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Conserved domains on  [gi|367021116|ref|XP_003659843|]
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copper binding domain-containing laccase [Thermothelomyces thermophilus ATCC 42464]

Protein Classification

multicopper oxidase( domain architecture ID 1002814)

multicopper oxidase family protein couples the one-electron oxidation of four substrate molecules to the four electron reductive cleavage of the O-O bond of dioxygen

Gene Ontology:  GO:0005507|GO:0016491
PubMed:  2404764

Graphical summary

 Zoom to residue level

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List of domain hits

 Name Accession Description Interval E-value
ascorbase super family cl37259
L-ascorbate oxidase, plant type; Members of this protein family are the copper-containing ...
 80-572 2.58e-69

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.


The actual alignment was detected with superfamily member TIGR03388:

Pssm-ID: 274555 [Multi-domain]  Cd Length: 541  Bit Score: 233.49  E-value: 2.58e-69
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 367021116   80 TRHYDFTVSRASIAPDGYLRDVLLVNGAFPGPLVEANWGDTIVVDVHNDITgpEEGTAIHWHGFLQHGTPWEDGVPGITQ 159
Cdd:TIGR03388   1 IRHYKWEVEYEFWSPDCFEKLVIGINGQFPGPTIRAQAGDTIVVELTNKLH--TEGVVIHWHGIRQIGTPWADGTAGVTQ 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 367021116  160 CPIPPRRSYRYEFVASLYGTSWYHSHYSAQFAGGLFGPIVIHGPTRE----NYDIDLGpILLTDWYHREyfdIIEEMLap 235
Cdd:TIGR03388  79 CAINPGETFIYNFVVDRPGTYFYHGHYGMQRSAGLYGSLIVDVPDGEkepfHYDGEFN-LLLSDWWHKS---IHEQEV-- 152

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 367021116  236 GGSAKVVS-----DNNLIDGKMHFDCStVAPGDNTPCFDNAGVSK--------FRFQTGKTHRLRLINGGADGVQRFSID 302
Cdd:TIGR03388 153 GLSSKPMRwigepQSLLINGRGQFNCS-LAAKFSSTNLPQCNLKGneqcapqiLHVEPGKTYRLRIASTTALAALNFAIE 231

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 367021116  303 EHTLTVIAEDFVPVKPYNTSVVTLGVGQRADVLVTANvGEPTSAFWMRSNLSScLPARQPYAVAAVYYDQAD-----TST 377
Cdd:TIGR03388 232 GHKLTVVEADGNYVEPFTVKDIDIYSGETYSVLLTTD-QDPSRNYWISVGVRG-RKPNTPPGLTVLNYYPNSpsrlpPTP 309

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 367021116  378 TPSSRAWDVLDPgtctndDLDITEPLFPIP-LPEPTLTHTMDIELFTNASNV---TLWKFNGVSM---------RADYNs 444
Cdd:TIGR03388 310 PPVTPAWDDFDR------SKAFSLAIKAAMgSPKPPETSDRRIVLLNTQNKIngyTKWAINNVSLtlphtpylgSLKYN- 382

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 367021116  445 pvLLLANDGNF---TYPPQWNVVN----------------QHNHTaIRIIVNN------RSPSAHPMHLHGHNFYVLHEG 499
Cdd:TIGR03388 383 --LLNAFDQKPppeNYPRDYDIFKpppnpntttgngiyrlKFNTT-VDVILQNantlngNNSETHPWHLHGHDFWVLGYG 459

                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 367021116  500 PGEWDGTIVRPS----NPRRRDVYSVRSKGHLVIQF--DGaPGVWPFHCHIAWHVsggFMATLIVKPDEVERM-EIPRDV 572
Cdd:TIGR03388 460 EGKFRPGVDEKSynlkNPPLRNTVVIFPYGWTALRFvaDN-PGVWAFHCHIEPHL---HMGMGVVFAEGVEKVgKLPKEA 535
 
Name Accession Description Interval E-value
ascorbase TIGR03388
L-ascorbate oxidase, plant type; Members of this protein family are the copper-containing ...
 80-572 2.58e-69

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.


Pssm-ID: 274555 [Multi-domain]  Cd Length: 541  Bit Score: 233.49  E-value: 2.58e-69
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 367021116   80 TRHYDFTVSRASIAPDGYLRDVLLVNGAFPGPLVEANWGDTIVVDVHNDITgpEEGTAIHWHGFLQHGTPWEDGVPGITQ 159
Cdd:TIGR03388   1 IRHYKWEVEYEFWSPDCFEKLVIGINGQFPGPTIRAQAGDTIVVELTNKLH--TEGVVIHWHGIRQIGTPWADGTAGVTQ 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 367021116  160 CPIPPRRSYRYEFVASLYGTSWYHSHYSAQFAGGLFGPIVIHGPTRE----NYDIDLGpILLTDWYHREyfdIIEEMLap 235
Cdd:TIGR03388  79 CAINPGETFIYNFVVDRPGTYFYHGHYGMQRSAGLYGSLIVDVPDGEkepfHYDGEFN-LLLSDWWHKS---IHEQEV-- 152

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 367021116  236 GGSAKVVS-----DNNLIDGKMHFDCStVAPGDNTPCFDNAGVSK--------FRFQTGKTHRLRLINGGADGVQRFSID 302
Cdd:TIGR03388 153 GLSSKPMRwigepQSLLINGRGQFNCS-LAAKFSSTNLPQCNLKGneqcapqiLHVEPGKTYRLRIASTTALAALNFAIE 231

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 367021116  303 EHTLTVIAEDFVPVKPYNTSVVTLGVGQRADVLVTANvGEPTSAFWMRSNLSScLPARQPYAVAAVYYDQAD-----TST 377
Cdd:TIGR03388 232 GHKLTVVEADGNYVEPFTVKDIDIYSGETYSVLLTTD-QDPSRNYWISVGVRG-RKPNTPPGLTVLNYYPNSpsrlpPTP 309

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 367021116  378 TPSSRAWDVLDPgtctndDLDITEPLFPIP-LPEPTLTHTMDIELFTNASNV---TLWKFNGVSM---------RADYNs 444
Cdd:TIGR03388 310 PPVTPAWDDFDR------SKAFSLAIKAAMgSPKPPETSDRRIVLLNTQNKIngyTKWAINNVSLtlphtpylgSLKYN- 382

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 367021116  445 pvLLLANDGNF---TYPPQWNVVN----------------QHNHTaIRIIVNN------RSPSAHPMHLHGHNFYVLHEG 499
Cdd:TIGR03388 383 --LLNAFDQKPppeNYPRDYDIFKpppnpntttgngiyrlKFNTT-VDVILQNantlngNNSETHPWHLHGHDFWVLGYG 459

                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 367021116  500 PGEWDGTIVRPS----NPRRRDVYSVRSKGHLVIQF--DGaPGVWPFHCHIAWHVsggFMATLIVKPDEVERM-EIPRDV 572
Cdd:TIGR03388 460 EGKFRPGVDEKSynlkNPPLRNTVVIFPYGWTALRFvaDN-PGVWAFHCHIEPHL---HMGMGVVFAEGVEKVgKLPKEA 535
CuRO_1_MaLCC_like cd13854
The first cupredoxin domain of the fungal laccases similar to Ma-LCC from Melanocarpus ...
 78-201 2.95e-69

The first cupredoxin domain of the fungal laccases similar to Ma-LCC from Melanocarpus albomyces; The subfamily of fungal laccases includes Ma-LCC and similar proteins. Ma-LCC is a multicopper oxidase (MCO) from Melanocarpus albomyces. Its crystal structure contains all four coppers at the mono- and trinuclear copper centers. Laccase is a blue multi-copper enzyme that catalyzes the oxidation of a variety aromatic - notably phenolic and inorganic substances coupled to the reduction of molecular oxygen to water. It has been implicated in a wide spectrum of biological activities and, in particular, plays a key role in morphogenesis, development and lignin metabolism in fungi and plants. Although MCOs have diverse functions, majority of them have three cupredoxin domain repeats that include one mononuclear and one trinuclear copper center. The copper ions are bound in several sites: Type 1, Type 2, and/or Type 3. The ensemble of types 2 and 3 copper is called a trinuclear cluster. MCOs oxidize their substrate by accepting electrons at a mononuclear copper center and transferring them to the active site trinuclear copper center. The cupredoxin domain 1 of 3-domain MCOs contains part the trinuclear copper binding site, which is located at the interface of domains 1 and 3.


Pssm-ID: 259923 [Multi-domain]  Cd Length: 122  Bit Score: 219.42  E-value: 2.95e-69
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 367021116  78 GVTRHYDFTVSRASIAPDGYLRDVLLVNGAFPGPLVEANWGDTIVVDVHNDItgPEEGTAIHWHGFLQHGTPWEDGVPGI 157
Cdd:cd13854    1 GVTRKYTLTITNSTLAPDGVEKEVMLINGQYPGPLIEANWGDTIEVTVINKL--QDNGTSIHWHGIRQLNTNWQDGVPGV 78

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....
gi 367021116 158 TQCPIPPRRSYRYEFVASLYGTSWYHSHYSAQFAGGLFGPIVIH 201
Cdd:cd13854   79 TECPIAPGDTRTYRFRATQYGTSWYHSHYSAQYGDGVVGPIVIH 122
PLN02604 PLN02604
oxidoreductase
 80-565 2.56e-62

oxidoreductase


Pssm-ID: 215324 [Multi-domain]  Cd Length: 566  Bit Score: 215.49  E-value: 2.56e-62
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 367021116  80 TRHYDFTVSRASIAPDGYLRDVLLVNGAFPGPLVEANWGDTIVVDVHNDITgpEEGTAIHWHGFLQHGTPWEDGVPGITQ 159
Cdd:PLN02604  24 IRRYKWEVKYEYKSPDCFKKLVITINGRSPGPTILAQQGDTVIVELKNSLL--TENVAIHWHGIRQIGTPWFDGTEGVTQ 101

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 367021116 160 CPIPPRRSYRYEFVASLYGTSWYHSHYSAQFAGGLFGPIVIHGPTREN----YDIDLGpILLTDWYHREYFDIIEEMLAP 235
Cdd:PLN02604 102 CPILPGETFTYEFVVDRPGTYLYHAHYGMQREAGLYGSIRVSLPRGKSepfsYDYDRS-IILTDWYHKSTYEQALGLSSI 180

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 367021116 236 GGSAKVVSDNNLIDGKMHFDCSTVA-PGDNTPCFDNAGVSKFRFQT----GKTHRLRLINGGADGVQRFSIDEHTLTVIA 310
Cdd:PLN02604 181 PFDWVGEPQSLLIQGKGRYNCSLVSsPYLKAGVCNATNPECSPYVLtvvpGKTYRLRISSLTALSALSFQIEGHNMTVVE 260

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 367021116 311 EDFVPVKPYNTSVVTLGVGQRADVLVTANvGEPTSAFWMRSNLSSCLPARQPYAVAAVYY----DQADTSTTPSSRAWDV 386
Cdd:PLN02604 261 ADGHYVEPFVVKNLFIYSGETYSVLVKAD-QDPSRNYWVTTSVVSRNNTTPPGLAIFNYYpnhpRRSPPTVPPSGPLWND 339

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 367021116 387 LDPGtcTNDDLDITEPLFPIPLPEPTLTHTMdieLFTNASN----VTLWKFNGVSmradYNSP--VLLLANDGNFTY--- 457
Cdd:PLN02604 340 VEPR--LNQSLAIKARHGYIHPPPLTSDRVI---VLLNTQNevngYRRWSVNNVS----FNLPhtPYLIALKENLTGafd 410

                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 367021116 458 ---PPQ---------WNVVNQHN------------HTAIRIIV------NNRSPSAHPMHLHGHNFYVLHEGPGEWDgti 507
Cdd:PLN02604 411 qtpPPEgydfanydiYAKPNNSNatssdsiyrlqfNSTVDIILqnantmNANNSETHPWHLHGHDFWVLGYGEGKFN--- 487

                        490       500       510       520       530       540
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 367021116 508 vRPSNPRR--------RDVYSVRSKGHLVIQFDG-APGVWPFHCHIAWHVsggFMATLIVKPDEVER 565
Cdd:PLN02604 488 -MSSDPKKynlvdpimKNTVPVHPYGWTALRFRAdNPGVWAFHCHIESHF---FMGMGVVFEEGIER 550
SufI COG2132
Multicopper oxidase with three cupredoxin domains (includes cell division protein FtsP and ...
 80-560 1.25e-60

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;


Pssm-ID: 441735 [Multi-domain]  Cd Length: 423  Bit Score: 207.09  E-value: 1.25e-60
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 367021116  80 TRHYDFTVSRASIA-PDGYLRDVLLVNGAFPGPLVEANWGDTIVVDVHNDItgpEEGTAIHWHGFLqhgTPWE-DGVPGI 157
Cdd:COG2132   13 GREYELTAQPATVElLPGKPTTVWGYNGQYPGPTIRVREGDRVRVRVTNRL---PEPTTVHWHGLR---VPNAmDGVPGD 86

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 367021116 158 tqcPIPPRRSYRYEFVAS-LYGTSWYHSHY----SAQFAGGLFGPIVIHGPTRE--NYDIDLgPILLTDWYHREYFDIIE 230
Cdd:COG2132   87 ---PIAPGETFTYEFPVPqPAGTYWYHPHThgstAEQVYRGLAGALIVEDPEEDlpRYDRDI-PLVLQDWRLDDDGQLLY 162

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 367021116 231 EMlaPGGSAKVVSDNNLIDGKmhfdcstVAPgdntpcfdnagvsKFRFQTGKTHRLRLINGGADGVQRFSI-DEHTLTVI 309
Cdd:COG2132  163 PM--DAAMGGRLGDTLLVNGR-------PNP-------------TLEVRPGERVRLRLLNASNARIYRLALsDGRPFTVI 220

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 367021116 310 AEDFVPV-KPYNTSVVTLGVGQRADVLVTANvGEPTSAFWMRSNLSsclpARQPYAVAAVYYDQADTSTTpssrawdvld 388
Cdd:COG2132  221 ATDGGLLpAPVEVDELLLAPGERADVLVDFS-ADPGEEVTLANPFE----GRSGRALLTLRVTGAAASAP---------- 285

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 367021116 389 pgtctnddldITEPLFPIP-LPEPTLTHTMDIELFTNASNvTLWKFNGVSMraDYNSPVLLLANDgnftyppqwnvvnqh 467
Cdd:COG2132  286 ----------LPANLAPLPdLEDREAVRTRELVLTGGMAG-YVWTINGKAF--DPDRPDLTVKLG--------------- 337

                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 367021116 468 nhTAIRIIVNNRSPSAHPMHLHGHNFYVLHEgpgewDGTivRPSNPRRRDVYSVRSKG--HLVIQFDGAPGVWPFHCHIA 545
Cdd:COG2132  338 --ERERWTLVNDTMMPHPFHLHGHQFQVLSR-----NGK--PPPEGGWKDTVLVPPGEtvRILFRFDNYPGDWMFHCHIL 408

                        490
                 ....*....|....*
gi 367021116 546 WHVSGGFMATLIVKP 560
Cdd:COG2132  409 EHEDAGMMGQFEVVP 423
Cu-oxidase_3 pfam07732
Multicopper oxidase; This entry contains many divergent copper oxidase-like domains that are ...
 86-203 1.25e-46

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


Pssm-ID: 462247 [Multi-domain]  Cd Length: 119  Bit Score: 159.72  E-value: 1.25e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 367021116   86 TVSRASIAPDGYLR-DVLLVNGAFPGPLVEANWGDTIVVDVHNDITgpeEGTAIHWHGFLQHGTPWEDGVPGITQCPIPP 164
Cdd:pfam07732   1 TVTYGTVSPLGGTRqAVIGVNGQFPGPTIRVREGDTVVVNVTNNLD---EPTSIHWHGLQQRGTPWMDGVPGVTQCPIPP 77

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 367021116  165 RRSYRYEF-VASLYGTSWYHSHYSAQFAGGLFGPIVIHGP 203
Cdd:pfam07732  78 GQSFTYRFqVKQQAGTYWYHSHTSGQQAAGLAGAIIIEDR 117
 
Name Accession Description Interval E-value
ascorbase TIGR03388
L-ascorbate oxidase, plant type; Members of this protein family are the copper-containing ...
 80-572 2.58e-69

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.


Pssm-ID: 274555 [Multi-domain]  Cd Length: 541  Bit Score: 233.49  E-value: 2.58e-69
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 367021116   80 TRHYDFTVSRASIAPDGYLRDVLLVNGAFPGPLVEANWGDTIVVDVHNDITgpEEGTAIHWHGFLQHGTPWEDGVPGITQ 159
Cdd:TIGR03388   1 IRHYKWEVEYEFWSPDCFEKLVIGINGQFPGPTIRAQAGDTIVVELTNKLH--TEGVVIHWHGIRQIGTPWADGTAGVTQ 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 367021116  160 CPIPPRRSYRYEFVASLYGTSWYHSHYSAQFAGGLFGPIVIHGPTRE----NYDIDLGpILLTDWYHREyfdIIEEMLap 235
Cdd:TIGR03388  79 CAINPGETFIYNFVVDRPGTYFYHGHYGMQRSAGLYGSLIVDVPDGEkepfHYDGEFN-LLLSDWWHKS---IHEQEV-- 152

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 367021116  236 GGSAKVVS-----DNNLIDGKMHFDCStVAPGDNTPCFDNAGVSK--------FRFQTGKTHRLRLINGGADGVQRFSID 302
Cdd:TIGR03388 153 GLSSKPMRwigepQSLLINGRGQFNCS-LAAKFSSTNLPQCNLKGneqcapqiLHVEPGKTYRLRIASTTALAALNFAIE 231

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 367021116  303 EHTLTVIAEDFVPVKPYNTSVVTLGVGQRADVLVTANvGEPTSAFWMRSNLSScLPARQPYAVAAVYYDQAD-----TST 377
Cdd:TIGR03388 232 GHKLTVVEADGNYVEPFTVKDIDIYSGETYSVLLTTD-QDPSRNYWISVGVRG-RKPNTPPGLTVLNYYPNSpsrlpPTP 309

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 367021116  378 TPSSRAWDVLDPgtctndDLDITEPLFPIP-LPEPTLTHTMDIELFTNASNV---TLWKFNGVSM---------RADYNs 444
Cdd:TIGR03388 310 PPVTPAWDDFDR------SKAFSLAIKAAMgSPKPPETSDRRIVLLNTQNKIngyTKWAINNVSLtlphtpylgSLKYN- 382

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 367021116  445 pvLLLANDGNF---TYPPQWNVVN----------------QHNHTaIRIIVNN------RSPSAHPMHLHGHNFYVLHEG 499
Cdd:TIGR03388 383 --LLNAFDQKPppeNYPRDYDIFKpppnpntttgngiyrlKFNTT-VDVILQNantlngNNSETHPWHLHGHDFWVLGYG 459

                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 367021116  500 PGEWDGTIVRPS----NPRRRDVYSVRSKGHLVIQF--DGaPGVWPFHCHIAWHVsggFMATLIVKPDEVERM-EIPRDV 572
Cdd:TIGR03388 460 EGKFRPGVDEKSynlkNPPLRNTVVIFPYGWTALRFvaDN-PGVWAFHCHIEPHL---HMGMGVVFAEGVEKVgKLPKEA 535
CuRO_1_MaLCC_like cd13854
The first cupredoxin domain of the fungal laccases similar to Ma-LCC from Melanocarpus ...
 78-201 2.95e-69

The first cupredoxin domain of the fungal laccases similar to Ma-LCC from Melanocarpus albomyces; The subfamily of fungal laccases includes Ma-LCC and similar proteins. Ma-LCC is a multicopper oxidase (MCO) from Melanocarpus albomyces. Its crystal structure contains all four coppers at the mono- and trinuclear copper centers. Laccase is a blue multi-copper enzyme that catalyzes the oxidation of a variety aromatic - notably phenolic and inorganic substances coupled to the reduction of molecular oxygen to water. It has been implicated in a wide spectrum of biological activities and, in particular, plays a key role in morphogenesis, development and lignin metabolism in fungi and plants. Although MCOs have diverse functions, majority of them have three cupredoxin domain repeats that include one mononuclear and one trinuclear copper center. The copper ions are bound in several sites: Type 1, Type 2, and/or Type 3. The ensemble of types 2 and 3 copper is called a trinuclear cluster. MCOs oxidize their substrate by accepting electrons at a mononuclear copper center and transferring them to the active site trinuclear copper center. The cupredoxin domain 1 of 3-domain MCOs contains part the trinuclear copper binding site, which is located at the interface of domains 1 and 3.


