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 30-NOV-2016, entry version 126.
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; Magnoliophyta; eudicotyledons; Gunneridae;
OC Pentapetalae; rosids; malvids; Brassicales; Brassicaceae; Camelineae;
OC 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.,
RA Ridley P., Hudson S.-A., Patel K., Murphy G., Piffanelli P.,
RA Wedler H., Wedler E., Wambutt R., Weitzenegger T., Pohl T., Terryn N.,
RA Gielen J., Villarroel R., De Clercq R., van Montagu M., Lecharny A.,
RA Aubourg S., Gy I., Kreis M., Lao N., Kavanagh T., Hempel S.,
RA Kotter P., Entian K.-D., Rieger M., Schaefer M., Funk B.,
RA Mueller-Auer S., Silvey M., James R., Monfort A., Pons A.,
RA Puigdomenech P., Douka A., Voukelatou E., Milioni D., Hatzopoulos P.,
RA Piravandi E., Obermaier B., Hilbert H., Duesterhoeft A., Moores T.,
RA Jones J.D.G., Eneva T., Palme K., Benes V., Rechmann S., Ansorge W.,
RA Cooke R., Berger C., Delseny M., Voet M., Volckaert G., Mewes H.-W.,
RA Klosterman S., Schueller C., Chalwatzis N.;
RT "Analysis of 1.9 Mb of contiguous sequence from chromosome 4 of
RT Arabidopsis 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.,
RA Pohl T., Duesterhoeft A., Stiekema W., Entian K.-D., Terryn N.,
RA Harris B., Ansorge W., Brandt P., Grivell L.A., Rieger M.,
RA Weichselgartner M., de Simone V., Obermaier B., Mache R., Mueller M.,
RA Kreis M., Delseny M., Puigdomenech P., Watson M., Schmidtheini T.,
RA Reichert B., Portetelle D., Perez-Alonso M., Boutry M., Bancroft I.,
RA Vos P., Hoheisel J., Zimmermann W., Wedler H., Ridley P.,
RA Langham S.-A., McCullagh B., Bilham L., Robben J.,
RA van der Schueren J., Grymonprez B., Chuang Y.-J., Vandenbussche F.,
RA Braeken M., Weltjens I., Voet M., Bastiaens I., Aert R., Defoor E.,
RA Weitzenegger T., Bothe G., Ramsperger U., Hilbert H., Braun M.,
RA Holzer E., Brandt A., Peters S., van Staveren M., Dirkse W.,
RA Mooijman P., Klein Lankhorst R., Rose M., Hauf J., Koetter P.,
RA Berneiser S., Hempel S., Feldpausch M., Lamberth S., Van den Daele H.,
RA De Keyser A., Buysshaert C., Gielen J., Villarroel R., De Clercq R.,
RA van Montagu M., Rogers J., Cronin A., Quail M.A., Bray-Allen S.,
RA Clark L., Doggett J., Hall S., Kay M., Lennard N., McLay K., Mayes R.,
RA Pettett A., Rajandream M.A., Lyne M., Benes V., Rechmann S.,
RA Borkova D., Bloecker H., Scharfe M., Grimm M., Loehnert T.-H.,
RA Dose S., de Haan M., Maarse A.C., Schaefer M., Mueller-Auer S.,
RA Gabel C., Fuchs M., Fartmann B., Granderath K., Dauner D., Herzl A.,
RA Neumann S., Argiriou A., Vitale D., Liguori R., Piravandi E.,
RA Massenet O., Quigley F., Clabauld G., Muendlein A., Felber R.,
RA Schnabl S., Hiller R., Schmidt W., Lecharny A., Aubourg S.,
RA Chefdor F., Cooke R., Berger C., Monfort A., Casacuberta E.,
RA Gibbons T., Weber N., Vandenbol M., Bargues M., Terol J., Torres A.,
RA Perez-Perez A., Purnelle B., Bent E., Johnson S., Tacon D., Jesse T.,
RA Heijnen L., Schwarz S., Scholler P., Heber S., Francs P., Bielke C.,
RA Frishman D., Haase D., Lemcke K., Mewes H.-W., Stocker S.,
RA Zaccaria P., Bevan M., Wilson R.K., de la Bastide M., Habermann K.,
RA Parnell L., Dedhia N., Gnoj L., Schutz K., Huang E., Spiegel L.,
RA Sekhon M., Murray J., Sheet P., Cordes M., Abu-Threideh J.,
RA Stoneking T., Kalicki J., Graves T., Harmon G., Edwards J.,
RA Latreille P., Courtney L., Cloud J., Abbott A., Scott K., Johnson D.,
RA 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.,
RA Du H., Ali J., Berghoff A., Jones K., Drone K., Cotton M., Joshu C.,
RA Antonoiu B., Zidanic M., Strong C., Sun H., Lamar B., Yordan C.,
RA Ma P., Zhong J., Preston R., Vil D., Shekher M., Matero A., Shah R.,
RA Swaby I.K., O'Shaughnessy A., Rodriguez M., Hoffman J., Till S.,
RA Granat S., Shohdy N., Hasegawa A., Hameed A., Lodhi M., Johnson A.,
RA Chen E., Marra M.A., Martienssen R., McCombie W.R.;
RT "Sequence and analysis of chromosome 4 of the plant Arabidopsis
RT thaliana.";
RL Nature 402:769-777(1999).
