Amino acids
608
Annotations
9
Features
41
PDB binders
0
Druggability
0.299
Overview
Basic information about this protein and its source genome.
- Accession
- PA2585
- Gene
- PA2585 uvrC
- Status
- annotated
- Amino acids
- 608
- Structure source
- AlphaFold
GO
GO:0005737 The contents of a cell excluding the plasma membrane and nucleus, but including other subcellular structures.
GO:0009380 Any of the protein complexes formed by the UvrABC excinuclease system, which carries out nucleotide excision repair. Three different complexes are formed by the 3 proteins as they proceed through the excision repair process. First a complex consisting of two A subunits and two B subunits bind DNA and unwind it around the damaged site. Then, the A subunits disassociate leaving behind a stable complex between B subunits and DNA. Now, subunit C binds to this B+DNA complex and causes subunit B to nick the DNA on one side of the complex while subunit C nicks the DNA on the other side of the complex. DNA polymerase I and DNA ligase can then repair the resulting gap.
GO:0003677 Any molecular function by which a gene product interacts selectively and non-covalently with DNA (deoxyribonucleic acid).
GO:0009381 Catalysis of the hydrolysis of ester linkages within deoxyribonucleic acid at sites flanking regions of damaged DNA to which the Uvr ABC excinuclease complexes bind.
GO:0006974 Any process that results in a change in state or activity of a cell (in terms of movement, secretion, enzyme production, gene expression, etc.) as a result of a stimulus indicating damage to its DNA from environmental insults or errors during metabolism.
GO:0006289 A DNA repair process in which a small region of the strand surrounding the damage is removed from the DNA helix as an oligonucleotide. The small gap left in the DNA helix is filled in by the sequential action of DNA polymerase and DNA ligase. Nucleotide excision repair recognizes a wide range of substrates, including damage caused by UV irradiation (pyrimidine dimers and 6-4 photoproducts) and chemicals (intrastrand cross-links and bulky adducts).
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
0.299
Sequence
Primary amino-acid sequence viewer.
Functional Annotations
Enzyme classification and Gene Ontology terms linked to this protein.
9 GO
Gene Ontology (GO)
9- GO:0005737 The contents of a cell excluding the plasma membrane and nucleus, but including other subcellular structures.
- GO:0009380 Any of the protein complexes formed by the UvrABC excinuclease system, which carries out nucleotide excision repair. Three different complexes are formed by the 3 proteins as they proceed through the excision repair process. First a complex consisting of two A subunits and two B subunits bind DNA and unwind it around the damaged site. Then, the A subunits disassociate leaving behind a stable complex between B subunits and DNA. Now, subunit C binds to this B+DNA complex and causes subunit B to nick the DNA on one side of the complex while subunit C nicks the DNA on the other side of the complex. DNA polymerase I and DNA ligase can then repair the resulting gap.
- GO:0003677 Any molecular function by which a gene product interacts selectively and non-covalently with DNA (deoxyribonucleic acid).
- GO:0009381 Catalysis of the hydrolysis of ester linkages within deoxyribonucleic acid at sites flanking regions of damaged DNA to which the Uvr ABC excinuclease complexes bind.
- GO:0006974 Any process that results in a change in state or activity of a cell (in terms of movement, secretion, enzyme production, gene expression, etc.) as a result of a stimulus indicating damage to its DNA from environmental insults or errors during metabolism.
- GO:0006289 A DNA repair process in which a small region of the strand surrounding the damage is removed from the DNA helix as an oligonucleotide. The small gap left in the DNA helix is filled in by the sequential action of DNA polymerase and DNA ligase. Nucleotide excision repair recognizes a wide range of substrates, including damage caused by UV irradiation (pyrimidine dimers and 6-4 photoproducts) and chemicals (intrastrand cross-links and bulky adducts).
- GO:0009432 An error-prone process for repairing damaged microbial DNA.
- GO:0006281 The process of restoring DNA after damage. Genomes are subject to damage by chemical and physical agents in the environment (e.g. UV and ionizing radiations, chemical mutagens, fungal and bacterial toxins, etc.) and by free radicals or alkylating agents endogenously generated in metabolism. DNA is also damaged because of errors during its replication. A variety of different DNA repair pathways have been reported that include direct reversal, base excision repair, nucleotide excision repair, photoreactivation, bypass, double-strand break repair pathway, and mismatch repair pathway.
- GO:0005515 Binding to a protein.