Pssm-ID: 259923 [Multi-domain]  Cd Length: 122  Bit Score: 219.42  E-value: 2.95e-69
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 367021116  78 GVTRHYDFTVSRASIAPDGYLRDVLLVNGAFPGPLVEANWGDTIVVDVHNDItgPEEGTAIHWHGFLQHGTPWEDGVPGI 157
Cdd:cd13854    1 GVTRKYTLTITNSTLAPDGVEKEVMLINGQYPGPLIEANWGDTIEVTVINKL--QDNGTSIHWHGIRQLNTNWQDGVPGV 78

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....
gi 367021116 158 TQCPIPPRRSYRYEFVASLYGTSWYHSHYSAQFAGGLFGPIVIH 201
Cdd:cd13854   79 TECPIAPGDTRTYRFRATQYGTSWYHSHYSAQYGDGVVGPIVIH 122
CuRO_3_MaLCC_like cd13901
The third cupredoxin domain of the fungal laccases similar to Ma-LCC from Melanocarpus ...
 407-552 3.12e-63

The third cupredoxin domain of the fungal laccases similar to Ma-LCC from Melanocarpus albomyces; The subfamily of fungal laccases includes Ma-LCC and similar proteins. Ma-LCC is a multicopper oxidase (MCO) from Melanocarpus albomyces. Its crystal structure contains all four coppers at the mono- and trinuclear copper centers. Laccase is a blue multi-copper enzyme that catalyzes the oxidation of a variety aromatic - notably phenolic and inorganic substances coupled to the reduction of molecular oxygen to water. It has been implicated in a wide spectrum of biological activities and, in particular, plays a key role in morphogenesis, development and lignin metabolism in fungi and plants. Although MCOs have diverse functions, majority of them have three cupredoxin domain repeats that include one mononuclear and one trinuclear copper center. The copper ions are bound in several sites: Type 1, Type 2, and/or Type 3. The ensemble of types 2 and 3 copper is called a trinuclear cluster. MCOs oxidize their substrate by accepting electrons at a mononuclear copper center and transferring them to the active site trinuclear copper center. The cupredoxin domain 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.


Pssm-ID: 259968 [Multi-domain]  Cd Length: 157  Bit Score: 205.15  E-value: 3.12e-63
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 367021116 407 PLPEPTLTHTMDIELFTNASNVTLWKFNGVSMRADYNSPVLLLANDGN-FTYPPQWNVVN-QHNHTAIRIIVNNRSPSAH 484
Cdd:cd13901    2 PVPDPSPTQTLTIDLGPNATGVFLWTLNGSSFRVDWNDPTLLLVADGNtSTFPPEWNVIElPKANKWVYIVIQNNSPLPH 81

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 367021116 485 PMHLHGHNFYVLHEGPGEW--DGTIVRPSNPRRRDVYSVRSKGHLVIQF--DGaPGVWPFHCHIAWHVSGGF 552
Cdd:cd13901   82 PIHLHGHDFYILAQGTGTFddDGTILNLNNPPRRDVAMLPAGGYLVIAFktDN-PGAWLMHCHIAWHASGGL 152
PLN02604 PLN02604
oxidoreductase
 80-565 2.56e-62

oxidoreductase


Pssm-ID: 215324 [Multi-domain]  Cd Length: 566  Bit Score: 215.49  E-value: 2.56e-62
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 367021116  80 TRHYDFTVSRASIAPDGYLRDVLLVNGAFPGPLVEANWGDTIVVDVHNDITgpEEGTAIHWHGFLQHGTPWEDGVPGITQ 159
Cdd:PLN02604  24 IRRYKWEVKYEYKSPDCFKKLVITINGRSPGPTILAQQGDTVIVELKNSLL--TENVAIHWHGIRQIGTPWFDGTEGVTQ 101

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 367021116 160 CPIPPRRSYRYEFVASLYGTSWYHSHYSAQFAGGLFGPIVIHGPTREN----YDIDLGpILLTDWYHREYFDIIEEMLAP 235
Cdd:PLN02604 102 CPILPGETFTYEFVVDRPGTYLYHAHYGMQREAGLYGSIRVSLPRGKSepfsYDYDRS-IILTDWYHKSTYEQALGLSSI 180

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 367021116 236 GGSAKVVSDNNLIDGKMHFDCSTVA-PGDNTPCFDNAGVSKFRFQT----GKTHRLRLINGGADGVQRFSIDEHTLTVIA 310
Cdd:PLN02604 181 PFDWVGEPQSLLIQGKGRYNCSLVSsPYLKAGVCNATNPECSPYVLtvvpGKTYRLRISSLTALSALSFQIEGHNMTVVE 260

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 367021116 311 EDFVPVKPYNTSVVTLGVGQRADVLVTANvGEPTSAFWMRSNLSSCLPARQPYAVAAVYY----DQADTSTTPSSRAWDV 386
Cdd:PLN02604 261 ADGHYVEPFVVKNLFIYSGETYSVLVKAD-QDPSRNYWVTTSVVSRNNTTPPGLAIFNYYpnhpRRSPPTVPPSGPLWND 339

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 367021116 387 LDPGtcTNDDLDITEPLFPIPLPEPTLTHTMdieLFTNASN----VTLWKFNGVSmradYNSP--VLLLANDGNFTY--- 457
Cdd:PLN02604 340 VEPR--LNQSLAIKARHGYIHPPPLTSDRVI---VLLNTQNevngYRRWSVNNVS----FNLPhtPYLIALKENLTGafd 410

                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 367021116 458 ---PPQ---------WNVVNQHN------------HTAIRIIV------NNRSPSAHPMHLHGHNFYVLHEGPGEWDgti 507
Cdd:PLN02604 411 qtpPPEgydfanydiYAKPNNSNatssdsiyrlqfNSTVDIILqnantmNANNSETHPWHLHGHDFWVLGYGEGKFN--- 487

                        490       500       510       520       530       540
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 367021116 508 vRPSNPRR--------RDVYSVRSKGHLVIQFDG-APGVWPFHCHIAWHVsggFMATLIVKPDEVER 565
Cdd:PLN02604 488 -MSSDPKKynlvdpimKNTVPVHPYGWTALRFRAdNPGVWAFHCHIESHF---FMGMGVVFEEGIER 550
PLN02191 PLN02191
L-ascorbate oxidase
 77-562 1.14e-60

L-ascorbate oxidase


Pssm-ID: 177843 [Multi-domain]  Cd Length: 574  Bit Score: 211.41  E-value: 1.14e-60
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 367021116  77 TGVTRHYDFTVSRASIAPDGYLRDVLLVNGAFPGPLVEANWGDTIVVDVHNDITgpEEGTAIHWHGFLQHGTPWEDGVPG 156
Cdd:PLN02191  20 SAAVREYTWEVEYKYWWPDCKEGAVMTVNGQFPGPTIDAVAGDTIVVHLTNKLT--TEGLVIHWHGIRQKGSPWADGAAG 97

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 367021116 157 ITQCPIPPRRSYRYEFVASLYGTSWYHSHYSAQFAGGLFGPIVI---HGPT-RENYDIDLGpILLTDWYHREYFDiiEEM 232
Cdd:PLN02191  98 VTQCAINPGETFTYKFTVEKPGTHFYHGHYGMQRSAGLYGSLIVdvaKGPKeRLRYDGEFN-LLLSDWWHESIPS--QEL 174

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 367021116 233 LAPGGSAKVVSDNN--LIDGKMHFDCSTVAP----GDNTPCF----DNAGVSKFRFQTGKTHRLRLINGGADGVQRFSID 302
Cdd:PLN02191 175 GLSSKPMRWIGEAQsiLINGRGQFNCSLAAQfsngTELPMCTfkegDQCAPQTLRVEPNKTYRIRLASTTALASLNLAVQ 254

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 367021116 303 EHTLTVIAEDFVPVKPYNTSVVTLGVGQRADVLVTANvGEPTSAFWMRSNLSSCLPaRQPYAVAAVYYDQADTSTTPSSR 382
Cdd:PLN02191 255 GHKLVVVEADGNYITPFTTDDIDIYSGESYSVLLTTD-QDPSQNYYISVGVRGRKP-NTTQALTILNYVTAPASKLPSSP 332

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 367021116 383 AwdvldPGTCTNDDLD----ITEPLFPI---PLPePTLTHTMDIELftNASNV----TLWKFNGVSMRA----------- 440
Cdd:PLN02191 333 P-----PVTPRWDDFErsknFSKKIFSAmgsPSP-PKKYRKRLILL--NTQNLidgyTKWAINNVSLVTpatpylgsvky 404

                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 367021116 441 ------DYNSPVLLLANDGNFTYPPQWNVVNQHN-------HTAIRIIVNNRS------PSAHPMHLHGHNFYVLHEGPG 501
Cdd:PLN02191 405 nlklgfNRKSPPRSYRMDYDIMNPPPFPNTTTGNgiyvfpfNVTVDVIIQNANvlkgvvSEIHPWHLHGHDFWVLGYGDG 484

                        490       500       510       520       530       540       550
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 367021116 502 EW----DGTIVRPSNPRRRDVYSVRSKGHLVIQF-DGAPGVWPFHCHIAWHVSGGfMATLIVK--------PDE 562
Cdd:PLN02191 485 KFkpgiDEKTYNLKNPPLRNTAILYPYGWTAIRFvTDNPGVWFFHCHIEPHLHMG-MGVVFAEglnrigkiPDE 557
SufI COG2132
Multicopper oxidase with three cupredoxin domains (includes cell division protein FtsP and ...
 80-560 1.25e-60

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;


Pssm-ID: 441735 [Multi-domain]  Cd Length: 423  Bit Score: 207.09  E-value: 1.25e-60
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 367021116  80 TRHYDFTVSRASIA-PDGYLRDVLLVNGAFPGPLVEANWGDTIVVDVHNDItgpEEGTAIHWHGFLqhgTPWE-DGVPGI 157
Cdd:COG2132   13 GREYELTAQPATVElLPGKPTTVWGYNGQYPGPTIRVREGDRVRVRVTNRL---PEPTTVHWHGLR---VPNAmDGVPGD 86

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 367021116 158 tqcPIPPRRSYRYEFVAS-LYGTSWYHSHY----SAQFAGGLFGPIVIHGPTRE--NYDIDLgPILLTDWYHREYFDIIE 230
Cdd:COG2132   87 ---PIAPGETFTYEFPVPqPAGTYWYHPHThgstAEQVYRGLAGALIVEDPEEDlpRYDRDI-PLVLQDWRLDDDGQLLY 162

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 367021116 231 EMlaPGGSAKVVSDNNLIDGKmhfdcstVAPgdntpcfdnagvsKFRFQTGKTHRLRLINGGADGVQRFSI-DEHTLTVI 309
Cdd:COG2132  163 PM--DAAMGGRLGDTLLVNGR-------PNP-------------TLEVRPGERVRLRLLNASNARIYRLALsDGRPFTVI 220

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 367021116 310 AEDFVPV-KPYNTSVVTLGVGQRADVLVTANvGEPTSAFWMRSNLSsclpARQPYAVAAVYYDQADTSTTpssrawdvld 388
Cdd:COG2132  221 ATDGGLLpAPVEVDELLLAPGERADVLVDFS-ADPGEEVTLANPFE----GRSGRALLTLRVTGAAASAP---------- 285

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 367021116 389 pgtctnddldITEPLFPIP-LPEPTLTHTMDIELFTNASNvTLWKFNGVSMraDYNSPVLLLANDgnftyppqwnvvnqh 467
Cdd:COG2132  286 ----------LPANLAPLPdLEDREAVRTRELVLTGGMAG-YVWTINGKAF--DPDRPDLTVKLG--------------- 337

                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 367021116 468 nhTAIRIIVNNRSPSAHPMHLHGHNFYVLHEgpgewDGTivRPSNPRRRDVYSVRSKG--HLVIQFDGAPGVWPFHCHIA 545
Cdd:COG2132  338 --ERERWTLVNDTMMPHPFHLHGHQFQVLSR-----NGK--PPPEGGWKDTVLVPPGEtvRILFRFDNYPGDWMFHCHIL 408

                        490
                 ....*....|....*
gi 367021116 546 WHVSGGFMATLIVKP 560
Cdd:COG2132  409 EHEDAGMMGQFEVVP 423
laccase TIGR03389
laccase, plant; Members of this protein family include the copper-containing enzyme laccase ...
 80-569 1.68e-59

laccase, plant; Members of this protein family include the copper-containing enzyme laccase (EC 1.10.3.2), often several from a single plant species, and additional, uncharacterized, closely related plant proteins termed laccase-like multicopper oxidases. This protein family shows considerable sequence similarity to the L-ascorbate oxidase (EC 1.10.3.3) family. Laccases are enzymes of rather broad specificity, and classification of all proteins scoring about the trusted cutoff of this model as laccases may be appropriate.


Pssm-ID: 274556 [Multi-domain]  Cd Length: 539  Bit Score: 207.28  E-value: 1.68e-59
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 367021116   80 TRHYDFTVSRASIAPDGYLRDVLLVNGAFPGPLVEANWGDTIVVDVHNDITgpeEGTAIHWHGFLQHGTPWEDGVPGITQ 159
Cdd:TIGR03389   3 VRHYTFDVQEKNVTRLCSTKSILTVNGKFPGPTLYAREGDTVIVNVTNNVQ---YNVTIHWHGVRQLRNGWADGPAYITQ 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 367021116  160 CPIPPRRSYRYEFVASLY-GTSWYHSHYSAQFAGgLFGPIVIHGPTRENY-----DIDLgPILLTDWYHREYFDIIEEML 233
Cdd:TIGR03389  80 CPIQPGQSYVYNFTITGQrGTLWWHAHISWLRAT-VYGAIVILPKPGVPYpfpkpDREV-PIILGEWWNADVEAVINQAN 157

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 367021116  234 APGGsAKVVSDNNLIDGKmhfdcstvaPGDNTPCfDNAGVSKFRFQTGKTHRLRLINGGADGVQRFSIDEHTLTVIAEDF 313
Cdd:TIGR03389 158 QTGG-APNVSDAYTINGH---------PGPLYNC-SSKDTFKLTVEPGKTYLLRIINAALNDELFFAIANHTLTVVEVDA 226

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 367021116  314 VPVKPYNTSVVTLGVGQRADVLVTANvgEPTSAFWM--RSNLSSCLPARQPYAVAAVYYDQADTSTTPSSRAWDVLDPGT 391
Cdd:TIGR03389 227 TYTKPFKTKTIVIGPGQTTNVLLTAD--QSPGRYFMaaRPYMDAPGAFDNTTTTAILQYKGTSNSAKPILPTLPAYNDTA 304

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 367021116  392 CTNDDLD----ITEPLFPIPLPEptlthTMDIELFT-------NASNVTLWKFNGVSMRADYN-------SPVLLLAN-- 451
Cdd:TIGR03389 305 AATNFSNklrsLNSAQYPANVPV-----TIDRRLFFtiglgldPCPNNTCQGPNGTRFAASMNnisfvmpTTALLQAHyf 379

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 367021116  452 --DG--------------NFTYPPQWNVVNQHNHTAIRIIVNNRS------------PSAHPMHLHGHNFYVLHEGPGEW 503
Cdd:TIGR03389 380 giSGvfttdfpanpptkfNYTGTNLPNNLFTTNGTKVVRLKFNSTvelvlqdtsilgSENHPIHLHGYNFFVVGTGFGNF 459

                         490       500       510       520       530       540       550
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 367021116  504 DGTiVRPSN-----PRRRDVYSVRSKGHLVIQFDG-APGVWPFHCHIAWHVSGGFMATLIVK--PDEVERMEIP 569
Cdd:TIGR03389 460 DPK-KDPAKfnlvdPPERNTVGVPTGGWAAIRFVAdNPGVWFMHCHLEVHTTWGLKMAFLVDngKGPNQSLLPP 532
CuRO_1_Diphenol_Ox cd13857
The first cupredoxin domain of fungal laccase, diphenol oxidase; Diphenol oxidase belongs to ...
 81-201 4.40e-57

The first cupredoxin domain of fungal laccase, diphenol oxidase; Diphenol oxidase belongs to the laccase family. It catalyzes the initial steps in melanin biosynthesis from diphenols. Melanin is one of the virulence factors of infectious fungi. In the pathogenesis of C. neoformans, melanin pigments have been shown to protect the fungal cells from oxidative and microbicidal activities of host defense systems. Laccase is a blue multicopper oxidase (MCO) which catalyzes the oxidation of a variety aromatic - notably phenolic and inorganic substances coupled to the reduction of molecular oxygen to water. It has been implicated in a wide spectrum of biological activities and, in particular, plays a key role in morphogenesis, development and lignin metabolism. Although MCOs have diverse functions, majority of them have three cupredoxin domain repeats that include one mononuclear and one trinuclear copper center. The copper ions are bound in several sites: Type 1, Type 2, and/or Type 3. The ensemble of types 2 and 3 copper is called a trinuclear cluster. MCOs oxidize their substrate by accepting electrons at a mononuclear copper center and transferring them to the active site trinuclear copper center. The cupredoxin domain 1 of 3-domain MCOs contains part the trinuclear copper binding site, which is located at the interface of domains 1 and 3.


