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P12364 (T3MO_ECOLX) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 80. 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:
Type III restriction-modification system EcoP15I enzyme mod

Short name=M.EcoP15I
EC=2.1.1.72
Alternative name(s):
EcoP15I methyltransferase
Gene names
Name:mod
Encoded onPlasmid p15B
OrganismEscherichia coli
Taxonomic identifier562 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia

Protein attributes

Sequence length645 AA.
Sequence statusComplete.
Protein existenceInferred from homology

General annotation (Comments)

Function

Binds the system-specific DNA recognition site 5'-CAGCAC-3'. Necessary for both restriction and methylation (of one of the two A's).

Catalytic activity

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

Subunit structure

Contains two different subunits: res and mod. Mod is a homotetramer.

Sequence similarities

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

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 645645Type III restriction-modification system EcoP15I enzyme mod
PRO_0000088031

Regions

Region123 – 1264Binding of S-adenosyl methionine Potential

Sequences

Sequence LengthMass (Da)Tools
P12364 [UniParc].

Last modified October 1, 1989. Version 1.
Checksum: 0EFE6653BAA3A705

FASTA64574,222
        10         20         30         40         50         60 
MKKETIFSEV ETANSKQLAV LKANFPQCFD KNGAFIQEKL LEIIRASEVE LSKESYSLNW 

        70         80         90        100        110        120 
LGKSYARLLA NLPPKTLLAE DKTHNQQEEN KNSQHLLIKG DNLEVLKHMV NAYAEKVKMI 

       130        140        150        160        170        180 
YIDPPYNTGK DGFVYNDDRK FTPEQLSELA GIDLDQAKRI LEFTTKGSSS HSAWLTFIYP 

       190        200        210        220        230        240 
RLYIARELMR EDGTIFISID HNEFSQLKLV CDEIFGEQNH VGDLVWKNAT DNNPSNIAVE 

       250        260        270        280        290        300 
HEYIIVYTKN KEQLISEWKS NISDVKNLLV NIGEEFASKY TGNELQEKYT QWFREHRSEL 

       310        320        330        340        350        360 
WPLDRYKYID KDGIYTGSQS VHNPGKEGYR YDIIHPKTKK PCKQQPLMGY RFPLDTMDRL 

       370        380        390        400        410        420 
LSEEKIIFGD DENKIIELKV YAKDYKQKLS SVIHLDGRVA TNELKELFPE MTQPFTNAKT 

       430        440        450        460        470        480 
IKLVEDLISF ACDGEGIVLD FFAGSGTTAH TVFNLNNKNK TSYQFITVQL DEPKKDKSDA 

       490        500        510        520        530        540 
MKHGYNTIFD LTKERLIRAS KKNRDQGFKV YQLMADFRAK DESELTLSNH TFFDDVVLTP 

       550        560        570        580        590        600 
EQYDTLLTTW CLYDGSLLTT PIEDVDLGGY KAHLCDGRLY LIAPNFTSEA LKALLQKVDS 

       610        620        630        640 
DKDFAPNKVV FYGSNFESAK QMELNEALKS YANKKSIELD LVVRN 

« Hide

References

[1]"Type III DNA restriction and modification systems EcoP1 and EcoP15. Nucleotide sequence of the EcoP1 operon, the EcoP15 mod gene and some EcoP1 mod mutants."
Huembelin M., Suri B., Rao D.N., Hornby D.P., Eberle H., Pripfl T., Kenel S., Bickle T.A.
J. Mol. Biol. 200:23-29(1988) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
X06288 Genomic DNA. Translation: CAA29616.1.
PIRS03208.

3D structure databases

ProteinModelPortalP12364.
ModBaseSearch...
MobiDBSearch...

Protein family/group databases

REBASE3389. M.EcoP15I.

Proteomic databases

PRIDEP12364.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Family and domain databases

InterProIPR002295. D21N6_MeTrfase.
IPR002941. DNA_methylase_N4/N6.
IPR002052. DNA_methylase_N6_adenine_CS.
[Graphical view]
PfamPF01555. N6_N4_Mtase. 1 hit.
[Graphical view]
PIRSFPIRSF015855. TypeIII_Mtase_mKpnI. 1 hit.
PRINTSPR00506. D21N6MTFRASE.
PROSITEPS00092. N6_MTASE. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameT3MO_ECOLX
AccessionPrimary (citable) accession number: P12364
Entry history
Integrated into UniProtKB/Swiss-Prot: October 1, 1989
Last sequence update: October 1, 1989
Last modified: April 16, 2014
This is version 80 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