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
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992389296  33 PLPVPPLLESRRGQPLFMTLQRSHWSFTQGTRAPVWGVNGRYLGPTIRVWKGDDVKLIYSNRLAENVSMTIAGLQVPGPL 112
Cdd:COG2132    1 PLPIPPLLESGGGREYELTAQPATVELLPGKPTTVWGYNGQYPGPTIRVREGDRVRVRVTNRLPEPTTVHWHGLRVPNAM 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992389296 113 MGGPARMMSPNADWAPVLPIRQNAATLWYHANTPNRTAQQVYNGLAGMWLVEDEVSKslpIPNhyGVDDFPIIIQDKRLD 192
Cdd:COG2132   81 DGVPGDPIAPGETFTYEFPVPQPAGTYWYHPHTHGSTAEQVYRGLAGALIVEDPEED---LPR--YDRDIPLVLQDWRLD 155

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992389296 193 NFGTPEYSEPGS-GGFVGDTLLVNGVQSPYVEVSRG-WVRLRLLNASNSRRYQLQMSDGRALHVISGDQGFLPAPVSVKQ 270
Cdd:COG2132  156 DDGQLLYPMDAAmGGRLGDTLLVNGRPNPTLEVRPGeRVRLRLLNASNARIYRLALSDGRPFTVIATDGGLLPAPVEVDE 235

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992389296 271 LSLAPGERREILVDMTNGDevsitcGEAASIVDRirgfFEPSSILVstlVLTLRPTGLLPlvTDSLPMRLLP-TEIMSGT 349
Cdd:COG2132  236 LLLAPGERADVLVDFSADP------GEEVTLANP----FEGRSGRA---LLTLRVTGAAA--SAPLPANLAPlPDLEDRE 300

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992389296 350 PIRSRDISLGDDPG-----INGQLWDVNRIDITAQQGSWERWTVRAD--MPQSFHIEGVSFLVRNVNGAMpfPEDRGWKD 422
Cdd:COG2132  301 AVRTRELVLTGGMAgyvwtINGKAFDPDRPDLTVKLGERERWTLVNDtmMPHPFHLHGHQFQVLSRNGKP--PPEGGWKD 378

                        410       420       430       440
                 ....*....|....*....|....*....|....*....|....*...
gi 992389296 423 TVWVD--GQVELLVYYGQPswaHFPFYFHSQTLEMADRGSIGQILVNP 468
Cdd:COG2132  379 TVLVPpgETVRILFRFDNY---PGDWMFHCHILEHEDAGMMGQFEVVP 423

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
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992389296   51 TLQRSHWSFTQGTRAPVWGVNGRYLGPTIRVWKGDDVKLIYSNRLAENVSMTIAGLQVPGP-----LMGGPARMMSPNAD 125
Cdd:pfam07732   1 TVTYGTVSPLGGTRQAVIGVNGQFPGPTIRVREGDTVVVNVTNNLDEPTSIHWHGLQQRGTpwmdgVPGVTQCPIPPGQS 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|...
gi 992389296  126 WAPVLPIRQNAATLWYHANTPnrtAQQVyNGLAGMWLVEDEVS 168
Cdd:pfam07732  81 FTYRFQVKQQAGTYWYHSHTS---GQQA-AGLAGAIIIEDRAS 119

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
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992389296  33 PLPVPPLLESRRGQPLFMTLQRSHWSFTQGTRAPVWGVNGRYLGPTIRVWKGDDVKLIYSNRLAENVSMTIAGLQVPGPL 112
Cdd:COG2132    1 PLPIPPLLESGGGREYELTAQPATVELLPGKPTTVWGYNGQYPGPTIRVREGDRVRVRVTNRLPEPTTVHWHGLRVPNAM 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992389296 113 MGGPARMMSPNADWAPVLPIRQNAATLWYHANTPNRTAQQVYNGLAGMWLVEDEVSKslpIPNhyGVDDFPIIIQDKRLD 192
Cdd:COG2132   81 DGVPGDPIAPGETFTYEFPVPQPAGTYWYHPHTHGSTAEQVYRGLAGALIVEDPEED---LPR--YDRDIPLVLQDWRLD 155

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992389296 193 NFGTPEYSEPGS-GGFVGDTLLVNGVQSPYVEVSRG-WVRLRLLNASNSRRYQLQMSDGRALHVISGDQGFLPAPVSVKQ 270
Cdd:COG2132  156 DDGQLLYPMDAAmGGRLGDTLLVNGRPNPTLEVRPGeRVRLRLLNASNARIYRLALSDGRPFTVIATDGGLLPAPVEVDE 235

