ID   SYN_STRA1               Reviewed;         448 AA.
AC   Q3K2E5;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   08-NOV-2005, sequence version 1.
DT   25-MAY-2022, entry version 100.
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=SAK_0677;
OS   Streptococcus agalactiae serotype Ia (strain ATCC 27591 / A909 / CDC
OS   SS700).
OC   Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae;
OC   Streptococcus.
OX   NCBI_TaxID=205921;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 27591 / A909 / CDC SS700;
RX   PubMed=16172379; DOI=10.1073/pnas.0506758102;
RA   Tettelin H., Masignani V., Cieslewicz M.J., Donati C., Medini D.,
RA   Ward N.L., Angiuoli S.V., Crabtree J., Jones A.L., Durkin A.S., DeBoy R.T.,
RA   Davidsen T.M., Mora M., Scarselli M., Margarit y Ros I., Peterson J.D.,
RA   Hauser C.R., Sundaram J.P., Nelson W.C., Madupu R., Brinkac L.M.,
RA   Dodson R.J., Rosovitz M.J., Sullivan S.A., Daugherty S.C., Haft D.H.,
RA   Selengut J., Gwinn M.L., Zhou L., Zafar N., Khouri H., Radune D.,
RA   Dimitrov G., Watkins K., O'Connor K.J., Smith S., Utterback T.R., White O.,
RA   Rubens C.E., Grandi G., Madoff L.C., Kasper D.L., Telford J.L.,
RA   Wessels M.R., Rappuoli R., Fraser C.M.;
RT   "Genome analysis of multiple pathogenic isolates of Streptococcus
RT   agalactiae: implications for the microbial 'pan-genome'.";
RL   Proc. Natl. Acad. Sci. U.S.A. 102:13950-13955(2005).
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; CP000114; ABA45162.1; -; Genomic_DNA.
DR   RefSeq; WP_000038470.1; NC_007432.1.
DR   AlphaFoldDB; Q3K2E5; -.
DR   SMR; Q3K2E5; -.
DR   KEGG; sak:SAK_0677; -.
DR   HOGENOM; CLU_004553_2_0_9; -.
DR   OMA; DNMDLAE; -.
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..448
FT                   /note="Asparagine--tRNA ligase"
FT                   /id="PRO_1000051440"
SQ   SEQUENCE   448 AA;  51153 MW;  0F3C0C0B11317738 CRC64;
     MSKKLISIVD VKDYVGQEVT IGAWVANKSG KGKIAFVQLR DGSAFFQGVA FKPNFIEKYG
     EESGLEKFDV IKRLNQETSV YVTGIVKEDE RSKFGYELDI TDLEVIGESH EYPITPKEHG
     TDFLMDNRHL WLRSRKQMAV MQIRNAIIYS TYEFFDQNGF IKFDSPILSE NAAEDSTELF
     ETDYFGKPAF LSQSGQLYLE AGAMALGRVF DFGPVFRAEK SKTRRHLTEF WMMDAEYSFL
     SHEESLDLQE AYVKALIQGV LDRAPQALDI LERDVEALKR YIAEPFKRVS YDDAITLLQE
     HEADEDTDYE HLEHGDDFGS PHETWISNYF GVPTFVVNYP ASFKAFYMKP VPGNPERVLC
     ADLLAPEGYG EIIGGSMRED DYDALVAKMD ELGMDKSEYD FYLDLRKYGS VPHGGFGIGI
     ERMVTFVAGT KHIREAIPFP RMLHRIKP