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Protein

Type-2 restriction enzyme BglI

Gene

bglIR

Organism
Bacillus subtilis
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Experimental evidence at protein leveli

Functioni

Recognizes the double-stranded sequence GCCNNNNNGGC and cleaves before N-8.

Catalytic activityi

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

Cofactori

Mg2+Note: Binds 2 magnesium ions per subunit.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi116 – 1161Magnesium 1
Metal bindingi116 – 1161Magnesium 2
Metal bindingi142 – 1421Magnesium 1
Metal bindingi143 – 1431Magnesium 1; via carbonyl oxygen

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Endonuclease, Hydrolase, Nuclease

Keywords - Biological processi

Restriction system

Keywords - Ligandi

Magnesium, Metal-binding

Protein family/group databases

REBASEi260. BglI.

Names & Taxonomyi

Protein namesi
Recommended name:
Type-2 restriction enzyme BglI (EC:3.1.21.4)
Short name:
R.BglI
Alternative name(s):
Endonuclease BglI
Type II restriction enzyme BglI
Gene namesi
Name:bglIR
OrganismiBacillus subtilis
Taxonomic identifieri1423 [NCBI]
Taxonomic lineageiBacteriaFirmicutesBacilliBacillalesBacillaceaeBacillus

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 299299Type-2 restriction enzyme BglIPRO_0000077285Add
BLAST

Structurei

Secondary structure

1
299
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Turni2 – 54Combined sources
Helixi6 – 2217Combined sources
Helixi24 – 4421Combined sources
Helixi46 – 5813Combined sources
Helixi60 – 634Combined sources
Beta strandi72 – 743Combined sources
Helixi83 – 897Combined sources
Helixi91 – 999Combined sources
Beta strandi105 – 1073Combined sources
Beta strandi116 – 1227Combined sources
Helixi124 – 1296Combined sources
Turni130 – 1323Combined sources
Beta strandi135 – 1439Combined sources
Beta strandi154 – 1574Combined sources
Helixi159 – 1613Combined sources
Beta strandi180 – 1834Combined sources
Beta strandi188 – 1914Combined sources
Beta strandi197 – 2004Combined sources
Beta strandi206 – 22015Combined sources
Helixi221 – 2233Combined sources
Beta strandi230 – 24011Combined sources
Helixi243 – 2475Combined sources
Helixi252 – 2543Combined sources
Helixi256 – 2583Combined sources
Beta strandi261 – 2644Combined sources
Beta strandi278 – 2814Combined sources
Helixi282 – 2854Combined sources
Beta strandi288 – 2903Combined sources
Beta strandi292 – 2965Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1DMUX-ray2.20A1-299[»]
ProteinModelPortaliO68557.
SMRiO68557. Positions 1-299.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiO68557.

Family & Domainsi

Family and domain databases

Gene3Di3.40.600.20. 1 hit.
InterProiIPR011335. Restrct_endonuc-II-like.
IPR011543. Restrct_endonuc_II_BglI.
[Graphical view]
SUPFAMiSSF52980. SSF52980. 1 hit.

Sequencei

Sequence statusi: Complete.

O68557-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MYNLHREKIF MSYNQNKQYL EDNPEIQEKI ELYGLNLLNE VISDNEEEIR
60 70 80 90 100
ADYNEANFLH PFWMNYPPLD RGKMPKGDQI PWIEVGEKAV GSKLTRLVSQ
110 120 130 140 150
REDITVREIG LPTGPDERYL LTSPTIYSLT NGFTDSIMMF VDIKSVGPRD
160 170 180 190 200
SDYDLVLSPN QVSGNGDWAQ LEGGIQNNQQ TIQGPRSSQI FLPTIPPLYI
210 220 230 240 250
LSDGTIAPVV HLFIKPIYAM RSLTKGDTGQ SLYKIKLASV PNGLGLFCNP
260 270 280 290
GYAFDSAYKF LFRPGKDDRT KSLLQKRVRV DLRVLDKIGP RVMTIDMDK
Length:299
Mass (Da):34,014
Last modified:August 1, 1998 - v1
Checksum:i40DF210E1173B02B
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF050216 Genomic DNA. Translation: AAC63973.1.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF050216 Genomic DNA. Translation: AAC63973.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1DMUX-ray2.20A1-299[»]
ProteinModelPortaliO68557.
SMRiO68557. Positions 1-299.
ModBaseiSearch...
MobiDBiSearch...

Protein family/group databases

REBASEi260. BglI.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Miscellaneous databases

EvolutionaryTraceiO68557.

Family and domain databases

Gene3Di3.40.600.20. 1 hit.
InterProiIPR011335. Restrct_endonuc-II-like.
IPR011543. Restrct_endonuc_II_BglI.
[Graphical view]
SUPFAMiSSF52980. SSF52980. 1 hit.
ProtoNetiSearch...

Publicationsi

  1. "Crystal structure of restriction endonuclease BGlI bound to its interrupted DNA recognition sequence."
    Newman M., Lunnen K.D., Wilson G.G., Greci J., Schildkraut I., Philips S.E.V.
    EMBO J. 17:5466-5476(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS).
    Strain: Globigii / RUB562.

Entry informationi

Entry nameiT2B1_BACIU
AccessioniPrimary (citable) accession number: O68557
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 11, 2002
Last sequence update: August 1, 1998
Last modified: May 27, 2015
This is version 69 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

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 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.