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A5F520 (DMA_VIBC3) Reviewed, UniProtKB/Swiss-Prot

Last modified June 11, 2014. Version 53. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | 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.VchADam
Gene names
Name:dam
Ordered Locus Names:VC0395_A2203, VC395_2739
OrganismVibrio cholerae serotype O1 (strain ATCC 39541 / Classical Ogawa 395 / O395) [Complete proteome] [HAMAP]
Taxonomic identifier345073 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaVibrionalesVibrionaceaeVibrio

Protein attributes

Sequence length277 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 By similarity.

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 – 277277DNA adenine methylase
PRO_0000324810

Sites

Binding site101S-adenosyl-L-methionine By similarity
Binding site141S-adenosyl-L-methionine; via amide nitrogen By similarity
Binding site541S-adenosyl-L-methionine By similarity
Binding site1811S-adenosyl-L-methionine By similarity

Sequences

Sequence LengthMass (Da)Tools
A5F520 [UniParc].

Last modified June 12, 2007. Version 1.
Checksum: 48D831240F9E7C60

FASTA27731,624
        10         20         30         40         50         60 
MKKQRAFLKW AGGKYSLVED IQRHLPEARE LVEPFVGAGS VFLNTDFERY LLADINPDLI 

        70         80         90        100        110        120 
NFYNLLKTEP QAYIHEAKRW FVPENNRKEV YLDIRKQFNQ SDDAMFRSLA FLYMNRFGFN 

       130        140        150        160        170        180 
GLCRYNKKGG FNVPFGSYKK PYFPEQELEF FAEKAQRATF ICASYGETFA RAQSDSVIYC 

       190        200        210        220        230        240 
DPPYAPLSTT ANFTSYAGNG FTLDDQAALA DIAEKTAKER GISVLISNHD TTHTRRLYRG 

       250        260        270 
AQLNVVKANR TISRNGAGRN KVDELLALFT PHLSSQA 

« Hide

References

« Hide 'large scale' references
[1]"DNA adenine methylase is essential for viability and plays a role in the pathogenesis of Yersinia pseudotuberculosis and Vibrio cholerae."
Julio S.M., Heithoff D.M., Provenzano D., Klose K.E., Sinsheimer R.L., Low D.A., Mahan M.J.
Infect. Immun. 69:7610-7615(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[2]Heidelberg J.
Submitted (MAR-2007) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 39541 / Classical Ogawa 395 / O395.
[3]"A recalibrated molecular clock and independent origins for the cholera pandemic clones."
Feng L., Reeves P.R., Lan R., Ren Y., Gao C., Zhou Z., Ren Y., Cheng J., Wang W., Wang J., Qian W., Li D., Wang L.
PLoS ONE 3:E4053-E4053(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 39541 / Classical Ogawa 395 / O395.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AF274317 Genomic DNA. Translation: AAG23174.1.
CP000627 Genomic DNA. Translation: ABQ21457.1.
CP001235 Genomic DNA. Translation: ACP10724.1.
RefSeqYP_001218119.1. NC_009457.1.
YP_002820960.1. NC_012582.1.

3D structure databases

ProteinModelPortalA5F520.
SMRA5F520. Positions 3-271.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING345073.VC0395_A2203.

Protein family/group databases

REBASE15105. M.VchO395ADamP.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaABQ21457; ABQ21457; VC0395_A2203.
ACP10724; ACP10724; VC395_2739.
GeneID5136322.
7776466.
KEGGvco:VC0395_A2203.
vcr:VC395_2739.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0338.
HOGENOMHOG000281348.
KOK06223.
OMAKFTREIY.

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. 1 hit.
[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_VIBC3
AccessionPrimary (citable) accession number: A5F520
Secondary accession number(s): C3LXM4, Q08318, Q9KNV4
Entry history
Integrated into UniProtKB/Swiss-Prot: March 18, 2008
Last sequence update: June 12, 2007
Last modified: June 11, 2014
This is version 53 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