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UniProtKB - P04390 (T2E5_ECOLX)

>sp|P04390|T2E5_ECOLX Type II restriction enzyme EcoRV OS=Escherichia coli OX=562 GN=ecoRVR PE=1 SV=3
MSLRSDLINALYDENQKYDVCGIISAEGKIYPLGSDTKVLSTIFELFSRPIINKIAEKHG
YIVEEPKQQNHYPDFTLYKPSEPNKKIAIDIKTTYTNKENEKIKFTLGGYTSFIRNNTKN
IVYPFDQYIAHWIIGYVYTRVATRKSSLKTYNINELNEIPKPYKGVKVFLQDKWVIAGDL
AGSGNTTNIGSIHAHYKDFVEGKGIFDSEDEFLDYWRNYERTSQLRNDKYNNISEYRNWI
YRGRK

Entry version 147 (23 Feb 2022)
Sequence version 3 (23 Jan 2007)
Previous versions | rss

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Protein

Type II restriction enzyme EcoRV

Gene

ecoRVR

Organism

Escherichia coli

Status

Reviewed-Annotation score: -Experimental evidence at protein levelⁱ

Functionⁱ

A P subtype restriction enzyme that recognizes the double-stranded sequence 5'-GATATC-3' and cleaves after T-3.

1 Publication3 Publications

Catalytic activityⁱ

Endonucleolytic cleavage of DNA to give specific double-stranded fragments with terminal 5'-phosphates.
2 Publications
Manual assertion based on experiment inⁱ
- Ref.2
  "The EcoRV restriction-modification system: genes, enzymes, synthetic substrates."
  Kraev A.S., Kravets A.N., Chernov B.K., Skryabin K.G., Baev A.A.
  Mol. Biol. (Mosk.) 19:236-242(1985)
  Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, CATALYTIC ACTIVITY.
- Ref.3
  "Site-directed mutagenesis studies with EcoRV restriction endonuclease to identify regions involved in recognition and catalysis."
  Thielking V., Selent U., Koehler E., Wolfes H., Pieper U., Geiger R., Urbanke C., Winkler F.K., Pingoud A.
  Biochemistry 30:6416-6422(1991) [PubMed] [Europe PMC] [Abstract]
  Cited for: FUNCTION, CATALYTIC ACTIVITY, SUBUNIT, MUTAGENESIS OF ASN-70; PRO-73; ASP-74; ASP-90; LYS-92; 183-SER--ASN-188; SER-183; ASN-185; THR-186; THR-187; ASN-188; GLY-190 AND 216-TRP--LYS-245.
EC:3.1.21.4

Cofactorⁱ

Mg²⁺Note: Binds 2 magnesium ions per subunit.

Sites

Feature key	Position(s)	DescriptionActions	Length
Metal bindingⁱ	45	Magnesium 2	1
Active siteⁱ	74		1
Metal bindingⁱ	74	Magnesium 1	1
Metal bindingⁱ	74	Magnesium 2	1
Active siteⁱ	90		1
Metal bindingⁱ	90	Magnesium 1	1
Active siteⁱ	92		1

GO - Molecular functionⁱ

DNA binding Source: InterPro
metal ion binding Source: UniProtKB-KW
type II site-specific deoxyribonuclease activity Source: UniProtKB-EC

Complete GO annotation on QuickGO ...

GO - Biological processⁱ

DNA restriction-modification system Source: UniProtKB-KW

Complete GO annotation on QuickGO ...

