SCO family protein, partial [Immundisolibacter sp.]
Protein Classification
SCO family protein( domain architecture ID 10005092)
SCO (Synthesis of Cytochrome c Oxidase) family protein is required for the proper assembly of cytochrome c oxidase
List of domain hits
| Name | Accession | Description | Interval | E-value | ||
| Sco1 | COG1999 | Cytochrome oxidase Cu insertion factor, SCO1/SenC/PrrC family [Posttranslational modification, ... |
53-112 | 4.47e-25 | ||
Cytochrome oxidase Cu insertion factor, SCO1/SenC/PrrC family [Posttranslational modification, protein turnover, chaperones]; : Pssm-ID: 441602 Cd Length: 156 Bit Score: 92.27 E-value: 4.47e-25
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| Name | Accession | Description | Interval | E-value | ||
| Sco1 | COG1999 | Cytochrome oxidase Cu insertion factor, SCO1/SenC/PrrC family [Posttranslational modification, ... |
53-112 | 4.47e-25 | ||
Cytochrome oxidase Cu insertion factor, SCO1/SenC/PrrC family [Posttranslational modification, protein turnover, chaperones]; Pssm-ID: 441602 Cd Length: 156 Bit Score: 92.27 E-value: 4.47e-25
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| SCO | cd02968 | SCO (an acronym for Synthesis of Cytochrome c Oxidase) family; composed of proteins similar to ... |
53-112 | 1.61e-24 | ||
SCO (an acronym for Synthesis of Cytochrome c Oxidase) family; composed of proteins similar to Sco1, a membrane-anchored protein possessing a soluble domain with a TRX fold. Members of this family are required for the proper assembly of cytochrome c oxidase (COX). They contain a metal binding motif, typically CXXXC, which is located in a flexible loop. COX, the terminal enzyme in the respiratory chain, is imbedded in the inner mitochondrial membrane of all eukaryotes and in the plasma membrane of some prokaryotes. It is composed of two subunits, COX I and COX II. It has been proposed that Sco1 specifically delivers copper to the CuA site, a dinuclear copper center, of the COX II subunit. Mutations in human Sco1 and Sco2 cause fatal infantile hepatoencephalomyopathy and cardioencephalomyopathy, respectively. Both disorders are associated with severe COX deficiency in affected tissues. More recently, it has been argued that the redox sensitivity of the copper binding properties of Sco1 implies that it participates in signaling events rather than functioning as a chaperone that transfers copper to COX II. Pssm-ID: 239266 Cd Length: 142 Bit Score: 90.35 E-value: 1.61e-24
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| SCO1-SenC | pfam02630 | SCO1/SenC; This family is involved in biogenesis of respiratory and photosynthetic systems. ... |
52-112 | 1.03e-20 | ||
SCO1/SenC; This family is involved in biogenesis of respiratory and photosynthetic systems. SCO1 is required for a post-translational step in the accumulation of subunits COXI and COXII of cytochrome c oxidase. SenC is required for optimal cytochrome c oxidase activity and maximal induction of genes encoding the light-harvesting and reaction centre complexes of R. capsulatus. Pssm-ID: 460630 Cd Length: 134 Bit Score: 80.30 E-value: 1.03e-20
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| Name | Accession | Description | Interval | E-value | ||
| Sco1 | COG1999 | Cytochrome oxidase Cu insertion factor, SCO1/SenC/PrrC family [Posttranslational modification, ... |
53-112 | 4.47e-25 | ||
Cytochrome oxidase Cu insertion factor, SCO1/SenC/PrrC family [Posttranslational modification, protein turnover, chaperones]; Pssm-ID: 441602 Cd Length: 156 Bit Score: 92.27 E-value: 4.47e-25
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| SCO | cd02968 | SCO (an acronym for Synthesis of Cytochrome c Oxidase) family; composed of proteins similar to ... |
53-112 | 1.61e-24 | ||
SCO (an acronym for Synthesis of Cytochrome c Oxidase) family; composed of proteins similar to Sco1, a membrane-anchored protein possessing a soluble domain with a TRX fold. Members of this family are required for the proper assembly of cytochrome c oxidase (COX). They contain a metal binding motif, typically CXXXC, which is located in a flexible loop. COX, the terminal enzyme in the respiratory chain, is imbedded in the inner mitochondrial membrane of all eukaryotes and in the plasma membrane of some prokaryotes. It is composed of two subunits, COX I and COX II. It has been proposed that Sco1 specifically delivers copper to the CuA site, a dinuclear copper center, of the COX II subunit. Mutations in human Sco1 and Sco2 cause fatal infantile hepatoencephalomyopathy and cardioencephalomyopathy, respectively. Both disorders are associated with severe COX deficiency in affected tissues. More recently, it has been argued that the redox sensitivity of the copper binding properties of Sco1 implies that it participates in signaling events rather than functioning as a chaperone that transfers copper to COX II. Pssm-ID: 239266 Cd Length: 142 Bit Score: 90.35 E-value: 1.61e-24
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| SCO1-SenC | pfam02630 | SCO1/SenC; This family is involved in biogenesis of respiratory and photosynthetic systems. ... |
52-112 | 1.03e-20 | ||
SCO1/SenC; This family is involved in biogenesis of respiratory and photosynthetic systems. SCO1 is required for a post-translational step in the accumulation of subunits COXI and COXII of cytochrome c oxidase. SenC is required for optimal cytochrome c oxidase activity and maximal induction of genes encoding the light-harvesting and reaction centre complexes of R. capsulatus. Pssm-ID: 460630 Cd Length: 134 Bit Score: 80.30 E-value: 1.03e-20
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| TrxA | COG0526 | Thiol-disulfide isomerase or thioredoxin [Posttranslational modification, protein turnover, ... |
44-112 | 1.55e-04 | ||
Thiol-disulfide isomerase or thioredoxin [Posttranslational modification, protein turnover, chaperones]; Pssm-ID: 440292 [Multi-domain] Cd Length: 139 Bit Score: 38.52 E-value: 1.55e-04
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