FtsI repressor; Provisional

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496081997   1 MSLSRRQFIKASGVALCAGAAPLKAHAAGQQLALPVPPLLESRRGQPLFLTLQRSHWSFTPGTRAPVWGINGRYMGPTIR 80
Cdd:PRK10883   1 MSLSRRQFIQASGIALCAGALPLRARAAGQQQPLPVPPLLESRRGQPLFLTLQRAHWSFTGGTKASVWGINGRYLGPTIR 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496081997  81 VWSGDDVKLIYSNRLTENVAMTIRGLQVPGPLIGGAARMMSPNADWAPVLPIRQSAATLWYQANTPNRMAKQVYNGLAGM 160
Cdd:PRK10883  81 VWKGDDVKLIYSNRLTEPVSMTVSGLQVPGPLMGGPARMMSPNADWAPVLPIRQNAATCWYHANTPNRMAQHVYNGLAGM 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496081997 161 WLVEDEVSKNLPIPNHYGVDDFPVIIQDKRLDNFGTPEYSEPGSGGFVGDTLLVNGVQSPYVEVSRGWVRLRLLNASNSR 240
Cdd:PRK10883 161 WLVEDEVSKSLPIPNHYGVDDFPVIIQDKRLDNFGTPEYNEPGSGGFVGDTLLVNGVQSPYVEVSRGWVRLRLLNASNAR 240

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496081997 241 RYQLQMSDGRLLHVISGDQGFLPAPVSLKQLSLGPGERREILVDMTNGDEVSITCGEAASIVDRIRGFFEPSSILVSTLV 320
Cdd:PRK10883 241 RYQLQMSDGRPLHVIAGDQGFLPAPVSVKQLSLAPGERREILVDMSNGDEVSITAGEAAGIVDRLRGFFEPSSILVSTLV 320

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496081997 321 LTLRPTGLLPLVTDSLPVRLLPTELLSGTPIRSRDITLGDD-PGINGQLWDPQRIDITAQQGTWERWTVRADRPQSFHIE 399
Cdd:PRK10883 321 LTLRPTGLLPLVTDNLPMRLLPDEIMEGSPIRSREISLGDDlPGINGALWDMNRIDVTAQQGTWERWTVRADMPQAFHIE 400

                        410       420       430       440       450       460       470
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 496081997 400 GVMFQIRNVNGSSPFPEDRGWKDTVWVDGQVELLVYYAQPSWPHFPFQYLSQTLELADRGSIGQMLVNPAP 470
Cdd:PRK10883 401 GVMFLIRNVNGAMPFPEDRGWKDTVWVDGQVELLVYFGQPSWAHFPFLFYSQTLEMADRGSIGQLLVNPAP 471

FtsI repressor; Provisional

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496081997   1 MSLSRRQFIKASGVALCAGAAPLKAHAAGQQLALPVPPLLESRRGQPLFLTLQRSHWSFTPGTRAPVWGINGRYMGPTIR 80
Cdd:PRK10883   1 MSLSRRQFIQASGIALCAGALPLRARAAGQQQPLPVPPLLESRRGQPLFLTLQRAHWSFTGGTKASVWGINGRYLGPTIR 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496081997  81 VWSGDDVKLIYSNRLTENVAMTIRGLQVPGPLIGGAARMMSPNADWAPVLPIRQSAATLWYQANTPNRMAKQVYNGLAGM 160
Cdd:PRK10883  81 VWKGDDVKLIYSNRLTEPVSMTVSGLQVPGPLMGGPARMMSPNADWAPVLPIRQNAATCWYHANTPNRMAQHVYNGLAGM 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496081997 161 WLVEDEVSKNLPIPNHYGVDDFPVIIQDKRLDNFGTPEYSEPGSGGFVGDTLLVNGVQSPYVEVSRGWVRLRLLNASNSR 240
Cdd:PRK10883 161 WLVEDEVSKSLPIPNHYGVDDFPVIIQDKRLDNFGTPEYNEPGSGGFVGDTLLVNGVQSPYVEVSRGWVRLRLLNASNAR 240

