EBI Databases InterPro	Search Open in usermanual InterPro:
Jump to: InterProScan Databases Documentation FTP site Help Click on the icon for context sensitive help from the user manual. Advanced search

InterPro: IPR004971 mRNA capping enzyme, large subunit

Protein matches Help

UniProtKB

Matches:

262 proteins

Overview:	sorted by AC,	sorted by name,	of known structure,	proteins with splice variants
Detailed:	sorted by AC,	sorted by name,	of known structure	proteins with splice variants
Table:	For all matching proteins,	of known structure
Architectures
Accession List
Matches in BioMart

Accession

IPR004971 Pox_MCEL

Type

Family

Signatures Help

Database	ID	Name	Proteins
Pfam	PF03291	Pox_MCEL	262
Signatures in BioMart

InterPro Relationships Help

Children

IPR016899 mRNA (guanine-N(7))-methyltransferase

GO Term annotation Help

Process

GO:0006370 mRNA capping

InterPro annotation

Entry Details in BioMart

Abstract

This is a family of viral mRNA capping enzymes. The enzyme catalyses the first two reactions in the mRNA cap formation pathway. It is a heterodimer consisting of a large and small subunit. This entry is the large subunit.

Structural links Help

PDB - click here

SCOP: c.66.1.34

CATH: 3.40.50.150

Database links Help

Enzyme: EC:2

PANDIT: PF03291

Blocks: IPB004971

Pfam Clan: CL0102.19

AC	CL0102.19
ID	Methyltransfer
DE	Methyltransferase superfamily
PF00145	IPR001525	DNA methylase, C-5 cytosine-specific
PF00398	IPR001737	Ribosomal RNA adenine methylase transferase
PF00891	IPR001077	O-methyltransferase, family 2
PF01135	IPR000682	Protein-L-isoaspartate(D-aspartate) O-methyltransferase
PF01170	IPR000241	Putative RNA methylase
PF01189	IPR001678	Bacterial Fmu (Sun)/eukaryotic nucleolar NOL1/Nop2p
PF01209	IPR004033	UbiE/COQ5 methyltransferase
PF01234	IPR000940	Methyltransferase, NNMT/PNMT/TEMT
PF01269	IPR000692	Fibrillarin
PF01358	IPR000176	Poly A polymerase regulatory subunit
PF01555	IPR002941	DNA methylase N-4/N-6
PF01564	IPR001045	Spermine synthase
PF01596	IPR002935	O-methyltransferase, family 3
PF01728	IPR002877	Ribosomal RNA methyltransferase RrmJ/FtsJ
PF01739	IPR000780	MCP methyltransferase, CheR-type
PF01795	IPR002903	S-adenosyl-L-methionine-dependent methyltransferase, MraW
PF01861	IPR002723	Protein of unknown function DUF43
PF02005	IPR002905	N2,N2-dimethylguanosine tRNA methyltransferase
PF02086	IPR012327	D12 class N6 adenine-specific DNA methyltransferase
PF02353	IPR003333	Cyclopropane-fatty-acyl-phospholipid synthase
PF02384	IPR003356	DNA methylase, adenine-specific
PF02390	IPR003358	tRNA (guanine-N-7) methyltransferase
PF02475	IPR003402	Protein of unknown function Met10
PF02527	IPR003682	rRNA small subunit methyltransferase G
PF03141	IPR004159	Protein of unknown function DUF248, methyltransferase putative
PF03269	IPR004951	Protein of unknown function DUF268, Caenorhabditis species
PF03291	IPR004971	mRNA capping enzyme, large subunit
PF03602	IPR016065	Protein of unknown function methylase putative
PF03848	IPR015985	Tellurite resistance methyltransferase, TehB, core
PF04378	IPR007473	Protein of unknown function DUF519
PF04445	IPR007536	Protein of unknown function DUF548
PF04672	IPR006764	Protein of unknown function DUF574
PF04816	IPR006901	Protein of unknown function DUF633
PF05063	IPR007757	MT-A70
PF05148	IPR007823	Methyltransferase-related
PF05175	IPR007848	Methyltransferase small
PF05219	IPR007884	DREV methyltransferase
PF05401	IPR008715	NodS
PF05430	IPR008471	Protein of unknown function DUF752
PF05724	IPR008854	Thiopurine S-methyltransferase
PF05891	IPR008576	Protein of unknown function DUF858, methyltransferase-like
PF05958	IPR010280	(Uracil-5)-methyltransferase
PF05971	IPR010286	S-adenosyl-L-methionine dependent methyltransferase, predicted
PF06080	IPR010342	Protein of unknown function DUF938
PF06325	IPR010456	Ribosomal L11 methyltransferase
PF06460	IPR009461	Coronavirus NSP13
PF06859	IPR010675	Bicoid-interacting 3
PF06962	IPR010719	Putative rRNA methylase
PF07021	IPR010743	Methionine biosynthesis MetW
PF07109	IPR010940	Magnesium-protoporphyrin IX methyltransferase, C-terminal
PF07279	IPR009902	Protein of unknown function DUF1442
PF07669	IPR011639	Restriction endonuclease, Eco57I
PF07757	IPR011671	AdoMet-dependent methyltransferase, predicted
PF07942	IPR012901	N2227-like
PF08003	IPR010017	tRNA (mo5U34)-methyltransferase
PF08123	IPR013110	Histone methylation DOT1
PF08241	IPR013216	Methyltransferase type 11
PF08242	IPR013217	Methyltransferase type 12
PF08704	IPR014816	tRNA methyltransferase complex GCD14 subunit
PF09243	IPR015324	Ribosomal protein Rsm22, bacterial-type
PF09445	IPR019012	RNA cap guanine-N2 methyltransferase
PF10294	IPR019410	Methyltransferase-16, putative
PF10672	IPR019614	S-adenosylmethionine-dependent methyltransferase

