KpKP13 Protein target profile

Cytidylate kinase

Accession: KP13_31499

Gene: AHE45430.1 cmk 3D evidence: AlphaFold DB model + ColabFold model UniProt A0A0H3GL15

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Length 227

Pocket druggability (P2Rank · AlphaFold DB model) 0.926

Direct ligand evidence 0 53 total records

Functional annotation 1 EC 8 GO

Target summary

Promising target candidate with multiple supporting evidence streams.

Automated synthesis of the evidence currently loaded. Review the underlying records before prioritizing this protein.

Main supporting evidence

Risks to review

Evidence gaps

No metabolic context No SBML/network-derived reaction evidence is loaded for this protein.

Terms and data sources used on this page

PDB: experimentally determined structures from the Protein Data Bank. These are the strongest structural evidence, but may cover only part of the protein.

AlphaFold DB model: a precomputed predicted structure downloaded from AlphaFold Database/UniProt, not an experiment performed here.

ColabFold model: a predicted structure generated for this workspace; interpret it with coverage and confidence.

pLDDT: confidence score for predicted structures. High values support local geometry; low values mean the region should not drive pocket interpretation.

FPocket / P2Rank: software tools that predict possible ligand-binding pockets on a 3D structure. They are useful screening signals, not experimental validation.

Druggability: a pocket-based estimate of whether a small molecule could bind productively. It does not mean a drug already exists.

PDB ligand: a compound observed in an experimental structure. Direct same-protein records are stronger than homolog-transferred records.

ChEMBL: a public database of measured compound bioactivity. Direct entries are stronger than entries transferred from similar proteins.

ZINC: a purchasable-compound database. Here it marks proposed candidates from chemical similarity, not measured binders.

LigQ / LigQ_2: an internal Target pipeline step that gathers PDB, ChEMBL, and ZINC ligand evidence for each protein.

Off-target: sequence similarity to proteins we prefer not to hit, such as human proteins or beneficial gut microbiome proteins.

DEG: Database of Essential Genes. A match suggests the protein resembles genes known to be essential in other organisms.

Roary / CoreCruncher: pan-genome tools used to decide whether a gene is core across analyzed strains or accessory/strain-specific.

EC / GO: functional annotations: EC describes enzyme reactions; GO describes biological process, molecular function, or cellular component.

KEGG pathway: a curated metabolic route label used here to group reactions imported from the metabolic model.

Chokepoint: a metabolic reaction that is the only producer or consumer of a metabolite in the imported model.

Prioritization evidence

Selectivity, essentiality, structural confidence, conservation, and predicted binding-site evidence.

Off-target risk

Human off-target: No hit
Gut microbiome similarity: 4.6% of screened genomes Lower prevalence suggests narrower overlap with the screened gut microbiome.

Essentiality

Essential (DEG): Y
DEG identity (%): 90.308 Higher values support similarity to known essential genes.
DEG E-value: 2.19e-150 Smaller values mean stronger essential-gene similarity.

Structure confidence

ColabFold pLDDT: 93.15 0-100 confidence; >70 supports local structural interpretation.

Binding-site evidence

AlphaFold DB / UniProt model

P2Rank's binding-site probability is the primary druggability signal shown across the app; FPocket's druggability score is shown alongside it for comparison. Both estimate small-molecule pocket quality after applying the curated structure priority — neither is experimental binding evidence. The 3D viewer may show a different loaded structure, so visible pockets can differ.

Druggability (P2Rank) 0.926

Structure A0A0H3GL15

Pocket Pocket 1

Druggability (FPocket) 0.592

Structure A0A0H3GL15

Pocket Pocket 5

ColabFold model

P2Rank 0.901 · Pocket 1

FPocket 0.581 · Pocket 2

Core conservation Conserved core gene

Roary core

CoreCruncher core

Gut microbiome 217 / 4744 genomes with a hit

Prevalence 4.6%

Sequence

Primary amino-acid sequence viewer.

