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Conserved domains on  [gi|1063710373|ref|NP_001326525|]
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laccase 7 [Arabidopsis thaliana]

Protein Classification

laccase family protein( domain architecture ID 1003049)

laccase acts as a multicopper oxidase that oxidizes a variety of phenolic substrates, performing one-electron oxidations, leading to crosslinking

Gene Ontology:  GO:0005507
PubMed:  21063888

Graphical summary

 Zoom to residue level

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List of domain hits

 Name Accession Description Interval E-value
laccase super family cl37260
laccase, plant; Members of this protein family include the copper-containing enzyme laccase ...
 2-453 0e+00

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.


The actual alignment was detected with superfamily member TIGR03389:

Pssm-ID: 274556 [Multi-domain]  Cd Length: 539  Bit Score: 603.27  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063710373   2 ITQCPIQPGQRYAYRFNITGQEGTLWWHAHASFLRATVYGALVIRPKSGHSYPFPKPHKEVPILFGEWWNTDVVALEEAA 81
Cdd:TIGR03389  77 ITQCPIQPGQSYVYNFTITGQRGTLWWHAHISWLRATVYGAIVILPKPGVPYPFPKPDREVPIILGEWWNADVEAVINQA 156

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063710373  82 IATGVPPNNSDAYTINGRPGNLYPCSKDRMFSLNVVKGKRYLLRIINAAMNIQLFFKIANHRLTVVAADAVYTAPYVTDV 161
Cdd:TIGR03389 157 NQTGGAPNVSDAYTINGHPGPLYNCSSKDTFKLTVEPGKTYLLRIINAALNDELFFAIANHTLTVVEVDATYTKPFKTKT 236

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063710373 162 IVIAPGQTIDALLFADQSVDTsYYMAAHPYASAPaVPFPNTTTRGVIHYGGASktGRSKPVlMPKLPSFFDTLTAYRFYS 241
Cdd:TIGR03389 237 IVIGPGQTTNVLLTADQSPGR-YFMAARPYMDAP-GAFDNTTTTAILQYKGTS--NSAKPI-LPTLPAYNDTAAATNFSN 311

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063710373 242 NLTALVNGPHWVPVPRYVDEEMLVTIGLGLEACADNT-TCP---KFSASMSNHSFVLPkKLSILEAVFHDVKGIFTADFP 317
Cdd:TIGR03389 312 KLRSLNSAQYPANVPVTIDRRLFFTIGLGLDPCPNNTcQGPngtRFAASMNNISFVMP-TTALLQAHYFGISGVFTTDFP 390

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063710373 318 DQPPVKFDYTNPNVtqtnPGLLFTQKSTSAKILKFNTTVEVVLQNHALIAAESHPMHLHGFNFHVLAQGFGNYDPSRDRS 397
Cdd:TIGR03389 391 ANPPTKFNYTGTNL----PNNLFTTNGTKVVRLKFNSTVELVLQDTSILGSENHPIHLHGYNFFVVGTGFGNFDPKKDPA 466

                         410       420       430       440       450
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1063710373 398 KLNLVDPQSRNTLAVPVGGWAVIRFTANNPGAWIFHCHIDVHLPFGLGMIFVVKNG 453
Cdd:TIGR03389 467 KFNLVDPPERNTVGVPTGGWAAIRFVADNPGVWFMHCHLEVHTTWGLKMAFLVDNG 522
 
Name Accession Description Interval E-value
laccase TIGR03389
laccase, plant; Members of this protein family include the copper-containing enzyme laccase ...
 2-453 0e+00

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: 603.27  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063710373   2 ITQCPIQPGQRYAYRFNITGQEGTLWWHAHASFLRATVYGALVIRPKSGHSYPFPKPHKEVPILFGEWWNTDVVALEEAA 81
Cdd:TIGR03389  77 ITQCPIQPGQSYVYNFTITGQRGTLWWHAHISWLRATVYGAIVILPKPGVPYPFPKPDREVPIILGEWWNADVEAVINQA 156

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063710373  82 IATGVPPNNSDAYTINGRPGNLYPCSKDRMFSLNVVKGKRYLLRIINAAMNIQLFFKIANHRLTVVAADAVYTAPYVTDV 161
Cdd:TIGR03389 157 NQTGGAPNVSDAYTINGHPGPLYNCSSKDTFKLTVEPGKTYLLRIINAALNDELFFAIANHTLTVVEVDATYTKPFKTKT 236

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063710373 162 IVIAPGQTIDALLFADQSVDTsYYMAAHPYASAPaVPFPNTTTRGVIHYGGASktGRSKPVlMPKLPSFFDTLTAYRFYS 241
Cdd:TIGR03389 237 IVIGPGQTTNVLLTADQSPGR-YFMAARPYMDAP-GAFDNTTTTAILQYKGTS--NSAKPI-LPTLPAYNDTAAATNFSN 311

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063710373 242 NLTALVNGPHWVPVPRYVDEEMLVTIGLGLEACADNT-TCP---KFSASMSNHSFVLPkKLSILEAVFHDVKGIFTADFP 317
Cdd:TIGR03389 312 KLRSLNSAQYPANVPVTIDRRLFFTIGLGLDPCPNNTcQGPngtRFAASMNNISFVMP-TTALLQAHYFGISGVFTTDFP 390

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063710373 318 DQPPVKFDYTNPNVtqtnPGLLFTQKSTSAKILKFNTTVEVVLQNHALIAAESHPMHLHGFNFHVLAQGFGNYDPSRDRS 397
Cdd:TIGR03389 391 ANPPTKFNYTGTNL----PNNLFTTNGTKVVRLKFNSTVELVLQDTSILGSENHPIHLHGYNFFVVGTGFGNFDPKKDPA 466