Pssm-ID: 259926 [Multi-domain]  Cd Length: 119  Bit Score: 187.47  E-value: 4.40e-57
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 367021116  81 RHYDFTVSRASIAPDGYLRDVLLVNGAFPGPLVEANWGDTIVVDVHNDITgpeEGTAIHWHGFLQHGTPWEDGVPGITQC 160
Cdd:cd13857    1 REYNFTISEITGAPDGFVRPMLVINGQFPGPLIEANQGDRIVVHVTNELD---EPTSIHWHGLFQNGTNWMDGTAGITQC 77

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|..
gi 367021116 161 PIPPRRSYRYEF-VASLYGTSWYHSHYSAQFAGGLFGPIVIH 201
Cdd:cd13857   78 PIPPGGSFTYNFtVDGQYGTYWYHSHYSTQYADGLVGPLIVH 119
CuRO_2_MaLCC_like cd13880
The second cupredoxin domain of the fungal laccases similar to Ma-LCC from Melanocarpus ...
 212-384 2.12e-55

The second cupredoxin domain of the fungal laccases similar to Ma-LCC from Melanocarpus albomyces; The subfamily of fungal laccases includes Ma-LCC and similar proteins. Ma-LCC is a multicopper oxidase (MCO) from Melanocarpus albomyces. Its crystal structure contains all four coppers at the mono- and trinuclear copper centers. Laccase is a blue multi-copper enzyme that catalyzes the oxidation of a variety aromatic - notably phenolic and inorganic substances coupled to the reduction of molecular oxygen to water. It has been implicated in a wide spectrum of biological activities and, in particular, plays a key role in morphogenesis, development and lignin metabolism in fungi and plants. Laccase is composed of three cupredoxin domains that include one mononuclear and one trinuclear copper center. The copper ions are bound in several sites: Type 1, Type 2, and/or Type 3. The ensemble of types 2 and 3 copper is called a trinuclear cluster. MCOs oxidize their substrate by accepting electrons at a mononuclear copper center and transferring them to the active site trinuclear copper center. The cupredoxin domain 2 of 3-domain MCOs has lost the ability to bind copper.


Pssm-ID: 259947 [Multi-domain]  Cd Length: 167  Bit Score: 184.76  E-value: 2.12e-55
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 367021116 212 LGPILLTDWYHREYFDIIEEMLAPGGsaKVVSDNNLIDGKMHFDCSTvapgdntpcfDNAGVSKFRFQTGKTHRLRLING 291
Cdd:cd13880    1 LGPVLLTDWYHRSAFELFSEELPTGG--PPPMDNILINGKGKFPCST----------GAGSYFETTFTPGKKYRLRLINT 68

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 367021116 292 GADGVQRFSIDEHTLTVIAEDFVPVKPYNTSVVTLGVGQRADVLVTANvGEPTSAFWMRS---NLSSCLPARQPYAVAAV 368
Cdd:cd13880   69 GVDTTFRFSIDGHNLTVIAADFVPIVPYTTDSLNIGIGQRYDVIVEAN-QDPVGNYWIRAepaTGCSGTNNNPDNRTGIL 147

                        170
                 ....*....|....*.
gi 367021116 369 YYDQADTSTTPSSRAW 384
Cdd:cd13880  148 RYDGASPTLDPSSTAN 163
CuRO_1_LCC_like cd04206
Cupredoxin domain 1 of laccase-like multicopper oxidases; including laccase, CueO, spore coat ...
 81-201 9.59e-48

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.


Pssm-ID: 259869 [Multi-domain]  Cd Length: 120  Bit Score: 162.84  E-value: 9.59e-48
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 367021116  81 RHYDFTVSRASIAPDGYLRDVLLVNGAFPGPLVEANWGDTIVVDVHNDItgPEEGTAIHWHGFLQHGTPWEDGVPGITQC 160
Cdd:cd04206    1 REYELTITETTVNPDGVLRQVITVNGQFPGPTIRVKEGDTVEVTVTNNL--PNEPTSIHWHGLRQPGTNDGDGVAGLTQC 78

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|..
gi 367021116 161 PIPPRRSYRYEF-VASLYGTSWYHSHYSAQFAGGLFGPIVIH 201
Cdd:cd04206   79 PIPPGESFTYRFtVDDQAGTFWYHSHVGGQRADGLYGPLIVE 120
Cu-oxidase_3 pfam07732
Multicopper oxidase; This entry contains many divergent copper oxidase-like domains that are ...
 86-203 1.25e-46

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


Pssm-ID: 462247 [Multi-domain]  Cd Length: 119  Bit Score: 159.72  E-value: 1.25e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 367021116   86 TVSRASIAPDGYLR-DVLLVNGAFPGPLVEANWGDTIVVDVHNDITgpeEGTAIHWHGFLQHGTPWEDGVPGITQCPIPP 164
Cdd:pfam07732   1 TVTYGTVSPLGGTRqAVIGVNGQFPGPTIRVREGDTVVVNVTNNLD---EPTSIHWHGLQQRGTPWMDGVPGVTQCPIPP 77

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 367021116  165 RRSYRYEF-VASLYGTSWYHSHYSAQFAGGLFGPIVIHGP 203
Cdd:pfam07732  78 GQSFTYRFqVKQQAGTYWYHSHTSGQQAAGLAGAIIIEDR 117
CuRO_1_tcLCC2_insect_like cd13858
The first cupredoxin domain of insect laccases similar to laccase 2 in Tribolium castaneum; ...
 95-201 3.36e-46

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.


Pssm-ID: 259927 [Multi-domain]  Cd Length: 105  Bit Score: 158.09  E-value: 3.36e-46
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 367021116  95 DGYLRDVLLVNGAFPGPLVEANWGDTIVVDVHNDItgPEEGTAIHWHGFLQHGTPWEDGVPGITQCPIPPRRSYRYEFVA 174
Cdd:cd13858    1 DGVERPVITVNGQLPGPSIEVCEGDTVVVDVKNRL--PGESTTIHWHGIHQRGTPYMDGVPMVTQCPILPGQTFRYKFKA 78

                         90       100
                 ....*....|....*....|....*..
gi 367021116 175 SLYGTSWYHSHYSAQFAGGLFGPIVIH 201
Cdd:cd13858   79 DPAGTHWYHSHSGTQRADGLFGALIVR 105
CuRO_1_Tv-LCC_like cd13856
The first cupredoxin domain of fungal laccases similar to Tv-LCC from Trametes versicolor; ...
 82-201 1.12e-45

The first cupredoxin domain of 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. 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.


Pssm-ID: 259925 [Multi-domain]  Cd Length: 125  Bit Score: 157.50  E-value: 1.12e-45
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 367021116  82 HYDFTVSRASIAPDGYLRDVLLVNGAFPGPLVEANWGDTIVVDVHNDITGP--EEGTAIHWHGFLQHGTPWEDGVPGITQ 159
Cdd:cd13856    2 TYTLNIVNTRLAPDGFERSAVLANGQFPGPLITANKGDTFRITVVNQLTDPtmRRSTSIHWHGIFQHGTNYADGPAFVTQ 81

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|...
gi 367021116 160 CPIPPRRSYRYEF-VASLYGTSWYHSHYSAQFAGGLFGPIVIH 201
Cdd:cd13856   82 CPIAPNHSFTYDFtAGDQAGTFWYHSHLSTQYCDGLRGPLVIY 124
CuRO_1_Abr2_like cd13850
The first cupredoxin domain of a group of fungal Laccases similar to Abr2 from Aspergillus ...
 83-201 1.93e-41

The first 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 1 of 3-domain MCOs contains part the trinuclear copper binding site, which is located at the interface of domains 1 and 3.


Pssm-ID: 259919 [Multi-domain]  Cd Length: 117  Bit Score: 145.52  E-value: 1.93e-41
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 367021116  83 YDFTVSRASIAPDGYLRDVLLVNGAFPGPLVEANWGDTIVVDVHNDItgPEEgTAIHWHGFLQHGTPWEDGVPGITQCPI 162
Cdd:cd13850    1 FTLTVTEGSPDGDGGEREVILINGQFPGPPIILDEGDEVEILVTNNL--PVN-TTIHFHGILQRGTPWSDGVPGVTQWPI 77

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|
gi 367021116 163 PPRRSYRYEFVASL-YGTSWYHSHYSAQFAGGLFGPIVIH 201
Cdd:cd13850   78 QPGGSFTYRWKAEDqYGLYWYHSHYRGYYMDGLYGPIYIR 117
ascorbOXfungal TIGR03390
L-ascorbate oxidase, fungal type; This model describes a family of fungal ascorbate oxidases, ...
 99-561 1.71e-40

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.


Pssm-ID: 132431 [Multi-domain]  Cd Length: 538  Bit Score: 154.61  E-value: 1.71e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 367021116   99 RDVLLVNGAFPGPLVEANWGDTIVVDVHNDItgPEEGTAIHWHGFLQHGTPWEDGVPGITQCPIPPRRSYRYEFVASL-- 176
Cdd:TIGR03390  27 RYSVVVNGTSPGPEIRLQEGQTTWIRVYNDI--PDNNVTMHWHGLTQRTAPFSDGTPLASQWPIPPGHFFDYEIKPEPgd 104

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 367021116  177 YGTSWYHSHYSAQfAGGLFGPIVIHGPTRENYDIDLG-PILLTDWYHREYFDIIEEMLA-----PGGSAKVvsdnnLIDG 250
Cdd:TIGR03390 105 AGSYFYHSHVGFQ-AVTAFGPLIVEDCEPPPYKYDDErILLVSDFFSATDEEIEQGLLStpftwSGETEAV-----LLNG 178

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 367021116  251 KmhfdcsTVAPGDNTPCFDNAGVSK--FRFQTGKTHRLRLINGGADGVQRFSIDEH-TLTVIAEDFVPVKPYNTSVVTLG 327
Cdd:TIGR03390 179 K------SGNKSFYAQINPSGSCMLpvIDVEPGKTYRLRFIGATALSLISLGIEDHeNLTIIEADGSYTKPAKIDHLQLG 252

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 367021116  328 VGQRADVLVTAN-----VGEPTSAFWMRSNLSSCLPARQPYAVaaVYYDQADTSTTPSSRAWDVLDPGTCTNDDLDIT-E 401
Cdd:TIGR03390 253 GGQRYSVLFKAKtedelCGGDKRQYFIQFETRDRPKVYRGYAV--LRYRSDKASKLPSVPETPPLPLPNSTYDWLEYElE 330

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 367021116  402 PL-------FPiPLPEPTLTHTMDI-ELFTNASNVTLWKFNGVSMRADY-NSPVLLLANDGNFTYPPQWNVVNQHNH--- 469
Cdd:TIGR03390 331 PLseennqdFP-TLDEVTRRVVIDAhQNVDPLNGRVAWLQNGLSWTESVrQTPYLVDIYENGLPATPNYTAALANYGfdp 409

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 367021116  470 ----------TAIRIIVNNRSPS--------AHPMHLHGHNFYVLHEGPGEWDGTI----VRPSNPRRRD---VYSVRSK 524
Cdd:TIGR03390 410 etrafpakvgEVLEIVWQNTGSYtgpnggvdTHPFHAHGRHFYDIGGGDGEYNATAneakLENYTPVLRDttmLYRYAVK 489

                         490       500       510       520       530
                  ....*....|....*....|....*....|....*....|....*....|
gi 367021116  525 GHlviqfDGAP-------------GVWPFHCHIAWHVSGGfMATLIVKPD 561
Cdd:TIGR03390 490 VV-----PGAPagwrawrirvtnpGVWMMHCHILQHMVMG-MQTVWVFGD 533
CuRO_1_AAO cd13845
The first cupredoxin domain of plant Ascorbate oxidase; Ascorbate oxidase catalyzes the ...
 81-200 4.73e-39

The first cupredoxin domain of plant Ascorbate oxidase; Ascorbate oxidase catalyzes the oxidation of ascorbic acid to dehydroascorbic acid. This multicopper oxidase (MCO) is found in cucurbitaceous plants such as pumpkin, cucumber, and melon. It can detect levels of ascorbic acid and eliminate it. The biological function of ascorbate oxidase is still not clear. Ascorbate oxidase belongs to MCO family which couple oxidation of substrates with reduction of dioxygen to water. MCOs are capable of oxidizing a vast range of substrates, varying from aromatic compounds to inorganic compounds such as metals. Although the members of this family have diverse functions, majority of them have three cupredoxin domain repeats. The copper ions are bound in several sites: Type 1, Type 2, and/or Type 3. The ensemble of types 2 and 3 copper is called a trinuclear cluster. MCOs oxidize their substrate by accepting electrons at a mononuclear copper center and transferring them to the active site trinuclear copper center. The cupredoxin domain 1 of 3-domain MCOs contains part the trinuclear copper binding site, which is located at the interface of domains 1 and 3.


Pssm-ID: 259914 [Multi-domain]  Cd Length: 120  Bit Score: 139.12  E-value: 4.73e-39
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 367021116  81 RHYDFTVSRASIAPDGYLRDVLLVNGAFPGPLVEANWGDTIVVDVHNDItgPEEGTAIHWHGFLQHGTPWEDGVPGITQC 160
Cdd:cd13845    1 RHYKWKVEYMFWAPDCVEKLVIGINGQFPGPTIRATAGDTIVVELENKL--PTEGVAIHWHGIRQRGTPWADGTASVSQC 78

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|
gi 367021116 161 PIPPRRSYRYEFVASLYGTSWYHSHYSAQFAGGLFGPIVI 200
Cdd:cd13845   79 PINPGETFTYQFVVDRPGTYFYHGHYGMQRSAGLYGSLIV 118
CuRO_1_Fet3p cd13851
The first Cupredoxin domain of multicopper oxidase Fet3P; Fet3p catalyzes the ferroxidase ...
 81-201 5.84e-38

The first Cupredoxin domain of multicopper oxidase Fet3P; Fet3p catalyzes the ferroxidase reaction, which couples the oxidation of Fe(II) to Fe(III) and a four-electron reduction of molecular oxygen to water. Fet3p is a type I membrane protein with the amino-terminal oxidase domain in the exocellular space and the carboxyl terminus in the cytoplasm. The periplamic produced Fe(III) is transferred to the permease Ftr1p for import into the cytosol. The four copper ions are inserted post-translationally and are essential for catalytic activity, thus linking copper and iron homeostasis. Like other related multicopper oxidases (MCOs), Fet3p is composed of three cupredoxin domains that include one mononuclear and one trinuclear copper center. The copper ions are bound in several sites: Type 1, Type 2, and/or Type 3. The ensemble of types 2 and 3 copper is called a trinuclear cluster. MCOs oxidize their substrate by accepting electrons at a mononuclear copper center and transferring them to the active site trinuclear copper center. The cupredoxin domain 1 of 3-domain MCOs contains part the trinuclear copper binding site, which is located at the interface of domains 1 and 3.


Pssm-ID: 259920 [Multi-domain]  Cd Length: 121  Bit Score: 136.24  E-value: 5.84e-38
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 367021116  81 RHYDFTVSRASIAPDG-YLRDVLLVNGAFPGPLVEANWGDTIVVDVHNDItgPEEGTAIHWHGFLQHGTPWEDGVPGITQ 159
Cdd:cd13851    1 VEFDWNITWVTANPDGlFERRVIGINGQWPPPPIEVNKGDTVVIHATNSL--GDQPTSLHFHGLFQNGTNYMDGPVGVTQ 78

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|...
gi 367021116 160 CPIPPRRSYRYEFVASL-YGTSWYHSHYSAQFAGGLFGPIVIH 201
Cdd:cd13851   79 CPIPPGQSFTYEFTVDTqVGTYWYHSHDGGQYPDGLRGPFIIH 121
CuRO_2_MCO_like_1 cd13886
The second cupredoxin domain of uncharacterized multicopper oxidase; Multicopper Oxidases ...
 215-353 3.98e-33

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.


Pssm-ID: 259953 [Multi-domain]  Cd Length: 163  Bit Score: 124.31  E-value: 3.98e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 367021116 215 ILLTDWYHREYFDIIEEMLAPG-GSAKVVSDNNLIDGKMHFDCSTvAPGDNTPCFDNAGVSKFRFQTGKTHRLRLINGGA 293
Cdd:cd13886    3 VMVNDYYHDPSSVLLARYLAPGnEGDEPVPDNGLINGIGQFDCAS-ATYKIYCCASNGTYYNFTLEPNKTYRLRLINAGS 81

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 367021116 294 DGVQRFSIDEHTLTVIAEDFVPVKPYNTSVVTLGVGQRADVLVTANvGEPTSAFWMRSNL 353
Cdd:cd13886   82 FADFTFSVDGHPLTVIEADGTLVEPVEVHSITISVAQRYSVILTTN-QPTGGNFWMRAEL 140
CuRO_2_LCC_like cd04205
Cupredoxin domain 2 of laccase-like multicopper oxidases; including laccase, CueO, spore coat ...
 214-366 3.77e-32

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.


Pssm-ID: 259868 [Multi-domain]  Cd Length: 152  Bit Score: 121.31  E-value: 3.77e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 367021116 214 PILLTDWYHREYFDIIEEMLAPGGSAKVVSDNNLIDGKMHFDCStvapgdNTPCFDNAGVSKFRFQTGKTHRLRLINGGA 293
Cdd:cd04205    2 VLLLSDWYHDSAEDVLAGYMPNSFGNEPVPDSLLINGRGRFNCS------MAVCNSGCPLPVITVEPGKTYRLRLINAGS 75

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 367021116 294 DGVQRFSIDEHTLTVIAEDFVPVKPYNTSVVTLGVGQRADVLVTANvgEPTSAFWMRSNL--SSCLPARQPYAVA 366
Cdd:cd04205   76 FASFNFAIDGHNMTVIEVDGGYVEPLEVDNLDLAPGQRYDVLVKAD--QPPGNYWIRASAdgRTFDEGGNPNGTA 148
CuRO_2_Diphenol_Ox cd13883
The second cupredoxin domain of fungal laccase, diphenol oxidase; Diphenol oxidase belongs to ...
 215-371 2.28e-31

The second cupredoxin domain of fungal laccase, diphenol oxidase; Diphenol oxidase belongs to the laccase family. It catalyzes the initial steps in melanin biosynthesis from diphenols. Melanin is one of the virulence factors of infectious fungi. In the pathogenesis of C. neoformans, melanin pigments have been shown to protect the fungal cells from oxidative and microbicidal activities of host defense systems. Laccase is a blue multi-copper enzyme that catalyzes the oxidation of a variety aromatic - notably phenolic and inorganic substances coupled to the reduction of molecular oxygen to water. It has been implicated in a wide spectrum of biological activities and, in particular, plays a key role in morphogenesis, development and lignin metabolism. Laccase is a multicopper oxidase (MCO) composed of three cupredoxin domains that include one mononuclear and one trinuclear copper center. The copper ions are bound in several sites: Type 1, Type 2, and/or Type 3. The ensemble of types 2 and 3 copper is called a trinuclear cluster. MCOs oxidize their substrate by accepting electrons at a mononuclear copper center and transferring them to the active site trinuclear copper center. The cupredoxin domain 2 of 3-domain MCOs has lost the ability to bind copper.


