Reviewed, UniProtKB/Swiss-Prot Q8SR66 (MCES_ENCCU)

Names and origin

Protein names

Recommended name:
    mRNA cap guanine-N7 methyltransferase
    EC=2.1.1.56
Alternative name(s):
    mRNA (guanine-N(7)-)-methyltransferase
    mRNA cap methyltransferase

Gene names

Name:	ABD1
Ordered Locus Names:	ECU10_0380

Organism

Encephalitozoon cuniculi [Complete proteome]

Taxonomic identifier

6035 [NCBI]

Taxonomic lineage

Eukaryota › Fungi › Microsporidia › Unikaryonidae › Encephalitozoon

Protein attributes

Sequence length	298 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Evidence at protein level.

General annotation (Comments)

Function	mRNA-capping methyltransferase that methylates the N7 position of the added guanosine to the 5'-cap structure of mRNAs. Binds RNA containing 5'-terminal GpppC. Ref.3
Catalytic activity	S-adenosyl-L-methionine + G(5')pppR-RNA = S-adenosyl-L-homocysteine + m7G(5')pppR-RNA.
Subunit structure	Monomer. Ref.3
Subcellular location	Nucleus By similarity.
Sequence similarities	Belongs to the mRNA cap methyltransferase family.
biophysicochemical properties	Kinetic parameters: KM=1 mM for GTP KM=25 µM for S-adenosyl-L-methionine KM=0.1 mM for cap dinucleotide GpppA

Ontologies

Keywords
Biological process	mRNA capping mRNA processing
Cellular component	Nucleus
Ligand	RNA-binding S-adenosyl-L-methionine
Molecular function	Methyltransferase Transferase
Technical term	3D-structure Complete proteome
Gene Ontology (GO)
Biological process	mRNA capping Inferred from electronic annotation. Source: UniProtKB-KW
Cellular component	nucleus Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular function	RNA binding Inferred from electronic annotation. Source: UniProtKB-KW mRNA (guanine-N7-)-methyltransferase activity Inferred from electronic annotation. Source: EC
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 298

298

mRNA cap guanine-N7 methyltransferase

PRO_0000210142

Regions

Region

50 – 51

2

mRNA cap binding

Region

122 – 123

2

S-adenosyl-L-methionine binding

Region

140 – 142

3

S-adenosyl-L-methionine binding

Sites

Binding site

54

1

S-adenosyl-L-methionine

Binding site

72

1

S-adenosyl-L-methionine; via carbonyl oxygen

Binding site

75

1

mRNA cap

Binding site

81

1

mRNA cap

Binding site

94

1

S-adenosyl-L-methionine

Binding site

106

1

mRNA cap

Binding site

144

1

mRNA cap

Binding site

225

1

mRNA cap

Binding site

284

1

mRNA cap

Experimental info

Mutagenesis

47

1

R → A: No effect. Loss of activity; when associated with A-75. Ref.2

Mutagenesis

50

1

N → A: No effect. Loss of activity; when associated with A-284. Ref.2

Mutagenesis

51

1

N → A: Reduces activity by 85%. Ref.2 Ref.4

Mutagenesis

51

1

N → D: Reduces activity by 96%. Ref.2 Ref.4

Mutagenesis

54

1

K → A, Q or R: Loss of activity. Ref.3 Ref.2 Ref.4

Mutagenesis

70

1

D → A or N: Reduces activity by 95%. Ref.3 Ref.4

Mutagenesis

70

1

D → E: Reduces activity by 60%. Ref.3 Ref.4

Mutagenesis

75

1

K → A: Reduces activity by 92%. Loss of activity; when associated with A-47. Ref.2 Ref.4

