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Reviewed, UniProtKB/Swiss-Prot P14870 (T2F1_FLAOK)

Last modified July 22, 2008. Version 66. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

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Names and origin

Protein namesRecommended name:
    Type-2 restriction enzyme FokI
      Short name(s)=R.FokI
    EC=3.1.21.4
Alternative name(s):
    Type II restriction enzyme FokI
    Type IIS restriction enzyme FokI
    Endonuclease FokI
Gene names
Name: fokIR
Synonyms: rfoKI
OrganismFlavobacterium okeanokoites (Planomicrobium okeanokoites)
Taxonomic identifier244 [NCBI]
Taxonomic lineageBacteria › Firmicutes › Bacillales › Planococcaceae › Planomicrobium

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Protein attributes

Sequence length583 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is not processed.
Protein existenceEvidence at protein level.

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General annotation (Comments)

Function

Recognizes the double-stranded sequences GGATG and CATCC and cleaves respectively 14 bases after G-1 and 13 bases before C-1.

Catalytic activity

Endonucleolytic cleavage of DNA to give specific double-stranded fragments with terminal 5'-phosphates.

Cofactor

Magnesium.

Subunit structure

Monomer. Homodimer when bound to DNA.

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Ontologies

Keywords

   Biological processRestriction system
   LigandMagnesium
   Molecular functionEndonuclease
Hydrolase
Nuclease
   Technical term3D-structure

Gene Ontology (GO)

None. [Check GOA]

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Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical view

Molecule processing

Chain1 – 583583Type-2 restriction enzyme FokI

Secondary structure

1 ................................................................................................. 583
Helix Strand Turn

Details...

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Sequences

Sequence LengthMass (Da)Tools
P14870-1 [UniParc].

Last modified April 1, 1990. Version 1.
Checksum: F4AF13DEEFA5CF09

FASTA58366,219
        10         20         30         40         50         60 
MFLSMVSKIR TFGWVQNPGK FENLKRVVQV FDRNSKVHNE VKNIKIPTLV KESKIQKELV 

        70         80         90        100        110        120 
AIMNQHDLIY TYKELVGTGT SIRSEAPCDA IIQATIADQG NKKGYIDNWS SDGFLRWAHA 

       130        140        150        160        170        180 
LGFIEYINKS DSFVITDVGL AYSKSADGSA IEKEILIEAI SSYPPAIRIL TLLEDGQHLT 

       190        200        210        220        230        240 
KFDLGKNLGF SGESGFTSLP EGILLDTLAN AMPKDKGEIR NNWEGSSDKY ARMIGGWLDK 

       250        260        270        280        290        300 
LGLVKQGKKE FIIPTLGKPD NKEFISHAFK ITGEGLKVLR RAKGSTKFTR VPKRVYWEML 

       310        320        330        340        350        360 
ATNLTDKEYV RTRRALILEI LIKAGSLKIE QIQDNLKKLG FDEVIETIEN DIKGLINTGI 

       370        380        390        400        410        420 
FIEIKGRFYQ LKDHILQFVI PNRGVTKQLV KSELEEKKSE LRHKLKYVPH EYIELIEIAR 

       430        440        450        460        470        480 
NSTQDRILEM KVMEFFMKVY GYRGKHLGGS RKPDGAIYTV GSPIDYGVIV DTKAYSGGYN 

       490        500        510        520        530        540 
LPIGQADEMQ RYVEENQTRN KHINPNEWWK VYPSSVTEFK FLFVSGHFKG NYKAQLTRLN 

       550        560        570        580 
HITNCNGAVL SVEELLIGGE MIKAGTLTLE EVRRKFNNGE INF

« Hide

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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: 2784436] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: ATCC 33414 / CIP 105082 / IFO 12536 / LMG 4030 / NCIMB 561.
[2]"Nucleotide sequence of the FokI restriction-modification system: separate strand-specificity domains in the methyltransferase."
Looney M.C., Moran L.S., Jack W.E., Feehery G.R., Benner J.S., Slatko B.E., Wilson G.G.
Gene 80:193-208(1989) [PubMed: 2684765] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[3]"Structure of the multimodular endonuclease FokI bound to DNA."
Wah D.A., Hirsch J.A., Dorner L.F., Schildkraut I., Aggarwal A.K.
Nature 388:97-100(1997) [PubMed: 9214510] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS).
Strain: ATCC 33414 / CIP 105082 / IFO 12536 / LMG 4030 / NCIMB 561.
[4]"Structure of FokI has implications for DNA cleavage."
Wah D.A., Bitinaite J., Schildkraut I., Aggarwal A.K.
Proc. Natl. Acad. Sci. U.S.A. 95:10564-10569(1998) [PubMed: 9724743] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS).
Strain: ATCC 33414 / CIP 105082 / IFO 12536 / LMG 4030 / NCIMB 561.
[5]"FokI dimerization is required for DNA cleavage."
Bitinaite J., Wah D.A., Aggarwal A.K., Schildkraut I.
Proc. Natl. Acad. Sci. U.S.A. 95:10570-10575(1998) [PubMed: 9724744] [Abstract]
Cited for: SUBUNIT.

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Cross-references

Sequence databases

J04623 Genomic DNA. Translation: AAA24927.1.
M28828 Genomic DNA. Translation: AAA24934.1. Different initiation.

3D structure databases

EntryMethodResolution (Å)ChainPositionsPDBsum
1FOKX-ray2.80A8-583[»]
2FOKX-ray2.30A/B5-583[»]
ModBaseSearch...

Protein family/group databases

REBASE1056. FokI.

Family and domain databases

InterProIPR011578. Restrict_endonuc_C/endonuc_I.
IPR015334. Restrict_endonuc_II_FokI_C.
IPR004233. Restrict_endonuc_II_FokI_cat.
IPR004234. Restrict_endonuc_II_FokI_N.
IPR011991. Wing_hlx_DNA_bd.
[Graphical view]
Gene3DG3DSA:3.40.91.30. Restrict_endonuc_C/endonuc_I. 1 hit.
G3DSA:1.10.10.10. Wing_hlx_DNA_bd. 1 hit.
PfamPF09254. Endonuc-FokI_C. 1 hit.
PF02980. FokI_C. 1 hit.
PF02981. FokI_N. 1 hit.
[Graphical view]
ProDomP14870.
[Graphical view] [Entries sharing at least one domain]
BLOCKSSearch...

Other Resources

LinkHubP14870.
ProtoNetSearch...

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Entry information

Entry nameT2F1_FLAOK
AccessionPrimary (citable) accession number: P14870
Entry history
Integrated into UniProtKB/Swiss-Prot: April 1, 1990
Last sequence update: April 1, 1990
Last modified: July 22, 2008
This is version 66 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHAMAP (High-quality Automated and Manual Annotation of microbial Proteomes)

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Relevant documents

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

Restriction enzymes and methylases

Classification of restriction enzymes and methylases and list of entries

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents