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.

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3CG8_B       48 VRHLKMYAEKLADGQMGYGFEKGKASVPGPLIEVNEGDTLHIEFTNTMDVRASLHVHGLDYEISSDGTAMNKSDVEPGGT 127
Cdd:cd14449   1 ARHLEMYAEKLTDDAWGYGLKGGVATVPGPVIEVREGDTLKILFRNTLDVPASLHPHGVDYTTASDGTGMNASIVAPGDT 80

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*
3CG8_B      128 RTYTWRTHKPGRRDDGTWRPGSAGYWHYHDHVVGTEHGTGGIRNGLYGPVIVRRK 182
Cdd:cd14449  81 RIYTWRTHGGYRRADGSWAEGTAGYWHYHDHVFGTEHGTEGLSRGLYGALIVRRV 135

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.

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3CG8_B       48 VRHLKMYAEKLADGQMGYGFEKGKASVPGPLIEVNEGDTLHIEFTNTMDVRASLHVHGLDYEISSDGTAMNKSDVEPGGT 127
Cdd:cd14449   1 ARHLEMYAEKLTDDAWGYGLKGGVATVPGPVIEVREGDTLKILFRNTLDVPASLHPHGVDYTTASDGTGMNASIVAPGDT 80

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*
3CG8_B      128 RTYTWRTHKPGRRDDGTWRPGSAGYWHYHDHVVGTEHGTGGIRNGLYGPVIVRRK 182
Cdd:cd14449  81 RIYTWRTHGGYRRADGSWAEGTAGYWHYHDHVFGTEHGTEGLSRGLYGALIVRRV 135

Multicopper oxidase; This entry contains many divergent copper oxidase-like domains that are not recognized by the pfam00394 model.

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3CG8_B        196 NDMTINNRKPHTG-PDFEATVGDRVEIVMITHGEYYHTFHMHGHRWADNRTGILTGPDDPSRVIDNKITGPADSF----- 269
Cdd:pfam07731  20 NDWAINGLLFPPNtNVITLPYGTVVEWVLQNTTTGVHPFHLHGHSFQVLGRGGGPWPEEDPKTYNLVDPVRRDTVqvppg 99

                          90       100       110
                  ....*....|....*....|....*....|....*....
3CG8_B        270 GFQIIAGEGVGAGAWMYHCHVQSHSDMGMVGLFLVKKPD 308
Cdd:pfam07731 100 GWVAIRFRADNPGVWLFHCHILWHLDQGMMGQFVVRPGD 138

Multicopper oxidase; This entry contains many divergent copper oxidase-like domains that are not recognized by the pfam00394 model.

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3CG8_B         73 SVPGPLIEVNEGDTLHIEFTNTMDVRASLHVHGLDY--EISSDGTAMNKSD-VEPGGTRTYTWRTHKPGrrddGTwrpgs 149
Cdd:pfam07732  23 QFPGPTIRVREGDTVVVNVTNNLDEPTSIHWHGLQQrgTPWMDGVPGVTQCpIPPGQSFTYRFQVKQQA----GT----- 93

                          90       100       110
                  ....*....|....*....|....*....|....*.
3CG8_B        150 agYWhYHDHvvgtehgTGGIR-NGLYGPVIVRRKGD 184
Cdd:pfam07732  94 --YW-YHSH-------TSGQQaAGLAGAIIIEDRAS 119

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        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3CG8_B         75 PGPLIEVNEGDTLHIEFTNTMDVRA-SLHVHGLdYEISS---DGTA-MNKSDVEPGGTRTYTWRTHKPGRrddgtwrpgs 149
Cdd:TIGR03388  30 PGPTIRAQAGDTIVVELTNKLHTEGvVIHWHGI-RQIGTpwaDGTAgVTQCAINPGETFIYNFVVDRPGT---------- 98

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|...
3CG8_B        150 agyWHYHDHVvgtehgtGGIRN-GLYGPVIVR-RKGDVLP---DATHTIVFND 197
Cdd:TIGR03388  99 ---YFYHGHY-------GMQRSaGLYGSLIVDvPDGEKEPfhyDGEFNLLLSD 141