Mutagenesis

78

1

D → A or N: Reduces activity by 99%. Ref.3 Ref.2 Ref.4

Mutagenesis

78

1

D → E: Reduces activity by 75%. Ref.3 Ref.2 Ref.4

Mutagenesis

81

1

K → A: Reduces activity by 80%. Ref.2 Ref.4

Mutagenesis

81

1

K → Q or R: Reduces activity by 90%. Ref.2 Ref.4

Mutagenesis

94

1

D → A or N: Loss of activity. Ref.3 Ref.2 Ref.4

Mutagenesis

94

1

D → E: Reduces activity by 77%. Ref.3 Ref.2 Ref.4

Mutagenesis

95

1

I → A: No effect. Strongly reduced activity; when associated with A-124. Ref.2

Mutagenesis

106

1

R → A or Q: Reduces activity by over 98%. Ref.2 Ref.4

Mutagenesis

106

1

R → K: Reduces activity by 96%. Ref.2 Ref.4

Mutagenesis

122 – 123

2

DS → AA: Slightly reduced activity.

Mutagenesis

124

1

Y → A: Reduces activity by 83%. Strongly reduced activity; when associated with A-95. Ref.2 Ref.4

Mutagenesis

141

1

F → A or N: Loss of activity. Ref.2 Ref.4

Mutagenesis

141

1

F → H: Reduces activity by 92%. Ref.2 Ref.4

Mutagenesis

141

1

F → I: Reduces activity by 75%. Ref.2 Ref.4

Mutagenesis

141

1

F → L: Reduces activity by 55%. Ref.2 Ref.4

Mutagenesis

141

1

F → V: Reduces activity by 84%. Ref.2 Ref.4

Mutagenesis

144

1

H → A: Reduces activity by 53%. Reduces activity by 99%; when associated with L-145. Ref.4

Mutagenesis

145

1

Y → A, S or V: Reduces activity by 98%. Ref.4

Mutagenesis

145

1

Y → F: Reduces activity by 66%. Ref.4

Mutagenesis

216

1

L → A: No effect. Ref.2

Mutagenesis

225

1

E → A: Reduces activity by 87%. Ref.4

Mutagenesis

284

1

Y → A: Reduced activity. Loss of activity; when associated with A-50. Ref.2

Secondary structure

1

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298

Helix Strand Turn

Details...

Helix

44 – 61

18

Beta strand

67 – 71

5

Turn

74 – 78

5

Helix

79 – 85

7

Beta strand

88 – 95

8

Helix

97 – 108

12

Beta strand

114 – 121

8

Beta strand

123 – 126

4

Beta strand

134 – 141

8

Helix

143 – 146

4

Helix

150 – 161

12

Beta strand

164 – 175

12

Helix

177 – 186

10

Beta strand

192 – 197

6

Helix

206 – 208

3

Beta strand

211 – 216

6

Beta strand

221 – 226

6

Helix

230 – 239

10

Beta strand

242 – 249

8

Helix

250 – 260

11

Turn

265 – 269

5

Helix

275 – 281

7

Beta strand

284 – 291

8

Sequences

	Sequence		Length	Mass (Da)
	Q8SR66-1 [UniParc]. Last modified June 1, 2002. Version 1. Checksum: 03EF2775B7B6B062	FASTA	298	34,767
	10 20 30 40 50 60 MDSSSPLKTF RKDQAMEGKK EEIREHYNSI RERGRESRQR SKTINIRNAN NFIKACLIRL 70 80 90 100 110 120 YTKRGDSVLD LGCGKGGDLL KYERAGIGEY YGVDIAEVSI NDARVRARNM KRRFKVFFRA 130 140 150 160 170 180 QDSYGRHMDL GKEFDVISSQ FSFHYAFSTS ESLDIAQRNI ARHLRPGGYF IMTVPSRDVI 190 200 210 220 230 240 LERYKQGRMS NDFYKIELEK MEDVPMESVR EYRFTLLDSV NNCIEYFVDF TRMVDGFKRL 250 260 270 280 290 GLSLVERKGF IDFYEDEGRR NPELSKKMGL GCLTREESEV VGIYEVVVFR KLVPESDA

