P23657 (T2P2_PROHU) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Type-2 restriction enzyme PvuII
Short name=R.PvuII
EC=3.1.21.4

Alternative name(s):
Endonuclease PvuII
Type II restriction enzyme PvuII

Gene names

Name:

pvuIIR

Organism

Proteus hauseri

Taxonomic identifier

183417 [NCBI]

Taxonomic lineage

cellular organisms › Bacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › Proteus

Protein attributes

Sequence length	157 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Recognizes the double-stranded sequence CAGCTG and cleaves after G-3.
Catalytic activity	Endonucleolytic cleavage of DNA to give specific double-stranded fragments with terminal 5'-phosphates.
Cofactor	Binds 2 magnesium ions per subunit.
Subunit structure	Homodimer.

Ontologies

Keywords
Biological process	Restriction system
Ligand	Magnesium Metal-binding
Molecular function	Endonuclease Hydrolase Nuclease
Technical term	3D-structure
Gene Ontology (GO)
Biological_process	DNA restriction-modification system Inferred from electronic annotation. Source: UniProtKB-KW nucleic acid phosphodiester bond hydrolysis Inferred from electronic annotation. Source: GOC
Molecular_function	Type II site-specific deoxyribonuclease activity Inferred from electronic annotation. Source: EC metal ion binding Inferred from electronic annotation. Source: UniProtKB-KW
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 157

157

Type-2 restriction enzyme PvuII

PRO_0000077356

Sites

Metal binding

58

1

Magnesium 1 By similarity

Metal binding

58

1

Magnesium 2 By similarity

Metal binding

68

1

Magnesium 1 By similarity

Secondary structure

1

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

157

Helix Strand Turn

Details...

Helix

6 – 25

20

Turn

31 – 33

3

Helix

36 – 46

11

Beta strand

55 – 57

3

Beta strand

58 – 60

3

Beta strand

66 – 73

8

Turn

74 – 76

3

Beta strand

78 – 80

3

Beta strand

84 – 86

3

Helix

88 – 95

8

Beta strand

99 – 105

7

Beta strand

108 – 115

8

Helix

117 – 133

17

Helix

146 – 152

7

Beta strand

153 – 155

3

Sequences

	Sequence		Length	Mass (Da)
	P23657 [UniParc]. Last modified November 1, 1991. Version 1. Checksum: 2146453E04E65570	FASTA	157	18,345
	10 20 30 40 50 60 MSHPDLNKLL ELWPHIQEYQ DLALKHGIND IFQDNGGKLL QVLLITGLTV LPGREGNDAV 70 80 90 100 110 120 DNAGQEYELK SINIDLTKGF STHHHMNPVI IAKYRQVPWI FAIYRGIAIE AIYRLEPKDL 130 140 150 EFYYDKWERK WYSDGHKDIN NPKIPVKYVM EHGTKIY

References

[1]	"Complete nucleotide sequence of the PvuII restriction enzyme gene from Proteus vulgaris." Athanasiadis A., Gregoriu M., Thanos D., Kokkinidis M., Papamatheakis J. Nucleic Acids Res. 18:6434-6434(1990) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: ATCC 13315 / DSM 30118 / JCM 1668 / NBRC 3851 / NCIMB 4175 / NCTC 4175 / NRRL B-3405.
[2]	"Structure of PvuII endonuclease with cognate DNA." Cheng X., Balendiran K., Schildkraut I., Anderson J.E. EMBO J. 13:3927-3935(1994) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (3.0 ANGSTROMS).
[3]	"Crystal structure of PvuII endonuclease reveals extensive structural homologies to EcoRV." Athanasiadis A., Vlassi M., Kotsifaki D., Tucker P.A., Wilson K.S., Kokkinidis M. Nat. Struct. Biol. 1:469-475(1994) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS).
[4]	"How is modification of the DNA substrate recognized by the PvuII restriction endonuclease?" Horton J.R., Bonventre J., Cheng X. Biol. Chem. 379:451-458(1998) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (1.76 ANGSTROMS).
[5]	"Asp34 of PvuII endonuclease is directly involved in DNA minor groove recognition and indirectly involved in catalysis." Horton J.R., Nastri H.G., Riggs P.D., Cheng X. J. Mol. Biol. 284:1491-1504(1998) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (1.59 ANGSTROMS).
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

X52681 Genomic DNA. Translation: CAA36904.1.
AF305615 Genomic DNA. Translation: AAA96334.1.

PIR

S12163.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1EYU	X-ray	1.78	A/B	1-157	[»]
1F0O	X-ray	2.50	A/B	1-157	[»]
1H56	X-ray	3.00	A/B	2-157	[»]
1K0Z	X-ray	2.05	A/B	2-157	[»]
1NI0	X-ray	2.50	A/B/C	1-157	[»]
1PVI	X-ray	2.60	A/B	1-157	[»]
1PVU	X-ray	2.40	A/B	2-157	[»]
2PVI	X-ray	1.76	A/B	1-157	[»]
3KSK	X-ray	2.35	A/B	2-157	[»]
3PVI	X-ray	1.59	A/B	1-157	[»]

ProteinModelPortal

P23657.

SMR

P23657. Positions 2-157.

ModBase

Search...

Protein family/group databases

REBASE

1542. PvuII.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Phylogenomic databases

ProtClustDB

CLSK688103.

Family and domain databases

Gene3D

3.40.210.10. 1 hit.

InterPro

IPR011335. Restrct_endonuc-II-like.
IPR015306. Restrct_endonuc_II_PvuII.
[Graphical view]

Pfam

PF09225. Endonuc-PvuII. 1 hit.
[Graphical view]

SUPFAM

SSF52980. Restrict_endonuc_II-like_core. 1 hit.

ProtoNet

Search...

Other

EvolutionaryTrace

P23657.

Entry information

Entry name

T2P2_PROHU

Accession

Primary (citable) accession number: P23657

Entry history

Integrated into UniProtKB/Swiss-Prot:	November 1, 1991
Last sequence update:	November 1, 1991
Last modified:	April 3, 2013
This is version 86 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program