SYN_MYCCT
ID SYN_MYCCT Reviewed; 454 AA.
AC Q2SR42;
DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT 24-JAN-2006, sequence version 1.
DT 25-MAY-2022, entry version 102.
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=MCAP_0824;
OS Mycoplasma capricolum subsp. capricolum (strain California kid / ATCC 27343
OS / NCTC 10154).
OC Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mycoplasma.
OX NCBI_TaxID=340047;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=California kid / ATCC 27343 / NCTC 10154;
RA Glass J.I., Lartigue C., Pfannkoch C., Baden-Tillson H., Smith H.O.,
RA Venter J.C., Roske K., Wise K.S., Calcutt M.J., Nelson W.C., Nierman W.C.;
RL Submitted (SEP-2005) 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: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; CP000123; ABC01510.1; -; Genomic_DNA.
DR RefSeq; WP_011387655.1; NC_007633.1.
DR AlphaFoldDB; Q2SR42; -.
DR SMR; Q2SR42; -.
DR PRIDE; Q2SR42; -.
DR EnsemblBacteria; ABC01510; ABC01510; MCAP_0824.
DR GeneID; 23778224; -.
DR KEGG; mcp:MCAP_0824; -.
DR HOGENOM; CLU_004553_2_0_14; -.
DR OMA; DNMDLAE; -.
DR OrthoDB; 1138123at2; -.
DR PhylomeDB; Q2SR42; -.
DR Proteomes; UP000001928; 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.
FT CHAIN 1..454
FT /note="Asparagine--tRNA ligase"
FT /id="PRO_1000051408"
SQ SEQUENCE 454 AA; 52217 MW; 608CBD2E6A39D063 CRC64;
MEIKQVFEQN SELIDQEIEL IARVRSNRQG KFVSFMILND GTTFTDLQVV YKTKTKGYEQ
ALQARVSSIV KVIGRVVLTP EKQQKFEVQA DAIELIDQAI EDYPLQKKEH TTEYLREIAH
LRAKTKTFNA IFKIRSAAAY AIHKFFNDRG FVYIHSPIIT SNDAEGAGEA FLVTTREDAD
YEKDFFAKKA SLTVSGQLHA EAFAQAFKKV YTFGPTFRAE NSNTAKHAAE FWMIEPEVAF
ADLKDNIQLI QDMVKYIINY IFKHNRRELE FCNEHLEDGL IDKLNSVRNS EFKVTTYTEA
IEILKQAVAN GHKFEVSDIE FGLDLGTEHE RYICEQVNKA PTFVTNYPKE IKAFYMKQNE
DNKTVAAVDL LVPGIGELVG GSQREDNYEK LIKRCKEVNI DIDQLEWYNN LRLYGYYKSA
GFGLGFERLI MYITGASNIR DVIPFPRTPK NLLF