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P14870 (T2F1_PLAOK) Reviewed, UniProtKB/Swiss-Prot

Last modified May 1, 2013. Version 90. 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
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-2 restriction enzyme FokI
Short name=R.FokI
EC=3.1.21.4
Alternative name(s):
Endonuclease FokI
Type II restriction enzyme FokI
Type IIS restriction enzyme FokI
Gene names
Name:fokIR
Synonyms:rfoKI
OrganismPlanomicrobium okeanokoites (Planococcus okeanokoites) (Flavobacterium okeanokoites)
Taxonomic identifier244 [NCBI]
Taxonomic lineageBacteria › Firmicutes › Bacilli › Bacillales › Planococcaceae › Planomicrobium

Protein attributes

Sequence length583 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

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. Ref.5

Sequence caution

The sequence AAA24934.1 differs from that shown. Reason: Erroneous initiation.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 583583Type-2 restriction enzyme FokI
PRO_0000077308

Secondary structure

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

Details...

Sequences

Sequence LengthMass (Da)Tools
P14870 [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

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].
Strain: ATCC 33414 / DSM 15489 / NBRC 12536 / NCIMB 561 / CIP 105082 / LMG 4030 / VKM B-1175.
[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] [Europe PMC] [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] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS).
Strain: ATCC 33414 / DSM 15489 / NBRC 12536 / NCIMB 561 / CIP 105082 / LMG 4030 / VKM B-1175.
[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] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS).
Strain: ATCC 33414 / DSM 15489 / NBRC 12536 / NCIMB 561 / CIP 105082 / LMG 4030 / VKM B-1175.
[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] [Europe PMC] [Abstract]
Cited for: SUBUNIT.

Cross-references

Sequence databases

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

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1FOKX-ray2.80A8-583[»]
2FOKX-ray2.30A/B5-583[»]
ProteinModelPortalP14870.
SMRP14870. Positions 8-583.
ModBaseSearch...

Protein family/group databases

REBASE1056. FokI.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Family and domain databases

Gene3D1.10.10.10. 1 hit.
3.40.91.30. 1 hit.
InterProIPR011335. Restrct_endonuc-II-like.
IPR011578. Restrct_endonuc_C/endonuc_I.
IPR015334. Restrct_endonuc_II_FokI_C.
IPR004233. Restrct_endonuc_II_FokI_cat.
IPR004234. Restrct_endonuc_II_FokI_N.
IPR011991. WHTH_DNA-bd_dom.
[Graphical view]
PfamPF09254. Endonuc-FokI_C. 1 hit.
PF02980. FokI_C. 1 hit.
PF02981. FokI_N. 1 hit.
[Graphical view]
SUPFAMSSF52980. Restrict_endonuc_II-like_core. 1 hit.
ProtoNetSearch...

Other

EvolutionaryTraceP14870.

Entry information

Entry nameT2F1_PLAOK
AccessionPrimary (citable) accession number: P14870
Entry history
Integrated into UniProtKB/Swiss-Prot: April 1, 1990
Last sequence update: April 1, 1990
Last modified: May 1, 2013
This is version 90 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

Restriction enzymes and methylases

Classification of restriction enzymes and methylases and list of entries

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

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