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O33844 (DMA_TREPA) Reviewed, UniProtKB/Swiss-Prot

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

Clusters with 100%, 90%, 50% identity | Documents (2) | 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:
DNA adenine methylase

EC=2.1.1.72
Alternative name(s):
DNA adenine methyltransferase
Deoxyadenosyl-methyltransferase
M.TpaI
Gene names
Name:dam
Ordered Locus Names:TP_0810
OrganismTreponema pallidum (strain Nichols) [Complete proteome] [HAMAP]
Taxonomic identifier243276 [NCBI]
Taxonomic lineageBacteriaSpirochaetesSpirochaetalesSpirochaetaceaeTreponema

Protein attributes

Sequence length303 AA.
Sequence statusComplete.
Protein existenceInferred from homology

General annotation (Comments)

Function

Methylates DNA within the sequence GATC. Directly involved in methyl-directed DNA mismatch repair, DNA replication, and gene expression.

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 processDNA replication
   LigandS-adenosyl-L-methionine
   Molecular functionMethyltransferase
Transferase
   Technical termComplete proteome
Gene Ontology (GO)
   Biological_processDNA replication

Inferred from electronic annotation. Source: UniProtKB-KW

   Molecular_functionnucleic acid binding

Inferred from electronic annotation. Source: InterPro

site-specific DNA-methyltransferase (adenine-specific) activity

Inferred from electronic annotation. Source: UniProtKB-EC

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 303303DNA adenine methylase
PRO_0000087998

Sites

Binding site131S-adenosyl-L-methionine By similarity
Binding site171S-adenosyl-L-methionine; via amide nitrogen By similarity
Binding site641S-adenosyl-L-methionine By similarity
Binding site2121S-adenosyl-L-methionine By similarity

Sequences

Sequence LengthMass (Da)Tools
O33844 [UniParc].

Last modified January 1, 1998. Version 1.
Checksum: 62D2155EAE22DB90

FASTA30333,919
        10         20         30         40         50         60 
MSRSDTARPF VKWAGGKRAL APTLFAHMPQ TFGSYFEPFV GGGALFWHLC ACTRVRLHDI 

        70         80         90        100        110        120 
YLSDINWPLL CAYAAVRDRV EELIVRVGQH IACHTPTYYR LARRKFAVCE HPLEVAALFL 

       130        140        150        160        170        180 
YLNRSCYNGL YRVNKAGQFN VPLGRAAPAS PFLNTTAPTP RSTQPAAQVG HLAIRIDEEN 

       190        200        210        220        230        240 
LRSCARALAN TTLNCQHFSC IQPARGDFVY LDPPYLGTFS AYDKTGFDRA AHESLAAFCM 

       250        260        270        280        290        300 
HLDARGVLFM LSNSDCPEVR AWYRPFRVQQ LNAPRCIARS AHARGKRCEV LITNYPCADT 


ATP 

« Hide

References

« Hide 'large scale' references
[1]"Identification and characterization of a Treponema pallidum subsp. pallidum gene encoding a DNA adenine methyltransferase."
Stamm L.V., Greene S.R., Barnes N.Y., Bergen H.L., Hardham J.M.
FEMS Microbiol. Lett. 155:115-119(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: Nichols.
[2]"Complete genome sequence of Treponema pallidum, the syphilis spirochete."
Fraser C.M., Norris S.J., Weinstock G.M., White O., Sutton G.G., Dodson R.J., Gwinn M.L., Hickey E.K., Clayton R.A., Ketchum K.A., Sodergren E., Hardham J.M., McLeod M.P., Salzberg S.L., Peterson J.D., Khalak H.G., Richardson D.L., Howell J.K. expand/collapse author list , Chidambaram M., Utterback T.R., McDonald L.A., Artiach P., Bowman C., Cotton M.D., Fujii C., Garland S.A., Hatch B., Horst K., Roberts K.M., Sandusky M., Weidman J.F., Smith H.O., Venter J.C.
Science 281:375-388(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: Nichols.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AF006263 Genomic DNA. Translation: AAB82782.1.
AE000520 Genomic DNA. Translation: AAC65779.1.
PIRH71277.
RefSeqNP_219247.1. NC_000919.1.
YP_008091637.1. NC_021490.2.

3D structure databases

ProteinModelPortalO33844.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

IntActO33844. 1 interaction.
STRING243276.TP0810.

Protein family/group databases

REBASE3131. M.TpaI.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAC65779; AAC65779; TP_0810.
GeneID15852101.
2610874.
KEGGtpa:TP0810.
tpw:TPANIC_0810.
PATRIC20531719. VBITrePal57110_0857.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0338.
KOK06223.
OMANSDSEFI.
OrthoDBEOG6CS08V.

Enzyme and pathway databases

BioCycTPAL243276:GC1H-858-MONOMER.

Family and domain databases

Gene3D1.10.1020.10. 1 hit.
3.40.50.150. 2 hits.
InterProIPR023095. Ade_MeTrfase_dom_2.
IPR002052. DNA_methylase_N6_adenine_CS.
IPR012263. M_m6A_EcoRV.
IPR012327. MeTrfase_D12.
IPR029063. SAM-dependent_MTases-like.
[Graphical view]
PfamPF02086. MethyltransfD12. 2 hits.
[Graphical view]
PIRSFPIRSF000398. M_m6A_EcoRV. 1 hit.
PRINTSPR00505. D12N6MTFRASE.
SUPFAMSSF53335. SSF53335. 1 hit.
TIGRFAMsTIGR00571. dam. 1 hit.
PROSITEPS00092. N6_MTASE. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameDMA_TREPA
AccessionPrimary (citable) accession number: O33844
Entry history
Integrated into UniProtKB/Swiss-Prot: December 15, 1998
Last sequence update: January 1, 1998
Last modified: June 11, 2014
This is version 96 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