SYNC1_ARATH
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 25-MAY-2022, entry version 158.
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 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 [5]
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 [6]
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 [7]
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=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: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; BT030358; ABO38771.1; -; mRNA.
DR RefSeq; NP_200479.1; NM_125051.4.
DR AlphaFoldDB; Q9SW96; -.
DR SMR; Q9SW96; -.
DR BioGRID; 21013; 2.
DR IntAct; Q9SW96; 1.
DR STRING; 3702.AT5G56680.1; -.
DR iPTMnet; Q9SW96; -.
DR PaxDb; Q9SW96; -.
DR PRIDE; Q9SW96; -.
DR ProteomicsDB; 245286; -.
DR EnsemblPlants; AT5G56680.1; AT5G56680.1; AT5G56680.
DR GeneID; 835769; -.
DR Gramene; AT5G56680.1; AT5G56680.1; AT5G56680.
DR KEGG; ath:AT5G56680; -.
DR Araport; AT5G56680; -.
DR TAIR; locus:2165001; AT5G56680.
DR eggNOG; KOG0554; Eukaryota.
DR HOGENOM; CLU_004553_2_0_1; -.
DR InParanoid; Q9SW96; -.
DR OMA; DNMDLAE; -.
DR OrthoDB; 1056670at2759; -.
DR PhylomeDB; Q9SW96; -.
DR PRO; PR:Q9SW96; -.
DR Proteomes; UP000006548; Chromosome 5.
DR ExpressionAtlas; Q9SW96; baseline and differential.
DR Genevisible; Q9SW96; AT.
DR GO; GO:0009507; C:chloroplast; IDA: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:UniProtKB-KW.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
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 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 InterPro; IPR000738; WHEP-TRS_dom.
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; SSF50249; SSF50249; 1.
DR SUPFAM; SSF55681; SSF55681; 1.
DR TIGRFAMs; TIGR00457; asnS; 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
