RecName: Full=Mitochondrial intermembrane space cysteine motif-containing protein MIX14; AltName: Full=Mitochondrial intermembrane space CX(n)C motif protein of 14 kDa
CX9C domain-containing protein( domain architecture ID 11245722)
CX9C domain-containing protein
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 ... |
12-53 | 2.23e-12 | ||
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: 56.94 E-value: 2.23e-12
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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 ... |
12-53 | 2.23e-12 | ||
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: 56.94 E-value: 2.23e-12
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Cyt_c_Oxidase_VIb | cd00926 | Cytochrome c oxidase subunit VIb. Cytochrome c oxidase (CcO), the terminal oxidase in the ... |
16-39 | 8.15e-03 | ||
Cytochrome c oxidase subunit VIb. Cytochrome c oxidase (CcO), the terminal oxidase in the respiratory chains of eukaryotes and most bacteria, is a multi-chain transmembrane protein located in the inner membrane of mitochondria and the cell membrane of prokaryotes. It catalyzes the reduction of O2 and simultaneously pumps protons across the membrane. The number of subunits varies from three to five in bacteria and up to 13 in mammalian mitochondria. Subunits I, II, and III of mammalian CcO are encoded within the mitochondrial genome and the remaining 10 subunits are encoded within the nuclear genome. Found only in eukaryotes, subunit VIb is one of three mammalian subunits that lacks a transmembrane region. It is located on the cytosolic side of the membrane and helps form the dimer interface with the corresponding subunit on the other monomer complex. Pssm-ID: 238466 Cd Length: 75 Bit Score: 33.05 E-value: 8.15e-03
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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 ... |
12-53 | 2.23e-12 | ||
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: 56.94 E-value: 2.23e-12
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CHCH | pfam06747 | CHCH domain; we have identified a conserved motif in the LOC118487 protein that we have called ... |
17-51 | 4.79e-05 | ||
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: 37.99 E-value: 4.79e-05
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Cyt_c_Oxidase_VIb | cd00926 | Cytochrome c oxidase subunit VIb. Cytochrome c oxidase (CcO), the terminal oxidase in the ... |
16-39 | 8.15e-03 | ||
Cytochrome c oxidase subunit VIb. Cytochrome c oxidase (CcO), the terminal oxidase in the respiratory chains of eukaryotes and most bacteria, is a multi-chain transmembrane protein located in the inner membrane of mitochondria and the cell membrane of prokaryotes. It catalyzes the reduction of O2 and simultaneously pumps protons across the membrane. The number of subunits varies from three to five in bacteria and up to 13 in mammalian mitochondria. Subunits I, II, and III of mammalian CcO are encoded within the mitochondrial genome and the remaining 10 subunits are encoded within the nuclear genome. Found only in eukaryotes, subunit VIb is one of three mammalian subunits that lacks a transmembrane region. It is located on the cytosolic side of the membrane and helps form the dimer interface with the corresponding subunit on the other monomer complex. Pssm-ID: 238466 Cd Length: 75 Bit Score: 33.05 E-value: 8.15e-03
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Blast search parameters | ||||
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