Multicopper oxidase; Many of the proteins in this family contain multiple similar copies of this plastocyanin-like domain.

                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2051735853   1 MHIIEADGEYVNPVRVDSVWIHAGQRYSVVVKADQPPLNYWIRAGPLKgyEGFDNGRNSAILHYLEA 67
Cdd:pfam00394  82 MTVVEVDGVYVNPFTVDSLDIFPGQRYSVLVTANQDPGNYWIVASPNI--PAFDNGTAAAILRYSGA 146

Multicopper oxidase; Many of the proteins in this family contain multiple similar copies of this plastocyanin-like domain.

                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2051735853   1 MHIIEADGEYVNPVRVDSVWIHAGQRYSVVVKADQPPLNYWIRAGPLKgyEGFDNGRNSAILHYLEA 67
Cdd:pfam00394  82 MTVVEVDGVYVNPFTVDSLDIFPGQRYSVLVTANQDPGNYWIVASPNI--PAFDNGTAAAILRYSGA 146

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.

                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*.
gi 2051735853   1 MHIIEADGEYVNPVRVDSVWIHAGQRYSVVVKADQ-PPLNYWIRAG 45
Cdd:TIGR03388 235 LTVVEADGNYVEPFTVKDIDIYSGETYSVLLTTDQdPSRNYWISVG 280

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;

                          10        20        30
                  ....*....|....*....|....*....|....*...
gi 2051735853   1 MHIIEADGEYVN-PVRVDSVWIHAGQRYSVVVKADQPP 37
Cdd:COG2132   217 FTVIATDGGLLPaPVEVDELLLAPGERADVLVDFSADP 254

Multicopper oxidase; Many of the proteins in this family contain multiple similar copies of this plastocyanin-like domain.

                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2051735853   1 MHIIEADGEYVNPVRVDSVWIHAGQRYSVVVKADQPPLNYWIRAGPLKgyEGFDNGRNSAILHYLEA 67
Cdd:pfam00394  82 MTVVEVDGVYVNPFTVDSLDIFPGQRYSVLVTANQDPGNYWIVASPNI--PAFDNGTAAAILRYSGA 146

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.

                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2051735853   1 MHIIEADGEYVNPVRVDSVWIHAGQRYSVVVKADQPPLNYWIRAGPLKG-YEGFDNGRNSAILHY 64
Cdd:cd04205    88 MTVIEVDGGYVEPLEVDNLDLAPGQRYDVLVKADQPPGNYWIRASADGRtFDEGGNPNGTAILRY 152

The second 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 2 of 3-domain MCOs has lost the ability to bind copper.

                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....
gi 2051735853   1 MHIIEADGEYVNPVRVDSVWIHAGQRYSVVVKADQPPLNYWIRA 44
Cdd:cd13876    77 MWVYAVDGGYIEPQLVDAISITNGERYSVLVKLDKPPGDYTIRV 120

The second 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. MCOs couple oxidation of substrates with reduction of dioxygen to water. 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.

                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*.
gi 2051735853   1 MHIIEADGEYVNPVRVDSVWIHAGQRYSVVVKADQ-PPLNYWIRAG 45
Cdd:cd13871   104 LTVVEADGNYVQPFEVSNLDIYSGETYSVLVTADQdPSRNYWVSVN 149

The second 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. 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.

                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2051735853   1 MHIIEADGEYVNPVRVDSVWIHAGQRYSVVVKADQPPL-NYWIRAGPLKGYEGFDNGRNS--AILHY 64
Cdd:cd13880    83 LTVIAADFVPIVPYTTDSLNIGIGQRYDVIVEANQDPVgNYWIRAEPATGCSGTNNNPDNrtGILRY 149

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.

                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*.
gi 2051735853   1 MHIIEADGEYVNPVRVDSVWIHAGQRYSVVVKA-DQPPLNYWIRAG 45
Cdd:cd13877    78 MTIIEVDGVYVKPYPVDTLYIAVGQRYSVLVKAkNDTDRNYAIING 123

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.

                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2051735853   1 MHIIEADGEYVNPVRVDSVWIHAGQRYSVVVKADQPPLNYWIRAGPlkgYE-----GFDNGRNSAILHY 64
Cdd:cd13875    83 LTVVAVDASYTKPFTTDYILIAPGQTTDVLLTADQPPGRYYMAARP---YQsappvPFDNTTATAILEY 148

The second cupredoxin domain of plant pollen multicopper oxidase homologous to ascorbate oxidase; The proteins in this subfamily are expressed in plant pollen. They share homology to ascorbate oxidase and other members of the blue copper oxidase family. The expression of the protein is detected during germination and pollen tube growth. Ascorbate oxidase catalyzes the oxidation of ascorbic acid to dehydroascorbic acid. It is a member of the multicopper oxidase (MCO) family that couples oxidation of substrates with reduction of dioxygen to water. 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.

                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2051735853   1 MHIIEADGEYVNPVRVDSVWIHAGQRYSVVVKADQPPLNYWIRAGPLkgyegFDNGR--NSAILHY 64
Cdd:cd13872    81 MLLVETEGSYTAQNTYDSLDVHVGQSYSVLVTADQSPKDYYIVASSR-----FLSPEltGVAILHY 141

The second 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 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. Laccase is a multicopper oxidase (MCO) 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.

                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*..
gi 2051735853   1 MHIIEADGEYVN-PVRVDSVWIHAGQRYSVVVKADQPPL--NYWIRA 44
Cdd:cd13883    95 LNVVEADDTPVYgPTVVHRIPIHNGQRYSVIIDTTSGKAgdSFWLRA 141

oxidoreductase

                          10        20        30        40
                  ....*....|....*....|....*....|....*....|..
gi 2051735853   1 MHIIEADGEYVNPVRVDSVWIHAGQRYSVVVKADQPPLNYWI 42
Cdd:PLN02792  225 LKLIEVEGTHTVQSMYTSLDIHVGQTYSVLVTMDQPPQNYSI 266

The second cupredoxin domain of CopA copper resistance protein like family; The members of this family are copper resistance protein (CopA) homologs. CopA is multicopper oxidase (MCO) related to laccase and L-ascorbate oxidase, both copper-containing enzymes. CopA 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 2 of 3-domain MCOs has lost the ability to bind copper.

                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2051735853   1 MHIIEADGEYVNPVRVDSVWIHAGQRYSVVVKADQpplNYW-IRAGPlkgyEGfDNGRNSAILHY 64
Cdd:cd13870    61 LTVTHTDGFPVEPVEVDALLIGMGERYDAIVTANN---GIWpLVALP----EG-KDGQARAVLRY 117

copper ion binding / oxidoreductase

                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....
gi 2051735853   1 MHIIEADGEYVNPVRVDSVWIHAGQRYSVVVKADQPPLNYWIRA 44
Cdd:PLN02354  239 MKLVEMEGSHVLQNDYDSLDVHVGQCFSVLVTANQAPKDYYMVA 282

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;

                          10        20        30
                  ....*....|....*....|....*....|....*...
gi 2051735853   1 MHIIEADGEYVN-PVRVDSVWIHAGQRYSVVVKADQPP 37
Cdd:COG2132   217 FTVIATDGGLLPaPVEVDELLLAPGERADVLVDFSADP 254