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Conserved domains on  [gi|574607837|emb|CDL72931|]
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Cytochrome c peroxidase, partial [uncultured Zetaproteobacteria bacterium]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
MauG super family cl43544
Cytochrome c peroxidase [Posttranslational modification, protein turnover, chaperones];
46-100 8.23e-26

Cytochrome c peroxidase [Posttranslational modification, protein turnover, chaperones];


The actual alignment was detected with superfamily member COG1858:

Pssm-ID: 441463 [Multi-domain]  Cd Length: 283  Bit Score: 96.77  E-value: 8.23e-26
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 574607837  46 AAKVELGKKLYFEPAISKSGHFSCNSCHNLATWGVDNQKFSIGHKWNRGGRNAPT 100
Cdd:COG1858    1 PEKVELGKKLFFDPRLSGNGTISCASCHNPALGFTDGLPTSIGVGGQLGPRNAPT 55
 
Name Accession Description Interval E-value
MauG COG1858
Cytochrome c peroxidase [Posttranslational modification, protein turnover, chaperones];
46-100 8.23e-26

Cytochrome c peroxidase [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 441463 [Multi-domain]  Cd Length: 283  Bit Score: 96.77  E-value: 8.23e-26
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 574607837  46 AAKVELGKKLYFEPAISKSGHFSCNSCHNLATWGVDNQKFSIGHKWNRGGRNAPT 100
Cdd:COG1858    1 PEKVELGKKLFFDPRLSGNGTISCASCHNPALGFTDGLPTSIGVGGQLGPRNAPT 55
CCP_MauG pfam03150
Di-haem cytochrome c peroxidase; This is a family of distinct cytochrome c peroxidases (CCPs) ...
 46-100 1.06e-25

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.


Pssm-ID: 427168  Cd Length: 151  Bit Score: 92.96  E-value: 1.06e-25
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 574607837   46 AAKVELGKKLYFEPAISKSGHFSCNSCHNLATWGVDNQKFSIGHKWNRGGRNAPT 100
Cdd:pfam03150   1 PEKVELGKKLFFDPRLSGNGTISCASCHDPALGFTDGLPVSIGVDGQLGPRNAPT 55
MXAN_0977_Heme2 TIGR04039
di-heme enzyme, MXAN_0977 family; This model describes a subfamily of di-heme proteins related ...
 38-99 1.47e-13

di-heme enzyme, MXAN_0977 family; This model describes a subfamily of di-heme proteins related to the di-heme cytochrome c peroxidase and to MauG (methylamine utilization G), an enzyme that performs a tryptophan tryptophylquinone modification to the methylamine dehydrogenase light chain.


Pssm-ID: 188554 [Multi-domain]  Cd Length: 336  Bit Score: 64.33  E-value: 1.47e-13
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 574607837   38 VPADNPMSAAKVELGKKLYFEPAISKSGHFSCNSCHNLATWGVDNQKFSIGHKWNRGGRNAP 99
Cdd:TIGR04039   1 VPADNPMTEEKVELGRHLFYDKRLSGNGTQSCASCHIQSLAFTDGLATPVGSTGERHPRNSQ 62
 
Name Accession Description Interval E-value
MauG COG1858
Cytochrome c peroxidase [Posttranslational modification, protein turnover, chaperones];
46-100 8.23e-26

Cytochrome c peroxidase [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 441463 [Multi-domain]  Cd Length: 283  Bit Score: 96.77  E-value: 8.23e-26
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 574607837  46 AAKVELGKKLYFEPAISKSGHFSCNSCHNLATWGVDNQKFSIGHKWNRGGRNAPT 100
Cdd:COG1858    1 PEKVELGKKLFFDPRLSGNGTISCASCHNPALGFTDGLPTSIGVGGQLGPRNAPT 55
CCP_MauG pfam03150
Di-haem cytochrome c peroxidase; This is a family of distinct cytochrome c peroxidases (CCPs) ...
 46-100 1.06e-25

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.


Pssm-ID: 427168  Cd Length: 151  Bit Score: 92.96  E-value: 1.06e-25
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 574607837   46 AAKVELGKKLYFEPAISKSGHFSCNSCHNLATWGVDNQKFSIGHKWNRGGRNAPT 100
Cdd:pfam03150   1 PEKVELGKKLFFDPRLSGNGTISCASCHDPALGFTDGLPVSIGVDGQLGPRNAPT 55
MXAN_0977_Heme2 TIGR04039
di-heme enzyme, MXAN_0977 family; This model describes a subfamily of di-heme proteins related ...
 38-99 1.47e-13

di-heme enzyme, MXAN_0977 family; This model describes a subfamily of di-heme proteins related to the di-heme cytochrome c peroxidase and to MauG (methylamine utilization G), an enzyme that performs a tryptophan tryptophylquinone modification to the methylamine dehydrogenase light chain.


Pssm-ID: 188554 [Multi-domain]  Cd Length: 336  Bit Score: 64.33  E-value: 1.47e-13
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 574607837   38 VPADNPMSAAKVELGKKLYFEPAISKSGHFSCNSCHNLATWGVDNQKFSIGHKWNRGGRNAP 99
Cdd:TIGR04039   1 VPADNPMTEEKVELGRHLFYDKRLSGNGTQSCASCHIQSLAFTDGLATPVGSTGERHPRNSQ 62
thiosulf_SoxA TIGR04484
sulfur oxidation c-type cytochrome SoxA; Members of this family are SoxA, a c-type cytochrome ...
 38-73 4.07e-04

sulfur oxidation c-type cytochrome SoxA; Members of this family are SoxA, a c-type cytochrome with a CxxCH motif, part of a heterodimer with SoxX. SoxXA, SoxYZ, and SoxB contribute to thiosulfate oxidation to sulfate.


Pssm-ID: 275277 [Multi-domain]  Cd Length: 211  Bit Score: 37.58  E-value: 4.07e-04
                          10        20        30
                  ....*....|....*....|....*....|....*...
gi 574607837   38 VPADNPMSAAKVELGKKLYFepaiSKSGH--FSCNSCH 73
Cdd:TIGR04484  97 VKIDHPRAKAAYELGKELFY----TRRGQldLSCASCH 130
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options: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.
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