multicopper oxidase family protein [Vibrio furnissii]
Protein Classification
multicopper oxidase family protein( domain architecture ID 11450234)
multicopper oxidase family protein couples the one-electron oxidation of four substrate molecules to the four electron reductive cleavage of the O-O bond of dioxygen
List of domain hits
| Name | Accession | Description | Interval | E-value | |||||||
| SufI | COG2132 | Multicopper oxidase with three cupredoxin domains (includes cell division protein FtsP and ... |
20-460 | 1.33e-138 | |||||||
Multicopper oxidase with three cupredoxin domains (includes cell division protein FtsP and spore coat protein CotA) [Cell cycle control, cell division, chromosome partitioning, Inorganic ion transport and metabolism, Cell wall/membrane/envelope biogenesis; : Pssm-ID: 441735 [Multi-domain] Cd Length: 423 Bit Score: 404.32 E-value: 1.33e-138
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| TAT_signal | pfam10518 | TAT (twin-arginine translocation) pathway signal sequence; |
2-26 | 4.53e-05 | |||||||
TAT (twin-arginine translocation) pathway signal sequence; : Pssm-ID: 463131 [Multi-domain] Cd Length: 26 Bit Score: 40.05 E-value: 4.53e-05
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| Name | Accession | Description | Interval | E-value | |||||||||
| SufI | COG2132 | Multicopper oxidase with three cupredoxin domains (includes cell division protein FtsP and ... |
20-460 | 1.33e-138 | |||||||||
Multicopper oxidase with three cupredoxin domains (includes cell division protein FtsP and spore coat protein CotA) [Cell cycle control, cell division, chromosome partitioning, Inorganic ion transport and metabolism, Cell wall/membrane/envelope biogenesis; Pssm-ID: 441735 [Multi-domain] Cd Length: 423 Bit Score: 404.32 E-value: 1.33e-138
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| CuRO_1_CumA_like | cd13861 | The first cupredoxin domain of CumA like multicopper oxidase; This multicopper oxidase (MCO) ... |
38-154 | 2.79e-65 | |||||||||
The first cupredoxin domain of CumA like multicopper oxidase; This multicopper oxidase (MCO) subfamily includes CumA from Pseudomonas putida, which is involved in the oxidation of Mn(II). However, the cumA gene has been identified in a variety of bacterial species, including both Mn(II)-oxidizing and non-Mn(II)-oxidizing strains. Thus, the proteins in this family may catalyze the oxidation of other substrates. MCO catalyzes the oxidation of a variety aromatic - notably phenolic and inorganic substances coupled to the reduction of molecular oxygen to water and has been implicated in a wide spectrum of biological activities and, in particular, plays a key role in morphogenesis, development and lignin metabolism. Although MCOs have diverse functions, majority of them have three cupredoxin domain repeats that include one mononuclear and one trinuclear copper center. The copper ions are bound in several sites: Type 1, Type 2, and/or Type 3. The ensemble of types 2 and 3 copper is called a trinuclear cluster. MCOs oxidize their substrate by accepting electrons at a mononuclear copper center and transferring them to the active site trinuclear copper center. The cupredoxin domain 1 of 3-domain MCOs contains part the trinuclear copper binding site, which is located at the interface of domains 1 and 3. Pssm-ID: 259930 [Multi-domain] Cd Length: 119 Bit Score: 205.55 E-value: 2.79e-65
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| copper_res_A | TIGR01480 | copper-resistance protein, CopA family; This model represents the CopA copper resistance ... |
3-460 | 2.79e-45 | |||||||||
copper-resistance protein, CopA family; This model represents the CopA copper resistance protein family. CopA is related to laccase (benzenediol:oxygen oxidoreductase) and L-ascorbate oxidase, both copper-containing enzymes. Most members have a typical TAT (twin-arginine translocation) signal sequence with an Arg-Arg pair. Twin-arginine translocation is observed for a large number of periplasmic proteins that cross the inner membrane with metal-containing cofactors already bound. The combination of copper-binding sites and TAT translocation motif suggests a mechansism of resistance by packaging and export. [Cellular processes, Detoxification, Transport and binding proteins, Cations and iron carrying compounds] Pssm-ID: 273649 [Multi-domain] Cd Length: 587 Bit Score: 166.21 E-value: 2.79e-45
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| Cu-oxidase_3 | pfam07732 | Multicopper oxidase; This entry contains many divergent copper oxidase-like domains that are ... |
41-154 | 7.61e-40 | |||||||||
Multicopper oxidase; This entry contains many divergent copper oxidase-like domains that are not recognized by the pfam00394 model. Pssm-ID: 462247 [Multi-domain] Cd Length: 119 Bit Score: 139.30 E-value: 7.61e-40
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| PRK10965 | PRK10965 | multicopper oxidase; Provisional |
3-456 | 1.07e-38 | |||||||||
multicopper oxidase; Provisional Pssm-ID: 236810 [Multi-domain] Cd Length: 523 Bit Score: 147.09 E-value: 1.07e-38
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| TAT_signal | pfam10518 | TAT (twin-arginine translocation) pathway signal sequence; |
2-26 | 4.53e-05 | |||||||||
TAT (twin-arginine translocation) pathway signal sequence; Pssm-ID: 463131 [Multi-domain] Cd Length: 26 Bit Score: 40.05 E-value: 4.53e-05
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| Name | Accession | Description | Interval | E-value | |||||||||
| SufI | COG2132 | Multicopper oxidase with three cupredoxin domains (includes cell division protein FtsP and ... |
20-460 | 1.33e-138 | |||||||||
Multicopper oxidase with three cupredoxin domains (includes cell division protein FtsP and spore coat protein CotA) [Cell cycle control, cell division, chromosome partitioning, Inorganic ion transport and metabolism, Cell wall/membrane/envelope biogenesis; Pssm-ID: 441735 [Multi-domain] Cd Length: 423 Bit Score: 404.32 E-value: 1.33e-138
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| CuRO_1_CumA_like | cd13861 | The first cupredoxin domain of CumA like multicopper oxidase; This multicopper oxidase (MCO) ... |
38-154 | 2.79e-65 | |||||||||
The first cupredoxin domain of CumA like multicopper oxidase; This multicopper oxidase (MCO) subfamily includes CumA from Pseudomonas putida, which is involved in the oxidation of Mn(II). However, the cumA gene has been identified in a variety of bacterial species, including both Mn(II)-oxidizing and non-Mn(II)-oxidizing strains. Thus, the proteins in this family may catalyze the oxidation of other substrates. MCO catalyzes the oxidation of a variety aromatic - notably phenolic and inorganic substances coupled to the reduction of molecular oxygen to water and has been implicated in a wide spectrum of biological activities and, in particular, plays a key role in morphogenesis, development and lignin metabolism. Although MCOs have diverse functions, majority of them have three cupredoxin domain repeats that include one mononuclear and one trinuclear copper center. The copper ions are bound in several sites: Type 1, Type 2, and/or Type 3. The ensemble of types 2 and 3 copper is called a trinuclear cluster. MCOs oxidize their substrate by accepting electrons at a mononuclear copper center and transferring them to the active site trinuclear copper center. The cupredoxin domain 1 of 3-domain MCOs contains part the trinuclear copper binding site, which is located at the interface of domains 1 and 3. Pssm-ID: 259930 [Multi-domain] Cd Length: 119 Bit Score: 205.55 E-value: 2.79e-65
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| CuRO_3_CumA_like | cd13906 | The third cupredoxin domain of CumA like multicopper oxidase; This multicopper oxidase (MCO) ... |
324-460 | 3.05e-60 | |||||||||
The third cupredoxin domain of CumA like multicopper oxidase; This multicopper oxidase (MCO) subfamily includes CumA from Pseudomonas putida, which is involved in the oxidation of Mn(II). However, the cumA gene has been identified in a variety of bacterial species, including both Mn(II)-oxidizing and non-Mn(II)-oxidizing strains. Thus, the proteins in this family may catalyze the oxidation of other substrates. MCO catalyzes the oxidation of a variety aromatic - notably phenolic and inorganic substances coupled to the reduction of molecular oxygen to water and has been implicated in a wide spectrum of biological activities and, in particular, plays a key role in morphogenesis, development and lignin metabolism. Although MCOs have diverse functions, majority of them have three cupredoxin domain repeats that include one mononuclear and one trinuclear copper center. The copper ions are bound in several sites: Type 1, Type 2, and/or Type 3. The ensemble of types 2 and 3 copper is called a trinuclear cluster. MCOs oxidize their substrate by accepting electrons at a mononuclear copper center and transferring them to the active site trinuclear copper center. The cupredoxin domain 3 of 3-domain MCOs contains the Type 1 (T1) copper binding site and part the trinuclear copper binding site, which is located at the interface of domains 1 and 3. Pssm-ID: 259973 [Multi-domain] Cd Length: 138 Bit Score: 193.37 E-value: 3.05e-60
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| CuRO_1_2dMco_1 | cd13860 | The first cupredoxin domain of bacteria two domain multicopper oxidase; This subfamily ... |
37-154 | 1.99e-50 | |||||||||
The first cupredoxin domain of bacteria two domain multicopper oxidase; This subfamily includes bacterial two domain multicopper oxidases (2dMCOs) with similarity to McoN from Nitrosomonas europaea. 2dMCO is a trimeric type C blue copper oxidase. Each subunit houses a type 1 copper site in domain 1 and a type 2/type 3 trinuclear copper cluster at the subunit-subunit interface. The 2dMCO is proposed to be a key intermediate in the evolution of three domain MCOs. Multicopper oxidases couple oxidation of substrates with reduction of dioxygen to water. These MCOs are capable of oxidizing a vast range of substrates, varying from aromatic to inorganic compounds such as metals. Pssm-ID: 259929 [Multi-domain] Cd Length: 119 Bit Score: 166.99 E-value: 1.99e-50
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| copper_res_A | TIGR01480 | copper-resistance protein, CopA family; This model represents the CopA copper resistance ... |
3-460 | 2.79e-45 | |||||||||
copper-resistance protein, CopA family; This model represents the CopA copper resistance protein family. CopA is related to laccase (benzenediol:oxygen oxidoreductase) and L-ascorbate oxidase, both copper-containing enzymes. Most members have a typical TAT (twin-arginine translocation) signal sequence with an Arg-Arg pair. Twin-arginine translocation is observed for a large number of periplasmic proteins that cross the inner membrane with metal-containing cofactors already bound. The combination of copper-binding sites and TAT translocation motif suggests a mechansism of resistance by packaging and export. [Cellular processes, Detoxification, Transport and binding proteins, Cations and iron carrying compounds] Pssm-ID: 273649 [Multi-domain] Cd Length: 587 Bit Score: 166.21 E-value: 2.79e-45
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| CuRO_1_LCC_like | cd04206 | Cupredoxin domain 1 of laccase-like multicopper oxidases; including laccase, CueO, spore coat ... |
38-153 | 2.23e-42 | |||||||||
Cupredoxin domain 1 of laccase-like multicopper oxidases; including laccase, CueO, spore coat protein A, ascorbate oxidase and similar proteins; Laccase-like multicopper oxidases (MCOs) in this family contain three cupredoxin domains. They are able to couple oxidation of substrates with reduction of dioxygen to water. MCOs are capable of oxidizing a vast range of substrates, varying from aromatic to inorganic compounds such as metals. Although the members of this family have diverse functions, majority of them have three cupredoxin domain repeats. The copper ions are bound in several sites; Type 1, Type 2, and/or Type 3. The ensemble of types 2 and 3 copper is called a trinuclear cluster. MCOs oxidize their substrate by accepting electrons at a mononuclear copper center and transferring them to the active site trinuclear copper center. The cupredoxin domain 1 of 3-domain MCOs contains part the trinuclear copper binding site, which is located at the interface of domains 1 and 3. Also included in this family are cupredoxin domains 1, 3, and 5 of the 6-domain MCO ceruloplasmin and similar proteins. Pssm-ID: 259869 [Multi-domain] Cd Length: 120 Bit Score: 145.89 E-value: 2.23e-42
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| Cu-oxidase_3 | pfam07732 | Multicopper oxidase; This entry contains many divergent copper oxidase-like domains that are ... |
41-154 | 7.61e-40 | |||||||||
Multicopper oxidase; This entry contains many divergent copper oxidase-like domains that are not recognized by the pfam00394 model. Pssm-ID: 462247 [Multi-domain] Cd Length: 119 Bit Score: 139.30 E-value: 7.61e-40
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| PRK10965 | PRK10965 | multicopper oxidase; Provisional |
3-456 | 1.07e-38 | |||||||||
multicopper oxidase; Provisional Pssm-ID: 236810 [Multi-domain] Cd Length: 523 Bit Score: 147.09 E-value: 1.07e-38
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| CuRO_1_CopA | cd13848 | The first cupredoxin domain of CopA copper resistance protein family; CopA is a multicopper ... |
60-154 | 1.19e-37 | |||||||||
The first cupredoxin domain of CopA copper resistance protein family; CopA is a multicopper oxidase (MCO) related to laccase and L-ascorbate oxidase, both copper-containing enzymes. It is part of the copper-regulatory cue operon, which employs a cytosolic metalloregulatory protein CueR that induces expression of CopA and CueO under copper stress conditions. CopA is a copper efflux P-type ATPase that is located in the inner cell membrane and is involved in copper resistance in bacteria. CopA mutant causes a loss of function including copper tolerance and oxidase activity, and copA transcription is inducible in the presence of copper. Although MCOs have diverse functions, majority of them have three cupredoxin domain repeats that include one mononuclear and one trinuclear copper center. The copper ions are bound in several sites: Type 1, Type 2, and/or Type 3. The ensemble of types 2 and 3 copper is called a trinuclear cluster. MCOs oxidize their substrate by accepting electrons at a mononuclear copper center and transferring them to the active site trinuclear copper center. The cupredoxin domain 1 of 3-domain MCOs contains part the trinuclear copper binding site, which is located at the interface of domains 1 and 3. Pssm-ID: 259917 [Multi-domain] Cd Length: 116 Bit Score: 133.17 E-value: 1.19e-37
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| CuRO_1_CueO_FtsP | cd04232 | The first Cupredoxin domain of the multicopper oxidase CueO, the cell division protein FtsP, ... |
37-154 | 1.26e-32 | |||||||||
