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Protein

Type-2 restriction enzyme EcoRV

Gene

ecoRVR

Organism
Escherichia coli
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Recognizes the double-stranded sequence GATATC and cleaves after T-3.

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)DescriptionActionsGraphical viewLength
Metal bindingi45Magnesium 21
Active sitei741
Metal bindingi74Magnesium 11
Metal bindingi74Magnesium 21
Active sitei901
Metal bindingi90Magnesium 11
Active sitei921

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

REBASEi995. EcoRV.

Names & Taxonomyi

Protein namesi
Recommended name:
Type-2 restriction enzyme EcoRV (EC:3.1.21.4)
Short name:
R.EcoRV
Alternative name(s):
Endonuclease EcoRV
Type II restriction enzyme EcoRV
Gene namesi
Name:ecoRVR
OrganismiEscherichia coli
Taxonomic identifieri562 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacteralesEnterobacteriaceaeEscherichia

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi70N → Q: Decrease in activity. 1 Publication1
Mutagenesisi73P → A or G: Loss of activity. 1 Publication1
Mutagenesisi74D → A: Loss of activity. 1 Publication1
Mutagenesisi74D → E: Decrease in activity. 1 Publication1
Mutagenesisi90D → A, N, E or T: Loss of activity. 1 Publication1
Mutagenesisi183S → A or T: Decrease in activity. 1 Publication1
Mutagenesisi183S → I: Loss of activity. 1 Publication1
Mutagenesisi185N → D, A or Q: Loss of activity. 1 Publication1
Mutagenesisi186T → S or N: Loss of activity. 1 Publication1
Mutagenesisi187T → S or N: No loss of activity. 1 Publication1
Mutagenesisi188N → A, Q or T: Decrease in activity. 1 Publication1
Mutagenesisi188N → D: Loss of activity. 1 Publication1
Mutagenesisi190G → A: No loss of activity. 1 Publication1

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Initiator methionineiRemoved
ChainiPRO_00000773052 – 245Type-2 restriction enzyme EcoRVAdd BLAST244

Proteomic databases

PRIDEiP04390.

Interactioni

Subunit structurei

Homodimer.

Structurei

Secondary structure

1245
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi3 – 17Combined sources15
Beta strandi20 – 25Combined sources6
Beta strandi30 – 32Combined sources3
Helixi37 – 58Combined sources22
Beta strandi62 – 64Combined sources3
Beta strandi67 – 70Combined sources4
Beta strandi74 – 78Combined sources5
Beta strandi86 – 98Combined sources13
Beta strandi106 – 112Combined sources7
Turni113 – 115Combined sources3
Beta strandi116 – 118Combined sources3
Beta strandi119 – 123Combined sources5
Helixi125 – 127Combined sources3
Beta strandi128 – 140Combined sources13
Turni145 – 148Combined sources4
Helixi153 – 158Combined sources6
Beta strandi162 – 172Combined sources11
Helixi173 – 176Combined sources4
Beta strandi177 – 183Combined sources7
Turni184 – 187Combined sources4
Beta strandi188 – 191Combined sources4
Helixi196 – 201Combined sources6
Helixi209 – 217Combined sources9
Helixi223 – 226Combined sources4
Beta strandi227 – 229Combined sources3
Helixi233 – 241Combined sources9

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1AZ0X-ray2.00A/B2-245[»]
1AZ3X-ray2.40A/B2-245[»]
1AZ4X-ray2.40A/B2-245[»]
1B94X-ray1.90A/B2-245[»]
1B95X-ray2.05A/B2-245[»]
1B96X-ray2.30A/B2-245[»]
1B97X-ray1.90A/B2-245[»]
1BGBX-ray2.00A/B2-245[»]
1BSSX-ray2.15A/B2-245[»]
1BSUX-ray2.00A/B2-245[»]
1BUAX-ray2.15A/B2-245[»]
1EO3X-ray2.00A/B1-245[»]
1EO4X-ray1.90A/B1-245[»]
1EONX-ray1.60A/B1-245[»]
1EOOX-ray2.16A/B1-245[»]
1EOPX-ray2.60A/B1-245[»]
1RV5X-ray2.10A/B2-245[»]
1RVAX-ray2.00A/B2-245[»]
1RVBX-ray2.10A/B2-245[»]
1RVCX-ray2.10A/B2-245[»]
1RVEX-ray2.50A/B1-245[»]
1STXX-ray2.10A/B2-245[»]
1SUZX-ray1.80A/B2-245[»]
1SX5X-ray1.50A/B2-245[»]
1SX8X-ray2.15A/B2-245[»]
2B0DX-ray2.00A/B1-245[»]
2B0EX-ray1.90A/B1-245[»]
2GE5X-ray2.40A/B2-220[»]
2RVEX-ray3.00A/B2-245[»]
4ORJX-ray2.10A/B2-245[»]
4RVEX-ray3.00A/B/C2-245[»]
ProteinModelPortaliP04390.
SMRiP04390.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP04390.