MTANIPVITIDGPGGAGKGTLCKAMAEALGWHLLDSGAIYRVLALAALHHHVDVESEEALVPMAAHLDVRFISTDGNLEVVLEGEDVSSEIRTQEVANAASKVAAFPRVREALLRRQRAFRELPGLIADGRDMGTVVFPDAPVKIFLDASADERAHRRMRQLQEKGFDVNFERLLSEIKERDDRDRNRAVAPLVPAADALVLDSTELNIEQVIEKALQYAREKLAVA

Functional annotations

Enzyme classification and Gene Ontology terms linked to this protein.

1 EC 8 GO

Subcellular localization

Localization: Cytoplasmic

Enzyme Commission (EC)

2.7.4.25

Gene Ontology (GO)

GO:0005524 Binding to ATP, adenosine 5'-triphosphate, a universally important coenzyme and enzyme regulator.
GO:0004127 OBSOLETE. Catalysis of the reaction: ATP + (d)CMP = ADP + (d)CDP.
GO:0006139 Any cellular metabolic process involving nucleobases, nucleosides, nucleotides and nucleic acids.
GO:0005829 The part of the cytoplasm that does not contain organelles but which does contain other particulate matter, such as protein complexes.
GO:0036430 Catalysis of the reaction: ATP + CMP = ADP + CDP.
GO:0036431 Catalysis of the reaction: ATP + dCMP = ADP + dCDP.
GO:0015949 The chemical reactions and pathways by which a nucleobase, nucleoside or nucleotide small molecule is synthesized from another nucleobase, nucleoside or nucleotide small molecule.
GO:0006220 The chemical reactions and pathways involving a pyrimidine nucleotide, a compound consisting of nucleoside (a pyrimidine base linked to a deoxyribose or ribose sugar) esterified with a phosphate group at either the 3' or 5'-hydroxyl group of the sugar.

Sequence domains and features

Domain and signature matches imported from InterPro and related databases.

15 records

Show feature table

Start	End	DB	Term	Name
7	205	CDD	cd02020	CMPK
7	205	InterPro	IPR011994	Cytidylate kinase domain
1	227	Gene3D	G3DSA:3.40.50.300	-
1	227	InterPro	IPR027417	P-loop containing nucleoside triphosphate hydrolase
4	215	PANTHER	PTHR21299	CYTIDYLATE KINASE/PANTOATE-BETA-ALANINE LIGASE
8	221	Pfam	PF02224	Cytidylate kinase
8	221	InterPro	IPR011994	Cytidylate kinase domain
6	224	Hamap	MF_00238	Cytidylate kinase [cmk].
6	224	InterPro	IPR003136	Cytidylate kinase
202	222	Coils	Coil	Coil
1	227	FunFam	G3DSA:3.40.50.300:FF:000262	Cytidylate kinase
6	224	SUPERFAMILY	SSF52540	P-loop containing nucleoside triphosphate hydrolases
6	224	InterPro	IPR027417	P-loop containing nucleoside triphosphate hydrolase
6	219	NCBIfam	TIGR00017	(d)CMP kinase
6	219	InterPro	IPR003136	Cytidylate kinase

3D structure

Selected loaded structure. Experimental PDB entries may cover only a portion of the sequence; AlphaFold DB and ColabFold models typically cover the full protein but remain computational predictions.

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Pocket score High Medium Low

How colors and pocket overlays are used

Uniform protein color marks the displayed model as a single molecular object.

Experimental PDB structures may be colored by chain to distinguish subunits or copies present in the file.

Pocket colors and alpha spheres are evidence overlays for predicted binding cavities; they are not alternative protein chains.

'Alpha spheres' is FPocket's own cavity-shape geometry, imported when available and aligned with the loaded structure.

'Pocket atoms'/'Predicted site atoms' show the pocket's residue atoms instead: P2Rank reports residues rather than alpha spheres, and FPocket falls back to this when alpha-sphere geometry is unavailable or doesn't align.

'No pocket geometry' means neither alpha spheres nor residue-position data could be found for that pocket; the layer just highlights the same residues as 'Nearby residues'.

