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InterPro: IPR001525 DNA methylase, C-5 cytosine-specific

Protein matches Help

UniProtKB

Matches:

2545 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

IPR001525 C5_DNA_meth

Type

Domain

Signatures Help

Database	ID	Name	Proteins
Pfam	PF00145	DNA_methylase	2447
PRINTS	PR00105	C5METTRFRASE	1884
PANTHER	PTHR10629	C5_DNA_meth	2334
TIGRFAMs	TIGR00675	dcm	1566
Signatures in BioMart

InterPro Relationships Help

Found in

IPR017198 DNA (cytosine-5)-methyltransferase 1

Contains

IPR018117 DNA methylase, C-5 cytosine-specific, active site

GO Term annotation Help

Process

GO:0006306 DNA methylation

Function

GO:0003677 DNA binding

InterPro annotation

Entry Details in BioMart

Abstract

C-5 cytosine-specific DNA methylases (EC:2.1.1.37) (C5 Mtase) are enzymes that specifically methylate the C-5 carbon of cytosines in DNA to produce C5-methylcytosine [1, 2, 3]. In mammalian cells, cytosine-specific methyltransferases methylate certain CpG sequences, which are believed to modulate gene expression and cell differentiation. In bacteria, these enzymes are a component of restriction-modification systems and serve as valuable tools for the manipulation of DNA [4, 2]. The structure of HhaI methyltransferase (M.HhaI) has been resolved to 2.5 A [5]: the molecule folds into 2 domains - a larger catalytic domain containing catalytic and cofactor binding sites, and a smaller DNA recognition domain.

Structural links Help

PDB - click here

SCOP: c.66.1.26

CATH: 3.40.50.150 , 3.90.120.10

Database links Help

PDBe-motif: PS00094 , PS00095

Enzyme: EC:2.1.1.37

PROSITE doc: PDOC00089

PANDIT: PF00145

Blocks: IPB001525

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

IPR001525

Numbers of overlapping proteins

Average numbers of overlapping amino acids

Example proteins Help

B1Q3J6 DNA (cytosine-5)-methyltransferase 1B

O14717 tRNA (cytosine-5-)-methyltransferase

O49139 Putative DNA (cytosine-5)-methyltransferase CMT1

O88509 DNA (cytosine-5)-methyltransferase 3B

P45968 Chromo domain-containing protein T09A5.8

More proteins

Example Proteins Key

InterPro entry accession number/name and structure databases		Colour code
IPR000953	Chromo domain
IPR017984	Chromo domain subgroup
IPR000313	PWWP
IPR001525	DNA methylase, C-5 cytosine-specific
IPR017198	DNA (cytosine-5)-methyltransferase 1
IPR011011	Zinc finger, FYVE/PHD-type
IPR016197	Chromo domain-like
IPR001025	Bromo adjacent homology (BAH) domain
IPR018117	DNA methylase, C-5 cytosine-specific, active site
	PDB Chain
	ModBase
	CATH Domain
	SWISS-MODEL
	SCOP Domain

Publications Open in usermanual
1.	Posfai J, Bhagwat AS, Roberts RJ. Sequence motifs specific for cytosine methyltransferases. Gene 74 261-5 1988 [PubMed: 3248729] http://dx.doi.org/10.1016/0378-1119(88)90299-5
2.	Kumar S, Cheng X, Klimasauskas S, Mi S, Posfai J, Roberts RJ, Wilson GG. The DNA (cytosine-5) methyltransferases. Nucleic Acids Res. 22 1-10 1994 [PubMed: 8127644] http://dx.doi.org/10.1093/nar/22.1.1
3.	Lauster R, Trautner TA, Noyer-Weidner M. Cytosine-specific type II DNA methyltransferases. A conserved enzyme core with variable target-recognizing domains. J. Mol. Biol. 206 305-12 1989 [PubMed: 2716049] http://dx.doi.org/10.1016/0022-2836(89)90480-4
4.	Cheng X. DNA modification by methyltransferases. Curr. Opin. Struct. Biol. 5 4-10 1995 [PubMed: 7773746] http://dx.doi.org/10.1016/0959-440X(95)80003-J
5.	Cheng X, Kumar S, Posfai J, Pflugrath JW, Roberts RJ. Crystal structure of the HhaI DNA methyltransferase complexed with S-adenosyl-L-methionine. Cell 74 299-307 1993 [PubMed: 8343957] http://dx.doi.org/10.1016/0092-8674(93)90421-L

Additional Reading Open in usermanual
	Youngblood B, Shieh FK, De Los Rios S, Perona JJ, Reich NO. Engineered extrahelical base destabilization enhances sequence discrimination of DNA methyltransferase M.HhaI. J. Mol. Biol. 362 2006 334-46 [PubMed: 16919299] http://dx.doi.org/10.1016/j.jmb.2006.07.031
	Neely RK, Daujotyte D, Grazulis S, Magennis SW, Dryden DT, Klimasauskas S, Jones AC. Time-resolved fluorescence of 2-aminopurine as a probe of base flipping in M.HhaI-DNA complexes. Nucleic Acids Res. 33 2005 6953-60 [PubMed: 16340006] http://dx.doi.org/10.1093/nar/gki995
	Shieh FK, Reich NO. AdoMet-dependent methyl-transfer: Glu119 is essential for DNA C5-cytosine methyltransferase M.HhaI. J. Mol. Biol. 373 2007 1157-68 [PubMed: 17897676] http://dx.doi.org/10.1016/j.jmb.2007.08.009
	Verdine GL. The flip side of DNA methylation. Cell 76 1994 197-200 [PubMed: 8293456] http://dx.doi.org/10.1016/0092-8674(94)90326-3
	Youngblood B, Shieh FK, Buller F, Bullock T, Reich NO. S-adenosyl-L-methionine-dependent methyl transfer: observable precatalytic intermediates during DNA cytosine methylation. Biochemistry 46 2007 8766-75 [PubMed: 17616174] http://dx.doi.org/10.1021/bi7005948
	Shieh FK, Youngblood B, Reich NO. The role of Arg165 towards base flipping, base stabilization and catalysis in M.HhaI. J. Mol. Biol. 362 2006 516-27 [PubMed: 16926025] http://dx.doi.org/10.1016/j.jmb.2006.07.030
	Klimasauskas S, Kumar S, Roberts RJ, Cheng X. HhaI methyltransferase flips its target base out of the DNA helix. Cell 76 1994 357-69 [PubMed: 8293469] http://dx.doi.org/10.1016/0092-8674(94)90342-5
	Som S, Bhagwat AS, Friedman S. Nucleotide sequence and expression of the gene encoding the EcoRII modification enzyme. Nucleic Acids Res. 15 1987 313-32 [PubMed: 3029675] http://dx.doi.org/10.1093/nar/15.1.313

InterPro 23.1