Protein profile

PA5050

primosome assembly protein PriA

Genome: NC_002516.2

Gene: PA5050 priA Structure source: AlphaFold UniProt Q9HUC9
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Amino acids 739
Annotations 15
Features 37
PDB binders 1
Druggability 0.595

Overview

Basic information about this protein and its source genome.

Accession
PA5050
Assembly
Pseudomonas aeruginosa PAO1, complete genome
Gene
PA5050 priA
Status
annotated
Amino acids
739
Structure source
AlphaFold
EC
5.6.2.4
GO
GO:1990077 Any of a family of protein complexes that form at the origin of replication or stalled replication forks and function in replication primer synthesis in all organisms. Early complexes initiate double-stranded DNA unwinding. The core unit consists of a replicative helicase and a primase. The helicase further unwinds the DNA and recruits the polymerase machinery. The primase synthesizes RNA primers that act as templates for complementary stand replication by the polymerase machinery. The primosome contains a number of associated proteins and protein complexes and contributes to the processes of replication initiation, lagging strand elongation, and replication restart. GO:0043138 Unwinding a DNA helix in the direction 5' to 3', driven by ATP hydrolysis. GO:0005524 Binding to ATP, adenosine 5'-triphosphate, a universally important coenzyme and enzyme regulator. GO:0016887 Catalysis of the reaction: ATP + H2O = ADP + H+ phosphate. ATP hydrolysis is used in some reactions as an energy source, for example to catalyze a reaction or drive transport against a concentration gradient. GO:0003677 Any molecular function by which a gene product interacts selectively and non-covalently with DNA (deoxyribonucleic acid). GO:0008270 Binding to a zinc ion (Zn).

Target profile

Computed evidence for target prioritization.

Human off-target
No hit
Gut microbiome off-target
hit
Essential (DEG)
Y
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 0.595
Structure –
Pocket –

Sequence

Primary amino-acid sequence viewer.

Functional Annotations

Enzyme classification and Gene Ontology terms linked to this protein.

1 EC 14 GO

Enzyme Commission (EC)

1

Gene Ontology (GO)

14
  • GO:1990077 Any of a family of protein complexes that form at the origin of replication or stalled replication forks and function in replication primer synthesis in all organisms. Early complexes initiate double-stranded DNA unwinding. The core unit consists of a replicative helicase and a primase. The helicase further unwinds the DNA and recruits the polymerase machinery. The primase synthesizes RNA primers that act as templates for complementary stand replication by the polymerase machinery. The primosome contains a number of associated proteins and protein complexes and contributes to the processes of replication initiation, lagging strand elongation, and replication restart.
  • GO:0043138 Unwinding a DNA helix in the direction 5' to 3', driven by ATP hydrolysis.
  • GO:0005524 Binding to ATP, adenosine 5'-triphosphate, a universally important coenzyme and enzyme regulator.
  • GO:0016887 Catalysis of the reaction: ATP + H2O = ADP + H+ phosphate. ATP hydrolysis is used in some reactions as an energy source, for example to catalyze a reaction or drive transport against a concentration gradient.
  • GO:0003677 Any molecular function by which a gene product interacts selectively and non-covalently with DNA (deoxyribonucleic acid).
  • GO:0008270 Binding to a zinc ion (Zn).
  • GO:0006310 Any process in which a new genotype is formed by reassortment of genes resulting in gene combinations different from those that were present in the parents. In eukaryotes genetic recombination can occur by chromosome assortment, intrachromosomal recombination, or nonreciprocal interchromosomal recombination. Interchromosomal recombination occurs by crossing over. In bacteria it may occur by genetic transformation, conjugation, transduction, or F-duction.
  • GO:0006270 The process in which DNA-dependent DNA replication is started; it begins when specific sequences, known as origins of replication, are recognized and bound by the origin recognition complex, followed by DNA unwinding.
  • GO:0006269 The synthesis of a short nucleotide polymer using one strand of unwound DNA as a template. The product is usually a RNA molecule between 4-15 nucleotides long that provides a free 3'-OH that can be extended by DNA-directed DNA polymerases. In certain conditions, for example in response to DNA damage, some primases synthesize a DNA primer.
  • GO:0006302 The repair of double-strand breaks in DNA via homologous and nonhomologous mechanisms to reform a continuous DNA helix.
  • GO:0003678 Unwinding of a DNA helix, driven by ATP hydrolysis.
  • GO:0003676 Binding to a nucleic acid.
  • GO:0006260 The cellular metabolic process in which a cell duplicates one or more molecules of DNA. DNA replication begins when specific sequences, known as origins of replication, are recognized and bound by the origin recognition complex, and ends when the original DNA molecule has been completely duplicated and the copies topologically separated. The unit of replication usually corresponds to the genome of the cell, an organelle, or a virus. The template for replication can either be an existing DNA molecule or RNA.
  • GO:0032508 OBSOLETE. The process in which interchain hydrogen bonds between two strands of DNA are broken or 'melted', generating a region of unpaired single strands.

Sequence Features

Domain/signature hits from InterPro and related databases.

37 records
Show feature table
Start End DB Term Name
4 117 Gene3D G3DSA:3.40.1440.60 -
4 117 InterPro IPR042115 Primosomal protein N', 3' DNA-binding domain superfamily
392 642 Gene3D G3DSA:3.40.50.300 -
392 642 InterPro IPR027417 P-loop containing nucleoside triphosphate hydrolase
215 381 ProSiteProfiles PS51192 Superfamilies 1 and 2 helicase ATP-binding type-1 domain profile.
215 381 InterPro IPR014001 Helicase superfamily 1/2, ATP-binding domain
207 384 CDD cd17929 DEXHc_priA
410 632 ProSiteProfiles PS51194 Superfamilies 1 and 2 helicase C-terminal domain profile.
410 632 InterPro IPR001650 Helicase, C-terminal
5 115 FunFam G3DSA:3.40.1440.60:FF:000001 Primosomal protein N
413 616 SUPERFAMILY SSF52540 P-loop containing nucleoside triphosphate hydrolases
413 616 InterPro IPR027417 P-loop containing nucleoside triphosphate hydrolase
5 738 PANTHER PTHR30580 PRIMOSOMAL PROTEIN N
199 395 SMART SM00487 ultradead3
199 395 InterPro IPR014001 Helicase superfamily 1/2, ATP-binding domain
207 367 Pfam PF00270 DEAD/DEAH box helicase
207 367 InterPro IPR011545 DEAD/DEAH box helicase domain
522 592 Pfam PF00271 Helicase conserved C-terminal domain
522 592 InterPro IPR001650 Helicase, C-terminal
225 736 NCBIfam TIGR00595 primosomal protein N'
225 736 InterPro IPR005259 Primosomal protein N'
194 383 Gene3D G3DSA:3.40.50.300 -
194 383 InterPro IPR027417 P-loop containing nucleoside triphosphate hydrolase
496 593 SMART SM00490 helicmild6
496 593 InterPro IPR001650 Helicase, C-terminal
175 383 SUPERFAMILY SSF52540 P-loop containing nucleoside triphosphate hydrolases
175 383 InterPro IPR027417 P-loop containing nucleoside triphosphate hydrolase
449 475 Pfam PF18319 PriA DNA helicase Cys-rich region (CRR) domain
449 475 InterPro IPR040498 PriA DNA helicase, Cys-rich region (CRR) domain
193 383 FunFam G3DSA:3.40.50.300:FF:000489 Primosome assembly protein PriA
396 630 CDD cd18804 SF2_C_priA
8 738 Hamap MF_00983 Probable primosomal protein N' [priA].
8 738 InterPro IPR005259 Primosomal protein N'
9 105 Pfam PF17764 3'DNA-binding domain (3'BD)
9 105 InterPro IPR041222 Primosomal protein N', 3' DNA-binding domain
636 735 Pfam PF18074 Primosomal protein N C-terminal domain
636 735 InterPro IPR041236 Primosomal protein N, C-terminal domain

3D Structure

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

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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 PA5050
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 0.595
7 0.288

Ligand evidence

Ligands grouped by evidence source. PDB ligands keep the source crystal visible, and loaded crystals can be opened directly in the structure viewer.

51 records

Structural evidence inferred from similar proteins. The source crystal indicates where the ligand was observed; the UniProt column identifies the homologous protein carrying that ligand.

Show only:
Ligand Source crystal UniProt (homolog) MW · LogP · TPSA Lipinski PAINS SMILES
AGS
6M6B
Q72KB4 523.2 Da LogP -1.51 TPSA 262.1 3 viol. ✓ Clean c1nc(c2c(n1)n(cn2)[C@H]3[C@@H]([C@@H]([C@H](O3)…

PDB and ChEMBL records on this protein are shown in full. ChEMBL records from similar proteins are capped at the top 100 per protein (by pchembl) and ZINC at the top 50 (Tanimoto ≥ 0.5). ADME columns are descriptor-based screening flags, not experimental toxicity results.