Sequence Features
Domain/signature hits from InterPro and related databases.
41 records
Show feature table
| Start | End | DB | Term | Name |
|---|---|---|---|---|
| 377 | 546 | Gene3D | G3DSA:3.30.420.340 | UvrC, RNAse H endonuclease domain |
| 377 | 546 | InterPro | IPR038476 | UvrC, RNAse H endonuclease domain superfamily |
| 16 | 94 | CDD | cd10434 | GIY-YIG_UvrC_Cho |
| 16 | 94 | InterPro | IPR047296 | UvrC/Cho-like, GIY-YIG domain |
| 16 | 94 | ProSiteProfiles | PS50164 | GIY-YIG domain profile. |
| 16 | 94 | InterPro | IPR000305 | GIY-YIG endonuclease |
| 190 | 243 | SUPERFAMILY | SSF46600 | C-terminal UvrC-binding domain of UvrB |
| 190 | 243 | InterPro | IPR036876 | UVR domain superfamily |
| 547 | 606 | Gene3D | G3DSA:1.10.150.20 | - |
| 518 | 606 | SUPERFAMILY | SSF47781 | RuvA domain 2-like |
| 518 | 606 | InterPro | IPR010994 | RuvA domain 2-like |
| 6 | 102 | Gene3D | G3DSA:3.40.1440.10 | - |
| 6 | 102 | InterPro | IPR035901 | GIY-YIG endonuclease superfamily |
| 4 | 604 | Hamap | MF_00203 | UvrABC system protein C [uvrC]. |
| 4 | 604 | InterPro | IPR004791 | UvrABC system, subunit C |
| 553 | 572 | SMART | SM00278 | HhH1_4 |
| 553 | 572 | InterPro | IPR003583 | Helix-hairpin-helix DNA-binding motif, class 1 |
| 585 | 604 | SMART | SM00278 | HhH1_4 |
| 585 | 604 | InterPro | IPR003583 | Helix-hairpin-helix DNA-binding motif, class 1 |
| 5 | 604 | PANTHER | PTHR30562 | UVRC/OXIDOREDUCTASE |
| 204 | 239 | ProSiteProfiles | PS50151 | UVR domain profile. |
| 204 | 239 | InterPro | IPR001943 | UVR domain |
| 10 | 586 | NCBIfam | TIGR00194 | excinuclease ABC subunit UvrC |
| 10 | 586 | InterPro | IPR004791 | UvrABC system, subunit C |
| 16 | 100 | SUPERFAMILY | SSF82771 | GIY-YIG endonuclease |
| 16 | 100 | InterPro | IPR035901 | GIY-YIG endonuclease superfamily |
| 254 | 480 | ProSiteProfiles | PS50165 | UvrC family, homology region profile. |
| 254 | 480 | InterPro | IPR001162 | UvrC, RNAse H endonuclease domain |
| 555 | 603 | Pfam | PF14520 | Helix-hairpin-helix domain |
| 384 | 539 | Pfam | PF08459 | UvrC RNAse H endonuclease domain |
| 384 | 539 | InterPro | IPR001162 | UvrC, RNAse H endonuclease domain |
| 214 | 234 | Pfam | PF02151 | UvrB/uvrC motif |
| 214 | 234 | InterPro | IPR001943 | UVR domain |
| 17 | 98 | SMART | SM00465 | uri_9 |
| 17 | 98 | InterPro | IPR000305 | GIY-YIG endonuclease |
| 18 | 93 | Pfam | PF01541 | GIY-YIG catalytic domain |
| 18 | 93 | InterPro | IPR000305 | GIY-YIG endonuclease |
| 5 | 102 | FunFam | G3DSA:3.40.1440.10:FF:000001 | UvrABC system protein C |
| 197 | 240 | Gene3D | G3DSA:4.10.860.10 | UVR domain |
| 377 | 546 | FunFam | G3DSA:3.30.420.340:FF:000001 | UvrABC system protein C |
| 545 | 605 | FunFam | G3DSA:1.10.150.20:FF:000005 | UvrABC system protein C |
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 + 1Experimental PDB entries and predicted models. Click Switch to display a different structure in the viewer.
| Entry | Method | Resolution | Chain | Coverage | Links | Status |
|---|---|---|---|---|---|---|
|
AlphaFold
PA2585
|
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 |
|---|---|---|---|---|---|---|---|
| 4 | 0.299 | ||||||
| 21 | 0.221 |