Target Pathogen

Overview

Basic information about this protein and its source genome.

Accession: PA3909
Assembly: Pseudomonas aeruginosa PAO1, complete genome
Gene: eddB PA3909
Status: annotated
Amino acids: 779
Structure source: AlphaFold

GO

GO:0004536 Catalysis of the cleavage of ester linkages within deoxyribonucleic acid. GO:0006308 The cellular DNA metabolic process resulting in the breakdown of DNA, deoxyribonucleic acid, one of the two main types of nucleic acid, consisting of a long unbranched macromolecule formed from one or two strands of linked deoxyribonucleotides, the 3'-phosphate group of each constituent deoxyribonucleotide being joined in 3',5'-phosphodiester linkage to the 5'-hydroxyl group of the deoxyribose moiety of the next one. GO:0003824 Catalysis of a biochemical reaction at physiological temperatures. In biologically catalyzed reactions, the reactants are known as substrates, and the catalysts are naturally occurring macromolecular substances known as enzymes. Enzymes possess specific binding sites for substrates, and are usually composed wholly or largely of protein, but RNA that has catalytic activity (ribozyme) is often also regarded as enzymatic.

Target profile

Computed evidence for target prioritization.

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

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 0.756

Structure –

Pocket –

Sequence

Primary amino-acid sequence viewer.

MHPLRNAALLGGLALLGLPVANAAELIISEYVEGSGNNKALEFYNSGSQVLDLSAYRVEFYFNGASAAGRSIDLSGSLAPGKTFVLANGVADPALLALASQRVEGSWFNGNDAVLLRRRGGEILDSLGQVGFNPGTTWGSGDVQTLDRSLVRKADIRDGDSDPSDAFDPAAQWLGYPRDTFANLGQHGAGEPGGEEAGLRPIHEVQGAGAESPLVNQRVAIEGVVVGDFQNASELKGFYVQQEDATVDGDPATSEGIFVYDGGNGSDVKLGDRVRVTGQVREFNGLTELVGPLQVSVLASGVALPTPAGISLPLASADALERYEGMRVQLRQTLTVNEVYNLGRYGEVLLSSGGRQMTPTNVVAPGEQAKAMQARNDLDRILLDDGRSGQNPDPIRYPAPELSAYNSLRVGDRTSAIDGVLDYSAGSYRIQPLQTPTFEAANPRPAQPAVEGRLRVASFNVLNYFNGDGKGGGFPTSRGANTAEEFQRQKAKIVAAILASKADIVGLMEIENDGYGEFSAIADLVNGLNASLPQGQRYAFVNPNRAKLGSDEIAVGLIYRGDKVRTYRSAAVLDSSVNPEFDDTRNRPTLAQTFQEINGGERLTIAVNHLKSKGSACDGDPDTGDGQGNCNLTRARAAQALVGWLAGDPTGAKEPDRLIIGDLNSYAKEDPVNVIRSAGYTDLVARQAGAGKGYSYVFSGQSGYLDHALANASLARQVRGAVEWHINADEPRVLDYNVEFKTPRQQDSLYNAEPYRASDHDPVVIGIDLRRVAMKKHRR

Functional Annotations

Enzyme classification and Gene Ontology terms linked to this protein.

3 GO

Gene Ontology (GO)

3

GO:0004536 Catalysis of the cleavage of ester linkages within deoxyribonucleic acid.
GO:0006308 The cellular DNA metabolic process resulting in the breakdown of DNA, deoxyribonucleic acid, one of the two main types of nucleic acid, consisting of a long unbranched macromolecule formed from one or two strands of linked deoxyribonucleotides, the 3'-phosphate group of each constituent deoxyribonucleotide being joined in 3',5'-phosphodiester linkage to the 5'-hydroxyl group of the deoxyribose moiety of the next one.
GO:0003824 Catalysis of a biochemical reaction at physiological temperatures. In biologically catalyzed reactions, the reactants are known as substrates, and the catalysts are naturally occurring macromolecular substances known as enzymes. Enzymes possess specific binding sites for substrates, and are usually composed wholly or largely of protein, but RNA that has catalytic activity (ribozyme) is often also regarded as enzymatic.

Sequence Features

Domain/signature hits from InterPro and related databases.

22 records

Show feature table

Start	End	DB	Term	Name
24	779	Phobius	NON_CYTOPLASMIC_DOMAIN	Region of a membrane-bound protein predicted to be outside the membrane, in the extracellular region.
19	131	ProSiteProfiles	PS51841	Lamin-tail (LTD) domain profile.
19	131	InterPro	IPR001322	Lamin tail domain
195	769	PANTHER	PTHR42834	ENDONUCLEASE/EXONUCLEASE/PHOSPHATASE FAMILY PROTEIN (AFU_ORTHOLOGUE AFUA_3G09210)
454	767	CDD	cd10283	MnuA_DNase1-like
221	301	CDD	cd04486	YhcR_OBF_like
21	129	Pfam	PF00932	Lamin Tail Domain
21	129	InterPro	IPR001322	Lamin tail domain
1	23	SignalP_GRAM_NEGATIVE	SignalP-noTM	SignalP-noTM
454	767	FunFam	G3DSA:3.60.10.10:FF:000072	Extracellular nuclease
454	767	Gene3D	G3DSA:3.60.10.10	Endonuclease/exonuclease/phosphatase
454	767	InterPro	IPR036691	Endonuclease/exonuclease/phosphatase superfamily
1	23	SignalP_GRAM_POSITIVE	SignalP-TM	SignalP-TM
457	760	Pfam	PF03372	Endonuclease/Exonuclease/phosphatase family
457	760	InterPro	IPR005135	Endonuclease/exonuclease/phosphatase
221	769	NCBIfam	NF033681	ExeM/NucH family extracellular endonuclease
1	6	Phobius	SIGNAL_PEPTIDE_N_REGION	N-terminal region of a signal peptide.
1	23	Phobius	SIGNAL_PEPTIDE	Signal peptide region
7	18	Phobius	SIGNAL_PEPTIDE_H_REGION	Hydrophobic region of a signal peptide.
452	768	SUPERFAMILY	SSF56219	DNase I-like
452	768	InterPro	IPR036691	Endonuclease/exonuclease/phosphatase superfamily
19	23	Phobius	SIGNAL_PEPTIDE_C_REGION	C-terminal region of a signal peptide.

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 PA3909	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
1				0.756

PA3909