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.

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2001526075  34 KREIFRLQQGKTYLVRILNAASLAFYNIAIASH-YFTILGVDGrSFTEPVDVNSIDLSSGQRYMALLhynppiqsahnyE 112
Cdd:TIGR03390 196 MLPVIDVEPGKTYRLRFIGATALSLISLGIEDHeNLTIIEADG-SYTKPAKIDHLQLGGGQRYSVLF------------K 262

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2001526075 113 TNAVNTLNAQN-LTYVMQVQTdwrgDDRTNAGISYAYVTYDENTDVIDTSLTDISPISPLNESRDWQEwYTLLQAIELPl 191
Cdd:TIGR03390 263 AKTEDELCGGDkRQYFIQFET----RDRPKVYRGYAVLRYRSDKASKLPSVPETPPLPLPNSTYDWLE-YELEPLSEEN- 336

                         170       180
                  ....*....|....*....|...
gi 2001526075 192 lsgVPLCPSSNEVTKSFTLHVKQ 214
Cdd:TIGR03390 337 ---NQDFPTLDEVTRRVVIDAHQ 356

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        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2001526075  33 GKREIFRLQQGKTYLVRILNAASLAFYNIAIASHYFTILGVDGrSFTEPVDVNSIDLSSGQRYMALLhynppiqsahnye 112
Cdd:cd04205    53 CPLPVITVEPGKTYRLRLINAGSFASFNFAIDGHNMTVIEVDG-GYVEPLEVDNLDLAPGQRYDVLV------------- 118

                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 2001526075 113 tnavnTLNAQNLTYVMQVQTDWRGDDRTNAGISYAYVTY 151
Cdd:cd04205   119 -----KADQPPGNYWIRASADGRTFDEGGNPNGTAILRY 152

L-ascorbate oxidase

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2001526075  19 YNDGTQSSISTYCKGKR---EIFRLQQGKTYLVRILNAASLAFYNIAIASHYFTILGVDGrSFTEPVDVNSIDLSSGQRY 95
Cdd:PLN02191  206 FSNGTELPMCTFKEGDQcapQTLRVEPNKTYRIRLASTTALASLNLAVQGHKLVVVEADG-NYITPFTTDDIDIYSGESY 284

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2001526075  96 MALLhynppiqsahnyetnAVNTLNAQNltYVMQVQTDWRGDDRTNAGISYAYVTYDENTdvidtsltdiSPISPlnesr 175
Cdd:PLN02191  285 SVLL---------------TTDQDPSQN--YYISVGVRGRKPNTTQALTILNYVTAPASK----------LPSSP----- 332

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2001526075 176 dwqewytllqaielPllsgvPLCPSSNEVTKSFTLHVKqqmidISSGKGL-TPPASSG------NSDGVQLGWTVY--NN 246
Cdd:PLN02191  333 --------------P-----PVTPRWDDFERSKNFSKK-----IFSAMGSpSPPKKYRkrlillNTQNLIDGYTKWaiNN 388

                         250
                  ....*....|.
gi 2001526075 247 SRLMMPTTPYL 257
Cdd:PLN02191  389 VSLVTPATPYL 399

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
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 2001526075  38 FRLQQGKTYLVRILNAASLAFYNIAIAS-HYFTILGVDGRSFTEPVDVNSIDLSSGQRY 95
Cdd:COG2132   186 LEVRPGERVRLRLLNASNARIYRLALSDgRPFTVIATDGGLLPAPVEVDELLLAPGERA 244

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        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2001526075  33 GKREIFRLQQGKTYLVRILNAASLAFYNIAIASHYFTILGVDGrSFTEPVDVNSIDLSSGQRYMALLhynppiqsahnye 112
Cdd:cd04205    53 CPLPVITVEPGKTYRLRLINAGSFASFNFAIDGHNMTVIEVDG-GYVEPLEVDNLDLAPGQRYDVLV------------- 118

                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 2001526075 113 tnavnTLNAQNLTYVMQVQTDWRGDDRTNAGISYAYVTY 151
Cdd:cd04205   119 -----KADQPPGNYWIRASADGRTFDEGGNPNGTAILRY 152

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.

