ID   SYNC1_ARATH             Reviewed;         572 AA.
AC   Q9SW96; A4FVR0;
DT   31-JAN-2002, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-2000, sequence version 1.
DT   02-SEP-2026, entry version 173.
DE   RecName: Full=Asparagine--tRNA ligase, cytoplasmic 1 {ECO:0000305};
DE            EC=6.1.1.22 {ECO:0000305};
DE   AltName: Full=Asparaginyl-tRNA synthetase 1 {ECO:0000305};
DE            Short=AsnRS 1 {ECO:0000305};
DE   AltName: Full=Protein EMBRYO DEFECTIVE 2755 {ECO:0000303|PubMed:16297076};
GN   Name=SYNC1 {ECO:0000303|PubMed:10824085};
GN   Synonyms=EMB2755 {ECO:0000303|PubMed:16297076};
GN   OrderedLocusNames=At5g56680; ORFNames=MIK19.13;
OS   Arabidopsis thaliana (Mouse-ear cress).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   rosids; malvids; Brassicales; Brassicaceae; Camelineae; Arabidopsis.
OX   NCBI_TaxID=3702;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=cv. Columbia;
RX   PubMed=10824085; DOI=10.1007/s002390010044;
RA   Peeters N.M., Chapron A., Giritch A., Grandjean O., Lancelin D., Lhomme T.,
RA   Vivrel A., Small I.;
RT   "Duplication and quadruplication of Arabidopsis thaliana cysteinyl- and
RT   asparaginyl-tRNA synthetase genes of organellar origin.";
RL   J. Mol. Evol. 50:413-423(2000).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. Columbia;
RX   PubMed=9734815; DOI=10.1093/dnares/5.3.203;
RA   Kotani H., Nakamura Y., Sato S., Asamizu E., Kaneko T., Miyajima N.,
RA   Tabata S.;
RT   "Structural analysis of Arabidopsis thaliana chromosome 5. VI. Sequence
RT   features of the regions of 1,367,185 bp covered by 19 physically assigned
RT   P1 and TAC clones.";
RL   DNA Res. 5:203-216(1998).
RN   [3]
RP   GENOME REANNOTATION.
RC   STRAIN=cv. Columbia;
RX   PubMed=27862469; DOI=10.1111/tpj.13415;
RA   Cheng C.Y., Krishnakumar V., Chan A.P., Thibaud-Nissen F., Schobel S.,
RA   Town C.D.;
RT   "Araport11: a complete reannotation of the Arabidopsis thaliana reference
RT   genome.";
RL   Plant J. 89:789-804(2017).
RN   [4]
RP   GENOME REANNOTATION.
RC   STRAIN=cv. Columbia;
RG   The Arabidopsis Information Resource (TAIR);
RT   "Community-consensus reference genome of Arabidopsis thaliana Col-0.";
RL   Submitted (FEB-2026) to the EMBL/GenBank/DDBJ databases.
RN   [5]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=cv. Columbia;
RA   Bautista V.R., Kim C.J., Chen H., Wu S.Y., De Los Reyes C., Ecker J.R.;
RT   "Arabidopsis ORF clones.";
RL   Submitted (MAR-2007) to the EMBL/GenBank/DDBJ databases.
RN   [6]
RP   DISRUPTION PHENOTYPE.
RX   PubMed=16297076; DOI=10.1111/j.1365-313x.2005.02580.x;
RA   Berg M., Rogers R., Muralla R., Meinke D.;
RT   "Requirement of aminoacyl-tRNA synthetases for gametogenesis and embryo
RT   development in Arabidopsis.";
RL   Plant J. 44:866-878(2005).
RN   [7]
RP   SUBCELLULAR LOCATION.
