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P14870

- T2F1_PLAOK

UniProt

P14870 - T2F1_PLAOK

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Protein

Type-2 restriction enzyme FokI

Gene

fokIR

Organism
Planomicrobium okeanokoites (Planococcus okeanokoites) (Flavobacterium okeanokoites)
Status
Reviewed - Annotation score: 3 out of 5- Experimental evidence at protein leveli

Functioni

Recognizes the double-stranded sequence 5'-GGATG-3'/3'-CATCC-5' and cleaves respectively 14 bases after G-1 and 13 bases before C-1.

Catalytic activityi

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

Cofactori

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei454 – 45411 Publication
Active sitei471 – 47111 Publication
Active sitei473 – 47311 Publication

GO - Molecular functioni

  1. DNA binding Source: InterPro
  2. Type II site-specific deoxyribonuclease activity Source: UniProtKB-EC

GO - Biological processi

  1. DNA restriction-modification system Source: UniProtKB-KW
Complete GO annotation...

Keywords - Molecular functioni

Endonuclease, Hydrolase, Nuclease

Keywords - Biological processi

Restriction system

Keywords - Ligandi

DNA-binding, Magnesium

Protein family/group databases

REBASEi1056. FokI.

Names & Taxonomyi

Protein namesi
Recommended name:
Type-2 restriction enzyme FokI (EC:3.1.21.4)
Short name:
R.FokI
Alternative name(s):
Endonuclease FokI
Type II restriction enzyme FokI
Type IIS restriction enzyme FokI
Gene namesi
Name:fokIR
Synonyms:rfoKI
OrganismiPlanomicrobium okeanokoites (Planococcus okeanokoites) (Flavobacterium okeanokoites)
Taxonomic identifieri244 [NCBI]
Taxonomic lineageiBacteriaFirmicutesBacilliBacillalesPlanococcaceaePlanomicrobium

Pathology & Biotechi

Biotechnological usei

Adding the endonuclease domain C-terminal to different DNA recognition domains from other enzymes allows generation of novel restriction enzymes that are used to genetically engineer eukaryotic cells.1 Publication1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 583583Type-2 restriction enzyme FokIPRO_0000077308Add
BLAST

Interactioni

Subunit structurei

Monomer, in which form it can cleave DNA. Homodimer when bound to DNA.2 Publications

Structurei

Secondary structure

1
583
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi21 – 288Combined sources
Helixi36 – 438Combined sources
Helixi45 – 495Combined sources
Helixi53 – 6412Combined sources
Beta strandi65 – 673Combined sources
Helixi72 – 765Combined sources
Helixi83 – 853Combined sources
Helixi91 – 955Combined sources
Beta strandi102 – 1054Combined sources
Helixi108 – 12013Combined sources
Beta strandi123 – 1275Combined sources
Turni128 – 1314Combined sources
Beta strandi132 – 1354Combined sources
Helixi137 – 1448Combined sources
Helixi150 – 16112Combined sources
Helixi164 – 17310Combined sources
Helixi181 – 1855Combined sources
Beta strandi188 – 1903Combined sources
Helixi201 – 2099Combined sources
Helixi213 – 22210Combined sources
Helixi226 – 24015Combined sources
Beta strandi243 – 2464Combined sources
Beta strandi249 – 2524Combined sources
Beta strandi262 – 27110Combined sources
Helixi273 – 28311Combined sources
Beta strandi286 – 2883Combined sources
Helixi297 – 2993Combined sources
Helixi307 – 32317Combined sources
Beta strandi325 – 3284Combined sources
Helixi329 – 33810Combined sources
Helixi345 – 35612Combined sources
Turni357 – 3593Combined sources
Beta strandi362 – 3654Combined sources
Beta strandi368 – 3714Combined sources
Turni381 – 3844Combined sources
Helixi386 – 3883Combined sources
Helixi393 – 40210Combined sources
Beta strandi406 – 4083Combined sources
Helixi410 – 4145Combined sources
Helixi415 – 4184Combined sources
Helixi422 – 4243Combined sources
Helixi425 – 43814Combined sources
Beta strandi443 – 4464Combined sources
Beta strandi449 – 4524Combined sources
Beta strandi454 – 4585Combined sources
Beta strandi460 – 4645Combined sources
Beta strandi467 – 4737Combined sources
Helixi483 – 49816Combined sources
Turni501 – 5033Combined sources
Helixi508 – 5114Combined sources
Beta strandi519 – 5268Combined sources
Helixi532 – 54312Combined sources
Beta strandi546 – 5516Combined sources
Helixi552 – 56413Combined sources
Helixi569 – 5735Combined sources
Beta strandi577 – 5804Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1FOKX-ray2.80A8-583[»]
2FOKX-ray2.30A/B5-583[»]
ProteinModelPortaliP14870.
SMRiP14870. Positions 8-583.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP14870.

