SYNO_ARATH
ID SYNO_ARATH Reviewed; 567 AA.
AC O48593; O23573; Q564D6;
DT 31-JAN-2002, integrated into UniProtKB/Swiss-Prot.
DT 09-NOV-2004, sequence version 3.
DT 25-MAY-2022, entry version 153.
DE RecName: Full=Asparagine--tRNA ligase, chloroplastic/mitochondrial {ECO:0000305};
DE EC=6.1.1.22 {ECO:0000305};
DE AltName: Full=Asparaginyl-tRNA synthetase {ECO:0000305};
DE Short=AsnRS {ECO:0000305};
DE AltName: Full=AtNS1 {ECO:0000303|PubMed:9655910};
DE AltName: Full=Protein OVULE ABORTION 8 {ECO:0000303|PubMed:16297076};
DE Flags: Precursor;
GN Name=SYNO {ECO:0000303|PubMed:10824085};
GN Synonyms=NS1 {ECO:0000303|PubMed:9655910},
GN OVA8 {ECO:0000303|PubMed:16297076}; OrderedLocusNames=At4g17300;
GN ORFNames=dl4685w;
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=9461215; DOI=10.1038/35140;
RA Bevan M., Bancroft I., Bent E., Love K., Goodman H.M., Dean C.,
RA Bergkamp R., Dirkse W., van Staveren M., Stiekema W., Drost L., Ridley P.,
RA Hudson S.-A., Patel K., Murphy G., Piffanelli P., Wedler H., Wedler E.,
RA Wambutt R., Weitzenegger T., Pohl T., Terryn N., Gielen J., Villarroel R.,
RA De Clercq R., van Montagu M., Lecharny A., Aubourg S., Gy I., Kreis M.,
RA Lao N., Kavanagh T., Hempel S., Kotter P., Entian K.-D., Rieger M.,
RA Schaefer M., Funk B., Mueller-Auer S., Silvey M., James R., Monfort A.,
RA Pons A., Puigdomenech P., Douka A., Voukelatou E., Milioni D.,
RA Hatzopoulos P., Piravandi E., Obermaier B., Hilbert H., Duesterhoeft A.,
RA Moores T., Jones J.D.G., Eneva T., Palme K., Benes V., Rechmann S.,
RA Ansorge W., Cooke R., Berger C., Delseny M., Voet M., Volckaert G.,
RA Mewes H.-W., Klosterman S., Schueller C., Chalwatzis N.;
RT "Analysis of 1.9 Mb of contiguous sequence from chromosome 4 of Arabidopsis
RT thaliana.";
RL Nature 391:485-488(1998).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=10617198; DOI=10.1038/47134;
RA Mayer K.F.X., Schueller C., Wambutt R., Murphy G., Volckaert G., Pohl T.,
RA Duesterhoeft A., Stiekema W., Entian K.-D., Terryn N., Harris B.,
RA Ansorge W., Brandt P., Grivell L.A., Rieger M., Weichselgartner M.,
RA de Simone V., Obermaier B., Mache R., Mueller M., Kreis M., Delseny M.,
RA Puigdomenech P., Watson M., Schmidtheini T., Reichert B., Portetelle D.,
RA Perez-Alonso M., Boutry M., Bancroft I., Vos P., Hoheisel J.,
RA Zimmermann W., Wedler H., Ridley P., Langham S.-A., McCullagh B.,
RA Bilham L., Robben J., van der Schueren J., Grymonprez B., Chuang Y.-J.,
RA Vandenbussche F., Braeken M., Weltjens I., Voet M., Bastiaens I., Aert R.,
RA Defoor E., Weitzenegger T., Bothe G., Ramsperger U., Hilbert H., Braun M.,
RA Holzer E., Brandt A., Peters S., van Staveren M., Dirkse W., Mooijman P.,
RA Klein Lankhorst R., Rose M., Hauf J., Koetter P., Berneiser S., Hempel S.,
RA Feldpausch M., Lamberth S., Van den Daele H., De Keyser A., Buysshaert C.,
RA Gielen J., Villarroel R., De Clercq R., van Montagu M., Rogers J.,
RA Cronin A., Quail M.A., Bray-Allen S., Clark L., Doggett J., Hall S.,
RA Kay M., Lennard N., McLay K., Mayes R., Pettett A., Rajandream M.A.,
RA Lyne M., Benes V., Rechmann S., Borkova D., Bloecker H., Scharfe M.,
RA Grimm M., Loehnert T.-H., Dose S., de Haan M., Maarse A.C., Schaefer M.,
RA Mueller-Auer S., Gabel C., Fuchs M., Fartmann B., Granderath K., Dauner D.,
RA Herzl A., Neumann S., Argiriou A., Vitale D., Liguori R., Piravandi E.,
RA Massenet O., Quigley F., Clabauld G., Muendlein A., Felber R., Schnabl S.,
RA Hiller R., Schmidt W., Lecharny A., Aubourg S., Chefdor F., Cooke R.,
RA Berger C., Monfort A., Casacuberta E., Gibbons T., Weber N., Vandenbol M.,
RA Bargues M., Terol J., Torres A., Perez-Perez A., Purnelle B., Bent E.,
RA Johnson S., Tacon D., Jesse T., Heijnen L., Schwarz S., Scholler P.,
RA Heber S., Francs P., Bielke C., Frishman D., Haase D., Lemcke K.,
RA Mewes H.-W., Stocker S., Zaccaria P., Bevan M., Wilson R.K.,
RA de la Bastide M., Habermann K., Parnell L., Dedhia N., Gnoj L., Schutz K.,
RA Huang E., Spiegel L., Sekhon M., Murray J., Sheet P., Cordes M.,
RA Abu-Threideh J., Stoneking T., Kalicki J., Graves T., Harmon G.,
RA Edwards J., Latreille P., Courtney L., Cloud J., Abbott A., Scott K.,
RA Johnson D., Minx P., Bentley D., Fulton B., Miller N., Greco T., Kemp K.,
RA Kramer J., Fulton L., Mardis E., Dante M., Pepin K., Hillier L.W.,
RA Nelson J., Spieth J., Ryan E., Andrews S., Geisel C., Layman D., Du H.,
RA Ali J., Berghoff A., Jones K., Drone K., Cotton M., Joshu C., Antonoiu B.,
RA Zidanic M., Strong C., Sun H., Lamar B., Yordan C., Ma P., Zhong J.,
RA Preston R., Vil D., Shekher M., Matero A., Shah R., Swaby I.K.,
RA O'Shaughnessy A., Rodriguez M., Hoffman J., Till S., Granat S., Shohdy N.,
RA Hasegawa A., Hameed A., Lodhi M., Johnson A., Chen E., Marra M.A.,
RA Martienssen R., McCombie W.R.;
RT "Sequence and analysis of chromosome 4 of the plant Arabidopsis thaliana.";
RL Nature 402:769-777(1999).
