UniProtKB - P04392 (DMA_BPT4)
Protein
DNA adenine methylase
Gene
DAM
Organism
Enterobacteria phage T4 (Bacteriophage T4)
Status
Functioni
Methyltransferase that methylates adenine residues in the dsDNA sequence GATC. May prevent degradation of viral DNA by the host restriction-modification antiviral defense system.Curated1 Publication
Catalytic activityi
- a 2'-deoxyadenosine in DNA + S-adenosyl-L-methionine = an N6-methyl-2'-deoxyadenosine in DNA + H+ + S-adenosyl-L-homocysteine1 PublicationEC:2.1.1.721 Publication
Kineticsi
- KM=0.1 µM for S-adenosylmethionine1 Publication
pH dependencei
Optimum pH is 7.0-8.5.1 Publication
Sites
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Binding sitei | 7 | S-adenosyl-L-methionineCombined sources | 1 | |
Binding sitei | 11 | S-adenosyl-L-methionine; via amide nitrogenCombined sources | 1 | |
Binding sitei | 50 | S-adenosyl-L-methionineCombined sources | 1 | |
Binding sitei | 171 | S-adenosyl-L-methionineCombined sources | 1 | |
Binding sitei | 181 | S-adenosyl-L-methionineCombined sources | 1 |
GO - Molecular functioni
- DNA-methyltransferase activity Source: CACAO
- nucleic acid binding Source: InterPro
- site-specific DNA-methyltransferase (adenine-specific) activity Source: UniProtKB-EC
GO - Biological processi
- DNA replication Source: UniProtKB-KW
- methylation Source: CACAO
- restriction-modification system evasion by virus Source: UniProtKB-KW
Keywordsi
Molecular function | Methyltransferase, Transferase |
Biological process | DNA replication, Host-virus interaction, Restriction-modification system evasion by virus |
Ligand | S-adenosyl-L-methionine |
Enzyme and pathway databases
BRENDAi | 2.1.1.72, 732 |
Protein family/group databases
REBASEi | 2837, M.EcoT4Dam |
Names & Taxonomyi
Protein namesi | Recommended name: DNA adenine methylase (EC:2.1.1.721 Publication)Alternative name(s): DNA-(N(6)-adenine)-methyltransferase1 Publication Deoxyadenosyl-methyltransferase M.EcoT4Dam |
Gene namesi | Name:DAM |
Organismi | Enterobacteria phage T4 (Bacteriophage T4) |
Taxonomic identifieri | 10665 [NCBI] |
Taxonomic lineagei | Viruses › Duplodnaviria › Heunggongvirae › Uroviricota › Caudoviricetes › Caudovirales › Myoviridae › Tevenvirinae › Tequatrovirus |
Virus hosti | Escherichia coli [TaxID: 562] |
Proteomesi |
|
Pathology & Biotechi
Mutagenesis
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Mutagenesisi | 126 | P → S in damh; hypermethylating mutant. | 1 |
Chemistry databases
DrugBanki | DB01752, S-adenosyl-L-homocysteine |
PTM / Processingi
Molecule processing
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
ChainiPRO_0000087990 | 1 – 259 | DNA adenine methylaseAdd BLAST | 259 |
Proteomic databases
PRIDEi | P04392 |
Interactioni
Subunit structurei
Monomer.
2 PublicationsStructurei
Secondary structure
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details3D structure databases
SMRi | P04392 |
ModBasei | Search... |
PDBe-KBi | Search... |
Miscellaneous databases
EvolutionaryTracei | P04392 |
Family & Domainsi
Region
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Regioni | 32 – 37 | S-adenosyl-L-methionine bindingCombined sources | 6 | |
Regioni | 156 – 157 | S-adenosyl-L-methionine bindingCombined sources | 2 |
Sequence similaritiesi
Belongs to the N(4)/N(6)-methyltransferase family.Curated
Family and domain databases
Gene3Di | 1.10.1020.10, 1 hit |
InterProi | View protein in InterPro IPR023095, Ade_MeTrfase_dom_2 IPR002052, DNA_methylase_N6_adenine_CS IPR012263, M_m6A_EcoRV IPR012327, MeTrfase_D12 IPR029063, SAM-dependent_MTases |
PANTHERi | PTHR30481, PTHR30481, 1 hit |
Pfami | View protein in Pfam PF02086, MethyltransfD12, 1 hit |
PIRSFi | PIRSF000398, M_m6A_EcoRV, 1 hit |
PRINTSi | PR00505, D12N6MTFRASE |
SUPFAMi | SSF53335, SSF53335, 1 hit |
TIGRFAMsi | TIGR00571, dam, 1 hit |
PROSITEi | View protein in PROSITE PS00092, N6_MTASE, 1 hit |
i Sequence
Sequence statusi: Complete.