Keywordsⁱ

Molecular function	DNA-binding, Endonuclease, Hydrolase, Nuclease
Biological process	Restriction system
Ligand	Magnesium, Metal-binding

Names & Taxonomyⁱ

Protein namesⁱ	Recommended name: Type II restriction enzyme EcoRV1 Publication (EC:3.1.21.41 Publication) Short name: R.EcoRV Alternative name(s): Endonuclease EcoRV Type-2 restriction enzyme EcoRV
Gene namesⁱ	Name:ecoRVR
Encoded onⁱ	Plasmid pLB11 Publication Plasmid pLG131 Publication
Organismⁱ	Escherichia coli
Taxonomic identifierⁱ	562 [NCBI]
Taxonomic lineageⁱ	cellular organisms › Bacteria › Proteobacteria › Gammaproteobacteria › Enterobacterales › Enterobacteriaceae › Escherichia

Pathology & Biotechⁱ

Mutagenesis

Feature key	Position(s)	DescriptionActions	Length
Mutagenesisⁱ	70	N → Q: Decrease in activity. 1 Publication	1
Mutagenesisⁱ	73	P → A or G: Loss of activity. 1 Publication	1
Mutagenesisⁱ	74	D → A: Loss of activity. 1 Publication	1
Mutagenesisⁱ	74	D → E: Decrease in activity. 1 Publication	1
Mutagenesisⁱ	90	D → A, N, E or T: Loss of activity. 1 Publication	1
Mutagenesisⁱ	92	K → E: Loss of activity. 1 Publication	1
Mutagenesisⁱ	183 – 188	Missing : Weak, non-specific phosphodiesterase activity. 1 Publication	6
Mutagenesisⁱ	183	S → A or T: Decrease in activity. 1 Publication	1
Mutagenesisⁱ	183	S → I: Loss of activity. 1 Publication	1
Mutagenesisⁱ	185	N → D, A or Q: Loss of activity. 1 Publication	1
Mutagenesisⁱ	186	T → S or N: Loss of activity. 1 Publication	1
Mutagenesisⁱ	187	T → S or N: No loss of activity. 1 Publication	1
Mutagenesisⁱ	188	N → A, Q or T: Decrease in activity. 1 Publication	1
Mutagenesisⁱ	188	N → D: Loss of activity. 1 Publication	1
Mutagenesisⁱ	190	G → A: No loss of activity. 1 Publication	1
Mutagenesisⁱ	216 – 245	Missing : Loss of activity. 1 PublicationAdd BLAST	30

Chemistry databases

Drug and drug target database More...DrugBankⁱ	DB08651, 3'-THIO-THYMIDINE-5'-PHOSPHATE

DrugBankⁱ

DB08651, 3'-THIO-THYMIDINE-5'-PHOSPHATE

PTM / Processingⁱ

Molecule processing

Feature key	Position(s)	DescriptionActions	Graphical view	Length
Initiator methionineⁱ		Removed1 Publication
ChainⁱPRO_0000077305	2 – 245	Type II restriction enzyme EcoRVAdd BLAST		244

Interactionⁱ

Subunit structureⁱ

Homodimer.

1 Publication1 Publication

Structureⁱ

Secondary structure

Legend: HelixTurnBeta strandPDB Structure known for this area

Feature key	Position(s)	DescriptionActions	Length
Helixⁱ	3 – 17	Combined sources	15
Beta strandⁱ	20 – 25	Combined sources	6
Beta strandⁱ	30 – 32	Combined sources	3
Helixⁱ	37 – 58	Combined sources	22
Beta strandⁱ	62 – 64	Combined sources	3
Beta strandⁱ	67 – 70	Combined sources	4
Beta strandⁱ	74 – 78	Combined sources	5
Beta strandⁱ	86 – 98	Combined sources	13
Beta strandⁱ	106 – 112	Combined sources	7
Turnⁱ	113 – 115	Combined sources	3
Beta strandⁱ	116 – 118	Combined sources	3
Beta strandⁱ	119 – 123	Combined sources	5
Helixⁱ	125 – 127	Combined sources	3
Beta strandⁱ	128 – 140	Combined sources	13
Turnⁱ	145 – 148	Combined sources	4
Helixⁱ	153 – 158	Combined sources	6
Beta strandⁱ	162 – 172	Combined sources	11
Helixⁱ	173 – 176	Combined sources	4
Beta strandⁱ	177 – 183	Combined sources	7
Turnⁱ	184 – 187	Combined sources	4
Beta strandⁱ	188 – 191	Combined sources	4
Helixⁱ	196 – 201	Combined sources	6
Helixⁱ	209 – 217	Combined sources	9
Helixⁱ	223 – 226	Combined sources	4
Beta strandⁱ	227 – 229	Combined sources	3
Helixⁱ	233 – 241	Combined sources	9

