ID SYN_MALP2 Reviewed; 453 AA.
AC Q8EW03;
DT 31-OCT-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2003, sequence version 1.
DT 27-MAR-2024, entry version 116.
DE RecName: Full=Asparagine--tRNA ligase {ECO:0000255|HAMAP-Rule:MF_00534};
DE EC=6.1.1.22 {ECO:0000255|HAMAP-Rule:MF_00534};
DE AltName: Full=Asparaginyl-tRNA synthetase {ECO:0000255|HAMAP-Rule:MF_00534};
DE Short=AsnRS {ECO:0000255|HAMAP-Rule:MF_00534};
GN Name=asnS {ECO:0000255|HAMAP-Rule:MF_00534}; OrderedLocusNames=MYPE4040;
OS Malacoplasma penetrans (strain HF-2) (Mycoplasma penetrans).
OC Bacteria; Mycoplasmatota; Mycoplasmoidales; Mycoplasmoidaceae;
OC Malacoplasma.
OX NCBI_TaxID=272633;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=HF-2;
RX PubMed=12466555; DOI=10.1093/nar/gkf667;
RA Sasaki Y., Ishikawa J., Yamashita A., Oshima K., Kenri T., Furuya K.,
RA Yoshino C., Horino A., Shiba T., Sasaki T., Hattori M.;
RT "The complete genomic sequence of Mycoplasma penetrans, an intracellular
RT bacterial pathogen in humans.";
RL Nucleic Acids Res. 30:5293-5300(2002).
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:0000255|HAMAP-Rule:MF_00534};
CC -!- SUBUNIT: Homodimer. {ECO:0000255|HAMAP-Rule:MF_00534}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00534}.
CC -!- SIMILARITY: Belongs to the class-II aminoacyl-tRNA synthetase family.
CC {ECO:0000255|HAMAP-Rule:MF_00534}.
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DR EMBL; BA000026; BAC44194.1; -; Genomic_DNA.
DR RefSeq; WP_011077230.1; NC_004432.1.
DR AlphaFoldDB; Q8EW03; -.
DR SMR; Q8EW03; -.
DR STRING; 272633.gene:10731520; -.
DR KEGG; mpe:MYPE4040; -.
DR eggNOG; COG0017; Bacteria.
DR HOGENOM; CLU_004553_2_0_14; -.
DR InParanoid; Q8EW03; -.
DR Proteomes; UP000002522; 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; ATP-binding; Cytoplasm; Ligase;
KW Nucleotide-binding; Protein biosynthesis; Reference proteome.
FT CHAIN 1..453
FT /note="Asparagine--tRNA ligase"
FT /id="PRO_0000176432"
SQ SEQUENCE 453 AA; 52087 MW; 7601F96A7D718966 CRC64;
METVAVRDIF KNYKEFSNVK LVGWVRSNRD NGSIGFISFT DGSCIHSIQL VYKNGETNNF
EEAKSTRTGS AILVEGVVVE SKQPNQSFEI KVTNFILLKQ ADEDYPLQKK EHGAEFLRTI
AHLRQRTNKY GTIMRLRSEL AFAIHNFFHQ NNFVWVSSPI ITSNDAEGAG ENFYVDSKTV
KNFFGKNASL TVSGQMHAEA YAQSYKRVYT FGPTFRAEKS NTNRHVSEFW MVEPEIAFCN
LEQLMYLIEE FVKYLIRFIL KNCKDEMTFL NKLSNNTLSE KLLNAISHPF EKITYKKAIA
ILKSDVANKK VKFENESIYF GMDLNSEHEK YLCEKVFNKP LFIYDYPAEI KAFYMKMNAD
GTTVGACDLL MPGIGEIVGG SERESDYTKL VKKCTKANMK VEDIEWYLAL RKYGYHKSAG
FGLGFERFLM YVTECENVKD TIPFPRSYGS LDF
//
