Di-haem cytochrome c peroxidase; This is a family of distinct cytochrome c peroxidases (CCPs) ...
599-1034
7.79e-156
Di-haem cytochrome c peroxidase; This is a family of distinct cytochrome c peroxidases (CCPs) that contain two haem groups. Similar to other cytochrome c peroxidases, they reduce hydrogen peroxide to water using c-type haem as an oxidisable substrate. However, since they possess two, instead of one, haem prosthetic groups, bacterial CCPs reduce hydrogen peroxide without the need to generate semi-stable free radicals. The two haem groups have significantly different redox potentials. The high potential (+320 mV) haem feeds electrons from electron shuttle proteins to the low potential (-330 mV) haem, where peroxide is reduced (indeed, the low potential site is known as the peroxidatic site). The CCP protein itself is structured into two domains, each containing one c-type haem group, with a calcium-binding site at the domain interface. This family also includes MauG proteins, whose similarity to di-haem CCP was previously recognized.
The actual alignment was detected with superfamily member COG3488:
Pssm-ID: 478002 Cd Length: 461 Bit Score: 469.29 E-value: 7.79e-156
Thrombospondin type 3 repeat; The thrombospondin repeat is a short aspartate rich repeat which ...
203-252
4.33e-03
Thrombospondin type 3 repeat; The thrombospondin repeat is a short aspartate rich repeat which binds to calcium ions. The repeat was initially identified in thrombospondin proteins that contained 7 of these repeats. The repeat lacks defined secondary structure.
:
Pssm-ID: 367074 Cd Length: 36 Bit Score: 35.80 E-value: 4.33e-03
Di-haem oxidoreductase, putative peroxidase; DHOR is a family of di-haem oxidoredictases. It ...
598-1034
1.39e-123
Di-haem oxidoreductase, putative peroxidase; DHOR is a family of di-haem oxidoredictases. It carries the two characteriztic Cys-X-Y-Cys-His haem-binding motifs. The C-terminal high-potential site functions as an electron transfer centre, and the N-terminal low-potential site corresponds to the peroxidatic centre. Its probable function is as a peroxidase.
Pssm-ID: 428995 [Multi-domain] Cd Length: 486 Bit Score: 386.19 E-value: 1.39e-123
SCO0930 family lipoprotein; Members of this family are full-length homologs to the lipoprotein ...
289-370
3.73e-17
SCO0930 family lipoprotein; Members of this family are full-length homologs to the lipoprotein SCO0930, Streptomyces coelicolor A3(2). SCO0930 contains four copies of the repeat described by Pfam model PF03640. By comparison, PA5359 from Pseudomonas aeruginosa PAO1 has only two copies of the repeat, differs substantially in several regions, and is excluded from this family.
Pssm-ID: 468525 [Multi-domain] Cd Length: 310 Bit Score: 83.58 E-value: 3.73e-17
SCO0930 family lipoprotein; Members of this family are full-length homologs to the lipoprotein ...
289-373
6.52e-15
SCO0930 family lipoprotein; Members of this family are full-length homologs to the lipoprotein SCO0930, Streptomyces coelicolor A3(2). SCO0930 contains four copies of the repeat described by Pfam model PF03640. By comparison, PA5359 from Pseudomonas aeruginosa PAO1 has only two copies of the repeat, differs substantially in several regions, and is excluded from this family.
Pssm-ID: 468525 [Multi-domain] Cd Length: 310 Bit Score: 76.65 E-value: 6.52e-15
Thrombospondin type 3 repeat; The thrombospondin repeat is a short aspartate rich repeat which ...
203-252
4.33e-03
Thrombospondin type 3 repeat; The thrombospondin repeat is a short aspartate rich repeat which binds to calcium ions. The repeat was initially identified in thrombospondin proteins that contained 7 of these repeats. The repeat lacks defined secondary structure.
Pssm-ID: 367074 Cd Length: 36 Bit Score: 35.80 E-value: 4.33e-03
Di-haem oxidoreductase, putative peroxidase; DHOR is a family of di-haem oxidoredictases. It ...
598-1034
1.39e-123
Di-haem oxidoreductase, putative peroxidase; DHOR is a family of di-haem oxidoredictases. It carries the two characteriztic Cys-X-Y-Cys-His haem-binding motifs. The C-terminal high-potential site functions as an electron transfer centre, and the N-terminal low-potential site corresponds to the peroxidatic centre. Its probable function is as a peroxidase.
Pssm-ID: 428995 [Multi-domain] Cd Length: 486 Bit Score: 386.19 E-value: 1.39e-123
SCO0930 family lipoprotein; Members of this family are full-length homologs to the lipoprotein ...
289-370
3.73e-17
SCO0930 family lipoprotein; Members of this family are full-length homologs to the lipoprotein SCO0930, Streptomyces coelicolor A3(2). SCO0930 contains four copies of the repeat described by Pfam model PF03640. By comparison, PA5359 from Pseudomonas aeruginosa PAO1 has only two copies of the repeat, differs substantially in several regions, and is excluded from this family.
Pssm-ID: 468525 [Multi-domain] Cd Length: 310 Bit Score: 83.58 E-value: 3.73e-17
SCO0930 family lipoprotein; Members of this family are full-length homologs to the lipoprotein ...
289-373
6.52e-15
SCO0930 family lipoprotein; Members of this family are full-length homologs to the lipoprotein SCO0930, Streptomyces coelicolor A3(2). SCO0930 contains four copies of the repeat described by Pfam model PF03640. By comparison, PA5359 from Pseudomonas aeruginosa PAO1 has only two copies of the repeat, differs substantially in several regions, and is excluded from this family.
Pssm-ID: 468525 [Multi-domain] Cd Length: 310 Bit Score: 76.65 E-value: 6.52e-15
Thrombospondin type 3 repeat; The thrombospondin repeat is a short aspartate rich repeat which ...
203-252
4.33e-03
Thrombospondin type 3 repeat; The thrombospondin repeat is a short aspartate rich repeat which binds to calcium ions. The repeat was initially identified in thrombospondin proteins that contained 7 of these repeats. The repeat lacks defined secondary structure.
Pssm-ID: 367074 Cd Length: 36 Bit Score: 35.80 E-value: 4.33e-03
Database: CDSEARCH/cdd Low complexity filter: no Composition Based Adjustment: yes E-value threshold: 0.01
References:
Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
of the residues that compose this conserved feature have been mapped to the query sequence.
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