The first Cupredoxin domain of the multicopper oxidase CueO, the cell division protein FtsP, and similar proteins; CueO is a multicopper oxidase (MCO) that is part of the copper-regulatory cue operon, which employs a cytosolic metalloregulatory protein CueR that induces expression of CopA and CueO under copper stress conditions. CueO is a periplasmic multicopper oxidase that is stimulated by exogenous copper(II). FtsP (also named SufI) is a component of the cell division apparatus. It is involved in protecting or stabilizing the assembly of divisomes under stress conditions. FtsP belongs to the multicopper oxidase superfamily but lacks metal cofactors. The protein is localized at septal rings and may serve as a scaffolding function. Members of this subfamily contain three cupredoxin domains and this model represents the first domain. Although MCOs have diverse functions, majority of them have three cupredoxin domain repeats that include one mononuclear and one trinuclear copper center. The copper ions are bound in several sites: Type 1, Type 2, and/or Type 3. The ensemble of types 2 and 3 copper is called a trinuclear cluster. MCOs oxidize their substrate by accepting electrons at a mononuclear copper center and transferring them to the active site trinuclear copper center. The cupredoxin domain 1 of 3-domain MCOs contains part the trinuclear copper binding site, which is located at the interface of domains 1 and 3. FtsP does not contain any copper binding sites. Pssm-ID: 259894 [Multi-domain] Cd Length: 120 Bit Score: 119.99 E-value: 1.26e-32
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| CuRO_1_tcLCC2_insect_like | cd13858 | The first cupredoxin domain of insect laccases similar to laccase 2 in Tribolium castaneum; ... |
56-153 | 1.73e-32 | |||||||||
The first cupredoxin domain of insect laccases similar to laccase 2 in Tribolium castaneum; This multicopper oxidase (MCO) family includes the majority of insect laccases. One member of the family is laccase 2 from Tribolium castaneum. Laccase 2 is required for beetle cuticle tanning. Laccase (polyphenol oxidase EC 1.10.3.2) is a blue multi-copper enzyme that catalyzes the oxidation of a variety of organic substrates coupled to the reduction of molecular oxygen to water. It displays broad substrate specificity, catalyzing the oxidation of a wide variety of aromatic - notably phenolic and inorganic substances. Laccase has been implicated in a wide spectrum of biological activities and, in particular, plays a key role in morphogenesis, development and lignin metabolism in fungi, plants and insects. Although MCOs have diverse functions, majority of them have three cupredoxin domain repeats that include one mononuclear and one trinuclear copper center. The copper ions are bound in several sites: Type 1, Type 2, and/or Type 3. The ensemble of types 2 and 3 copper is called a trinuclear cluster. MCOs oxidize their substrate by accepting electrons at a mononuclear copper center and transferring them to the active site trinuclear copper center. The cupredoxin domain 1 of 3-domain MCOs contains part the trinuclear copper binding site, which is located at the interface of domains 1 and 3. Pssm-ID: 259927 [Multi-domain] Cd Length: 105 Bit Score: 119.18 E-value: 1.73e-32
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| ascorbase | TIGR03388 | L-ascorbate oxidase, plant type; Members of this protein family are the copper-containing ... |
51-457 | 2.50e-32 | |||||||||
L-ascorbate oxidase, plant type; Members of this protein family are the copper-containing enzyme L-ascorbate oxidase (EC 1.10.3.3), also called ascorbase. This family is found in flowering plants, and shows greater sequence similarity to a family of laccases (EC 1.10.3.2) from plants than to other known ascorbate oxidases. Pssm-ID: 274555 [Multi-domain] Cd Length: 541 Bit Score: 129.10 E-value: 2.50e-32
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| PLN02191 | PLN02191 | L-ascorbate oxidase |
57-457 | 5.30e-32 | |||||||||
L-ascorbate oxidase Pssm-ID: 177843 [Multi-domain] Cd Length: 574 Bit Score: 128.59 E-value: 5.30e-32
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| CuRO_1_McoC_like | cd13855 | The first cupredoxin domain of a multicopper oxidase McoC and similar proteins; This family ... |
40-153 | 8.81e-32 | |||||||||
The first cupredoxin domain of a multicopper oxidase McoC and similar proteins; This family includes bacteria multicopper oxidases (MCOs) represented by McoC from pathogenic bacterium Campylobacter jejuni. McoC is a periplasmic multicopper oxidase, which has been characterized to be associated with copper homeostasis. McoC may also function to protect against oxidative stress as it may convert metallic ions into their less toxic form. MCOs are multi-domain enzymes that are able to couple oxidation of substrates with reduction of dioxygen to water. They are capable of oxidizing a vast range of substrates, varying from aromatic compunds to inorganic compounds such as metals. Most MCOs have three cupredoxin domain repeats that include one mononuclear and one trinuclear copper center. The copper ions are bound in several sites: Type 1, Type 2, and/or Type 3. The ensemble of types 2 and 3 copper is called a trinuclear cluster. MCOs oxidize their substrate by accepting electrons at a mononuclear copper center and transferring them to the active site trinuclear copper center. The cupredoxin domain 1 of 3-domain MCOs contains part the trinuclear copper binding site, which is located at the interface of domains 1 and 3. Pssm-ID: 259924 [Multi-domain] Cd Length: 121 Bit Score: 117.96 E-value: 8.81e-32
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| CuRO_1_McoP_like | cd13852 | The first cupredoxin domain of multicopper oxidase McoP and similar proteins; This family ... |
67-154 | 3.00e-31 | |||||||||
The first cupredoxin domain of multicopper oxidase McoP and similar proteins; This family includes archaeal and bacterial multicopper oxidases (MCOs), represented by the extremely thermostable McoP from the hyperthermophilic archaeon Pyrobaculum aerophilum. McoP is an efficient metallo-oxidase that catalyzes the oxidation of cuprous and ferrous ions. It is noteworthy that McoP has three-fold higher catalytic efficiency when using nitrous oxide as the electron acceptor than when using dioxygen, the typical oxidizing substrate of MCOs. McoP may function as a novel archaeal nitrous oxide reductase that is probably involved in the denitrification pathway in archaea. Although MCOs have diverse functions, majority of them have three cupredoxin domain repeats that include one mononuclear and one trinuclear copper center. The copper ions are bound in several sites: Type 1, Type 2, and/or Type 3. The ensemble of types 2 and 3 copper is called a trinuclear cluster. MCOs oxidize their substrate by accepting electrons at a mononuclear copper center and transferring them to the active site trinuclear copper center. The cupredoxin domain 1 of 3-domain MCOs contains part the trinuclear copper binding site, which is located at the interface of domains 1 and 3. Pssm-ID: 259921 [Multi-domain] Cd Length: 114 Bit Score: 116.23 E-value: 3.00e-31
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| CuRO_D1_2dMcoN_like | cd13859 | The first cupredoxin domain of bacterial two domain multicopper oxidase McoN and similar ... |
38-154 | 2.28e-30 | |||||||||
The first cupredoxin domain of bacterial two domain multicopper oxidase McoN and similar proteins; This family includes bacterial two domain multicopper oxidases (2dMCOs) represented by the McoN from Nitrosomonas europaea. McoN is a trimeric type C blue copper oxidase. Each subunit houses a type 1 copper site in domain 1 and a type 2/type 3 trinuclear copper cluster at the subunit-subunit interface. The 2dMCO is proposed to be a key intermediate in the evolution of three domain MCOs. Its biological function has not been characterized. Multicopper oxidases couple oxidation of substrates with reduction of dioxygen to water. These MCOs are capable of oxidizing a vast range of substrates, varying from aromatic to inorganic compounds such as metals. Pssm-ID: 259928 [Multi-domain] Cd Length: 122 Bit Score: 114.11 E-value: 2.28e-30
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| CuRO_1_2DMCO_NIR_like | cd11024 | The cupredoxin domain 1 of a two-domain laccase related to nitrite reductase; The two-domain ... |
38-156 | 4.11e-30 | |||||||||
The cupredoxin domain 1 of a two-domain laccase related to nitrite reductase; The two-domain laccase (small laccase) in this family differs significantly from all laccases. It resembles the two domain nitrite reductase in both sequence and structure. It consists of two cupredoxin domains and forms trimers and hence resembles the quaternary structure of nitrite reductases more than that of large laccases. There are three trinuclear copper clusters in the enzyme localized between domains 1 and 2 of each pair of neighbor chains. Three copper ions of type 1 lie close to one another near the surface of the central part of the trimer, and, effectively, a trimeric substrate binding site is formed in their vicinity. Laccase is a blue multi-copper enzyme that catalyzes the oxidation of a variety of organic substrates coupled to the reduction of molecular oxygen to water. It displays broad substrate specificity, catalyzing the oxidation of a wide variety of aromatic, notably phenolic, and inorganic substances. Laccase has been implicated in a wide spectrum of biological activities. Pssm-ID: 259910 [Multi-domain] Cd Length: 119 Bit Score: 113.13 E-value: 4.11e-30
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| CuRO_1_Fet3p | cd13851 | The first Cupredoxin domain of multicopper oxidase Fet3P; Fet3p catalyzes the ferroxidase ... |
35-153 | 1.97e-28 | |||||||||
The first Cupredoxin domain of multicopper oxidase Fet3P; Fet3p catalyzes the ferroxidase reaction, which couples the oxidation of Fe(II) to Fe(III) and a four-electron reduction of molecular oxygen to water. Fet3p is a type I membrane protein with the amino-terminal oxidase domain in the exocellular space and the carboxyl terminus in the cytoplasm. The periplamic produced Fe(III) is transferred to the permease Ftr1p for import into the cytosol. The four copper ions are inserted post-translationally and are essential for catalytic activity, thus linking copper and iron homeostasis. Like other related multicopper oxidases (MCOs), Fet3p is composed of three cupredoxin domains that include one mononuclear and one trinuclear copper center. The copper ions are bound in several sites: Type 1, Type 2, and/or Type 3. The ensemble of types 2 and 3 copper is called a trinuclear cluster. MCOs oxidize their substrate by accepting electrons at a mononuclear copper center and transferring them to the active site trinuclear copper center. The cupredoxin domain 1 of 3-domain MCOs contains part the trinuclear copper binding site, which is located at the interface of domains 1 and 3. Pssm-ID: 259920 [Multi-domain] Cd Length: 121 Bit Score: 108.51 E-value: 1.97e-28
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| CuRO_1_Diphenol_Ox | cd13857 | The first cupredoxin domain of fungal laccase, diphenol oxidase; Diphenol oxidase belongs to ... |
45-153 | 3.81e-28 | |||||||||
The first cupredoxin domain of fungal laccase, diphenol oxidase; Diphenol oxidase belongs to the laccase family. It catalyzes the initial steps in melanin biosynthesis from diphenols. Melanin is one of the virulence factors of infectious fungi. In the pathogenesis of C. neoformans, melanin pigments have been shown to protect the fungal cells from oxidative and microbicidal activities of host defense systems. Laccase is a blue multicopper oxidase (MCO) which catalyzes the oxidation of a variety aromatic - notably phenolic and inorganic substances coupled to the reduction of molecular oxygen to water. It has been implicated in a wide spectrum of biological activities and, in particular, plays a key role in morphogenesis, development and lignin metabolism. Although MCOs have diverse functions, majority of them have three cupredoxin domain repeats that include one mononuclear and one trinuclear copper center. The copper ions are bound in several sites: Type 1, Type 2, and/or Type 3. The ensemble of types 2 and 3 copper is called a trinuclear cluster. MCOs oxidize their substrate by accepting electrons at a mononuclear copper center and transferring them to the active site trinuclear copper center. The cupredoxin domain 1 of 3-domain MCOs contains part the trinuclear copper binding site, which is located at the interface of domains 1 and 3. Pssm-ID: 259926 [Multi-domain] Cd Length: 119 Bit Score: 107.73 E-value: 3.81e-28
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| CuRO_1_MaLCC_like | cd13854 | The first cupredoxin domain of the fungal laccases similar to Ma-LCC from Melanocarpus ... |
45-154 | 3.91e-26 | |||||||||
The first cupredoxin domain of the fungal laccases similar to Ma-LCC from Melanocarpus albomyces; The subfamily of fungal laccases includes Ma-LCC and similar proteins. Ma-LCC is a multicopper oxidase (MCO) from Melanocarpus albomyces. Its crystal structure contains all four coppers at the mono- and trinuclear copper centers. Laccase is a blue multi-copper enzyme that catalyzes the oxidation of a variety aromatic - notably phenolic and inorganic substances coupled to the reduction of molecular oxygen to water. It has been implicated in a wide spectrum of biological activities and, in particular, plays a key role in morphogenesis, development and lignin metabolism in fungi and plants. Although MCOs have diverse functions, majority of them have three cupredoxin domain repeats that include one mononuclear and one trinuclear copper center. The copper ions are bound in several sites: Type 1, Type 2, and/or Type 3. The ensemble of types 2 and 3 copper is called a trinuclear cluster. MCOs oxidize their substrate by accepting electrons at a mononuclear copper center and transferring them to the active site trinuclear copper center. The cupredoxin domain 1 of 3-domain MCOs contains part the trinuclear copper binding site, which is located at the interface of domains 1 and 3. Pssm-ID: 259923 [Multi-domain] Cd Length: 122 Bit Score: 102.32 E-value: 3.91e-26
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| CuRO_1_AAO | cd13845 | The first cupredoxin domain of plant Ascorbate oxidase; Ascorbate oxidase catalyzes the ... |
51-154 | 8.79e-26 | |||||||||
The first cupredoxin domain of plant Ascorbate oxidase; Ascorbate oxidase catalyzes the oxidation of ascorbic acid to dehydroascorbic acid. This multicopper oxidase (MCO) is found in cucurbitaceous plants such as pumpkin, cucumber, and melon. It can detect levels of ascorbic acid and eliminate it. The biological function of ascorbate oxidase is still not clear. Ascorbate oxidase belongs to MCO family which couple oxidation of substrates with reduction of dioxygen to water. MCOs are capable of oxidizing a vast range of substrates, varying from aromatic compounds to inorganic compounds such as metals. Although the members of this family have diverse functions, majority of them have three cupredoxin domain repeats. The copper ions are bound in several sites: Type 1, Type 2, and/or Type 3. The ensemble of types 2 and 3 copper is called a trinuclear cluster. MCOs oxidize their substrate by accepting electrons at a mononuclear copper center and transferring them to the active site trinuclear copper center. The cupredoxin domain 1 of 3-domain MCOs contains part the trinuclear copper binding site, which is located at the interface of domains 1 and 3. Pssm-ID: 259914 [Multi-domain] Cd Length: 120 Bit Score: 101.37 E-value: 8.79e-26
