(data stored in SCRATCH zone)

SWISSPROT: SYRM_ARATH

ID   SYRM_ARATH              Reviewed;         642 AA.
AC   O23247;
DT   22-JUL-2015, integrated into UniProtKB/Swiss-Prot.
DT   01-JAN-1998, sequence version 1.
DT   11-DEC-2019, entry version 149.
DE   RecName: Full=Arginine--tRNA ligase, chloroplastic/mitochondrial {ECO:0000305};
DE            EC=6.1.1.19 {ECO:0000305};
DE   AltName: Full=Arginyl-tRNA synthetase {ECO:0000305};
DE            Short=ArgRS {ECO:0000305};
DE   AltName: Full=Protein EMBRYO DEFECTIVE 1027 {ECO:0000303|PubMed:16297076};
DE   Flags: Precursor;
GN   Name=EMB1027 {ECO:0000303|PubMed:16297076};
GN   OrderedLocusNames=At4g26300 {ECO:0000312|Araport:AT4G26300};
GN   ORFNames=T25K17.110 {ECO:0000312|EMBL:CAB38959.1};
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 [GENOMIC DNA].
RA   Small I.D., Lancelin D.;
RT   "Duplicated arginyl-tRNA synthetase genes in Arabidopsis thaliana.";
RL   Submitted (AUG-1997) to the EMBL/GenBank/DDBJ databases.
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   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   [5]
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   [6]
RP   ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-54, CLEAVAGE OF TRANSIT PEPTIDE
RP   [LARGE SCALE ANALYSIS] AFTER MET-53, AND IDENTIFICATION BY MASS
RP   SPECTROMETRY [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   -!- FUNCTION: Forms part of a macromolecular complex that catalyzes the
CC       attachment of specific amino acids to cognate tRNAs during protein
CC       synthesis. {ECO:0000250|UniProtKB:P54136}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + L-arginine + tRNA(Arg) = AMP + diphosphate + L-arginyl-
CC         tRNA(Arg); Xref=Rhea:RHEA:20301, Rhea:RHEA-COMP:9658, Rhea:RHEA-
CC         COMP:9673, ChEBI:CHEBI:30616, ChEBI:CHEBI:32682, ChEBI:CHEBI:33019,
CC         ChEBI:CHEBI:78442, ChEBI:CHEBI:78513, ChEBI:CHEBI:456215;
CC         EC=6.1.1.19; Evidence={ECO:0000305};
CC   -!- SUBCELLULAR LOCATION: Plastid, chloroplast
CC       {ECO:0000269|PubMed:16251277}. Mitochondrion
CC       {ECO:0000250|UniProtKB:Q8RXK8}.
CC   -!- DISRUPTION PHENOTYPE: Embryo defective. Developmental arrest of the
CC       embryo at the globular stage. {ECO:0000305|PubMed:16297076}.
CC   -!- SIMILARITY: Belongs to the class-I aminoacyl-tRNA synthetase family.
CC       {ECO:0000305}.
DR   EMBL; Z98760; CAB11468.1; -; Genomic_DNA.
DR   EMBL; AL049171; CAB38959.1; -; Genomic_DNA.
DR   EMBL; AL161565; CAB79485.1; -; Genomic_DNA.
DR   EMBL; CP002687; AEE85182.1; -; Genomic_DNA.
DR   PIR; T06014; T06014.
DR   RefSeq; NP_194360.1; NM_118763.3.
DR   SMR; O23247; -.
DR   STRING; 3702.AT4G26300.1; -.
DR   iPTMnet; O23247; -.
DR   PaxDb; O23247; -.
DR   PRIDE; O23247; -.
DR   EnsemblPlants; AT4G26300.1; AT4G26300.1; AT4G26300.
DR   GeneID; 828736; -.
DR   Gramene; AT4G26300.1; AT4G26300.1; AT4G26300.
DR   KEGG; ath:AT4G26300; -.
DR   Araport; AT4G26300; -.
DR   TAIR; locus:2136794; AT4G26300.
DR   eggNOG; KOG4426; Eukaryota.
DR   eggNOG; COG0018; LUCA.
DR   HOGENOM; HOG000247212; -.
DR   InParanoid; O23247; -.
DR   KO; K01887; -.
DR   OrthoDB; 463402at2759; -.
DR   PhylomeDB; O23247; -.
DR   PRO; PR:O23247; -.