Pssm-ID: 259950 [Multi-domain]  Cd Length: 164  Bit Score: 119.37  E-value: 2.28e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 367021116 215 ILLTDWYHREYFDIIEEMLAP----GGSAKVVSDNNLIDGKMHFDCSTVAPGdnTPCFDNaGVSKFRFQTGKTHRLRLIN 290
Cdd:cd13883    3 LFISDWYHDQSEVIVAGLLSPqgykGSPAAPSPDSALINGIGQFNCSAADPG--TCCTQT-SPPEIQVEAGKRTRFRLIN 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 367021116 291 GGADGVQRFSIDEHTLTVIAEDFVPV-KPYNTSVVTLGVGQRADVLVTANVGEPTSAFWMRSNL-SSCL--PARQPYAVA 366
Cdd:cd13883   80 AGSHAMFRFSVDNHTLNVVEADDTPVyGPTVVHRIPIHNGQRYSVIIDTTSGKAGDSFWLRARMaTDCFawDLQQQTGKA 159


                 ....*
gi 367021116 367 AVYYD 371
Cdd:cd13883  160 ILRYV 164
Cu-oxidase_2 pfam07731
Multicopper oxidase; This entry contains many divergent copper oxidase-like domains that are ...
 441-562 2.37e-31

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


Pssm-ID: 462246 [Multi-domain]  Cd Length: 138  Bit Score: 118.69  E-value: 2.37e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 367021116  441 DYNSPVLLLANDGNF----------TYPPQWNVVNQHNHTAIRIIVNNRSPSAHPMHLHGHNFYVLHEGPGEWDGTIVRP 510
Cdd:pfam07731   3 PPKLPTLLQITSGNFrrndwainglLFPPNTNVITLPYGTVVEWVLQNTTTGVHPFHLHGHSFQVLGRGGGPWPEEDPKT 82

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 367021116  511 ---SNPRRRDVYSVRSKGHLVIQFD-GAPGVWPFHCHIAWHVSGGFMATLIVKPDE 562
Cdd:pfam07731  83 ynlVDPVRRDTVQVPPGGWVAIRFRaDNPGVWLFHCHILWHLDQGMMGQFVVRPGD 138
CuRO_1_CopA cd13848
The first cupredoxin domain of CopA copper resistance protein family; CopA is a multicopper ...
 81-201 6.10e-31

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.


Pssm-ID: 259917 [Multi-domain]  Cd Length: 116  Bit Score: 116.61  E-value: 6.10e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 367021116  81 RHYDFTVSRASIAPDGYLRDVLLVNGAFPGPLVEANWGDTIVVDVHNDItgpEEGTAIHWHGFLqhgTPWE-DGVPGITQ 159
Cdd:cd13848    1 VEYDLVIAETPVNIGGKEGEAITVNGQVPGPLLRFKEGDDATIRVHNRL---DEDTSIHWHGLL---LPNDmDGVPGLSF 74

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|..
gi 367021116 160 CPIPPRRSYRYEFVASLYGTSWYHSHYSAQFAGGLFGPIVIH 201
Cdd:cd13848   75 PGIKPGETFTYRFPVRQSGTYWYHSHSGLQEQTGLYGPIIID 116
PLN02168 PLN02168
copper ion binding / pectinesterase
 83-504 2.37e-28

copper ion binding / pectinesterase


Pssm-ID: 215113 [Multi-domain]  Cd Length: 545  Bit Score: 119.31  E-value: 2.37e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 367021116  83 YDFTVSRASIAPDGYLRDVLLVNGAFPGPLVEANWGDTIVVDVHNDITGPEEGTaihWHGFLQHGTPWEDGVPGiTQCPI 162
Cdd:PLN02168  29 YQWVVSYSQRFILGGNKQVIVINDMFPGPLLNATANDVINVNIFNNLTEPFLMT---WNGLQLRKNSWQDGVRG-TNCPI 104

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 367021116 163 PPRRSYRYEF-VASLYGTSWYHSHYSAQFAGGLFGPIVIHGPT---------RENYDidlgpILLTDWYHREYFDIieEM 232
Cdd:PLN02168 105 LPGTNWTYRFqVKDQIGSYFYFPSLLLQKAAGGYGAIRIYNPElvpvpfpkpDEEYD-----ILIGDWFYADHTVM--RA 177

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 367021116 233 LAPGGSAKVVSDNNLIDGKmhfdcstvAPGDNTpcfdnagvskFRFQTGKTHRLRLINGGADGVQRFSIDEHTLTVIAED 312
Cdd:PLN02168 178 SLDNGHSLPNPDGILFNGR--------GPEETF----------FAFEPGKTYRLRISNVGLKTCLNFRIQDHDMLLVETE 239

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 367021116 313 FVPVKPYNTSVVTLGVGQRADVLVTANvgeptsafwmrsnlssclpaRQPYAVAAVYYDQAdtsttpSSRAWDVLDPGTC 392
Cdd:PLN02168 240 GTYVQKRVYSSLDIHVGQSYSVLVTAK--------------------TDPVGIYRSYYIVA------TARFTDAYLGGVA 293

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 367021116 393 T----NDDLDITEPLFPIPLP-------EPTLTHTMDIELFTNASN---------------------VTL------WKFN 434
Cdd:PLN02168 294 LirypNSPLDPVGPLPLAPALhdyfssvEQALSIRMDLNVGAARSNpqgsyhygrinvtrtiilhndVMLssgklrYTIN 373

                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 367021116 435 GVSM--------RADYNS------PVLLLANDGNFTYPPQWNVVNQHNHTAIRIIVNNRSPSAHPMHLHGHNFYVLHEGP 500
Cdd:PLN02168 374 GVSFvypgtplkLVDHFQlndtiiPGMFPVYPSNKTPTLGTSVVDIHYKDFYHIVFQNPLFSLESYHIDGYNFFVVGYGF 453


                 ....
gi 367021116 501 GEWD 504
Cdd:PLN02168 454 GAWS 457
Cu-oxidase pfam00394
Multicopper oxidase; Many of the proteins in this family contain multiple similar copies of ...
 211-373 1.39e-27

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


Pssm-ID: 395317 [Multi-domain]  Cd Length: 146  Bit Score: 108.17  E-value: 1.39e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 367021116  211 DLGPILLTDWYHREYFDIIEEMLAPGGSAKV---VSDNNLIDGKmhfdcstvapgdntpcfDNAGVSKFRFQTGKTHRLR 287
Cdd:pfam00394   1 EDYVITLSDWYHKDAKDLEKELLASGKAPTDfppVPDAVLINGK-----------------DGASLATLTVTPGKTYRLR 63

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 367021116  288 LINGGADGVQRFSIDEHTLTVIAEDFVPVKPYNTSVVTLGVGQRADVLVTANvgEPTSAFWMRSNlSSCLPARQPYAVAA 367
Cdd:pfam00394  64 IINVALDDSLNFSIEGHKMTVVEVDGVYVNPFTVDSLDIFPGQRYSVLVTAN--QDPGNYWIVAS-PNIPAFDNGTAAAI 140


                  ....*.
gi 367021116  368 VYYDQA 373
Cdd:pfam00394 141 LRYSGA 146
CuRO_3_Fet3p cd13899
The third Cupredoxin domain of multicopper oxidase Fet3p; Fet3p catalyzes the ferroxidase ...
 414-560 3.77e-27

The third Cupredoxin domain of multicopper oxidase Fet3p; Fet3p catalyzes the ferroxidase reaction, which couples the oxidation of Fe(II) to Fe(III) with the four-electron reduction of molecular oxygen to water. Fet3p is a type I membrane protein with the amino-terminal oxidase domain in the extracellular space and the carboxyl terminus in the cytoplasm. The periplasmic produced Fe(III) is transferred to the permease Ftr1p for import into the cytosol. The four copper ions are inserted post-translationally and are essential for catalytic activity, thus linking copper and iron homeostasis. Like other related multicopper oxidases (MCOs), Fet3p is composed of three cupredoxin domains that include one mononuclear and one trinuclear copper center. The copper ions are bound in several sites: Type 1, Type 2, and/or Type 3. The ensemble of types 2 and 3 copper is called a trinuclear cluster. MCOs oxidize their substrate by accepting electrons at a mononuclear copper center and transferring them to the active site trinuclear copper center. The cupredoxin domain 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.


Pssm-ID: 259966 [Multi-domain]  Cd Length: 160  Bit Score: 107.34  E-value: 3.77e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 367021116 414 THTMDIELFTNASNVTLWKFNGVSmradYNSPV---LLLANDGNF------TYPPQWN-VVNQHNHTaIRIIVNNRSPSA 483
Cdd:cd13899    3 SITLNVDFDTFDDGVNRAAFNNIT----YVSPKvptLYTALSMGDdaldpaIYGPQTNaFVLNHGEV-VELVVNNWDAGK 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 367021116 484 HPMHLHGHNFYVLHEGPGEWDGTIVRP-----SNPRRRDVYSVRSKGHLVIQF--DGaPGVWPFHCHIAWHVSGGFMATL 556
Cdd:cd13899   78 HPFHLHGHKFQVVQRSPDVASDDPNPPinefpENPMRRDTVMVPPGGSVVIRFraDN-PGVWFFHCHIEWHLEAGLAATF 156


                 ....
gi 367021116 557 IVKP 560
Cdd:cd13899  157 IEAP 160
CuRO_1_LCC_plant cd13849
The first cupredoxin domain of plant laccases; Laccase is a blue multicopper oxidase (MCO) ...
 83-201 4.52e-27

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.


Pssm-ID: 259918 [Multi-domain]  Cd Length: 117  Bit Score: 105.80  E-value: 4.52e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 367021116  83 YDFTVSRASIAPDGYLRDVLLVNGAFPGPLVEANWGDTIVVDVHNDITGpeeGTAIHWHGFLQHGTPWEDGVPGITQCPI 162
Cdd:cd13849    1 YTFVVQEKNVTRLCSTKSILTVNGQFPGPTIRVHEGDTVVVNVTNRSPY---NITIHWHGIRQLRSGWADGPAYITQCPI 77

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|
gi 367021116 163 PPRRSYRYEF-VASLYGTSWYHSHYSAQFAgGLFGPIVIH 201
Cdd:cd13849   78 QPGQSYTYRFtVTGQEGTLWWHAHISWLRA-TVYGAFIIR 116
PLN02354 PLN02354
copper ion binding / oxidoreductase
 82-538 6.68e-27

copper ion binding / oxidoreductase


Pssm-ID: 177987 [Multi-domain]  Cd Length: 552  Bit Score: 114.89  E-value: 6.68e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 367021116  82 HYDFTVSRASIAPDGYLRDVLLVNGAFPGPLVEANWGDTIVVDVHNDITGPeegTAIHWHGFLQHGTPWEDGVPGiTQCP 161
Cdd:PLN02354  29 FFTWNVTYGTASPLGVPQQVILINGQFPGPNINSTSNNNIVINVFNNLDEP---FLLTWSGIQQRKNSWQDGVPG-TNCP 104

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 367021116 162 IPPRRSYRYEF-VASLYGTSWYHSHYSAQFAGGLFGPIVIHG----PTRENYDIDLGPILLTDWYHREYfDIIEEMLAPG 236
Cdd:PLN02354 105 IPPGTNFTYHFqPKDQIGSYFYYPSTGMHRAAGGFGGLRVNSrlliPVPYADPEDDYTVLIGDWYTKSH-TALKKFLDSG 183

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 367021116 237 GSAKvVSDNNLIDGKmhfdcSTVAPGDNTPCFDnagvskfrFQTGKTHRLRLINGGADGVQRFSIDEHTLTVIAEDFVPV 316
Cdd:PLN02354 184 RTLG-RPDGVLINGK-----SGKGDGKDEPLFT--------MKPGKTYRYRICNVGLKSSLNFRIQGHKMKLVEMEGSHV 249

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 367021116 317 KPYNTSVVTLGVGQRADVLVTANvgEPTSAFWMrsnLSSCLPARQPY-AVAAVYYDQADTSTT------PSSRAWDvLDP 389
Cdd:PLN02354 250 LQNDYDSLDVHVGQCFSVLVTAN--QAPKDYYM---VASTRFLKKVLtTTGIIRYEGGKGPASpelpeaPVGWAWS-LNQ 323

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 367021116 390 GTCTNDDLDITEPLfpiPLPEPTLTH-----TMDIELFTNASNV---TLWKFNGVSMRaDYNSPVLLL----ANDGNFTY 457
Cdd:PLN02354 324 FRSFRWNLTASAAR---PNPQGSYHYgkiniTRTIKLVNSASKVdgkLRYALNGVSHV-DPETPLKLAeyfgVADKVFKY 399

                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 367021116 458 ------PP--------QWNVVNQHNHTAIRIIVNNRSPSAHPMHLHGHNFYVLHEGPGEWdgtivrpsNPRRRDVYSV-- 521
Cdd:PLN02354 400 dtikdnPPakitkikiQPNVLNITFRTFVEIIFENHEKSMQSWHLDGYSFFAVAVEPGTW--------TPEKRKNYNLld 471

                        490       500
                 ....*....|....*....|....*...
gi 367021116 522 -----------RSKGHLVIQFDGApGVW 538
Cdd:PLN02354 472 avsrhtvqvypKSWAAILLTFDNA-GMW 498
CuRO_3_MCO_like_4 cd13910
The third cupredoxin domain of uncharacterized multicopper oxidase; Multicopper Oxidases (MCOs) ...
 422-558 1.51e-26

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.


Pssm-ID: 259977 [Multi-domain]  Cd Length: 166  Bit Score: 105.84  E-value: 1.51e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 367021116 422 FTNASNVTLWKFNGVSMRADYNSPVLLLANDGNFTY------------PPQWNVVNQHNHTAIRIIVNNRSPSAHPMHLH 489
Cdd:cd13910    9 ILAYNNLPRGFFNGTSWRPLPGPATLLLALDADNAEevaagnglstfdGNQLVITVDDIDKVVDLVINNLDDGDHPFHLH 88

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 367021116 490 GHNFYVLHEGPGEW--------DGTIVRPSNPRRRDVYSVRSKGHLVIQF--DGaPGVWPFHCHIAWHVSGGFMATLIV 558
Cdd:cd13910   89 GHKFWVLGSGDGRYggggytapDGTSLNTTNPLRRDTVSVPGFGWAVLRFvaDN-PGLWAFHCHILWHMAAGMLMQFAV 166
PLN02792 PLN02792
oxidoreductase
 76-514 6.38e-25

oxidoreductase


Pssm-ID: 178389 [Multi-domain]  Cd Length: 536  Bit Score: 108.91  E-value: 6.38e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 367021116  76 RTGVTRHYDFTVSRASIAPDGYLRDVLLVNGAFPGPLVEANWGDTIVVDVHNDITGPeegTAIHWHGFLQHGTPWEDGVP 155
Cdd:PLN02792  12 KADDTLFYNWRVTYGNISLLTLPRRGILINGQFPGPEIRSLTNDNLVINVHNDLDEP---FLLSWNGVHMRKNSYQDGVY 88

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 367021116 156 GiTQCPIPPRRSYRYEF-VASLYGTSWYHSHYSAQFAGGLFGPIVIHGPTR---------ENYDidlgpILLTDWYHREY 225
Cdd:PLN02792  89 G-TTCPIPPGKNYTYDFqVKDQVGSYFYFPSLAVQKAAGGYGSLRIYSLPRipvpfpepaGDFT-----FLIGDWYRRNH 162

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 367021116 226 fDIIEEMLAPGGSAKVVSDNNLIDGKmhfdcstvapGDNTpcfdnagVSKFRFQTGKTHRLRLINGGADGVQRFSIDEHT 305
Cdd:PLN02792 163 -TTLKKILDGGRKLPLMPDGVMINGQ----------GVSY-------VYSITVDKGKTYRFRISNVGLQTSLNFEILGHQ 224

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 367021116 306 LTVI-AEDFVPVKPYNTSvVTLGVGQRADVLVT------------------ANVGEPTSAFWMRSNLSSCLPARQPYAVA 366
Cdd:PLN02792 225 LKLIeVEGTHTVQSMYTS-LDIHVGQTYSVLVTmdqppqnysivvstrfiaAKVLVSSTLHYSNSKGHKIIHARQPDPDD 303

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 367021116 367 AVY-YDQADTSTTPSSRAWDVLDP-GTCTNDDLDITEPLFpiplpeptlthtmdieLFTNASNV---TLWKFNGVSMRAD 441
Cdd:PLN02792 304 LEWsIKQAQSIRTNLTASGPRTNPqGSYHYGKMKISRTLI----------------LESSAALVkrkQRYAINGVSFVPS 367

                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 367021116 442 yNSPvLLLAND---------GNFTYPPQ--------WNVVNQHNHTAIRIIVNNRSPSAHPMHLHGHNFYVLHEGPGEWD 504
Cdd:PLN02792 368 -DTP-LKLADHfkikgvfkvGSIPDKPRrgggmrldTSVMGAHHNAFLEIIFQNREKIVQSYHLDGYNFWVVGINKGIWS 445

                        490
                 ....*....|
gi 367021116 505 GTIVRPSNPR 514
Cdd:PLN02792 446 RASRREYNLK 455
CuRO_1_CumA_like cd13861
The first cupredoxin domain of CumA like multicopper oxidase; This multicopper oxidase (MCO) ...
 83-200 1.45e-24

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.


Pssm-ID: 259930 [Multi-domain]  Cd Length: 119  Bit Score: 98.85  E-value: 1.45e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 367021116  83 YDFTVSRASIAPDGYLR-DVLLVNGAFPGPLVEANWGDTIVVDVHNDItgpEEGTAIHWHGFlqhGTPWE-DGVPGITQC 160
Cdd:cd13861    3 YTLTAAPAELLDLGGPTtRTWGYNGQVPGPELRVRQGDTLRVRLTNRL---PEPTTIHWHGL---RLPNAmDGVPGLTQP 76

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|..
gi 367021116 161 PIPPRRSYRYEFVASLYGTSWYHSHYSAQFAG--GLFGPIVI 200
Cdd:cd13861   77 PVPPGESFTYEFTPPDAGTYWYHPHVGSQEQLdrGLYGPLIV 118
CuRO_2_LCC_plant cd13875
The second cupredoxin domain of the plant laccases; Laccase is a blue multi-copper enzyme that ...
 214-368 3.50e-24

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.