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2001526075  19 YNDGTQSSISTYCKGKREIFRLQQGKTYLVRILNAASLAFYNIAIASHYFTILGVDGrSFTEPVDVNSIDLSSGQRYMAL 98
Cdd:cd13886    45 CASATYKIYCCASNGTYYNFTLEPNKTYRLRLINAGSFADFTFSVDGHPLTVIEADG-TLVEPVEVHSITISVAQRYSVI 123

                  ....*.
gi 2001526075  99 LHYNPP 104
Cdd:cd13886   124 LTTNQP 129

The second 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. 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        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2001526075  19 YNDGTQSSISTyckgkreiFRLQQGKTYLVRILNAASLAFYNIAIASHYFTILGVDGRSfTEPVDVNSIDLSSGQRYMAL 98
Cdd:cd13882    38 FDGGPTSPLAV--------INVKRGKRYRFRVINISCIPSFTFSIDGHNLTVIEADGVE-TKPLTVDSVQIYAGQRYSVV 108

                          90
                  ....*....|....*..
gi 2001526075  99 LHYNppiQSAHNYETNA 115
Cdd:cd13882   109 VEAN---QPVDNYWIRA 122

The second cupredoxin domain of the insect laccases similar to laccase 2 in Tribolium castaneum; This multicopper oxidase (MCO) subfamily includes the majority of insect laccases. One member is laccase 2 from Tribolium castaneum, which 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. 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        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2001526075  35 REIFRLQQGKTYLVRILNAASLAF-YNIAIASHYFTILGVDGrSFTEPVDVNSIDLSSGQRYMALLHYNPPIqsaHNY 111
Cdd:cd13884    54 LEVFTVEQGKRYRFRLINAGATNCpFRVSIDGHTLTVIASDG-NDVEPVEVDSIIIYPGERYDFVLNANQPI---GNY 127

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        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2001526075  31 CKGKrEIFRL--QQGKTYLVRILNAA---SLAFyniAIASHYFTILGVDGrSFTEPVDVNSIDLSSGQRYMALLHYNppi 105
Cdd:cd13875    45 CSSK-DTFVLtvEPGKTYLLRIINAAlneELFF---KIANHTLTVVAVDA-SYTKPFTTDYILIAPGQTTDVLLTAD--- 116

                  ....*.
gi 2001526075 106 QSAHNY 111
Cdd:cd13875   117 QPPGRY 122

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        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2001526075  35 REIFRLQQGKTYLVRILNAASLAFYNIAIASHYFTILGVDGRsFTEPVDVNSIDLSSGQRYMALLHYN 102
Cdd:cd13871    71 PFILHVSPGKTYRLRIASVTALSSLNFIIEGHNLTVVEADGN-YVQPFEVSNLDIYSGETYSVLVTAD 137

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.

                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*..
gi 2001526075  49 RILNAASLAFYNIAIASHYFTILGVDGRSFTEPVDVNSIDLSSGQRY 95
Cdd:cd13881    55 RIVNAASARYFRLALDGHKFRLIGTDGGLLEAPREVDELLLAPGERA 101

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
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 2001526075  38 FRLQQGKTYLVRILNAASLAFYNIAIAS-HYFTILGVDGRSFTEPVDVNSIDLSSGQRY 95
Cdd:COG2132   186 LEVRPGERVRLRLLNASNARIYRLALSDgRPFTVIATDGGLLPAPVEVDELLLAPGERA 244

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.

                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 2001526075  36 EIFRLQQGKTYLVRILNAASLAFYNIAIASHYFTILGVDGrSFTEPVDVNSIDLSSGQR 94
Cdd:cd13887    24 EVVRVEPGGRVRLRVINGSTATNFHIDLGDLKGTLIAVDG-NPVQPVEGRRFPLATAQR 81

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        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 2001526075  50 ILNAASLAFYNIAIASHYFTILGVDGRsFTEPVDVNSIDLSSGQRYMALLHYNPP 104
Cdd:cd13876    59 FINAGGFHTLAFSIDEHPMWVYAVDGG-YIEPQLVDAISITNGERYSVLVKLDKP 112

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.

                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 2001526075  45 TYLVRILNAASLAFYNIAIASH-YFTILGVDGRSFTEPVDVNSIDLSSGQRY 95
Cdd:cd14448    53 WYRLRLLNASNARHYNLALSDGlPFHVIGSDGGLLEAPVKVKELVLAPAERI 104

oxidoreductase

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2001526075  38 FRLQQGKTYLVRILNAASLAFYNIAIASHYFTILGVDGrSFTEPVDVNSIDLSSGQRYMALLHYNppiQSAHNYETNAVN 117
Cdd:PLN02835  204 FSGDQGKTYMFRISNVGLSTSLNFRIQGHTMKLVEVEG-SHTIQNIYDSLDVHVGQSVAVLVTLN---QSPKDYYIVAST 279

                  ....*...
gi 2001526075 118 TLNAQNLT 125
Cdd:PLN02835  280 RFTRQILT 287