Reviewed, UniProtKB/Swiss-Prot P11409 (MTP2_PROVU)

Names and origin

Protein names

Recommended name:
    Modification methylase PvuII
      Short name=M.PvuII
    EC=2.1.1.113
Alternative name(s):
    N-4 cytosine-specific methyltransferase PvuII

Gene names

Name:

pvuIIM

Organism

Proteus vulgaris

Taxonomic identifier

585 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › Proteus

Protein attributes

Sequence length	336 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 CAGCTG, causes specific methylation on C-4 on both strands, and protects the DNA from cleavage by the PvuII endonuclease.
Catalytic activity	S-adenosyl-L-methionine + DNA cytosine = S-adenosyl-L-homocysteine + DNA N(4)-methylcytosine.
Sequence similarities	Belongs to the N(4)/N(6)-methyltransferase family. N(4) subfamily.

Ontologies

Keywords
Biological process	Restriction system
Domain	Repeat
Ligand	S-adenosyl-L-methionine
Molecular function	Methyltransferase Transferase
Technical term	3D-structure
Gene Ontology (GO)
Biological process	DNA methylation on cytosine Inferred from electronic annotation. Source: InterPro DNA restriction-modification system Inferred from electronic annotation. Source: UniProtKB-KW
Molecular function	DNA binding Inferred from electronic annotation. Source: InterPro N-methyltransferase activity Inferred from electronic annotation. Source: InterPro site-specific DNA-methyltransferase (cytosine-N4-specific) 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 – 336

336

Modification methylase PvuII

PRO_0000087931

Regions

Repeat

11 – 113

103

1

Repeat

181 – 293

113

2

Experimental info

Sequence conflict

44

1

D → E in CAA32026. Ref.1

Secondary structure

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336

Helix Strand Turn

Details...

Beta strand

22 – 24

3

Beta strand

26 – 33

8

Helix

35 – 38

4

Helix

39 – 41

3

Beta strand

47 – 52

6

Beta strand

57 – 59

3

Helix

68 – 86

19

Beta strand

87 – 97

11

Beta strand

105 – 108

4

Helix

111 – 121

11

Beta strand

126 – 134

9

Helix

144 – 148

5

Beta strand

157 – 168

12

Helix

173 – 175

3

Beta strand

221 – 224

4

Helix

232 – 240

9

Helix

253 – 262

10

Beta strand

268 – 271

4

Helix

278 – 285

8

Beta strand

289 – 295

7

Helix

297 – 304

8

Helix

305 – 307

3

Helix

314 – 325

12

Sequences

	Sequence		Length	Mass (Da)
	P11409-1 [UniParc]. Last modified October 1, 1996. Version 2. Checksum: 084371A667F86B91	FASTA	336	38,365
	10 20 30 40 50 60 MMTLNLQTMS SNDMLNFGKK PAYTTSNGSM YIGDSLELLE SFPDESISLV MTSPPFALQR 70 80 90 100 110 120 KKEYGNLEQH EYVDWFLSFA KVVNKKLKPD GSFVVDFGGA YMKGVPARSI YNFRVLIRMI 130 140 150 160 170 180 DEVGFFLAED FYWFNPSKLP SPIEWVNKRK IRVKDAVNTV WWFSKTEWPK SDITKVLAPY 190 200 210 220 230 240 SDRMKKLIED PDKFYTPKTR PSGHDIGKSF SKDNGGSIPP NLLQISNSES NGQYLANCKL 250 260 270 280 290 300 MGIKAHPARF PAKLPEFFIR MLTEPDDLVV DIFGGSNTTG LVAERESRKW ISFEMKPEYV 310 320 330 AASAFRFLDN NISEEKITDI YNRILNGESL DLNSII

References

[1]	"Sequence, internal homology and high-level expression of the gene for a DNA-(cytosine N4)-methyltransferase, M.Pvu II." Tao T., Walter J., Brennan K.J., Cotterman M.M., Blumenthal R.M. Nucleic Acids Res. 17:4161-4175(1989) [PubMed: 2662138] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: ATCC 13315 / DSM 30118 / IFO 3851 / NCIB 4175 / NCTC 4175.
[2]	"Gene pvuIIW: a possible modulator of PvuII endonuclease subunit association." Adams G.M., Blumenthal R.M. Gene 157:193-199(1995) [PubMed: 7607491] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-80, SEQUENCE REVISION TO 44.
[3]	"Structure of pvu II DNA-(cytosine N4) methyltransferase, an example of domain permutation and protein fold assignment." Gong W., O'Gara M., Blumenthal R.M., Cheng X. Nucleic Acids Res. 25:2702-2715(1997) [PubMed: 9207015] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS).

Cross-references

Sequence databases

EMBLGenBankDDBJ

X13778 Genomic DNA. Translation: CAA32026.1.
AF305615 Genomic DNA. Translation: AAA96336.1.

PIR

S04739.

RefSeq

NP_072082.1.

3D structure databases

PDBPDBe

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1BOO	X-ray	2.80	A	14-336	[»]

DisProt

DP00060.

ModBase

Search...

Genome annotation databases

GeneID

1238796.

Enzyme and pathway databases

BRENDA

2.1.1.113. 641.

Family and domain databases

InterPro

IPR002941. DNA_methylase_N4/N6.
IPR001091. MeTrfase_CN4.
IPR017985. MeTrfase_CN4_CS.
[Graphical view]

Pfam

PF01555. N6_N4_Mtase. 1 hit.
[Graphical view]

PRINTS

PR00508. S21N4MTFRASE.

PROSITE

PS00093. N4_MTASE. 1 hit.
[Graphical view]

ProtoNet

Search...

Entry information

Entry name

MTP2_PROVU

Accession

Primary (citable) accession number: P11409

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 1, 1989
Last sequence update:	October 1, 1996
Last modified:	July 7, 2009
This is version 83 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

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