Pocket details Inspect a specific pocket, or open the full viewer

Binding pockets · P2Rank

Druggability (P2Rank): high ≥ 0.5 · medium 0.2–0.49 · low < 0.2

Pocket 1 P2Rank #1

0.926

Likely same site as FPocket 1 0.9 Å 29 shared residues 94% of smaller site

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Surrounding area

Pocket 2 P2Rank #2

0.003

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Surrounding area

Binding pockets · FPocket

Druggability (FPocket): high ≥ 0.7 · medium 0.4–0.69 · low < 0.4

Pocket 1 FPocket #5

0.592

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Surrounding area

Pocket 2 FPocket #1

0.402 Unusual size

Likely same site as P2Rank 1 0.9 Å 29 shared residues 94% of smaller site

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Surrounding area

Pocket 3 FPocket #13

0.377

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Surrounding area

Residue sets

UniProt: Binding site:27-35

Binding pockets · FPocket

Druggability (FPocket): high ≥ 0.7 · medium 0.4–0.69 · low < 0.4

Pocket 1 FPocket #2

0.581

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Surrounding area

Pocket 2 FPocket #1

0.408 Unusual size

Likely same site as P2Rank 1 1.4 Å 28 shared residues 90% of smaller site

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Surrounding area

All structural evidence 0 experimental · 2 predicted

Structural evidence

0 + 2

Experimental PDB entries plus predicted AlphaFold DB or ColabFold models. Click Switch to display a different loaded structure in the viewer.

Entry	Method	Resolution	Chain	Coverage	Links	Status
AlphaFold DB AF_A0A0H3GL15	AlphaFold DB	—	—	full sequence	—	Viewing
ColabFold KP13_31499	ColabFold	—	—	full sequence	—	Loaded

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.

53 records

Chemistry signal

Structural ligand evidence is available for this target.

Direct evidence 0 same-protein records

Transferred evidence 3 records from similar proteins

Structural ligands 3 0 loaded crystals

Measured bioactivity 0 direct and transferred ChEMBL records

Proposed compounds 50 similarity-based ZINC candidates

Best available ligand signal

CAR PDB via homolog 323.2 Da · LogP -2.45 · TPSA 177.4 Open detail RCSB PDB

DC PDB via homolog Detail RCSB PDB

DOC PDB via homolog Detail RCSB PDB

ZINC12503923 ZINC proposed compound · Tanimoto 1.000 Detail ZINC

ZINC12503924 ZINC proposed compound · Tanimoto 1.000 Detail ZINC

Highest-confidence structural evidence: ligands co-crystallized with this exact protein. If the source PDB is loaded in Target, use Open crystal to inspect it in the structure viewer.

No PDB structure with a co-crystallized ligand found for this exact protein.

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.

Ligand	Source crystal	UniProt (homolog)	MW · LogP · TPSA	Lipinski	PAINS	SMILES
CAR RCSB PDB	1KDR	P0A6I0	323.2 Da LogP -2.45 TPSA 177.4	✓ Ro5	✓ Clean	`C1=CN(C(=O)N=C1N)[C@H]2[C@H]([C@@H]([C@H](O2)CO…`
DC RCSB PDB	2FEO	P0A6I0	307.2 Da LogP -1.42 TPSA 157.1	✓ Ro5	✓ Clean	`C1[C@@H]([C@H](O[C@H]1N2C=CC(=NC2=O)N)COP(=O)(O…`
DOC RCSB PDB	1KDT	P0A6I0	291.2 Da LogP -0.39 TPSA 136.9	✓ Ro5	✓ Clean	`C1C[C@@H](O[C@@H]1COP(=O)(O)O)N2C=CC(=NC2=O)N`

Experimental bioactivity from ChEMBL measured directly on this protein. Score = pchembl (−log Ki/IC₅₀; higher = more potent).

No ChEMBL bioactivity data found for this exact protein.

Bioactivity inferred from similar proteins in ChEMBL. Score = pchembl (−log Ki/IC₅₀; higher = more potent).

No ChEMBL hits found through similar proteins.

Proposed virtual-screening candidates from ZINC. Score = Tanimoto similarity to a known binder (0–1; higher = more similar).

