Reviewed, UniProtKB/Swiss-Prot P20589 (MTH3_HAEAE)

Names and origin

Protein names

Recommended name:
    Modification methylase HaeIII
      Short name=M.HaeIII
    EC=2.1.1.37
Alternative name(s):
    Cytosine-specific methyltransferase HaeIII

Gene names

Name:

haeIIIM

Organism

Haemophilus aegyptius

Taxonomic identifier

197575 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Gammaproteobacteria › Pasteurellales › Pasteurellaceae › Haemophilus

Protein attributes

Sequence length	330 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Evidence at protein level.

General annotation (Comments)

Function	This methylase recognizes the double-stranded sequence GGCC, causes specific methylation on C-3 on both strands, and protects the DNA from cleavage by the HaeIII endonuclease.
Catalytic activity	S-adenosyl-L-methionine + DNA = S-adenosyl-L-homocysteine + DNA containing 5-methylcytosine.
Sequence similarities	Belongs to the C5-methyltransferase family.

Ontologies

Keywords
Biological process	Restriction system
Ligand	S-adenosyl-L-methionine
Molecular function	Methyltransferase Transferase
Technical term	3D-structure Direct protein sequencing
Gene Ontology (GO)
Biological process	DNA methylation Inferred from electronic annotation. Source: InterPro DNA restriction-modification system Inferred from electronic annotation. Source: UniProtKB-KW
Molecular function	DNA (cytosine-5-)-methyltransferase activity Inferred from electronic annotation. Source: EC DNA binding Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 330

330

Modification methylase HaeIII

PRO_0000087878

Sites

Active site

71

1

Ref.3

Secondary structure

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330

Helix Strand Turn

Details...

Beta strand

2 – 7

6

Helix

12 – 20

9

Beta strand

23 – 29

7

Turn

32 – 34

3

Helix

35 – 41

7

Beta strand

44 – 49

6

Turn

51 – 53

3

Helix

56 – 58

3

Beta strand

63 – 67

5

Turn

72 – 74

3

Beta strand

75 – 78

4

Beta strand

83 – 85

3

Helix

86 – 101

16

Beta strand

104 – 111

8

Helix

112 – 115

4

Helix

117 – 119

3

Helix

120 – 134

15

Beta strand

135 – 143

9

Helix

144 – 147

4

Beta strand

154 – 162

9

Helix

163 – 165

3

Helix

181 – 183

3

Helix

186 – 188

3

Turn

197 – 199

3

Helix

203 – 205

3

Beta strand

206 – 208

3

Helix

220 – 223

4

Helix

242 – 244

3

Beta strand

255 – 258

4

Beta strand

261 – 263

3

Turn

266 – 268

3

Helix

269 – 271

3

Helix

277 – 284

8

Helix

297 – 305

9

Helix

310 – 322

13

Sequences

	Sequence		Length	Mass (Da)
	P20589-1 [UniParc]. Last modified February 1, 1991. Version 1. Checksum: 928C6D5390DBED25	FASTA	330	37,686
	10 20 30 40 50 60 MNLISLFSGA GGLDLGFQKA GFRIICANEY DKSIWKTYES NHSAKLIKGD ISKISSDEFP 70 80 90 100 110 120 KCDGIIGGPP CQSWSEGGSL RGIDDPRGKL FYEYIRILKQ KKPIFFLAEN VKGMMAQRHN 130 140 150 160 170 180 KAVQEFIQEF DNAGYDVHII LLNANDYGVA QDRKRVFYIG FRKELNINYL PPIPHLIKPT 190 200 210 220 230 240 FKDVIWDLKD NPIPALDKNK TNGNKCIYPN HEYFIGSYST IFMSRNRVRQ WNEPAFTVQA 250 260 270 280 290 300 SGRQCQLHPQ APVMLKVSKN LNKFVEGKEH LYRRLTVREC ARVQGFPDDF IFHYESLNDG 310 320 330 YKMIGNAVPV NLAYEIAKTI KSALEICKGN

References

[1]	"Cloning and analysis of the HaeIII and HaeII methyltransferase genes." Slatko B.E., Croft R., Moran L.S., Wilson G.G. Gene 74:45-50(1988) [PubMed: 3248732] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: ATCC 11116 / CCUG 25716 / NCTC 8502.
[2]	Zhang B.-H., Wilson G.G. Submitted (FEB-1998) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: ATCC 11116 / CCUG 25716 / NCTC 8502.
[3]	"Direct identification of the active-site nucleophile in a DNA (cytosine-5)-methyltransferase." Chen L., McMillan A.M., Chang W., Ezak-Nipkay K., Lane W.S., Verdine G.L. Biochemistry 30:11018-11025(1991) [PubMed: 1932026] [Abstract] Cited for: ACTIVE SITE, PROTEIN SEQUENCE OF 62-81.
[4]	"The crystal structure of HaeIII methyltransferase covalently complexed to DNA: an extrahelical cytosine and rearranged base pairing." Reinisch K.M., Chen L., Verdine G.L., Lipscomb W.N. Cell 82:143-153(1995) [PubMed: 7606780] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS).

Cross-references

Sequence databases

EMBLGenBankDDBJ

M24625 Genomic DNA. Translation: AAA24970.1.
AF051375 Genomic DNA. Translation: AAC05696.1.

PIR

JS0102.

3D structure databases

PDBPDBe

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1DCT	X-ray	2.80	A/B	1-324	[»]

ModBase

Search...

Protein family/group databases

REBASE

3410. M.HaeIII.

Family and domain databases

InterPro

IPR001525. C5_DNA_meth.
IPR018117. C5_DNA_meth_AS.
[Graphical view]

PANTHER

PTHR10629. C5_DNA_meth. 1 hit.

Pfam

PF00145. DNA_methylase. 1 hit.
[Graphical view]

PRINTS

PR00105. C5METTRFRASE.

TIGRFAMs

TIGR00675. dcm. 1 hit.

PROSITE

PS00094. C5_MTASE_1. 1 hit.
PS00095. C5_MTASE_2. 1 hit.
[Graphical view]

ProtoNet

Search...

Entry information

Entry name

MTH3_HAEAE

Accession

Primary (citable) accession number: P20589

Entry history

Integrated into UniProtKB/Swiss-Prot:	February 1, 1991
Last sequence update:	February 1, 1991
Last modified:	June 16, 2009
This is version 71 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HAMAP (High-quality Automated and Manual Annotation of microbial Proteomes)