SYNC_BRUMA
ID SYNC_BRUMA Reviewed; 548 AA.
AC P10723;
DT 01-JUL-1989, integrated into UniProtKB/Swiss-Prot.
DT 01-JUL-1989, sequence version 1.
DT 25-MAY-2022, entry version 111.
DE RecName: Full=Asparagine--tRNA ligase, cytoplasmic;
DE EC=6.1.1.22;
DE AltName: Full=Asparaginyl-tRNA synthetase;
DE Short=AsnRS;
DE AltName: Full=Potentially protective 63 kDa antigen;
OS Brugia malayi (Filarial nematode worm).
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Spirurina; Spiruromorpha; Filarioidea; Onchocercidae; Brugia.
OX NCBI_TaxID=6279;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=2840577; DOI=10.1016/0166-6851(88)90137-5;
RA Perrine K.G., Denker J.A., Nilsen T.W.;
RT "A multi-copy gene encodes a potentially protective antigen in Brugia
RT malayi.";
RL Mol. Biochem. Parasitol. 30:97-104(1988).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=3368467; DOI=10.1073/pnas.85.10.3604;
RA Nilsen T.W., Maroney P.A., Goodwin R.G., Perrine K.G., Denker J.A.,
RA Nanduri J., Kazura J.W.;
RT "Cloning and characterization of a potentially protective antigen in
RT lymphatic filariasis.";
RL Proc. Natl. Acad. Sci. U.S.A. 85:3604-3607(1988).
RN [3]
RP FUNCTION.
RX PubMed=7589498; DOI=10.1016/0014-5793(95)01092-s;
RA Kron M., Marquard K., Hartlein M., Price S., Leberman R.;
RT "An immunodominant antigen of Brugia malayi is an asparaginyl-tRNA
RT synthetase.";
RL FEBS Lett. 374:122-124(1995).
CC -!- FUNCTION: Potentially protective antigen in lymphatic filariasis.
CC {ECO:0000269|PubMed:7589498}.
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 -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the class-II aminoacyl-tRNA synthetase family.
CC {ECO:0000305}.
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DR EMBL; J03971; AAA27852.1; -; Genomic_DNA.
DR EMBL; J03266; AAA27849.1; -; mRNA.
DR PIR; A28209; A28209.
DR PIR; A54510; A54510.
DR PDB; 2KQR; NMR; -; A=1-111.
DR PDBsum; 2KQR; -.
DR AlphaFoldDB; P10723; -.
DR BMRB; P10723; -.
DR SMR; P10723; -.
DR STRING; 6279.P10723; -.
DR BRENDA; 6.1.1.22; 997.
DR EvolutionaryTrace; P10723; -.
DR Proteomes; UP000006672; Unassembled WGS sequence.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0004816; F:asparagine-tRNA ligase activity; IEA:UniProtKB-EC.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0003676; F:nucleic acid binding; IEA:InterPro.
DR GO; GO:0006421; P:asparaginyl-tRNA aminoacylation; IEA:InterPro.
DR Gene3D; 2.40.50.140; -; 1.
DR Gene3D; 3.30.930.10; -; 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 1: Evidence at protein level;
KW 3D-structure; Aminoacyl-tRNA synthetase; ATP-binding; Cytoplasm; Ligase;
KW Nucleotide-binding; Protein biosynthesis; Reference proteome.
FT CHAIN 1..548
FT /note="Asparagine--tRNA ligase, cytoplasmic"
FT /id="PRO_0000176494"
FT REGION 81..131
FT /note="Region of immunological reactivity"
FT CONFLICT 50
FT /note="I -> V (in Ref. 2; AAA27849)"
FT /evidence="ECO:0000305"
FT CONFLICT 65
FT /note="H -> R (in Ref. 2; AAA27849)"
FT /evidence="ECO:0000305"
FT CONFLICT 212
FT /note="P -> S (in Ref. 2; AAA27849)"
FT /evidence="ECO:0000305"
FT CONFLICT 265
FT /note="L -> V (in Ref. 2; AAA27849)"
FT /evidence="ECO:0000305"
FT CONFLICT 454
FT /note="Q -> K (in Ref. 2; AAA27849)"
FT /evidence="ECO:0000305"
FT STRAND 3..5
FT /evidence="ECO:0007829|PDB:2KQR"
FT TURN 7..9
FT /evidence="ECO:0007829|PDB:2KQR"
FT STRAND 17..20
FT /evidence="ECO:0007829|PDB:2KQR"
FT HELIX 25..32
FT /evidence="ECO:0007829|PDB:2KQR"
FT STRAND 35..37
FT /evidence="ECO:0007829|PDB:2KQR"
FT STRAND 39..45
FT /evidence="ECO:0007829|PDB:2KQR"
FT STRAND 48..53
FT /evidence="ECO:0007829|PDB:2KQR"
FT HELIX 56..72
FT /evidence="ECO:0007829|PDB:2KQR"
SQ SEQUENCE 548 AA; 62339 MW; 7E4F6EA248255095 CRC64;
MTVYICPETG DDGNDGSELK PLRTLYQAMI ITKSSKGDFL IRTKKDGKQI WEAASKTALK
KSWKHYEQEM LKNEKVAAKM LEKDATEVGV KAALEEAKKV QIELDTSLSY ITGVKIRDLV
KHRNERVCIK GWIHRMRRQG KSLMFFILRD GTGFLQVLLM DKLCQTYDAL TVNTECTVEI
YGAIKEVPEG KEAPNGHELI ADFWKIIGNA PPGGIDNVLN EEASVDKMLD NRHLVIRGEN
AAALLRLRAA ATRAMREHFY NAGYLEVAPP TLVQTQVEGG STLFNLDYFG EQSFLTQSSQ
LYLETCIPTL GDVFLHCSVL QGGKISHSST LAEYAHVEAE CPFITLDDLM EKIEELVCDT
VDRLLADEEA KKLLEHINPK FQPPERPFLR MEYKDAIKWL QEHNVENEFG NTFTYGEDIA
EAAERFMTDT INKPILLNRF PSEIKAFYMQ RDAQDNTLTE SVDLLMPGVG EIVGGSMRIW
KFDELSKAFK NVEIDPKPYY WYLDQRLYGT CPHGGYGLGL ERFICWLTNT NHIRDVCLYP
RFVGRCVP
