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SYN_MICAN
ID   SYN_MICAN               Reviewed;         454 AA.
AC   B0JN99;
DT   20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT   18-MAR-2008, sequence version 1.
DT   03-AUG-2022, entry version 84.
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=MAE_04410;
OS   Microcystis aeruginosa (strain NIES-843 / IAM M-2473).
OC   Bacteria; Cyanobacteria; Oscillatoriophycideae; Chroococcales;
OC   Microcystaceae; Microcystis.
OX   NCBI_TaxID=449447;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NIES-843 / IAM M-247;
RX   PubMed=18192279; DOI=10.1093/dnares/dsm026;
RA   Kaneko T., Nakajima N., Okamoto S., Suzuki I., Tanabe Y., Tamaoki M.,
RA   Nakamura Y., Kasai F., Watanabe A., Kawashima K., Kishida Y., Ono A.,
RA   Shimizu Y., Takahashi C., Minami C., Fujishiro T., Kohara M., Katoh M.,
RA   Nakazaki N., Nakayama S., Yamada M., Tabata S., Watanabe M.M.;
RT   "Complete genomic structure of the bloom-forming toxic cyanobacterium
RT   Microcystis aeruginosa NIES-843.";
RL   DNA Res. 14:247-256(2007).
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; AP009552; BAG00263.1; -; Genomic_DNA.
DR   RefSeq; WP_012264099.1; NC_010296.1.
DR   AlphaFoldDB; B0JN99; -.
DR   SMR; B0JN99; -.
DR   STRING; 449447.MAE_04410; -.
DR   PaxDb; B0JN99; -.
DR   PRIDE; B0JN99; -.
DR   EnsemblBacteria; BAG00263; BAG00263; MAE_04410.
DR   KEGG; mar:MAE_04410; -.
DR   PATRIC; fig|449447.4.peg.416; -.
DR   eggNOG; COG0017; Bacteria.
DR   HOGENOM; CLU_004553_2_0_3; -.
DR   OMA; DNMDLAE; -.
DR   OrthoDB; 1138123at2; -.
DR   BioCyc; MAER449447:MAE_RS02030-MON; -.
DR   Proteomes; UP000001510; 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..454
FT                   /note="Asparagine--tRNA ligase"
FT                   /id="PRO_1000081851"
SQ   SEQUENCE   454 AA;  51586 MW;  81C4CCD80AE6287B CRC64;
     MTTRIKEIFQ TGQPDQSVTV QGWVRTKREL KEFTFLEVND GSSLANLQVI LEPTLPDYEN
     VLKTISTGAA IAVSGNLVPS PGKGQNIELK AAEITLYGDC PPDYPLQKKR HSFEFLRTIA
     HLRARTNTLG AVMRVRNACA TAIHSFFQEK GFIWVHTPII TANDCEGAGE LFTVTSLDLK
     KPANFAEDFF GKRAYLTVSG QLQAEVMAMA LSNVYTFGPT FRAENSNTSR HLAEFWMVEP
     EMAFCDLEGD QDLAEAFLKY IFKFVLENCP EDLQFFNERI DKTVLSTAEN IVNSEFGRIT
     YSEAIELLEK ADRQFEFPVE WGVDLQSEHE RYLAEELFKK PVIVTNYPKT IKAFYMRLDD
     NNKTVSAMDI LAPKIGEIIG GSQREERLDV LIQRMQEQGM NPDDLWWYLD LRRYGSVPHA
     GFGLGFERLV QFMTGMTNIR DVIPFPRTPL SADF
 
 
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