Taxonomic coverage Help

Overlapping InterPro entries Help

IPR004971

Numbers of overlapping proteins

Average numbers of overlapping amino acids

Example proteins Help

O43148 mRNA cap guanine-N7 methyltransferase

P32783 mRNA cap guanine-N7 methyltransferase

Q9D0L8 mRNA cap guanine-N7 methyltransferase

Q9VJQ4 mRNA cap guanine-N7 methyltransferase

Q9XVS1 mRNA cap guanine-N7 methyltransferase

More proteins

Example Proteins Key

InterPro entry accession number/name and structure databases		Colour code
IPR004971	mRNA capping enzyme, large subunit
IPR016899	mRNA (guanine-N(7))-methyltransferase
	SWISS-MODEL
	PDB Chain
	ModBase
	CATH Domain

Publications Help

Additional Reading Open in usermanual
	Wang SP, Deng L, Ho CK, Shuman S. Phylogeny of mRNA capping enzymes. Proc. Natl. Acad. Sci. U.S.A. 94 1997 9573-8 [PubMed: 9275164] http://dx.doi.org/10.1073/pnas.94.18.9573
	Zheng S, Hausmann S, Liu Q, Ghosh A, Schwer B, Lima CD, Shuman S. Mutational analysis of Encephalitozoon cuniculi mRNA cap (guanine-N7) methyltransferase, structure of the enzyme bound to sinefungin, and evidence that cap methyltransferase is the target of sinefungin's antifungal activity. J. Biol. Chem. 281 2006 35904-13 [PubMed: 16971388] http://dx.doi.org/10.1074/jbc.M607292200
	Hausmann S, Zheng S, Fabrega C, Schneller SW, Lima CD, Shuman S. Encephalitozoon cuniculi mRNA cap (guanine N-7) methyltransferase: methyl acceptor specificity, inhibition BY S-adenosylmethionine analogs, and structure-guided mutational analysis. J. Biol. Chem. 280 2005 20404-12 [PubMed: 15760890] http://dx.doi.org/10.1074/jbc.M501073200
	Fabrega C, Hausmann S, Shen V, Shuman S, Lima CD. Structure and mechanism of mRNA cap (guanine-N7) methyltransferase. Mol. Cell 13 2004 77-89 [PubMed: 14731396] http://dx.doi.org/10.1016/S1097-2765(03)00522-7

InterPro 23.1