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| CuRO_1_LCC_like_3 | cd13865 | The second cupredoxin domain of uncharacterized multicopper oxidase; Multicopper Oxidases ... |
57-152 | 1.17e-25 | |||||||||
The second cupredoxin domain of uncharacterized multicopper oxidase; Multicopper Oxidases (MCOs) are multi-domain enzymes that are able to couple oxidation of substrates with reduction of dioxygen to water. MCOs oxidize their substrate by accepting electrons at a mononuclear copper centre and transferring them to a trinuclear copper centre which binds a dioxygen. The dioxygen, following the transfer of four electrons, is reduced to two molecules of water. These MCOs are capable of oxidizing a vast range of substrates, varying from aromatic to inorganic compounds such as metals. This subfamily of MCOs is composed of three cupredoxin domains. The cupredoxin domain 1 of 3-domain MCOs contains part the trinuclear copper binding site, which is located at the interface of domains 1 and 3. Pssm-ID: 259933 [Multi-domain] Cd Length: 115 Bit Score: 100.85 E-value: 1.17e-25
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| CuRO_1_Tth-MCO_like | cd13853 | The first cupredoxin domain of the bacterial laccases similar to Tth-MCO from Thermus ... |
37-154 | 1.60e-25 | |||||||||
The first cupredoxin domain of the bacterial laccases similar to Tth-MCO from Thermus Thermophilus; The subfamily of bacterial laccases includes Tth-MCO and similar proteins. Tth-MCO is a hyperthermophilic multicopper oxidase (MCO) from thermus thermophilus HB27. Laccase is a blue multi-copper enzyme that catalyzes the oxidation of a variety aromatic - notably phenolic and inorganic substances coupled to the reduction of molecular oxygen to water. It has been implicated in a wide spectrum of biological activities and, in particular, plays a key role in morphogenesis, development and lignin metabolism in fungi and plants. Although MCOs have diverse functions, majority of them have three cupredoxin domain repeats that include one mononuclear and one trinuclear copper center. The copper ions are bound in several sites: Type 1, Type 2, and/or Type 3. The ensemble of types 2 and 3 copper is called a trinuclear cluster. MCOs oxidize their substrate by accepting electrons at a mononuclear copper center and transferring them to the active site trinuclear copper center. The cupredoxin domain 1 of 3-domain MCOs contains part the trinuclear copper binding site, which is located at the interface of domains 1 and 3. Pssm-ID: 259922 [Multi-domain] Cd Length: 139 Bit Score: 101.18 E-value: 1.60e-25
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| CuRO_1_Tv-LCC_like | cd13856 | The first cupredoxin domain of fungal laccases similar to Tv-LCC from Trametes versicolor; ... |
41-154 | 3.48e-25 | |||||||||
The first cupredoxin domain of fungal laccases similar to Tv-LCC from Trametes versicolor; This subfamily of fungal laccases includes Tv-LCC from Trametes versicolor and Rs-LCC2 from plant pathogenic fungus Rhizoctonia solani. Laccase is a blue multi-copper enzyme that catalyzes the oxidation of a variety aromatic - notably phenolic and inorganic substances coupled to the reduction of molecular oxygen to water. It has been implicated in a wide spectrum of biological activities and, in particular, plays a key role in morphogenesis, development and lignin metabolism. Although MCOs have diverse functions, majority of them have three cupredoxin domain repeats that include one mononuclear and one trinuclear copper center. The copper ions are bound in several sites: Type 1, Type 2, and/or Type 3. The ensemble of types 2 and 3 copper is called a trinuclear cluster. MCOs oxidize their substrate by accepting electrons at a mononuclear copper center and transferring them to the active site trinuclear copper center. The cupredoxin domain 1 of 3-domain MCOs contains part the trinuclear copper binding site, which is located at the interface of domains 1 and 3. Pssm-ID: 259925 [Multi-domain] Cd Length: 125 Bit Score: 99.72 E-value: 3.48e-25
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| CuRO_1_MCO_like_1 | cd13862 | The first cupredoxin domain of uncharacterized multicopper oxidase; Multicopper Oxidases (MCOs) ... |
37-154 | 2.53e-24 | |||||||||
The first cupredoxin domain of uncharacterized multicopper oxidase; Multicopper Oxidases (MCOs) are multi-domain enzymes that are able to couple oxidation of substrates with reduction of dioxygen to water. MCOs oxidize their substrate by accepting electrons at a mononuclear copper centre and transferring them to a trinuclear copper centre which binds a dioxygen. The dioxygen, following the transfer of four electrons, is reduced to two molecules of water. These MCOs are capable of oxidizing a vast range of substrates, varying from aromatic to inorganic compounds such as metals. This subfamily of MCOs is composed of three cupredoxin domains. The cupredoxin domain 1 of 3-domain MCOs contains part the trinuclear copper binding site, which is located at the interface of domains 1 and 3. Pssm-ID: 259931 [Multi-domain] Cd Length: 123 Bit Score: 97.59 E-value: 2.53e-24
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| CuRO_3_LCC_like | cd04207 | Cupredoxin domain 3 of laccase-like multicopper oxidases; including laccase, CueO, spore coat ... |
351-458 | 2.67e-24 | |||||||||
Cupredoxin domain 3 of laccase-like multicopper oxidases; including laccase, CueO, spore coat protein A, ascorbate oxidase and similar proteins; Laccase-like multicopper oxidases (MCOs) in this family contain three cupredoxin domains. They are able to couple oxidation of substrates with reduction of dioxygen to water. MCOs are capable of oxidizing a vast range of substrates, varying from aromatic to inorganic compounds such as metals. Although the members of this family have diverse functions, majority of them have three cupredoxin domain repeats. The copper ions are bound in several sites; Type 1, Type 2, and/or Type 3. The ensemble of types 2 and 3 copper is called a trinuclear cluster. MCOs oxidize their substrate by accepting electrons at a mononuclear copper center and transferring them to the active site trinuclear copper center. The cupredoxin domain 3 of 3-domain MCOs contains the Type 1 (T1) copper binding site and part the trinuclear copper binding site, which is located at the interface of domains 1 and 3. Also included in this family are cupredoxin domains 2, 4, and 6 of the 6-domain MCO ceruloplasmin and similar proteins. Pssm-ID: 259870 [Multi-domain] Cd Length: 132 Bit Score: 97.53 E-value: 2.67e-24
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| Cu-oxidase_2 | pfam07731 | Multicopper oxidase; This entry contains many divergent copper oxidase-like domains that are ... |
344-458 | 2.98e-24 | |||||||||
Multicopper oxidase; This entry contains many divergent copper oxidase-like domains that are not recognized by the pfam00394 model. Pssm-ID: 462246 [Multi-domain] Cd Length: 138 Bit Score: 97.89 E-value: 2.98e-24
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| CuRO_1_Abr2_like | cd13850 | The first cupredoxin domain of a group of fungal Laccases similar to Abr2 from Aspergillus ... |
61-153 | 8.03e-24 | |||||||||
The first cupredoxin domain of a group of fungal Laccases similar to Abr2 from Aspergillus fumigatus; Abr2 is involved in conidial pigment biosynthesis in Aspergillus fumigatus. Laccase is a blue multi-copper enzyme that catalyzes the oxidation of a variety aromatic - notably phenolic and inorganic substances coupled to the reduction of molecular oxygen to water. Laccase has been implicated in a wide spectrum of biological activities and, in particular, plays a key role in morphogenesis, development and lignin metabolism in fungi and plants. Like other related multicopper oxidases (MCOs), laccase is composed of three cupredoxin domains that include one mononuclear and one trinuclear copper center. The copper ions are bound in several sites: Type 1, Type 2, and/or Type 3. The ensemble of types 2 and 3 copper is called a trinuclear cluster. MCOs oxidize their substrate by accepting electrons at a mononuclear copper center and transferring them to the active site trinuclear copper center. The cupredoxin domain 1 of 3-domain MCOs contains part the trinuclear copper binding site, which is located at the interface of domains 1 and 3. Pssm-ID: 259919 [Multi-domain] Cd Length: 117 Bit Score: 95.83 E-value: 8.03e-24
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| ascorbOXfungal | TIGR03390 | L-ascorbate oxidase, fungal type; This model describes a family of fungal ascorbate oxidases, ... |
33-459 | 1.29e-23 | |||||||||
L-ascorbate oxidase, fungal type; This model describes a family of fungal ascorbate oxidases, within a larger family of multicopper oxidases that also includes plant ascorbate oxidases (TIGR03388), plant laccases and laccase-like proteins (TIGR03389), and related proteins. The member from Acremonium sp. HI-25 is characterized. Pssm-ID: 132431 [Multi-domain] Cd Length: 538 Bit Score: 103.38 E-value: 1.29e-23
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| PLN02604 | PLN02604 | oxidoreductase |
51-457 | 1.45e-23 | |||||||||
oxidoreductase Pssm-ID: 215324 [Multi-domain] Cd Length: 566 Bit Score: 103.40 E-value: 1.45e-23
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| laccase | TIGR03389 | laccase, plant; Members of this protein family include the copper-containing enzyme laccase ... |
54-457 | 2.11e-23 | |||||||||
laccase, plant; Members of this protein family include the copper-containing enzyme laccase (EC 1.10.3.2), often several from a single plant species, and additional, uncharacterized, closely related plant proteins termed laccase-like multicopper oxidases. This protein family shows considerable sequence similarity to the L-ascorbate oxidase (EC 1.10.3.3) family. Laccases are enzymes of rather broad specificity, and classification of all proteins scoring about the trusted cutoff of this model as laccases may be appropriate. Pssm-ID: 274556 [Multi-domain] Cd Length: 539 Bit Score: 102.89 E-value: 2.11e-23
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| CuRO_3_MCO_like_3 | cd13909 | The third cupredoxin domain of uncharacterized multicopper oxidase; Multicopper Oxidases (MCOs) ... |
349-460 | 1.14e-22 | |||||||||
The third cupredoxin domain of uncharacterized multicopper oxidase; Multicopper Oxidases (MCOs) are multi-domain enzymes that are able to couple oxidation of substrates with reduction of dioxygen to water. MCOs oxidize their substrate by accepting electrons at a mononuclear copper centre and transferring them to a trinuclear copper centre which binds a dioxygen. The dioxygen, following the transfer of four electrons, is reduced to two molecules of water. These MCOs are capable of oxidizing a vast range of substrates, varying from aromatic to inorganic compounds such as metals. This subfamily of MCOs is composed of three cupredoxin domains. The cupredoxin domain 3 of 3-domain MCOs contains the Type 1 (T1) copper binding site and part the trinuclear copper binding site, which is located at the interface of domains 1 and 3. Pssm-ID: 259976 [Multi-domain] Cd Length: 137 Bit Score: 93.35 E-value: 1.14e-22
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| CuRO_1_MCO_like_2 | cd13864 | The second cupredoxin domain of uncharacterized multicopper oxidase; Multicopper Oxidases ... |
59-154 | 5.09e-22 | |||||||||
The second cupredoxin domain of uncharacterized multicopper oxidase; Multicopper Oxidases (MCOs) are multi-domain enzymes that are able to couple oxidation of substrates with reduction of dioxygen to water. MCOs oxidize their substrate by accepting electrons at a mononuclear copper centre and transferring them to a trinuclear copper centre which binds a dioxygen. The dioxygen, following the transfer of four electrons, is reduced to two molecules of water. These MCOs are capable of oxidizing a vast range of substrates, varying from aromatic to inorganic compounds such as metals. This subfamily of MCOs is composed of three cupredoxin domains. The cupredoxin domain 1 of 3-domain MCOs contains part the trinuclear copper binding site, which is located at the interface of domains 1 and 3. Pssm-ID: 259932 [Multi-domain] Cd Length: 139 Bit Score: 91.44 E-value: 5.09e-22
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| CuRO_3_CopA | cd13896 | The third cupredoxin domain of CopA copper resistance protein family; CopA is a multicopper ... |
344-459 | 1.43e-21 | |||||||||
The third cupredoxin domain of CopA copper resistance protein family; CopA is a multicopper oxidase (MCO) related to laccase and L-ascorbate oxidase, both copper-containing enzymes. It is part of the copper-regulatory cue operon, which employs a cytosolic metalloregulatory protein CueR that induces expression of CopA and CueO under copper stress conditions. CopA is a copper efflux P-type ATPase that is located in the inner cell membrane and is is involved in copper resistance in bacteria. CopA mutant causes a loss of function including copper tolerance and oxidase activity and copA transcription is inducible in the presence of copper. Although MCOs have diverse functions, majority of them have three cupredoxin domain repeats that include one mononuclear and one trinuclear copper center. The copper ions are bound in several sites: Type 1, Type 2, and/or Type 3. The ensemble of types 2 and 3 copper is called a trinuclear cluster. MCOs oxidize their substrate by accepting electrons at a mononuclear copper center and transferring them to the active site trinuclear copper center. The cupredoxin domain 3 of 3-domain MCOs contains the Type 1 (T1) copper binding site and part the trinuclear copper binding site, which is located at the interface of domains 1 and 3. Pssm-ID: 259963 [Multi-domain] Cd Length: 115 Bit Score: 89.62 E-value: 1.43e-21
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| CuRO_D2_2dMcoN_like | cd04202 | The second cupredoxin domain of bacterial two domain multicopper oxidase McoN and similar ... |
328-459 | 8.91e-21 | |||||||||
The second cupredoxin domain of bacterial two domain multicopper oxidase McoN and similar proteins; This family includes bacterial two domain multicopper oxidases (2dMCOs) represented by the McoN from Nitrosomonas europaea. McoN is a trimeric type C blue copper oxidase. Each subunit houses a type 1 copper site in domain 1 and a type 2/type 3 trinuclear copper cluster at the subunit-subunit interface. The 2dMCO is proposed to be a key intermediate in the evolution of three domain MCOs. The biological function of McoN has not been characterized. Multicopper oxidases couple oxidation of substrates with reduction of dioxygen to water. These MCOs are capable of oxidizing a vast range of substrates, varying from aromatic to inorganic compounds such as metals. Pssm-ID: 259865 [Multi-domain] Cd Length: 138 Bit Score: 88.08 E-value: 8.91e-21
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| CuRO_3_MCO_like_2 | cd13908 | The third cupredoxin domain of uncharacterized multicopper oxidase; Multicopper Oxidases (MCOs) ... |
324-459 | 9.22e-21 | |||||||||