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496081997 241 RYQLQMSDGRLLHVISGDQGFLPAPVSLKQLSLGPGERREILVDMTNGDEVSITCGEAASIVDRIRGFFEPSSILVSTLV 320
Cdd:PRK10883 241 RYQLQMSDGRPLHVIAGDQGFLPAPVSVKQLSLAPGERREILVDMSNGDEVSITAGEAAGIVDRLRGFFEPSSILVSTLV 320

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496081997 321 LTLRPTGLLPLVTDSLPVRLLPTELLSGTPIRSRDITLGDD-PGINGQLWDPQRIDITAQQGTWERWTVRADRPQSFHIE 399
Cdd:PRK10883 321 LTLRPTGLLPLVTDNLPMRLLPDEIMEGSPIRSREISLGDDlPGINGALWDMNRIDVTAQQGTWERWTVRADMPQAFHIE 400

                        410       420       430       440       450       460       470
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 496081997 400 GVMFQIRNVNGSSPFPEDRGWKDTVWVDGQVELLVYYAQPSWPHFPFQYLSQTLELADRGSIGQMLVNPAP 470
Cdd:PRK10883 401 GVMFLIRNVNGAMPFPEDRGWKDTVWVDGQVELLVYFGQPSWAHFPFLFYSQTLEMADRGSIGQLLVNPAP 471

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 496081997 180 DDFPVIIQDKRLDNFGTPEY-SEPGSGGFVGDTLLVNGVQSPYVEVSRGWVRLRLLNASNSRRYQLQMSDGRLLHVISGD 258
Cdd:cd13867    1 DDIPLILQDRRFDEDGQLDYrMMDDMDGFLGDTLLVNGTINPYLDVPRGWVRLRLLNGSNARTYNLGFSDNRPFYQIASD 80

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 496081997 259 QGFLPAPVSLKQLSLGPGERREILVDMTNGDEVSITCGEAASIVDRIRgfFEPSSILVSTLVLTLRP 325
Cdd:cd13867   81 GGLLPAPVELKRLLLAPGERAEILVDFSDGEPVSLRSGPDEGGLGMIG--FGDSGEDDDFDLLTLRV 145

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
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496081997   64 RAPVWGINGRYMGPTIRVWSGDDVKLIYSNRL-TENVAMTIRGL-QVPGPLIGGAARMMSpnadwAPVLP--------IR 133
Cdd:TIGR03388  19 EKLVIGINGQFPGPTIRAQAGDTIVVELTNKLhTEGVVIHWHGIrQIGTPWADGTAGVTQ-----CAINPgetfiynfVV 93

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 496081997  134 QSAATLWYQANtpnrMAKQVYNGLAGMWLVedEVSKNLPIPNHYGvDDFPVIIQD 188
Cdd:TIGR03388  94 DRPGTYFYHGH----YGMQRSAGLYGSLIV--DVPDGEKEPFHYD-GEFNLLLSD 141

FtsI repressor; Provisional

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496081997   1 MSLSRRQFIKASGVALCAGAAPLKAHAAGQQLALPVPPLLESRRGQPLFLTLQRSHWSFTPGTRAPVWGINGRYMGPTIR 80
Cdd:PRK10883   1 MSLSRRQFIQASGIALCAGALPLRARAAGQQQPLPVPPLLESRRGQPLFLTLQRAHWSFTGGTKASVWGINGRYLGPTIR 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496081997  81 VWSGDDVKLIYSNRLTENVAMTIRGLQVPGPLIGGAARMMSPNADWAPVLPIRQSAATLWYQANTPNRMAKQVYNGLAGM 160
Cdd:PRK10883  81 VWKGDDVKLIYSNRLTEPVSMTVSGLQVPGPLMGGPARMMSPNADWAPVLPIRQNAATCWYHANTPNRMAQHVYNGLAGM 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496081997 161 WLVEDEVSKNLPIPNHYGVDDFPVIIQDKRLDNFGTPEYSEPGSGGFVGDTLLVNGVQSPYVEVSRGWVRLRLLNASNSR 240
Cdd:PRK10883 161 WLVEDEVSKSLPIPNHYGVDDFPVIIQDKRLDNFGTPEYNEPGSGGFVGDTLLVNGVQSPYVEVSRGWVRLRLLNASNAR 240

