SYNC2_ARATH
ID SYNC2_ARATH Reviewed; 638 AA.
AC Q9SW95; O48594; Q8GZ48; Q9SRS4;
DT 31-JAN-2002, integrated into UniProtKB/Swiss-Prot.
DT 31-JAN-2002, sequence version 2.
DT 25-MAY-2022, entry version 146.
DE RecName: Full=Asparagine--tRNA ligase, cytoplasmic 2 {ECO:0000305};
DE EC=6.1.1.22 {ECO:0000305};
DE AltName: Full=Asparaginyl-tRNA synthetase 2 {ECO:0000305};
DE Short=AsnRS 2 {ECO:0000305};
DE AltName: Full=AtNS2 {ECO:0000303|PubMed:9655910};
GN Name=SYNC2 {ECO:0000303|PubMed:10824085};
GN Synonyms=NS2 {ECO:0000303|PubMed:9655910}; OrderedLocusNames=At3g07420;
GN ORFNames=F21O3.13;
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=11130713; DOI=10.1038/35048706;
RA Salanoubat M., Lemcke K., Rieger M., Ansorge W., Unseld M., Fartmann B.,
RA Valle G., Bloecker H., Perez-Alonso M., Obermaier B., Delseny M.,
RA Boutry M., Grivell L.A., Mache R., Puigdomenech P., De Simone V.,
RA Choisne N., Artiguenave F., Robert C., Brottier P., Wincker P.,
RA Cattolico L., Weissenbach J., Saurin W., Quetier F., Schaefer M.,
RA Mueller-Auer S., Gabel C., Fuchs M., Benes V., Wurmbach E., Drzonek H.,
RA Erfle H., Jordan N., Bangert S., Wiedelmann R., Kranz H., Voss H.,
RA Holland R., Brandt P., Nyakatura G., Vezzi A., D'Angelo M., Pallavicini A.,
RA Toppo S., Simionati B., Conrad A., Hornischer K., Kauer G., Loehnert T.-H.,
RA Nordsiek G., Reichelt J., Scharfe M., Schoen O., Bargues M., Terol J.,
RA Climent J., Navarro P., Collado C., Perez-Perez A., Ottenwaelder B.,
RA Duchemin D., Cooke R., Laudie M., Berger-Llauro C., Purnelle B., Masuy D.,
RA de Haan M., Maarse A.C., Alcaraz J.-P., Cottet A., Casacuberta E.,
RA Monfort A., Argiriou A., Flores M., Liguori R., Vitale D., Mannhaupt G.,
RA Haase D., Schoof H., Rudd S., Zaccaria P., Mewes H.-W., Mayer K.F.X.,
RA Kaul S., Town C.D., Koo H.L., Tallon L.J., Jenkins J., Rooney T., Rizzo M.,
RA Walts A., Utterback T., Fujii C.Y., Shea T.P., Creasy T.H., Haas B.,
RA Maiti R., Wu D., Peterson J., Van Aken S., Pai G., Militscher J.,
RA Sellers P., Gill J.E., Feldblyum T.V., Preuss D., Lin X., Nierman W.C.,
RA Salzberg S.L., White O., Venter J.C., Fraser C.M., Kaneko T., Nakamura Y.,
RA Sato S., Kato T., Asamizu E., Sasamoto S., Kimura T., Idesawa K.,
RA Kawashima K., Kishida Y., Kiyokawa C., Kohara M., Matsumoto M., Matsuno A.,
RA Muraki A., Nakayama S., Nakazaki N., Shinpo S., Takeuchi C., Wada T.,
RA Watanabe A., Yamada M., Yasuda M., Tabata S.;
RT "Sequence and analysis of chromosome 3 of the plant Arabidopsis thaliana.";
RL Nature 408:820-822(2000).