The third cupredoxin domain of uncharacterized multicopper oxidase; Multicopper Oxidases (MCOs) are multi-domain enzymes that are able to couple oxidation of substrates with reduction of dioxygen to water. MCOs oxidize their substrate by accepting electrons at a mononuclear copper centre and transferring them to a trinuclear copper centre which binds a dioxygen. The dioxygen, following the transfer of four electrons, is reduced to two molecules of water. These MCOs are capable of oxidizing a vast range of substrates, varying from aromatic to inorganic compounds such as metals. This subfamily of MCOs is composed of three cupredoxin domains. The cupredoxin domain 3 of 3-domain MCOs contains the Type 1 (T1) copper binding site and part the trinuclear copper binding site, which is located at the interface of domains 1 and 3. Pssm-ID: 259975 [Multi-domain] Cd Length: 122 Bit Score: 87.51 E-value: 9.22e-21
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| CuRO_3_McoC_like | cd13902 | The third cupredoxin domain of a multicopper oxidase McoC and similar proteins; This family ... |
375-459 | 2.80e-19 | |||||||||
The third cupredoxin domain of a multicopper oxidase McoC and similar proteins; This family includes bacteria multicopper oxidases (MCOs) represented by McoC from pathogenic bacterium Campylobacter jejuni. McoC is a periplasmic multicopper oxidase, which has been characterized to be associated with copper homeostasis. McoC may also function to protect against oxidative stress as it may convert metallic ions into their less toxic form. MCOs are multi-domain enzymes that are able to couple oxidation of substrates with reduction of dioxygen to water. They are capable of oxidizing a vast range of substrates, varying from aromatic compunds to inorganic compounds such as metals. Most MCOs have three cupredoxin domain repeats that include one mononuclear and one trinuclear copper center. The copper ions are bound in several sites: Type 1, Type 2, and/or Type 3. The ensemble of types 2 and 3 copper is called a trinuclear cluster. MCOs oxidize their substrate by accepting electrons at a mononuclear copper center and transferring them to the active site trinuclear copper center. The cupredoxin domain 3 of 3-domain MCOs contains the Type 1 (T1) copper binding site and part the trinuclear copper binding site, which is located at the interface of domains 1 and 3. Pssm-ID: 259969 [Multi-domain] Cd Length: 125 Bit Score: 83.60 E-value: 2.80e-19
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| CuRO_1_AAO_like_2 | cd13847 | The first cupredoxin domain of Ascorbate oxidase homologs; This family includes fungal ... |
45-137 | 2.82e-19 | |||||||||
The first cupredoxin domain of Ascorbate oxidase homologs; This family includes fungal proteins with similarity to ascorbate oxidase. Ascorbate oxidase catalyzes the oxidation of ascorbic acid to dehydroascorbic acid. It can detect levels of ascorbic acid and eliminate it. The biological function of ascorbate oxidase is still not clear. Ascorbate oxidase belongs to multicopper oxidase (MCO) family which couple oxidation of substrates with reduction of dioxygen to water. MCOs are capable of oxidizing a vast range of substrates, varying from aromatic compounds to inorganic compounds such as metals. Although the members of this family have diverse functions, majority of them have three cupredoxin domain repeats. The copper ions are bound in several sites: Type 1, Type 2, and/or Type 3. The ensemble of types 2 and 3 copper is called a trinuclear cluster. MCOs oxidize their substrate by accepting electrons at a mononuclear copper center and transferring them to the active site trinuclear copper center. The cupredoxin domain 1 of 3-domain MCOs contains part the trinuclear copper binding site, which is located at the interface of domains 1 and 3. Pssm-ID: 259916 [Multi-domain] Cd Length: 117 Bit Score: 83.35 E-value: 2.82e-19
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| CuRO_1_LCC_plant | cd13849 | The first cupredoxin domain of plant laccases; Laccase is a blue multicopper oxidase (MCO) ... |
54-136 | 6.91e-19 | |||||||||
The first cupredoxin domain of plant laccases; Laccase is a blue multicopper oxidase (MCO) which catalyzes the oxidation of a variety aromatic - notably phenolic and inorganic substances coupled to the reduction of molecular oxygen to water. Laccase has been implicated in a wide spectrum of biological activities and, in particular, plays a key role in morphogenesis, development and lignin metabolism. Plants usually express multiple laccase genes, but their precise physiological/biochemical roles remain largely unclear. MCOs are capable of oxidizing a vast range of substrates, varying from aromatic compounds to inorganic compounds such as metals. Although the members of this family have diverse functions, majority of them have three cupredoxin domain repeats. The copper ions are bound in several sites: Type 1, Type 2, and/or Type 3. The ensemble of types 2 and 3 copper is called a trinuclear cluster. MCOs oxidize their substrate by accepting electrons at a mononuclear copper center and transferring them to the active site trinuclear copper center. The cupredoxin domain 1 of 3-domain MCOs contains part the trinuclear copper binding site, which is located at the interface of domains 1 and 3. Pssm-ID: 259918 [Multi-domain] Cd Length: 117 Bit Score: 81.92 E-value: 6.91e-19
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| CuRO_2_CumA_like | cd13885 | The second cupredoxin domain of CumA like multicopper oxidase; This multicopper oxidase (MCO) ... |
167-291 | 1.17e-17 | |||||||||
The second cupredoxin domain of CumA like multicopper oxidase; This multicopper oxidase (MCO) subfamily includes CumA from Pseudomonas putida. CumA is involved in the oxidation of Mn(II) in Pseudomonas putida; however, the cumA gene has been identified in a variety of bacterial species, including both Mn(II)-oxidizing and non-Mn(II)-oxidizing strains. Thus, the proteins in this family may catalyze the oxidation of other substrates. MCOs catalyze the oxidation of a variety aromatic - notably phenolic and inorganic substances coupled to the reduction of molecular oxygen to water and has been implicated in a wide spectrum of biological activities and, in particular, plays a key role in morphogenesis, development and lignin metabolism. The MCOs in this subfamily are composed of three cupredoxin domains that include one mononuclear and one trinuclear copper center. The copper ions are bound in several sites: Type 1, Type 2, and/or Type 3. The ensemble of types 2 and 3 copper is called a trinuclear cluster. MCOs oxidize their substrate by accepting electrons at a mononuclear copper center and transferring them to the active site trinuclear copper center. The cupredoxin domain 2 of 3-domain MCOs has lost the ability to bind copper. Pssm-ID: 259952 [Multi-domain] Cd Length: 132 Bit Score: 78.91 E-value: 1.17e-17
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| PLN02354 | PLN02354 | copper ion binding / oxidoreductase |
57-224 | 1.73e-16 | |||||||||
copper ion binding / oxidoreductase Pssm-ID: 177987 [Multi-domain] Cd Length: 552 Bit Score: 81.76 E-value: 1.73e-16
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| PRK10883 | PRK10883 | FtsI repressor; Provisional |
1-268 | 6.92e-16 | |||||||||
FtsI repressor; Provisional Pssm-ID: 182808 [Multi-domain] Cd Length: 471 Bit Score: 79.75 E-value: 6.92e-16
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| CuRO_3_tcLLC2_insect_like | cd13905 | The third cupredoxin domain of the insect laccases similar to laccase 2 in Tribolium castaneum; ... |
372-457 | 2.52e-15 | |||||||||
The third cupredoxin domain of the insect laccases similar to laccase 2 in Tribolium castaneum; This multicopper oxidase (MCO) family includes the majority of insect laccases. One member of the family is laccase 2 from Tribolium castaneum. Laccase 2 is required for beetle cuticle tanning. Laccase (polyphenol oxidase EC 1.10.3.2) is a blue multi-copper enzyme that catalyzes the oxidation of a variety of organic substrates coupled to the reduction of molecular oxygen to water. It displays broad substrate specificity, catalyzing the oxidation of a wide variety of aromatic - notably phenolic and inorganic substances. Laccase has been implicated in a wide spectrum of biological activities and, in particular, plays a key role in morphogenesis, development and lignin metabolism in fungi, plants and insects. Although MCOs have diverse functions, majority of them have three cupredoxin domain repeats that include one mononuclear and one trinuclear copper center. The copper ions are bound in several sites: Type 1, Type 2, and/or Type 3. The ensemble of types 2 and 3 copper is called a trinuclear cluster. MCOs oxidize their substrate by accepting electrons at a mononuclear copper center and transferring them to the active site trinuclear copper center. The cupredoxin domain 3 of 3-domain MCOs contains the Type 1 (T1) copper binding site and part the trinuclear copper binding site, which is located at the interface of domains 1 and 3. Pssm-ID: 259972 [Multi-domain] Cd Length: 174 Bit Score: 73.48 E-value: 2.52e-15
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| CuRO_3_CueO_FtsP | cd13890 | The third Cupredoxin domain of the multicopper oxidase CueO, the cell division protein FtsP, ... |
375-459 | 2.97e-14 | |||||||||
The third Cupredoxin domain of the multicopper oxidase CueO, the cell division protein FtsP, and similar proteins; CueO is a multicopper oxidase (MCO) that is part of the copper-regulatory cue operon, which employs a cytosolic metalloregulatory protein CueR that induces expression of CopA and CueO under copper stress conditions. CueO is a periplasmic multicopper oxidase that is stimulated by exogenous copper(II). FtsP (also named SufI) is a component of the cell division apparatus. It is involved in protecting or stabilizing the assembly of divisomes under stress conditions. FtsP belongs to the multicopper oxidase superfamily but lacks metal cofactors. The protein is localized at septal rings and may serve as a scaffolding function. Members of this subfamily contain three cupredoxin domains and this model represents the first domain. Although MCOs have diverse functions, majority of them have three cupredoxin domain repeats that include one mononuclear and one trinuclear copper center. The copper ions are bound in several sites: Type 1, Type 2, and/or Type 3. The ensemble of types 2 and 3 copper is called a trinuclear cluster. MCOs oxidize their substrate by accepting electrons at a mononuclear copper center and transferring them to the active site trinuclear copper center. The cupredoxin domain 3 of 3-domain MCOs contains the Type 1 (T1) copper binding site and part the trinuclear copper binding site, which is located at the interface of domains 1 and 3. FtsP does not contain any copper binding sites. Pssm-ID: 259957 [Multi-domain] Cd Length: 124 Bit Score: 69.20 E-value: 2.97e-14
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| CuRO_1_CuNIR | cd11020 | Cupredoxin domain 1 of Copper-containing nitrite reductase; Copper-containing nitrite ... |
60-154 | 9.52e-14 | |||||||||
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: 67.62 E-value: 9.52e-14
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| CuRO_3_Fet3p | cd13899 | The third Cupredoxin domain of multicopper oxidase Fet3p; Fet3p catalyzes the ferroxidase ... |
391-458 | 1.02e-13 | |||||||||
The third Cupredoxin domain of multicopper oxidase Fet3p; Fet3p catalyzes the ferroxidase reaction, which couples the oxidation of Fe(II) to Fe(III) with the four-electron reduction of molecular oxygen to water. Fet3p is a type I membrane protein with the amino-terminal oxidase domain in the extracellular space and the carboxyl terminus in the cytoplasm. The periplasmic produced Fe(III) is transferred to the permease Ftr1p for import into the cytosol. The four copper ions are inserted post-translationally and are essential for catalytic activity, thus linking copper and iron homeostasis. Like other related multicopper oxidases (MCOs), Fet3p is composed of three cupredoxin domains that include one mononuclear and one trinuclear copper center. The copper ions are bound in several sites: Type 1, Type 2, and/or Type 3. The ensemble of types 2 and 3 copper is called a trinuclear cluster. MCOs oxidize their substrate by accepting electrons at a mononuclear copper center and transferring them to the active site trinuclear copper center. The cupredoxin domain 3 of 3-domain MCOs contains the Type 1 (T1) copper binding site and part the trinuclear copper binding site, which is located at the interface of domains 1 and 3. Pssm-ID: 259966 [Multi-domain] Cd Length: 160 Bit Score: 68.82 E-value: 1.02e-13
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| CuRO_1_CuNIR_like | cd04201 | Cupredoxin domain 1 of Copper-containing nitrite reductase and two-domain laccase; ... |
60-154 | 1.06e-13 | |||||||||
Cupredoxin domain 1 of Copper-containing nitrite reductase and two-domain laccase; 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. The two-domain laccase (small laccase) in this family differs significantly from all laccases. It resembles two domain nitrite reductase in both sequence homology and structure similarity. It consists of two domains and forms trimers and hence resembles the quaternary structure of nitrite reductases more than that of larger laccases. Pssm-ID: 259864 [Multi-domain] Cd Length: 120 Bit Score: 67.52 E-value: 1.06e-13
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| CuRO_1_Ceruloplasmin_like_1 | cd04229 | cupredoxin domain of ceruloplasmin homologs; Uncharacterized subfamily of ceruloplasmin ... |
53-156 | 6.78e-13 | |||||||||
cupredoxin domain of ceruloplasmin homologs; Uncharacterized subfamily of ceruloplasmin homologous proteins. Ceruloplasmin (ferroxidase) is a multicopper oxidase essential for normal iron homeostasis. Ceruloplasmin also functions in copper transport, amine oxidase and as an antioxidant preventing free radicals in serum. The protein has 6 cupredoxin domains and exhibits internal sequence homology that appears to have evolved from the triplication of a sequence unit composed of two tandem cupredoxin domains. This model represents the first domain of the triplicated units. Pssm-ID: 259891 [Multi-domain] Cd Length: 175 Bit Score: 66.67 E-value: 6.78e-13
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| CuRO_3_MCO_like_4 | cd13910 | The third cupredoxin domain of uncharacterized multicopper oxidase; Multicopper Oxidases (MCOs) ... |
391-458 | 9.99e-13 | |||||||||
The third cupredoxin domain of uncharacterized multicopper oxidase; Multicopper Oxidases (MCOs) are multi-domain enzymes that are able to couple oxidation of substrates with reduction of dioxygen to water. MCOs oxidize their substrate by accepting electrons at a mononuclear copper centre and transferring them to a trinuclear copper centre which binds a dioxygen. The dioxygen, following the transfer of four electrons, is reduced to two molecules of water. These MCOs are capable of oxidizing a vast range of substrates, varying from aromatic to inorganic compounds such as metals. This subfamily of MCOs is composed of three cupredoxin domains. The cupredoxin domain 3 of 3-domain MCOs contains the Type 1 (T1) copper binding site and part the trinuclear copper binding site, which is located at the interface of domains 1 and 3. Pssm-ID: 259977 [Multi-domain] Cd Length: 166 Bit Score: 66.17 E-value: 9.99e-13
