prmt-7 Protein arginine N-methyltransferase 7 [Caenorhabditis elegans] - Gene

Summary

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Official Symbol: prmt-7
Official Full Name: Protein arginine N-methyltransferase 7
Primary source: WormBase:WBGene00012298
Locus tag: CELE_W06D4.4
See related: AllianceGenome:WB:WBGene00012298
Gene type: protein coding
RefSeq status: REVIEWED
Organism: Caenorhabditis elegans (strain: Bristol N2)
Lineage: Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida; Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae; Caenorhabditis
Summary: Predicted to enable histone methyltransferase activity and protein-arginine N-methyltransferase activity. Predicted to be involved in chromatin remodeling and regulation of DNA-templated transcription. Orthologous to human PRMT7 (protein arginine methyltransferase 7). [provided by Alliance of Genome Resources, Dec 2024]
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Genomic context

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See prmt-7 in Genome Data Viewer

Location:: chromosome: I

Exon count:: 9

Sequence:: Chromosome: I; NC_003279.8 (9060493..9063160, complement)

Chromosome I - NC_003279.8 Genomic Context describing neighboring genes

Genomic regions, transcripts, and products

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Go to reference sequence details

Genomic Sequence:: NC_003279.8

Go to nucleotide: Graphics FASTA GenBank

Bibliography

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GeneRIFs: Gene References Into Functions

What's a GeneRIF?

C. elegans PRMT-7 has a substrate specificity and a substrate preference different from those of mammalian PRMT7, and the available X-ray crystal structures of the PRMT7 orthologs show differences in active site architecture
Title: Caenorhabditis elegans PRMT-7 and PRMT-9 Are Evolutionarily Conserved Protein Arginine Methyltransferases with Distinct Substrate Specificities.
Data indicate that only the N-terminal catalytic site of protein arginine methyltransferase 7 (PRMT7) is responsible for cofactor binding.
Title: Protein arginine methyltransferase 7 has a novel homodimer-like structure formed by tandem repeats.

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Pathways from PubChem

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Interactions

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Products	Interactant	Other Gene	Complex	Source	Pubs	Description

General gene information

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Markers

W06D4.5 (e-PCR)
- UniSTS:317538

W06D4.4 (e-PCR)
- UniSTS:311149

Homology

Orthologs from OrthoDB

Gene Ontology Provided by WormBase

Function	Evidence Code	Pubs
enables histone methyltransferase activity	IBA Inferred from Biological aspect of Ancestor more info
enables methyltransferase activity	IEA Inferred from Electronic Annotation more info
enables protein-arginine N-methyltransferase activity	IBA Inferred from Biological aspect of Ancestor more info
enables protein-arginine N-methyltransferase activity	IEA Inferred from Electronic Annotation more info

Process	Evidence Code	Pubs
involved_in chromatin remodeling	IBA Inferred from Biological aspect of Ancestor more info
involved_in methylation	IEA Inferred from Electronic Annotation more info
involved_in peptidyl-arginine methylation	IEA Inferred from Electronic Annotation more info
involved_in protein methylation	IEA Inferred from Electronic Annotation more info
involved_in regulation of DNA-templated transcription	IBA Inferred from Biological aspect of Ancestor more info

General protein information

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Preferred Names: Protein arginine N-methyltransferase 7

NP_492436.2

Confirmed by transcript evidence

NCBI Reference Sequences (RefSeq)

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Genome Annotation

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

Reference assembly

Genomic

NC_003279.8 Reference assembly

Range

9060493..9063160 complement

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GenBank, FASTA, Sequence Viewer (Graphics)

mRNA and Protein(s)

NM_060035.4 → NP_492436.2 Protein arginine N-methyltransferase 7 [Caenorhabditis elegans]

See identical proteins and their annotated locations for NP_492436.2

Status: REVIEWED

UniProtKB/Swiss-Prot

Q9XW42

Conserved Domains (2) summary

COG0500
Location:19 → 258

SmtA; SAM-dependent methyltransferase [Secondary metabolites biosynthesis, transport and catabolism, General function prediction only]

cl17173
Location:34 → 238

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). ...