Show more details

3D structure databases

SMRⁱ	P04390
ModBaseⁱ	Search...
PDBe-KBⁱ	Search...

Miscellaneous databases

EvolutionaryTraceⁱ

P04390

Family & Domainsⁱ

Family and domain databases

Gene3Dⁱ	3.40.600.10, 1 hit
InterProⁱ	View protein in InterPro IPR037057, DNA_rep_MutH/RE_typeII_sf IPR011335, Restrct_endonuc-II-like IPR015314, Restrct_endonuc_II_EcoRV IPR019755, Restrct_endonuc_II_EcoRV_Pbac
Pfam protein domain database More...Pfamⁱ	View protein in Pfam PF09233, Endonuc-EcoRV, 1 hit
PIRSFⁱ	PIRSF000995, RE_EcoRV, 1 hit
SUPFAMⁱ	SSF52980, SSF52980, 1 hit

Sequenceⁱ

Sequence statusⁱ: Complete.

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

P04390-1 [UniParc]FASTA Add 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

Sequence databases

Select the link destinations: EMBLⁱ GenBankⁱ DDBJⁱ Links Updated	X00530 Genomic DNA Translation: CAA25208.1 M19941 Genomic DNA Translation: AAA24615.1
PIRⁱ	A00784, NDECR5
NCBI Reference Sequences More...RefSeqⁱ	NP_863580.1, NC_005019.1 WP_011117659.1, NZ_VUDS01000061.1 YP_007316617.1, NC_019982.1

Protein	Similar proteins		Species	Score	Length	Source
P04390	Type-2 restriction enzyme EcoRV		Escherichia coli H20		245	UniRef100_P04390
REcoRV		ECOLX		245
REase protein (Fragment)		ECOLX		11
+2

Protein	Similar proteins		Species	Score	Length	Source
P04390	Type-2 restriction enzyme EcoRV		Escherichia coli H20		245	UniRef90_P04390
REcoRV		ECOLX		245
REase protein (Fragment)		ECOLX		11
+7

Protein	Similar proteins		Species	Score	Length	Source
P04390	Type-2 restriction enzyme EcoRV		Escherichia coli H20		245	UniRef50_P04390
REcoRV		ECOLX		245
Type II restriction enzyme EcoRV (Endonuclease EcoRV) (R.EcoRV)		THIA3		258
Restriction endonuclease		Flavobacterium sp. CLA17		249
Type II site-specific deoxyribonuclease		ZYMMT		247
+19

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
PIRⁱ	A00784, NDECR5
RefSeqⁱ	NP_863580.1, NC_005019.1 WP_011117659.1, NZ_VUDS01000061.1 YP_007316617.1, NC_019982.1