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| CuRO_3_Tth-MCO_like | cd13900 | The third cupredoxin domain of the bacterial laccases similar to Tth-MCO from Thermus ... |
367-459 | 1.49e-12 | |||||||||
The third cupredoxin domain of the bacterial laccases similar to Tth-MCO from Thermus Thermophilus; The subfamily of bacterial laccases includes Tth-MCO and similar proteins. Tth-MCO is a hyperthermophilic multicopper oxidase (MCO) from thermus thermophilus HB27. Laccase is a blue multi-copper enzyme that catalyzes the oxidation of a variety aromatic - notably phenolic and inorganic substances coupled to the reduction of molecular oxygen to water. It has been implicated in a wide spectrum of biological activities and, in particular, plays a key role in morphogenesis, development and lignin metabolism in fungi and plants. Although MCOs have diverse functions, majority of them have three cupredoxin domain repeats that include one mononuclear and one trinuclear copper center. The copper ions are bound in several sites: Type 1, Type 2, and/or Type 3. The ensemble of types 2 and 3 copper is called a trinuclear cluster. MCOs oxidize their substrate by accepting electrons at a mononuclear copper center and transferring them to the active site trinuclear copper center. The cupredoxin domain 3 of 3-domain MCOs contains the Type 1 (T1) copper binding site and part the trinuclear copper binding site, which is located at the interface of domains 1 and 3. Pssm-ID: 259967 [Multi-domain] Cd Length: 123 Bit Score: 64.19 E-value: 1.49e-12
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| CuRO_1_AAO_like_1 | cd13846 | The first cupredoxin domain of plant Ascorbate oxidase homologs; This subfamily is composed of ... |
57-152 | 5.89e-12 | |||||||||
The first cupredoxin domain of plant Ascorbate oxidase homologs; This subfamily is composed of plant pollen multicopper oxidase homologous to ascorbate oxidase. Ascorbate oxidase catalyzes the oxidation of ascorbic acid to dehydroascorbic acid. This multicopper oxidase (MCO) is found in cucurbitaceous plants such as pumpkin, cucumber, and melon. It can detect levels of ascorbic acid and eliminate it. The biological function of ascorbate oxidase is still not clear. Ascorbate oxidase belongs to MCO family which couple oxidation of substrates with reduction of dioxygen to water. MCOs are capable of oxidizing a vast range of substrates, varying from aromatic compounds to inorganic compounds such as metals. Although the members of this family have diverse functions, majority of them have three cupredoxin domain repeats. The copper ions are bound in several sites: Type 1, Type 2, and/or Type 3. The ensemble of types 2 and 3 copper is called a trinuclear cluster. MCOs oxidize their substrate by accepting electrons at a mononuclear copper center and transferring them to the active site trinuclear copper center. The cupredoxin domain 1 of 3-domain MCOs contains part the trinuclear copper binding site, which is located at the interface of domains 1 and 3. This subfamily does not harbor trinuclear copper binding histidines. Pssm-ID: 259915 [Multi-domain] Cd Length: 118 Bit Score: 62.42 E-value: 5.89e-12
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| CuRO_3_Tv-LCC_like | cd13903 | The third cupredoxin domain of the fungal laccases similar to Tv-LCC from Trametes Versicolor; ... |
391-453 | 6.08e-12 | |||||||||
The third cupredoxin domain of the fungal laccases similar to Tv-LCC from Trametes Versicolor; This subfamily of fungal laccases includes Tv-LCC from Trametes versicolor and Rs-LCC2 from plant pathogenic fungus Rhizoctonia solani. Laccase is a blue multi-copper enzyme that catalyzes the oxidation of a variety aromatic - notably phenolic and inorganic substances coupled to the reduction of molecular oxygen to water. It has been implicated in a wide spectrum of biological activities and, in particular, plays a key role in morphogenesis, development and lignin metabolism. Although MCOs have diverse functions, majority of them have three cupredoxin domain repeats that include one mononuclear and one trinuclear copper center. The copper ions are bound in several sites: Type 1, Type 2, and/or Type 3. The ensemble of types 2 and 3 copper is called a trinuclear cluster. MCOs oxidize their substrate by accepting electrons at a mononuclear copper center and transferring them to the active site trinuclear copper center. The cupredoxin domain 3 of 3-domain MCOs contains the Type 1 (T1) copper binding site and part the trinuclear copper binding site, which is located at the interface of domains 1 and 3. Pssm-ID: 259970 [Multi-domain] Cd Length: 147 Bit Score: 63.07 E-value: 6.08e-12
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| CuRO_1_ceruloplasmin_like | cd04199 | Cupredoxin domains 1, 3, and 5 of ceruloplasmin and similar proteins; This family includes the ... |
58-153 | 1.22e-11 | |||||||||
Cupredoxin domains 1, 3, and 5 of ceruloplasmin and similar proteins; This family includes the first, third, and fifth cupredoxin domains of ceruloplasmin and similar proteins including the first, third and fifth cupredoxin domains of unprocessed coagulation factors V and VIII. Ceruloplasmin (ferroxidase) is a multicopper oxidase essential for normal iron homeostasis. It functions in copper transport, amine oxidation and as an antioxidant preventing free radicals in serum. The protein has 6 cupredoxin domains and exhibits internal sequence homology that appears to have evolved from the triplication of a sequence unit composed of two tandem cupredoxin domains. Human Factor VIII facilitates blood clotting by acting as a cofactor for factor IXa. Factor VIII and IXa forms a complex in the presence of Ca+2 and phospholipids that converts factor X to the activated form Xa. Pssm-ID: 259862 [Multi-domain] Cd Length: 177 Bit Score: 63.19 E-value: 1.22e-11
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| PLN02792 | PLN02792 | oxidoreductase |
23-253 | 2.73e-11 | |||||||||
oxidoreductase Pssm-ID: 178389 [Multi-domain] Cd Length: 536 Bit Score: 65.39 E-value: 2.73e-11
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| CuRO_3_MaLCC_like | cd13901 | The third cupredoxin domain of the fungal laccases similar to Ma-LCC from Melanocarpus ... |
376-453 | 3.66e-11 | |||||||||
The third cupredoxin domain of the fungal laccases similar to Ma-LCC from Melanocarpus albomyces; The subfamily of fungal laccases includes Ma-LCC and similar proteins. Ma-LCC is a multicopper oxidase (MCO) from Melanocarpus albomyces. Its crystal structure contains all four coppers at the mono- and trinuclear copper centers. Laccase is a blue multi-copper enzyme that catalyzes the oxidation of a variety aromatic - notably phenolic and inorganic substances coupled to the reduction of molecular oxygen to water. It has been implicated in a wide spectrum of biological activities and, in particular, plays a key role in morphogenesis, development and lignin metabolism in fungi and plants. Although MCOs have diverse functions, majority of them have three cupredoxin domain repeats that include one mononuclear and one trinuclear copper center. The copper ions are bound in several sites: Type 1, Type 2, and/or Type 3. The ensemble of types 2 and 3 copper is called a trinuclear cluster. MCOs oxidize their substrate by accepting electrons at a mononuclear copper center and transferring them to the active site trinuclear copper center. The cupredoxin domain 3 of 3-domain MCOs contains the Type 1 (T1) copper binding site and part the trinuclear copper binding site, which is located at the interface of domains 1 and 3. Pssm-ID: 259968 [Multi-domain] Cd Length: 157 Bit Score: 61.09 E-value: 3.66e-11
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| CuRO_3_MCO_like_5 | cd13911 | The third cupredoxin domain of uncharacterized multicopper oxidase; Multicopper Oxidases (MCOs) ... |
351-454 | 8.22e-11 | |||||||||
The third cupredoxin domain of uncharacterized multicopper oxidase; Multicopper Oxidases (MCOs) are multi-domain enzymes that are able to couple oxidation of substrates with reduction of dioxygen to water. MCOs oxidize their substrate by accepting electrons at a mononuclear copper centre and transferring them to a trinuclear copper centre which binds a dioxygen. The dioxygen, following the transfer of four electrons, is reduced to two molecules of water. These MCOs are capable of oxidizing a vast range of substrates, varying from aromatic to inorganic compounds such as metals. This subfamily of MCOs is composed of three cupredoxin domains. The cupredoxin domain 3 of 3-domain MCOs contains the Type 1 (T1) copper binding site and part the trinuclear copper binding site, which is located at the interface of domains 1 and 3. Pssm-ID: 259978 [Multi-domain] Cd Length: 119 Bit Score: 59.10 E-value: 8.22e-11
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| CuRO_3_LCC_plant | cd13897 | The third cupredoxin domain of the plant laccases; Laccase is a blue multicopper oxidase (MCO) ... |
386-457 | 1.23e-10 | |||||||||
The third cupredoxin domain of the plant laccases; Laccase is a blue multicopper oxidase (MCO) which catalyzes the oxidation of a variety aromatic - notably phenolic and inorganic substances coupled to the reduction of molecular oxygen to water. Laccase has been implicated in a wide spectrum of biological activities and, in particular, plays a key role in morphogenesis, development and lignin metabolism. Plants usually express multiple laccase genes, but their precise physiological/biochemical roles remain largely unclear. MCOs are capable of oxidizing a vast range of substrates, varying from aromatic compounds to inorganic compounds such as metals. Although the members of this family have diverse functions, majority of them have three cupredoxin domain repeats. The copper ions are bound in several sites: Type 1, Type 2, and/or Type 3. The ensemble of types 2 and 3 copper is called a trinuclear cluster. MCOs oxidize their substrate by accepting electrons at a mononuclear copper center and transferring them to the active site trinuclear copper center. The cupredoxin domain 3 of 3-domain MCOs contains the Type 1 (T1) copper binding site and part the trinuclear copper binding site, which is located at the interface of domains 1 and 3. Pssm-ID: 259964 [Multi-domain] Cd Length: 139 Bit Score: 59.20 E-value: 1.23e-10
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| CuRO_1_BOD_CotA_like | cd13844 | The first Cupredoxin domain of Bilirubin oxidase (BOD), the bacterial endospore coat component ... |
38-156 | 2.04e-10 | |||||||||
The first Cupredoxin domain of Bilirubin oxidase (BOD), the bacterial endospore coat component CotA, and similar proteins; Bilirubin oxidase (BOD) catalyzes the oxidation of bilirubin to biliverdin and the four-electron reduction of molecular oxygen to water. CotA protein is an abundant component of the outer coat layer in bacterial endospore coat and it is required for spore resistance against hydrogen peroxide and UV light. Also included in this subfamily are phenoxazinone synthase (PHS), which catalyzes the oxidative coupling of substituted o-aminophenols to produce phenoxazinones. PHS has been shown to participate in diverse biological functions such as spore pigmentation and biosynthesis of the antibiotic grixazone. These are Laccase-like multicopper oxidases (MCOs) that are able to couple oxidation of substrates with reduction of dioxygen to water. MCOs are capable of oxidizing a vast range of substrates, varying from aromatic compounds to inorganic compounds such as metals. Although the members of this family have diverse functions, majority of them have three cupredoxin domain repeats. The copper ions are bound in several sites: Type 1, Type 2, and/or Type 3. The ensemble of types 2 and 3 copper is called a trinuclear cluster. MCOs oxidize their substrate by accepting electrons at a mononuclear copper center and transferring them to the active site trinuclear copper center. The cupredoxin domain 1 of 3-domain MCOs contains part the trinuclear copper binding site, which is located at the interface of domains 1 and 3. Pssm-ID: 259913 [Multi-domain] Cd Length: 162 Bit Score: 59.23 E-value: 2.04e-10
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| CuRO_2_McoC_like | cd13881 | The second cupredoxin domain of a multicopper oxidase McoC and similar proteins; This family ... |
167-291 | 4.39e-10 | |||||||||
The second cupredoxin domain of a multicopper oxidase McoC and similar proteins; This family includes bacterial multicopper oxidases (MCOs) represented by McoC from the pathogenic bacterium Campylobacter jejuni. McoC is a periplasmic MCO, which has been characterized to be associated with copper homeostasis. McoC may also function to protect against oxidative stress as it may convert metallic ions into their less toxic form. MCOs are multi-domain enzymes that are able to couple oxidation of substrates with the reduction of dioxygen to water. These MCOs are capable of oxidizing a vast range of substrates, varying from aromatic to inorganic compounds such as metals. They are composed of three cupredoxin domains that include one mononuclear and one trinuclear copper center. The copper ions are bound in several sites: Type 1, Type 2, and/or Type 3. The ensemble of types 2 and 3 copper is called a trinuclear cluster. MCOs oxidize their substrate by accepting electrons at a mononuclear copper center and transferring them to the active site trinuclear copper center. The cupredoxin domain 2 of 3-domain MCOs has lost the ability to bind copper. Pssm-ID: 259948 [Multi-domain] Cd Length: 142 Bit Score: 57.62 E-value: 4.39e-10
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| CuRO_3_BOD | cd13889 | The third cupredoxin domain of Bilirubin oxidase (BOD); Bilirubin oxidase (BOD) catalyzes the ... |
351-454 | 7.94e-10 | |||||||||
The third cupredoxin domain of Bilirubin oxidase (BOD); Bilirubin oxidase (BOD) catalyzes the oxidation of bilirubin to biliverdin and the four-electron reduction of molecular oxygen to water. It is used in diagnosing jaundice through the determination of bilirubin in serum. BOD is a member of the multicopper oxidase (MCO) family that also includes laccase, ascorbate oxidase and ceruloplasmin. MCOs are capable of oxidizing a vast range of substrates, varying from aromatic compounds to inorganic compounds such as metals. Although the members of this family have diverse functions, majority of them have three cupredoxin domain repeats. The copper ions are bound in several sites: Type 1, Type 2, and/or Type 3. The ensemble of types 2 and 3 copper is called a trinuclear cluster. MCOs oxidize their substrate by accepting electrons at a mononuclear copper center and transferring them to the active site trinuclear copper center. The cupredoxin domain 3 of 3-domain MCOs contains the Type 1 (T1) copper binding site and part the trinuclear copper binding site, which is located at the interface of domains 1 and 3. Pssm-ID: 259956 [Multi-domain] Cd Length: 124 Bit Score: 56.55 E-value: 7.94e-10
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| CuRO_3_Diphenol_Ox | cd13904 | The third cupredoxin domain of fungal laccase, diphenol oxidase; Diphenol oxidase belongs to ... |
391-457 | 8.90e-10 | |||||||||
