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LOC25493072 isoflavone 4'-O-methyltransferase-like [ Medicago truncatula (barrel medic) ]

Gene ID: 25493072, updated on 25-Apr-2024

Summary

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Gene symbol
LOC25493072
Gene description
isoflavone 4'-O-methyltransferase-like
Locus tag
MtrunA17_Chr4g0046341
Gene type
protein coding
RefSeq status
MODEL
Organism
Medicago truncatula
Lineage
Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta; Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae; rosids; fabids; Fabales; Fabaceae; Papilionoideae; 50 kb inversion clade; NPAAA clade; Hologalegina; IRL clade; Trifolieae; Medicago
Also known as
HI4'OMT; MtHI4'OMT
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Genomic context

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See LOC25493072 in Genome Data Viewer
Location:
chromosome: 4
Exon count:
4
Annotation release Status Assembly Chr Location
102 current MtrunA17r5.0-ANR (GCF_003473485.1) 4 NC_053045.1 (42735519..42745592)
101 previous assembly MedtrA17_4.0 (GCF_000219495.3) 4 NC_016410.2 (34775319..34785291)

Chromosome 4 - NC_053045.1Genomic Context describing neighboring genes Neighboring gene 2-hydroxyisoflavanone synthase Neighboring gene 2-hydroxyisoflavanone synthase Neighboring gene 2-hydroxyisoflavanone synthase Neighboring gene auxin response factor 3 Neighboring gene guanylate-binding protein 1

Genomic regions, transcripts, and products

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Go to nucleotide: Graphics FASTA GenBank

Bibliography

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Related articles in PubMed

  1. Expression dynamics of the Medicago truncatula transcriptome during the symbiotic interaction with Sinorhizobium meliloti: which role for nitric oxide? Boscari A, et al. Plant Physiol, 2013 Jan. PMID 23136381, Free PMC Article
  2. Dual RNA-Seq analysis of Medicago truncatula and the pea powdery mildew Erysiphe pisi uncovers distinct host transcriptional signatures during incompatible and compatible interactions and pathogen effector candidates. Gupta M, et al. Genomics, 2020 May. PMID 31837401

GeneRIFs: Gene References Into Functions

General gene information

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Homology

Gene Ontology Provided by RefSeq

Function Evidence Code Pubs
enables O-methyltransferase activity IEA
Inferred from Electronic Annotation
more info
 PubMed 
enables S-adenosylmethionine-dependent methyltransferase activity IEA
Inferred from Electronic Annotation
more info
 PubMed 
enables protein dimerization activity IEA
Inferred from Electronic Annotation
more info
 PubMed 
Process Evidence Code Pubs
involved_in methylation IEA
Inferred from Electronic Annotation
more info
 PubMed 

General protein information

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Preferred Names
isoflavone 4'-O-methyltransferase-like
Names
2,7,4'-trihydroxyisoflavanone 4'-O-methyltransferase
isoflavone-7-O-methyltransferase
putative methyltransferase

NCBI Reference Sequences (RefSeq)

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RefSeqs of Annotated Genomes: Medicago truncatula Annotation Release 102 details...Open this link in a new tab

The following sections contain reference sequences that belong to a specific genome build. Explain

Reference MtrunA17r5.0-ANR Primary Assembly

Genomic

  1. NC_053045.1 Reference MtrunA17r5.0-ANR Primary Assembly

    Range
    42735519..42745592
    Download
    GenBank, FASTA, Sequence Viewer (Graphics)

mRNA and Protein(s)

  1. XM_013601478.3 → XP_013456932.2  isoflavone 4'-O-methyltransferase-like isoform X3

    Conserved Domains (2) summary
    pfam08100
    Location:31 → 79
    Dimerisation; Dimerisation domain
    cl17173
    Location:132 → 347
    AdoMet_MTases; S-adenosylmethionine-dependent methyltransferases (SAM or AdoMet-MTase), class I; AdoMet-MTases are enzymes that use S-adenosyl-L-methionine (SAM or AdoMet) as a substrate for methyltransfer, creating the product S-adenosyl-L-homocysteine (AdoHcy). ...

  2. XM_039833091.1 → XP_039689025.1  isoflavone 4'-O-methyltransferase-like isoform X2

    UniProtKB/TrEMBL
    A0A072UPM0
    Conserved Domains (2) summary
    pfam08100
    Location:31 → 79
    dimerization; dimerization domain
    cl17173
    Location:132 → 343
    AdoMet_MTases; S-adenosylmethionine-dependent methyltransferases (SAM or AdoMet-MTase), class I; AdoMet-MTases are enzymes that use S-adenosyl-L-methionine (SAM or AdoMet) as a substrate for methyltransfer, creating the product S-adenosyl-L-homocysteine (AdoHcy). ...

  3. XM_013601476.3 → XP_013456930.1  isoflavone 4'-O-methyltransferase-like isoform X1

    UniProtKB/Swiss-Prot
    Q29U70
    UniProtKB/TrEMBL
    A0A072UNK8
    Conserved Domains (2) summary
    pfam08100
    Location:31 → 79
    Dimerisation; Dimerisation domain
    cl17173
    Location:135 → 350
    AdoMet_MTases; S-adenosylmethionine-dependent methyltransferases (SAM or AdoMet-MTase), class I; AdoMet-MTases are enzymes that use S-adenosyl-L-methionine (SAM or AdoMet) as a substrate for methyltransfer, creating the product S-adenosyl-L-homocysteine (AdoHcy). ...
Nucleotide Protein
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