Pssm-ID: 259943 [Multi-domain]  Cd Length: 148  Bit Score: 98.82  E-value: 3.50e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 367021116 214 PILLTDWYHREYFDIIEEMLAPGGSAKVvSDNNLIDGKmhfdcstvaPGDNTPCfDNAGVSKFRFQTGKTHRLRLINGGA 293
Cdd:cd13875    2 PIILGEWWNRDVNDVEDQALLTGGGPNI-SDAYTINGQ---------PGDLYNC-SSKDTFVLTVEPGKTYLLRIINAAL 70

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 367021116 294 DGVQRFSIDEHTLTVIAEDFVPVKPYNTSVVTLGVGQRADVLVTANvgEPTSAFWMRSNLSSCLPARQPYAVAAV 368
Cdd:cd13875   71 NEELFFKIANHTLTVVAVDASYTKPFTTDYILIAPGQTTDVLLTAD--QPPGRYYMAARPYQSAPPVPFDNTTAT 143
CuRO_1_2dMco_1 cd13860
The first cupredoxin domain of bacteria two domain multicopper oxidase; This subfamily ...
 105-201 6.58e-24

The first cupredoxin domain of bacteria two domain multicopper oxidase; This subfamily includes bacterial two domain multicopper oxidases (2dMCOs) with similarity to McoN from Nitrosomonas europaea. 2dMCO is a trimeric type C blue copper oxidase. Each subunit houses a type 1 copper site in domain 1 and a type 2/type 3 trinuclear copper cluster at the subunit-subunit interface. The 2dMCO is proposed to be a key intermediate in the evolution of three domain MCOs. Multicopper oxidases couple oxidation of substrates with reduction of dioxygen to water. These MCOs are capable of oxidizing a vast range of substrates, varying from aromatic to inorganic compounds such as metals.


Pssm-ID: 259929 [Multi-domain]  Cd Length: 119  Bit Score: 96.88  E-value: 6.58e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 367021116 105 NGAFPGPLVEANWGDTIVVDVHNDItgPEEgTAIHWHGF-LQHGtpwEDGVPGITQCPIPPRRSYRYEFVASLYGTSWYH 183
Cdd:cd13860   26 NGSVPGPTIEVTEGDRVRILVTNEL--PEP-TTVHWHGLpVPNG---MDGVPGITQPPIQPGETFTYEFTAKQAGTYMYH 99

                         90       100
                 ....*....|....*....|
gi 367021116 184 SHY--SAQFAGGLFGPIVIH 201
Cdd:cd13860  100 SHVdeAKQEDMGLYGAFIVH 119
CuRO_2_Tv-LCC_like cd13882
The second cupredoxin domain of the fungal laccases similar to Tv-LCC from Trametes versicolor; ...
 215-362 7.40e-23

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.


Pssm-ID: 259949 [Multi-domain]  Cd Length: 159  Bit Score: 95.17  E-value: 7.40e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 367021116 215 ILLTDWYHreyfDIIEEMLAPGGSAKVVSDNNLIDGKMHFDcstvapGDNTPCFdnagvSKFRFQTGKTHRLRLINGGAD 294
Cdd:cd13882    3 ITLGDWYH----TAAPDLLATTAGVPPVPDSGTINGKGRFD------GGPTSPL-----AVINVKRGKRYRFRVINISCI 67

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 367021116 295 GVQRFSIDEHTLTVIAEDFVPVKPYNTSVVTLGVGQRADVLVTANvgEPTSAFWMRSNLSSCLPARQP 362
Cdd:cd13882   68 PSFTFSIDGHNLTVIEADGVETKPLTVDSVQIYAGQRYSVVVEAN--QPVDNYWIRAPPTGGTPANNG 133
CuRO_1_AAO_like_1 cd13846
The first cupredoxin domain of plant Ascorbate oxidase homologs; This subfamily is composed of ...
 83-201 1.90e-22

The first cupredoxin domain of plant Ascorbate oxidase homologs; This subfamily is composed of plant pollen multicopper oxidase homologous to ascorbate oxidase. Ascorbate oxidase catalyzes the oxidation of ascorbic acid to dehydroascorbic acid. This multicopper oxidase (MCO) is found in cucurbitaceous plants such as pumpkin, cucumber, and melon. It can detect levels of ascorbic acid and eliminate it. The biological function of ascorbate oxidase is still not clear. Ascorbate oxidase belongs to MCO family which couple oxidation of substrates with reduction of dioxygen to water. MCOs are capable of oxidizing a vast range of substrates, varying from aromatic compounds to inorganic compounds such as metals. Although the members of this family have diverse functions, majority of them have three cupredoxin domain repeats. The copper ions are bound in several sites: Type 1, Type 2, and/or Type 3. The ensemble of types 2 and 3 copper is called a trinuclear cluster. MCOs oxidize their substrate by accepting electrons at a mononuclear copper center and transferring them to the active site trinuclear copper center. The cupredoxin domain 1 of 3-domain MCOs contains part the trinuclear copper binding site, which is located at the interface of domains 1 and 3. This subfamily does not harbor trinuclear copper binding histidines.


Pssm-ID: 259915 [Multi-domain]  Cd Length: 118  Bit Score: 92.86  E-value: 1.90e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 367021116  83 YDFTVSRASIAPDGYLRDVLLVNGAFPGPLVEANWGDTIVVDVHNDItgpEEGTAIHWHGFLQHGTPWEDGVPGiTQCPI 162
Cdd:cd13846    3 FDWNVSYITASPLGVPQQVIAINGQFPGPTINVTTNDNVVVNVFNSL---DEPLLLTWNGIQQRRNSWQDGVLG-TNCPI 78

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|
gi 367021116 163 PPRRSYRYEF-VASLYGTSWYHSHYSAQFAGGLFGPIVIH 201
Cdd:cd13846   79 PPGWNWTYKFqVKDQIGSFFYFPSLHFQRAAGGFGGIRVN 118
CuRO_2_Fet3p_like cd13877
The second Cupredoxin domain of multicopper oxidase Fet3P; Fet3p catalyzes the ferroxidase ...
 215-339 1.99e-22

The second Cupredoxin domain of multicopper oxidase Fet3P; Fet3p catalyzes the ferroxidase reaction, which couples the oxidation of Fe(II) to Fe(III) with the four-electron reduction of molecular oxygen to water. Fet3p is a type I membrane protein with the amino-terminal oxidase domain in the extracellular space and the carboxyl terminus in the cytoplasm. The periplasmic produced Fe(III) is transferred to the permease Ftr1p for import into the cytosol. The four copper ions are inserted post-translationally and are essential for catalytic activity, thus linking copper and iron homeostasis. Like other related multicopper oxidases (MCOs), Fet3p is composed of three cupredoxin domains that include one mononuclear and one trinuclear copper center. The copper ions are bound in several sites: Type 1, Type 2, and/or Type 3. The ensemble of types 2 and 3 copper is called a trinuclear cluster. MCOs oxidize their substrate by accepting electrons at a mononuclear copper center and transferring them to the active site trinuclear copper center. The cupredoxin domain 2 of 3-domain MCOs has lost the ability to bind copper.


Pssm-ID: 259945 [Multi-domain]  Cd Length: 148  Bit Score: 93.77  E-value: 1.99e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 367021116 215 ILLTDWYHREYFDIIEEML---APGGsAKVVSDNNLIDGKMHfdcstvapgdntpcfdnagvSKFRFQTGKTHRLRLING 291
Cdd:cd13877    5 LTLSDWYHDQSPDLLRDFLspyNPTG-AEPIPDSSLFNDTQN--------------------ATINFEPGKTYLLRIINM 63

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*...
gi 367021116 292 GADGVQRFSIDEHTLTVIAEDFVPVKPYNTSVVTLGVGQRADVLVTAN 339
Cdd:cd13877   64 GAFASQYFHIEGHDMTIIEVDGVYVKPYPVDTLYIAVGQRYSVLVKAK 111
CuRO_D1_2dMcoN_like cd13859
The first cupredoxin domain of bacterial two domain multicopper oxidase McoN and similar ...
 81-200 2.25e-22

The first cupredoxin domain of bacterial two domain multicopper oxidase McoN and similar proteins; This family includes bacterial two domain multicopper oxidases (2dMCOs) represented by the McoN from Nitrosomonas europaea. McoN is a trimeric type C blue copper oxidase. Each subunit houses a type 1 copper site in domain 1 and a type 2/type 3 trinuclear copper cluster at the subunit-subunit interface. The 2dMCO is proposed to be a key intermediate in the evolution of three domain MCOs. Its biological function has not been characterized. Multicopper oxidases couple oxidation of substrates with reduction of dioxygen to water. These MCOs are capable of oxidizing a vast range of substrates, varying from aromatic to inorganic compounds such as metals.


Pssm-ID: 259928 [Multi-domain]  Cd Length: 122  Bit Score: 92.54  E-value: 2.25e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 367021116  81 RHYDFTV--SRASIAPDGYLRdVLLVNGAFPGPLVEANWGDTIVVDVHNDITGPEegtAIHWHGFLQHGTPWEDGVPGIT 158
Cdd:cd13859    1 REFEMTIdeTVITVVPGLDFK-TFAFNGQVPGPLIHVKEGDDLVVHVTNNTTLPH---TIHWHGVLQMGSWKMDGVPGVT 76

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*
gi 367021116 159 QCPIPPRRSYRYEFVASLYGTSWYHSHYSA-QFAG--GLFGPIVI 200
Cdd:cd13859   77 QPAIEPGESFTYKFKAERPGTLWYHCHVNVnEHVGmrGMWGPLIV 121
CuRO_3_LCC_like cd04207
Cupredoxin domain 3 of laccase-like multicopper oxidases; including laccase, CueO, spore coat ...
 472-556 1.75e-21

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.


Pssm-ID: 259870 [Multi-domain]  Cd Length: 132  Bit Score: 90.60  E-value: 1.75e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 367021116 472 IRIIVNNRSPSAHPMHLHGHNFYVLHEGPGEWDGTIvRPSNPRRRDVYSVRSKGHLVIQFD-GAPGVWPFHCHIAWHVSG 550
Cdd:cd04207   47 IVLINAGNHDMQHPFHLHGHSFWVLGSGGGPFDAPL-NLTNPPWRDTVLVPPGGWVVIRFKaDNPGVWMLHCHILEHEDA 125


                 ....*.
gi 367021116 551 GFMATL 556
Cdd:cd04207  126 GMMTVF 131
PLN02835 PLN02835
oxidoreductase
 81-521 2.93e-21

oxidoreductase


Pssm-ID: 178429 [Multi-domain]  Cd Length: 539  Bit Score: 97.73  E-value: 2.93e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 367021116  81 RHYDFTVSRASIAPDGYLRDVLLVNGAFPGPLVEANWGDTIVVDVHNDITGPeegTAIHWHGFLQHGTPWEDGVPGiTQC 160
Cdd:PLN02835  30 KYYTWTVTYGTISPLGVPQQVILINGQFPGPRLDVVTNDNIILNLINKLDQP---FLLTWNGIKQRKNSWQDGVLG-TNC 105

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 367021116 161 PIPPRRSYRYEF-VASLYGTSWYHSHYSAQFAGGLFGPIVIHGPTR-----ENYDIDLgPILLTDWYHREYfDIIEEMLA 234
Cdd:PLN02835 106 PIPPNSNYTYKFqTKDQIGTFTYFPSTLFHKAAGGFGAINVYERPRipipfPLPDGDF-TLLVGDWYKTSH-KTLQQRLD 183

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 367021116 235 PGGSAKvVSDNNLIDGKMHfdcstvapgdntpcfdnagvSKFRFQTGKTHRLRLINGGADGVQRFSIDEHTLTVIAEDFV 314
Cdd:PLN02835 184 SGKVLP-FPDGVLINGQTQ--------------------STFSGDQGKTYMFRISNVGLSTSLNFRIQGHTMKLVEVEGS 242

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 367021116 315 PVKPYNTSVVTLGVGQRADVLVTANvgEPTSAFWMrsnLSSCLPARQPYAVAAVYYdqADTSTTPSSRAWDVLDPGTCTN 394
Cdd:PLN02835 243 HTIQNIYDSLDVHVGQSVAVLVTLN--QSPKDYYI---VASTRFTRQILTATAVLH--YSNSRTPASGPLPALPSGELHW 315

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 367021116 395 DDLDITEPLFPI------PLPEPT-----LTHTMDIELFTNASNVT---LWKFNGVSM--------RADYNSPVLLLAND 452
Cdd:PLN02835 316 SMRQARTYRWNLtasaarPNPQGSfhygkITPTKTIVLANSAPLINgkqRYAVNGVSYvnsdtplkLADYFGIPGVFSVN 395

                        410       420       430       440       450       460       470
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 367021116 453 GNFTYPP------QWNVVNQHNHTAIRIIVNNRSPSAHPMHLHGHNFYVLHEGPGEWdgtivrpsNPRRRDVYSV 521
Cdd:PLN02835 396 SIQSLPSggpafvATSVMQTSLHDFLEVVFQNNEKTMQSWHLDGYDFWVVGYGSGQW--------TPAKRSLYNL 462
CuRO_1_AAO_like_2 cd13847
The first cupredoxin domain of Ascorbate oxidase homologs; This family includes fungal ...
 99-200 3.12e-21

The first cupredoxin domain of Ascorbate oxidase homologs; This family includes fungal proteins with similarity to ascorbate oxidase. Ascorbate oxidase catalyzes the oxidation of ascorbic acid to dehydroascorbic acid. It can detect levels of ascorbic acid and eliminate it. The biological function of ascorbate oxidase is still not clear. Ascorbate oxidase belongs to multicopper oxidase (MCO) family which couple oxidation of substrates with reduction of dioxygen to water. MCOs are capable of oxidizing a vast range of substrates, varying from aromatic compounds to inorganic compounds such as metals. Although the members of this family have diverse functions, majority of them have three cupredoxin domain repeats. The copper ions are bound in several sites: Type 1, Type 2, and/or Type 3. The ensemble of types 2 and 3 copper is called a trinuclear cluster. MCOs oxidize their substrate by accepting electrons at a mononuclear copper center and transferring them to the active site trinuclear copper center. The cupredoxin domain 1 of 3-domain MCOs contains part the trinuclear copper binding site, which is located at the interface of domains 1 and 3.


Pssm-ID: 259916 [Multi-domain]  Cd Length: 117  Bit Score: 89.13  E-value: 3.12e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 367021116  99 RDVLLVNGAFPGPLVEANWGDTIVVDVHNDItgPEEGTAIHWHGFLQHGTPWEDGVPGITQCPIPPRRSYRYEFV--ASL 176
Cdd:cd13847   15 RPSTLINGSFPGPELRVQEGQHLWVRVYNDL--EAGNTTMHFHGLSQYMSPFSDGTPLASQWPIPPGKFFDYEFPleAGD 92

                         90       100
                 ....*....|....*....|....
gi 367021116 177 YGTSWYHSHYSAQfAGGLFGPIVI 200
Cdd:cd13847   93 AGTYYYHSHVGFQ-SVTAYGALIV 115
CuRO_3_Diphenol_Ox cd13904
The third cupredoxin domain of fungal laccase, diphenol oxidase; Diphenol oxidase belongs to ...
 474-558 5.83e-21

The third cupredoxin domain of fungal laccase, diphenol oxidase; Diphenol oxidase belongs to the laccase family. It catalyzes the initial steps in melanin biosynthesis from diphenols. Melanin is one of the virulence factors of infectious fungi. In the pathogenesis of C. neoformans, melanin pigments have been shown to protect the fungal cells from oxidative and microbicidal activities of host defense systems. Laccase is a blue multicopper oxidase (MCO) which catalyzes the oxidation of a variety aromatic - notably phenolic and inorganic substances coupled to the reduction of molecular oxygen to water. It has been implicated in a wide spectrum of biological activities and, in particular, plays a key role in morphogenesis, development and lignin metabolism. Although MCOs have diverse functions, majority of them have three cupredoxin domain repeats that include one mononuclear and one trinuclear copper center. The copper ions are bound in several sites: Type 1, Type 2, and/or Type 3. The ensemble of types 2 and 3 copper is called a trinuclear cluster. MCOs oxidize their substrate by accepting electrons at a mononuclear copper center and transferring them to the active site trinuclear copper center. The cupredoxin domain 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.


Pssm-ID: 259971 [Multi-domain]  Cd Length: 158  Bit Score: 89.66  E-value: 5.83e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 367021116 474 IIVNNR-SPSAHPMHLHGHNFYVLHEGPG-----EWDGTIVRPSNPRRRDVYSVRSKGHLVIQFD-GAPGVWPFHCHIAW 546
Cdd:cd13904   67 IVINNLdPAIDHPYHLHGVDFHIVARGSGtltleQLANVQYNTTNPLRRDTIVIPGGSWAVLRIPaDNPGVWALHCHIGW 146

                         90
                 ....*....|..
gi 367021116 547 HVSGGFMATLIV 558
Cdd:cd13904  147 HLAAGFAGVVVV 158
PLN00044 PLN00044
multi-copper oxidase-related protein; Provisional
 82-503 3.53e-20

multi-copper oxidase-related protein; Provisional


Pssm-ID: 165622 [Multi-domain]  Cd Length: 596  Bit Score: 94.35  E-value: 3.53e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 367021116  82 HYDFTVSRASIAPDGYL--RDVLLVNGAFPGPL--VEANWgdTIVVDVHNditGPEEGTAIHWHGFLQHGTPWEDGVPGi 157
Cdd:PLN00044  29 YYDWEVSYVSAAPLGGVkkQEAIGINGQFPGPAlnVTTNW--NLVVNVRN---ALDEPLLLTWHGVQQRKSAWQDGVGG- 102

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 367021116 158 TQCPIPPRRSYRYEF-VASLYGTSWYHSHYSAQFAGGLFGPIVIHG--------PTRENYDIDLgpiLLTDWYHREYFDI 228
Cdd:PLN00044 103 TNCAIPAGWNWTYQFqVKDQVGSFFYAPSTALHRAAGGYGAITINNrdvipipfGFPDGGDITL---FIADWYARDHRAL 179

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 367021116 229 IEEMlaPGGSAKVVSDNNLID--GKMHFDCSTVAPGdntpcfdnAGVSKFRFQTGKTHRLRLINGGADGVQRFSIDEHTL 306
Cdd:PLN00044 180 RRAL--DAGDLLGAPDGVLINafGPYQYNDSLVPPG--------ITYERINVDPGKTYRFRVHNVGVATSLNFRIQGHNL 249

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 367021116 307 TVIAEDFVPVKPYNTSVVTLGVGQRADVLVTANVGEPTSAFWMRS-NLSSCLPARQPYAVAAVYY--------------- 370
Cdd:PLN00044 250 LLVEAEGSYTSQQNYTNLDIHVGQSYSFLLTMDQNASTDYYVVASaRFVDAAVVDKLTGVAILHYsnsqgpasgplpdap 329

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 367021116 371 -DQADTS---TTPSSRAWDVLDPGTCTNDD-----LDITeplfpipLPEPTLTHTMDIELFTNASNVTLwkfNGVSMRAD 441
Cdd:PLN00044 330 dDQYDTAfsiNQARSIRWNVTASGARPNPQgsfhyGDIT-------VTDVYLLQSMAPELIDGKLRATL---NEISYIAP 399