DR   Proteomes; UP000006548; Chromosome 4.
DR   ExpressionAtlas; O23247; baseline and differential.
DR   Genevisible; O23247; AT.
DR   GO; GO:0009507; C:chloroplast; IDA:TAIR.
DR   GO; GO:0009570; C:chloroplast stroma; IDA:TAIR.
DR   GO; GO:0005829; C:cytosol; HDA:TAIR.
DR   GO; GO:0005739; C:mitochondrion; IDA:TAIR.
DR   GO; GO:0004814; F:arginine-tRNA ligase activity; IBA:GO_Central.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0006420; P:arginyl-tRNA aminoacylation; IBA:GO_Central.
DR   GO; GO:0009793; P:embryo development ending in seed dormancy; IMP:TAIR.
DR   CDD; cd00671; ArgRS_core; 1.
DR   Gene3D; 3.30.1360.70; -; 1.
DR   Gene3D; 3.40.50.620; -; 1.
DR   HAMAP; MF_00123; Arg_tRNA_synth; 1.
DR   InterPro; IPR001412; aa-tRNA-synth_I_CS.
DR   InterPro; IPR001278; Arg-tRNA-ligase.
DR   InterPro; IPR005148; Arg-tRNA-synth_N.
DR   InterPro; IPR036695; Arg-tRNA-synth_N_sf.
DR   InterPro; IPR035684; ArgRS_core.
DR   InterPro; IPR008909; DALR_anticod-bd.
DR   InterPro; IPR014729; Rossmann-like_a/b/a_fold.
DR   InterPro; IPR009080; tRNAsynth_Ia_anticodon-bd.
DR   PANTHER; PTHR11956; PTHR11956; 1.
DR   Pfam; PF03485; Arg_tRNA_synt_N; 1.
DR   Pfam; PF05746; DALR_1; 1.
DR   Pfam; PF00750; tRNA-synt_1d; 1.
DR   PRINTS; PR01038; TRNASYNTHARG.
DR   SMART; SM01016; Arg_tRNA_synt_N; 1.
DR   SMART; SM00836; DALR_1; 1.
DR   SUPFAM; SSF47323; SSF47323; 1.
DR   SUPFAM; SSF55190; SSF55190; 1.
DR   TIGRFAMs; TIGR00456; argS; 1.
DR   PROSITE; PS00178; AA_TRNA_LIGASE_I; 1.
PE   1: Evidence at protein level;
DR   PRODOM; O23247.
DR   SWISS-2DPAGE; O23247.
KW   Acetylation; Aminoacyl-tRNA synthetase; ATP-binding; Chloroplast; Ligase;
KW   Mitochondrion; Nucleotide-binding; Plastid; Protein biosynthesis;
KW   Reference proteome; Transit peptide.
FT   TRANSIT         1..53
FT                   /note="Chloroplast and mitochondrion"
FT                   /evidence="ECO:0000244|PubMed:22223895"
FT   CHAIN           54..642
FT                   /note="Arginine--tRNA ligase, chloroplastic/mitochondrial"
FT                   /evidence="ECO:0000305"
FT                   /id="PRO_0000433552"
FT   MOTIF           190..201
FT                   /note="'HIGH' region"
FT                   /evidence="ECO:0000305"
FT   MOD_RES         54
FT                   /note="N-acetylalanine"
FT                   /evidence="ECO:0000244|PubMed:22223895"
SQ   SEQUENCE   642 AA;  72387 MW;  0CE2674AE2BBEEFC CRC64;
     MFIFPKDENR RETLTTKLRF SADHLTFTTV TEKLRATAWR FAFSSRAKSV VAMAANEEFT
     GNLKRQLAKL FDVSLKLTVP DEPSVEPLVA ASALGKFGDY QCNNAMGLWS IIKGKGTQFK
     GPPAVGQALV KSLPTSEMVE SCSVAGPGFI NVVLSAKWMA KSIENMLIDG VDTWAPTLSV
     KRAVVDFSSP NIAKEMHVGH LRSTIIGDTL ARMLEYSHVE VLRRNHVGDW GTQFGMLIEY
     LFEKFPDTDS VTETAIGDLQ VFYKASKHKF DLDEAFKEKA QQAVVRLQGG DPVYRKAWAK
     ICDISRTEFA KVYQRLRVEL EEKGESFYNP HIAKVIEELN SKGLVEESEG ARVIFLEGFD
     IPLMVVKSDG GFNYASTDLT ALWYRLNEEK AEWIIYVTDV GQQQHFNMFF KAARKAGWLP
     DNDKTYPRVN HVGFGLVLGE DGKRFRTRAT DVVRLVDLLD EAKTRSKLAL IERGKDKEWT
     PEELDQTAEA VGYGAVKYAD LKNNRLTNYT FSFDQMLNDK GNTAVYLLYA HARICSIIRK
     SGKDIDELKK TGKLALDHAD ERALGLHLLR FAETVEEACT NLLPSVLCEY LYNLSEHFTR
     FYSNCQVNGS PEETSRLLLC EATAIVMRKC FHLLGITPVY KI
//

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