3D structure databases

Select the link destinations: Protein Data Bank Europe More...PDBeⁱ Protein Data Bank RCSB More...RCSB PDBⁱ Protein Data Bank Japan More...PDBjⁱ Links Updated	PDB entry	Method	Resolution (Å)	Chain	Positions	PDBsum
	1AZ0	X-ray	2.00	A/B	2-245	[»]
	1AZ3	X-ray	2.40	A/B	2-245	[»]
	1AZ4	X-ray	2.40	A/B	2-245	[»]
	1B94	X-ray	1.90	A/B	2-245	[»]
	1B95	X-ray	2.05	A/B	2-245	[»]
	1B96	X-ray	2.30	A/B	2-245	[»]
	1B97	X-ray	1.90	A/B	2-245	[»]
	1BGB	X-ray	2.00	A/B	2-245	[»]
	1BSS	X-ray	2.15	A/B	2-245	[»]
	1BSU	X-ray	2.00	A/B	2-245	[»]
	1BUA	X-ray	2.15	A/B	2-245	[»]
	1EO3	X-ray	2.00	A/B	1-245	[»]
	1EO4	X-ray	1.90	A/B	1-245	[»]
	1EON	X-ray	1.60	A/B	1-245	[»]
	1EOO	X-ray	2.16	A/B	1-245	[»]
	1EOP	X-ray	2.60	A/B	1-245	[»]
	1RV5	X-ray	2.10	A/B	2-245	[»]
	1RVA	X-ray	2.00	A/B	2-245	[»]
	1RVB	X-ray	2.10	A/B	2-245	[»]
	1RVC	X-ray	2.10	A/B	2-245	[»]
	1RVE	X-ray	2.50	A/B	1-245	[»]
	1STX	X-ray	2.10	A/B	2-245	[»]
	1SUZ	X-ray	1.80	A/B	2-245	[»]
	1SX5	X-ray	1.50	A/B	2-245	[»]
	1SX8	X-ray	2.15	A/B	2-245	[»]
	2B0D	X-ray	2.00	A/B	1-245	[»]
	2B0E	X-ray	1.90	A/B	1-245	[»]
	2GE5	X-ray	2.40	A/B	2-220	[»]
	2RVE	X-ray	3.00	A/B	2-245	[»]
	4RVE	X-ray	3.00	A/B/C	2-245	[»]
	5F8A	X-ray	1.76	A/B	2-245	[»]
	5HLK	X-ray	2.00	A/B	2-245	[»]
SMRⁱ	P04390
ModBaseⁱ	Search...
PDBe-KBⁱ	Search...

Chemistry databases

DrugBankⁱ	DB08651, 3'-THIO-THYMIDINE-5'-PHOSPHATE

DrugBankⁱ

DB08651, 3'-THIO-THYMIDINE-5'-PHOSPHATE

Miscellaneous databases

EvolutionaryTraceⁱ	P04390
Protein Ontology More...PROⁱ	PR:P04390

Family and domain databases

Gene3Dⁱ	3.40.600.10, 1 hit
InterProⁱ	View protein in InterPro IPR037057, DNA_rep_MutH/RE_typeII_sf IPR011335, Restrct_endonuc-II-like IPR015314, Restrct_endonuc_II_EcoRV IPR019755, Restrct_endonuc_II_EcoRV_Pbac
Pfamⁱ	View protein in Pfam PF09233, Endonuc-EcoRV, 1 hit
PIRSFⁱ	PIRSF000995, RE_EcoRV, 1 hit
SUPFAMⁱ	SSF52980, SSF52980, 1 hit
MobiDBⁱ	Search...

Entry informationⁱ

Entry nameⁱ	T2E5_ECOLX
Accessionⁱ	P04390Primary (citable) accession number: P04390
Entry historyⁱ	Integrated into UniProtKB/Swiss-Prot:	March 20, 1987
	Last sequence update:	January 23, 2007
	Last modified:	February 23, 2022
	This is version 147 of the entry and version 3 of the sequence. See complete history.
Entry statusⁱ	Reviewed (UniProtKB/Swiss-Prot)
Annotation program	Prokaryotic Protein Annotation Program

Miscellaneousⁱ

Keywords - Technical termⁱ

3D-structure, Direct protein sequencing, Plasmid

Documents

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

UniProtKB - P04390 (T2E5_ECOLX)

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Type II restriction enzyme EcoRV

ecoRVR

Select a section on the left to see content.