Ligand	Tanimoto	MW · LogP · TPSA	Lipinski	PAINS	SMILES
ZINC12503923 ZINC	1.000	307.2 Da LogP -1.42 TPSA 157.1	✓ Ro5	✓ Clean	`Nc1ccn([C@@H]2C[C@@H](O)[C@@H](COP(=O)(O)O)O2)c…`
ZINC12503924 ZINC	1.000	307.2 Da LogP -1.42 TPSA 157.1	✓ Ro5	✓ Clean	`Nc1ccn([C@H]2C[C@@H](O)[C@@H](COP(=O)(O)O)O2)c(…`
ZINC1532524 ZINC	1.000	323.2 Da LogP -2.45 TPSA 177.4	✓ Ro5	✓ Clean	`Nc1ccn([C@H]2O[C@@H](COP(=O)(O)O)[C@H](O)[C@@H]…`
ZINC1532581 ZINC	1.000	307.2 Da LogP -1.42 TPSA 157.1	✓ Ro5	✓ Clean	`Nc1ccn([C@@H]2C[C@@H](O)[C@H](COP(=O)(O)O)O2)c(…`
ZINC1611080 ZINC	1.000	291.2 Da LogP -0.39 TPSA 136.9	✓ Ro5	✓ Clean	`Nc1ccn([C@H]2CC[C@@H](COP(=O)(O)O)O2)c(=O)n1`
ZINC16546001 ZINC	1.000	323.2 Da LogP -2.45 TPSA 177.4	✓ Ro5	✓ Clean	`Nc1ccn([C@@H]2O[C@H](COP(=O)(O)O)[C@H](O)[C@@H]…`
ZINC1785780 ZINC	1.000	323.2 Da LogP -2.45 TPSA 177.4	✓ Ro5	✓ Clean	`Nc1ccn([C@@H]2O[C@H](COP(=O)(O)O)[C@@H](O)[C@@H…`
ZINC1785781 ZINC	1.000	323.2 Da LogP -2.45 TPSA 177.4	✓ Ro5	✓ Clean	`Nc1ccn([C@H]2O[C@H](COP(=O)(O)O)[C@@H](O)[C@@H]…`
ZINC3645374 ZINC	1.000	307.2 Da LogP -1.42 TPSA 157.1	✓ Ro5	✓ Clean	`Nc1ccn([C@@H]2C[C@H](O)[C@@H](COP(=O)(O)O)O2)c(…`
ZINC3861744 ZINC	1.000	323.2 Da LogP -2.45 TPSA 177.4	✓ Ro5	✓ Clean	`Nc1ccn([C@@H]2O[C@H](COP(=O)(O)O)[C@@H](O)[C@H]…`
ZINC3861759 ZINC	1.000	307.2 Da LogP -1.42 TPSA 157.1	✓ Ro5	✓ Clean	`Nc1ccn([C@H]2C[C@H](O)[C@@H](COP(=O)(O)O)O2)c(=…`
ZINC3869480 ZINC	1.000	323.2 Da LogP -2.45 TPSA 177.4	✓ Ro5	✓ Clean	`Nc1ccn([C@H]2O[C@@H](COP(=O)(O)O)[C@@H](O)[C@H]…`
ZINC3869481 ZINC	1.000	323.2 Da LogP -2.45 TPSA 177.4	✓ Ro5	✓ Clean	`Nc1ccn([C@@H]2O[C@@H](COP(=O)(O)O)[C@@H](O)[C@H…`
ZINC3869482 ZINC	1.000	323.2 Da LogP -2.45 TPSA 177.4	✓ Ro5	✓ Clean	`Nc1ccn([C@H]2O[C@@H](COP(=O)(O)O)[C@@H](O)[C@@H…`
ZINC3869483 ZINC	1.000	323.2 Da LogP -2.45 TPSA 177.4	✓ Ro5	✓ Clean	`Nc1ccn([C@@H]2O[C@@H](COP(=O)(O)O)[C@@H](O)[C@@…`
ZINC3869816 ZINC	1.000	307.2 Da LogP -1.42 TPSA 157.1	✓ Ro5	✓ Clean	`Nc1ccn([C@@H]2C[C@H](O)[C@H](COP(=O)(O)O)O2)c(=…`
ZINC3869817 ZINC	1.000	307.2 Da LogP -1.42 TPSA 157.1	✓ Ro5	✓ Clean	`Nc1ccn([C@H]2C[C@H](O)[C@H](COP(=O)(O)O)O2)c(=O…`
