SYN_BUCAI
ID SYN_BUCAI Reviewed; 466 AA.
AC P57441;
DT 01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-2000, sequence version 1.
DT 25-MAY-2022, entry version 119.
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=BU360;
OS Buchnera aphidicola subsp. Acyrthosiphon pisum (strain APS) (Acyrthosiphon
OS pisum symbiotic bacterium).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Erwiniaceae; Buchnera.
OX NCBI_TaxID=107806;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=APS;
RX PubMed=10993077; DOI=10.1038/35024074;
RA Shigenobu S., Watanabe H., Hattori M., Sakaki Y., Ishikawa H.;
RT "Genome sequence of the endocellular bacterial symbiont of aphids Buchnera
RT sp. APS.";
RL Nature 407:81-86(2000).
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; BA000003; BAB13064.1; -; Genomic_DNA.
DR RefSeq; NP_240178.1; NC_002528.1.
DR RefSeq; WP_010896085.1; NC_002528.1.
DR AlphaFoldDB; P57441; -.
DR SMR; P57441; -.
DR STRING; 107806.10039030; -.
DR PRIDE; P57441; -.
DR EnsemblBacteria; BAB13064; BAB13064; BAB13064.
DR KEGG; buc:BU360; -.
DR PATRIC; fig|107806.10.peg.373; -.
DR eggNOG; COG0017; Bacteria.
DR HOGENOM; CLU_004553_2_0_6; -.
DR OMA; DNMDLAE; -.
DR Proteomes; UP000001806; 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..466
FT /note="Asparagine--tRNA ligase"
FT /id="PRO_0000176397"
SQ SEQUENCE 466 AA; 53975 MW; D97B360FD0AF26D0 CRC64;
MNRVSISDIY KDDIIVNSLI TVCGWVRNRR SSKSGFSFIT IYDGSCFNSI QVIANNTLPN
YYKEILHLTT GCSVMLSGKL ILSIGDKQKY EIQLKKIKVL GWVENPETYP ISSKKHSTEY
LREVAHLRSR TNLIGAIARI RNYILHSLHH FFYKEKYYWV PTPIITSLNT EGAGEMFRVS
TLDMENIPKN LDSSVDFKKD FFGKESFLTV SGQLNLETYA CSLSKVYTFG PTFRAENSNT
GRHLAEFWML EVESAFTDLN DISDFAECML KYVCKSLLKK CITDINFLEN YTNSNIVDRL
EKFLLVDFVR IDYVEVINIL LDSKIKFNNS VFLGIDLSSE HERFLVENYF KIPVIVKNYP
KELKAFYMRL NNDKKTVAAI DILVPNVGEL IGGSQREERI AILDERLLEL GLKKEDYWWY
RDLRRYGTVP HSGFGMGFER LISYFTGITN IRDLIPFPRT VNNAYF