Chain D, Cytochrome c-L
cytochrome_MoxG family protein( domain architecture ID 10024009)
cytochrome_MoxG family protein
List of domain hits
Name | Accession | Description | Interval | E-value | |||
cytochrome_MoxG | TIGR03872 | cytochrome c(L), periplasmic; This model describes a periplasmic c-type cytochrome that serves ... |
2-135 | 2.47e-88 | |||
cytochrome c(L), periplasmic; This model describes a periplasmic c-type cytochrome that serves as the primary electron acceptor for the quinoprotein methanol dehydrogenase, a PQQ enzyme. The member from Paracoccus denitrificans is also characterized as an electron acceptor for methylamine dehydrogenase, a tryptophan tryptophylquinone enzyme. This protein is called cytochrome c(L) in methylotrophic bacteria such Methylobacterium extorquens, but c551i in Paracoccus denitrificans. [Energy metabolism, Electron transport] : Pssm-ID: 274829 Cd Length: 133 Bit Score: 253.11 E-value: 2.47e-88
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Name | Accession | Description | Interval | E-value | |||
cytochrome_MoxG | TIGR03872 | cytochrome c(L), periplasmic; This model describes a periplasmic c-type cytochrome that serves ... |
2-135 | 2.47e-88 | |||
cytochrome c(L), periplasmic; This model describes a periplasmic c-type cytochrome that serves as the primary electron acceptor for the quinoprotein methanol dehydrogenase, a PQQ enzyme. The member from Paracoccus denitrificans is also characterized as an electron acceptor for methylamine dehydrogenase, a tryptophan tryptophylquinone enzyme. This protein is called cytochrome c(L) in methylotrophic bacteria such Methylobacterium extorquens, but c551i in Paracoccus denitrificans. [Energy metabolism, Electron transport] Pssm-ID: 274829 Cd Length: 133 Bit Score: 253.11 E-value: 2.47e-88
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CccA | COG2010 | Cytochrome c, mono- and diheme variants [Energy production and conversion]; |
42-124 | 4.32e-09 | |||
Cytochrome c, mono- and diheme variants [Energy production and conversion]; Pssm-ID: 441613 [Multi-domain] Cd Length: 169 Bit Score: 52.26 E-value: 4.32e-09
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PRK14486 | PRK14486 | putative bifunctional cbb3-type cytochrome c oxidase subunit II/cytochrome c; Provisional |
36-123 | 8.71e-09 | |||
putative bifunctional cbb3-type cytochrome c oxidase subunit II/cytochrome c; Provisional Pssm-ID: 184704 [Multi-domain] Cd Length: 294 Bit Score: 52.51 E-value: 8.71e-09
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Cytochrom_C | pfam00034 | Cytochrome c; The Pfam entry does not include all Prosite members. The cytochrome 556 and ... |
51-123 | 3.31e-04 | |||
Cytochrome c; The Pfam entry does not include all Prosite members. The cytochrome 556 and cytochrome c' families are not included. All these are now in a new clan together. The C-terminus of DUF989, pfam06181, has now been merged into this family. Pssm-ID: 459641 [Multi-domain] Cd Length: 89 Bit Score: 37.52 E-value: 3.31e-04
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Name | Accession | Description | Interval | E-value | |||
cytochrome_MoxG | TIGR03872 | cytochrome c(L), periplasmic; This model describes a periplasmic c-type cytochrome that serves ... |
2-135 | 2.47e-88 | |||
cytochrome c(L), periplasmic; This model describes a periplasmic c-type cytochrome that serves as the primary electron acceptor for the quinoprotein methanol dehydrogenase, a PQQ enzyme. The member from Paracoccus denitrificans is also characterized as an electron acceptor for methylamine dehydrogenase, a tryptophan tryptophylquinone enzyme. This protein is called cytochrome c(L) in methylotrophic bacteria such Methylobacterium extorquens, but c551i in Paracoccus denitrificans. [Energy metabolism, Electron transport] Pssm-ID: 274829 Cd Length: 133 Bit Score: 253.11 E-value: 2.47e-88
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CccA | COG2010 | Cytochrome c, mono- and diheme variants [Energy production and conversion]; |
42-124 | 4.32e-09 | |||
Cytochrome c, mono- and diheme variants [Energy production and conversion]; Pssm-ID: 441613 [Multi-domain] Cd Length: 169 Bit Score: 52.26 E-value: 4.32e-09
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PRK14486 | PRK14486 | putative bifunctional cbb3-type cytochrome c oxidase subunit II/cytochrome c; Provisional |
36-123 | 8.71e-09 | |||
putative bifunctional cbb3-type cytochrome c oxidase subunit II/cytochrome c; Provisional Pssm-ID: 184704 [Multi-domain] Cd Length: 294 Bit Score: 52.51 E-value: 8.71e-09
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ccoP | TIGR00782 | cytochrome c oxidase, cbb3-type, subunit III; This model describes a di-heme subunit of ... |
42-118 | 2.64e-05 | |||
cytochrome c oxidase, cbb3-type, subunit III; This model describes a di-heme subunit of approximately 26 kDa of the cbb3 type copper and heme-containing cytochrome oxidase. [Energy metabolism, Electron transport] Pssm-ID: 129864 [Multi-domain] Cd Length: 285 Bit Score: 42.57 E-value: 2.64e-05
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Cytochrom_C | pfam00034 | Cytochrome c; The Pfam entry does not include all Prosite members. The cytochrome 556 and ... |
51-123 | 3.31e-04 | |||
Cytochrome c; The Pfam entry does not include all Prosite members. The cytochrome 556 and cytochrome c' families are not included. All these are now in a new clan together. The C-terminus of DUF989, pfam06181, has now been merged into this family. Pssm-ID: 459641 [Multi-domain] Cd Length: 89 Bit Score: 37.52 E-value: 3.31e-04
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Cytochrome_CBB3 | pfam13442 | Cytochrome C oxidase, cbb3-type, subunit III; |
48-80 | 1.27e-03 | |||
Cytochrome C oxidase, cbb3-type, subunit III; Pssm-ID: 463879 [Multi-domain] Cd Length: 67 Bit Score: 35.46 E-value: 1.27e-03
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CytC553 | COG2863 | Cytochrome c553 [Energy production and conversion]; |
47-123 | 2.12e-03 | |||
Cytochrome c553 [Energy production and conversion]; Pssm-ID: 442110 [Multi-domain] Cd Length: 98 Bit Score: 35.48 E-value: 2.12e-03
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Blast search parameters | ||||
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