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        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3CG8_B        187 PDATHTIVfndMTINNRKPhtGPDFEATVGDRVeIVMITHGeyYHT----FHMHGHR-----WADNRTGILTGPddpsrv 257
Cdd:TIGR03388  15 PDCFEKLV---IGINGQFP--GPTIRAQAGDTI-VVELTNK--LHTegvvIHWHGIRqigtpWADGTAGVTQCA------ 80

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|..
3CG8_B        258 idnkiTGPADSFGFQIIAGEgvgAGAWMYHCHVQSHSDMGMVGLFLVKKPDG 309
Cdd:TIGR03388  81 -----INPGETFIYNFVVDR---PGTYFYHGHYGMQRSAGLYGSLIVDVPDG 124

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.

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3CG8_B       48 VRHLKMYAEKLADGQMGYGFEKGKASVPGPLIEVNEGDTLHIEFTNTMDVRASLHVHGLDYEISSDGTAMNKSDVEPGGT 127
Cdd:cd14449   1 ARHLEMYAEKLTDDAWGYGLKGGVATVPGPVIEVREGDTLKILFRNTLDVPASLHPHGVDYTTASDGTGMNASIVAPGDT 80

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*
3CG8_B      128 RTYTWRTHKPGRRDDGTWRPGSAGYWHYHDHVVGTEHGTGGIRNGLYGPVIVRRK 182
Cdd:cd14449  81 RIYTWRTHGGYRRADGSWAEGTAGYWHYHDHVFGTEHGTEGLSRGLYGALIVRRV 135

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        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3CG8_B       37 ITARTAPAGGEVRHLKM-YAE-KLADGQ----MGYGfekgkASVPGPLIEVNEGDTLHIEFTNTMDVRASLHVHGLDYEI 110
Cdd:COG2132   4 IPPLLESGGGREYELTAqPATvELLPGKpttvWGYN-----GQYPGPTIRVREGDRVRVRVTNRLPEPTTVHWHGLRVPN 78

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3CG8_B      111 SSDGTAMNKsdVEPGGTRTYTWRTHKPGrrddGTwrpgsagYWhYHDHVvgteHGTGG--IRNGLYGPVIVRRKGDVLP- 187
Cdd:COG2132  79 AMDGVPGDP--IAPGETFTYEFPVPQPA----GT-------YW-YHPHT----HGSTAeqVYRGLAGALIVEDPEEDLPr 140

                       170
                ....*....|....*.
3CG8_B      188 -DATHTIVFNDMTINN 202
Cdd:COG2132 141 yDRDIPLVLQDWRLDD 156

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.

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3CG8_B       73 SVPGPLIEVNEGDTLHIEFTNTMDVRASLHVHGLDYEISSDGTA-MNKSDVEPGGTRTYTWRThkpgrRDDGTwrpgsag 151
Cdd:cd13861  28 QVPGPELRVRQGDTLRVRLTNRLPEPTTIHWHGLRLPNAMDGVPgLTQPPVPPGESFTYEFTP-----PDAGT------- 95

                        90       100
                ....*....|....*....|....*....
3CG8_B      152 YWhYHDHVVGTEHgtggIRNGLYGPVIVR 180
Cdd:cd13861  96 YW-YHPHVGSQEQ----LDRGLYGPLIVE 119

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.

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3CG8_B       73 SVPGPLIEVNEGDTLHIEFTNTMDVRASLHVHGLDYEISSDGTAMNKsdVEPGGTRTYTWRTHKpgrrddgtwrpGSAGY 152
Cdd:cd13855  29 SVPGPLIEVFEGDTVEITFRNRLPEPTTVHWHGLPVPPDQDGNPHDP--VAPGNDRVYRFTLPQ-----------DSAGT 95

                        90       100
                ....*....|....*....|....*...
3CG8_B      153 WHYHDHVVGteHGTGGIRNGLYGPVIVR 180
Cdd:cd13855  96 YWYHPHPHG--HTAEQVYRGLAGAFVVK 121

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.