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496081997 241 RYQLQMSDGRLLHVISGDQGFLPAPVSLKQLSLGPGERREILVDMTNGDEVSITCGEAASIVDRIRGFFEPSSILVSTLV 320
Cdd:PRK10883 241 RYQLQMSDGRPLHVIAGDQGFLPAPVSVKQLSLAPGERREILVDMSNGDEVSITAGEAAGIVDRLRGFFEPSSILVSTLV 320

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496081997 321 LTLRPTGLLPLVTDSLPVRLLPTELLSGTPIRSRDITLGDD-PGINGQLWDPQRIDITAQQGTWERWTVRADRPQSFHIE 399
Cdd:PRK10883 321 LTLRPTGLLPLVTDNLPMRLLPDEIMEGSPIRSREISLGDDlPGINGALWDMNRIDVTAQQGTWERWTVRADMPQAFHIE 400

                        410       420       430       440       450       460       470
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 496081997 400 GVMFQIRNVNGSSPFPEDRGWKDTVWVDGQVELLVYYAQPSWPHFPFQYLSQTLELADRGSIGQMLVNPAP 470
Cdd:PRK10883 401 GVMFLIRNVNGAMPFPEDRGWKDTVWVDGQVELLVYFGQPSWAHFPFLFYSQTLEMADRGSIGQLLVNPAP 471

multicopper oxidase; Provisional

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496081997   3 LSRRQFIKASGVALCAGAAPL--KAHAAGQQLALPVPPLLESRRGQPLFLTLQRSHWSFTPGTRAPVWGINGRYMGPTIR 80
Cdd:PRK10965   1 MQRRDFLKLSAALGAASALPLwsRAAFAAERPALPIPPLLTPDARGRIQLTIQAGQSSFAGKTATATWGYNGNLLGPAVR 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496081997  81 VWSGDDVKLIYSNRLTENVAMTIRGLQVPGPLIGGAARMMSPNADWAPVLPIRQSAATLWYQANTPNRMAKQVYNGLAGM 160
Cdd:PRK10965  81 LQRGKAVTVDITNQLPEETTLHWHGLEVPGEVDGGPQGIIAPGGKRTVTFTVDQPAATCWFHPHQHGKTGRQVAMGLAGL 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496081997 161 WLVEDEVSKNLPIPNHYGVDDFPVIIQDKRLDNFGTPEYS---EPGSGGFVGDTLLVNGVQSPYVEVSRGWVRLRLLNAS 237
Cdd:PRK10965 161 VLIEDDESLKLGLPKQWGVDDIPVILQDKRFSADGQIDYQldvMTAAVGWFGDTLLTNGAIYPQHAAPRGWLRLRLLNGC 240

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496081997 238 NSRRYQLQMSDGRLLHVISGDQGFLPAPVSLKQLSLGPGERREILVDMTNGDEVSITCGEAASIVDRIRGFFEPSSilvs 317
Cdd:PRK10965 241 NARSLNLATSDGRPLYVIASDGGLLAEPVKVSELPILMGERFEVLVDTSDGKAFDLVTLPVSQMGMALAPFDKPLP---- 316

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496081997 318 tlVLTLRPT-----GLLPLVTDSLPvrllptELLSGTPIRSRDITLGDDP------------------------------ 362
Cdd:PRK10965 317 --VLRIQPLlisasGTLPDSLASLP------ALPSLEGLTVRRLQLSMDPrldmmgmqmlmekygdqamagmdmdhmmgh 388