                        410       420       430       440       450       460       470
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 367021116 442 ynSPVLLLANDGN------FTYP-------PQWN--VVNQHNHTAIRIIVNNRSPSAHPMHLHGHNFYVLHEGPGEW 503
Cdd:PLN00044 400 --STPLMLAQIFNvpgvfkLDFPnhpmnrlPKLDtsIINGTYKGFMEIIFQNNATNVQSYHLDGYAFFVVGMDYGLW 474
PLN02991 PLN02991
oxidoreductase
 81-521 4.37e-20

oxidoreductase


Pssm-ID: 215536 [Multi-domain]  Cd Length: 543  Bit Score: 93.93  E-value: 4.37e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 367021116  81 RHYDFTVSRASIAPDGYLRDVLLVNGAFPGPLVEANWGDTIVVDVHNDItgpEEGTAIHWHGFLQHGTPWEDGVPGiTQC 160
Cdd:PLN02991  29 RFFEWHVTYGNISPLGVAQQGILINGKFPGPDIISVTNDNLIINVFNHL---DEPFLISWSGIRNWRNSYQDGVYG-TTC 104

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 367021116 161 PIPPRRSYRYEF-VASLYGTSWYHSHYSAQFAGGLFGPIVIHG----PTRENYDIDLGPILLTDWYHREYFDIIEEMlaP 235
Cdd:PLN02991 105 PIPPGKNYTYALqVKDQIGSFYYFPSLGFHKAAGGFGAIRISSrpliPVPFPAPADDYTVLIGDWYKTNHKDLRAQL--D 182

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 367021116 236 GGSAKVVSDNNLIDGKmhfdcstvapgdntpcfdNAGVSkFRFQTGKTHRLRLINGGADGVQRFSIDEHTLTVIAEDFVP 315
Cdd:PLN02991 183 NGGKLPLPDGILINGR------------------GSGAT-LNIEPGKTYRLRISNVGLQNSLNFRIQNHTMKLVEVEGTH 243

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 367021116 316 VKPYNTSVVTLGVGQRADVLVTANvgEPTSAFWMRsnLSSCLPARQPYAVAAVYYDQADTSTT------PSSRAWDvLDP 389
Cdd:PLN02991 244 TIQTPFSSLDVHVGQSYSVLITAD--QPAKDYYIV--VSSRFTSKILITTGVLHYSNSAGPVSgpipdgPIQLSWS-FDQ 318

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 367021116 390 GTCTNDDLDITEPLfpiPLPEPTLTH-----TMDIELFTNASNVTLWKFNGVSMRADY--NSPVLL--------LANDGN 454
Cdd:PLN02991 319 ARAIKTNLTASGPR---PNPQGSYHYgkiniTRTIRLANSAGNIEGKQRYAVNSASFYpaDTPLKLadyfkiagVYNPGS 395

                        410       420       430       440       450       460       470
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 367021116 455 FTYPPQW-------NVVNQHNHTAIRIIVNNRSPSAHPMHLHGHNFYVLHEGPGEWdgtivrpsNPRRRDVYSV 521
Cdd:PLN02991 396 IPDQPTNgaifpvtSVMQTDYKAFVEIVFENWEDIVQTWHLDGYSFYVVGMELGKW--------SAASRKVYNL 461
CuRO_1_MCO_like_2 cd13864
The second cupredoxin domain of uncharacterized multicopper oxidase; Multicopper Oxidases ...
 84-200 1.66e-19

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 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 1 of 3-domain MCOs contains part the trinuclear copper binding site, which is located at the interface of domains 1 and 3.


Pssm-ID: 259932 [Multi-domain]  Cd Length: 139  Bit Score: 84.89  E-value: 1.66e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 367021116  84 DFTVSRASIAPDGYLRDVLLVNG--AFPGPLVEANWGDTIVVDVHNDITGPEEG---------TAIHWHGFLQHGTPWE- 151
Cdd:cd13864    3 LLIILRISVEYNKDGKQIISINGsnDTIGPTIRVKSGDTLNLLVTNHLCNEQELskiwqdycpTSIHFHGLVLENFGKQl 82

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 367021116 152 ----DGVPGITQCPIPPRRSYRYEFV--ASLYGTSWYHSHYSAQFAGGLFGPIVI 200
Cdd:cd13864   83 anlvDGVPGLTQYPIGVGESYWYNFTipEDTCGTFWYHSHSSVQYGDGLRGVFIV 137
CuRO_1_LCC_like_3 cd13865
The second cupredoxin domain of uncharacterized multicopper oxidase; Multicopper Oxidases ...
 86-201 2.09e-19

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 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 1 of 3-domain MCOs contains part the trinuclear copper binding site, which is located at the interface of domains 1 and 3.


Pssm-ID: 259933 [Multi-domain]  Cd Length: 115  Bit Score: 83.90  E-value: 2.09e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 367021116  86 TVSRASIAPDGYLRDVLLVNGAFPGPLVEANWGDTIVVDVHNDITGPeegTAIHWHGFLqhgTPW-EDGVPGITQCPIPP 164
Cdd:cd13865    4 TVASRTIEVNGKAATVYGIRQPDGTEGLRLTEGDRFDVELENRLDEP---TTIHWHGLI---PPNlQDGVPDVTQPPIPP 77

                         90       100       110
                 ....*....|....*....|....*....|....*..
gi 367021116 165 RRSYRYEFVASLYGTSWYHSHYSAQFAGGLFGPIVIH 201
Cdd:cd13865   78 GQSQRYDFPLVQPGTFWMHSHYGLQEQKLLAAPLIIR 114
CuRO_2_tcLCC_insect_like cd13884
The second cupredoxin domain of the insect laccases similar to laccase 2 in Tribolium ...
 215-350 6.30e-18

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.


Pssm-ID: 259951 [Multi-domain]  Cd Length: 150  Bit Score: 80.74  E-value: 6.30e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 367021116 215 ILLTDWYHReyfDIIEEMLAPGGSAKVVS-DNNLIDGKMHFDCSTVAPGDNTPcfdnagVSKFRFQTGKTHRLRLINGGA 293
Cdd:cd13884    4 ILIQDWTHE---LSSERFVGRGHNGGGQPpDSILINGKGRYYDPKTGNTNNTP------LEVFTVEQGKRYRFRLINAGA 74

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 367021116 294 DGVQ-RFSIDEHTLTVIAEDFVPVKPY-NTSVVTLGvGQRADVLVTANvgEPTSAFWMR 350
Cdd:cd13884   75 TNCPfRVSIDGHTLTVIASDGNDVEPVeVDSIIIYP-GERYDFVLNAN--QPIGNYWIR 130
CuRO_3_CopA cd13896
The third cupredoxin domain of CopA copper resistance protein family; CopA is a multicopper ...
 472-558 1.06e-17

The third cupredoxin domain of CopA copper resistance protein family; CopA is a multicopper oxidase (MCO) related to laccase and L-ascorbate oxidase, both copper-containing enzymes. It is part of the copper-regulatory cue operon, which employs a cytosolic metalloregulatory protein CueR that induces expression of CopA and CueO under copper stress conditions. CopA is a copper efflux P-type ATPase that is located in the inner cell membrane and is is involved in copper resistance in bacteria. CopA mutant causes a loss of function including copper tolerance and oxidase activity and copA transcription is inducible in the presence of copper. Although MCOs have diverse functions, majority of them have three cupredoxin domain repeats that include one mononuclear and one trinuclear copper center. The copper ions are bound in several sites: Type 1, Type 2, and/or Type 3. The ensemble of types 2 and 3 copper is called a trinuclear cluster. MCOs oxidize their substrate by accepting electrons at a mononuclear copper center and transferring them to the active site trinuclear copper center. The cupredoxin domain 3 of 3-domain MCOs contains the Type 1 (T1) copper binding site and part the trinuclear copper binding site, which is located at the interface of domains 1 and 3.


Pssm-ID: 259963 [Multi-domain]  Cd Length: 115  Bit Score: 79.22  E-value: 1.06e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 367021116 472 IRIIVNNRSPSAHPMHLHGHNFYVlHEGPGEwdgtivrpSNPrRRDVYSVRSKGHLVIQFD-GAPGVWPFHCHIAWHVSG 550
Cdd:cd13896   38 VRIVFVNDTMMAHPMHLHGHFFQV-ENGNGE--------YGP-RKDTVLVPPGETVSVDFDaDNPGRWAFHCHNLYHMEA 107


                 ....*...
gi 367021116 551 GFMATLIV 558
Cdd:cd13896  108 GMMRVVEY 115
CuRO_3_Tv-LCC_like cd13903
The third cupredoxin domain of the fungal laccases similar to Tv-LCC from Trametes Versicolor; ...
 422-552 9.60e-17

The third 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. 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.


Pssm-ID: 259970 [Multi-domain]  Cd Length: 147  Bit Score: 77.32  E-value: 9.60e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 367021116 422 FTNASNVTLWKFNGVSmradYNSP---VLLLANDGN---FTYPPQWNV-VNQHNHTAIRIIVNNRSPSAHPMHLHGHNFY 494
Cdd:cd13903    8 FGLNGTTGLFTINGVS----YVSPtvpVLLQILSGAtsaEDLLPTESTiILPRNKVVEITIPGGAIGGPHPFHLHGHAFS 83

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 367021116 495 VLHEGPGEWDGTIvrpsNPRRRDVYSVRSKGHLV-IQF--DGaPGVWPFHCHIAWHVSGGF 552
Cdd:cd13903   84 VVRSAGSNTYNYV----NPVRRDVVSVGTPGDGVtIRFvtDN-PGPWFLHCHIDWHLEAGL 139
CuRO_3_LCC_plant cd13897
The third cupredoxin domain of the plant laccases; Laccase is a blue multicopper oxidase (MCO) ...
 481-559 1.50e-16

The third cupredoxin domain of the 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 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.


Pssm-ID: 259964 [Multi-domain]  Cd Length: 139  Bit Score: 76.53  E-value: 1.50e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 367021116 481 PSAHPMHLHGHNFYVLHEGPGEWDGTIVRPS----NPRRRDVYSVRSKGHLVIQFDGA-PGVWPFHCHIAWHVSGGFMAT 555
Cdd:cd13897   54 AENHPMHLHGFDFYVVGRGFGNFDPSTDPATfnlvDPPLRNTVGVPRGGWAAIRFVADnPGVWFMHCHFERHTSWGMATV 133


                 ....
gi 367021116 556 LIVK 559
Cdd:cd13897  134 FIVK 137
CuRO_D2_2dMcoN_like cd04202
The second cupredoxin domain of bacterial two domain multicopper oxidase McoN and similar ...
 472-559 1.12e-13

The second cupredoxin domain of bacterial two domain multicopper oxidase McoN and similar proteins; This family includes bacterial two domain multicopper oxidases (2dMCOs) represented by the McoN from Nitrosomonas europaea. McoN is a trimeric type C blue copper oxidase. Each subunit houses a type 1 copper site in domain 1 and a type 2/type 3 trinuclear copper cluster at the subunit-subunit interface. The 2dMCO is proposed to be a key intermediate in the evolution of three domain MCOs. The biological function of McoN has not been characterized. Multicopper oxidases couple oxidation of substrates with reduction of dioxygen to water. These MCOs are capable of oxidizing a vast range of substrates, varying from aromatic to inorganic compounds such as metals.


Pssm-ID: 259865 [Multi-domain]  Cd Length: 138  Bit Score: 68.43  E-value: 1.12e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 367021116 472 IRIIvnNRSPSAHPMHLHGHNFYVLHEgpgewDGTIVRPSNPRRRDVYSVRSKGHLVIQFDG-APGVWPFHCHIAWHVS- 549
Cdd:cd04202   53 IRLI--NLSMDHHPMHLHGHFFLVTAT-----DGGPIPGSAPWPKDTLNVAPGERYDIEFVAdNPGDWMFHCHKLHHAMn 125

                         90
                 ....*....|...
gi 367021116 550 ---GGFMATLIVK 559
Cdd:cd04202  126 gmgGGMMTLIGYE 138
CuRO_3_tcLLC2_insect_like cd13905
The third cupredoxin domain of the insect laccases similar to laccase 2 in Tribolium castaneum; ...
 462-557 6.34e-13

The third cupredoxin domain of the 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 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.


Pssm-ID: 259972 [Multi-domain]  Cd Length: 174  Bit Score: 67.32  E-value: 6.34e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 367021116 462 NVVNQHNHTAIRIIVNNRSP---SAHPMHLHGHNFYVLHEGPGE------------------WDGTIVRP--SNPRRRDV 518
Cdd:cd13905   45 HVIKLPLNSVVEIVLINEGPgpgLSHPFHLHGHSFYVLGMGFPGynsttgeilsqnwnnkllDRGGLPGRnlVNPPLKDT 124

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|.
gi 367021116 519 YSVRSKGHLVIQF--DGaPGVWPFHCHIAWHVSGGfMATLI 557
Cdd:cd13905  125 VVVPNGGYVVIRFraDN-PGYWLLHCHIEFHLLEG-MALVL 163
CuRO_2_AAO cd13871
The second cupredoxin domain of plant Ascorbate oxidase; Ascorbate oxidase catalyzes the ...
 215-362 8.07e-13

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.


Pssm-ID: 259939 [Multi-domain]  Cd Length: 166  Bit Score: 66.80  E-value: 8.07e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 367021116 215 ILLTDWYHReyfDIIEEMLapGGSAKVVS-----DNNLIDGKMHFDCSTVAPGDNTPCFDNAGVSK-------FRFQTGK 282
Cdd:cd13871    6 ILLSDWWHK---SIYEQET--GLSSKPFRwvgepQSLLIEGRGRYNCSLAPAYPSSLPSPVCNKSNpqcapfiLHVSPGK 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 367021116 283 THRLRLINGGADGVQRFSIDEHTLTVIAEDFVPVKPYNTSVVTLGVGQRADVLVTANvGEPTSAFWMRSNLSSCLPARQP 362
Cdd:cd13871   81 TYRLRIASVTALSSLNFIIEGHNLTVVEADGNYVQPFEVSNLDIYSGETYSVLVTAD-QDPSRNYWVSVNVRGRRPNTPP 159
CuRO_1_MCO_like_1 cd13862
The first cupredoxin domain of uncharacterized multicopper oxidase; Multicopper Oxidases (MCOs) ...
 105-200 1.93e-12

The first 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 1 of 3-domain MCOs contains part the trinuclear copper binding site, which is located at the interface of domains 1 and 3.


Pssm-ID: 259931 [Multi-domain]  Cd Length: 123  Bit Score: 64.46  E-value: 1.93e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 367021116 105 NGAFPGPLVEANWGDTIVVDVHNDITGPEEgtaIHWHGFL----QHGTPwEDGVPgitqcPIPPRRSYRYEFVASLYGTS 180
Cdd:cd13862   26 NGQVPGPLLRMRQGVSVTVDVFNDTDIPEY---VHWHGLPlpadVDGAM-EEGTP-----SVPPHGHRRYRMTPRPAGFR 96

                         90       100
                 ....*....|....*....|....*..
gi 367021116 181 WYHSH-------YSAQFAgGLFGPIVI 200
Cdd:cd13862   97 WYHTHvmtmddlTRGQYS-GLFGFVYI 122
CuRO_3_Abr2_like cd13898
The third cupredoxin domain of a group of fungal Laccases similar to Abr2 from Aspergillus ...
 421-557 2.22e-12

The third 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 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.


Pssm-ID: 259965 [Multi-domain]  Cd Length: 164  Bit Score: 65.36  E-value: 2.22e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 367021116 421 LFTNASNVTL-WKFNGVSM-RADYNSPVLLLANDGNFTYPPQWNVVNQHNHTAIRIIVNNRSPSA--HPMHLHGHNFYVL 496
Cdd:cd13898    6 LTLGRVGSAYsWTLNGTELyPLDEEAYPPLLFLPDPATALDSALTISTKNGTWVDLIFQVTGPPQppHPIHKHGNKAFVI 85

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 367021116 497 HEGPGEWDGTIV------RPS-----NPRRRDVY----SVRSKGHLVIQFD-GAPGVWPFHCHIAWHVSGGfMATLI 557
Cdd:cd13898   86 GTGTGPFNWSSVaeaaeaAPEnfnlvNPPLRDTFttppSTEGPSWLVIRYHvVNPGAWLLHCHIQSHLAGG-MAVVL 161
CuRO_3_AAO_like_2 cd13895
The third cupredoxin domain of Ascorbate oxidase homologs; This family includes fungal ...
 474-557 2.29e-12

The third cupredoxin domain of Ascorbate oxidase homologs; This family includes fungal proteins with similarity to ascorbate oxidase. Ascorbate oxidase catalyzes the oxidation of ascorbic acid to dehydroascorbic acid. It can detect levels of ascorbic acid and eliminate it. The biological function of ascorbate oxidase is still not clear. Ascorbate oxidase belongs to multicopper oxidase (MCO) family which couple oxidation of substrates with reduction of dioxygen to water. MCOs are capable of oxidizing a vast range of substrates, varying from aromatic compounds to inorganic compounds such as metals. Although the members of this family have diverse functions, majority of them have three cupredoxin domain repeats. The copper ions are bound in several sites: Type 1, Type 2, and/or Type 3. The ensemble of types 2 and 3 copper is called a trinuclear cluster. MCOs oxidize their substrate by accepting electrons at a mononuclear copper center and transferring them to the active site trinuclear copper center. The cupredoxin domain 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.


Pssm-ID: 259962 [Multi-domain]  Cd Length: 188  Bit Score: 65.80  E-value: 2.29e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 367021116 474 IIVNNRSPS----AHPMHLHGHNFYVLHEGPGEWDGT------IVRPSNPRRRD---VYSVRSKGHLVIQFDGA------ 534
Cdd:cd13895   79 VWQNTASPTggldAHPWHAHGAHYYDLGSGLGTYSATalaneeKLRGYNPIRRDttmLYRYGGKGYYPPPGTGSgwrawr 158

                         90       100
                 ....*....|....*....|....*...
gi 367021116 535 -----PGVWPFHCHIAWHVSGGFMATLI 557
Cdd:cd13895  159 lrvddPGVWMLHCHILQHMIMGMQTVWV 186
CuRO_3_AAO cd13893
The third cupredoxin domain of plant Ascorbate oxidase; Ascorbate oxidase catalyzes the ...
 484-566 3.57e-12

The third cupredoxin domain of plant Ascorbate oxidase; Ascorbate oxidase catalyzes the oxidation of ascorbic acid to dehydroascorbic acid. This multicopper oxidase (MCO) is found in cucurbitaceous plants such as pumpkin, cucumber, and melon. It can detect levels of ascorbic acid and eliminate it. The biological function of ascorbate oxidase is still not clear. Ascorbate oxidase belongs to MCO family which couple oxidation of substrates with reduction of dioxygen to water. MCOs are capable of oxidizing a vast range of substrates, varying from aromatic compounds to inorganic compounds such as metals. Although the members of this family have diverse functions, majority of them have three cupredoxin domain repeats. The copper ions are bound in several sites: Type 1, Type 2, and/or Type 3. The ensemble of types 2 and 3 copper is called a trinuclear cluster. MCOs oxidize their substrate by accepting electrons at a mononuclear copper center and transferring them to the active site trinuclear copper center. The cupredoxin domain 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.


