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Protein

DNA adenine methylase

Gene

DAM

Organism
Enterobacteria phage T4 (Bacteriophage T4)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Experimental evidence at protein leveli

Functioni

This methylase recognizes the double-stranded sequence GATC, causes specific methylation on A-2 on both strands.

Catalytic activityi

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

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei7 – 71S-adenosyl-L-methionine
Binding sitei11 – 111S-adenosyl-L-methionine; via amide nitrogen
Binding sitei50 – 501S-adenosyl-L-methionine
Binding sitei171 – 1711S-adenosyl-L-methionine

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Methyltransferase, Transferase

Keywords - Biological processi

DNA replication

Keywords - Ligandi

S-adenosyl-L-methionine

Enzyme and pathway databases

BRENDAi2.1.1.72. 732.

Protein family/group databases

REBASEi2837. M.EcoT4Dam.

Names & Taxonomyi

Protein namesi
Recommended name:
DNA adenine methylase (EC:2.1.1.72)
Alternative name(s):
Deoxyadenosyl-methyltransferase
M.EcoT4Dam
Gene namesi
Name:DAM
OrganismiEnterobacteria phage T4 (Bacteriophage T4)
Taxonomic identifieri10665 [NCBI]
Taxonomic lineageiVirusesdsDNA viruses, no RNA stageCaudoviralesMyoviridaeTevenvirinaeT4likevirus
Virus hostiEscherichia coli [TaxID: 562]
ProteomesiUP000009087 Componenti: Genome

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi126 – 1261P → S in damh; hypermethylating mutant.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 259259DNA adenine methylasePRO_0000087990Add
BLAST

Structurei

Secondary structure

1
259
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Turni12 – 143Combined sources
Helixi15 – 206Combined sources
Beta strandi26 – 305Combined sources
Helixi39 – 413Combined sources
Beta strandi44 – 496Combined sources
Helixi53 – 6210Combined sources
Helixi67 – 7610Combined sources
Helixi84 – 9714Combined sources
Helixi100 – 1078Combined sources
Helixi111 – 1133Combined sources
Helixi136 – 14611Combined sources
Helixi147 – 1493Combined sources
Beta strandi150 – 1534Combined sources
Helixi157 – 1593Combined sources
Beta strandi166 – 1705Combined sources
Beta strandi175 – 1773Combined sources
Helixi180 – 1845Combined sources
Helixi187 – 20115Combined sources
Turni202 – 2043Combined sources
Beta strandi206 – 21510Combined sources
Helixi221 – 2277Combined sources
Beta strandi230 – 2345Combined sources
Helixi237 – 2426Combined sources
Beta strandi254 – 2585Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1Q0SX-ray2.30A1-259[»]
1Q0TX-ray3.10A/B1-259[»]
1YF3X-ray2.29A/B1-259[»]
1YFJX-ray2.69A/B/C/D/E/F1-259[»]
1YFLX-ray3.09A/B/D/E1-259[»]
ProteinModelPortaliP04392.
SMRiP04392. Positions 1-259.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP04392.

Family & Domainsi

Sequence similaritiesi

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

Phylogenomic databases

KOiK06223.

Family and domain databases

Gene3Di1.10.1020.10. 1 hit.
3.40.50.150. 2 hits.
InterProiIPR023095. Ade_MeTrfase_dom_2.
IPR002052. DNA_methylase_N6_adenine_CS.
IPR012263. M_m6A_EcoRV.
IPR012327. MeTrfase_D12.
IPR029063. SAM-dependent_MTases.
[Graphical view]
PfamiPF02086. MethyltransfD12. 1 hit.
[Graphical view]
PIRSFiPIRSF000398. M_m6A_EcoRV. 1 hit.
PRINTSiPR00505. D12N6MTFRASE.
SUPFAMiSSF53335. SSF53335. 1 hit.
TIGRFAMsiTIGR00571. dam. 1 hit.
PROSITEiPS00092. N6_MTASE. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P04392-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MLGAIAYTGN KQSLLPELKS HFPKYNRFVD LFCGGLSVSL NVNGPVLAND
60 70 80 90 100
IQEPIIEMYK RLINVSWDDV LKVIKQYKLS KTSKEEFLKL REDYNKTRDP
110 120 130 140 150
LLLYVLHFHG FSNMIRINDK GNFTTPFGKR TINKNSEKQY NHFKQNCDKI
160 170 180 190 200
IFSSLHFKDV KILDGDFVYV DPPYLITVAD YNKFWSEDEE KDLLNLLDSL
210 220 230 240 250
NDRGIKFGQS NVLEHHGKEN TLLKEWSKKY NVKHLNKKYV FNIYHSKEKN