Family & Domainsi

Domaini

Has an N-terminal DNA recognition domain (approximately residues 1-292) joined to an endonuclease domain (residues 389-583) by a flexible linker.1 Publication

Family and domain databases

Gene3Di1.10.10.10. 1 hit.
3.40.91.30. 1 hit.
InterProiIPR011335. 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]
PfamiPF09254. Endonuc-FokI_C. 1 hit.
PF02980. FokI_C. 1 hit.
PF02981. FokI_N. 1 hit.
[Graphical view]
SUPFAMiSSF52980. SSF52980. 1 hit.

Sequencei

Sequence statusi: Complete.

P14870-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MFLSMVSKIR TFGWVQNPGK FENLKRVVQV FDRNSKVHNE VKNIKIPTLV
60 70 80 90 100
KESKIQKELV AIMNQHDLIY TYKELVGTGT SIRSEAPCDA IIQATIADQG
110 120 130 140 150
NKKGYIDNWS SDGFLRWAHA LGFIEYINKS DSFVITDVGL AYSKSADGSA
160 170 180 190 200
IEKEILIEAI SSYPPAIRIL TLLEDGQHLT KFDLGKNLGF SGESGFTSLP
210 220 230 240 250
EGILLDTLAN AMPKDKGEIR NNWEGSSDKY ARMIGGWLDK LGLVKQGKKE
260 270 280 290 300
FIIPTLGKPD NKEFISHAFK ITGEGLKVLR RAKGSTKFTR VPKRVYWEML
310 320 330 340 350
ATNLTDKEYV RTRRALILEI LIKAGSLKIE QIQDNLKKLG FDEVIETIEN
360 370 380 390 400
DIKGLINTGI FIEIKGRFYQ LKDHILQFVI PNRGVTKQLV KSELEEKKSE
410 420 430 440 450
LRHKLKYVPH EYIELIEIAR NSTQDRILEM KVMEFFMKVY GYRGKHLGGS
460 470 480 490 500
RKPDGAIYTV GSPIDYGVIV DTKAYSGGYN LPIGQADEMQ RYVEENQTRN
510 520 530 540 550
KHINPNEWWK VYPSSVTEFK FLFVSGHFKG NYKAQLTRLN HITNCNGAVL
560 570 580
SVEELLIGGE MIKAGTLTLE EVRRKFNNGE INF
Length:583
Mass (Da):66,219
Last modified:April 1, 1990 - v1
Checksum:iF4AF13DEEFA5CF09
GO

Sequence cautioni

The sequence AAA24934.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extendedCurated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
J04623 Genomic DNA. Translation: AAA24927.1.
M28828 Genomic DNA. Translation: AAA24934.1. Different initiation.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
J04623 Genomic DNA. Translation: AAA24927.1 .
M28828 Genomic DNA. Translation: AAA24934.1 . Different initiation.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
1FOK X-ray 2.80 A 8-583 [» ]
2FOK X-ray 2.30 A/B 5-583 [» ]
ProteinModelPortali P14870.
SMRi P14870. Positions 8-583.
ModBasei Search...
MobiDBi Search...

Protein family/group databases

REBASEi 1056. FokI.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Miscellaneous databases

EvolutionaryTracei P14870.

Family and domain databases

Gene3Di 1.10.10.10. 1 hit.
3.40.91.30. 1 hit.
InterProi IPR011335. 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 ]
Pfami PF09254. Endonuc-FokI_C. 1 hit.
PF02980. FokI_C. 1 hit.
PF02981. FokI_N. 1 hit.
[Graphical view ]
SUPFAMi SSF52980. SSF52980. 1 hit.
ProtoNeti Search...

Publicationsi

  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. Cited for: SUBUNIT.
  4. "Programmable DNA-binding proteins from Burkholderia provide a fresh perspective on the TALE-like repeat domain."
    de Lange O., Wolf C., Dietze J., Elsaesser J., Morbitzer R., Lahaye T.
    Nucleic Acids Res. 42:7436-7449(2014) [PubMed] [Europe PMC] [Abstract]
    Cited for: BIOTECHNOLOGY.
  5. "TALEN-mediated genome editing: prospects and perspectives."
    Wright D.A., Li T., Yang B., Spalding M.H.
    Biochem. J. 462:15-24(2014) [PubMed] [Europe PMC] [Abstract]
    Cited for: BIOTECHNOLOGY USES REVIEW.
  6. "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), SUBUNIT, DOMAIN, DNA-BINDING, ACTIVE SITE.
    Strain: ATCC 33414 / DSM 15489 / NBRC 12536 / NCIMB 561 / CIP 105082 / LMG 4030 / VKM B-1175.
  7. Cited for: X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS).
    Strain: ATCC 33414 / DSM 15489 / NBRC 12536 / NCIMB 561 / CIP 105082 / LMG 4030 / VKM B-1175.

Entry informationi

Entry nameiT2F1_PLAOK
AccessioniPrimary (citable) accession number: P14870
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 1, 1990
Last sequence update: April 1, 1990
Last modified: November 26, 2014
This is version 96 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. Restriction enzymes and methylases
    Classification of restriction enzymes and methylases and list of entries

External Data

Dasty 3