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=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 [5]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 2-566.
RC STRAIN=cv. Columbia;
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 [6]
RP SUBCELLULAR LOCATION.
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 [7]
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).
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: Plastid, chloroplast
CC {ECO:0000269|PubMed:10824085}. Mitochondrion
CC {ECO:0000269|PubMed:10824085}.
CC -!- DISRUPTION PHENOTYPE: Lethal. In heterozygous plants, aborted ovules.
CC {ECO:0000269|PubMed:16297076}.
CC -!- SIMILARITY: Belongs to the class-II aminoacyl-tRNA synthetase family.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAB10511.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC Sequence=CAB78733.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; Z97343; CAB10511.1; ALT_SEQ; Genomic_DNA.
DR EMBL; AL161546; CAB78733.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002687; AEE83874.1; -; Genomic_DNA.
DR EMBL; AY078967; AAL84964.1; -; mRNA.
DR EMBL; AJ222644; CAA10904.1; -; mRNA.
DR RefSeq; NP_193462.1; NM_117835.5.
DR AlphaFoldDB; O48593; -.
DR SMR; O48593; -.
DR STRING; 3702.AT4G17300.1; -.
DR PaxDb; O48593; -.
DR PRIDE; O48593; -.
DR ProteomicsDB; 228467; -.
DR EnsemblPlants; AT4G17300.1; AT4G17300.1; AT4G17300.
DR GeneID; 827443; -.
DR Gramene; AT4G17300.1; AT4G17300.1; AT4G17300.
DR KEGG; ath:AT4G17300; -.
DR Araport; AT4G17300; -.
DR TAIR; locus:2130804; AT4G17300.
DR eggNOG; KOG0554; Eukaryota.
DR HOGENOM; CLU_004553_2_0_1; -.
DR InParanoid; O48593; -.
DR PhylomeDB; O48593; -.
DR PRO; PR:O48593; -.
DR Proteomes; UP000006548; Chromosome 4.
DR ExpressionAtlas; O48593; baseline and differential.
DR Genevisible; O48593; AT.
DR GO; GO:0009507; C:chloroplast; IDA:TAIR.
DR GO; GO:0009570; C:chloroplast stroma; HDA:TAIR.
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:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR GO; GO:0006421; P:asparaginyl-tRNA aminoacylation; ISS:TAIR.
DR GO; GO:0048481; P:plant ovule development; 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 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 2: Evidence at transcript level;
KW Aminoacyl-tRNA synthetase; ATP-binding; Chloroplast; DNA-binding; Ligase;
KW Mitochondrion; Nucleotide-binding; Plastid; Protein biosynthesis;
KW Reference proteome; Transit peptide.
FT TRANSIT 1..?
FT /note="Chloroplast and mitochondrion"
FT /evidence="ECO:0000255"
FT CHAIN ?..567
FT /note="Asparagine--tRNA ligase,
FT chloroplastic/mitochondrial"
FT /id="PRO_0000035800"
FT DNA_BIND 113..191
FT /note="OB"
FT /evidence="ECO:0000255"
FT CONFLICT 279
FT /note="N -> Y (in Ref. 5; CAA10904)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 567 AA; 63698 MW; D5CAE4EBB7780264 CRC64;
MAATFLPATS LRLTQNSTLR FLSFFTISNP SYSLFRPLRR RVLPPFDAFP ANSRRRCFCT
AVSESLGSGD GNKVESYEKR FGSKVGEFRK KLRIAEVKGG ADEGLSRVGQ SLNIMGWVRT
LRSQSSVTFI EINDGSCLSN LQCVMTSDAE GYDQVESGSI LTGASVSVQG TIVASQGTKQ
KVELKVEKII VVGECDSSYP IQKKRVSREF LRTKAHLRPR TNTFGAVARV RNTLAYATHK
FFQESGFVWV ASPIITASDC EGAGEQFCVT TLIPSSHENT DTSIDAIPKT KGGLIDWSQD
FFGKPAFLTV SGQLNGETYA TALSDVYTFG PTFRAENSNT SRHLAEFWMI EPELAFADLD
DDMACATAYL QYVVKYVLDN CKEDMEFFDT WIEKGIIRRL SDVAEKEFLQ LGYTDAIEIL
LKANKKFDFP VKWGLDLQSE HERYITEEAF GGRPVIIRDY PKEIKAFYMR ENDDGKTVAA
MDMLVPRIGE LIGGSQREER LEVLEARLDE LKLNKESYWW YLDLRRYGSV PHAGFGLGFE
RLVQFVTGID NIRDVIPFPR TPASAEF
