NosZ, partial [uncultured Rhodothermaceae bacterium]
Protein Classification
List of domain hits
| Name | Accession | Description | Interval | E-value | ||||
| nitrous_NosZ_Gp super family | cl30234 | nitrous-oxide reductase, Sec-dependent; This model represents the nitrous-oxide reductase ... |
1-233 | 2.58e-154 | ||||
nitrous-oxide reductase, Sec-dependent; This model represents the nitrous-oxide reductase protein NosZ as characterized in Geobacillus thermodenitrificans. In contrast to the related form in Pseudomonas stutzeri, this version lacks a recognizable twin-arginine translocation (TAT) signal at the N-terminus. Consequently, its accessory protein may differ. Some members of this family have an additional cytochrome c-like domain at the C-terminus. The actual alignment was detected with superfamily member TIGR04246: Pssm-ID: 275078 Cd Length: 578 Bit Score: 440.65 E-value: 2.58e-154
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| Name | Accession | Description | Interval | E-value | |||||
| nitrous_NosZ_Gp | TIGR04246 | nitrous-oxide reductase, Sec-dependent; This model represents the nitrous-oxide reductase ... |
1-233 | 2.58e-154 | |||||
nitrous-oxide reductase, Sec-dependent; This model represents the nitrous-oxide reductase protein NosZ as characterized in Geobacillus thermodenitrificans. In contrast to the related form in Pseudomonas stutzeri, this version lacks a recognizable twin-arginine translocation (TAT) signal at the N-terminus. Consequently, its accessory protein may differ. Some members of this family have an additional cytochrome c-like domain at the C-terminus. Pssm-ID: 275078 Cd Length: 578 Bit Score: 440.65 E-value: 2.58e-154
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| NosZ | COG4263 | Nitrous oxide reductase [Inorganic ion transport and metabolism]; |
1-233 | 4.64e-144 | |||||
Nitrous oxide reductase [Inorganic ion transport and metabolism]; Pssm-ID: 443405 [Multi-domain] Cd Length: 621 Bit Score: 415.85 E-value: 4.64e-144
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| PRK02888 | PRK02888 | nitrous-oxide reductase; Validated |
1-233 | 6.85e-66 | |||||
nitrous-oxide reductase; Validated Pssm-ID: 235082 [Multi-domain] Cd Length: 635 Bit Score: 214.84 E-value: 6.85e-66
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| nos_propeller | pfam18764 | Nitrous oxide reductase propeller repeat; Nitrous oxide reductases usually contain a ... |
37-107 | 2.17e-45 | |||||
Nitrous oxide reductase propeller repeat; Nitrous oxide reductases usually contain a seven-bladed beta-propeller domain with external short alpha-helices. This entry represents a single blade of the propeller, with imperfect alpha-helix, usually at the C-terminus of the repeat region. Pssm-ID: 436720 [Multi-domain] Cd Length: 71 Bit Score: 145.80 E-value: 2.17e-45
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| N2OR_C | cd04223 | The C-terminal cupredoxin domain of Nitrous-oxide reductase; Nitrous-oxide reductase ... |
150-233 | 8.75e-44 | |||||
The C-terminal cupredoxin domain of Nitrous-oxide reductase; Nitrous-oxide reductase participates in nitrogen metabolism and catalyzes the last step in dissimilatory nitrate reduction, the two-electron reduction of N2O to N2. It contains copper ions as cofactors in the form of a binuclear CuA center at the site of electron entry and a tetranuclear CuZ centre at the active site. The C-terminus of Nitrous-oxide reductase is a cupredoxin domain. Pssm-ID: 259885 [Multi-domain] Cd Length: 95 Bit Score: 142.37 E-value: 8.75e-44
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| Name | Accession | Description | Interval | E-value | |||||
| nitrous_NosZ_Gp | TIGR04246 | nitrous-oxide reductase, Sec-dependent; This model represents the nitrous-oxide reductase ... |
1-233 | 2.58e-154 | |||||
nitrous-oxide reductase, Sec-dependent; This model represents the nitrous-oxide reductase protein NosZ as characterized in Geobacillus thermodenitrificans. In contrast to the related form in Pseudomonas stutzeri, this version lacks a recognizable twin-arginine translocation (TAT) signal at the N-terminus. Consequently, its accessory protein may differ. Some members of this family have an additional cytochrome c-like domain at the C-terminus. Pssm-ID: 275078 Cd Length: 578 Bit Score: 440.65 E-value: 2.58e-154
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| NosZ | COG4263 | Nitrous oxide reductase [Inorganic ion transport and metabolism]; |
1-233 | 4.64e-144 | |||||
Nitrous oxide reductase [Inorganic ion transport and metabolism]; Pssm-ID: 443405 [Multi-domain] Cd Length: 621 Bit Score: 415.85 E-value: 4.64e-144
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| PRK02888 | PRK02888 | nitrous-oxide reductase; Validated |
1-233 | 6.85e-66 | |||||
nitrous-oxide reductase; Validated Pssm-ID: 235082 [Multi-domain] Cd Length: 635 Bit Score: 214.84 E-value: 6.85e-66
