Protein profile

KP13_01656

UvrABC system protein C

Genome: KpKP13

Gene: AHE43822.1 uvrC Structure source: AlphaFold + ColabFold UniProt A0A0H3GQ96

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Amino acids 610

Annotations 8

Features 43

PDB binders 0

Druggability 0.303

Overview

Basic information about this protein and its source genome.

Accession: KP13_01656
Assembly: Klebsiella pneumoniae subsp. pneumoniae Kp13, complete sequence
Gene: AHE43822.1 uvrC
Status: annotated
Amino acids: 610
Structure source: AlphaFold + ColabFold

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: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:0005515 Binding to a protein. 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: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).

Target profile

Computed evidence for target prioritization.

Human off-target: No hit
Human identity (%): 0.0
Gut microbiome off-target: hit
Essential (DEG): N
DEG identity (%): 0.0
Localization: Cytoplasmic
ColabFold pLDDT: 85.96

Selected Druggability evidence

AlphaFold / UniProt model

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 0.303

Structure A0A0H3GQ96

Pocket Pocket 7

P2Rank 0.656

Structure A0A0H3GQ96

Pocket Pocket 1

ColabFold model

FPocket 0.09 · Pocket 28

P2Rank 0.613 · Pocket 1

Core conservation Conserved core gene

Roary core

CoreCruncher core

Gut microbiome 171 / 4744 genomes with a hit

Normalized 0.036

Sequence

Primary amino-acid sequence viewer.

Functional Annotations

Enzyme classification and Gene Ontology terms linked to this protein.

8 GO

Gene Ontology (GO)

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: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:0005515 Binding to a protein.
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: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:0005737 The contents of a cell excluding the plasma membrane and nucleus, but including other subcellular structures.
GO:0009432 An error-prone process for repairing damaged microbial DNA.

Sequence Features

Domain/signature hits from InterPro and related databases.

43 records

Show feature table

Start	End	DB	Term	Name
548	608	FunFam	G3DSA:1.10.150.20:FF:000005	UvrABC system protein C
17	98	SMART	SM00465	uri_9
17	98	InterPro	IPR000305	GIY-YIG endonuclease
190	243	SUPERFAMILY	SSF46600	C-terminal UvrC-binding domain of UvrB
190	243	InterPro	IPR036876	UVR domain superfamily
18	93	Pfam	PF01541	GIY-YIG catalytic domain
18	93	InterPro	IPR000305	GIY-YIG endonuclease
377	552	Gene3D	G3DSA:3.30.420.340	UvrC, RNAse H endonuclease domain
377	552	InterPro	IPR038476	UvrC, RNAse H endonuclease domain superfamily
204	239	ProSiteProfiles	PS50151	UVR domain profile.
204	239	InterPro	IPR001943	UVR domain
207	227	Coils	Coil	Coil
16	94	ProSiteProfiles	PS50164	GIY-YIG domain profile.
16	94	InterPro	IPR000305	GIY-YIG endonuclease
9	589	NCBIfam	TIGR00194	excinuclease ABC subunit UvrC
9	589	InterPro	IPR004791	UvrABC system, subunit C
17	94	CDD	cd10434	GIY-YIG_UvrC_Cho
17	94	InterPro	IPR047296	UvrC/Cho-like, GIY-YIG domain
4	102	FunFam	G3DSA:3.40.1440.10:FF:000001	UvrABC system protein C
2	606	PANTHER	PTHR30562	UVRC/OXIDOREDUCTASE
254	479	ProSiteProfiles	PS50165	UvrC family, homology region profile.
254	479	InterPro	IPR001162	UvrC, RNAse H endonuclease domain
17	100	SUPERFAMILY	SSF82771	GIY-YIG endonuclease
17	100	InterPro	IPR035901	GIY-YIG endonuclease superfamily
204	240	Gene3D	G3DSA:4.10.860.10	UVR domain
378	549	FunFam	G3DSA:3.30.420.340:FF:000001	UvrABC system protein C
4	607	Hamap	MF_00203	UvrABC system protein C [uvrC].
4	607	InterPro	IPR004791	UvrABC system, subunit C
204	240	FunFam	G3DSA:4.10.860.10:FF:000002	UvrABC system protein C
521	607	SUPERFAMILY	SSF47781	RuvA domain 2-like
521	607	InterPro	IPR010994	RuvA domain 2-like
205	237	Pfam	PF02151	UvrB/uvrC motif
205	237	InterPro	IPR001943	UVR domain
558	605	Pfam	PF14520	Helix-hairpin-helix domain
5	102	Gene3D	G3DSA:3.40.1440.10	-
5	102	InterPro	IPR035901	GIY-YIG endonuclease superfamily
588	607	SMART	SM00278	HhH1_4
588	607	InterPro	IPR003583	Helix-hairpin-helix DNA-binding motif, class 1
556	575	SMART	SM00278	HhH1_4
556	575	InterPro	IPR003583	Helix-hairpin-helix DNA-binding motif, class 1
386	542	Pfam	PF08459	UvrC RNAse H endonuclease domain
386	542	InterPro	IPR001162	UvrC, RNAse H endonuclease domain
555	610	Gene3D	G3DSA:1.10.150.20	-

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 + 2

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

Entry	Method	Resolution	Chain	Coverage	Links	Status
AlphaFold AF_A0A0H3GQ96	AlphaFold	—	—	full sequence	—	Viewing
ColabFold KP13_01656	ColabFold	—	—	full sequence	—	Loaded

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
7				0.303

Pockets (P2RANK)

Showing top-ranked P2Rank candidates by probability. Probability is color-coded per P2Rank calibration: high (≥ 0.5), medium (0.2 – 0.49), low (< 0.2).

P2RANK	Score	Probability
1	9.16	0.49
2	8.62	0.461
3	1.53	0.022
4	1.11	0.008

Pockets (P2RANK)

Showing top-ranked P2Rank candidates by probability. Probability is color-coded per P2Rank calibration: high (≥ 0.5), medium (0.2 – 0.49), low (< 0.2).

P2RANK	Score	Probability
1	9.39	0.505
2	7.39	0.387
3	1.24	0.012
4	1.06	0.007
5	0.97	0.005