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3CG8_B       76 GPLIEVNEGDTLHIEFTN---TMDVraSLHVHGLDYEISSDGTAMNKSD-VEPGGTRTYTWrtHKPGRRDDGTWRPGSAG 151
Cdd:cd04229  73 GPVIRAEVGDTIKVVFKNnldEFPV--NMHPHGGLYSKDNEGTTDGAGDvVAPGETYTYRW--IVPEDAGPGPGDPSSRL 148

                        90       100       110
                ....*....|....*....|....*....|..
3CG8_B      152 YWhYHDHVVGTEHGTGgirnGLYGPVIVRRKG 183
Cdd:cd04229 149 WL-YHSHVDVFAHTNA----GLVGPIIVTSKG 175

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.

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3CG8_B       75 PGPLIEVNEGDTLHIEFTNTMDVRASLHVHGLDYEISS--DGTA-MNKSDVEPGGTRTYTWRThkpgrrDD--GTwrpgs 149
Cdd:cd13857  29 PGPLIEANQGDRIVVHVTNELDEPTSIHWHGLFQNGTNwmDGTAgITQCPIPPGGSFTYNFTV------DGqyGT----- 97

                        90       100       110
                ....*....|....*....|....*....|
3CG8_B      150 agYWhYHDHvvgteHGTGGIrNGLYGPVIV 179
Cdd:cd13857  98 --YW-YHSH-----YSTQYA-DGLVGPLIV 118

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.

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3CG8_B       74 VPGPLIEVNEGDTLHIEFTNTMDVRASLHVHGLDYEISSDGTAMnksDVEPGGTRTYtwrthkpgrrddgTWRPGSAGYW 153
Cdd:cd11024  30 VPGPTLRATEGDLVRIHFINTGDHPHTIHFHGIHDAAMDGTGLG---PIMPGESFTY-------------EFVAEPAGTH 93

                        90       100
                ....*....|....*....|....*..
3CG8_B      154 HYHDHVV-GTEHgtggIRNGLYGPVIV 179
Cdd:cd11024  94 LYHCHVQpLKEH----IAMGLYGAFIV 116

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.

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3CG8_B      184 DVLPDATHTIVFNDMTiNNRKPHTGPDFEATVGDRVEIVMI--THGEYYHTFHMHGHRWADNRTGilTGPDDPSRVIDNK 261
Cdd:cd04207  11 TGAPDGTTRWVINGMP-FKEGDANTDIFSVEAGDVVEIVLInaGNHDMQHPFHLHGHSFWVLGSG--GGPFDAPLNLTNP 87

                        90       100       110       120
                ....*....|....*....|....*....|....*....|....
3CG8_B      262 I---TGPADSFGFQIIAGEGVGAGAWMYHCHVQSHSDMGMVGLF 302
Cdd:cd04207  88 PwrdTVLVPPGGWVVIRFKADNPGVWMLHCHILEHEDAGMMTVF 131

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.

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3CG8_B       74 VPGPLIEVNEGDTLHIEFTNTMDVRASLHVHGLDYEIS--SDGTA-MNKSDVEPGGTRTYTWRTHKPGRrddgtwrpgsa 150
Cdd:cd13859  29 VPGPLIHVKEGDDLVVHVTNNTTLPHTIHWHGVLQMGSwkMDGVPgVTQPAIEPGESFTYKFKAERPGT----------- 97

                        90       100
                ....*....|....*....|....*....
3CG8_B      151 gYWhYHDHVVGTEHgtGGIRnGLYGPVIV 179
Cdd:cd13859  98 -LW-YHCHVNVNEH--VGMR-GMWGPLIV 121

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.

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3CG8_B       76 GPLIEVNEGDTLHIEFTNTMDVRASLHVHGLDYEISSDG-------TAMNKSD--VEPGGTRTYTWRTHK---PGrRDDG 143
Cdd:cd04199  69 GPTIRAEVGDTIKVHFKNKASRPYSIHPHGVSYEKDSEGasysdqtGPDEKKDdaVAPGETYTYVWIVTEesgPT-KGDP 147

                        90       100       110
                ....*....|....*....|....*....|....*....
3CG8_B      144 TWRPgsagyWHYHDHVVGTEHgtggIRNGLYGPVIVRRK 182
Cdd:cd04199 148 ACLT-----WAYYSHVDLEKD----INSGLIGPLLICKK 177

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.