GTDEVYIFN
Length:259
Mass (Da):30,417
Last modified:March 20, 1987 - v1
Checksum:iA49401D059A4388D
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti139 – 1402QY → RF (PubMed:2510127).Curated
Sequence conflicti209 – 2091Q → L (PubMed:2510127).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X01416 Genomic DNA. Translation: CAA25660.1.
K03113 Genomic DNA. Translation: AAA32555.1.
X17641 Genomic DNA. No translation available.
AF158101 Genomic DNA. Translation: AAD42553.1.
PIRiA00554. XYBPT4.
RefSeqiNP_049647.1. NC_000866.4.

Genome annotation databases

GeneIDi1258548.
KEGGivg:1258548.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X01416 Genomic DNA. Translation: CAA25660.1.
K03113 Genomic DNA. Translation: AAA32555.1.
X17641 Genomic DNA. No translation available.
AF158101 Genomic DNA. Translation: AAD42553.1.
PIRiA00554. XYBPT4.
RefSeqiNP_049647.1. NC_000866.4.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1Q0SX-ray2.30A1-259[»]
1Q0TX-ray3.10A/B1-259[»]
1YF3X-ray2.29A/B1-259[»]
1YFJX-ray2.69A/B/C/D/E/F1-259[»]
1YFLX-ray3.09A/B/D/E1-259[»]
ProteinModelPortaliP04392.
SMRiP04392. Positions 1-259.
ModBaseiSearch...
MobiDBiSearch...

Protein family/group databases

REBASEi2837. M.EcoT4Dam.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

GeneIDi1258548.
KEGGivg:1258548.

Phylogenomic databases

KOiK06223.

Enzyme and pathway databases

BRENDAi2.1.1.72. 732.

Miscellaneous databases

EvolutionaryTraceiP04392.

Family and domain databases

Gene3Di1.10.1020.10. 1 hit.
3.40.50.150. 2 hits.
InterProiIPR023095. Ade_MeTrfase_dom_2.
IPR002052. DNA_methylase_N6_adenine_CS.
IPR012263. M_m6A_EcoRV.
IPR012327. MeTrfase_D12.
IPR029063. SAM-dependent_MTases.
[Graphical view]
PfamiPF02086. MethyltransfD12. 1 hit.
[Graphical view]
PIRSFiPIRSF000398. M_m6A_EcoRV. 1 hit.
PRINTSiPR00505. D12N6MTFRASE.
SUPFAMiSSF53335. SSF53335. 1 hit.
TIGRFAMsiTIGR00571. dam. 1 hit.
PROSITEiPS00092. N6_MTASE. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Regulation of a new bacteriophage T4 gene, 69, that spans an origin of DNA replication."
    McDonald P.M., Mosig G.
    EMBO J. 3:2863-2871(1984) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  2. "Single amino acid changes that alter the DNA sequence specificity of the DNA-[N6-adenine] methyltransferase (Dam) of bacteriophage T4."
    Miner Z., Schlagman S.L., Hattman S.
    Nucleic Acids Res. 17:8149-8157(1989) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], MUTANT DAMH.
  3. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  4. Cited for: X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS).

Entry informationi

Entry nameiDMA_BPT4
AccessioniPrimary (citable) accession number: P04392
Entry historyi
Integrated into UniProtKB/Swiss-Prot: March 20, 1987
Last sequence update: March 20, 1987
Last modified: April 1, 2015
This is version 103 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programViral Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. Restriction enzymes and methylases
    Classification of restriction enzymes and methylases and list of entries
  3. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.