Homology analysis

Gene ID At1g66530
Gene name arginyl-tRNA synthetase, putative / arginine--tRNA ligase, putative
Functional description F:aminoacyl-tRNA ligase activity, nucleotide binding, arginine-tRNA ligase activity, ATP binding;P:arginyl-tRNA aminoacylation, translation, tRNA aminoacylation for protein translation;C:cytoplasm;OBMAFPV

Click gene/probe ID to show a list of genes that are homologous to the gene.

Paralogous genes

HFEvBSGene IDRepr. IDGene NameFunctional DescriptionO.I.C.G.S.X.Other DB
0.8502030At4g26300828736emb1027 (embryo defective 1027)F:nucleotide binding, aminoacyl-tRNA ligase activity, arginine-tRNA ligase activity, ATP binding;P:embryonic development ending in seed dormancy, arginyl-tRNA aminoacylation;C:mitochondrion, chloroplast;OBMAFPVO.I.C.G.S.X.
0.019e-136At4g10930826692unknown proteinF:unknown;P:unknown;C:cellular_component unknown;MOFBPO.I.C.G.S.X.
0.019e-136At3g22450821816structural constituent of ribosomeF:structural constituent of ribosome;P:translation;C:mitochondrion, ribosome, intracellular;PBOMO.I.C.G.S.X.
0.014e+034At5g528825008305ATP binding / nucleoside-triphosphatase/ nucleotide bindingF:nucleoside-triphosphatase activity, nucleotide binding, ATP binding;P:biological_process unknown;C:endomembrane system;BOMFPAVO.I.C.G.S.X.
0.014e+034At5g55740835668CRR21 (chlororespiratory reduction 21)Encodes a member of the E+ subgroup of the PPR protein family, containing the E and E+ motifs following a tandem array of PPR motifs. It also contains an unknown motif consisting of 15 aa, which is highly conserved in some PPR proteins, including CRR4. CRR21 is involved in RNA editing of the site 2 of ndhD (ndhD-2),which encodes a subunit of the NDH complex. The RNA editing changes aa 128 from Ser to Leu. Mutants have impaired NDH complex activity.O.I.C.G.S.X.
0.014e+034At5g23570832422SGS3 (SUPPRESSOR OF GENE SILENCING 3)Required for posttranscriptional gene silencing and natural virus resistance.SGS3 is a member of an 'unknown' protein family. Members of this family have predicted coiled coiled domains suggesting oligomerization and a potential zinc finger domain. Involved in the production of trans-acting siRNAs, through direct or indirect stabilization of cleavage fragments of the primary ta-siRNA transcript. Acts before RDR6 in this pathway.O.I.C.G.S.X.
0.014e+034At5g58380835951SIP1 (SOS3-INTERACTING PROTEIN 1)Encodes a CBL-interacting protein kinase with similarity to SOS protein kinase.O.I.C.G.S.X.
0.014e+034At4g14570827104acylaminoacyl-peptidase-relatedF:serine-type peptidase activity;P:proteolysis;C:chloroplast, vacuole;BOMFPAO.I.C.G.S.X.
0.014e+034At4g35970829751APX5 (ASCORBATE PEROXIDASE 5)Encodes a microsomal ascorbate peroxidase APX5. Ascorbate peroxidases are enzymes that scavenge hydrogen peroxide in plant cells. Eight types of APX have been described for Arabidopsis: three cytosolic (APX1, APX2, APX6), two chloroplastic types (stromal sAPX, thylakoid tAPX), and three microsomal (APX3, APX4, APX5) isoforms.O.I.C.G.S.X.

Orthologous genes

HFEvBSGene IDOrganismRepr. IDGene NameFunctional DescriptionEvAGI codeArabidopsis gene nameO.I.C.G.S.X.Other DB
0.162e-861Gma.10893.1.S1_atGlycine maxBE659457arginyl-tRNA synthetase-7e-20At4g26300emb1027 (embryo defective 1027)O.I.C.G.S.X.
0.181e-22107Contig9377_atHordeum vulgareContig9377--4e-27At4g26300emb1027 (embryo defective 1027)O.I.C.G.S.X.
0.209e-1893Os05g0163000Oryza sativaAK066161.1-Arginyl-tRNA synthetase, class Ic family protein2e-20At4g26300emb1027 (embryo defective 1027)O.I.C.G.S.X.
0.316e-1893Ptp.1743.1.A1_a_atPopulus trichocarpaCV271562hypothetical protein-3e-45At4g26300emb1027 (embryo defective 1027)O.I.C.G.S.X.
0.211e-1895Ta.2176.1.S1_atTriticum aestivumCK206562--1e-25At4g26300emb1027 (embryo defective 1027)O.I.C.G.S.X.
0.023e-1361611954_atVitis viniferaCF516533hypothetical protein LOC100250957-1e+0At4g08260protein phosphatase 2C, putative / PP2C, putativeO.I.C.G.S.X.
0.092e-654Zm.7543.1.A1_atZea maysCD997722hypothetical protein LOC100192002-4e-6At1g66530arginyl-tRNA synthetase, putative / arginine--tRNA ligase, putativeO.I.C.G.S.X.

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