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3CG8_B       76 GPLIEVNEGDTLHIEFTNTMDVRASLHVHGLDYEISSDGTAMNKSD------VEPGGTRTYTWRTHKPGRRDDGTwrPGS 149
Cdd:cd04224  82 GPVIRAEVGDTIKVTFRNKASRPFSIQPHGVFYEKNYEGAMYRDGDpspgshVSPGETFTYEWTVPEGVGPTNQD--PPC 159

                        90       100       110       120
                ....*....|....*....|....*....|....*....|...
3CG8_B      150 AGYWHYH--DHVVGTEhgtggirNGLYGPVIVRRKGDVLPDAT 190
Cdd:cd04224 160 LTYLYFSavDPVRDTN-------SGLVGPLLVCKKGSLNANGR 195

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.

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3CG8_B      197 DMTINNRK-PHTGPDFEATVGDrVEIVMITHGEY-YHTFHMHGHRW----------ADNRTG----ILTGPDDPSRVIdN 260
Cdd:cd13890  15 AFTINGKRfDMNRIDFTVKLGT-TEIWEVTNTDGmPHPFHIHGVQFrilsrngqppPPNEAGwkdtVWVPPGETVRIL-V 92

                        90       100       110       120
                ....*....|....*....|....*....|....*....|....
3CG8_B      261 KITGPADSfgfqiiagegvgAGAWMYHCHVQSHSDMGMVGLFLV 304
Cdd:cd13890  93 KFDHYADP------------TGPFMYHCHILEHEDNGMMGQFVV 124

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.

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3CG8_B       73 SVPGPLIEVNEGDTLHIEFTNTMDVRASlhvHGLDYEISSDGTAMNKSDVEPGGTRTYTWRTHKPgrrddgtwrpgsaGY 152
Cdd:cd11020  29 QVPGPVIRVREGDTVELTLTNPGTNTMP---HSIDFHAATGPGGGEFTTIAPGETKTFSFKALYP-------------GV 92

                        90       100
                ....*....|....*....|....*...
3CG8_B      153 WHYHDHVVGT-EHgtggIRNGLYGPVIV 179
Cdd:cd11020  93 FMYHCATAPVlMH----IANGMYGAIIV 116

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.

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3CG8_B      199 TINNRKPHTGPDFEATVGDRVEIVMITHGEYYHTFHMHGHRWAdnrtgiLTGPDDPSRVI-DNKITGPADSFGFQIIAGE 277
Cdd:cd13896  18 TINGKAYPDADPLRVREGERVRIVFVNDTMMAHPMHLHGHFFQ------VENGNGEYGPRkDTVLVPPGETVSVDFDADN 91

                        90       100
                ....*....|....*....|.
3CG8_B      278 gvgAGAWMYHCHVQSHSDMGM 298
Cdd:cd13896  92 ---PGRWAFHCHNLYHMEAGM 109

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.

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3CG8_B       76 GPLIEVNEGDTLHIEFTNTMDVRASLHVHGLDYEISSDGTAMNKsdVEPGGTRTYTWRTHKPgrrddgtwrpgSAGYWhY 155
Cdd:cd04232  31 GPTIRVKKGDTVRINVTNNLDEETTVHWHGLHVPGEMDGGPHQP--IAPGQTWSPTFTIDQP-----------AATLW-Y 96

                        90       100
                ....*....|....*....|....*..
3CG8_B      156 HDHVvgteHGTGGIR--NGLYGPVIVR 180
Cdd:cd04232  97 HPHT----HGKTAEQvyRGLAGLFIIE 119

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.