The third cupredoxin domain of fungal laccase, diphenol oxidase; Diphenol oxidase belongs to the laccase family. It catalyzes the initial steps in melanin biosynthesis from diphenols. Melanin is one of the virulence factors of infectious fungi. In the pathogenesis of C. neoformans, melanin pigments have been shown to protect the fungal cells from oxidative and microbicidal activities of host defense systems. Laccase is a blue multicopper oxidase (MCO) which catalyzes the oxidation of a variety aromatic - notably phenolic and inorganic substances coupled to the reduction of molecular oxygen to water. It has been implicated in a wide spectrum of biological activities and, in particular, plays a key role in morphogenesis, development and lignin metabolism. Although MCOs have diverse functions, majority of them have three cupredoxin domain repeats that include one mononuclear and one trinuclear copper center. The copper ions are bound in several sites: Type 1, Type 2, and/or Type 3. The ensemble of types 2 and 3 copper is called a trinuclear cluster. MCOs oxidize their substrate by accepting electrons at a mononuclear copper center and transferring them to the active site trinuclear copper center. The cupredoxin domain 3 of 3-domain MCOs contains the Type 1 (T1) copper binding site and part the trinuclear copper binding site, which is located at the interface of domains 1 and 3. Pssm-ID: 259971 [Multi-domain] Cd Length: 158 Bit Score: 57.30 E-value: 8.90e-10
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| CuRO_3_FV_like | cd14450 | The third cupredoxin domain of coagulation factor V and similar proteins; Factor V is an ... |
64-153 | 9.30e-10 | |||||||||
The third cupredoxin domain of coagulation factor V and similar proteins; Factor V is an essential coagulation protein with both pro- and anti-coagulant functions. Aberrant expression of human factor V can lead to bleeding or thromboembolic disease, which may be life-threatening. Bovine factor Va serves as the cofactor in the prothrombinase complex that results in a 300,000-fold increase in the rate of thrombin generation. Factor V is synthesized as a single polypeptide with six cupredoxin domains and a domain structure of 1-2-3-4-B-5-6-C1-C2, where 1-6 are cupredoxin domains, B is a domain with no known structural homologs and is dispensible for coagulant activity, and C are domains distantly related to discoidin protein-fold family members. Factor V has little activity prior to proteolytic cleavage by thrombin or FXa upon secretion. The resulting Factor Va is a heterodimer consisting of a heavy chain (1-2-3-4) and a light chain (5-6-C1-C2). This model represents the cupredoxin domain 3 of unprocessed Factor V or the heavy chain of Factor Va, and similar proteins including pseutarin C non-catalytic subunit. Pseutarin C is a prothrombin activator from Pseudonaja textilis venom. Pssm-ID: 259992 [Multi-domain] Cd Length: 181 Bit Score: 57.96 E-value: 9.30e-10
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| CuRO_3_ceruloplasmin | cd04224 | The third cupredoxin domain of Ceruloplasmin; Ceruloplasmin is a multicopper oxidase essential ... |
64-153 | 9.30e-10 | |||||||||
The third cupredoxin domain of Ceruloplasmin; Ceruloplasmin is a multicopper oxidase essential for normal iron homeostasis and copper transport in blood. It also functions in amine oxidation and as an antioxidant preventing free radicals in serum. The protein has 6 cupredoxin domains with six copper centers; three mononuclear sites in domain 2, 4 and 6 and three in the form of trinuclear clusters at the interface of domains 1 and 6. Ceruloplasmin exhibits internal sequence homology that appears to have evolved from the triplication of a sequence unit composed of two tandem cupredoxin domains. This model represents the third cupredoxin domain of ceruloplasmin. Pssm-ID: 259886 [Multi-domain] Cd Length: 197 Bit Score: 58.25 E-value: 9.30e-10
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| Cupredoxin | cd00920 | Cupredoxin superfamily; Cupredoxins contain type I copper centers and are involved in ... |
46-152 | 9.76e-10 | |||||||||
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: 55.70 E-value: 9.76e-10
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| CuRO_1_2DMCO_NIR_like_2 | cd14449 | The cupredoxin domain 1 of a two-domain laccase related to nitrite reductase; The two-domain ... |
63-153 | 1.38e-09 | |||||||||
The cupredoxin domain 1 of a two-domain laccase related to nitrite reductase; The two-domain laccase (small laccase) in this family differs significantly from all laccases. It resembles the two domain nitrite reductase in both sequence and structure. It consists of two cupredoxin domains and forms trimers, and hence resembles the quaternary structure of nitrite reductases more than that of large laccases. There are three trinuclear copper clusters in the enzyme localized between domains 1 and 2 of each pair of neighbor chains. Laccase is a blue multi-copper enzyme that catalyzes the oxidation of a variety of organic substrates coupled to the reduction of molecular oxygen to water. It displays broad substrate specificity, catalyzing the oxidation of a wide variety of aromatic, notably phenolic, and inorganic substances. Laccase has been implicated in a wide spectrum of biological activities. This subfamily has lost the type 1 (T1) copper binding site in domain 1 that is present in other two-domain laccases. Pssm-ID: 259991 [Multi-domain] Cd Length: 135 Bit Score: 56.12 E-value: 1.38e-09
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| CuRO_3_McoP_like | cd13888 | The third cupredoxin domain of multicopper oxidase McoP and similar proteins; This subfamily ... |
351-454 | 2.49e-09 | |||||||||
The third cupredoxin domain of multicopper oxidase McoP and similar proteins; This subfamily includes archaeal and bacterial multicopper oxidases (MCOs), represented by the extremely thermostable McoP from the hyperthermophilic archaeon Pyrobaculum aerophilum. McoP is an efficient metallo-oxidase that catalyzes the oxidation of cuprous and ferrous ions. It is noteworthy that McoP has three-fold higher catalytic efficiency when using nitrous oxide as electron acceptor than when using dioxygen, the typical oxidizing substrate of multicopper oxidases. McoP may function as a novel archaeal nitrous oxide reductase that is probably involved in the denitrification pathway in archaea. Members of this subfamily contain three cupredoxin domain repeats. The copper ions are bound in several sites; Type 1, Type 2, and/or Type 3. The ensemble of types 2 and 3 copper is called a trinuclear cluster. MCOs oxidize their substrate by accepting electrons at a mononuclear copper center and transferring them to the active site trinuclear copper center. The cupredoxin domain 3 of 3-domain MCOs contains the Type 1 (T1) copper binding site and part the trinuclear copper binding site, which is located at the interface of domains 1 and 3. Pssm-ID: 259955 [Multi-domain] Cd Length: 139 Bit Score: 55.65 E-value: 2.49e-09
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| CuRO_3_AAO | cd13893 | The third cupredoxin domain of plant Ascorbate oxidase; Ascorbate oxidase catalyzes the ... |
382-454 | 3.43e-09 | |||||||||
The third cupredoxin domain of plant Ascorbate oxidase; Ascorbate oxidase catalyzes the oxidation of ascorbic acid to dehydroascorbic acid. This multicopper oxidase (MCO) is found in cucurbitaceous plants such as pumpkin, cucumber, and melon. It can detect levels of ascorbic acid and eliminate it. The biological function of ascorbate oxidase is still not clear. Ascorbate oxidase belongs to MCO family which couple oxidation of substrates with reduction of dioxygen to water. MCOs are capable of oxidizing a vast range of substrates, varying from aromatic compounds to inorganic compounds such as metals. Although the members of this family have diverse functions, majority of them have three cupredoxin domain repeats. The copper ions are bound in several sites: Type 1, Type 2, and/or Type 3. The ensemble of types 2 and 3 copper is called a trinuclear cluster. MCOs oxidize their substrate by accepting electrons at a mononuclear copper center and transferring them to the active site trinuclear copper center. The cupredoxin domain 3 of 3-domain MCOs contains the Type 1 (T1) copper binding site and part the trinuclear copper binding site, which is located at the interface of domains 1 and 3. Pssm-ID: 259960 [Multi-domain] Cd Length: 155 Bit Score: 55.50 E-value: 3.43e-09
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| PLN02168 | PLN02168 | copper ion binding / pectinesterase |
57-224 | 4.71e-09 | |||||||||
copper ion binding / pectinesterase Pssm-ID: 215113 [Multi-domain] Cd Length: 545 Bit Score: 58.45 E-value: 4.71e-09
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| PLN02991 | PLN02991 | oxidoreductase |
61-253 | 2.23e-08 | |||||||||
oxidoreductase Pssm-ID: 215536 [Multi-domain] Cd Length: 543 Bit Score: 56.18 E-value: 2.23e-08
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| CuRO_2_ceruloplasmin_like | cd04200 | Cupredoxin domains 2, 4, and 6 of ceruloplasmin and similar proteins; This family includes the ... |
379-459 | 2.32e-08 | |||||||||
Cupredoxin domains 2, 4, and 6 of ceruloplasmin and similar proteins; This family includes the second, fourth and sixth cupredoxin domains of ceruloplasmin and similar proteins, including the second, fourth, and sixth cupredoxin domains of unprocessed coagulation factors V and VIII. Ceruloplasmin (ferroxidase) is a multicopper oxidase essential for normal iron homeostasis. Ceruloplasmin also functions in copper transport, amine oxidase and as an antioxidant preventing free radicals in serum. The protein has 6 cupredoxin domains and exhibits internal sequence homology that appears to have evolved from the triplication of a sequence unit composed of two tandem cupredoxin domains. Human Factor VIII facilitates blood clotting by acting as a cofactor for factor IXa Factor VIII and IXa forms a complex in the presence of Ca+2 and phospholipids that converts factor X to the activated form Xa. Pssm-ID: 259863 [Multi-domain] Cd Length: 141 Bit Score: 52.80 E-value: 2.32e-08
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| PLN02835 | PLN02835 | oxidoreductase |
17-247 | 2.59e-08 | |||||||||
oxidoreductase Pssm-ID: 178429 [Multi-domain] Cd Length: 539 Bit Score: 56.13 E-value: 2.59e-08
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| CuRO_2_LCC_like | cd04205 | Cupredoxin domain 2 of laccase-like multicopper oxidases; including laccase, CueO, spore coat ... |
165-284 | 4.22e-08 | |||||||||
Cupredoxin domain 2 of laccase-like multicopper oxidases; including laccase, CueO, spore coat protein A, ascorbate oxidase and similar proteins; Laccase-like multicopper oxidases (MCOs) are able to couple oxidation of substrates with reduction of dioxygen to water. MCOs are capable of oxidizing a vast range of substrates, varying from aromatic compounds to inorganic compounds such as metals. Although the members of this family have diverse functions, majority of them have three cupredoxin domain repeats. The copper ions are bound in several sites: Type 1, Type 2, and/or Type 3. The ensemble of types 2 and 3 copper is called a trinuclear cluster. MCOs oxidize their substrate by accepting electrons at a mononuclear copper center and transferring them to the active site trinuclear copper center. The cupredoxin domain 2 of 3-domain MCOs has lost the ability to bind copper. Pssm-ID: 259868 [Multi-domain] Cd Length: 152 Bit Score: 52.36 E-value: 4.22e-08
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| CuRO_2_ceruloplasmin | cd11021 | The second cupredoxin domain of Ceruloplasmin; Ceruloplasmin is a multicopper oxidase ... |
391-459 | 7.34e-08 | |||||||||
The second cupredoxin domain of Ceruloplasmin; Ceruloplasmin is a multicopper oxidase essential for normal iron homeostasis and copper transport in blood. It also functions in amine oxidation and as an antioxidant preventing free radicals in serum. The protein has 6 cupredoxin domains with six copper centers; three mononuclear sites in domain 2, 4 and 6 and three in the form of trinuclear clusters at the interface of domains 1 and 6. Ceruloplasmin exhibits internal sequence homology that appears to have evolved from the triplication of a sequence unit composed of two tandem cupredoxin domains. This model represents the second cupredoxin domain of ceruloplasmin. Pssm-ID: 259907 [Multi-domain] Cd Length: 141 Bit Score: 51.32 E-value: 7.34e-08
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| CuRO_D2_2dMcoN_like | cd04202 | The second cupredoxin domain of bacterial two domain multicopper oxidase McoN and similar ... |
162-276 | 1.26e-07 | |||||||||
The second cupredoxin domain of bacterial two domain multicopper oxidase McoN and similar proteins; This family includes bacterial two domain multicopper oxidases (2dMCOs) represented by the McoN from Nitrosomonas europaea. McoN is a trimeric type C blue copper oxidase. Each subunit houses a type 1 copper site in domain 1 and a type 2/type 3 trinuclear copper cluster at the subunit-subunit interface. The 2dMCO is proposed to be a key intermediate in the evolution of three domain MCOs. The biological function of McoN has not been characterized. Multicopper oxidases couple oxidation of substrates with reduction of dioxygen to water. These MCOs are capable of oxidizing a vast range of substrates, varying from aromatic to inorganic compounds such as metals. Pssm-ID: 259865 [Multi-domain] Cd Length: 138 Bit Score: 50.72 E-value: 1.26e-07
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| Cu-oxidase | pfam00394 | Multicopper oxidase; Many of the proteins in this family contain multiple similar copies of ... |
164-268 | 1.28e-07 | |||||||||
Multicopper oxidase; Many of the proteins in this family contain multiple similar copies of this plastocyanin-like domain. Pssm-ID: 395317 [Multi-domain] Cd Length: 146 Bit Score: 50.78 E-value: 1.28e-07
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| N2OR_C | cd04223 | The C-terminal cupredoxin domain of Nitrous-oxide reductase; Nitrous-oxide reductase ... |
67-133 | 2.71e-07 | |||||||||
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: 48.39 E-value: 2.71e-07
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| CuRO_3_MCO_like_1 | cd13907 | The third cupredoxin domain of uncharacterized multicopper oxidase; Multicopper Oxidases (MCOs) ... |
391-454 | 3.00e-07 | |||||||||
The third cupredoxin domain of uncharacterized multicopper oxidase; Multicopper Oxidases (MCOs) are multi-domain enzymes that are able to couple oxidation of substrates with reduction of dioxygen to water. MCOs oxidize their substrate by accepting electrons at a mononuclear copper centre and transferring them to a trinuclear copper centre which binds a dioxygen. The dioxygen, following the transfer of four electrons, is reduced to two molecules of water. These MCOs are capable of oxidizing a vast range of substrates, varying from aromatic to inorganic compounds such as metals. This subfamily of MCOs is composed of three cupredoxin domains. The cupredoxin domain 3 of 3-domain MCOs contains the Type 1 (T1) copper binding site and part the trinuclear copper binding site, which is located at the interface of domains 1 and 3. Pssm-ID: 259974 [Multi-domain] Cd Length: 154 Bit Score: 49.79 E-value: 3.00e-07
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| CuRO_5_ceruloplasmin | cd04225 | The fifth cupredoxin domain of Ceruloplasmin; Ceruloplasmin is a multicopper oxidase essential ... |