ZINC3869818 ZINC	1.000	307.2 Da LogP -1.42 TPSA 157.1	✓ Ro5	✓ Clean	`Nc1ccn([C@H]2C[C@@H](O)[C@H](COP(=O)(O)O)O2)c(=…`
ZINC3954230 ZINC	1.000	323.2 Da LogP -2.45 TPSA 177.4	✓ Ro5	✓ Clean	`Nc1ccn([C@H]2O[C@@H](COP(=O)(O)O)[C@H](O)[C@H]2…`
ZINC8613159 ZINC	1.000	323.2 Da LogP -2.45 TPSA 177.4	✓ Ro5	✓ Clean	`Nc1ccn([C@@H]2O[C@H](COP(=O)(O)O)[C@H](O)[C@H]2…`
ZINC8952080 ZINC	1.000	323.2 Da LogP -2.45 TPSA 177.4	✓ Ro5	✓ Clean	`Nc1ccn([C@@H]2O[C@@H](COP(=O)(O)O)[C@H](O)[C@@H…`
ZINC9007749 ZINC	1.000	323.2 Da LogP -2.45 TPSA 177.4	✓ Ro5	✓ Clean	`Nc1ccn([C@@H]2O[C@@H](COP(=O)(O)O)[C@H](O)[C@H]…`
ZINC13435042 ZINC	0.837	387.2 Da LogP -1.30 TPSA 203.7	✓ Ro5	✓ Clean	`Nc1ccn([C@@H]2C[C@H](O)[C@H](CO[P@](=O)(O)OP(=O…`
ZINC14960508 ZINC	0.837	387.2 Da LogP -1.30 TPSA 203.7	✓ Ro5	✓ Clean	`Nc1ccn([C@@H]2C[C@H](O)[C@@H](CO[P@](=O)(O)OP(=…`
ZINC104864216 ZINC	0.833	403.2 Da LogP -2.33 TPSA 223.9	2 viol.	✓ Clean	`Nc1ccn([C@H]2O[C@@H](CO[P@](=O)(O)OP(=O)(O)O)[C…`
ZINC12504412 ZINC	0.833	403.2 Da LogP -2.33 TPSA 223.9	2 viol.	✓ Clean	`Nc1ccn([C@@H]2O[C@@H](CO[P@@](=O)(O)OP(=O)(O)O)…`
ZINC12504413 ZINC	0.833	403.2 Da LogP -2.33 TPSA 223.9	2 viol.	✓ Clean	`Nc1ccn([C@H]2O[C@@H](CO[P@@](=O)(O)OP(=O)(O)O)[…`
ZINC12504414 ZINC	0.833	403.2 Da LogP -2.33 TPSA 223.9	2 viol.	✓ Clean	`Nc1ccn([C@@H]2O[C@H](CO[P@@](=O)(O)OP(=O)(O)O)[…`
ZINC13431045 ZINC	0.833	403.2 Da LogP -2.33 TPSA 223.9	2 viol.	✓ Clean	`Nc1ccn([C@H]2O[C@@H](CO[P@@](=O)(O)OP(=O)(O)O)[…`
ZINC13431047 ZINC	0.833	403.2 Da LogP -2.33 TPSA 223.9	2 viol.	✓ Clean	`Nc1ccn([C@@H]2O[C@@H](CO[P@@](=O)(O)OP(=O)(O)O)…`
ZINC13548733 ZINC	0.833	403.2 Da LogP -2.33 TPSA 223.9	2 viol.	✓ Clean	`Nc1ccn([C@@H]2O[C@H](CO[P@@](=O)(O)OP(=O)(O)O)[…`
ZINC33913782 ZINC	0.833	403.2 Da LogP -2.33 TPSA 223.9	2 viol.	✓ Clean	`Nc1ccn([C@@H]2O[C@H](CO[P@@](=O)(O)OP(=O)(O)O)[…`
ZINC36471998 ZINC	0.833	483.2 Da LogP -2.21 TPSA 270.4	2 viol.	✓ Clean	`Nc1ccn([C@@H]2O[C@H](COP(=O)(OP(=O)(O)O)OP(=O)(…`
ZINC8215624 ZINC	0.833	403.2 Da LogP -2.33 TPSA 223.9	2 viol.	✓ Clean	`Nc1ccn([C@@H]2O[C@H](CO[P@@](=O)(O)OP(=O)(O)O)[…`
