SYN_MYCPN
ID SYN_MYCPN Reviewed; 455 AA.
AC P75521;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1997, sequence version 1.
DT 03-AUG-2022, entry version 126.
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=MPN_252;
GN ORFNames=MP580;
OS Mycoplasma pneumoniae (strain ATCC 29342 / M129) (Mycoplasmoides
OS pneumoniae).
OC Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mycoplasma.
OX NCBI_TaxID=272634;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 29342 / M129;
RX PubMed=8948633; DOI=10.1093/nar/24.22.4420;
RA Himmelreich R., Hilbert H., Plagens H., Pirkl E., Li B.-C., Herrmann R.;
RT "Complete sequence analysis of the genome of the bacterium Mycoplasma
RT pneumoniae.";
RL Nucleic Acids Res. 24:4420-4449(1996).
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; U00089; AAB96228.1; -; Genomic_DNA.
DR PIR; S73906; S73906.
DR RefSeq; NP_109940.1; NC_000912.1.
DR RefSeq; WP_010874609.1; NC_000912.1.
DR AlphaFoldDB; P75521; -.
DR SMR; P75521; -.
DR IntAct; P75521; 3.
DR STRING; 272634.MPN_252; -.
DR EnsemblBacteria; AAB96228; AAB96228; MPN_252.
DR KEGG; mpn:MPN_252; -.
DR PATRIC; fig|272634.6.peg.271; -.
DR HOGENOM; CLU_004553_2_0_14; -.
DR OMA; DNMDLAE; -.
DR BioCyc; MPNE272634:G1GJ3-398-MON; -.
DR Proteomes; UP000000808; 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 Gene3D; 2.40.50.140; -; 1.
DR Gene3D; 3.30.930.10; -; 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 Pfam; PF00152; tRNA-synt_2; 1.
DR Pfam; PF01336; tRNA_anti-codon; 1.
DR PRINTS; PR01042; TRNASYNTHASP.
DR SUPFAM; SSF50249; SSF50249; 1.
DR SUPFAM; SSF55681; SSF55681; 1.
DR TIGRFAMs; TIGR00457; asnS; 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..455
FT /note="Asparagine--tRNA ligase"
FT /id="PRO_0000176433"
SQ SEQUENCE 455 AA; 51898 MW; 1AB74ADF708E09C9 CRC64;
MSATAISDLF EKPAQFKNKK IKLTGWLKNK RTSANIIFLE VNDGSTLLNL QAVVKQDQPE
LFALAESISL ASAVSVSGTV ALTPKSKQPL ELVVKQINVL STARADYPLQ KKEHSLEFFR
NNAYLRVRAR TYFAIMKVRS LLSQAIFDYF FKNDFVLVHS PILTSNDCEG AGETFELKQG
KEFFNKTTYL TVSGQFGAEC YAQAFKKVFT FGPTFRAEKS HTSRHLSEFW MIEPEVAFAN
LKDLIKLIES TVKTVIKQVM QKAKQELDFL EKQFDVKLME RLKQITSTKN FHVLEYTKAL
EILKTAQASG QANFEVQDFN FGLDLKTEHE RFLCEQHFHN QPVFVINYPK DFKAFYMKQN
ADGRTVGAVD LLFPQIGEIC GGSEREGNLE KLVERCQAMQ IDTQTLNWYL DMRKWGYFAS
AGFGLGFDRL LAYICGLENI RDAIPFPRAH GSINY