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Genome sequence and gene compaction of the eukaryote parasite Encephalitozoon cuniculi." Katinka M.D., Duprat S., Cornillot E., Metenier G., Thomarat F., Prensier G., Barbe V., Peyretaillade E., Brottier P., Wincker P., Delbac F., El Alaoui H., Peyret P., Saurin W., Gouy M., Weissenbach J., Vivares C.P. Nature 414:450-453(2001) [PubMed: 11719806] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: GB-M1.
[2]	"Structure and mechanism of mRNA cap (guanine-N7) methyltransferase." Fabrega C., Hausmann S., Shen V., Shuman S., Lima C.D. Mol. Cell 13:77-89(2004) [PubMed: 14731396] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) IN COMPLEXES WITH SUBSTRATES, MUTAGENESIS OF ARG-47; ASN-50; ASN-51; LYS-54; LYS-75; ASP-78; LYS-81; ASP-94; ILE-95; ARG-106; 122-ASP-SER-123; TYR-124; PHE-141; LEU-216 AND TYR-284.
[3]	"Encephalitozoon cuniculi mRNA cap (guanine N-7) methyltransferase: methyl acceptor specificity, inhibition by S-adenosylmethionine analogs, and structure-guided mutational analysis." Hausmann S., Zheng S., Fabrega C., Schneller S.W., Lima C.D., Shuman S. J. Biol. Chem. 280:20404-20412(2005) [PubMed: 15760890] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS) IN COMPLEX WITH SUBSTRATE ANALOG, FUNCTION, SUBUNIT, BIOPHYSICOCHEMICAL PROPERTIES, MUTAGENESIS OF LYS-54; ASP-70; ASP-78 AND ASP-94.
[4]	"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." Zheng S., Hausmann S., Liu Q., Ghosh A., Schwer B., Lima C.D., Shuman S. J. Biol. Chem. 281:35904-35913(2006) [PubMed: 16971388] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.6 ANGSTROMS) IN COMPLEX WITH SUBSTRATE ANALOG, MUTAGENESIS OF ASN-51; LYS-54; ASP-70; LYS-75; ASP-78; LYS-81; ASP-94; ARG-106; TYR-124; PHE-141; HIS-144; TYR-145 AND GLU-225.

Cross-references

Sequence databases

EMBLGenBankDDBJ

AL590449 Genomic DNA. Translation: CAD25757.1.

RefSeq

NP_586153.1.

3D structure databases

PDBPDBe

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1RI1	X-ray	2.50	A	1-298	[»]
1RI2	X-ray	2.70	A	1-298	[»]
1RI3	X-ray	2.50	A	1-298	[»]
1RI4	X-ray	2.40	A	1-298	[»]
1RI5	X-ray	2.10	A	1-298	[»]
1Z3C	X-ray	2.20	A	1-298	[»]
2HV9	X-ray	2.60	A	1-298	[»]

ModBase

Search...

Genome annotation databases

GeneID

859802.

GenomeReviews

Gene locus ECU10_0380 in contig AL590449_GR.

KEGG

ecu:ECU10_0380.

NMPDR

fig|6035.1.peg.1267.

Phylogenomic databases

HOGENOM

Q8SR66.

Enzyme and pathway databases

BRENDA

2.1.1.56. 276319.

Family and domain databases

InterPro

IPR004971. Pox_MCEL.
[Graphical view]

Pfam

PF03291. Pox_MCEL. 1 hit.
[Graphical view]

ProtoNet

Search...

Entry information

Entry name

MCES_ENCCU

Accession

Primary (citable) accession number: Q8SR66

Entry history

Integrated into UniProtKB/Swiss-Prot:	February 1, 2005
Last sequence update:	June 1, 2002
Last modified:	June 16, 2009
This is version 39 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

FPAP (Fungal Proteome Annotation Project)