                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496081997 363 --------------------------GINGQLWDPQRIDITAQQGTWERWTV--RADR-PQSFHIEGVMFQIRNVNGSSP 413
Cdd:PRK10965 389 mghgnmdhmnhgaadagpafdfhhanKINGKAFDMNKPMFAAKKGQYERWVIsgVGDMmLHPFHIHGTQFRILSENGKPP 468

                        490       500       510       520
                 ....*....|....*....|....*....|....*....|....*..
gi 496081997 414 FPEDRGWKDTVWVDGQV-ELLVYYAQPSWPHFPFQYLSQTLELADRG 459
Cdd:PRK10965 469 AAHRAGWKDTVRVEGGRsEVLVKFDHDAPKEHAYMAHCHLLEHEDTG 515

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
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496081997  46 QPLFLTLQRSHWSFTPGTRAPVWGINGRYMGPTIRVWSGDDVKLIYSNRLTENVAMTIRGLQVPGPLIGGAARMMSPNAD 125
Cdd:cd04232    1 KPFTLTAQKGETEFLPGKKTATWGYNGSYLGPTIRVKKGDTVRINVTNNLDEETTVHWHGLHVPGEMDGGPHQPIAPGQT 80

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|
gi 496081997 126 WAPVLPIRQSAATLWYQANTPNRMAKQVYNGLAGMWLVED 165
Cdd:cd04232   81 WSPTFTIDQPAATLWYHPHTHGKTAEQVYRGLAGLFIIED 120

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 496081997 181 DFPVIIQDKRLDNFGTPEYSEPG-----SGGFVGDTLLVNGVQSPYVEVSRGWVRLRLLNASNSRRYQLQMSDGRLLHVI 255
Cdd:cd14448    1 DLPLVITDRQFNADGTLYYPSPPtnmewVPGFFGDVILVNGKIWPYLEVEPGWYRLRLLNASNARHYNLALSDGLPFHVI 80

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 496081997 256 SGDQGFLPAPVSLKQLSLGPGERREILVDMTN--GDEVSITCGEAASIvdrirgffEPSSILVSTLVLTLRP 325
Cdd:cd14448   81 GSDGGLLEAPVKVKELVLAPAERIDVVVDFSQyaGEEVELVNLGGASM--------AILPTDYDTDVMQFRV 144

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 496081997   51 TLQRSHWSFTPGTRAPVWGINGRYMGPTIRVWSGDDVKLIYSNRLTENVAMTIRGLQVPGPLI-----GGAARMMSPNAD 125
Cdd:pfam07732   1 TVTYGTVSPLGGTRQAVIGVNGQFPGPTIRVREGDTVVVNVTNNLDEPTSIHWHGLQQRGTPWmdgvpGVTQCPIPPGQS 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|...
gi 496081997  126 WAPVLPIRQSAATLWYQANTPNRMAkqvyNGLAGMWLVEDEVS 168
Cdd:pfam07732  81 FTYRFQVKQQAGTYWYHSHTSGQQA----AGLAGAIIIEDRAS 119

The second Cupredoxin domain of bacterial laccases including CotA, a bacterial endospore coat component; 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. Laccase is composed of three cupredoxin-like domains and includes one mononuclear and one trinuclear copper center. 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. 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 496081997 181 DFPVIIQDKRLDNFGTPEYSEPGSGG---------FVGDTLLVNGVQSPYVEVSRGWVRLRLLNASNSRRYQLQMSDGRL 251
Cdd:cd13868    2 EIPLLIQDRSFNADGSLFYPATGANPsphpswvpeFFGDTIVVNGKAWPYLEVEPRRYRFRILNGSNARFYNLSLSNGDG 81

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*..
gi 496081997 252 L--HVISGDQGFLPAPVSLKQLSLGPGERREILVDMTN--GDEVSIT 294
Cdd:cd13868   82 LpfWQIGTDGGFLPKPVPLDSLLIGPAERADVIVDFSDyaGQTLILK 128