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3CG8_B       74 VPGPLIEVNEGDTLHIEFTNTM-DVRASLHVHGLDYEIS--SDGT-AMNKSDVEPGGTRTYTWRTHKPGRrddgTWrpgs 149
Cdd:cd13854  31 YPGPLIEANWGDTIEVTVINKLqDNGTSIHWHGIRQLNTnwQDGVpGVTECPIAPGDTRTYRFRATQYGT----SW---- 102

                        90       100       110
                ....*....|....*....|....*....|
3CG8_B      150 agywhYHDHvVGTEHGtggirNGLYGPVIV 179
Cdd:cd13854 103 -----YHSH-YSAQYG-----DGVVGPIVI 121

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.

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3CG8_B      209 PDFEATVGDRVEIVMITHGEYYHTFHMHGHRW-ADNRTGILtgpdDPSRviDNKITGPADSFGFQIIAGEgvgAGAWMYH 287
Cdd:cd13909  49 PLLEARRGETVRIEMVNNTGFPHGMHLHGHHFrAILPNGAL----GPWR--DTLLMDRGETREIAFVADN---PGDWLLH 119

                        90
                ....*....|....*..
3CG8_B      288 CHVQSHSDMGMVGLFLV 304
Cdd:cd13909 120 CHMLEHAAAGMMSWFRV 136

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.

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3CG8_B       73 SVPGPLIEVNEGDTLHIEFTNTMD-VRASLHVHGLDYEIS--SDGTAM-NKSDVEPGGTRTYTWRThkpgrrddgtwRPG 148
Cdd:cd13847  23 SFPGPELRVQEGQHLWVRVYNDLEaGNTTMHFHGLSQYMSpfSDGTPLaSQWPIPPGKFFDYEFPL-----------EAG 91

                        90       100       110
                ....*....|....*....|....*....|.
3CG8_B      149 SAGYWHYHDHvVGTEHGTGgirnglYGPVIV 179
Cdd:cd13847  92 DAGTYYYHSH-VGFQSVTA------YGALIV 115

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.

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3CG8_B      187 PDATHTIVFNDMTINNRKPHTGPDFEATVGDRVEIVMITHGEYYHTFHMHGHRWADNRTGILTGPDDPSRVIDNKITGPA 266
Cdd:cd04202  19 PMPPEGMDFNYFTINGKSFPATPPLVVKEGDRVRIRLINLSMDHHPMHLHGHFFLVTATDGGPIPGSAPWPKDTLNVAPG 98

                        90       100       110       120
                ....*....|....*....|....*....|....*....|...
3CG8_B      267 DSFGFQIIAGEgvgAGAWMYHCHVQSH----SDMGMVGLFLVK 305
Cdd:cd04202  99 ERYDIEFVADN---PGDWMFHCHKLHHamngMGGGMMTLIGYE 138

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.

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3CG8_B       75 PGPLIEVNEGDTLHIEFTNTMDVRA-SLHVHGLdYEISS---DGTA-MNKSDVEPGGTRTYTWRTHKPGRrddgtwrpgs 149
Cdd:cd13845  29 PGPTIRATAGDTIVVELENKLPTEGvAIHWHGI-RQRGTpwaDGTAsVSQCPINPGETFTYQFVVDRPGT---------- 97

                        90       100       110
                ....*....|....*....|....*....|
3CG8_B      150 agyWHYHDHvVGTEHGTggirnGLYGPVIV 179
Cdd:cd13845  98 ---YFYHGH-YGMQRSA-----GLYGSLIV 118

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        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3CG8_B         75 PGPLIEVNEGDTLHIEFTNTMDVRA-SLHVHGLdYEISS---DGTA-MNKSDVEPGGTRTYTWRTHKPGRrddgtwrpgs 149
Cdd:TIGR03388  30 PGPTIRAQAGDTIVVELTNKLHTEGvVIHWHGI-RQIGTpwaDGTAgVTQCAINPGETFIYNFVVDRPGT---------- 98

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|...
3CG8_B        150 agyWHYHDHVvgtehgtGGIRN-GLYGPVIVR-RKGDVLP---DATHTIVFND 197
Cdd:TIGR03388  99 ---YFYHGHY-------GMQRSaGLYGSLIVDvPDGEKEPfhyDGEFNLLLSD 141