ID D5E544_MYCCM Unreviewed; 451 AA.
AC D5E544;
DT 15-JUN-2010, integrated into UniProtKB/TrEMBL.
DT 15-JUN-2010, sequence version 1.
DT 27-MAR-2024, entry version 84.
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 ECO:0000313|EMBL:ADE19951.1};
GN OrderedLocusNames=MCRO_0234 {ECO:0000313|EMBL:ADE19951.1};
OS Mycoplasma crocodyli (strain ATCC 51981 / MP145).
OC Bacteria; Mycoplasmatota; Mollicutes; Mycoplasmataceae; Mycoplasma.
OX NCBI_TaxID=512564 {ECO:0000313|EMBL:ADE19951.1, ECO:0000313|Proteomes:UP000001845};
RN [1] {ECO:0000313|Proteomes:UP000001845}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 51981 / MP145 {ECO:0000313|Proteomes:UP000001845};
RA Glass J.I., Durkin A.S., Hostetler J., Jackson J., Johnson J., May M.A.,
RA Paralanov V., Radune D., Szczypinski B., Brown D.R.;
RT "The complete genome of Mycoplasma crocodyli MP145.";
RL Submitted (MAR-2010) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=MP145;
RA Ma Z., Wang X., Liu H.;
RL Submitted (MAR-2010) to the EMBL/GenBank/DDBJ databases.
RN [3] {ECO:0000313|EMBL:ADE19951.1, ECO:0000313|Proteomes:UP000001845}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 51981 / MP145 {ECO:0000313|Proteomes:UP000001845};
RX PubMed=21460083; DOI=10.1128/JB.00309-11;
RA Brown D.R., Farmerie W.G., May M., Benders G.A., Durkin A.S., Hlavinka K.,
RA Hostetler J., Jackson J., Johnson J., Miller R.H., Paralanov V., Radune D.,
RA Szczypinski B., Glass J.I.;
RT "Genome sequences of Mycoplasma alligatoris A21JP2T and Mycoplasma
RT crocodyli MP145T.";
RL J. Bacteriol. 193:2892-2893(2011).
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; CP001991; ADE19951.1; -; Genomic_DNA.
DR RefSeq; WP_013054727.1; NC_014014.1.
DR AlphaFoldDB; D5E544; -.
DR STRING; 512564.MCRO_0234; -.
DR KEGG; mcd:MCRO_0234; -.
DR eggNOG; COG0017; Bacteria.
DR HOGENOM; CLU_004553_2_0_14; -.
DR OrthoDB; 9762036at2; -.
DR Proteomes; UP000001845; 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; 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}; Reference proteome {ECO:0000313|Proteomes:UP000001845}.
FT DOMAIN 136..441
FT /note="Aminoacyl-transfer RNA synthetases class-II family
FT profile"
FT /evidence="ECO:0000259|PROSITE:PS50862"
SQ SEQUENCE 451 AA; 51379 MW; 9FDC94AB02A9403D CRC64;
MHTIKLILLR PNYYNNWEDF TIKAWVDSNR GNNKLRFINI NDGSTVKNLQ VVLKGKEFDF
NLLDQIKNGA AIKVIGTLKA TPDAPQPIEL VATSIELLSN TENDYPIQNQ EINIETLREI
PHVRHRTKTL RSAMLIRSTL AQEIHKYFMA NDFYLMSSPI ITSNDGEGAG EAFNVSDNSP
EPFFGQNKKA TLGVTGQLHA ESYAIGFKKV YTFAPTFRAE HSNTKKHAAE FWMVEPEVAF
YELNDVVKLA DHMLKTVIKA TLAKCKFEFD YLEDHIDKNL RNRLALFTGS KLNVIDYADA
IKELAKVKSR FENQDIKFGL DLATEHERYL AEELFNGPVA VINFPKSFKA FYMHQNEDGK
TVAAFDLLVP GIGELIGGSQ REVRYDKLLE RIKEIGIDQE EIQWYLDLRK FGDSGSSGFG
LGFERLVMYI TGLDNIRDVI PYPRTTGNIR M
//