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| nitrous_NosZ_RR | TIGR04244 | nitrous-oxide reductase, TAT-dependent; Members of this family are the nitrous-oxide reductase ... |
1-233 | 3.52e-62 | |||||
nitrous-oxide reductase, TAT-dependent; Members of this family are the nitrous-oxide reductase structural protein, NosZ, with an N-terminal twin-arginine translocation (TAT) signal sequence (see TIGR01409). The TAT system replaces the Sec system for export of proteins with bound cofactor. Pssm-ID: 275077 Cd Length: 627 Bit Score: 204.60 E-value: 3.52e-62
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| nos_propeller | pfam18764 | Nitrous oxide reductase propeller repeat; Nitrous oxide reductases usually contain a ... |
37-107 | 2.17e-45 | |||||
Nitrous oxide reductase propeller repeat; Nitrous oxide reductases usually contain a seven-bladed beta-propeller domain with external short alpha-helices. This entry represents a single blade of the propeller, with imperfect alpha-helix, usually at the C-terminus of the repeat region. Pssm-ID: 436720 [Multi-domain] Cd Length: 71 Bit Score: 145.80 E-value: 2.17e-45
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| N2OR_C | cd04223 | The C-terminal cupredoxin domain of Nitrous-oxide reductase; Nitrous-oxide reductase ... |
150-233 | 8.75e-44 | |||||
The C-terminal cupredoxin domain of Nitrous-oxide reductase; Nitrous-oxide reductase participates in nitrogen metabolism and catalyzes the last step in dissimilatory nitrate reduction, the two-electron reduction of N2O to N2. It contains copper ions as cofactors in the form of a binuclear CuA center at the site of electron entry and a tetranuclear CuZ centre at the active site. The C-terminus of Nitrous-oxide reductase is a cupredoxin domain. Pssm-ID: 259885 [Multi-domain] Cd Length: 95 Bit Score: 142.37 E-value: 8.75e-44
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| ba3_CcO_II_C | cd13913 | C-terminal cupredoxin domain of Ba3-like heme-copper oxidase subunit II; The ba3 family of ... |
149-233 | 4.52e-09 | |||||
C-terminal cupredoxin domain of Ba3-like heme-copper oxidase subunit II; The ba3 family of heme-copper oxidases are transmembrane protein complexes in the respiratory chains of prokaryotes and some archaea, which catalyze the reduction of O2 and simultaneously pump protons across the membrane. It has been proposed that archaea acquired heme-copper oxidases through gene transfer from gram-positive bacteria. The ba3 family contains oxidases that lack the conserved residues that form the D- and K-pathways in CcO and ubiquinol oxidase. Instead, they contain a potential alternative K-pathway. Additional proton channels have been proposed for this family of oxidases but none have been identified definitively. Pssm-ID: 259980 [Multi-domain] Cd Length: 99 Bit Score: 52.19 E-value: 4.52e-09
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| CuRO_HCO_II_like | cd13842 | Cupredoxin domain of Heme-copper oxidase subunit II; Heme-copper oxidases are transmembrane ... |
153-233 | 1.86e-06 | |||||
Cupredoxin domain of Heme-copper oxidase subunit II; Heme-copper oxidases are transmembrane protein complexes in the respiratory chains of prokaryotes and mitochondria which catalyze the reduction of O2 and simultaneously pump protons across the membrane. The superfamily is diverse in terms of electron donors, subunit composition, and heme types. The number of subunits varies from two to five in bacteria and up to 13 in mammalian mitochondria. Subunits I, II, and III of mammalian cytochrome c oxidase (CcO) are encoded within the mitochondrial genome and the remaining 10 subunits are encoded within the nuclear genome. It has been proposed that archaea acquired heme-copper oxidases through gene transfer from gram-positive bacteria. Subunit II is found in CcO, ubiquinol oxidase, and the ba3-like oxidases, while the cbb3 oxidases contain alternative additional subunits. Additionally, nitrous oxide reductase contains the globular portion of subunit II as a domain within its structure. In some families, subunit II contains a copper-copper binuclear center that is involved in the transfer of electrons from the substrate to the binuclear center (active site) in subunit I. Pssm-ID: 259911 [Multi-domain] Cd Length: 95 Bit Score: 44.98 E-value: 1.86e-06
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| CuRO_HCO_II_like_3 | cd13914 | Uncharacterized subfamily with similarity to Heme-copper oxidase subunit II cupredoxin domain; ... |
176-233 | 4.51e-06 | |||||