Functionⁱ

Catalytic activityⁱ

Cofactorⁱ

Sites

GO - Molecular functionⁱ

GO - Biological processⁱ

Keywordsⁱ

Names & Taxonomyⁱ

Pathology & Biotechⁱ

Mutagenesis

Chemistry databases

PTM / Processingⁱ

Molecule processing

Interactionⁱ

Subunit structureⁱ

Structureⁱ

Secondary structure

3D structure databases

Miscellaneous databases

Family & Domainsⁱ

Family and domain databases

Sequenceⁱ

Sequence databases

Similar proteinsⁱ

Cross-referencesⁱ

Sequence databases

3D structure databases

Chemistry databases

Miscellaneous databases

Family and domain databases

Entry informationⁱ

Miscellaneousⁱ

Keywords - Technical termⁱ

Documents

UniProt is an ELIXIR core data resource

UniProtKB

UniParc

Help

UniRef

Proteomes

Annotation systems

Supporting data

UniProtKB - P04390 (T2E5_ECOLX)

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Type II restriction enzyme EcoRV

ecoRVR

Select a section on the left to see content.

<p>This section provides any useful information about the protein, mostly biological knowledge.<p><a href='/help/function_section' target='_top'>More...</a></p>Functioni

<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> section describes the catalytic activity of an enzyme, i.e. a chemical reaction that the enzyme catalyzes.<p><a href='/help/catalytic_activity' target='_top'>More...</a></p>Catalytic activityi

Sites

<p>The <a href="http://www.geneontology.org/">Gene Ontology (GO)</a> project provides a set of hierarchical controlled vocabulary split into 3 categories:<p><a href='/help/gene_ontology' target='_top'>More...</a></p>GO - Molecular functioni

GO - Biological processi

<p>This section provides information about the protein and gene name(s) and synonym(s) and about the organism that is the source of the protein sequence.<p><a href='/help/names_and_taxonomy_section' target='_top'>More...</a></p>Names & Taxonomyi

<p>This section provides information on the disease(s) and phenotype(s) associated with a protein.<p><a href='/help/pathology_and_biotech_section' target='_top'>More...</a></p>Pathology & Biotechi

Mutagenesis

Chemistry databases

<p>This section describes post-translational modifications (PTMs) and/or processing events.<p><a href='/help/ptm_processing_section' target='_top'>More...</a></p>PTM / Processingi

Molecule processing

<p>This section provides information on the quaternary structure of a protein and on interaction(s) with other proteins or protein complexes.<p><a href='/help/interaction_section' target='_top'>More...</a></p>Interactioni

<p>This section provides information on the tertiary and secondary structure of a protein.<p><a href='/help/structure_section' target='_top'>More...</a></p>Structurei

Secondary structure

3D structure databases

Miscellaneous databases

<p>This section provides information on sequence similarities with other proteins and the domain(s) present in a protein.<p><a href='/help/family_and_domains_section' target='_top'>More...</a></p>Family & Domainsi

Family and domain databases

Sequence databases

<p>This section is used to point to information related to entries and found in data collections other than UniProtKB.<p><a href='/help/cross_references_section' target='_top'>More...</a></p>Cross-referencesi

Sequence databases

3D structure databases

Chemistry databases

Miscellaneous databases

Family and domain databases

<p>This section provides general information on the entry.<p><a href='/help/entry_information_section' target='_top'>More...</a></p>Entry informationi

<p>This section contains any relevant information that doesn't fit in any other defined sections<p><a href='/help/miscellaneous_section' target='_top'>More...</a></p>Miscellaneousi

Keywords - Technical termi

Documents

UniProt is an ELIXIR core data resource

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Functionⁱ

Catalytic activityⁱ

GO - Molecular functionⁱ

GO - Biological processⁱ

Names & Taxonomyⁱ

Pathology & Biotechⁱ

PTM / Processingⁱ

Interactionⁱ

Structureⁱ

Family & Domainsⁱ

Cross-referencesⁱ

Entry informationⁱ

Miscellaneousⁱ

Keywords - Technical termⁱ