K21016

RIKEN rice full-length cDNA overexpressed Arabidopsis lines

Original: K21016

Phenotypes

Morphological phenotypes

Generation Anatomical entity
/structure development stage
Phenotypes
T2 seed (PO:0009010)
  • increased size (PATO:0000586)
    (Seed::Shape::large)
  • increased length (PATO:0000573)
    (Seed::Shape::long)

Invisible phenotypes

Specific phenotypes were NOT observed.

Original: K21016

Determination of introduced cDNA(s)

  • J013072D16 - Rice Full-length cDNAs - Original: J013072D16

    full reading [+] show sequence

    Nucleotide sequence: J013072D16 - full reading
    GCTCCTCTTT CTTGGAGCAA AAGAAGAAAA AAAAATAAAT CCAATAACAC 
    CACAAGGAGC CCGAAGCGAG GAGAGAGAGA GAGATGGCGC TCGCAATCCT
    GGCGAGGAGG CGGGCGGCGG AGGCGCTGCT GCGGCGGCCG CTGGGGGCGG
    CGGGGGTGTC GGCGCTGAGG GCGTCGTACG CGGCGGTGGC GGGGGAGGAG
    AGCGACGTGG TGGTGGTGGG CGGCGGGCCG GGAGGGTACG TGGCGGCGAT
    CAAGGCGGCG CAGCTGGGGC TCAAGACCAC CTGCATCGAG AAGAGGGGCA
    CCCTCGGCGG GACATGCCTC AACGTCGGCT GCATCCCCTC CAAGGCTCTG
    TTGCACTCAT CTCATATGTA CCATGAAGCA AAAAGTTCCT TTGCACACCA
    TGGAGTGAAA TTTTCCAATC TGGAGGTAGA CCTCCCAGCT ATGATGGCAC
    AGAAAGACAA GGCTGTGGCA GGCCTGACTA AGGGGATTGA AGGTCTCTTC
    AAGAAGAACA AAGTGACGTA TGTCAAAGGC TTTGGGAAAC TTGCTTCGCC
    CTCAGAGGTG TCTGTTGATC TGAGCGATGG TGGCAGCACA GTTGTCAAAG
    GGAAAAACAT AATCATTGCT ACAGGGTCTG ATGTAAAATC ACTCCCTGGA
    GTCACAATTG ATGAGAAGAA AATCGTCTCA TCTACTGGGG CCTTGTGCTT
    GTCAGAGATT CCAAAGAAAT TGGTGGTTAT TGGAACAGGT TACATTGGTC
    TGGAGATGGG TTCGGTCTGG AACCGCCTTG GTTCAGAGGT CACCGTTGTT
    GAATTTGCCC CAGATATAGA TCCATCAATG GATGGTGAAG TCAGGAAGCA
    GTTCCAGCGC ATGTTGGAGA AGCAGAAGAT GAAGTTCATG CTCAAGACAA
    AGGTAGTTGG GGTTGATACC TCCGGAGATG GTGTGAAGCT AACACTTGAA
    CCTGCAGCTG GAGGTGAGCA GAGTGTCATT GAAGCTGATA TTGTATTGGT
    TTCTGCTGGA AGAGTCCCAT ATACTGCTGG TATTGGGTTG GAAAGTGTTG
    GTGTTGAGAC AGACAAAGCT GGCAGGATCC TCGTGGATAA GCGCTTCATG
    ACTAACGTCA ATGGAGTCTA TGCAATTGGG GATGCCATCC CTGGGCCCAT
    GCTTGCCCAC AAAGCTGAAG AGGATGGTGT TGCCTGTGTT GAGTTCATTG
    CTGGCAAGGA GGGGCACGTC GACTATGACA CAGTGCCTGG TGTGGTCTAT
    ACACATCCAG AGGTCGCGTC TGTTGGAAAG ACTGAAGAGC AGGTGAAAGC
    TTTAGGAATT CCCTACCGTG TTGGCAAATT TCCGCTGTTG GCAAACAGCC
    GTGCAAAGGC CATTGACGAT GCTGAGGGCT TGGTGAAGGT GGTGGCTGAG
    AAGGAAACTG ACAAGATTCT GGGCGTGCAT ATCATGGCTC CCGGTGCTGG
    AGAGATAATA CATGAGGCTG TCCTTGCTTT GCAGTATGGA GCATCAAGTG
    AGGACATAGC TCGTACATGC CACGCTCATC CCACCGTGAG CGAAGCCTTG
    AAGGAGGCCT GCCTGCAAAC CTTCACAAAG GCGATTCACA TTTAAGTTCT
    GTTTTGCTTT TAACATCCAA ACTGCTTGGC TTCACAAATT CCAAAATTTT
    GTAATAATTT TGGATATATG GGATCAAAAA GCCACTGTCT GTCATTTTAC
    TCTCGTTCGT GATGCTGTGA ATTGACACTA GTTGCCACAG CCAATAGTAT
    ATGCTATTGA TTCCATTCCC TTAGATGCC