P04392-1 [UniParc]FASTAAdd to basket
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
Experimental Info
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Sequence conflicti | 139 – 140 | QY → RF in X17641 (PubMed:2510127).Curated | 2 | |
Sequence conflicti | 209 | Q → L in X17641 (PubMed:2510127).Curated | 1 |
Sequence databases
Select the link destinations: EMBLi GenBanki DDBJi Links Updated | X01416 Genomic DNA Translation: CAA25660.1 X17641 Genomic DNA No translation available. K03113 Genomic DNA Translation: AAA32555.1 AF158101 Genomic DNA Translation: AAD42553.1 |
PIRi | A00554, XYBPT4 |
RefSeqi | NP_049647.1, NC_000866.4 |
Genome annotation databases
GeneIDi | 1258548 |
KEGGi | vg:1258548 |
Similar proteinsi
Cross-referencesi
Sequence databases
Select the link destinations: EMBLi GenBanki DDBJi Links Updated | X01416 Genomic DNA Translation: CAA25660.1 X17641 Genomic DNA No translation available. K03113 Genomic DNA Translation: AAA32555.1 AF158101 Genomic DNA Translation: AAD42553.1 |
PIRi | A00554, XYBPT4 |
RefSeqi | NP_049647.1, NC_000866.4 |
3D structure databases
Select the link destinations: PDBei RCSB PDBi PDBji Links Updated | PDB entry | Method | Resolution (Å) | Chain | Positions | PDBsum |
1Q0S | X-ray | 2.30 | A | 1-259 | [»] | |
1Q0T | X-ray | 3.10 | A/B | 1-259 | [»] | |
1YF3 | X-ray | 2.29 | A/B | 1-259 | [»] | |
1YFJ | X-ray | 2.69 | A/B/C/D/E/F | 1-259 | [»] | |
1YFL | X-ray | 3.09 | A/B/D/E | 1-259 | [»] | |
SMRi | P04392 | |||||
ModBasei | Search... | |||||
PDBe-KBi | Search... |
Chemistry databases
DrugBanki | DB01752, S-adenosyl-L-homocysteine |
Protein family/group databases
REBASEi | 2837, M.EcoT4Dam |
Proteomic databases
PRIDEi | P04392 |
Genome annotation databases
GeneIDi | 1258548 |
KEGGi | vg:1258548 |
Enzyme and pathway databases
BRENDAi | 2.1.1.72, 732 |
Miscellaneous databases
EvolutionaryTracei | P04392 |
Family and domain databases
Gene3Di | 1.10.1020.10, 1 hit |
InterProi | View protein in InterPro IPR023095, Ade_MeTrfase_dom_2 IPR002052, DNA_methylase_N6_adenine_CS IPR012263, M_m6A_EcoRV IPR012327, MeTrfase_D12 IPR029063, SAM-dependent_MTases |
PANTHERi | PTHR30481, PTHR30481, 1 hit |
Pfami | View protein in Pfam PF02086, MethyltransfD12, 1 hit |
PIRSFi | PIRSF000398, M_m6A_EcoRV, 1 hit |
PRINTSi | PR00505, D12N6MTFRASE |
SUPFAMi | SSF53335, SSF53335, 1 hit |
TIGRFAMsi | TIGR00571, dam, 1 hit |
PROSITEi | View protein in PROSITE PS00092, N6_MTASE, 1 hit |
ProtoNeti | Search... |
MobiDBi | Search... |
Entry informationi
Entry namei | DMA_BPT4 | |
Accessioni | P04392Primary (citable) accession number: P04392 | |
Entry historyi | Integrated into UniProtKB/Swiss-Prot: | March 20, 1987 |
Last sequence update: | March 20, 1987 | |
Last modified: | December 2, 2020 | |
This is version 125 of the entry and version 1 of the sequence. See complete history. | ||
Entry statusi | Reviewed (UniProtKB/Swiss-Prot) | |
Annotation program | Viral Protein Annotation Program |
Miscellaneousi
Keywords - Technical termi
3D-structure, Reference proteomeDocuments
- PDB cross-references
Index of Protein Data Bank (PDB) cross-references - SIMILARITY comments
Index of protein domains and families - Restriction enzymes and methylases
Classification of restriction enzymes and methylases and list of entries