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 496081997 183 PVIIQDKRLDNFGTPEYS---EPGSGGFVGDTLLVNGVQS--------------PYVEVSRG-WVRLRLLNASNSRRYQL 244
Cdd:cd04205    2 VLLLSDWYHDSAEDVLAGympNSFGNEPVPDSLLINGRGRfncsmavcnsgcplPVITVEPGkTYRLRLINAGSFASFNF 81

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*.
gi 496081997 245 QMsDGRLLHVISGDQGFLpAPVSLKQLSLGPGERREILVDMTNGDE 290
Cdd:cd04205   82 AI-DGHNMTVIEVDGGYV-EPLEVDNLDLAPGQRYDVLVKADQPPG 125

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 496081997  57 WSFTP----GTRAPVWGINGRYMGPTIRVWSGDDVKLIYSNRLTENVAMTIRGLQVPGPLIGGAARMMSPNADWAPVLPI 132
Cdd:cd13852    1 WKYSGkllkGDPAALQNLPDSYLGPILRLRKGQKVRITFKNNLPEPTIIHWHGLHVPAAMDGHPRYAIDPGETYVYEFEV 80

                         90       100       110
                 ....*....|....*....|....*....|....
gi 496081997 133 RQSAATLWYQANTPNRMAKQVYNGLAGMWLVEDE 166
Cdd:cd13852   81 LNRAGTYWYHPHPHGLTAKQVYRGLAGLFLVTDE 114

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
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 496081997 364 INGQLWDPQRIDITAQQGTWERWTVRADRPQSFHIEGVMFQIRNVNGSSPFPEDRGWKDTV 424
Cdd:cd13911   19 VNGKVFDPDHIAARPRLGTTEIWVFSSDGRHPVHLHGAHFQVVSRTGGRPGEWDAGWKDTV 79

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
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496081997  50 LTLQRSHWSFTPGTRAPVWGINGRYMGPTIRVWSGDDVKLIYSNRLTENVAMTIRGLQVPGPLIGGAARMMSPNADWAPV 129
Cdd:cd13855    6 LTAAEVRIRLLPGKPTEFWAYNGSVPGPLIEVFEGDTVEITFRNRLPEPTTVHWHGLPVPPDQDGNPHDPVAPGNDRVYR 85

                         90       100       110
                 ....*....|....*....|....*....|....*
gi 496081997 130 LPIRQ-SAATLWYQANTPNRMAKQVYNGLAGMWLV 163
Cdd:cd13855   86 FTLPQdSAGTYWYHPHPHGHTAEQVYRGLAGAFVV 120

The third cupredoxin domain of Bilirubin oxidase (BOD); Bilirubin oxidase (BOD) catalyzes the oxidation of bilirubin to biliverdin and the four-electron reduction of molecular oxygen to water. It is used in diagnosing jaundice through the determination of bilirubin in serum. BOD is a member of the multicopper oxidase (MCO) family that also includes laccase, ascorbate oxidase and ceruloplasmin. MCOs are capable of oxidizing a vast range of substrates, varying from aromatic compounds to inorganic compounds such as metals. Although the members of this family have diverse functions, majority of them have three cupredoxin domain repeats. The copper ions are bound in several sites: Type 1, Type 2, and/or Type 3. The ensemble of types 2 and 3 copper is called a trinuclear cluster. MCOs oxidize their substrate by accepting electrons at a mononuclear copper center and transferring them to the active site trinuclear copper center. The cupredoxin domain 3 of 3-domain MCOs contains the Type 1 (T1) copper binding site and part the trinuclear copper binding site, which is located at the interface of domains 1 and 3.

