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P11409 (MTP2_PROHU) Reviewed, UniProtKB/Swiss-Prot

Last modified June 11, 2014. Version 96. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended 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
OrganismProteus hauseri
Taxonomic identifier183417 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeProteus

Protein attributes

Sequence length336 AA.
Sequence statusComplete.
Protein existenceEvidence 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.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 336336Modification methylase PvuII
PRO_0000087931

Regions

Repeat11 – 1131031
Repeat181 – 2931132

Experimental info

Sequence conflict441D → E in CAA32026. Ref.1

Secondary structure

............................................ 336
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P11409 [UniParc].

Last modified October 1, 1996. Version 2.
Checksum: 084371A667F86B91

FASTA33638,365
        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 

« Hide

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] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: ATCC 13315 / DSM 30118 / JCM 1668 / NBRC 3851 / NCIMB 4175 / NCTC 4175 / NRRL B-3405.
[2]"Gene pvuIIW: a possible modulator of PvuII endonuclease subunit association."
Adams G.M., Blumenthal R.M.
Gene 157:193-199(1995) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-80, SEQUENCE REVISION TO 44.
Strain: ATCC 13315 / DSM 30118 / JCM 1668 / NBRC 3851 / NCIMB 4175 / NCTC 4175 / NRRL B-3405.
[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] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS).

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
X13778 Genomic DNA. Translation: CAA32026.1.
AF305615 Genomic DNA. Translation: AAA96336.1.
PIRS04739.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1BOOX-ray2.80A14-336[»]
DisProtDP00060.
ProteinModelPortalP11409.
SMRP11409. Positions 16-335.
ModBaseSearch...
MobiDBSearch...

Protein family/group databases

REBASE3485. M.PvuII.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Enzyme and pathway databases

BRENDA2.1.1.113. 5049.

Family and domain databases

Gene3D3.40.50.150. 2 hits.
InterProIPR002941. DNA_methylase_N4/N6.
IPR017985. MeTrfase_CN4_CS.
IPR001091. RM_Methylase.
IPR029063. SAM-dependent_MTases-like.
[Graphical view]
PfamPF01555. N6_N4_Mtase. 1 hit.
[Graphical view]
PRINTSPR00508. S21N4MTFRASE.
SUPFAMSSF53335. SSF53335. 1 hit.
PROSITEPS00093. N4_MTASE. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceP11409.

Entry information

Entry nameMTP2_PROHU
AccessionPrimary (citable) accession number: P11409
Entry history
Integrated into UniProtKB/Swiss-Prot: July 1, 1989
Last sequence update: October 1, 1996
Last modified: June 11, 2014
This is version 96 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

Restriction enzymes and methylases

Classification of restriction enzymes and methylases and list of entries

PDB cross-references

Index of Protein Data Bank (PDB) cross-references