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Conserved domains on  [gi|28076873|ref|NP_079671|]
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coiled-coil-helix-coiled-coil-helix domain-containing protein 5 [Mus musculus]

Protein Classification

coiled-coil-helix-coiled-coil-helix domain-containing protein( domain architecture ID 11245729)

coiled-coil-helix-coiled-coil-helix (CHCH) domain-containing protein carries (CX9C) type motifs and is imported into the mitochondrion with the help of the disulfide relay-dependent MIA import pathway

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
CX9C pfam16860
CHCH-CHCH-like Cx9C, IMS import disulfide relay-system,; CX9C is the first half of a twin Cx9C ...
7-49 1.37e-09

CHCH-CHCH-like Cx9C, IMS import disulfide relay-system,; CX9C is the first half of a twin Cx9C motif in eukaryotic proteins. The function of this motif is to import nuclear-encoded mitochondrial intermembrane-space-proteins into the IMS (intermembrane space), as these latter lack a mitochondrial targeting sequence. The Cx9C proteins have a disulfide-bonded alpha-hairpin conformation. Cx9C-containing proteins are thus putative substrates for the Mia40-dependent thiol-disulfide exchange mechanism that carries out an oxidative folding process resulting in the proteins being trapped in the IMS.


:

Pssm-ID: 465284  Cd Length: 42  Bit Score: 49.62  E-value: 1.37e-09
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|...
gi 28076873     7 VTARYCSRELDQYGQCVAaKPESWHRDCHHLKMSIARCTSSHP 49
Cdd:pfam16860   1 DVAKHCPKEFEAYHKCVS-KNPDWPENCHELKKELAKCIKSHV 42
CHCH pfam06747
CHCH domain; we have identified a conserved motif in the LOC118487 protein that we have called ...
58-92 5.85e-04

CHCH domain; we have identified a conserved motif in the LOC118487 protein that we have called the CHCH motif. Alignment of this protein with related members showed the presence of three subgroups of proteins, which are called the S (Small), N (N-terminal extended) and C (C-terminal extended) subgroups. All three sub-groups of proteins have in common that they contain a predicted conserved [coiled coil 1]-[helix 1]-[coiled coil 2]-[helix 2] domain (CHCH domain). Within each helix of the CHCH domain, there are two cysteines present in a C-X9-C motif. The N-group contains an additional double helix domain, and each helix contains the C-X9-C motif. This family contains a number of characterized proteins: Cox19 protein - a nuclear gene of Saccharomyces cerevisiae, codes for an 11-kDa protein (Cox19p) required for expression of cytochrome oxidase. Because cox19 mutants are able to synthesize the mitochondrial and nuclear gene products of cytochrome oxidase, Cox19p probably functions post-translationally during assembly of the enzyme. Cox19p is present in the cytoplasm and mitochondria, where it exists as a soluble intermembrane protein. This dual location is similar to what was previously reported for Cox17p, a low molecular weight copper protein thought to be required for maturation of the CuA centre of subunit 2 of cytochrome oxidase. Cox19p have four conserved potential metal ligands, these are three cysteines and one histidine. Mrp10 - belongs to the class of yeast mitochondrial ribosomal proteins that are essential for translation. Eukaryotic NADH-ubiquinone oxidoreductase 19 kDa (NDUFA8) subunit. The CHCH domain was previously called DUF657.


:

Pssm-ID: 429096  Cd Length: 35  Bit Score: 34.90  E-value: 5.85e-04
                          10        20        30
                  ....*....|....*....|....*....|....*
gi 28076873    58 CAEPFEAFEKCLRLNEAAVGNCAEHMRRFLQCAEQ 92
Cdd:pfam06747   1 CGEEFKAFLKCLKDNEDELSKCRKQFDAFRQCVKK 35
 
Name Accession Description Interval E-value
CX9C pfam16860
CHCH-CHCH-like Cx9C, IMS import disulfide relay-system,; CX9C is the first half of a twin Cx9C ...
7-49 1.37e-09

CHCH-CHCH-like Cx9C, IMS import disulfide relay-system,; CX9C is the first half of a twin Cx9C motif in eukaryotic proteins. The function of this motif is to import nuclear-encoded mitochondrial intermembrane-space-proteins into the IMS (intermembrane space), as these latter lack a mitochondrial targeting sequence. The Cx9C proteins have a disulfide-bonded alpha-hairpin conformation. Cx9C-containing proteins are thus putative substrates for the Mia40-dependent thiol-disulfide exchange mechanism that carries out an oxidative folding process resulting in the proteins being trapped in the IMS.