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496081997 364 INGQLW-DPQRIDITAQQGTWERWTVRA-----DRPqsFHIEGVMFQI--RNVNGSSPFPEDRGWKDTVWVD--GQVELL 433
Cdd:cd13889   17 INGKTWaDPNRIDAAPQLGTVEIWTLINggggwSHP--IHIHLEDFQIlsRNGGSRAVPPYERGRKDVVYLGpgEEVRVL 94

                 ....
gi 496081997 434 VYYA 437
Cdd:cd13889   95 MRFR 98

Cupredoxin superfamily; Cupredoxins contain type I copper centers and are involved in inter-molecular electron transfer reactions. Cupredoxins are blue copper proteins, having an intense blue color due to the presence of a mononuclear type 1 (T1) copper site. Structurally, the cupredoxin-like fold consists of a beta-sandwich with 7 strands in 2 beta-sheets, which is arranged in a Greek-key beta-barrel. Some of these proteins have lost the ability to bind copper. The majority of family members contain multiple cupredoxin domain repeats: ceruloplasmin and the coagulation factors V/VIII have six repeats; laccase, ascorbate oxidase, spore coat protein A, and multicopper oxidase CueO contain three repeats; and nitrite reductase has two repeats. Others are mono-domain cupredoxins, such as plastocyanin, pseudoazurin, plantacyanin, azurin, rusticyanin, stellacyanin, quinol oxidase, and the periplasmic domain of cytochrome c oxidase subunit II.

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496081997 203 GSGGFVGDTLLVNGVQSPYVEVSRG-WVRLRLLNaSNSRRYQLQMSDGRLLHVISGDQGFlpaPVSLKQLSLGPGERREI 281
Cdd:cd00920    6 SDWGWSFTYNGVLLFGPPVLVVPVGdTVRVQFVN-KLGENHSVTIAGFGVPVVAMAGGAN---PGLVNTLVIGPGESAEV 81

                         90
                 ....*....|....*....
gi 496081997 282 LVDMTNGDEVSITCGEAAS 300
Cdd:cd00920   82 TFTTDQAGVYWFYCTIPGH 100

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 496081997 352 RSRDITLGDDP---GINGQLW--DPQRIDITAQQGTWERWTVRADR---PQSFHIEGVMFQIRNVNGSSPF--------- 414
Cdd:cd13888    2 TPRRIHLSMGRmqwTINGETWadDPDAFPVERVGGTVEIWELVNDAasmPHPMHIHGFQFQVLERSDSPPQvaelavaps 81

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 496081997 415 ---PEDRGWKDTV--WVDGQVELLVYYAQPSWPHFPFQYLSQTLELADRGsigqMLVN 467
Cdd:cd13888   82 grtATDLGWKDTVlvWPGETVRIAVDFTHDYPGDQLYLLHCHNLEHEDDG----MMVN 135

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 496081997 185 IIQDKRLDN-------FGTPEysEPGSGGFVGDTLLVNGVQSPYVEVSRG-WVRLRLLNASNSRRYQLQMsDGRLLHVIS 256
Cdd:cd13885    6 VLDDWRLDPdgqavpgFGTPH--DAAHAGRIGNLYTINGRVQPDFTVRAGeRVRLRLINAANARVFALKF-PGHEARVIA 82

                         90       100       110
                 ....*....|....*....|....*....|.
gi 496081997 257 GD-QGFLPAPVSLKQLSLGPGERREILVDMT 286
Cdd:cd13885   83 LDgQPAEPFVARNGAVVLAPGMRIDLVIDAP 113

Cupredoxin domain 1 of Copper-containing nitrite reductase and two-domain laccase; Copper-containing nitrite reductase (CuNIR), which catalyzes the reduction of NO2- to NO, is the key enzyme in the denitrification process in denitrifying bacteria. CuNIR contains at least one type 1 copper center and a type 2 copper center, which serves as the active site of the enzyme. A histidine, bound to the Type 2 Cu center, is responsible for binding and reducing nitrite. A Cys-His bridge plays an important role in facilitating rapid electron transfer from the type 1 center to the type 2 center. A reduced type I blue copper protein (pseudoazurin) was found to be a specific electron transfer donor for the copper-containing NIR in bacteria Alcaligenes faecalis. The two-domain laccase (small laccase) in this family differs significantly from all laccases. It resembles two domain nitrite reductase in both sequence homology and structure similarity. It consists of two domains and forms trimers and hence resembles the quaternary structure of nitrite reductases more than that of larger laccases.