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992389296 271 LSLAPGERREILVDMTNGDevsitcGEAASIVDRirgfFEPSSILVstlVLTLRPTGLLPlvTDSLPMRLLP-TEIMSGT 349
Cdd:COG2132  236 LLLAPGERADVLVDFSADP------GEEVTLANP----FEGRSGRA---LLTLRVTGAAA--SAPLPANLAPlPDLEDRE 300

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992389296 350 PIRSRDISLGDDPG-----INGQLWDVNRIDITAQQGSWERWTVRAD--MPQSFHIEGVSFLVRNVNGAMpfPEDRGWKD 422
Cdd:COG2132  301 AVRTRELVLTGGMAgyvwtINGKAFDPDRPDLTVKLGERERWTLVNDtmMPHPFHLHGHQFQVLSRNGKP--PPEGGWKD 378

                        410       420       430       440
                 ....*....|....*....|....*....|....*....|....*...
gi 992389296 423 TVWVD--GQVELLVYYGQPswaHFPFYFHSQTLEMADRGSIGQILVNP 468
Cdd:COG2132  379 TVLVPpgETVRILFRFDNY---PGDWMFHCHILEHEDAGMMGQFEVVP 423

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.

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992389296 180 DDFPIIIQDKRLDNFGTPEY-SEPGSGGFVGDTLLVNGVQSPYVEVSRGWVRLRLLNASNSRRYQLQMSDGRALHVISGD 258
Cdd:cd13867    1 DDIPLILQDRRFDEDGQLDYrMMDDMDGFLGDTLLVNGTINPYLDVPRGWVRLRLLNGSNARTYNLGFSDNRPFYQIASD 80

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 992389296 259 QGFLPAPVSVKQLSLAPGERREILVDMTNGDEVSITCGEAASIVDRIRgfFEPSSILVSTLVLTLRP 325
Cdd:cd13867   81 GGLLPAPVELKRLLLAPGERAEILVDFSDGEPVSLRSGPDEGGLGMIG--FGDSGEDDDFDLLTLRV 145

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        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992389296 181 DFPIIIQDKRLDNFGTPEYSEPG-----SGGFVGDTLLVNGVQSPYVEVSRGWVRLRLLNASNSRRYQLQMSDGRALHVI 255
Cdd:cd14448    1 DLPLVITDRQFNADGTLYYPSPPtnmewVPGFFGDVILVNGKIWPYLEVEPGWYRLRLLNASNARHYNLALSDGLPFHVI 80

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 992389296 256 SGDQGFLPAPVSVKQLSLAPGERREILVDMTN--GDEVSITCGEAASIvdrirgffEPSSILVSTLVLTLRP 325
Cdd:cd14448   81 GSDGGLLEAPVKVKELVLAPAERIDVVVDFSQyaGEEVELVNLGGASM--------AILPTDYDTDVMQFRV 144

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.

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992389296 181 DFPIIIQDKRLDNFGTPEYSEPGSG---GFVGDTLLVNGVQSPYVEVSRGWVRLRLLNASNSRRYQLQMSDGRALHVISG 257
Cdd:cd13879    2 DLPLVIQDRRFDANNQLVYLPNGMDrmmGFLGDRILVNGTPDPTLSVATRAYRLRLLNGSNARIYKLAWSDGSPLTVIGT 81

                         90       100       110
                 ....*....|....*....|....*....|....*...
gi 992389296 258 DQGFLPAPVSVKQLSLAPGERREILVDMTN---GDEVS 292
Cdd:cd13879   82 DGGLLEAPKTVPYVMLAPGERVDLWVDFSGrpvGTELK 119

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

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992389296 181 DFPIIIQDKRLDNFGTPEYSEPGSGGFVGDTLLVNGVQSPYVEVSRGWVRLRLLNASNSRRYQLQMSDGRA-----LHVI 255
Cdd:cd13866    5 DIPLVLADKQFDPNGQLMFDEFNLDGLLGDVILVNGVPWPFLNVEPRKYRFRLLNASVSRFFQLALVDGDNptripFTVI 84

                         90       100       110
                 ....*....|....*....|....*....|....*....
gi 992389296 256 SGDQGFLPAPVSVKQLSLAPGERREILVDMT---NGDEV 291
Cdd:cd13866   85 ASDGGLLSHPVETTLLRLGMAERYDIVVDFSkyaAGTRL 123

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.

