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P00640

- T2PS_PROST

UniProt

P00640 - T2PS_PROST

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Protein

Type-2 restriction enzyme PstI

Gene

pstIR

Organism
Providencia stuartii
Status
Reviewed - Annotation score: 3 out of 5- Protein inferred from homologyi

Functioni

Recognizes the double-stranded sequence CTGCAG and cleaves after A-5.

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. magnesium ion binding Source: InterPro
  3. 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

REBASEi1536. PstI.

Names & Taxonomyi

Protein namesi
Recommended name:
Type-2 restriction enzyme PstI (EC:3.1.21.4)
Short name:
R.PstI
Alternative name(s):
Endonuclease PstI
Type II restriction enzyme PstI
Gene namesi
Name:pstIR
OrganismiProvidencia stuartii
Taxonomic identifieri588 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeProvidencia

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 326326Type-2 restriction enzyme PstIPRO_0000077354Add
BLAST

Interactioni

Subunit structurei

Homodimer.

Structurei

3D structure databases

ProteinModelPortaliP00640.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Family and domain databases

InterProiIPR009528. Restrct_endonuc_II_BsuBI_C.
[Graphical view]
PfamiPF06616. BsuBI_PstI_RE. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P00640-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MKELKLKEAK EILKALGLPP QQYNDRSGWV LLALANIKPE DSWKEAKAPL
60 70 80 90 100
LPTVSIMEFI RTEYGKDYKP NSRETIRRQT LHQFEQARIV DRNRDLPSRA
110 120 130 140 150
TNSKDNNYSL NQVIIDILHN YPNGNWKELI QQFLTHVPSL QELYERALAR
160 170 180 190 200
DRIPIKLLDG TQISLSPGEH NQLHADIVHE FCPRFVGDMG KILYIGDTAS
210 220 230 240 250
SRNEGGKLMV LDSEYLKKLG VPPMSHDKLP DVVVYDEKRK WLFLIEAVTS
260 270 280 290 300
HGPISPKRWL ELEAALSSCT VGKVYVTAFP TRTEFRKNAA NIAWETEVWI
310 320
ADNPDHMVHF NGDRFLGPHD KKPELS
Length:326
Mass (Da):37,414
Last modified:July 21, 1986 - v1
Checksum:i475841183B414504
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
K02081 Genomic DNA. Translation: AAA25673.1.
PIRiA00783. NDOFS.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
K02081 Genomic DNA. Translation: AAA25673.1 .
PIRi A00783. NDOFS.

3D structure databases

ProteinModelPortali P00640.
ModBasei Search...
MobiDBi Search...

Chemistry

BindingDBi P00640.
ChEMBLi CHEMBL5713.

Protein family/group databases

REBASEi 1536. PstI.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Family and domain databases

InterProi IPR009528. Restrct_endonuc_II_BsuBI_C.
[Graphical view ]
Pfami PF06616. BsuBI_PstI_RE. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

  1. "The organization and complete nucleotide sequence of the PstI restriction-modification system."
    Walder R.Y., Walder J.A., Donelson J.E.
    J. Biol. Chem. 259:8015-8026(1984) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: 164.

Entry informationi

Entry nameiT2PS_PROST
AccessioniPrimary (citable) accession number: P00640
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: July 21, 1986
Last modified: October 1, 2014
This is version 73 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Documents

  1. Restriction enzymes and methylases
    Classification of restriction enzymes and methylases and list of entries
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3