Pssm-ID: 259960 [Multi-domain]  Cd Length: 155  Bit Score: 64.36  E-value: 3.57e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 367021116 484 HPMHLHGHNFYVLHEGPGEWDGTiVRPS-----NPRRRDVYSVRSKGHLVIQFDG-APGVWPFHCHIAWHVsggFMATLI 557
Cdd:cd13893   67 HPWHLHGHDFWVLGYGLGGFDPA-ADPSslnlvNPPMRNTVTIFPYGWTALRFKAdNPGVWAFHCHIEWHF---HMGMGV 142


                 ....*....
gi 367021116 558 VKPDEVERM 566
Cdd:cd13893  143 VFAEGVERV 151
CuRO_1_McoC_like cd13855
The first cupredoxin domain of a multicopper oxidase McoC and similar proteins; This family ...
 105-200 6.07e-12

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.


Pssm-ID: 259924 [Multi-domain]  Cd Length: 121  Bit Score: 62.88  E-value: 6.07e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 367021116 105 NGAFPGPLVEANWGDTIVVDVHNDITgpeEGTAIHWHGFlqHGTPWEDGVPgitQCPIPP--RRSYRYEFVASLYGTSWY 182
Cdd:cd13855   27 NGSVPGPLIEVFEGDTVEITFRNRLP---EPTTVHWHGL--PVPPDQDGNP---HDPVAPgnDRVYRFTLPQDSAGTYWY 98

                         90       100
                 ....*....|....*....|..
gi 367021116 183 HSH----YSAQFAGGLFGPIVI 200
Cdd:cd13855   99 HPHphghTAEQVYRGLAGAFVV 120
CuRO_1_2DMCO_NIR_like cd11024
The cupredoxin domain 1 of a two-domain laccase related to nitrite reductase; The two-domain ...
 80-200 7.77e-12

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.


Pssm-ID: 259910 [Multi-domain]  Cd Length: 119  Bit Score: 62.29  E-value: 7.77e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 367021116  80 TRHYDFTV--SRASIAPdGYLRDVLLVNGAFPGPLVEANWGDTIVVDVHNdiTGPEEGTaIHWHGFlqHgTPWEDGVPGI 157
Cdd:cd11024    1 VREFTLVAedAEIEIAP-GVVFKAWTYNGTVPGPTLRATEGDLVRIHFIN--TGDHPHT-IHFHGI--H-DAAMDGTGLG 73

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*.
gi 367021116 158 tqcPIPPRRSYRYEFVASLYGTSWYHSHY---SAQFAGGLFGPIVI 200
Cdd:cd11024   74 ---PIMPGESFTYEFVAEPAGTHLYHCHVqplKEHIAMGLYGAFIV 116
CuRO_3_McoC_like cd13902
The third cupredoxin domain of a multicopper oxidase McoC and similar proteins; This family ...
 475-558 1.18e-11

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.


Pssm-ID: 259969 [Multi-domain]  Cd Length: 125  Bit Score: 62.03  E-value: 1.18e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 367021116 475 IVNNRSPSAHPMHLHGHNFYVLhegpgEWDGTIVRPSNPRRRDVYSV--RSKGHLVIQFDgAPGVWPFHCHIAWHVSGGF 552
Cdd:cd13902   46 EVTNTSHMDHPFHLHGTQFQVL-----EIDGNPQKPEYRAWKDTVNLppGEAVRIATRQD-DPGMWMYHCHILEHEDAGM 119


                 ....*.
gi 367021116 553 MATLIV 558
Cdd:cd13902  120 MGMLHV 125
CuRO_2_CopA_like_1 cd13870
The second cupredoxin domain of CopA copper resistance protein like family; The members of ...
 276-341 1.45e-11

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.


Pssm-ID: 259938 [Multi-domain]  Cd Length: 117  Bit Score: 61.58  E-value: 1.45e-11
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 367021116 276 FRFQTGKTHRLRLINGGADGVQRFSIDEHTLTVIAEDFVPVKPYNTSVVTLGVGQRADVLVTANVG 341
Cdd:cd13870   31 FTARPGDRLRLRLINAAGDTAFRVALAGHRLTVTHTDGFPVEPVEVDALLIGMGERYDAIVTANNG 96
CuRO_1_CueO_FtsP cd04232
The first Cupredoxin domain of the multicopper oxidase CueO, the cell division protein FtsP, ...
 81-200 1.85e-11

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.


Pssm-ID: 259894 [Multi-domain]  Cd Length: 120  Bit Score: 61.44  E-value: 1.85e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 367021116  81 RHYDFTVSRASIAP-DGYLRDVLLVNGAFPGPLVEANWGDTIVVDVHNDITgpeEGTAIHWHGFLQHGTpwEDGVPgitQ 159
Cdd:cd04232    1 KPFTLTAQKGETEFlPGKKTATWGYNGSYLGPTIRVKKGDTVRINVTNNLD---EETTVHWHGLHVPGE--MDGGP---H 72

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*.
gi 367021116 160 CPIPPRRSYRYEF-VASLYGTSWYHSHYSA----QFAGGLFGPIVI 200
Cdd:cd04232   73 QPIAPGQTWSPTFtIDQPAATLWYHPHTHGktaeQVYRGLAGLFII 118
CuRO_1_Tth-MCO_like cd13853
The first cupredoxin domain of the bacterial laccases similar to Tth-MCO from Thermus ...
 84-200 9.81e-11

The first 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 1 of 3-domain MCOs contains part the trinuclear copper binding site, which is located at the interface of domains 1 and 3.


Pssm-ID: 259922 [Multi-domain]  Cd Length: 139  Bit Score: 59.96  E-value: 9.81e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 367021116  84 DFTVSRASIAPDGYLrdVLLVNGAFPGPLVEANWGDTIVVDVHNDITGPE--------------EGTAIHWHGFlqHGTP 149
Cdd:cd13853    7 TVEYGRVTLAGLPVT--LRTYNGSIPGPTLRVRPGDTLRITLKNDLPPEGaaneapapntphcpNTTNLHFHGL--HVSP 82

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 367021116 150 wedgvpgitQCP-------IPPRRSYRYEF---VASLYGTSWYHSHY----SAQFAGGLFGPIVI 200
Cdd:cd13853   83 ---------TGNsdnvfltIAPGESFTYEYdipADHPPGTYWYHPHLhgstALQVAGGMAGALVV 138
CuRO_3_MCO_like_2 cd13908
The third cupredoxin domain of uncharacterized multicopper oxidase; Multicopper Oxidases (MCOs) ...
 430-556 1.15e-10

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.


Pssm-ID: 259975 [Multi-domain]  Cd Length: 122  Bit Score: 59.39  E-value: 1.15e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 367021116 430 LWKFNGVSMRADYNSPVLllandgnftyppqwnvvnqHNHTAIRIIVNNRSPSAHPMHLHGHNFYVLhegpgEWDGTivr 509
Cdd:cd13908   20 LWTINGKSYPDEDPPLVV-------------------QQGRRYRLVFRNASDDAHPMHLHRHTFEVT-----RIDGK--- 72

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*...
gi 367021116 510 PSNPRRRDVYSVRSKGHLVIQFDG-APGVWPFHCHIAWHVSGGFMATL 556
Cdd:cd13908   73 PTSGLRKDVVMLGGYQRVEVDFVAdNPGLTLFHCHQQLHMDYGFMALF 120
CuRO_3_CumA_like cd13906
The third cupredoxin domain of CumA like multicopper oxidase; This multicopper oxidase (MCO) ...
 478-559 1.31e-10

The third 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 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.


Pssm-ID: 259973 [Multi-domain]  Cd Length: 138  Bit Score: 59.70  E-value: 1.31e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 367021116 478 NRSPSAHPMHLHGHNFYVLhegpgEWDGTIVRPsnPRRRDVYSVRSKGHLVIQFDG-APGVWPFHCHIAWHVSGGFMATL 556
Cdd:cd13906   63 NETAFLHPMHLHGHFFRVL-----SRNGRPVPE--PFWRDTVLLGPKETVDIAFVAdNPGDWMFHCHILEHQETGMMGVI 135


                 ...
gi 367021116 557 IVK 559
Cdd:cd13906  136 RVA 138
CuRO_2_MCO_like_2 cd13887
The second cupredoxin domain of uncharacterized multicopper oxidase; Multicopper Oxidases ...
 277-337 2.80e-10

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.


Pssm-ID: 259954 [Multi-domain]  Cd Length: 114  Bit Score: 57.72  E-value: 2.80e-10
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 367021116 277 RFQTGKTHRLRLINGGADGVQRFSIDEHTLTVIAEDFVPVKPYNTSVVTLGVGQRADVLVT 337
Cdd:cd13887   27 RVEPGGRVRLRVINGSTATNFHIDLGDLKGTLIAVDGNPVQPVEGRRFPLATAQRLDLLVT 87
CuRO_1_McoP_like cd13852
The first cupredoxin domain of multicopper oxidase McoP and similar proteins; This family ...
 94-201 5.05e-10

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.


Pssm-ID: 259921 [Multi-domain]  Cd Length: 114  Bit Score: 57.30  E-value: 5.05e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 367021116  94 PDGYLrdvllvngafpGPLVEANWGDTIVVDVHNDITgpeEGTAIHWHGFlqHgTPWE-DGVPGITqcpIPPRRSYRYEF 172
Cdd:cd13852   19 PDSYL-----------GPILRLRKGQKVRITFKNNLP---EPTIIHWHGL--H-VPAAmDGHPRYA---IDPGETYVYEF 78

                         90       100       110
                 ....*....|....*....|....*....|....
gi 367021116 173 -VASLYGTSWYHSH----YSAQFAGGLFGPIVIH 201
Cdd:cd13852   79 eVLNRAGTYWYHPHphglTAKQVYRGLAGLFLVT 112
PRK10965 PRK10965
multicopper oxidase; Provisional
 104-343 8.18e-09

multicopper oxidase; Provisional


Pssm-ID: 236810 [Multi-domain]  Cd Length: 523  Bit Score: 58.11  E-value: 8.18e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 367021116 104 VNGAFPGPLVEANWGDTIVVDVHNDItgPEEgTAIHWHGFLQHGTpwEDGVPgitQCPIPPRRSYRYEF-VASLYGTSWY 182
Cdd:PRK10965  70 YNGNLLGPAVRLQRGKAVTVDITNQL--PEE-TTLHWHGLEVPGE--VDGGP---QGIIAPGGKRTVTFtVDQPAATCWF 141

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 367021116 183 HSHY----SAQFAGGLFGPIVIH-GPTR-----ENYDIDLGPILLTDwyhreyfdiieemlapggsaKVVSDNNLIDGKM 252
Cdd:PRK10965 142 HPHQhgktGRQVAMGLAGLVLIEdDESLklglpKQWGVDDIPVILQD--------------------KRFSADGQIDYQL 201

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 367021116 253 hfDCSTVAPG--DNTPCFDNAGVSKFRFQTGKThRLRLING-GADGVQRFSIDEHTLTVIAED--FVPvKPYNTSVVTLG 327
Cdd:PRK10965 202 --DVMTAAVGwfGDTLLTNGAIYPQHAAPRGWL-RLRLLNGcNARSLNLATSDGRPLYVIASDggLLA-EPVKVSELPIL 277

                        250
                 ....*....|....*.
gi 367021116 328 VGQRADVLVTANVGEP 343
Cdd:PRK10965 278 MGERFEVLVDTSDGKA 293
CuRO_3_MCO_like_3 cd13909
The third cupredoxin domain of uncharacterized multicopper oxidase; Multicopper Oxidases (MCOs) ...
 430-553 2.04e-08

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.


Pssm-ID: 259976 [Multi-domain]  Cd Length: 137  Bit Score: 53.29  E-value: 2.04e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 367021116 430 LWKFNGVSMRADynSPvLLLANDGNftyppqwnvvnqhnhtAIRIIVNNRSPSAHPMHLHGHNFYVL--HEGPGEWDGTI 507
Cdd:cd13909   36 FWAFNGVAGRPD--DP-LLEARRGE----------------TVRIEMVNNTGFPHGMHLHGHHFRAIlpNGALGPWRDTL 96

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*..
gi 367021116 508 VRPSNPRRRdvysvrskghlvIQF-DGAPGVWPFHCHIAWHVSGGFM 553
Cdd:cd13909   97 LMDRGETRE------------IAFvADNPGDWLLHCHMLEHAAAGMM 131
CuRO_2_AAO_like_2 cd13873
The second cupredoxin domain of plant Ascorbate oxidase homologs; This family includes plant ...
 214-350 1.29e-07

The second cupredoxin domain of plant Ascorbate oxidase homologs; This family includes plant laccases similar to ascorbate oxidase. Ascorbate oxidase catalyzes the oxidation of ascorbic acid to dehydroascorbic acid. It can detect levels of ascorbic acid and eliminate it. The biological function of ascorbate oxidase is still not clear. Ascorbate oxidase belongs to multicopper oxidase (MCO) family which couples oxidation of substrates with reduction of dioxygen to water. Although MCOs have diverse functions, majority of them have three cupredoxin domain repeats that include one mononuclear and one trinuclear copper center. The copper ions are bound in several sites: Type 1, Type 2, and/or Type 3. The ensemble of types 2 and 3 copper is called a trinuclear cluster. MCOs oxidize their substrate by accepting electrons at a mononuclear copper center and transferring them to the active site trinuclear copper center. The cupredoxin domain 2 of 3-domain MCOs has lost the ability to bind copper.


Pssm-ID: 259941 [Multi-domain]  Cd Length: 161  Bit Score: 51.52  E-value: 1.29e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 367021116 214 PILLTDWYHREYFDIIEEMLA-----PGGSAKVvsdnnLIDGKMHFDCSTVAPGDntpCFDNAGVSKFRFQTGKTHRLRL 288
Cdd:cd13873    4 ILLFSDYFPKTDSTIETGLTAtpfvwPGEPNAL-----LVNGKSGGTCNKSATEG---CTTSCHPPVIDVEPGKTYRFRF 75

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 367021116 289 INGGADGVQRFSIDEH-TLTVIAEDFVPVKPYNTSVVTLGVGQRADVLVTANVGEPT-----SAFWMR 350
Cdd:cd13873   76 IGATALSFVSLGIEGHdNLTIIEADGSYTKPAETDHLQLGSGQRYSFLLKTKSLEELaalnkTTFWIQ 143
CuRO_2_McoC_like cd13881
The second cupredoxin domain of a multicopper oxidase McoC and similar proteins; This family ...
 279-388 2.04e-07

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.


Pssm-ID: 259948 [Multi-domain]  Cd Length: 142  Bit Score: 50.30  E-value: 2.04e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 367021116 279 QTGKTHRLRLINGGADGVQRFSIDEHTLTVIAEDFVPV-KPYNTSVVTLGVGQRADVLVTAnvGEPTSafwmrsnlsscl 357
Cdd:cd13881   47 RPGEVQRWRIVNAASARYFRLALDGHKFRLIGTDGGLLeAPREVDELLLAPGERAEVLVTA--GEPGG------------ 112

                         90       100       110
                 ....*....|....*....|....*....|.
gi 367021116 358 parqPYAVAAVYYDQADTSTTPSSRAWDVLD 388
Cdd:cd13881  113 ----RLVLLALPYDRGHMGGMEPRPPLTLAT 139
CuRO_2_Abr2_like cd13876
The second cupredoxin domain of a group of fungal Laccases similar to Abr2 from Aspergillus ...
 214-336 3.78e-07

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.


Pssm-ID: 259944 [Multi-domain]  Cd Length: 138  Bit Score: 49.51  E-value: 3.78e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 367021116 214 PILLTDWYHREYFDIIEEMLAPGGSAkVVSDNNLIDGKMHFDCSTVAPGDNTpcfdnagvskfRFQTgkthrLRLINGGA 293
Cdd:cd13876    2 PIILSDWRHLTSEEYWKIMRASGIEP-FCYDSILINGKGRVYCLIVIVDPGE-----------RWVS-----LNFINAGG 64

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|...
gi 367021116 294 DGVQRFSIDEHTLTVIAEDFVPVKPYNTSVVTLGVGQRADVLV 336
Cdd:cd13876   65 FHTLAFSIDEHPMWVYAVDGGYIEPQLVDAISITNGERYSVLV 107
CuRO_3_PHS cd13892
The third Cupredoxin domain of phenoxazinone synthase (PHS); Phenoxazinone synthase (PHS, ...
 476-560 1.61e-06

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.


Pssm-ID: 259959 [Multi-domain]  Cd Length: 184  Bit Score: 48.68  E-value: 1.61e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 367021116 476 VNNRSPSAHPMHLHGHNFYVLHEGPGEWDG--TIVRPSNPRRR---------------DVYSVRSkGHLV---IQFDGAP 535
Cdd:cd13892   79 VNLGEGHPHPMHIHLAEFQVLERQPYDVTGfdTTVGGTDRPITpgeaaplepvelgwkDTVVVGP-GELVtvlVQFDGAT 157

                         90       100
                 ....*....|....*....|....*
gi 367021116 536 GVWPFHCHIAWHVSGGFMATLIVKP 560
Cdd:cd13892  158 GRFMYHCHILEHEDHDMMRPFVVQP 182
CuRO_3_Tth-MCO_like cd13900
The third cupredoxin domain of the bacterial laccases similar to Tth-MCO from Thermus ...
 478-556 2.22e-06

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.


Pssm-ID: 259967 [Multi-domain]  Cd Length: 123  Bit Score: 46.85  E-value: 2.22e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 367021116 478 NRSPSAHPMHLHGHNFYVLHEGPGEWDGTIVRpsnprrrDVYSVRSKGHLVI--QFDGAPGVWPFHCHIAWHVSGGFMAT 555
Cdd:cd13900   48 NTSGEDHPFHIHVNPFQVVSINGKPGLPPVWR-------DTVNVPAGGSVTIrtRFRDFTGEFVLHCHILDHEDQGMMQV 120


                 .
gi 367021116 556 L 556
Cdd:cd13900  121 V 121
CuRO_3_CotA_like cd13891
The third Cupredoxin domain of bacterial laccases including CotA, a bacterial endospore coat ...
 475-547 4.29e-06

The third 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 is required for spore resistance against hydrogen peroxide and UV light. CotA belongs to 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.


Pssm-ID: 259958 [Multi-domain]  Cd Length: 143  Bit Score: 46.52  E-value: 4.29e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 367021116 475 IVNNrSPSAHPMHLHGHNFYVLHEGP---GEW--DGTIVRPSNPRRRDVY------SVRSK-GH---LVIQFDGAPGVWP 539
Cdd:cd13891   46 IINL-TPDAHPIHLHLVQFQVLDRQPfdvDEYnaTGEIYYTGPPRPPAPNergwkdTVRAYpGEvtrIIVRFDGPEGGYV 124


                 ....*...
gi 367021116 540 FHCHIAWH 547
Cdd:cd13891  125 WHCHILEH 132
CuRO_3_MCO_like_5 cd13911
The third cupredoxin domain of uncharacterized multicopper oxidase; Multicopper Oxidases (MCOs) ...
 479-555 6.49e-06

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.


