Protein profile

KP13_02808

Multifunctional CCA protein

Genome: KpKP13

Gene: AHE42622.1 cca Structure source: AlphaFold + ColabFold UniProt A0A0H3GXS6
Amino acids 423
Annotations 12
Features 27
PDB binders 4
Druggability 0.414

Overview

Basic information about this protein and its source genome.

Accession
KP13_02808
Gene
AHE42622.1 cca
Status
annotated
Amino acids
423
Structure source
AlphaFold + ColabFold

Target profile

Computed evidence for target prioritization.

Human off-target
hit
Human identity (%)
31.373
Human E-value
1.31e-08
Gut microbiome off-target
hit
Essential (DEG)
Y
DEG identity (%)
86.165
DEG E-value
0.0
Localization
Cytoplasmic
ColabFold pLDDT
92.86

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 0.414
Structure A0A0H3GXS6
Pocket Pocket 3
P2Rank 0.641
Structure A0A0H3GXS6
Pocket Pocket 1
ColabFold model
FPocket 0.286 · Pocket 23
P2Rank 0.776 · Pocket 1
Core conservation Conserved core gene
Roary core
CoreCruncher core
Gut microbiome 196 / 4744 genomes with a hit
Normalized 0.041

Sequence

Primary amino-acid sequence viewer.

Functional Annotations

Enzyme classification and Gene Ontology terms linked to this protein.

12 GO

Gene Ontology (GO)

12
  • GO:0001680 Post-transcriptional addition of the terminal 3' CCA sequence to a tRNA which does not encode this sequence within the primary transcript. CCA addition proceeds by the sequential addition of CTP, CTP, and then ATP to the 3' end of the tRNA, yielding a diphosphate with each nucleotide addition.
  • GO:0016779 Catalysis of the transfer of a nucleotidyl group from one compound (donor) to another (acceptor).
  • GO:0004810 Catalysis of the reaction: a tRNA precursor + ATP + 2 CTP = a tRNA with a 3' CCA end + 3 diphosphate.
  • GO:0006396 Any process involved in the conversion of one or more primary RNA transcripts into one or more mature RNA molecules.
  • GO:0003723 Binding to an RNA molecule or a portion thereof.
  • GO:0005524 Binding to ATP, adenosine 5'-triphosphate, a universally important coenzyme and enzyme regulator.
  • GO:0160016 Catalysis of the reaction: a tRNA with a 3' CCA end + 2 CTP + ATP = a tRNA with a 3' CCACCA end + 3 diphosphate.
  • GO:0004112 Catalysis of the reaction: a nucleoside cyclic phosphate + H2O = a nucleoside phosphate.
  • GO:0000287 Binding to a magnesium (Mg) ion.
  • GO:0016791 Catalysis of the hydrolysis of a phosphoric monoester, releasing a phosphate.
  • GO:0000049 Binding to a transfer RNA.
  • GO:0042245 Any process that results in the repair of damaged RNA.

Sequence Features

Domain/signature hits from InterPro and related databases.

27 records
Show feature table
Start End DB Term Name
11 411 Hamap MF_01262 CCA-adding enzyme [cca].
11 411 InterPro IPR012006 tRNA nucleotidyltransferase, proteobacteria
130 412 SUPERFAMILY SSF81891 Poly A polymerase C-terminal region-like
241 340 CDD cd00077 HDc
241 340 InterPro IPR003607 HD/PDEase domain
10 128 CDD cd05398 NT_ClassII-CCAase
10 128 InterPro IPR002646 Poly A polymerase, head domain
159 222 Pfam PF12627 Probable RNA and SrmB- binding site of polymerase A
159 222 InterPro IPR032828 tRNA nucleotidyltransferase/poly(A) polymerase, RNA and SrmB- binding domain
135 417 Gene3D G3DSA:1.10.3090.10 -
11 134 FunFam G3DSA:3.30.460.10:FF:000016 Multifunctional CCA protein
8 129 SUPERFAMILY SSF81301 Nucleotidyltransferase
8 129 InterPro IPR043519 Nucleotidyltransferase superfamily
11 417 Hamap MF_01261 Multifunctional CCA protein [cca].
11 417 InterPro IPR012006 tRNA nucleotidyltransferase, proteobacteria
14 132 Pfam PF01743 Poly A polymerase head domain
14 132 InterPro IPR002646 Poly A polymerase, head domain
135 360 FunFam G3DSA:1.10.3090.10:FF:000001 Multifunctional CCA protein
11 418 PIRSF PIRSF000813 CCA_bact
11 418 InterPro IPR012006 tRNA nucleotidyltransferase, proteobacteria
3 134 Gene3D G3DSA:3.30.460.10 Beta Polymerase, domain 2
3 134 InterPro IPR043519 Nucleotidyltransferase superfamily
12 416 PANTHER PTHR47545 MULTIFUNCTIONAL CCA PROTEIN
241 338 Pfam PF01966 HD domain
241 338 InterPro IPR006674 HD domain
238 339 ProSiteProfiles PS51831 HD domain profile.
238 339 InterPro IPR006674 HD domain

3D Structure

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

3D visualization script Full viewer

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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_A0A0H3GXS6
AlphaFold full sequence Viewing
ColabFold KP13_02808
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
3 0.414

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 Sticks Spheres Surfaces Score Probability Labels Zoom Positions
1 11.36 0.607
2 6.64 0.337
3 1.6 0.025
4 1.19 0.01
5 1.11 0.008

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.

54 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
2TM A0A1C7DQ98 481.2 Da LogP -2.10 TPSA 261.2 2 viol. ✓ Clean C1=CN(C(=O)N=C1N)[C@H]2[C@@H]([C@@H]([C@H](O2)C…
APC O66728 505.2 Da LogP -1.52 TPSA 269.9 3 viol. ✓ Clean c1nc(c2c(n1)n(cn2)[C@H]3[C@@H]([C@@H]([C@H](O3)…
FLC Q96Q11 189.1 Da LogP -5.25 TPSA 140.6 ✓ Ro5 ✓ Clean C(C(=O)[O-])C(CC(=O)[O-])(C(=O)[O-])O
POP O67911 176.0 Da LogP -2.08 TPSA 129.9 ✓ Ro5 ✓ Clean O[P@@](=O)([O-])O[P@@](=O)(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.