64-153 | 3.71e-07 | |||||||||
The fifth cupredoxin domain of Ceruloplasmin; Ceruloplasmin is a multicopper oxidase essential for normal iron homeostasis and copper transport in blood. It also functions in amine oxidation and as an antioxidant preventing free radicals in serum. The protein has 6 cupredoxin domains with six copper centers; three mononuclear sites in domain 2, 4 and 6 and three in the form of trinuclear clusters at the interface of domains 1 and 6. Ceruloplasmin exhibits internal sequence homology that appears to have evolved from the triplication of a sequence unit composed of two tandem cupredoxin domains. This model represents the fifth cupredoxin domain of ceruloplasmin. Pssm-ID: 259887 [Multi-domain] Cd Length: 171 Bit Score: 50.16 E-value: 3.71e-07
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| CuRO_1_ceruloplasmin | cd04222 | The first cupredoxin domain of Ceruloplasmin; Ceruloplasmin is a multicopper oxidase essential ... |
58-153 | 5.37e-07 | |||||||||
The first cupredoxin domain of Ceruloplasmin; Ceruloplasmin is a multicopper oxidase essential for normal iron homeostasis and copper transport in blood. It also functions in amine oxidation and as an antioxidant preventing free radicals in serum. The protein has 6 cupredoxin domains with six copper centers; three mononuclear sites in domain 2, 4 and 6 and three in the form of trinuclear clusters at the interface of domains 1 and 6. Ceruloplasmin exhibits internal sequence homology that appears to have evolved from the triplication of a sequence unit composed of two tandem cupredoxin domains. This model represents the first cupredoxin domain of ceruloplasmin. Pssm-ID: 259884 [Multi-domain] Cd Length: 183 Bit Score: 49.73 E-value: 5.37e-07
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| CuRO_2_ceruloplasmin_like_2 | cd11023 | cupredoxin domain of ceruloplasmin homologs; Uncharacterized subfamily of ceruloplasmin ... |
391-454 | 1.35e-06 | |||||||||
cupredoxin domain of ceruloplasmin homologs; Uncharacterized subfamily of ceruloplasmin homologous proteins. Ceruloplasmin (ferroxidase) is a multicopper oxidase essential for normal iron homeostasis. Ceruloplasmin also functions in copper transport, amine oxidase and as an antioxidant preventing free radicals in serum. The protein has 6 cupredoxin domains and exhibits internal sequence homology that appears to have evolved from the triplication of a sequence unit composed of two tandem cupredoxin domains. This model represents the first domain of the triplicated units. Pssm-ID: 259909 [Multi-domain] Cd Length: 118 Bit Score: 47.22 E-value: 1.35e-06
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| CuRO_D2_2dMcoN_like | cd04202 | The second cupredoxin domain of bacterial two domain multicopper oxidase McoN and similar ... |
41-154 | 1.41e-06 | |||||||||
The second cupredoxin domain of bacterial two domain multicopper oxidase McoN and similar proteins; This family includes bacterial two domain multicopper oxidases (2dMCOs) represented by the McoN from Nitrosomonas europaea. McoN is a trimeric type C blue copper oxidase. Each subunit houses a type 1 copper site in domain 1 and a type 2/type 3 trinuclear copper cluster at the subunit-subunit interface. The 2dMCO is proposed to be a key intermediate in the evolution of three domain MCOs. The biological function of McoN has not been characterized. Multicopper oxidases couple oxidation of substrates with reduction of dioxygen to water. These MCOs are capable of oxidizing a vast range of substrates, varying from aromatic to inorganic compounds such as metals. Pssm-ID: 259865 [Multi-domain] Cd Length: 138 Bit Score: 47.63 E-value: 1.41e-06
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| CuRO_5_FV_like | cd14451 | The fifth cupredoxin domain of coagulation factor V and similar proteins; Factor V is an ... |
64-153 | 2.28e-06 | |||||||||
The fifth cupredoxin domain of coagulation factor V and similar proteins; Factor V is an essential coagulation protein with both pro- and anti-coagulant functions. Aberrant expression of human factor V can lead to bleeding or thromboembolic disease, which may be life-threatening. Bovine factor Va serves as the cofactor in the prothrombinase complex that results in a 300,000-fold increase in the rate of thrombin generation. Factor V is synthesized as a single polypeptide with six cupredoxin domains and a domain structure of 1-2-3-4-B-5-6-C1-C2, where 1-6 are cupredoxin domains, B is a domain with no known structural homologs and is dispensible for coagulant activity, and C are domains distantly related to discoidin protein-fold family members. Factor V has little activity prior to proteolytic cleavage by thrombin or FXa upon secretion. The resulting Factor Va is a heterodimer consisting of a heavy chain (1-2-3-4) and a light chain (5-6-C1-C2). This model represents the cupredoxin domain 5 of unprocessed Factor V or the first cupredoxin domain of the light chain of coagulation factor Va, and similar proteins including pseutarin C non-catalytic subunit. Pseutarin C is a prothrombin activator from Pseudonaja textilis venom. Pssm-ID: 259993 [Multi-domain] Cd Length: 173 Bit Score: 47.53 E-value: 2.28e-06
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| CuRO_1_FV_like | cd04226 | The first cupredoxin domain of coagulation factor VIII and similar proteins; Factor V is an ... |
67-153 | 2.73e-06 | |||||||||
The first cupredoxin domain of coagulation factor VIII and similar proteins; Factor V is an essential coagulation protein with both pro- and anti-coagulant functions. Aberrant expression of human factor V can lead to bleeding or thromboembolic disease, which may be life-threatening. Bovine factor Va serves as the cofactor in the prothrombinase complex that results in a 300,000-fold increase in the rate of thrombin generation. Factor V is synthesized as a single polypeptide with six cupredoxin domains and a domain structure of 1-2-3-4-B-5-6-C1-C2, where 1-6 are cupredoxin domains, B is a domain with no known structural homologs and is dispensible for coagulant activity, and C are domains distantly related to discoidin protein-fold family members. Factor V has little activity prior to proteolytic cleavage by thrombin or FXa upon secretion. The resulting Factor Va is a heterodimer consisting of a heavy chain (1-2-3-4) and a light chain (5-6-C1-C2). This model represents the cupredoxin domain 1 of unprocessed Factor V or the heavy chain of Factor Va, and similar proteins including pseutarin C non-catalytic subunit. Pseutarin C is a prothrombin activator from Pseudonaja textilis venom. Pssm-ID: 259888 [Multi-domain] Cd Length: 165 Bit Score: 47.16 E-value: 2.73e-06
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| PLN00044 | PLN00044 | multi-copper oxidase-related protein; Provisional |
57-135 | 7.38e-06 | |||||||||
multi-copper oxidase-related protein; Provisional Pssm-ID: 165622 [Multi-domain] Cd Length: 596 Bit Score: 48.51 E-value: 7.38e-06
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| Cu-oxidase | pfam00394 | Multicopper oxidase; Many of the proteins in this family contain multiple similar copies of ... |
376-453 | 1.13e-05 | |||||||||
Multicopper oxidase; Many of the proteins in this family contain multiple similar copies of this plastocyanin-like domain. Pssm-ID: 395317 [Multi-domain] Cd Length: 146 Bit Score: 45.00 E-value: 1.13e-05
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| CuRO_3_FVIII_like | cd04227 | The third cupredoxin domain of coagulation factor VIII and similar proteins; Factor VIII ... |
63-153 | 4.31e-05 | |||||||||
The third cupredoxin domain of coagulation factor VIII and similar proteins; Factor VIII functions in the factor X-activating complex of the intrinsic coagulation pathway. It facilitates blood clotting by acting as a cofactor for factor IXa. In the presence of Ca2+ and phospholipids, Factor VIII and IXa form a complex that converts factor X to the activated form Xa. A variety of mutations in the Factor VIII gene can cause hemophilia A, which typically requires replacement therapy with purified protein. Factor VIII is synthesized as a single polypeptide with six cupredoxin domains and a domain structure of 1-2-3-4-B-5-6-C1-C2, where 1-6 are cupredoxin domains, B is a domain with no known structural homologs and is dispensible for coagulant activity, and C are domains distantly related to discoidin protein-fold family members. Factor VIII is initially processed through proteolysis to generate a heterodimer consisting of a heavy chain (1-2-3-4) and a light chain (5-6-C1-C2), which circulates in a tight complex with von Willebrand factor (VWF). Further processing of the heavy chain produces activated factor VIIIa, a heterotrimer composed of polypeptides (1-2), (3-4), and the light chain. This model represents the cupredoxin domain 3 of unprocessed Factor VIII or the heavy chain of circulating Factor VIII, and similar proteins. Pssm-ID: 259889 [Multi-domain] Cd Length: 177 Bit Score: 44.15 E-value: 4.31e-05
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| TAT_signal | pfam10518 | TAT (twin-arginine translocation) pathway signal sequence; |
2-26 | 4.53e-05 | |||||||||
TAT (twin-arginine translocation) pathway signal sequence; Pssm-ID: 463131 [Multi-domain] Cd Length: 26 Bit Score: 40.05 E-value: 4.53e-05
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| CuRO_1_2DMCO_NIR_like | cd11024 | The cupredoxin domain 1 of a two-domain laccase related to nitrite reductase; The two-domain ... |
366-459 | 5.03e-05 | |||||||||
The cupredoxin domain 1 of a two-domain laccase related to nitrite reductase; The two-domain laccase (small laccase) in this family differs significantly from all laccases. It resembles the two domain nitrite reductase in both sequence and structure. It consists of two cupredoxin domains and forms trimers and hence resembles the quaternary structure of nitrite reductases more than that of large laccases. There are three trinuclear copper clusters in the enzyme localized between domains 1 and 2 of each pair of neighbor chains. Three copper ions of type 1 lie close to one another near the surface of the central part of the trimer, and, effectively, a trimeric substrate binding site is formed in their vicinity. Laccase is a blue multi-copper enzyme that catalyzes the oxidation of a variety of organic substrates coupled to the reduction of molecular oxygen to water. It displays broad substrate specificity, catalyzing the oxidation of a wide variety of aromatic, notably phenolic, and inorganic substances. Laccase has been implicated in a wide spectrum of biological activities. Pssm-ID: 259910 [Multi-domain] Cd Length: 119 Bit Score: 42.64 E-value: 5.03e-05
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| CuRO_2_McoP_like | cd13879 | The second cupredoxin domain of multicopper oxidase McoP and similar proteins; This family ... |
163-282 | 5.63e-05 | |||||||||
The second cupredoxin domain of multicopper oxidase McoP and similar proteins; This family includes archaeal and bacterial multicopper oxidases (MCOs), represented by the extremely thermostable McoP from the hyperthermophilic archaeon Pyrobaculum aerophilum. McoP is an efficient metallo-oxidase that catalyzes the oxidation of cuprous and ferrous ions. It is noteworthy that McoP has three-fold higher catalytic efficiency when using nitrous oxide as electron acceptor than when using dioxygen, the typical oxidizing substrate of multicopper oxidases. McoP may function as a novel archaeal nitrous oxide reductase that is probably involved in the denitrification pathway in archaea. Although MCOs have diverse functions, majority of them have three cupredoxin domain repeats that include one mononuclear and one trinuclear copper center. The copper ions are bound in several sites: Type 1, Type 2, and/or Type 3. The ensemble of types 2 and 3 copper is called a trinuclear cluster. MCOs oxidize their substrate by accepting electrons at a mononuclear copper center and transferring them to the active site trinuclear copper center. The cupredoxin domain 2 of 3-domain MCOs has lost the ability to bind copper. Pssm-ID: 259946 [Multi-domain] Cd Length: 162 Bit Score: 43.42 E-value: 5.63e-05
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| CuRO_3_AAO_like_2 | cd13895 | The third cupredoxin domain of Ascorbate oxidase homologs; This family includes fungal ... |
391-454 | 6.39e-05 | |||||||||
The third cupredoxin domain of Ascorbate oxidase homologs; This family includes fungal proteins with similarity to ascorbate oxidase. Ascorbate oxidase catalyzes the oxidation of ascorbic acid to dehydroascorbic acid. It can detect levels of ascorbic acid and eliminate it. The biological function of ascorbate oxidase is still not clear. Ascorbate oxidase belongs to multicopper oxidase (MCO) family which couple oxidation of substrates with reduction of dioxygen to water. MCOs are capable of oxidizing a vast range of substrates, varying from aromatic compounds to inorganic compounds such as metals. Although the members of this family have diverse functions, majority of them have three cupredoxin domain repeats. The copper ions are bound in several sites: Type 1, Type 2, and/or Type 3. The ensemble of types 2 and 3 copper is called a trinuclear cluster. MCOs oxidize their substrate by accepting electrons at a mononuclear copper center and transferring them to the active site trinuclear copper center. The cupredoxin domain 3 of 3-domain MCOs contains the Type 1 (T1) copper binding site and part the trinuclear copper binding site, which is located at the interface of domains 1 and 3. Pssm-ID: 259962 [Multi-domain] Cd Length: 188 Bit Score: 43.84 E-value: 6.39e-05
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| CuRO_2_BOD_CotA_like | cd14448 | Cupredoxin domain 2 of Bilirubin oxidase (BOD), the bacterial endospore coat component CotA, ... |
164-281 | 6.60e-05 | |||||||||
Cupredoxin domain 2 of Bilirubin oxidase (BOD), the bacterial endospore coat component CotA, and similar proteins; Bilirubin oxidase (BOD) catalyzes the oxidation of bilirubin to biliverdin and the four-electron reduction of molecular oxygen to water. CotA protein is an abundant component of the outer coat layer in bacterial endospore coat and is required for spore resistance against hydrogen peroxide and UV light. Also included in this subfamily are phenoxazinone synthase (PHS), which catalyzes the oxidative coupling of substituted o-aminophenols to produce phenoxazinones, and FtsP (also named SufI), which is a component of the cell division apparatus. These proteins are laccase-like multicopper oxidases (MCOs) that are able to couple oxidation of substrates with reduction of dioxygen to water. MCOs are capable of oxidizing a vast range of substrates, varying from aromatic compounds to inorganic compounds such as metals. Although the members of this family have diverse functions, majority of them have three cupredoxin domain repeats. The copper ions are bound in several sites: Type 1, Type 2, and/or Type 3. The ensemble of types 2 and 3 copper is called a trinuclear cluster. MCOs oxidize their substrate by accepting electrons at a mononuclear copper center and transferring them to the active site trinuclear copper center. The cupredoxin domain 2 of 3-domain MCOs has lost the ability to bind copper. Pssm-ID: 259990 [Multi-domain] Cd Length: 144 Bit Score: 42.68 E-value: 6.60e-05