Family & Domainsi

Family and domain databases

Gene3Di3.40.600.10. 1 hit.
InterProiIPR011337. DNA_rep_MutH/RE_typeII.
IPR011335. Restrct_endonuc-II-like.
IPR015314. Restrct_endonuc_II_EcoRV.
IPR019755. Restrct_endonuc_II_EcoRV_Pbac.
[Graphical view]
PfamiPF09233. Endonuc-EcoRV. 1 hit.
[Graphical view]
PIRSFiPIRSF000995. RE_EcoRV. 1 hit.
SUPFAMiSSF52980. SSF52980. 1 hit.

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P04390-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSLRSDLINA LYDENQKYDV CGIISAEGKI YPLGSDTKVL STIFELFSRP
60 70 80 90 100
IINKIAEKHG YIVEEPKQQN HYPDFTLYKP SEPNKKIAID IKTTYTNKEN
110 120 130 140 150
EKIKFTLGGY TSFIRNNTKN IVYPFDQYIA HWIIGYVYTR VATRKSSLKT
160 170 180 190 200
YNINELNEIP KPYKGVKVFL QDKWVIAGDL AGSGNTTNIG SIHAHYKDFV
210 220 230 240
EGKGIFDSED EFLDYWRNYE RTSQLRNDKY NNISEYRNWI YRGRK
Length:245
Mass (Da):28,650
Last modified:January 23, 2007 - v3
Checksum:i7DB7EC640A746281
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X00530 Genomic DNA. Translation: CAA25208.1.
M19941 Genomic DNA. Translation: AAA24615.1.
PIRiA00784. NDECR5.
RefSeqiNP_863580.1. NC_005019.1.
WP_011117659.1. NC_019982.1.
YP_007316617.1. NC_019982.1.

Genome annotation databases

GeneIDi14401263.
1446621.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X00530 Genomic DNA. Translation: CAA25208.1.
M19941 Genomic DNA. Translation: AAA24615.1.
PIRiA00784. NDECR5.
RefSeqiNP_863580.1. NC_005019.1.
WP_011117659.1. NC_019982.1.
YP_007316617.1. NC_019982.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1AZ0X-ray2.00A/B2-245[»]
1AZ3X-ray2.40A/B2-245[»]
1AZ4X-ray2.40A/B2-245[»]
1B94X-ray1.90A/B2-245[»]
1B95X-ray2.05A/B2-245[»]
1B96X-ray2.30A/B2-245[»]
1B97X-ray1.90A/B2-245[»]
1BGBX-ray2.00A/B2-245[»]
1BSSX-ray2.15A/B2-245[»]
1BSUX-ray2.00A/B2-245[»]
1BUAX-ray2.15A/B2-245[»]
1EO3X-ray2.00A/B1-245[»]
1EO4X-ray1.90A/B1-245[»]
1EONX-ray1.60A/B1-245[»]
1EOOX-ray2.16A/B1-245[»]
1EOPX-ray2.60A/B1-245[»]
1RV5X-ray2.10A/B2-245[»]
1RVAX-ray2.00A/B2-245[»]
1RVBX-ray2.10A/B2-245[»]
1RVCX-ray2.10A/B2-245[»]
1RVEX-ray2.50A/B1-245[»]
1STXX-ray2.10A/B2-245[»]
1SUZX-ray1.80A/B2-245[»]
1SX5X-ray1.50A/B2-245[»]
1SX8X-ray2.15A/B2-245[»]
2B0DX-ray2.00A/B1-245[»]
2B0EX-ray1.90A/B1-245[»]
2GE5X-ray2.40A/B2-220[»]
2RVEX-ray3.00A/B2-245[»]
4ORJX-ray2.10A/B2-245[»]
4RVEX-ray3.00A/B/C2-245[»]
ProteinModelPortaliP04390.
SMRiP04390.
ModBaseiSearch...
MobiDBiSearch...

Protein family/group databases

REBASEi995. EcoRV.

Proteomic databases

PRIDEiP04390.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

GeneIDi14401263.
1446621.

Miscellaneous databases

EvolutionaryTraceiP04390.

Family and domain databases

Gene3Di3.40.600.10. 1 hit.
InterProiIPR011337. DNA_rep_MutH/RE_typeII.
IPR011335. Restrct_endonuc-II-like.
IPR015314. Restrct_endonuc_II_EcoRV.
IPR019755. Restrct_endonuc_II_EcoRV_Pbac.
[Graphical view]
PfamiPF09233. Endonuc-EcoRV. 1 hit.
[Graphical view]
PIRSFiPIRSF000995. RE_EcoRV. 1 hit.
SUPFAMiSSF52980. SSF52980. 1 hit.
ProtoNetiSearch...

Entry informationi

Entry nameiT2E5_ECOLX
AccessioniPrimary (citable) accession number: P04390
Entry historyi
Integrated into UniProtKB/Swiss-Prot: March 20, 1987
Last sequence update: January 23, 2007
Last modified: November 30, 2016
This is version 128 of the entry and version 3 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.