RX   PubMed=16251277; DOI=10.1073/pnas.0504682102;
RA   Duchene A.-M., Giritch A., Hoffmann B., Cognat V., Lancelin D.,
RA   Peeters N.M., Zaepfel M., Marechal-Drouard L., Small I.D.;
RT   "Dual targeting is the rule for organellar aminoacyl-tRNA synthetases in
RT   Arabidopsis thaliana.";
RL   Proc. Natl. Acad. Sci. U.S.A. 102:16484-16489(2005).
RN   [8]
RP   ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, CLEAVAGE OF INITIATOR
RP   METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY
RP   [LARGE SCALE ANALYSIS].
RX   PubMed=22223895; DOI=10.1074/mcp.m111.015131;
RA   Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C., Meinnel T.,
RA   Giglione C.;
RT   "Comparative large-scale characterisation of plant vs. mammal proteins
RT   reveals similar and idiosyncratic N-alpha acetylation features.";
RL   Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012).
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=tRNA(Asn) + L-asparagine + ATP = L-asparaginyl-tRNA(Asn) + AMP
CC         + diphosphate + H(+); 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:0000305};
CC   -!- SUBCELLULAR LOCATION: Cytoplasm, cytosol {ECO:0000305|PubMed:16251277}.
CC   -!- DISRUPTION PHENOTYPE: Embryo defective. Developmental arrest of the
CC       embryo at the cotyledon stage. {ECO:0000305|PubMed:16297076}.
CC   -!- SIMILARITY: Belongs to the class-II aminoacyl-tRNA synthetase family.
CC       {ECO:0000305}.
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DR   EMBL; AF170909; AAD46681.1; -; mRNA.
DR   EMBL; AB013392; BAB09886.1; -; Genomic_DNA.
DR   EMBL; CP002688; AED96795.1; -; Genomic_DNA.
DR   EMBL; OZ408687; CAO7056749.1; -; Genomic_DNA.
DR   EMBL; BT030358; ABO38771.1; -; mRNA.
DR   RefSeq; NP_200479.1; NM_125051.4.
DR   AlphaFoldDB; Q9SW96; -.
DR   SMR; Q9SW96; -.
DR   BioGRID; 21013; 2.
DR   FunCoup; Q9SW96; 3444.
DR   IntAct; Q9SW96; 1.
DR   STRING; 3702.Q9SW96; -.
DR   GlyGen; Q9SW96; 1 site.
DR   iPTMnet; Q9SW96; -.
DR   PaxDb; 3702-Q9SW96; -.
DR   ProteomicsDB; 245286; -.
DR   GeneID; 835769; -.
DR   KEGG; ath:AT5G56680; -.
DR   Araport; AT5G56680; -.
DR   TAIR; AT5G56680; SYNC1.
DR   eggNOG; KOG0554; Eukaryota.
DR   HOGENOM; CLU_004553_2_0_1; -.
DR   InParanoid; Q9SW96; -.
DR   OMA; PRFPGQC; -.
DR   OrthoDB; 1931232at2759; -.
DR   PhylomeDB; Q9SW96; -.
DR   PRO; PR:Q9SW96; -.
DR   Proteomes; UP000006548; Chromosome 5.
DR   ExpressionAtlas; Q9SW96; baseline and differential.
DR   GO; GO:0009507; C:chloroplast; IDA:TAIR.
DR   GO; GO:0005737; C:cytoplasm; ISM:TAIR.
DR   GO; GO:0005829; C:cytosol; HDA:TAIR.
DR   GO; GO:0005739; C:mitochondrion; IDA:TAIR.
DR   GO; GO:0009536; C:plastid; HDA:TAIR.
DR   GO; GO:0004816; F:asparagine-tRNA ligase activity; IBA:GO_Central.
DR   GO; GO:0005524; F:ATP binding; IEA:InterPro.
DR   GO; GO:0003676; F:nucleic acid binding; IEA:InterPro.
DR   GO; GO:0006421; P:asparaginyl-tRNA aminoacylation; IBA:GO_Central.
DR   GO; GO:0009793; P:embryo development ending in seed dormancy; IMP:TAIR.