Pssm-ID: 465284  Cd Length: 42  Bit Score: 49.62  E-value: 1.37e-09
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|...
gi 28076873     7 VTARYCSRELDQYGQCVAaKPESWHRDCHHLKMSIARCTSSHP 49
Cdd:pfam16860   1 DVAKHCPKEFEAYHKCVS-KNPDWPENCHELKKELAKCIKSHV 42
CHCH pfam06747
CHCH domain; we have identified a conserved motif in the LOC118487 protein that we have called ...
58-92 5.85e-04

CHCH domain; we have identified a conserved motif in the LOC118487 protein that we have called the CHCH motif. Alignment of this protein with related members showed the presence of three subgroups of proteins, which are called the S (Small), N (N-terminal extended) and C (C-terminal extended) subgroups. All three sub-groups of proteins have in common that they contain a predicted conserved [coiled coil 1]-[helix 1]-[coiled coil 2]-[helix 2] domain (CHCH domain). Within each helix of the CHCH domain, there are two cysteines present in a C-X9-C motif. The N-group contains an additional double helix domain, and each helix contains the C-X9-C motif. This family contains a number of characterized proteins: Cox19 protein - a nuclear gene of Saccharomyces cerevisiae, codes for an 11-kDa protein (Cox19p) required for expression of cytochrome oxidase. Because cox19 mutants are able to synthesize the mitochondrial and nuclear gene products of cytochrome oxidase, Cox19p probably functions post-translationally during assembly of the enzyme. Cox19p is present in the cytoplasm and mitochondria, where it exists as a soluble intermembrane protein. This dual location is similar to what was previously reported for Cox17p, a low molecular weight copper protein thought to be required for maturation of the CuA centre of subunit 2 of cytochrome oxidase. Cox19p have four conserved potential metal ligands, these are three cysteines and one histidine. Mrp10 - belongs to the class of yeast mitochondrial ribosomal proteins that are essential for translation. Eukaryotic NADH-ubiquinone oxidoreductase 19 kDa (NDUFA8) subunit. The CHCH domain was previously called DUF657.


Pssm-ID: 429096  Cd Length: 35  Bit Score: 34.90  E-value: 5.85e-04
                          10        20        30
                  ....*....|....*....|....*....|....*
gi 28076873    58 CAEPFEAFEKCLRLNEAAVGNCAEHMRRFLQCAEQ 92
Cdd:pfam06747   1 CGEEFKAFLKCLKDNEDELSKCRKQFDAFRQCVKK 35
 
Name Accession Description Interval E-value
CX9C pfam16860
CHCH-CHCH-like Cx9C, IMS import disulfide relay-system,; CX9C is the first half of a twin Cx9C ...
7-49 1.37e-09

CHCH-CHCH-like Cx9C, IMS import disulfide relay-system,; CX9C is the first half of a twin Cx9C motif in eukaryotic proteins. The function of this motif is to import nuclear-encoded mitochondrial intermembrane-space-proteins into the IMS (intermembrane space), as these latter lack a mitochondrial targeting sequence. The Cx9C proteins have a disulfide-bonded alpha-hairpin conformation. Cx9C-containing proteins are thus putative substrates for the Mia40-dependent thiol-disulfide exchange mechanism that carries out an oxidative folding process resulting in the proteins being trapped in the IMS.


Pssm-ID: 465284  Cd Length: 42  Bit Score: 49.62  E-value: 1.37e-09
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|...
gi 28076873     7 VTARYCSRELDQYGQCVAaKPESWHRDCHHLKMSIARCTSSHP 49
Cdd:pfam16860   1 DVAKHCPKEFEAYHKCVS-KNPDWPENCHELKKELAKCIKSHV 42
CHCH pfam06747
CHCH domain; we have identified a conserved motif in the LOC118487 protein that we have called ...
58-92 5.85e-04

CHCH domain; we have identified a conserved motif in the LOC118487 protein that we have called the CHCH motif. Alignment of this protein with related members showed the presence of three subgroups of proteins, which are called the S (Small), N (N-terminal extended) and C (C-terminal extended) subgroups. All three sub-groups of proteins have in common that they contain a predicted conserved [coiled coil 1]-[helix 1]-[coiled coil 2]-[helix 2] domain (CHCH domain). Within each helix of the CHCH domain, there are two cysteines present in a C-X9-C motif. The N-group contains an additional double helix domain, and each helix contains the C-X9-C motif. This family contains a number of characterized proteins: Cox19 protein - a nuclear gene of Saccharomyces cerevisiae, codes for an 11-kDa protein (Cox19p) required for expression of cytochrome oxidase. Because cox19 mutants are able to synthesize the mitochondrial and nuclear gene products of cytochrome oxidase, Cox19p probably functions post-translationally during assembly of the enzyme. Cox19p is present in the cytoplasm and mitochondria, where it exists as a soluble intermembrane protein. This dual location is similar to what was previously reported for Cox17p, a low molecular weight copper protein thought to be required for maturation of the CuA centre of subunit 2 of cytochrome oxidase. Cox19p have four conserved potential metal ligands, these are three cysteines and one histidine. Mrp10 - belongs to the class of yeast mitochondrial ribosomal proteins that are essential for translation. Eukaryotic NADH-ubiquinone oxidoreductase 19 kDa (NDUFA8) subunit. The CHCH domain was previously called DUF657.


Pssm-ID: 429096  Cd Length: 35  Bit Score: 34.90  E-value: 5.85e-04
                          10        20        30
                  ....*....|....*....|....*....|....*
gi 28076873    58 CAEPFEAFEKCLRLNEAAVGNCAEHMRRFLQCAEQ 92
Cdd:pfam06747   1 CGEEFKAFLKCLKDNEDELSKCRKQFDAFRQCVKK 35
 
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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