SYNC3_ARATH
ID SYNC3_ARATH Reviewed; 571 AA.
AC Q9SSK1;
DT 31-JAN-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 25-MAY-2022, entry version 146.
DE RecName: Full=Asparagine--tRNA ligase, cytoplasmic 3 {ECO:0000305};
DE EC=6.1.1.22 {ECO:0000305};
DE AltName: Full=Asparaginyl-tRNA synthetase 3 {ECO:0000305};
DE Short=AsnRS 3 {ECO:0000305};
GN Name=SYNC3 {ECO:0000305}; OrderedLocusNames=At1g70980; ORFNames=F15H11.17;
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 [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=11130712; DOI=10.1038/35048500;
RA Theologis A., Ecker J.R., Palm C.J., Federspiel N.A., Kaul S., White O.,
RA Alonso J., Altafi H., Araujo R., Bowman C.L., Brooks S.Y., Buehler E.,
RA Chan A., Chao Q., Chen H., Cheuk R.F., Chin C.W., Chung M.K., Conn L.,
RA Conway A.B., Conway A.R., Creasy T.H., Dewar K., Dunn P., Etgu P.,
RA Feldblyum T.V., Feng J.-D., Fong B., Fujii C.Y., Gill J.E., Goldsmith A.D.,
RA Haas B., Hansen N.F., Hughes B., Huizar L., Hunter J.L., Jenkins J.,
RA Johnson-Hopson C., Khan S., Khaykin E., Kim C.J., Koo H.L.,
RA Kremenetskaia I., Kurtz D.B., Kwan A., Lam B., Langin-Hooper S., Lee A.,
RA Lee J.M., Lenz C.A., Li J.H., Li Y.-P., Lin X., Liu S.X., Liu Z.A.,
RA Luros J.S., Maiti R., Marziali A., Militscher J., Miranda M., Nguyen M.,
RA Nierman W.C., Osborne B.I., Pai G., Peterson J., Pham P.K., Rizzo M.,
RA Rooney T., Rowley D., Sakano H., Salzberg S.L., Schwartz J.R., Shinn P.,
RA Southwick A.M., Sun H., Tallon L.J., Tambunga G., Toriumi M.J., Town C.D.,
RA Utterback T., Van Aken S., Vaysberg M., Vysotskaia V.S., Walker M., Wu D.,
RA Yu G., Fraser C.M., Venter J.C., Davis R.W.;
RT "Sequence and analysis of chromosome 1 of the plant Arabidopsis thaliana.";
RL Nature 408:816-820(2000).
RN [2]
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 [3]
RP SUBCELLULAR LOCATION.
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 [4]
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 [5]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT GLY-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 ECO:0000305|PubMed:16297076}.
CC -!- SIMILARITY: Belongs to the class-II aminoacyl-tRNA synthetase family.
CC {ECO:0000305}.
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DR EMBL; AC008148; AAD55509.1; -; Genomic_DNA.
DR EMBL; CP002684; AEE35146.1; -; Genomic_DNA.
DR PIR; B96734; B96734.
DR RefSeq; NP_177254.1; NM_105766.3.
DR AlphaFoldDB; Q9SSK1; -.
DR SMR; Q9SSK1; -.
DR BioGRID; 28656; 2.
DR STRING; 3702.AT1G70980.1; -.
DR iPTMnet; Q9SSK1; -.
DR PaxDb; Q9SSK1; -.
DR PRIDE; Q9SSK1; -.
DR ProteomicsDB; 234128; -.
DR EnsemblPlants; AT1G70980.1; AT1G70980.1; AT1G70980.
DR GeneID; 843436; -.
DR Gramene; AT1G70980.1; AT1G70980.1; AT1G70980.
DR KEGG; ath:AT1G70980; -.
DR Araport; AT1G70980; -.
DR TAIR; locus:2014005; AT1G70980.
DR eggNOG; KOG0554; Eukaryota.
DR HOGENOM; CLU_004553_2_0_1; -.
DR InParanoid; Q9SSK1; -.
DR OMA; FVSPGHE; -.
DR OrthoDB; 1056670at2759; -.
DR PhylomeDB; Q9SSK1; -.
DR PRO; PR:Q9SSK1; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; Q9SSK1; baseline and differential.
DR Genevisible; Q9SSK1; AT.
DR GO; GO:0005829; C:cytosol; IEA:UniProtKB-SubCell.
DR GO; GO:0005739; C:mitochondrion; IBA:GO_Central.
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 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..571
FT /note="Asparagine--tRNA ligase, cytoplasmic 3"
FT /id="PRO_0000176493"
FT DOMAIN 233..289
FT /note="WHEP-TRS"
FT DNA_BIND 50..128
FT /note="OB"
FT /evidence="ECO:0000255"
FT MOD_RES 2
FT /note="N-acetylglycine"
FT /evidence="ECO:0007744|PubMed:22223895"
SQ SEQUENCE 571 AA; 63700 MW; 1D5BF624B55FA1AE CRC64;
MGDEIVPPAN QLAADNLEND GSTVQKAQFS DRVLIRSILG GGAKLAGQKV RIGGWVKTGR
QQGKGTFAFL EVNDGSCPAN LQVMVDSSLY DLSRLVATGT CVTVDGVLKI PPEGKGLKQS
IELSVETVIA VGTVDPTTYP LPKTKLTPEF LRDVLHLRSR TNLISAVARI RNALAFATHS
FFQEHSFLYI HTPIITTSDC EGAGEMFQVT TLINHTERVE QDLIDNPPPT EADVEAARLI
VKERGEAVAQ LKVAKASKEE ITASVAQLSV AKASLAHVEE RLRLKPGLPK NDGKIDYSND
FFGRQAFLTV SGQLQVETYA CALSSVYTFG PTFRAENSHT SRHLAEFWMV EPEIAFADIH
DDMNCAEAYV KYMCKWLMDK CGDDMELMDK NVDEGCTKRL NMVAKASFKR VTYTEAIERL
EKAVAQGKVV FDNKVEWGID LASEHERYLT EVEFDQKPII VYNYPKGIKA FYMRLNDDEK
TVAAMDVLVP KVGELIGGSQ REERYDVIKQ RIEEMGLPME PYEWYLDLRR YGTVKHCGFG
LGFERMIQFA TGIDNIRDVI PFPRYPGKAD L
