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P14870

- T2F1_PLAOK

UniProt

P14870 - T2F1_PLAOK

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Protein
Type-2 restriction enzyme FokI
Gene
fokIR, rfoKI
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 sequences GGATG and CATCC 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

Magnesium.

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

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

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 583583Type-2 restriction enzyme FokI
PRO_0000077308Add
BLAST

Interactioni

Subunit structurei

Monomer. Homodimer when bound to DNA.1 Publication

Structurei

Secondary structure

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

3D structure databases

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

Miscellaneous databases

EvolutionaryTraceiP14870.

Family & Domainsi

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

MFLSMVSKIR TFGWVQNPGK FENLKRVVQV FDRNSKVHNE VKNIKIPTLV    50
KESKIQKELV AIMNQHDLIY TYKELVGTGT SIRSEAPCDA IIQATIADQG 100
NKKGYIDNWS SDGFLRWAHA LGFIEYINKS DSFVITDVGL AYSKSADGSA 150
IEKEILIEAI SSYPPAIRIL TLLEDGQHLT KFDLGKNLGF SGESGFTSLP 200
EGILLDTLAN AMPKDKGEIR NNWEGSSDKY ARMIGGWLDK LGLVKQGKKE 250
FIIPTLGKPD NKEFISHAFK ITGEGLKVLR RAKGSTKFTR VPKRVYWEML 300
ATNLTDKEYV RTRRALILEI LIKAGSLKIE QIQDNLKKLG FDEVIETIEN 350
DIKGLINTGI FIEIKGRFYQ LKDHILQFVI PNRGVTKQLV KSELEEKKSE 400
LRHKLKYVPH EYIELIEIAR NSTQDRILEM KVMEFFMKVY GYRGKHLGGS 450
RKPDGAIYTV GSPIDYGVIV DTKAYSGGYN LPIGQADEMQ RYVEENQTRN 500
KHINPNEWWK VYPSSVTEFK FLFVSGHFKG NYKAQLTRLN HITNCNGAVL 550
SVEELLIGGE MIKAGTLTLE EVRRKFNNGE INF 583
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.

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
J04623 Genomic DNA. Translation: AAA24927.1.
M28828 Genomic DNA. Translation: AAA24934.1. Different initiation.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
J04623 Genomic DNA. Translation: AAA24927.1 .
M28828 Genomic DNA. Translation: AAA24934.1 . Different initiation.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
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. "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. 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. Cited for: SUBUNIT.

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: April 16, 2014
This is version 93 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