Skip Header

You are using a version of Internet Explorer that may not display all features of this website. Please upgrade to a modern browser.
Contribute Send feedback
Read comments (?) or add your own

P14871 (MTF1_PLAOK) Reviewed, UniProtKB/Swiss-Prot

Last modified June 11, 2014. Version 88. 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:
Modification methylase FokI

Short name=M.FokI
EC=2.1.1.72
Alternative name(s):
Adenine-specific methyltransferase FokI
Gene names
Name:fokIM
Synonyms:mfoKI
OrganismPlanomicrobium okeanokoites (Planococcus okeanokoites) (Flavobacterium okeanokoites)
Taxonomic identifier244 [NCBI]
Taxonomic lineageBacteriaFirmicutesBacilliBacillalesPlanococcaceaePlanomicrobium

Protein attributes

Sequence length647 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

This methylase recognizes the double-stranded sequence 5'-GGATG-3' in one strand and 3'-CATCC-5' in the other, causes specific methylation on the A of both strands, and protects the DNA from cleavage by the FokI endonuclease. The 2 domains of the protein participates in modification of the two strands.

Catalytic activity

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

Subunit structure

Monomer.

Sequence similarities

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

Ontologies

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 647647Modification methylase FokI
PRO_0000087960

Sequences

Sequence LengthMass (Da)Tools
P14871 [UniParc].

Last modified April 1, 1990. Version 1.
Checksum: 66F7D05F17345836

FASTA64775,626
        10         20         30         40         50         60 
MRFIGSKVNL LDNIQEVIEE NVKDDAHVFM DLFSGTGIVG ENFKKDYQVL SNDSLYFSYI 

        70         80         90        100        110        120 
LLKAKIENNS IPNFSELKKI GIKEPLHYLE NEEFEISHEF FLTHNYSPYM GCERMYFTVE 

       130        140        150        160        170        180 
NASRIDFIRL TLNRWKNESL INELEFAYLL AILIEAVPFI SNISGTYGAY LKHWDKRALG 

       190        200        210        220        230        240 
KLKLRTLDIG NNHYANKTYN EDANSLIEKV YGDILYIDPP YNGRQYISNY HLLETIALYD 

       250        260        270        280        290        300 
YPEIYGKTGL RPYVESKSLY CQKKEVGNAF NHLIEKANFR HILVSYSSEG LLLEEEIESI 

       310        320        330        340        350        360 
LKSHGLPETY RIYKMPYRKY KSKHKQEASE LHEYIFYIQK DIALTNSVKS NKKIEVGKHK 

       370        380        390        400        410        420 
TNSYIKSPLN YVGGKHKLLN QIVPLFPDKI DTFVDLFSGG FNVGINVNAN KIIATDINTY 

       430        440        450        460        470        480 
VVEVLDTMKK TSVEEVIAHI ERRIEEYGLS KSNEEGFKAF RNYYNKTKKP LDLYTLICYS 

       490        500        510        520        530        540 
FNYQFRFNNN QEYNNPFGRE RSQFSPALKK KLVLFIEALH EKNVQFVCSE FEHFNFSQLD 

       550        560        570        580        590        600 
QNDLVYCDPP YLITTGSYND GNRGFKDWNR LQEIKLLDIL DHLNSKGVYF ALSNVLSHKG 

       610        620        630        640 
LENELLLEWS KKYNIHHLQH SYSNSSHNTT RGESQEVLIT NYTNYTK 

« Hide

References

[1]"The fokI restriction-modification system. I. Organization and nucleotide sequences of the restriction and modification genes."
Kita K., Kotani H., Sugisaki H., Takanami M.
J. Biol. Chem. 264:5751-5756(1989) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 1-9.
Strain: ATCC 33414 / DSM 15489 / NBRC 12536 / NCIMB 561 / CIP 105082 / LMG 4030 / VKM B-1175.
[2]"The FokI restriction-modification system. II. Presence of two domains in FokI methylase responsible for modification of different DNA strands."
Sugisaki H., Kita K., Takanami M.
J. Biol. Chem. 264:5757-5761(1989) [PubMed] [Europe PMC] [Abstract]
Cited for: DOMAINS.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
J04623 Genomic DNA. Translation: AAA24926.1.

3D structure databases

ProteinModelPortalP14871.
ModBaseSearch...
MobiDBSearch...

Protein family/group databases

REBASE3405. M.FokI.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Family and domain databases

Gene3D1.10.1020.10. 1 hit.
3.40.50.150. 4 hits.
InterProIPR012186. Ade-mod_methylase_MStsI.
IPR023095. Ade_MeTrfase_dom_2.
IPR002052. DNA_methylase_N6_adenine_CS.
IPR012327. MeTrfase_D12.
IPR029063. SAM-dependent_MTases-like.
[Graphical view]
PfamPF02086. MethyltransfD12. 2 hits.
[Graphical view]
PIRSFPIRSF036638. M_m6A_StsI. 1 hit.
PRINTSPR00505. D12N6MTFRASE.
SUPFAMSSF53335. SSF53335. 3 hits.
TIGRFAMsTIGR00571. dam. 1 hit.
PROSITEPS00092. N6_MTASE. 2 hits.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameMTF1_PLAOK
AccessionPrimary (citable) accession number: P14871
Entry history
Integrated into UniProtKB/Swiss-Prot: April 1, 1990
Last sequence update: April 1, 1990
Last modified: June 11, 2014
This is version 88 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