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992389296  60 TQGTRAPVWGVNGRYLGPTIRVWKGDDVKLIYSNRLAENvsmTIA---GLQVPGPLMGGPARMMSPNADWAPVLPIRQNA 136
Cdd:cd13852    8 LKGDPAALQNLPDSYLGPILRLRKGQKVRITFKNNLPEP---TIIhwhGLHVPAAMDGHPRYAIDPGETYVYEFEVLNRA 84

                         90       100       110
                 ....*....|....*....|....*....|
gi 992389296 137 ATLWYHANTPNRTAQQVYNGLAGMWLVEDE 166
Cdd:cd13852   85 GTYWYHPHPHGLTAKQVYRGLAGLFLVTDE 114

The second 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 participates in diverse biological functions such as spore pigmentation and biosynthesis of the antibiotic grixazone. It is a member of the multicopper oxidase (MCO) family, which couples the oxidation of a substrate with a four-electron reduction of molecular oxygen 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        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992389296 195 GTPEYSEPGSGGFVGDTLLVNGVQSPYVEVSRGWVRLRLLNASNSRRYQLQM---SDGR----ALHVISGDQGFLPAPVS 267
Cdd:cd13869   33 GVGTGDAALEIPFTGPYTLVNGVIWPYLEVRPGWYRLRLLNASNARIYRLALldeTDEHpvpgALVVIGTDAGLLPRPVP 112

                         90       100
                 ....*....|....*....|
gi 992389296 268 V--KQLSLAPGERREILVDM 285
Cdd:cd13869  113 VpgGAVNLGPGERADVLVDF 132

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
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992389296  359 GDDPGINGQLWDVNRIDITAQQGSWERWTVR--ADMPQSFHIEGVSFLVRNVNGAMPFPEDR--------GWKDTVWVDG 428
Cdd:pfam07731  19 RNDWAINGLLFPPNTNVITLPYGTVVEWVLQntTTGVHPFHLHGHSFQVLGRGGGPWPEEDPktynlvdpVRRDTVQVPP 98

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|.
gi 992389296  429 QVELLVYYgQPSWAHfPFYFHSQTLEMADRGSIGQILVNPA 469
Cdd:pfam07731  99 GGWVAIRF-RADNPG-VWLFHCHILWHLDQGMMGQFVVRPG 137

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.

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992389296 363 GINGQLWDVNRIDITAQQGSWERWTV--RADMPQSFHIEGVSFLVRNVNGAMPFPEDRGWKDTVWV--DGQVELLVYYGQ 438
Cdd:cd13902   22 LINGKTFDMNRIDFVAKVGEVEVWEVtnTSHMDHPFHLHGTQFQVLEIDGNPQKPEYRAWKDTVNLppGEAVRIATRQDD 101

                         90       100
                 ....*....|....*....|....*...
gi 992389296 439 PSwahfPFYFHSQTLEMADRGSIGQILV 466
Cdd:cd13902  102 PG----MWMYHCHILEHEDAGMMGMLHV 125

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.

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992389296 349 TPIRSRDISLGDDPG------INGQLWDVNRIDITAQQGSWERWTV--RADMPQSFHIEGVSFLVRNVNGamPFPEDRGW 420
Cdd:cd13900    1 AGTRRLVFSEGMSPGgggaftINGKPFDPDRPDRTVRLGTVEEWTLinTSGEDHPFHIHVNPFQVVSING--KPGLPPVW 78

                         90
                 ....*....|....*...
gi 992389296 421 KDTVWVD--GQVELLVYY 436
Cdd:cd13900   79 RDTVNVPagGSVTIRTRF 96

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.

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992389296  53 QRSHWSFTQGTRAP------VWGVNGRYLGPTIRVWKGDDVKLIYSNRL-AENVSMTIAGLQVPG-PLMGGPARMMSPna 124
Cdd:cd04206    1 REYELTITETTVNPdgvlrqVITVNGQFPGPTIRVKEGDTVEVTVTNNLpNEPTSIHWHGLRQPGtNDGDGVAGLTQC-- 78

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*....
gi 992389296 125 dwaPVLP---------IRQNAATLWYHANTPNrtaqQVYNGLAGMWLVE 164
Cdd:cd04206   79 ---PIPPgesftyrftVDDQAGTFWYHSHVGG----QRADGLYGPLIVE 120

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.

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992389296  65 APVWG----VNGRYLGPTIRVWKGDDVKLIYSNRLAEN-----------VSMTIAGLQVPGP-------LMGG------- 115
Cdd:cd13844   22 TTVWGyggsNSTSYPGPTIEARRGVPVRVTWVNNLPDKhhlplddtlpsTEEATPGAEPPVPpvptvvhLHGGevppesd 101

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 992389296 116 --------PARMMSPNADWAP-VLPIRQNAATLWYHANTPNRTAQQVYNGLAGMWLVEDEV 167
Cdd:cd13844  102 gypeawftPGGEEGPGFGSATyYYPNDQSAATLWYHDHALGITRLNVYAGLAGFYLIRDEA 162

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.

