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Protein

Type-2 restriction enzyme FokI

Gene

fokIR

Organism
Planomicrobium okeanokoites (Planococcus okeanokoites) (Flavobacterium okeanokoites)
Status
Reviewed-Annotation score: Annotation score: 4 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)DescriptionActionsGraphical viewLength
Active sitei4541 Publication1
Active sitei4711 Publication1
Active sitei4731 Publication1

GO - Molecular functioni

GO - Biological processi

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)DescriptionActionsGraphical viewLength
ChainiPRO_00000773081 – 583Type-2 restriction enzyme FokIAdd BLAST583

Interactioni

Subunit structurei

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

Structurei

Secondary structure

1583
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi21 – 28Combined sources8
Helixi36 – 43Combined sources8
Helixi45 – 49Combined sources5
Helixi53 – 64Combined sources12
Beta strandi65 – 67Combined sources3
Helixi72 – 76Combined sources5
Helixi83 – 85Combined sources3
Helixi91 – 95Combined sources5
Beta strandi102 – 105Combined sources4
Helixi108 – 120Combined sources13
Beta strandi123 – 127Combined sources5
Turni128 – 131Combined sources4
Beta strandi132 – 135Combined sources4
Helixi137 – 144Combined sources8
Helixi150 – 161Combined sources12
Helixi164 – 173Combined sources10
Helixi181 – 185Combined sources5
Beta strandi188 – 190Combined sources3
Helixi201 – 209Combined sources9
Helixi213 – 222Combined sources10
Helixi226 – 240Combined sources15
Beta strandi243 – 246Combined sources4
Beta strandi249 – 252Combined sources4
Beta strandi262 – 271Combined sources10
Helixi273 – 283Combined sources11
Beta strandi286 – 288Combined sources3
Helixi297 – 299Combined sources3
Helixi307 – 323Combined sources17
Beta strandi325 – 328Combined sources4
Helixi329 – 338Combined sources10
Helixi345 – 356Combined sources12
Turni357 – 359Combined sources3
Beta strandi362 – 365Combined sources4
Beta strandi368 – 371Combined sources4
Turni381 – 384Combined sources4
Helixi386 – 388Combined sources3
Helixi393 – 402Combined sources10
Beta strandi406 – 408Combined sources3
Helixi410 – 414Combined sources5
Helixi415 – 418Combined sources4
Helixi422 – 424Combined sources3
Helixi425 – 438Combined sources14
Beta strandi443 – 446Combined sources4
Beta strandi449 – 452Combined sources4
Beta strandi454 – 458Combined sources5
Beta strandi460 – 464Combined sources5
Beta strandi467 – 473Combined sources7
Helixi483 – 498Combined sources16
Turni501 – 503Combined sources3
Helixi508 – 511Combined sources4
Beta strandi519 – 526Combined sources8
Helixi532 – 543Combined sources12
Beta strandi546 – 551Combined sources6
Helixi552 – 564Combined sources13
Helixi569 – 573Combined sources5
Beta strandi577 – 580Combined sources4

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1FOKX-ray2.80A8-583[»]
2FOKX-ray2.30A/B5-583[»]
ProteinModelPortaliP14870.
SMRiP14870.
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.
IPR031655. Type2_restr_D3.
IPR011991. WHTH_DNA-bd_dom.
[Graphical view]
PfamiPF09254. Endonuc-FokI_C. 1 hit.
PF02980. FokI_C. 1 hit.
PF02981. FokI_N. 1 hit.
PF16902. Type2_restr_D3. 1 hit.
[Graphical view]
SUPFAMiSSF46785. SSF46785. 3 hits.
SSF52980. 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 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.Curated

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
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1FOKX-ray2.80A8-583[»]
2FOKX-ray2.30A/B5-583[»]
ProteinModelPortaliP14870.
SMRiP14870.
ModBaseiSearch...
MobiDBiSearch...

Protein family/group databases

REBASEi1056. FokI.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Miscellaneous databases

EvolutionaryTraceiP14870.

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.
IPR031655. Type2_restr_D3.
IPR011991. WHTH_DNA-bd_dom.
[Graphical view]
PfamiPF09254. Endonuc-FokI_C. 1 hit.
PF02980. FokI_C. 1 hit.
PF02981. FokI_N. 1 hit.
PF16902. Type2_restr_D3. 1 hit.
[Graphical view]
SUPFAMiSSF46785. SSF46785. 3 hits.
SSF52980. SSF52980. 1 hit.
ProtoNetiSearch...

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 2, 2016
This is version 104 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

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.