evidence="ECO:0000259|PROSITE:PS50862"
SQ   SEQUENCE   462 AA;  52449 MW;  96CF8271E4E80C37 CRC64;
     MERTEILSLF KSTPADGTEI TVCGWAKNIR DSKNIGFIAL SDGGCFKTLQ IVLEAGKLAN
     YDEVIHTGLY SSLRIKGKLV LTPQAKQPFE LNAESVEILG DCPADEYPLQ KKKMSMEYLR
     TMPTLRPRTN TFNAAFRVRS VAAYAIHKFF QENGFVYAHS PLITASDCEG AGEMFRVTTL
     DLDNLPKTED GAVDYSKDFF EKPVNLTVSG QLEAEAMAMA FGKVYTFGPT FRAEKSFTTR
     HAAEFWMIEP EMAFCDLNGY MDNAEAMIKY VIRYVLDNCP DEMAFFNQFI DKGLVERLEL
     VANSEFARIS YTEAIEILKK NNKKFQYPVE WGVDIQTEHE RYLTEVVYKK PVFVTDYPKE
     IKSFYMKQNA DGKTVAAADM LVPGIGELIG GSQREEDYGK LVARMDELGM DKTNYEWYLN
     LRKFGGVEHA GYGLGFERMI MYLTGIQNIR DVLPFPRTAY GF
//

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