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992389296 185 IIQDKRLDN-------FGTPEysEPGSGGFVGDTLLVNGVQSPYVEVSRGW-VRLRLLNASNSRRYQLQMsDGRALHVIS 256
Cdd:cd13885    6 VLDDWRLDPdgqavpgFGTPH--DAAHAGRIGNLYTINGRVQPDFTVRAGErVRLRLINAANARVFALKF-PGHEARVIA 82

                         90       100       110
                 ....*....|....*....|....*....|.
gi 992389296 257 GD-QGFLPAPVSVKQLSLAPGERREILVDMT 286
Cdd:cd13885   83 LDgQPAEPFVARNGAVVLAPGMRIDLVIDAP 113

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.

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992389296 352 RSRDISLGDDP---GINGQLW--DVNRIDITAQQGSWERWTVRAD---MPQSFHIEGVSFLV------------RNVNGA 411
Cdd:cd13888    2 TPRRIHLSMGRmqwTINGETWadDPDAFPVERVGGTVEIWELVNDaasMPHPMHIHGFQFQVlersdsppqvaeLAVAPS 81

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 992389296 412 MPFPEDRGWKDTV--WVDGQVELLVYYGQPSWAHFPFYFHSQTLEMADRGSIGQILVN 467
Cdd:cd13888   82 GRTATDLGWKDTVlvWPGETVRIAVDFTHDYPGDQLYLLHCHNLEHEDDGMMVNVRVP 139

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.

                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 992389296  70 VNGRYLGPTIRVWKGDDVKLIYSNRLAENVSMTIAGLQVPGPLMGGP---ARMMSPNADWAPVLPIRQnAATLWYHANT 145
Cdd:cd13848   24 VNGQVPGPLLRFKEGDDATIRVHNRLDEDTSIHWHGLLLPNDMDGVPglsFPGIKPGETFTYRFPVRQ-SGTYWYHSHS 101

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
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992389296  62 GTRAPVWGVNGRYLGPTIRVWKGDDVKLIYSNRLAENVSMTIAGLQVPGPLMGGPARMMSPNA-----DWAPVLPirqNA 136
Cdd:cd13861   17 GPTTRTWGYNGQVPGPELRVRQGDTLRVRLTNRLPEPTTIHWHGLRLPNAMDGVPGLTQPPVPpgesfTYEFTPP---DA 93

                         90       100
                 ....*....|....*....|....*...
gi 992389296 137 ATLWYHANtpNRTAQQVYNGLAGMWLVE 164
Cdd:cd13861   94 GTYWYHPH--VGSQEQLDRGLYGPLIVE 119

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        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992389296 205 GGFVGDT----LLVNG---VQSPYVEVSRG-WVRLRLLNASNSRRYQLQMsDGRALHVISGDqGFLPAPVSVKQLSLAPG 276
Cdd:cd13870    7 GGDAGDVrypyYLINGrppEDPAVFTARPGdRLRLRLINAAGDTAFRVAL-AGHRLTVTHTD-GFPVEPVEVDALLIGMG 84

                         90
                 ....*....|..
gi 992389296 277 ERREILVDMTNG 288
Cdd:cd13870   85 ERYDAIVTANNG 96

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.

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992389296  70 VNGRYLGPTIRVWKGDDVKLIYSNRLAENVSMTIAGLQvpgplmggpaRMMSPNADWAPVL---PIRQN----------- 135
Cdd:cd13849   22 VNGQFPGPTIRVHEGDTVVVNVTNRSPYNITIHWHGIR----------QLRSGWADGPAYItqcPIQPGqsytyrftvtg 91

                 ....*....
gi 992389296 136 -AATLWYHA 143
Cdd:cd13849   92 qEGTLWWHA 100

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.

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992389296 364 INGQLWDVNriDITAQQGSWERWT---VRADMPQSFHIEGVSFLV------------RNVNG----------AMPFPEDR 418
Cdd:cd13892   56 IAKLFDDDV--NFTAAAGSWERWTfvnLGEGHPHPMHIHLAEFQVlerqpydvtgfdTTVGGtdrpitpgeaAPLEPVEL 133

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|..
gi 992389296 419 GWKDTVWVdGQVELLVYYGQPSWAHFPFYFHSQTLEMADRGSIGQILVNPAA 470
Cdd:cd13892  134 GWKDTVVV-GPGELVTVLVQFDGATGRFMYHCHILEHEDHDMMRPFVVQPPH 184