ZINC5811818 ZINC	0.809	339.2 Da LogP -2.51 TPSA 186.6	✓ Ro5	✓ Clean	`Nc1ccn([C@H]2O[C@@H](COP(=O)(O)O)[C@@H](O)O[C@H…`
ZINC5811821 ZINC	0.809	339.2 Da LogP -2.51 TPSA 186.6	✓ Ro5	✓ Clean	`Nc1ccn([C@@H]2O[C@@H](COP(=O)(O)O)[C@@H](O)O[C@…`
ZINC13516800 ZINC	0.808	451.2 Da LogP -0.15 TPSA 230.0	1 viol.	✓ Clean	`Nc1ccn([C@H]2CC[C@@H](CO[P@@](=O)(O)O[P@@](=O)(…`
ZINC32016993 ZINC	0.808	451.2 Da LogP -0.15 TPSA 230.0	1 viol.	✓ Clean	`Nc1ccn([C@@H]2CC[C@H](CO[P@@](=O)(O)O[P@](=O)(O…`
ZINC12503365 ZINC	0.804	467.2 Da LogP -1.18 TPSA 250.2	2 viol.	✓ Clean	`Nc1ccn([C@H]2C[C@@H](O)[C@@H](CO[P@](=O)(O)O[P@…`
ZINC13435050 ZINC	0.804	467.2 Da LogP -1.18 TPSA 250.2	2 viol.	✓ Clean	`Nc1ccn([C@@H]2C[C@H](O)[C@H](CO[P@@](=O)(O)O[P@…`
ZINC8215945 ZINC	0.804	467.2 Da LogP -1.18 TPSA 250.2	2 viol.	✓ Clean	`Nc1ccn([C@H]2C[C@H](O)[C@@H](CO[P@@](=O)(O)O[P@…`
ZINC12502055 ZINC	0.800	483.2 Da LogP -2.21 TPSA 270.4	2 viol.	✓ Clean	`Nc1ccn([C@@H]2O[C@@H](CO[P@@](=O)(O)O[P@@](=O)(…`
ZINC12502057 ZINC	0.800	483.2 Da LogP -2.21 TPSA 270.4	2 viol.	✓ Clean	`Nc1ccn([C@H]2O[C@@H](CO[P@@](=O)(O)O[P@@](=O)(O…`
ZINC12502058 ZINC	0.800	483.2 Da LogP -2.21 TPSA 270.4	2 viol.	✓ Clean	`Nc1ccn([C@@H]2O[C@H](CO[P@@](=O)(O)O[P@@](=O)(O…`
ZINC13431059 ZINC	0.800	483.2 Da LogP -2.21 TPSA 270.4	2 viol.	✓ Clean	`Nc1ccn([C@@H]2O[C@@H](CO[P@@](=O)(O)O[P@@](=O)(…`
ZINC25726736 ZINC	0.800	483.2 Da LogP -2.21 TPSA 270.4	2 viol.	✓ Clean	`Nc1ccn([C@H]2O[C@@H](CO[P@@](=O)(O)O[P@@](=O)(O…`
ZINC3861746 ZINC	0.800	483.2 Da LogP -2.21 TPSA 270.4	2 viol.	✓ Clean	`Nc1ccn([C@@H]2O[C@H](CO[P@](=O)(O)O[P@@](=O)(O)…`
ZINC53683723 ZINC	0.800	483.2 Da LogP -2.21 TPSA 270.4	2 viol.	✓ Clean	`Nc1ccn([C@@H]2O[C@@H](CO[P@@](=O)(O)O[P@@](=O)(…`
ZINC82142138 ZINC	0.800	483.2 Da LogP -2.21 TPSA 270.4	2 viol.	✓ Clean	`Nc1ccn([C@@H]2O[C@H](CO[P@@](=O)(O)O[P@@](=O)(O…`
ZINC82142140 ZINC	0.800	483.2 Da LogP -2.21 TPSA 270.4	2 viol.	✓ Clean	`Nc1ccn([C@@H]2O[C@H](CO[P@@](=O)(O)O[P@@](=O)(O…`

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.

Cross-references

External database identifiers for this protein, its structures, ligands, and metabolic reactions.

Sequence

UniProt A0A0H3GL15