Uncharacterized subfamily with similarity to Heme-copper oxidase subunit II cupredoxin domain; Heme-copper oxidases are transmembrane protein complexes in the respiratory chains of prokaryotes and mitochondria which catalyze the reduction of O2 and simultaneously pump protons across the membrane. The superfamily is diverse in terms of electron donors, subunit composition, and heme types. The number of subunits varies from two to five in bacteria and up to 13 in mammalian mitochondria. Subunits I, II, and III of mammalian cytochrome c oxidase (CcO) are encoded within the mitochondrial genome and the remaining 10 subunits are encoded within the nuclear genome. It has been proposed that archaea acquired heme-copper oxidases through gene transfer from gram-positive bacteria. Subunit II is found in CcO, ubiquinol oxidase, and the ba3-like oxidases, while the cbb3 oxidases contain alternative additional subunits. Additionally, nitrous oxide reductase contains the globular portion of subunit II as a domain within its structure. In some families, subunit II contains a copper-copper binuclear center that is involved in the transfer of electrons from the substrate to the binuclear center (active site) in subunit I. Pssm-ID: 259981 [Multi-domain] Cd Length: 108 Bit Score: 44.32 E-value: 4.51e-06
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| CuRO_HCO_II_like_1 | cd13916 | Uncharacterized subfamily with similarity to Heme-copper oxidase subunit II cupredoxin domain; ... |
170-233 | 1.24e-05 | |||||
Uncharacterized subfamily with similarity to Heme-copper oxidase subunit II cupredoxin domain; Heme-copper oxidases are transmembrane protein complexes in the respiratory chains of prokaryotes and mitochondria which catalyze the reduction of O2 and simultaneously pump protons across the membrane. The superfamily is diverse in terms of electron donors, subunit composition, and heme types. The number of subunits varies from two to five in bacteria and up to 13 in mammalian mitochondria. Subunits I, II, and III of mammalian cytochrome c oxidase (CcO) are encoded within the mitochondrial genome and the remaining 10 subunits are encoded within the nuclear genome. It has been proposed that archaea acquired heme-copper oxidases through gene transfer from gram-positive bacteria. Subunit II is found in CcO, ubiquinol oxidase, and the ba3-like oxidases, while the cbb3 oxidases contain alternative additional subunits. Additionally, nitrous oxide reductase contains the globular portion of subunit II as a domain within its structure. In some families, subunit II contains a copper-copper binuclear center that is involved in the transfer of electrons from the substrate to the binuclear center (active site) in subunit I. Pssm-ID: 259983 [Multi-domain] Cd Length: 93 Bit Score: 42.75 E-value: 1.24e-05
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| CuRO_HCO_II_like_4 | cd13917 | Uncharacterized subfamily with similarity to Heme-copper oxidase subunit II cupredoxin domain; ... |
153-231 | 1.79e-05 | |||||
Uncharacterized subfamily with similarity to Heme-copper oxidase subunit II cupredoxin domain; Heme-copper oxidases are transmembrane protein complexes in the respiratory chains of prokaryotes and mitochondria which catalyze the reduction of O2 and simultaneously pump protons across the membrane. The superfamily is diverse in terms of electron donors, subunit composition, and heme types. The number of subunits varies from two to five in bacteria and up to 13 in mammalian mitochondria. Subunits I, II, and III of mammalian cytochrome c oxidase (CcO) are encoded within the mitochondrial genome and the remaining 10 subunits are encoded within the nuclear genome. It has been proposed that archaea acquired heme-copper oxidases through gene transfer from gram-positive bacteria. Subunit II is found in CcO, ubiquinol oxidase, and the ba3-like oxidases, while the cbb3 oxidases contain alternative additional subunits. Additionally, nitrous oxide reductase contains the globular portion of subunit II as a domain within its structure. In some families, subunit II contains a copper-copper binuclear center that is involved in the transfer of electrons from the substrate to the binuclear center (active site) in subunit I. Pssm-ID: 259984 [Multi-domain] Cd Length: 88 Bit Score: 41.97 E-value: 1.79e-05
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| CuRO_1_CuNIR | cd11020 | Cupredoxin domain 1 of Copper-containing nitrite reductase; Copper-containing nitrite ... |
170-227 | 1.98e-05 | |||||
Cupredoxin domain 1 of Copper-containing nitrite reductase; Copper-containing nitrite reductase (CuNIR), which catalyzes the reduction of NO2- to NO, is the key enzyme in the denitrification process in denitrifying bacteria. CuNIR contains at least one type 1 copper center and a type 2 copper center, which serves as the active site of the enzyme. A histidine, bound to the Type 2 Cu center, is responsible for binding and reducing nitrite. A Cys-His bridge plays an important role in facilitating rapid electron transfer from the type 1 center to the type 2 center. A reduced type I blue copper protein (pseudoazurin) was found to be a specific electron transfer donor for the copper-containing NIR in bacteria Alcaligenes faecalis. Pssm-ID: 259906 [Multi-domain] Cd Length: 119 Bit Score: 42.58 E-value: 1.98e-05
