SYN_CLONN
ID SYN_CLONN Reviewed; 463 AA.
AC A0PY64;
DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT 09-JAN-2007, sequence version 1.
DT 03-AUG-2022, entry version 98.
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=NT01CX_1233;
OS Clostridium novyi (strain NT).
OC Bacteria; Firmicutes; Clostridia; Eubacteriales; Clostridiaceae;
OC Clostridium.
OX NCBI_TaxID=386415;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NT;
RX PubMed=17115055; DOI=10.1038/nbt1256;
RA Bettegowda C., Huang X., Lin J., Cheong I., Kohli M., Szabo S.A., Zhang X.,
RA Diaz L.A. Jr., Velculescu V.E., Parmigiani G., Kinzler K.W., Vogelstein B.,
RA Zhou S.;
RT "The genome and transcriptomes of the anti-tumor agent Clostridium novyi-
RT NT.";
RL Nat. Biotechnol. 24:1573-1580(2006).
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; CP000382; ABK61604.1; -; Genomic_DNA.
DR RefSeq; WP_011721324.1; NC_008593.1.
DR AlphaFoldDB; A0PY64; -.
DR SMR; A0PY64; -.
DR STRING; 386415.NT01CX_1233; -.
DR PRIDE; A0PY64; -.
DR EnsemblBacteria; ABK61604; ABK61604; NT01CX_1233.
DR KEGG; cno:NT01CX_1233; -.
DR PATRIC; fig|386415.7.peg.343; -.
DR eggNOG; COG0017; Bacteria.
DR HOGENOM; CLU_004553_2_0_9; -.
DR OMA; DNMDLAE; -.
DR OrthoDB; 1138123at2; -.
DR Proteomes; UP000008220; 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..463
FT /note="Asparagine--tRNA ligase"
FT /id="PRO_1000051386"
SQ SEQUENCE 463 AA; 53332 MW; 928A023A4390A264 CRC64;
METVLVKQLY RETEKFAGKE VKISGWIRTL RASNKFGFIE VNDGSFFKNI QVVFGAELEN
FKEISKYAIS SSISVEGEVV ITEGAKQPFE IHAKKVVLEG KSDADYPLQK KRHTFEYLRS
IAHLRPRSNA FSAVFRVRSL AAYAIHKFFQ DQGFVYVHTP IITGSDCEGA GEMFRVTTLD
MENPPKDEKG NVDYKEDFFG KQANLTVSGQ LEAEIYALAF RNVYTFGPTF RAENSNTARH
ASEFWMIEPE MAFAELKDYM DVAEQMVKYI INYVRENAPE EMEFFNKFID KGLLERLDNV
VNSDFARISY TEAVEILQKS GAEFEYPVEW GIDLQTEHER YLTEQIYKKP VFVTDYPKDI
KAFYMRMNDD NKTVAAADLL VPGIGEIIGG SQREERLDIL EARMAELGLE KEDYWWYLEL
RKYGETKHAG YGLGFERMIM YLTGMGNIRD VIPFPRTPGV SEF