RN [3]
RP GENOME REANNOTATION.
RC STRAIN=cv. Columbia;
RG The Arabidopsis Information Resource (TAIR);
RL Submitted (APR-2011) to the EMBL/GenBank/DDBJ databases.
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.,
RA Southwick A.M., Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F.,
RA Karlin-Newmann G., Liu S.X., Lam B., Sakano H., Wu T., Yu G.,
RA Miranda M., Quach H.L., Tripp M., Chang C.H., Lee J.M., Toriumi M.J.,
RA Chan M.M., Tang C.C., Onodera C.S., Deng J.M., Akiyama K., Ansari Y.,
RA Arakawa T., Banh J., Banno F., Bowser L., Brooks S.Y., Carninci P.,
RA Chao Q., Choy N., Enju A., Goldsmith A.D., Gurjal M., Hansen N.F.,
RA Hayashizaki Y., Johnson-Hopson C., Hsuan V.W., Iida K., Karnes M.,
RA Khan S., Koesema E., Ishida J., Jiang P.X., Jones T., Kawai J.,
RA Kamiya A., Meyers C., Nakajima M., Narusaka M., Seki M., Sakurai T.,
RA Satou M., Tamse R., Vaysberg M., Wallender E.K., Wong C., Yamamura Y.,
RA Yuan S., Shinozaki K., Davis R.W., Theologis A., 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
RT located on chromosome IV of Arabidopsis thaliana and adjacent to a
RT novel large gene of 15 exons.";
RL Biochim. Biophys. Acta 1398:225-231(1998).
RN [6]
RP SUBCELLULAR LOCATION.
RX PubMed=10824085;
RA Peeters N.M., Chapron A., Giritch A., Grandjean O., Lancelin D.,
RA Lhomme T., Vivrel A., Small I.;
RT "Duplication and quadruplication of Arabidopsis thaliana cysteinyl-
RT and 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
RT embryo development in Arabidopsis.";
RL Plant J. 44:866-878(2005).
CC -!- CATALYTIC ACTIVITY: ATP + L-asparagine + tRNA(Asn) = AMP +
CC diphosphate + L-asparaginyl-tRNA(Asn). {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
CC ovules. {ECO:0000269|PubMed:16297076}.
CC -!- SIMILARITY: Belongs to the class-II aminoacyl-tRNA synthetase
CC family. {ECO:0000305}.
CC -!- SIMILARITY: Contains 1 OB DNA-binding domain. {ECO:0000255}.
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};
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 UniGene; At.123; -.
DR UniGene; At.26556; -.
DR ProteinModelPortal; O48593; -.
DR STRING; 3702.AT4G17300.1; -.
DR PaxDb; O48593; -.
DR PRIDE; O48593; -.
DR EnsemblPlants; AT4G17300.1; AT4G17300.1; AT4G17300.
DR GeneID; 827443; -.
DR Gramene; AT4G17300.1; AT4G17300.1; AT4G17300.
DR KEGG; ath:AT4G17300; -.
DR TAIR; AT4G17300; -.
DR eggNOG; KOG0554; Eukaryota.
DR eggNOG; COG0017; LUCA.
DR HOGENOM; HOG000226033; -.
DR InParanoid; O48593; -.
DR KO; K01893; -.
DR OMA; ADIKGGP; -.
DR OrthoDB; EOG09360702; -.
DR PhylomeDB; O48593; -.
DR BioCyc; ARA:AT4G17300-MONOMER; -.
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; IDA: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 HAMAP; MF_00534; Asn_tRNA_synth; 1.
DR InterPro; IPR004364; aa-tRNA-synt_II.
DR InterPro; IPR018150; aa-tRNA-synt_II-like.
DR InterPro; IPR006195; aa-tRNA-synth_II.
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 PANTHER; PTHR22594; PTHR22594; 2.
DR PANTHER; PTHR22594:SF6; PTHR22594:SF6; 2.
DR Pfam; PF00152; tRNA-synt_2; 1.
DR Pfam; PF01336; tRNA_anti-codon; 1.
DR PRINTS; PR01042; TRNASYNTHASP.
DR SUPFAM; SSF50249; SSF50249; 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;
KW Complete proteome; DNA-binding; Ligase; Mitochondrion;
KW Nucleotide-binding; Plastid; Protein biosynthesis; Reference proteome;
KW Transit peptide.
FT TRANSIT 1 ? Chloroplast and mitochondrion.
FT {ECO:0000255}.
FT CHAIN ? 567 Asparagine--tRNA ligase,
FT chloroplastic/mitochondrial.
FT /FTId=PRO_0000035800.
FT DNA_BIND 113 191 OB. {ECO:0000255}.
FT CONFLICT 279 279 N -> Y (in Ref. 5; CAA10904).
FT {ECO:0000305}.
CC --------------------------------------------------------------------------
CC The following FT lines are automated annotations from the MyHits database.
CC --------------------------------------------------------------------------
FT MYHIT 208 561 ipfam:tRNA-synt_2 [T]
FT MYHIT 97 567 ihamap:Asn_tRNA_synth [T]
FT MYHIT 229 557 iprf:AA_TRNA_LIGASE_II [T]
FT MYHIT 113 191 ipfam:tRNA_anti-codon [T]
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
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