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| Cupredoxin | cd00920 | Cupredoxin superfamily; Cupredoxins contain type I copper centers and are involved in ... |
152-233 | 4.17e-05 | |||||
Cupredoxin superfamily; Cupredoxins contain type I copper centers and are involved in inter-molecular electron transfer reactions. Cupredoxins are blue copper proteins, having an intense blue color due to the presence of a mononuclear type 1 (T1) copper site. Structurally, the cupredoxin-like fold consists of a beta-sandwich with 7 strands in 2 beta-sheets, which is arranged in a Greek-key beta-barrel. Some of these proteins have lost the ability to bind copper. The majority of family members contain multiple cupredoxin domain repeats: ceruloplasmin and the coagulation factors V/VIII have six repeats; laccase, ascorbate oxidase, spore coat protein A, and multicopper oxidase CueO contain three repeats; and nitrite reductase has two repeats. Others are mono-domain cupredoxins, such as plastocyanin, pseudoazurin, plantacyanin, azurin, rusticyanin, stellacyanin, quinol oxidase, and the periplasmic domain of cytochrome c oxidase subunit II. Pssm-ID: 259860 [Multi-domain] Cd Length: 110 Bit Score: 41.45 E-value: 4.17e-05
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| PetE | COG3794 | Plastocyanin [Energy production and conversion]; |
161-228 | 6.37e-05 | |||||
Plastocyanin [Energy production and conversion]; Pssm-ID: 443008 [Multi-domain] Cd Length: 76 Bit Score: 40.36 E-value: 6.37e-05
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| COG4454 | COG4454 | Uncharacterized copper-binding protein, cupredoxin-like subfamily [General function prediction ... |
149-228 | 1.33e-04 | |||||
Uncharacterized copper-binding protein, cupredoxin-like subfamily [General function prediction only]; Pssm-ID: 443552 [Multi-domain] Cd Length: 151 Bit Score: 41.10 E-value: 1.33e-04
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| Amicyanin | cd13921 | Amicyanin is a type I blue copper protein that plays an essential role in electron transfer; ... |
162-228 | 2.95e-03 | |||||
Amicyanin is a type I blue copper protein that plays an essential role in electron transfer; In Paracoccus denitrificans bacteria, amicyanin acts as an intermediary of a three-member redox complex along with methylamine dehydrogenase (MADH) and cytochrome c-551i. The electron is transferred from the active site of MADH via the amicyanin copper ion to the cytochrome heme iron. The electron transfer from MADH to cytochrome c-551i does not involve a ternary complex but occurs via a ping-pong mechanism in which amicyanin uses the same interface for the reactions with MADH and cytochrome c-551i. Pssm-ID: 259988 [Multi-domain] Cd Length: 81 Bit Score: 35.77 E-value: 2.95e-03
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| Copper-bind | pfam00127 | Copper binding proteins, plastocyanin/azurin family; |
162-228 | 3.53e-03 | |||||
Copper binding proteins, plastocyanin/azurin family; Pssm-ID: 395076 [Multi-domain] Cd Length: 99 Bit Score: 35.81 E-value: 3.53e-03
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| CuRO_HCO_II_like_2 | cd13915 | Uncharacterized subfamily with similarity to Heme-copper oxidase subunit II cupredoxin domain; ... |
207-231 | 4.78e-03 | |||||
Uncharacterized subfamily with similarity to Heme-copper oxidase subunit II cupredoxin domain; Heme-copper oxidases are transmembrane protein complexes in the respiratory chains of prokaryotes and mitochondria which catalyze the reduction of O2 and simultaneously pump protons across the membrane. The superfamily is diverse in terms of electron donors, subunit composition, and heme types. The number of subunits varies from two to five in bacteria and up to 13 in mammalian mitochondria. Subunits I, II, and III of mammalian cytochrome c oxidase (CcO) are encoded within the mitochondrial genome and the remaining 10 subunits are encoded within the nuclear genome. It has been proposed that archaea acquired heme-copper oxidases through gene transfer from gram-positive bacteria. Subunit II is found in CcO, ubiquinol oxidase, and the ba3-like oxidases, while the cbb3 oxidases contain alternative additional subunits. Additionally, nitrous oxide reductase contains the globular portion of subunit II as a domain within its structure. In some families, subunit II contains a copper-copper binuclear center that is involved in the transfer of electrons from the substrate to the binuclear center (active site) in subunit I. Pssm-ID: 259982 [Multi-domain] Cd Length: 98 Bit Score: 35.30 E-value: 4.78e-03
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