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496081997  61 PGTRAPVWGINGRYMGPTIRVWSGDDVKLIYSNRLTENVAMTIRGLQVPGPLIGGAARMMSPNADWAPVLPIRQSAATLW 140
Cdd:cd04201   17 DGVEYRYWTFDGDIPGPMLRVREGDTVELHFSNNPSSTMPHNIDFHAATGAGGGAGATFIAPGETSTFSFKATQPGLYVY 96

                         90       100
                 ....*....|....*....|....*.
gi 496081997 141 YQANTPnrMAKQVYNGLAGMWLVEDE 166
Cdd:cd04201   97 HCAVAP--VPMHIANGMYGLILVEPK 120

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
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 496081997 364 INGQ---LWDPQRIDITAQQGTWERWTVR----ADRPQSFHIEGVMFQIRNVNGSSP----FPEDRGWKDTVWVDGQ 429
Cdd:cd04207   22 INGMpfkEGDANTDIFSVEAGDVVEIVLInagnHDMQHPFHLHGHSFWVLGSGGGPFdaplNLTNPPWRDTVLVPPG 98

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 496081997  46 QPLFLTLQRSHWSFTPGTRAPVWGINGRYMGPTIRVWSGDDVKLIYSNRLTEnvAMTI--RGLQVPGPLIGgaarmmSPN 123
Cdd:cd13861    1 VEYTLTAAPAELLDLGGPTTRTWGYNGQVPGPELRVRQGDTLRVRLTNRLPE--PTTIhwHGLRLPNAMDG------VPG 72

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*....
gi 496081997 124 ADWAPVLP--------IRQSAATLWYQANtpNRMAKQVYNGLAGMWLVE 164
Cdd:cd13861   73 LTQPPVPPgesftyefTPPDAGTYWYHPH--VGSQEQLDRGLYGPLIVE 119

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
                 ....*....|....*....|....*....|...
gi 496081997  61 PGTRAPVWGINGRYMGPTIRVWSGDDVKLIYSN 93
Cdd:cd11024   17 PGVVFKAWTYNGTVPGPTLRATEGDLVRIHFIN 49

The first cupredoxin domain of insect laccases similar to laccase 2 in Tribolium castaneum; This multicopper oxidase (MCO) family includes the majority of insect laccases. One member of the family is laccase 2 from Tribolium castaneum. Laccase 2 is required for beetle cuticle tanning. Laccase (polyphenol oxidase EC 1.10.3.2) is a blue multi-copper enzyme that catalyzes the oxidation of a variety of organic substrates coupled to the reduction of molecular oxygen to water. It displays broad substrate specificity, catalyzing the oxidation of a wide variety of aromatic - notably phenolic and inorganic substances. Laccase has been implicated in a wide spectrum of biological activities and, in particular, plays a key role in morphogenesis, development and lignin metabolism in fungi, plants and insects. Although MCOs have diverse functions, majority of them have three cupredoxin domain repeats that include one mononuclear and one trinuclear copper center. The copper ions are bound in several sites: Type 1, Type 2, and/or Type 3. The ensemble of types 2 and 3 copper is called a trinuclear cluster. MCOs oxidize their substrate by accepting electrons at a mononuclear copper center and transferring them to the active site trinuclear copper center. The cupredoxin domain 1 of 3-domain MCOs contains part the trinuclear copper binding site, which is located at the interface of domains 1 and 3.

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496081997  62 GTRAPVWGINGRYMGPTIRVWSGDDVKLIYSNRL-TENVAMTIRGL-QVPGPLIGGAArMMSPnadwAPVLP-------- 131
Cdd:cd13858    2 GVERPVITVNGQLPGPSIEVCEGDTVVVDVKNRLpGESTTIHWHGIhQRGTPYMDGVP-MVTQ----CPILPgqtfrykf 76

                         90       100       110
                 ....*....|....*....|....*....|..
gi 496081997 132 IRQSAATLWYQANTPNRMAkqvyNGLAGMWLV 163
Cdd:cd13858   77 KADPAGTHWYHSHSGTQRA----DGLFGALIV 104