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| CuRO_2_FV_like | cd14453 | The second cupredoxin domain of coagulation factor V and similar proteins; Factor V is an ... |
390-459 | 1.18e-04 | |||||||||
The second cupredoxin domain of coagulation factor V and similar proteins; Factor V is an essential coagulation protein with both pro- and anti-coagulant functions. Aberrant expression of human factor V can lead to bleeding or thromboembolic disease, which may be life-threatening. Bovine factor Va serves as the cofactor in the prothrombinase complex that results in a 300,000-fold increase in the rate of thrombin generation. Factor V is synthesized as a single polypeptide with six cupredoxin domains and a domain structure of 1-2-3-4-B-5-6-C1-C2, where 1-6 are cupredoxin domains, B is a domain with no known structural homologs and is dispensible for coagulant activity, and C are domains distantly related to discoidin protein-fold family members. Factor V has little activity prior to proteolytic cleavage by thrombin or FXa upon secretion. The resulting Factor Va is a heterodimer consisting of a heavy chain (1-2-3-4) and a light chain (5-6-C1-C2). This model represents the cupredoxin domain 2 of unprocessed Factor V or the heavy chain of Factor Va, and similar proteins including pseutarin C non-catalytic subunit. Pseutarin C is a prothrombin activator from Pseudonaja textilis venom. Pssm-ID: 259995 [Multi-domain] Cd Length: 123 Bit Score: 41.77 E-value: 1.18e-04
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| CuRO_1_FVIII_like | cd14452 | The first cupredoxin domain of coagulation factor VIII and similar proteins; Factor VIII ... |
50-153 | 1.29e-04 | |||||||||
The first cupredoxin domain of coagulation factor VIII and similar proteins; Factor VIII functions in the factor X-activating complex of the intrinsic coagulation pathway. It facilitates blood clotting by acting as a cofactor for factor IXa. In the presence of Ca2+ and phospholipids, Factor VIII and IXa form a complex that converts factor X to the activated form Xa. A variety of mutations in the Factor VIII gene can cause hemophilia A, which typically requires replacement therapy with purified protein. Factor VIII is synthesized as a single polypeptide with six cupredoxin domains and a domain structure of 1-2-3-4-B-5-6-C1-C2, where 1-6 are cupredoxin domains, B is a domain with no known structural homologs and is dispensible for coagulant activity, and C are domains distantly related to discoidin protein-fold family members. Factor VIII is initially processed through proteolysis to generate a heterodimer consisting of a heavy chain (1-2-3-4) and a light chain (5-6-C1-C2), which circulates in a tight complex with von Willebrand factor (VWF). Further processing of the heavy chain produces activated factor VIIIa, a heterotrimer composed of polypeptides (1-2), (3-4), and the light chain. This model represents the cupredoxin domain 1 of unprocessed Factor VIII or the heavy chain of circulating Factor VIII, and similar proteins. Pssm-ID: 259994 [Multi-domain] Cd Length: 173 Bit Score: 42.66 E-value: 1.29e-04
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| CuRO_1_CuNIR | cd11020 | Cupredoxin domain 1 of Copper-containing nitrite reductase; Copper-containing nitrite ... |
366-459 | 2.21e-04 | |||||||||
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: 40.66 E-value: 2.21e-04
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| CuRO_6_ceruloplasmin | cd11012 | The sixth cupredoxin domain of Ceruloplasmin; Ceruloplasmin is a multicopper oxidase essential ... |
391-453 | 2.74e-04 | |||||||||
The sixth cupredoxin domain of Ceruloplasmin; Ceruloplasmin is a multicopper oxidase essential for normal iron homeostasis and copper transport in blood. It also functions in amine oxidation and as an antioxidant preventing free radicals in serum. The protein has 6 cupredoxin domains with six copper centers; three mononuclear sites in domain 2, 4 and 6 and three in the form of trinuclear clusters at the interface of domains 1 and 6. Ceruloplasmin exhibits internal sequence homology that appears to have evolved from the triplication of a sequence unit composed of two tandem cupredoxin domains. This model represents the sixth cupredoxin domain of ceruloplasmin. Pssm-ID: 259898 [Multi-domain] Cd Length: 145 Bit Score: 41.01 E-value: 2.74e-04
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| Cupredoxin | cd00920 | Cupredoxin superfamily; Cupredoxins contain type I copper centers and are involved in ... |
372-458 | 4.56e-04 | |||||||||
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: 39.52 E-value: 4.56e-04
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| CuRO_2_CueO_FtsP | cd13867 | The second Cupredoxin domain of the multicopper oxidase CueO, the cell division protein FtsP, ... |
166-268 | 4.81e-04 | |||||||||
The second Cupredoxin domain of the multicopper oxidase CueO, the cell division protein FtsP, and similar proteins; CueO is a multicopper oxidase (MCO) that is part of the copper-regulatory cue operon, which employs a cytosolic metalloregulatory protein CueR that induces expression of CopA and CueO under copper stress conditions. CueO is a periplasmic multicopper oxidase that is stimulated by exogenous copper(II). FtsP (also named SufI) is a component of the cell division apparatus. It is involved in protecting or stabilizing the assembly of divisomes under stress conditions. FtsP belongs to the multicopper oxidase superfamily but lacks metal cofactors. The protein is localized at septal rings and may serve as a scaffolding function. Members of this subfamily contain three cupredoxin domains and this model represents the second domain. Although MCOs have diverse functions, majority of them have three cupredoxin domain repeats that include one mononuclear and one trinuclear copper center. The copper ions are bound in several sites: Type 1, Type 2, and/or Type 3. The ensemble of types 2 and 3 copper is called a trinuclear cluster. MCOs oxidize their substrate by accepting electrons at a mononuclear copper center and transferring them to the active site trinuclear copper center. The cupredoxin domain 2 of 3-domain MCOs has lost the ability to bind copper. Pssm-ID: 259935 [Multi-domain] Cd Length: 146 Bit Score: 40.26 E-value: 4.81e-04
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| CuRO_2_Fet3p_like | cd13877 | The second Cupredoxin domain of multicopper oxidase Fet3P; Fet3p catalyzes the ferroxidase ... |
376-421 | 5.62e-04 | |||||||||
The second Cupredoxin domain of multicopper oxidase Fet3P; Fet3p catalyzes the ferroxidase reaction, which couples the oxidation of Fe(II) to Fe(III) with the four-electron reduction of molecular oxygen to water. Fet3p is a type I membrane protein with the amino-terminal oxidase domain in the extracellular space and the carboxyl terminus in the cytoplasm. The periplasmic produced Fe(III) is transferred to the permease Ftr1p for import into the cytosol. The four copper ions are inserted post-translationally and are essential for catalytic activity, thus linking copper and iron homeostasis. Like other related multicopper oxidases (MCOs), Fet3p is composed of three cupredoxin domains that include one mononuclear and one trinuclear copper center. The copper ions are bound in several sites: Type 1, Type 2, and/or Type 3. The ensemble of types 2 and 3 copper is called a trinuclear cluster. MCOs oxidize their substrate by accepting electrons at a mononuclear copper center and transferring them to the active site trinuclear copper center. The cupredoxin domain 2 of 3-domain MCOs has lost the ability to bind copper. Pssm-ID: 259945 [Multi-domain] Cd Length: 148 Bit Score: 40.23 E-value: 5.62e-04
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| CuRO_3_Abr2_like | cd13898 | The third cupredoxin domain of a group of fungal Laccases similar to Abr2 from Aspergillus ... |
391-457 | 5.96e-04 | |||||||||
The third cupredoxin domain of a group of fungal Laccases similar to Abr2 from Aspergillus fumigatus; Abr2 is involved in conidial pigment biosynthesis in Aspergillus fumigatus. Laccase is a blue multi-copper enzyme that catalyzes the oxidation of a variety aromatic - notably phenolic and inorganic substances coupled to the reduction of molecular oxygen to water. Laccase has been implicated in a wide spectrum of biological activities and, in particular, plays a key role in morphogenesis, development and lignin metabolism in fungi and plants. Like other related multicopper oxidases (MCOs), laccase is composed of three cupredoxin domains that include one mononuclear and one trinuclear copper center. The copper ions are bound in several sites: Type 1, Type 2, and/or Type 3. The ensemble of types 2 and 3 copper is called a trinuclear cluster. MCOs oxidize their substrate by accepting electrons at a mononuclear copper center and transferring them to the active site trinuclear copper center. The cupredoxin domain 3 of 3-domain MCOs contains the Type 1 (T1) copper binding site and part the trinuclear copper binding site, which is located at the interface of domains 1 and 3. Pssm-ID: 259965 [Multi-domain] Cd Length: 164 Bit Score: 40.32 E-value: 5.96e-04
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| CuRO_3_PHS | cd13892 | The third Cupredoxin domain of phenoxazinone synthase (PHS); Phenoxazinone synthase (PHS, ... |
376-454 | 1.04e-03 | |||||||||
The third Cupredoxin domain of phenoxazinone synthase (PHS); Phenoxazinone synthase (PHS, 2-aminophenol:oxygen oxidoreductase) catalyzes the oxidative coupling of substituted o-aminophenols to produce phenoxazinones. PHS has been shown to participate in diverse biological functions such as spore pigmentation and biosynthesis of the antibiotic grixazone. PHS is a member of the laccase-like multicopper oxidase (MCO) family, which are able to couple oxidation of substrates with reduction of dioxygen to water. MCOs are capable of oxidizing a vast range of substrates, varying from aromatic compounds to inorganic compounds such as metals. Although the members of this family have diverse functions, majority of them have three cupredoxin domain repeats. The copper ions are bound in several sites: Type 1, Type 2, and/or Type 3. The ensemble of types 2 and 3 copper is called a trinuclear cluster. MCOs oxidize their substrate by accepting electrons at a mononuclear copper center and transferring them to the active site trinuclear copper center. The cupredoxin domain 3 of 3-domain MCOs contains the Type 1 (T1) copper binding site and part the trinuclear copper binding site, which is located at the interface of domains 1 and 3. Pssm-ID: 259959 [Multi-domain] Cd Length: 184 Bit Score: 40.21 E-value: 1.04e-03
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| CuRO_D1_2dMcoN_like | cd13859 | The first cupredoxin domain of bacterial two domain multicopper oxidase McoN and similar ... |
364-445 | 1.66e-03 | |||||||||
The first cupredoxin domain of bacterial two domain multicopper oxidase McoN and similar proteins; This family includes bacterial two domain multicopper oxidases (2dMCOs) represented by the McoN from Nitrosomonas europaea. McoN is a trimeric type C blue copper oxidase. Each subunit houses a type 1 copper site in domain 1 and a type 2/type 3 trinuclear copper cluster at the subunit-subunit interface. The 2dMCO is proposed to be a key intermediate in the evolution of three domain MCOs. Its biological function has not been characterized. Multicopper oxidases couple oxidation of substrates with reduction of dioxygen to water. These MCOs are capable of oxidizing a vast range of substrates, varying from aromatic to inorganic compounds such as metals. Pssm-ID: 259928 [Multi-domain] Cd Length: 122 Bit Score: 38.23 E-value: 1.66e-03
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| NosZ | COG4263 | Nitrous oxide reductase [Inorganic ion transport and metabolism]; |
68-133 | 1.66e-03 | |||||||||
Nitrous oxide reductase [Inorganic ion transport and metabolism]; Pssm-ID: 443405 [Multi-domain] Cd Length: 621 Bit Score: 40.66 E-value: 1.66e-03
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| CuRO_2_MCO_like_2 | cd13887 | The second cupredoxin domain of uncharacterized multicopper oxidase; Multicopper Oxidases ... |
206-276 | 2.48e-03 | |||||||||
The second cupredoxin domain of uncharacterized multicopper oxidase; Multicopper Oxidases (MCOs) are multi-domain enzymes that are able to couple oxidation of substrates with reduction of dioxygen to water. MCOs oxidise their substrate by accepting electrons at a mononuclear copper centre and transferring them to a trinuclear copper centre which binds a dioxygen. The dioxygen, following the transfer of four electrons, is reduced to two molecules of water. These MCOs are capable of oxidizing a vast range of substrates, varying from aromatic to inorganic compounds such as metals. This family of MCOs is composed of three cupredoxin domains that include one mononuclear and one trinuclear copper center. The copper ions are bound in several sites: Type 1, Type 2, and/or Type 3. The ensemble of types 2 and 3 copper is called a trinuclear cluster. MCOs oxidize their substrate by accepting electrons at a mononuclear copper center and transferring them to the active site trinuclear copper center. The cupredoxin domain 2 of 3-domain MCOs has lost the ability to bind copper. Pssm-ID: 259954 [Multi-domain] Cd Length: 114 Bit Score: 37.69 E-value: 2.48e-03
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| Cu-oxidase_2 | pfam07731 | Multicopper oxidase; This entry contains many divergent copper oxidase-like domains that are ... |
59-157 | 2.64e-03 | |||||||||
Multicopper oxidase; This entry contains many divergent copper oxidase-like domains that are not recognized by the pfam00394 model. Pssm-ID: 462246 [Multi-domain] Cd Length: 138 Bit Score: 38.19 E-value: 2.64e-03
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| CuRO_2_LCC_plant | cd13875 | The second cupredoxin domain of the plant laccases; Laccase is a blue multi-copper enzyme that ... |
376-422 | 7.42e-03 | |||||||||
The second cupredoxin domain of the plant laccases; Laccase is a blue multi-copper enzyme that catalyzes the oxidation of a variety aromatic - notably phenolic and inorganic substances coupled to the reduction of molecular oxygen to water. Laccase has been implicated in a wide spectrum of biological activities and, in particular, plays a key role in morphogenesis, development and lignin metabolism. Plants usually express multiple laccase genes, but their precise physiological/biochemical roles remain largely unclear. Like other related multicopper oxidases (MCOs), laccase is composed of three cupredoxin domains that include one mononuclear and one trinuclear copper center. The copper ions are bound in several sites: Type 1, Type 2, and/or Type 3. The ensemble of types 2 and 3 copper is called a trinuclear cluster. MCOs oxidize their substrate by accepting electrons at a mononuclear copper center and transferring them to the active site trinuclear copper center. The cupredoxin domain 2 of 3-domain MCOs has lost the ability to bind copper. Pssm-ID: 259943 [Multi-domain] Cd Length: 148 Bit Score: 36.81 E-value: 7.42e-03
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