DR   CDD; cd00776; AsxRS_core; 1.
DR   CDD; cd04318; EcAsnRS_like_N; 1.
DR   FunFam; 3.30.930.10:FF:000016; Asparagine--tRNA ligase; 1.
DR   Gene3D; 3.30.930.10; Bira Bifunctional Protein, Domain 2; 1.
DR   Gene3D; 2.40.50.140; Nucleic acid-binding proteins; 1.
DR   Gene3D; 1.10.287.10; S15/NS1, RNA-binding; 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   InterPro; IPR000738; WHEP-TRS_dom.
DR   NCBIfam; TIGR00457; asnS; 1.
DR   NCBIfam; NF003037; PRK03932.1; 1.
DR   PANTHER; PTHR22594:SF54; ASPARAGINE--TRNA LIGASE, CYTOPLASMIC 1-RELATED; 1.
DR   PANTHER; PTHR22594; ASPARTYL/LYSYL-TRNA SYNTHETASE; 1.
DR   Pfam; PF00152; tRNA-synt_2; 2.
DR   Pfam; PF01336; tRNA_anti-codon; 1.
DR   PRINTS; PR01042; TRNASYNTHASP.
DR   SMART; SM00991; WHEP-TRS; 1.
DR   SUPFAM; SSF55681; Class II aaRS and biotin synthetases; 1.
DR   SUPFAM; SSF50249; Nucleic acid-binding proteins; 1.
DR   PROSITE; PS50862; AA_TRNA_LIGASE_II; 1.
DR   PROSITE; PS51185; WHEP_TRS_2; 1.
PE   1: Evidence at protein level;
KW   Acetylation; Aminoacyl-tRNA synthetase; ATP-binding; Cytoplasm;
KW   DNA-binding; Ligase; Nucleotide-binding; Protein biosynthesis;
KW   Reference proteome.
FT   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0007744|PubMed:22223895"
FT   CHAIN           2..572
FT                   /note="Asparagine--tRNA ligase, cytoplasmic 1"
FT                   /id="PRO_0000176491"
FT   DOMAIN          236..292
FT                   /note="WHEP-TRS"
FT   DNA_BIND        53..131
FT                   /note="OB"
FT                   /evidence="ECO:0000255"
FT   MOD_RES         2
FT                   /note="N-acetylalanine"
FT                   /evidence="ECO:0007744|PubMed:22223895"
SQ   SEQUENCE   572 AA;  63783 MW;  DBFBCF0139A48770 CRC64;
     MADEIVPPAT QLAAVSLEND GSTVQRAQFS NRVLIRTILD RPDGGAGLAG QTVRIGGWVK
     SGRDQGKRTF SFLAVNDGSC PANLQVMVDP SLYDVSNLVA TGTCVTVDGV LKVPPKGKGT
     QQQIELNVVK VIDVGTVDAS KYPLPKTKLT LETLRDVLHL RSRTNSISAV ARIRNALAFA
     THSFFQEHSF LYIHTPIITT SDCEGAGEMF QATTLINYTE RLEQDLIDNP PPTEADVEAA
     RLIVIERGNV VAELKAAKAS KEAITAAVAE LKIAKETFAH IDERSRLRPG LPKKDGNIDY
     SKDFFGRQAF LTVSGQLQVE TYACALSNVY TFGPTFRAEN SHTSRHLAEF WMVEPEIAFA
     DLEDDMNCAE AYVKYMCNWL LEKCYADMEL MAKNFDSGCI DRLKLVASTP FGRITYTKAI
     ELLEEAVAKG KEFDNNVEWG IDLASEHERY LTEVLFQKPL IVYNYPKGIK AFYMRLNDDE
     KTVAAMDVLV PKVGELIGGS QREERYDVIK KRIEEMGLPI EPYEWYLDLR RYGTVKHCGF
     GLGFERMILF ATGLDNIRDV IPFPRYPGKA DL
//