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Goto SSAP Server GRATH Server Gene3D Navigation Home Top of hierarchy	Home > Top > DHS   DHS: version 2.5.1 ( built on CATH version 2.5.1) Structural Diversity of Domain Superfamilies in the CATH Database Supplementary Material Link to dynamic summary table Table 1 supplement. Summary sequence, structure and function data for all 1459 superfamilies included in the Dictionary of Homologous superfamiles. CATH Name Perc Var Total S35reps Largest SSE Smallest SSE Av SSAP Lowest SSAP 1.10.10.10 "Winged helix" repressor DNA binding dom 63 11 8 3 79.91 57.74 1.10.150.70 Transferase 67 7 12 4 74.83 58.63 1.10.20.10 Histone, subunit A 71 13 7 2 87.16 61.96 1.10.275.10 Fumarase/Aspartase N-Terminal Domain 71 5 14 4 77.74 64.32 1.10.606.10 Vanadium-containing Cloroperoxidase, dom2 41 3 29 17 76.21 69.06 1.10.620.20 Ribonucleotide Reductase, subunit A 54 6 26 12 76.15 52.88 1.10.760.10 Cytochrome C 56 22 9 4 80.59 57.82 1.20.58.60 Cytoskeleton 75 9 8 2 84.9 75.29 1.25.40.10 Tetratricopeptide Repeats (TPR) 79 6 19 4 85.09 72.33 1.25.40.20 Transcription activator 60 4 15 6 88.2 76 2.10.50.10 Tumor necrosis factor receptor,  sub A dom2 60 7 5 2 82.65 75.28 2.10.90.10 Cystine Knot Cytokines 67 7 12 4 77.73 65.73 2.40.70.10 Acid Proteases 75 16 20 5 78.26 49.86 2.60.120.20 Virus Coat Protein 55 13 18 8 72.01 38.53 2.60.120.200 Galectin type carbohudrate recognition domain 50 18 20 10 75.61 54.84 2.60.120.260 Galactose Binding domain-like 60 17 15 6 74.4 57.96 2.60.40.420 Cupredoxins 63 19 16 6 79.3 45.52 3.10.28.10 Homing endonucleases 73 7 11 3 83.9 79.01 3.20.20.140 Metal dependent hydrolases 35 6 26 17 72.22 55.65 3.20.20.80 Glycosidases 32 7 25 17 71.9 53.1 3.20.20.90 Triose Phosphate Isomerase,FMN dependent oxidoreductase, phosphate binding enzymes & tryptophan biosynthesis. 46 15 24 13 78.29 63.54 3.30.160.60 Classic zinc finger 67 4 3 1 88.13 86.23 3.30.360.10 Dihydrodipicolinate Reductase, domain 2 68 5 19 6 80.73 74.68 3.30.40.10 Zinc/RING finger domain, C3HC4 60 4 5 2 75.97 70.65 3.30.420.10 Nucleotydyl Transferase 43 7 14 8 72.1 54.84 3.30.470.20 ATP Grasp B domain 63 13 19 7 77.84 57.58 3.30.565.10 Chaperone 50 7 16 8 75.71 56.6 3.30.70.270 Transferase/DNA 69 7 13 4 77.9 64.52 3.30.830.10 Cytochrome Bc1 Complex, chain A dom 1 50 11 14 7 82.28 76.45 3.30.930.10 Bira Bifunctional  Protein, Domain 2 57 13 23 10 75.47 52.29 3.40.190.10 Periplasmic Binding protein-like 50 14 14 7 73.33 45.14 3.40.225.10 L-fuculose-1-phosphate aldolase 40 4 20 12 87.73 82.69 3.40.47.10  Peroxisomal Thiolase, subunit A, domain 1 50 7 16 8 78.06 57.91 3.40.50.1100 Complex Lyase/Peptide 56 7 16 7 81.38 71.51 3.40.50.1240 Phosphoglycerate mutase-like 43 7 23 13 79.52 74.33 3.40.50.1820 Alpha Beta Hydrolases 64 15 28 10 74.37 43.38 3.40.50.610 Glutamine Amidotransferases 50 6 22 11 78.16 71.7 3.40.50.720 NAD(P)-binding Rossman-like Domain 50 13 18 9 76.43 51.79 3.40.50.970 DHS-like NAD/FAD-binding domain 54 14 24 11 80.27 61.53 3.40.510.10 Tyrosyl-transfer RNA synthetase, sub E dom 1 44 8 25 14 75.7 60.52 3.40.640.10 Type I PLP aspartate aminotransferase-like 41 25 22 13 80.98 71.52 3.40.710.10 DD-peptidase /beta-lactamase 46 12 24 13 80.06 70.14 3.60.20.10 Glutamine Phosphoribosylpyrophosphate dom1 41 17 24 14 76.4 53.68 3.60.21.10 Hydrolase 35 5 26 17 71.88 59.5 3.80.10.10 Ribonuclease Inhibitor 69 6 23 7 80.46 71.26 3.90.190.10 Protein tyrosine phosphatase superfamily 52 7 21 10 83.25 79.02 3.90.226.10 2-enoyl-CoA Hydratase 45 9 20 11 81.72 72.4 3.90.550.10 Biosynthesis protein spsa (spore coat protein) 43 14 23 13 74.51 56.02 Table 2 supplement. The 48 superfamilies with the most variation in number of secondary structure elements (SSE). CATH Maximum Insert # SSEs in Max Insert   Total SSEs Total Extra SSEs Description of Embellishments 2.60.40.10   4 1dr9A1 3S   1H 11 5S  2H Insertions in 3 places. Largest insertion localised at the edges of both β-sheets. 2.60.40.30 3 1hft02 2S   1H 9 3S  1H Insertion is in two regions. Localised at the edge of one β-sheet. 2.60.40.420 4 1kcw02 2S   2H 13 3S  3H Insertions in 4 areas, one at beginning, two in the middle and one at the end of the chain. All insertions are localised on one edge of the β-sheet. 2.60.120.200 6 1a8d01 5S   1H 19 8S  3H Insertions throughout. Insertion at the beginning of 1a8d01 extends the edges of both β-sheets. Other insertions embellish the other end of the β-sheet. 