Pssm-ID: 259978 [Multi-domain]  Cd Length: 119  Bit Score: 45.61  E-value: 6.49e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 367021116 479 RSPSAHPMHLHGHNFYVLHE---GPGEWDGTIvrpsnprrRDVYSVRSKG--HLVIQFDGAPGVWPFHCHIAWHVSGGFM 553
Cdd:cd13911   44 SSDGRHPVHLHGAHFQVVSRtggRPGEWDAGW--------KDTVLLRPREsvTVIIRFDGYRGRYVFHCHNLEHEDMGMM 115


                 ..
gi 367021116 554 AT 555
Cdd:cd13911  116 AN 117
CuRO_1_2DMCO_NIR_like cd11024
The cupredoxin domain 1 of a two-domain laccase related to nitrite reductase; The two-domain ...
 472-561 9.71e-06

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.


Pssm-ID: 259910 [Multi-domain]  Cd Length: 119  Bit Score: 44.95  E-value: 9.71e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 367021116 472 IRIIVNNRSPSAHPMHLHGHNfyvlhegPGEWDGTIVRPSNPRRRDVYsvrskghlviQFDGAP-GVWPFHCHI---AWH 547
Cdd:cd11024   43 VRIHFINTGDHPHTIHFHGIH-------DAAMDGTGLGPIMPGESFTY----------EFVAEPaGTHLYHCHVqplKEH 105

                         90
                 ....*....|....
gi 367021116 548 VSGGFMATLIVKPD 561
Cdd:cd11024  106 IAMGLYGAFIVDPK 119
CuRO_3_McoP_like cd13888
The third cupredoxin domain of multicopper oxidase McoP and similar proteins; This subfamily ...
 475-559 2.69e-05

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.


Pssm-ID: 259955 [Multi-domain]  Cd Length: 139  Bit Score: 44.09  E-value: 2.69e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 367021116 475 IVNNRSPSAHPMHLHGHNFYVLH--EGPGEWDGTIVRPSNPRRRDV-----------YSVRskghLVIQFDGA-PG--VW 538
Cdd:cd13888   43 LVNDAASMPHPMHIHGFQFQVLErsDSPPQVAELAVAPSGRTATDLgwkdtvlvwpgETVR----IAVDFTHDyPGdqLY 118

                         90       100
                 ....*....|....*....|.
gi 367021116 539 PFHCHIAWHVSGGFMATLIVK 559
Cdd:cd13888  119 LLHCHNLEHEDDGMMVNVRVP 139
CuRO_2_CumA_like cd13885
The second cupredoxin domain of CumA like multicopper oxidase; This multicopper oxidase (MCO) ...
 276-338 4.29e-05

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.


Pssm-ID: 259952 [Multi-domain]  Cd Length: 132  Bit Score: 43.47  E-value: 4.29e-05
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 367021116 276 FRFQTGKTHRLRLINGGADGVQRFSIDEHTLTVIAEDFVPVKPYNTS--VVTLGVGQRADVLVTA 338
Cdd:cd13885   48 FTVRAGERVRLRLINAANARVFALKFPGHEARVIALDGQPAEPFVARngAVVLAPGMRIDLVIDA 112
CuRO_2_AAO_like_1 cd13872
The second cupredoxin domain of plant pollen multicopper oxidase homologous to ascorbate ...
 215-339 7.12e-05

The second cupredoxin domain of plant pollen multicopper oxidase homologous to ascorbate oxidase; The proteins in this subfamily are expressed in plant pollen. They share homology to ascorbate oxidase and other members of the blue copper oxidase family. The expression of the protein is detected during germination and pollen tube growth. Ascorbate oxidase catalyzes the oxidation of ascorbic acid to dehydroascorbic acid. It is a member of the multicopper oxidase (MCO) family that couples oxidation of substrates with reduction of dioxygen to water. Although MCOs have diverse functions, majority of them have three cupredoxin domain repeats that include one mononuclear and one trinuclear copper center. The copper ions are bound in several sites: Type 1, Type 2, and/or Type 3. The ensemble of types 2 and 3 copper is called a trinuclear cluster. MCOs oxidize their substrate by accepting electrons at a mononuclear copper center and transferring them to the active site trinuclear copper center. The cupredoxin domain 2 of 3-domain MCOs has lost the ability to bind copper.


Pssm-ID: 259940 [Multi-domain]  Cd Length: 141  Bit Score: 43.16  E-value: 7.12e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 367021116 215 ILLTDWYHREYFDIIEEMlaPGGSAKVVSDNNLIDGKmhfdcstvapgdnTPCFDNAGVSKFRFQTGKTHRLRLINGGAD 294
Cdd:cd13872    5 VLIGDWYKTDHKTLRQSL--DKGRTLGRPDGILINGK-------------GPYGYGANETSFTVEPGKTYRLRISNVGLR 69

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*.
gi 367021116 295 GVQRFSIDEHTLTVI-AEDFVPVKPYNTSvVTLGVGQRADVLVTAN 339
Cdd:cd13872   70 TSLNFRIQGHKMLLVeTEGSYTAQNTYDS-LDVHVGQSYSVLVTAD 114
CuRO_3_CueO_FtsP cd13890
The third Cupredoxin domain of the multicopper oxidase CueO, the cell division protein FtsP, ...
 475-558 7.33e-05

The third Cupredoxin domain of the multicopper oxidase CueO, the cell division protein FtsP, and similar proteins; CueO is a multicopper oxidase (MCO) that is part of the copper-regulatory cue operon, which employs a cytosolic metalloregulatory protein CueR that induces expression of CopA and CueO under copper stress conditions. CueO is a periplasmic multicopper oxidase that is stimulated by exogenous copper(II). FtsP (also named SufI) is a component of the cell division apparatus. It is involved in protecting or stabilizing the assembly of divisomes under stress conditions. FtsP belongs to the multicopper oxidase superfamily but lacks metal cofactors. The protein is localized at septal rings and may serve as a scaffolding function. Members of this subfamily contain three cupredoxin domains and this model represents the first domain. Although MCOs have diverse functions, majority of them have three cupredoxin domain repeats that include one mononuclear and one trinuclear copper center. The copper ions are bound in several sites: Type 1, Type 2, and/or Type 3. The ensemble of types 2 and 3 copper is called a trinuclear cluster. MCOs oxidize their substrate by accepting electrons at a mononuclear copper center and transferring them to the active site trinuclear copper center. The cupredoxin domain 3 of 3-domain MCOs contains the Type 1 (T1) copper binding site and part the trinuclear copper binding site, which is located at the interface of domains 1 and 3. FtsP does not contain any copper binding sites.


Pssm-ID: 259957 [Multi-domain]  Cd Length: 124  Bit Score: 42.62  E-value: 7.33e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 367021116 475 IVNNRSPSAHPMHLHGHNFYVLHEgpgewDGTIVRPSNPRRRDVYSVRSKG--HLVIQFDGAP---GVWPFHCHIAWHVS 549
Cdd:cd13890   41 EVTNTDGMPHPFHIHGVQFRILSR-----NGQPPPPNEAGWKDTVWVPPGEtvRILVKFDHYAdptGPFMYHCHILEHED 115


                 ....*....
gi 367021116 550 GGFMATLIV 558
Cdd:cd13890  116 NGMMGQFVV 124
CuRO_1_CuNIR_like cd04201
Cupredoxin domain 1 of Copper-containing nitrite reductase and two-domain laccase; ...
 92-200 9.19e-05

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.


Pssm-ID: 259864 [Multi-domain]  Cd Length: 120  Bit Score: 42.09  E-value: 9.19e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 367021116  92 IAPDGYLRdVLLVNGAFPGPLVEANWGDTivVDVHndITGPEEGTAIHWHGFlqHGTPWEDGVPGITQcpIPPRRSYRYE 171
Cdd:cd04201   15 LDDGVEYR-YWTFDGDIPGPMLRVREGDT--VELH--FSNNPSSTMPHNIDF--HAATGAGGGAGATF--IAPGETSTFS 85

                         90       100       110
                 ....*....|....*....|....*....|..
gi 367021116 172 FVASLYGTSWYHSHYSA---QFAGGLFGPIVI 200
Cdd:cd04201   86 FKATQPGLYVYHCAVAPvpmHIANGMYGLILV 117
CuRO_3_MCO_like_1 cd13907
The third cupredoxin domain of uncharacterized multicopper oxidase; Multicopper Oxidases (MCOs) ...
 460-559 1.20e-04

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.


Pssm-ID: 259974 [Multi-domain]  Cd Length: 154  Bit Score: 42.85  E-value: 1.20e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 367021116 460 QWNVVNQHN--------HTAIRIIVNNRSPSAHPMHLHGHNFYVLHegpgewdgtivRPSNPRRRDVYSVRSKGH----- 526
Cdd:cd13907   40 VWEIINDLGgmgggggmMGGGGMMMGGMMAMPHPIHLHGVQFQVLE-----------RSVGPKDRAYWATVKDGFidegw 108

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*.
gi 367021116 527 -------------LVIQFDGAPGVWPFHCHIAWHVSGGFMATLIVK 559
Cdd:cd13907  109 kdtvlvmpgervrIIKPFDDYKGLFLYHCHNLEHEDMGMMRNFLVE 154
CuRO_2_CopA cd13874
The second cupredoxin domain of CopA copper resistance protein family; CopA is a multicopper ...
 278-337 1.88e-04

The second cupredoxin domain of CopA copper resistance protein family; CopA is a multicopper oxidase (MCO) related to laccase and L-ascorbate oxidase, both copper-containing enzymes. It is part of the copper-regulatory cue operon, which employs a cytosolic metalloregulatory protein CueR that induces expression of CopA and CueO under copper stress conditions. CopA is a copper efflux P-type ATPase that is located in the inner cell membrane and is is involved in copper resistance in bacteria. CopA mutant causes a loss of function including copper tolerance and oxidase activity and copA transcription is inducible in the presence of copper. Although MCOs have diverse functions, majority of them have three cupredoxin domain repeats that include one mononuclear and one trinuclear copper center. The copper ions are bound in several sites: Type 1, Type 2, and/or Type 3. The ensemble of types 2 and 3 copper is called a trinuclear cluster. MCOs oxidize their substrate by accepting electrons at a mononuclear copper center and transferring them to the active site trinuclear copper center. The cupredoxin domain 2 of 3-domain MCOs has lost the ability to bind copper.


Pssm-ID: 259942 [Multi-domain]  Cd Length: 112  Bit Score: 41.13  E-value: 1.88e-04
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 367021116 278 FQTGKTHRLRLINGGADGVQRFSIDEHTLTVIAEDFVPVKPYNTSVVTLGVGQRADVLVT 337
Cdd:cd13874   29 FKPGERVRLRFINAAASTYFDVRIPGGKMTVVAADGQDVRPVEVDEFRIGVAETYDVIVT 88
CuRO_1_Ceruloplasmin_like_1 cd04229
cupredoxin domain of ceruloplasmin homologs; Uncharacterized subfamily of ceruloplasmin ...
 110-200 4.55e-04

cupredoxin domain of ceruloplasmin homologs; Uncharacterized subfamily of ceruloplasmin homologous proteins. Ceruloplasmin (ferroxidase) is a multicopper oxidase essential for normal iron homeostasis. Ceruloplasmin also functions in copper transport, amine oxidase and as an antioxidant preventing free radicals in serum. The protein has 6 cupredoxin domains and exhibits internal sequence homology that appears to have evolved from the triplication of a sequence unit composed of two tandem cupredoxin domains. This model represents the first domain of the triplicated units.


Pssm-ID: 259891 [Multi-domain]  Cd Length: 175  Bit Score: 41.25  E-value: 4.55e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 367021116 110 GPLVEANWGDTIVVDVHNDITGPEegTAIHWHGflqhGTPWEDGVPGITQC--PIPP--RRSYRY-----------EFVA 174
Cdd:cd04229   73 GPVIRAEVGDTIKVVFKNNLDEFP--VNMHPHG----GLYSKDNEGTTDGAgdVVAPgeTYTYRWivpedagpgpgDPSS 146

                         90       100
                 ....*....|....*....|....*...
gi 367021116 175 SLYgtsWYHSHYSAQFA--GGLFGPIVI 200
Cdd:cd04229  147 RLW---LYHSHVDVFAHtnAGLVGPIIV 171
CuRO_3_BOD cd13889
The third cupredoxin domain of Bilirubin oxidase (BOD); Bilirubin oxidase (BOD) catalyzes the ...
 466-543 1.05e-03

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.


Pssm-ID: 259956 [Multi-domain]  Cd Length: 124  Bit Score: 39.22  E-value: 1.05e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 367021116 466 QHNHTAIRIIVNNRSPSAHPMHLHGHNFYVLhegpgEWDGTI--VRPSNPRRRDVYSVRSKGHLVI--QFDGAPGVWPFH 541
Cdd:cd13889   33 QLGTVEIWTLINGGGGWSHPIHIHLEDFQIL-----SRNGGSraVPPYERGRKDVVYLGPGEEVRVlmRFRPFRGKYMMH 107


                 ..
gi 367021116 542 CH 543
Cdd:cd13889  108 CH 109
CuRO_2_CueO_FtsP cd13867
The second Cupredoxin domain of the multicopper oxidase CueO, the cell division protein FtsP, ...
 285-345 1.59e-03

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.


Pssm-ID: 259935 [Multi-domain]  Cd Length: 146  Bit Score: 39.10  E-value: 1.59e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 367021116 285 RLRLINGGadgVQR-----FSiDEHTLTVIAED--FVPvKPYNTSVVTLGVGQRADVLVTANVGEPTS 345
Cdd:cd13867   52 RLRLLNGS---NARtynlgFS-DNRPFYQIASDggLLP-APVELKRLLLAPGERAEILVDFSDGEPVS 114
CuRO_1_ceruloplasmin cd04222
The first cupredoxin domain of Ceruloplasmin; Ceruloplasmin is a multicopper oxidase essential ...
 108-200 1.81e-03

The first cupredoxin domain of Ceruloplasmin; Ceruloplasmin is a multicopper oxidase essential for normal iron homeostasis and copper transport in blood. It also functions in amine oxidation and as an antioxidant preventing free radicals in serum. The protein has 6 cupredoxin domains with six copper centers; three mononuclear sites in domain 2, 4 and 6 and three in the form of trinuclear clusters at the interface of domains 1 and 6. Ceruloplasmin exhibits internal sequence homology that appears to have evolved from the triplication of a sequence unit composed of two tandem cupredoxin domains. This model represents the first cupredoxin domain of ceruloplasmin.


Pssm-ID: 259884 [Multi-domain]  Cd Length: 183  Bit Score: 39.71  E-value: 1.81e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 367021116 108 FPGPLVEANWGDTIVVDVHNDITGPeegTAIHWHGFL----QHGTPWEDGVPGITQC--PIPPRRSYRYEF-VASLYG-- 178
Cdd:cd04222   73 FLGPILKAEVGDVIVVHLKNFASRP---YSLHPHGVFynkeNEGALYPDNTSGFEKAddAVPPGGSYTYTWtVPEEQApt 149

                         90       100       110
                 ....*....|....*....|....*....|.
gi 367021116 179 -------TSWYHSHYSA--QFAGGLFGPIVI 200
Cdd:cd04222  150 kadanclTRIYHSHIDApkDIASGLIGPLII 180
CuRO_2_ceruloplasmin_like_2 cd11023
cupredoxin domain of ceruloplasmin homologs; Uncharacterized subfamily of ceruloplasmin ...
 502-558 5.08e-03

cupredoxin domain of ceruloplasmin homologs; Uncharacterized subfamily of ceruloplasmin homologous proteins. Ceruloplasmin (ferroxidase) is a multicopper oxidase essential for normal iron homeostasis. Ceruloplasmin also functions in copper transport, amine oxidase and as an antioxidant preventing free radicals in serum. The protein has 6 cupredoxin domains and exhibits internal sequence homology that appears to have evolved from the triplication of a sequence unit composed of two tandem cupredoxin domains. This model represents the first domain of the triplicated units.


Pssm-ID: 259909 [Multi-domain]  Cd Length: 118  Bit Score: 37.20  E-value: 5.08e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 367021116 502 EWDGTIVRPSNPRRRDVYSVRSKGHLVIQFDGA-PGVWPFHCHIAWHVSGGFMATLIV 558
Cdd:cd11023   61 HWHGQTVEADKSRRTDVAELMPASMRVADMTAAdVGTWLLHCHVHDHYMAGMMTQFAV 118
CuRO_6_ceruloplasmin cd11012
The sixth cupredoxin domain of Ceruloplasmin; Ceruloplasmin is a multicopper oxidase essential ...
 484-558 6.93e-03

The sixth cupredoxin domain of Ceruloplasmin; Ceruloplasmin is a multicopper oxidase essential for normal iron homeostasis and copper transport in blood. It also functions in amine oxidation and as an antioxidant preventing free radicals in serum. The protein has 6 cupredoxin domains with six copper centers; three mononuclear sites in domain 2, 4 and 6 and three in the form of trinuclear clusters at the interface of domains 1 and 6. Ceruloplasmin exhibits internal sequence homology that appears to have evolved from the triplication of a sequence unit composed of two tandem cupredoxin domains. This model represents the sixth cupredoxin domain of ceruloplasmin.


Pssm-ID: 259898 [Multi-domain]  Cd Length: 145  Bit Score: 37.54  E-value: 6.93e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 367021116 484 HPMHLHGHNFYVLHEGPgewdgtivrpsnpRRRDVYS-VRSKGHLVIQFDGAPGVWPFHCHIAWHVSGGFMATLIV 558
Cdd:cd11012   82 HTAHFHGHSFDYKHRGV-------------YRSDVFDlFPGTFQTVEMIPRTPGTWLLHCHVTDHIHAGMETTYTV 144
Cupredoxin cd00920
Cupredoxin superfamily; Cupredoxins contain type I copper centers and are involved in ...
 472-557 8.08e-03

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.


Pssm-ID: 259860 [Multi-domain]  Cd Length: 110  Bit Score: 36.44  E-value: 8.08e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 367021116 472 IRIIVNNRSPSAHPMHLHGHNfyvlheGPGEWDGTIVRPSNPRRRDVYSVRSkGHLVIQFDgAPGVWPFHCHIAWHVSGG 551
Cdd:cd00920   33 VRVQFVNKLGENHSVTIAGFG------VPVVAMAGGANPGLVNTLVIGPGES-AEVTFTTD-QAGVYWFYCTIPGHNHAG 104


                 ....*.
gi 367021116 552 FMATLI 557
Cdd:cd00920  105 MVGTIN 110
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
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