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;
RX PubMed=11910074; DOI=10.1126/science.1071006;
RA Seki M., Narusaka M., Kamiya A., Ishida J., Satou M., Sakurai T.,
RA Nakajima M., Enju A., Akiyama K., Oono Y., Muramatsu M., Hayashizaki Y.,
RA Kawai J., Carninci P., Itoh M., Ishii Y., Arakawa T., Shibata K.,
RA Shinagawa A., Shinozaki K.;
RT "Functional annotation of a full-length Arabidopsis cDNA collection.";
RL Science 296:141-145(2002).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. Columbia;
RX PubMed=14593172; DOI=10.1126/science.1088305;
RA Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J., Southwick A.M.,
RA Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., Karlin-Newmann G.,
RA Liu S.X., Lam B., Sakano H., Wu T., Yu G., Miranda M., Quach H.L.,
RA Tripp M., Chang C.H., Lee J.M., Toriumi M.J., Chan M.M., Tang C.C.,
RA Onodera C.S., Deng J.M., Akiyama K., Ansari Y., Arakawa T., Banh J.,
RA Banno F., Bowser L., Brooks S.Y., Carninci P., Chao Q., Choy N., Enju A.,
RA Goldsmith A.D., Gurjal M., Hansen N.F., Hayashizaki Y., Johnson-Hopson C.,
RA Hsuan V.W., Iida K., Karnes M., Khan S., Koesema E., Ishida J., Jiang P.X.,
RA Jones T., Kawai J., Kamiya A., Meyers C., Nakajima M., Narusaka M.,
RA Seki M., Sakurai T., Satou M., Tamse R., Vaysberg M., Wallender E.K.,
RA Wong C., Yamamura Y., Yuan S., Shinozaki K., Davis R.W., Theologis A.,
RA Ecker J.R.;
RT "Empirical analysis of transcriptional activity in the Arabidopsis
RT genome.";
RL Science 302:842-846(2003).
RN [6]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 363-638.
RC STRAIN=cv. Columbia; TISSUE=Leaf;
RX PubMed=9655910; DOI=10.1016/s0167-4781(98)00068-2;
RA Aubourg S., Cheron A., Kreis M., Lecharny A.;
RT "Structure and expression of an asparaginyl-tRNA synthetase gene located on
RT chromosome IV of Arabidopsis thaliana and adjacent to a novel large gene of
RT 15 exons.";
RL Biochim. Biophys. Acta 1398:225-231(1998).
RN [7]
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 [8]
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 [9]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19376835; DOI=10.1104/pp.109.138677;
RA Reiland S., Messerli G., Baerenfaller K., Gerrits B., Endler A.,
RA Grossmann J., Gruissem W., Baginsky S.;
RT "Large-scale Arabidopsis phosphoproteome profiling reveals novel
RT chloroplast kinase substrates and phosphorylation networks.";
RL Plant Physiol. 150:889-903(2009).
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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AF170910; AAD46682.1; -; mRNA.
DR EMBL; AC009853; AAF02166.1; -; Genomic_DNA.
DR EMBL; CP002686; AEE74540.1; -; Genomic_DNA.
DR EMBL; AK117215; BAC41891.1; -; mRNA.
DR EMBL; BT005942; AAO64877.1; -; mRNA.
DR EMBL; AJ222645; CAA10905.1; -; mRNA.
DR RefSeq; NP_187398.1; NM_111621.4.
DR AlphaFoldDB; Q9SW95; -.
DR SMR; Q9SW95; -.
DR IntAct; Q9SW95; 1.
DR STRING; 3702.AT3G07420.1; -.
DR iPTMnet; Q9SW95; -.
DR PaxDb; Q9SW95; -.
DR PRIDE; Q9SW95; -.
DR ProteomicsDB; 228480; -.
DR EnsemblPlants; AT3G07420.1; AT3G07420.1; AT3G07420.
DR GeneID; 819930; -.
DR Gramene; AT3G07420.1; AT3G07420.1; AT3G07420.
DR KEGG; ath:AT3G07420; -.
DR Araport; AT3G07420; -.
DR TAIR; locus:2079646; AT3G07420.
DR eggNOG; KOG0554; Eukaryota.
