P12427 (DMA_BPT2) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
DNA adenine methylase
EC=2.1.1.72

Alternative name(s):
Deoxyadenosyl-methyltransferase
M.EcoT2Dam

Gene names

Name:

DAM

Organism

Enterobacteria phage T2 (Bacteriophage T2)

Taxonomic identifier

10664 [NCBI]

Taxonomic lineage

Viruses › dsDNA viruses, no RNA stage › Caudovirales › Myoviridae › Tevenvirinae › T4likevirus › Enterobacteria phage T4 sensu lato

Virus host

Escherichia coli [TaxID: 562]

Protein attributes

Sequence length	259 AA.
Sequence status	Complete.
Protein existence	Inferred from homology

General annotation (Comments)

Function	This methylase recognizes the double-stranded sequence GATC, causes specific methylation on A-2 on both strands.
Catalytic activity	S-adenosyl-L-methionine + DNA adenine = S-adenosyl-L-homocysteine + DNA 6-methylaminopurine.
Sequence similarities	Belongs to the N(4)/N(6)-methyltransferase family.

Ontologies

Keywords
Biological process	DNA replication
Ligand	S-adenosyl-L-methionine
Molecular function	Methyltransferase Transferase
Gene Ontology (GO)
Biological_process	DNA replication Inferred from electronic annotation. Source: UniProtKB-KW
Molecular_function	nucleic acid binding Inferred from electronic annotation. Source: InterPro site-specific DNA-methyltransferase (adenine-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 – 259	259	DNA adenine methylase		PRO_0000087989
Sites
	Binding site	7	1	S-adenosyl-L-methionine By similarity
	Binding site	11	1	S-adenosyl-L-methionine; via amide nitrogen By similarity
	Binding site	50	1	S-adenosyl-L-methionine By similarity
	Binding site	171	1	S-adenosyl-L-methionine By similarity

Sequences

	Sequence		Length	Mass (Da)
	P12427 [UniParc]. Last modified October 1, 1989. Version 1. Checksum: B3551303CFE71FD5	FASTA	259	30,439
	10 20 30 40 50 60 MLGAIAYTGN KQSLLPELKP HFPKYDRFVD LFCGGLSVSL NVNGPVLAND IQEPIIEMYK 70 80 90 100 110 120 RLINVSWDDV LKVIKQYKLS KTSKEEFLKL REDYNKTRDP LLLYVLHFHG FSNMIRINDK 130 140 150 160 170 180 GNFTTPFGKR TINKNSEKRF NHFKQNCDKI IFSSLHFKDV KILDGDFVYV DPPYLITVAD 190 200 210 220 230 240 YNKFWSEEEE KDLLNLLDSL NDRGIKFGLS NVLEHHGKEN TLLKEWSKKY NVKHLNKKYV 250 FNIYHSKEKN GTDEVYIFN

References

[1]	"Molecular cloning, sequencing, and mapping of the bacteriophage T2 dam gene." Miner Z., Hattman S. J. Bacteriol. 170:5177-5184(1988) [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: MUTAGENESIS.

Cross-references

Sequence databases
EMBL GenBank DDBJ	M22342 Genomic DNA. Translation: AAA32477.1.
PIR	XYBPT2. A30195.
3D structure databases
ProteinModelPortal	P12427.
SMR	P12427. Positions 1-259.
ModBase	Search...
Protein family/group databases
REBASE	2685. M.EcoT2Dam.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Family and domain databases
Gene3D	1.10.1020.10. 1 hit.
InterPro	IPR023095. Ade_MeTrfase_dom_2. IPR002052. DNA_methylase_N6_adenine_CS. IPR012263. M_m6A_EcoRV. IPR012327. MeTrfase_D12. [Graphical view]
Pfam	PF02086. MethyltransfD12. 1 hit. [Graphical view]
PIRSF	PIRSF000398. M_m6A_EcoRV. 1 hit.
PRINTS	PR00505. D12N6MTFRASE.
TIGRFAMs	TIGR00571. dam. 1 hit.
PROSITE	PS00092. N6_MTASE. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

DMA_BPT2

Accession

Primary (citable) accession number: P12427

Entry history

Integrated into UniProtKB/Swiss-Prot:	October 1, 1989
Last sequence update:	October 1, 1989
Last modified:	May 1, 2013
This is version 73 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Viral Protein Annotation Program