2.60.120.20 2  2bbvA0 1S   1H 18 7S  3H Insertions throughout the structure. They extend both ends of each β-sheet in the sandwich. 3.30.360.10 4 1dpgA2 2S   2H 19 4S  7H Insertions in 4 places in the chain. Additional strands occur on either side of the β-sheet. Additional helices congregate on one side of the β-sheet. 3.30.470.20   10 1bncA2 5S   5H 20 6S  8H Insertions at beginning and end of the chain embellish the edges of the β-sheet. Additional helices 3.30.420.10 4 1tgoA2 3S   3H 14 4S  3H Insertions in 4 areas, at the N terminal, two in the middle and one at the end of the chain. Middle strand insertion extends β-sheet. 3.30.930.10 7 1atiA1 5S   2H 22 7S  4H Insertions are in 5 areas. One side of the sheet is embellished by the central strand insertions. 3.40.190.10   8 1anf01 2S   6H 14 3S  6H Insertions mostly at the C-terminal end of the structure do not contribute to central sheet. The embellishment forms an extra lobe. 3.40.630.30   5  1m4iA0 4S   1H 13 5S  2H Main insertions are at the C- and N-termini  but they embellish the same side of the sheet. 3.40.47.10 6  1i88A1 2S   4H 16 3S  6H Helical insertions form an extra lobe of helices. 3.40.50.1240 10 1dkqA0 2S   8H 23 3S  11H Insertions form an extra lobe of helices. 3.40.50.970   7 1kekA6 2S   5H 24 2S  10H Insertions are at the C- and N-termini. Most insertions form a separate lobe. 3.40.50.610 6 1ct9A2 0S   6H 22 0S  14H Insertions are throughout the structure. The α-helices pack against the consensus α-helices. 3.40.710.10 6 1l0gB0 4S   2H 24 6S  5H Insertions are in 5 areas. Strand insertions contribute to one side of the β-sheet. 3.40.50.1820 12 1ivyA0 4S   8H 28 11S  9H Insertions are throughout the structure. Inserted strands are added to one side of the β sandwich. The inserted α-helices form an extra lobe. 3.40.510.10 10 1ile03 5S   5H 25 5S  9H Insertions are throughout. Insertions are co-located in 3D forming a large lobe. Table 3 supplement. Description of secondary structure embellishments in the mainly β 2-layer sandwiches (2.60), the α β 2-Layer Sandwiches (3.30) and the 3-Layer (αβα) sandwiches (3.40). The maximum number of inserted secondary structures identified in a specified relative is given. Also, the number of secondary structures embellishments (SSEs) α-helices and β-strands in the largest continuous insertion, the total number of secondary structures, and the total number of inserted secondary structures in that representative. The last column contains a brief description of the insertions throughout the peptide chain and how they are orientated in the three-dimensional structure. Figure 1 supplement. The average indel length plotted for different sequence identity bins. Figure 2 supplement. Representatives from the superfamilies identified as structurally conserved. 1) The pleckstrin homology domain from dynamin (2dynA0). 2) Bovine odorant binding protein (1obpA0) with odorant ligand bound from the lipocalin superfamily. 3) Ferredoxin from the 2Fe-2S ferredoxxin superfamily. 4) Rabbit muscle phosphorylase kinase (1phk) from the kinase superfamily. The whole protein is shown in figure (a) and the structurally conserved domain is shown in (b) and 5) Cytochrome P450 (1bvyA0). Figure 3 supplement. 2DSEC diagram showing four areas of embellishment in the Galectin type carbohudrate recognition domain 2.60.120.200. Figure 4 supplement. 2DSEC diagram showing four areas of embellishment in the cupredoxin superfamily 2.60.40.420. Figure 5 supplement. 2DSEC diagram shows the embellishments present in the oligomerisation domain in the NADP oxidoreductase superfamily. Figure 6 supplement. The 2DSEC diagram illustrates the positions of the embellishments along the peptide chain in selected members of the αβ hydrolase superfamily. Figure 7 supplement. Three domains from the αβ hydrolase superfamily (3.40.50.950) showing the extent of structural embellishments in the superfamily. In mammalian hormone-sensitive lipase (1evq) and human gastric lipase (1hlg) the embellished helices form an extra lobe at the top of the beta-sheet. Figure 8 supplement. Structural similarity measured by SSAP versus EC conservation for all homologous pairs in CATH with EC classifications. EC4 indicates that all 4 levels in the EC classification are the same, EC3 indicates the first 3 levels are the same, less than 3 EC indicates that one or two EC levels are the same.