Target Pathogen

Overview

Basic information about this protein and its source genome.

Accession: PA2734
Assembly: Pseudomonas aeruginosa PAO1, complete genome
Gene: PA2734
Status: annotated
Amino acids: 431
Structure source: AlphaFold

GO

GO:0019812 A multisubunit complex composed of two copies of a restriction (R) subunit, two copies of a methylation (M) subunit, and one copy of a specificity (S) subunit. This complex recognizes specific short DNA sequences (through the S subunit), and binds to them. If the recognition site is hemimethylated, the complex acts as a methyltransferase which modifies the recognition site, using S-adenosylmethionine as the methyl donor. Only the M and S subunits are required for this reaction. If the complex binds to an unmethylated recognition site, then the complex translocates the DNA bidirectionally in an ATP-dependent manner. When the translocation is stalled by impact with another complex or unusual DNA structure, the enzyme functions as an endonuclease and cleavage of the DNA will occur, hundreds or thousands of base pairs away from the recognition site. These DNA restriction systems are used by bacteria to defend against phage and other foreign DNA that may enter a cell. GO:0003677 Any molecular function by which a gene product interacts selectively and non-covalently with DNA (deoxyribonucleic acid). GO:0009307 A defense process found in many bacteria and archaea that protects the organism from invading foreign DNA by cleaving it with a restriction endonuclease. The organism's own DNA is protected by methylation of a specific nucleotide, which occurs immediately following replication, in the same target site as the restriction enzyme.

Target profile

Computed evidence for target prioritization.

Human off-target: No hit
Gut microbiome off-target: hit
Essential (DEG): N
Localization: Cytoplasmic

Selected Druggability evidence

Selected Druggability is the FPocket score chosen for ranking using the curated structure priority. The 3D viewer may show a different loaded structure, so its visible pockets can differ.

FPocket 0.682

Structure –

Pocket –

Sequence

Primary amino-acid sequence viewer.

MLRNGRLFGHRVETGFPDLPILEVSLRTGVRVRDMDNLKRKQVMSQKEKYKRAVKGDIAYNMMRMWQGAVGPVPEDGLVSPAYVVVKPYAEANSTYFSYLFRTAAYMQEVNKFSRGIVADRNRLYWESFKQMPSLVPPRPEQDQIVTYLRTQDAHIACFIRAKRDLIALLTEQKLRIIDHAVTRGLDASVKLKPSDIEWLGEVPAHWEVKRLKFLAGNITSQTTTKADDEIYLALEHVQSWTGVARPLGGEVEFASTVKRFVADDVLFGKLRPYLAKVTRVVCAGVCVSEFLVLRSRQELILPAYLEQLLRCKRVIDLISSSTAGAKMPRADWNFIGNVRLPIPRKDEQEAILSHIGRETKDLDETIARAEDEIKLIREYRDRLIADAVTGQVDLRGWQPGPDDVVSDDDLAALGDDDAGSSDDEEADAED

Functional Annotations

Enzyme classification and Gene Ontology terms linked to this protein.

3 GO

Gene Ontology (GO)

3

GO:0019812 A multisubunit complex composed of two copies of a restriction (R) subunit, two copies of a methylation (M) subunit, and one copy of a specificity (S) subunit. This complex recognizes specific short DNA sequences (through the S subunit), and binds to them. If the recognition site is hemimethylated, the complex acts as a methyltransferase which modifies the recognition site, using S-adenosylmethionine as the methyl donor. Only the M and S subunits are required for this reaction. If the complex binds to an unmethylated recognition site, then the complex translocates the DNA bidirectionally in an ATP-dependent manner. When the translocation is stalled by impact with another complex or unusual DNA structure, the enzyme functions as an endonuclease and cleavage of the DNA will occur, hundreds or thousands of base pairs away from the recognition site. These DNA restriction systems are used by bacteria to defend against phage and other foreign DNA that may enter a cell.
GO:0003677 Any molecular function by which a gene product interacts selectively and non-covalently with DNA (deoxyribonucleic acid).
GO:0009307 A defense process found in many bacteria and archaea that protects the organism from invading foreign DNA by cleaving it with a restriction endonuclease. The organism's own DNA is protected by methylation of a specific nucleotide, which occurs immediately following replication, in the same target site as the restriction enzyme.

Sequence Features

Domain/signature hits from InterPro and related databases.

11 records

Show feature table

Start	End	DB	Term	Name
190	401	SUPERFAMILY	SSF116734	DNA methylase specificity domain
34	188	SUPERFAMILY	SSF116734	DNA methylase specificity domain
409	431	MobiDBLite	mobidb-lite	consensus disorder prediction
30	174	CDD	cd16961	RMtype1_S_TRD-CR_like
397	431	MobiDBLite	mobidb-lite	consensus disorder prediction
367	387	Coils	Coil	Coil
190	392	Gene3D	G3DSA:3.90.220.20	DNA methylase specificity domains
190	392	InterPro	IPR044946	Type I restriction modification DNA specificity domain superfamily
3	185	Gene3D	G3DSA:3.90.220.20	DNA methylase specificity domains
3	185	InterPro	IPR044946	Type I restriction modification DNA specificity domain superfamily
25	398	PANTHER	PTHR43140	TYPE-1 RESTRICTION ENZYME ECOKI SPECIFICITY PROTEIN

3D Structure

Selected loaded structure. Experimental PDB entries may cover only a portion of the sequence; predicted models typically cover the full protein.

Loading 3D structure...

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Structural evidence

0 + 1

Experimental PDB entries and predicted models. Click Switch to display a different structure in the viewer.

Entry	Method	Resolution	Chain	Coverage	Links	Status
AlphaFold PA2734	AlphaFold	—	—	full sequence	—	Viewing

Pocket details FPocket · P2Rank — toggle visibility and zoom from here, or open full viewer

Pockets (FPOCKET)

Showing top-ranked FPocket candidates by druggability. Druggability is color-coded: high (0.7 or higher), medium (0.4 to 0.69), low (below 0.4).

FPOCKET	Sticks	Spheres	Surfaces	Druggability	Labels	Zoom	Positions
8				0.682
1				0.208

PA2734