tag-72 mRNA cap guanine-N7 methyltransferase [Caenorhabditis elegans] - Gene

Summary

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Gene symbol: tag-72
Gene description: mRNA cap guanine-N7 methyltransferase
Primary source: WormBase:WBGene00006447
Locus tag: CELE_C25A1.3
See related: AllianceGenome:WB:WBGene00006447
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 RNA binding activity and mRNA (guanine-N7-)-methyltransferase activity. Predicted to be involved in 7-methylguanosine mRNA capping. Predicted to be part of mRNA cap binding activity complex. Predicted to be active in nucleus. Orthologous to human RNMT (RNA guanine-7 methyltransferase). [provided by Alliance of Genome Resources, Apr 2022]
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Genomic context

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Location:: chromosome: I

Exon count:: 6

Sequence:: Chromosome: I; NC_003279.8 (10159982..10161883, 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

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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

C25A1.3 (e-PCR)
- UniSTS:305577

C25A1.1 (e-PCR)
- UniSTS:315593

Homology

Orthologs from OrthoDB

Gene Ontology Provided by WormBase

Function	Evidence Code	Pubs
enables RNA binding	IEA Inferred from Electronic Annotation more info
enables RNA binding	ISS Inferred from Sequence or Structural Similarity more info
enables mRNA 5'-cap (guanine-N7-)-methyltransferase activity	IBA Inferred from Biological aspect of Ancestor more info
enables mRNA 5'-cap (guanine-N7-)-methyltransferase activity	IEA Inferred from Electronic Annotation more info
enables mRNA 5'-cap (guanine-N7-)-methyltransferase activity	ISS Inferred from Sequence or Structural Similarity more info
enables methyltransferase activity	IEA Inferred from Electronic Annotation more info
enables transferase activity	IEA Inferred from Electronic Annotation more info

Process	Evidence Code	Pubs
involved_in 7-methylguanosine mRNA capping	IBA Inferred from Biological aspect of Ancestor more info
involved_in 7-methylguanosine mRNA capping	IEA Inferred from Electronic Annotation more info
involved_in 7-methylguanosine mRNA capping	ISS Inferred from Sequence or Structural Similarity more info
involved_in RNA 5'-cap (guanine-N7)-methylation	IEA Inferred from Electronic Annotation more info
involved_in mRNA processing	IEA Inferred from Electronic Annotation more info
involved_in methylation	IEA Inferred from Electronic Annotation more info

Component	Evidence Code	Pubs
is_active_in nucleus	IBA Inferred from Biological aspect of Ancestor more info
located_in nucleus	IEA Inferred from Electronic Annotation more info
located_in nucleus	ISS Inferred from Sequence or Structural Similarity more info

General protein information

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Preferred Names: mRNA cap guanine-N7 methyltransferase

NP_492674.2

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

10159982..10161883 complement

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GenBank, FASTA, Sequence Viewer (Graphics)

mRNA and Protein(s)

NM_060273.10 → NP_492674.2 mRNA cap guanine-N7 methyltransferase [Caenorhabditis elegans]

See identical proteins and their annotated locations for NP_492674.2

Status: REVIEWED

UniProtKB/Swiss-Prot

Q9XVS1

Conserved Domains (1) summary

cl17173
Location:3 → 332

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). ...