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P04043 (MTD21_STREE) Reviewed, UniProtKB/Swiss-Prot

Last modified October 16, 2013. Version 97. 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 DpnIIA

Short name=M.DpnIIA
EC=2.1.1.72
Alternative name(s):
Adenine-specific methyltransferase DpnIIA
M.DpnII 1
Gene names
Name:dpnM
OrganismStreptococcus pneumoniae
Taxonomic identifier1313 [NCBI]
Taxonomic lineageBacteriaFirmicutesBacilliLactobacillalesStreptococcaceaeStreptococcus

Protein attributes

Sequence length284 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

This methylase recognizes the double-stranded sequence GATC, causes specific methylation on A-2 on both strands, and protects the DNA from cleavage by the DpnII endonuclease.

Catalytic activity

S-adenosyl-L-methionine + DNA adenine = S-adenosyl-L-homocysteine + DNA 6-methylaminopurine.

Subunit structure

Homodimer.

Miscellaneous

The DpnII restriction system has two different methylases.

Sequence similarities

Belongs to the N(4)/N(6)-methyltransferase family.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 284284Modification methylase DpnIIA
PRO_0000087957

Sites

Binding site171S-adenosyl-L-methionine
Binding site211S-adenosyl-L-methionine; via amide nitrogen
Binding site621S-adenosyl-L-methionine
Binding site1941S-adenosyl-L-methionine

Secondary structure

......................................... 284
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P04043 [UniParc].

Last modified November 1, 1986. Version 1.
Checksum: 9F1525575CFA3E1E

FASTA28432,907
        10         20         30         40         50         60 
MKIKEIKKVT LQPFTKWTGG KRQLLPVIRE LIPKTYNRYF EPFVGGGALF FDLAPKDAVI 

        70         80         90        100        110        120 
NDFNAELINC YQQIKDNPQE LIEILKVHQE YNSKEYYLDL RSADRDERID MMSEVQRAAR 

       130        140        150        160        170        180 
ILYMLRVNFN GLYRVNSKNQ FNVPYGRYKN PKIVDEELIS AISVYINNNQ LEIKVGDFEK 

       190        200        210        220        230        240 
AIVDVRTGDF VYFDPPYIPL SETSAFTSYT HEGFSFADQV RLRDAFKRLS DTGAYVMLSN 

       250        260        270        280 
SSSALVEELY KDFNIHYVEA TRTNGAKSSS RGKISEIIVT NYEK 

« Hide

References

[1]"Nucleotide sequence of the Dpn II DNA methylase gene of Streptococcus pneumoniae and its relationship to the dam gene of Escherichia coli."
Mannarelli B.M., Balganesh T.S., Greenberg B., Springhorn S.S., Lacks S.A.
Proc. Natl. Acad. Sci. U.S.A. 82:4468-4472(1985) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[2]"Genetic basis of the complementary DpnI and DpnII restriction systems of S. pneumoniae: an intercellular cassette mechanism."
Lacks S.A., Mannarelli B.M., Springhorn S.S., Greenberg B.
Cell 46:993-1000(1986) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[3]"Proteins encoded by the DpnII restriction gene cassette. Two methylases and an endonuclease."
de la Campa A.G., Purushottam K., Springhorn S.S., Lacks S.A.
J. Mol. Biol. 196:457-469(1987) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 1-14.
[4]"Crystal structure of the DpnM DNA adenine methyltransferase from the DpnII restriction system of Streptococcus pneumoniae bound to S-adenosylmethionine."
Tran P.H., Korszun Z.R., Cerritelli S., Springhorn S.S., Lacks S.A.
Structure 6:1563-1575(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS) OF 10-284.
Strain: HB264.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
M11226 Genomic DNA. Translation: AAA26872.1.
M14339 Genomic DNA. Translation: AAA88580.1.
PIRXYSONA. A00556.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
2DPMX-ray1.80A1-284[»]
ProteinModelPortalP04043.
SMRP04043. Positions 10-284.
ModBaseSearch...
MobiDBSearch...

Protein family/group databases

REBASE3636. M1.DpnII.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Family and domain databases

Gene3D1.10.1020.10. 1 hit.
InterProIPR023095. Ade_MeTrfase_dom_2.
IPR002052. DNA_methylase_N6_adenine_CS.
IPR012263. M_m6A_EcoRV.
IPR012327. MeTrfase_D12.
[Graphical view]
PfamPF02086. MethyltransfD12. 1 hit.
[Graphical view]
PIRSFPIRSF000398. M_m6A_EcoRV. 1 hit.
PRINTSPR00505. D12N6MTFRASE.
TIGRFAMsTIGR00571. dam. 1 hit.
PROSITEPS00092. N6_MTASE. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceP04043.

Entry information

Entry nameMTD21_STREE
AccessionPrimary (citable) accession number: P04043
Entry history
Integrated into UniProtKB/Swiss-Prot: November 1, 1986
Last sequence update: November 1, 1986
Last modified: October 16, 2013
This is version 97 of the entry and version 1 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