DR HOGENOM; CLU_004553_2_0_1; -.
DR InParanoid; Q9SW95; -.
DR OMA; THATHNF; -.
DR OrthoDB; 1056670at2759; -.
DR PhylomeDB; Q9SW95; -.
DR PRO; PR:Q9SW95; -.
DR Proteomes; UP000006548; Chromosome 3.
DR ExpressionAtlas; Q9SW95; baseline and differential.
DR Genevisible; Q9SW95; AT.
DR GO; GO:0009507; C:chloroplast; IDA:TAIR.
DR GO; GO:0005829; C:cytosol; IEA:UniProtKB-SubCell.
DR GO; GO:0005739; C:mitochondrion; IDA:TAIR.
DR GO; GO:0004816; F:asparagine-tRNA ligase activity; ISS:TAIR.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0006421; P:asparaginyl-tRNA aminoacylation; ISS:TAIR.
DR Gene3D; 3.30.930.10; -; 1.
DR InterPro; IPR004364; Aa-tRNA-synt_II.
DR InterPro; IPR045864; aa-tRNA-synth_II/BPL/LPL.
DR InterPro; IPR004522; Asn-tRNA-ligase.
DR Pfam; PF00152; tRNA-synt_2; 1.
DR SUPFAM; SSF55681; SSF55681; 1.
DR TIGRFAMs; TIGR00457; asnS; 1.
PE 1: Evidence at protein level;
KW Aminoacyl-tRNA synthetase; ATP-binding; Cytoplasm; Ligase;
KW Nucleotide-binding; Protein biosynthesis; Reference proteome.
FT CHAIN 1..638
FT /note="Asparagine--tRNA ligase, cytoplasmic 2"
FT /id="PRO_0000176492"
FT REGION 1..23
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 62..87
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..18
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CONFLICT 24
FT /note="S -> L (in Ref. 1; AAD46682)"
FT /evidence="ECO:0000305"
FT CONFLICT 284
FT /note="L -> F (in Ref. 1; AAD46682)"
FT /evidence="ECO:0000305"
FT CONFLICT 329
FT /note="R -> Q (in Ref. 1; AAD46682)"
FT /evidence="ECO:0000305"
FT CONFLICT 460
FT /note="S -> L (in Ref. 4; AAO64877 and 5; CAA10905)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 638 AA; 71364 MW; C90838CF5649FF8C CRC64;
MESHGKTHQK EHDNDLSPKP ITLSKYSKRV ELKTLLDRSD RGAGLAGKRV VIGGWVKSAR
AVKKNSPPPP LPVVAAPSPS SGGDQAHTTA NIRCTEIIQS KMNIFKRFFD VLSGGGKTYP
IFDKTELAGQ KAVPPPEYVF YFLISDGSSI SSLQVVVDSA LSTVPATQLM ALGTCIVAEG
VLRLPLAASA KHVIELEAEK LLHVGTVDPE KYPLSKKQLP LHMLRDFSHF RPRTTTVGSV
TRVHSALTLA SHTFLQYHGF QYVQVPVITT TTGFGEMFRV TTLLGKTDDK EEKKPPVQEK
DGFSIDTVKA VIKEKTRLID HLKRSDSNRE TVVAAVHDLK KTNDLASQIE MKQKSKTGTL
VKPEKLDFSK DFFGRDTYLT ASGRFHLESY ASALGKVYTF GPRFIADKID NARHLAEKWN
VETEMAFAEL DDAMDCADEY FKFLCKYVLE NRDEDMKFIS KRVDKTITTR LEATASSSLL
RFSYTEVISL LQKATTTKFE TKPEWGVALT TEHLSYLTDE IYKGPVIVHT YPKAIKQFYV
RLNDDKKTVA AFDLVVPKVG VVITGSQNEE RFEILDARIG ESGFTREKFE WYLDLRRHGT
VKHSGISLSM EQMLLYATGL PDIKDAIPFP RSWGKANN