    Gene models with high sequence identity

    1. AT1G48030.2 [+] show detail - mitochondrial lipoamide dehydrogenase 1
      E-value: 0; Score: 746.00

     

    InterPro Scan Digest

    Program Description E-value
    FPrintScan PNDRDTASEI 1.2e-81
    FPrintScan PNDRDTASEI 1.2e-81
    FPrintScan PNDRDTASEI 1.2e-81
    FPrintScan PNDRDTASEI 1.2e-81
    FPrintScan PNDRDTASEI 1.2e-81
    FPrintScan PNDRDTASEI 1.2e-81
    FPrintScan PNDRDTASEI 1.2e-81
    FPrintScan PNDRDTASEI 1.2e-81
    FPrintScan PNDRDTASEI 1.2e-81
    FPrintScan FAD-dependent pyridine nucleotide-disulphide oxidoreductase 3.3e-37
    FPrintScan FAD-dependent pyridine nucleotide-disulphide oxidoreductase 3.3e-37
    FPrintScan FAD-dependent pyridine nucleotide-disulphide oxidoreductase 3.3e-37
    FPrintScan FAD-dependent pyridine nucleotide-disulphide oxidoreductase 3.3e-37
    FPrintScan FAD-dependent pyridine nucleotide-disulphide oxidoreductase 3.3e-37
    FPrintScan Mercuric reductase 2.2e-13
    FPrintScan Mercuric reductase 2.2e-13
    FPrintScan Mercuric reductase 2.2e-13
    FPrintScan Mercuric reductase 2.2e-13
    FPrintScan Mercuric reductase 2.2e-13
    FPrintScan Mercuric reductase 2.2e-13
    HMMPfam FAD-dependent pyridine nucleotide-disulphide oxidoreductase 1.3e-49
    HMMPfam Pyridine nucleotide-disulphide oxidoreductase, dimerisation 2.2e-39
    HMMPfam Pyridine nucleotide-disulphide oxidoreductase, NAD-binding region 2.7e-20
    superfamily FAD/NAD(P)-binding domain 5.3e-73
    superfamily FAD/NAD-linked reductase, dimerisation 3.2e-43
    Gene3D no description 3.6e-66
    Gene3D Pyridine nucleotide-disulphide oxidoreductase, dimerisation 7.5e-43
    PatternScan Pyridine nucleotide-disulphide oxidoreductase, class I, active site 0
    HMMTigr Dihydrolipoamide dehydrogenase 7.2e-232
    HMMPanther Dihydrolipoamide dehydrogenase 9.2e-255
    HMMPanther DISULFIDE OXIDOREDUCTASE 9.2e-255

    See the detailed result >

    AT1G48030.2

    Model type
    Protein coding
    Short Description
    mitochondrial lipoamide dehydrogenase 1
    Curator Summary
    Encodes a mitochondrial lipoamide dehydrogenase whose expression is induced by light.
    Computational Description
    lipoamide dehydrogenase 1 (LPD1); FUNCTIONS IN: dihydrolipoyl dehydrogenase activity, copper ion binding, cobalt ion binding, zinc ion binding, ATP binding; INVOLVED IN: response to cadmium ion, response to light stimulus; LOCATED IN: mitochondrion, apoplast, mitochondrial respiratory chain complex I, mitochondrial matrix; EXPRESSED IN: 28 plant structures; EXPRESSED DURING: 16 growth stages; CONTAINS InterPro DOMAIN/s: FAD-dependent pyridine nucleotide-disulphide oxidoreductase (InterPro:IPR013027), Pyridine nucleotide-disulphide oxidoreductase, class I, active site (InterPro:IPR012999), Pyridine nucleotide-disulphide oxidoreductase, dimerisation (InterPro:IPR004099), Dihydrolipoamide dehydrogenase (InterPro:IPR006258), FAD/NAD-linked reductase, dimerisation (InterPro:IPR016156), Mercuric reductase (InterPro:IPR000815), Pyridine nucleotide-disulphide oxidoreductase, NAD-binding region (InterPro:IPR001327); BEST Arabidopsis thaliana protein match is: lipoamide dehydrogenase 2 (TAIR:AT3G17240.3); Has 41519 Blast hits to 41478 proteins in 3269 species: Archae - 1065; Bacteria - 30177; Metazoa - 918; Fungi - 552; Plants - 652; Viruses - 0; Other Eukaryotes - 8155 (source: NCBI BLink).
    Link
    InterPro Scan - TAIR