                         410       420       430       440       450
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1063710373 398 KLNLVDPQSRNTLAVPVGGWAVIRFTANNPGAWIFHCHIDVHLPFGLGMIFVVKNG 453
Cdd:TIGR03389 467 KFNLVDPPERNTVGVPTGGWAAIRFVADNPGVWFMHCHLEVHTTWGLKMAFLVDNG 522
CuRO_2_LCC_plant cd13875
The second cupredoxin domain of the plant laccases; Laccase is a blue multi-copper enzyme that ...
 62-210 6.13e-91

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: 272.93  E-value: 6.13e-91
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063710373  62 VPILFGEWWNTDVVALEEAAIATGVPPNNSDAYTINGRPGNLYPCSKDRMFSLNVVKGKRYLLRIINAAMNIQLFFKIAN 141
Cdd:cd13875     1 VPIILGEWWNRDVNDVEDQALLTGGGPNISDAYTINGQPGDLYNCSSKDTFVLTVEPGKTYLLRIINAALNEELFFKIAN 80

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1063710373 142 HRLTVVAADAVYTAPYVTDVIVIAPGQTIDALLFADQSVDtSYYMAAHPYASAPAVPFPNTTTRGVIHY 210
Cdd:cd13875    81 HTLTVVAVDASYTKPFTTDYILIAPGQTTDVLLTADQPPG-RYYMAARPYQSAPPVPFDNTTATAILEY 148
PLN02604 PLN02604
oxidoreductase
 2-448 9.42e-60

oxidoreductase


Pssm-ID: 215324 [Multi-domain]  Cd Length: 566  Bit Score: 205.48  E-value: 9.42e-60
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063710373   2 ITQCPIQPGQRYAYRFnITGQEGTLWWHAHASFLR-ATVYGALVIRPKSGHSYPFPKPHKEvPILFGEWWNTDVValEEA 80
Cdd:PLN02604   99 VTQCPILPGETFTYEF-VVDRPGTYLYHAHYGMQReAGLYGSIRVSLPRGKSEPFSYDYDR-SIILTDWYHKSTY--EQA 174

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063710373  81 AIATGVP---PNNSDAYTINGRpgNLYPCSKDR-----------------MFSLNVVKGKRYLLRIINAAMNIQLFFKIA 140
Cdd:PLN02604  175 LGLSSIPfdwVGEPQSLLIQGK--GRYNCSLVSspylkagvcnatnpecsPYVLTVVPGKTYRLRISSLTALSALSFQIE 252

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063710373 141 NHRLTVVAADAVYTAPYVTDVIVIAPGQTIDALLFADQSVDTSYYMAAHPYASAPAVPfpntTTRGVIHYGgASKTGRSK 220
Cdd:PLN02604  253 GHNMTVVEADGHYVEPFVVKNLFIYSGETYSVLVKADQDPSRNYWVTTSVVSRNNTTP----PGLAIFNYY-PNHPRRSP 327

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063710373 221 PVLMPKLPSFFDTLTayRFYSNLTALVNGPHWVPVPRYVDEemlVTIGLGLEACADNTtcpkFSASMSNHSFVLPKKlSI 300
Cdd:PLN02604  328 PTVPPSGPLWNDVEP--RLNQSLAIKARHGYIHPPPLTSDR---VIVLLNTQNEVNGY----RRWSVNNVSFNLPHT-PY 397

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063710373 301 LEAVFHDVKGIFTadfPDQPPVKFDYTNPNV--TQTNpgllfTQKSTSAKI--LKFNTTVEVVLQNHALIAA---ESHPM 373
Cdd:PLN02604  398 LIALKENLTGAFD---QTPPPEGYDFANYDIyaKPNN-----SNATSSDSIyrLQFNSTVDIILQNANTMNAnnsETHPW 469

                         410       420       430       440       450       460       470
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1063710373 374 HLHGFNFHVLAQGFGNYDPSRDRSKLNLVDPQSRNTLAVPVGGWAVIRFTANNPGAWIFHCHIDVHLPFGLGMIF 448
Cdd:PLN02604  470 HLHGHDFWVLGYGEGKFNMSSDPKKYNLVDPIMKNTVPVHPYGWTALRFRADNPGVWAFHCHIESHFFMGMGVVF 544
Cu-oxidase pfam00394
Multicopper oxidase; Many of the proteins in this family contain multiple similar copies of ...
 60-213 1.32e-45

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: 155.55  E-value: 1.32e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063710373  60 KEVPILFGEWWNTDVVALEEAAIATGVP----PNNSDAYTINGRPGNLYpcskdrmFSLNVVKGKRYLLRIINAAMNIQL 135
Cdd:pfam00394   1 EDYVITLSDWYHKDAKDLEKELLASGKAptdfPPVPDAVLINGKDGASL-------ATLTVTPGKTYRLRIINVALDDSL 73

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1063710373 136 FFKIANHRLTVVAADAVYTAPYVTDVIVIAPGQTIDALLFADQSVDTsYYMAAHPyasaPAVPFPNTTTRGVIHYGGA 213
Cdd:pfam00394  74 NFSIEGHKMTVVEVDGVYVNPFTVDSLDIFPGQRYSVLVTANQDPGN-YWIVASP----NIPAFDNGTAAAILRYSGA 146
SufI COG2132
Multicopper oxidase with three cupredoxin domains (includes cell division protein FtsP and ...
 6-450 2.22e-31

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: 125.05  E-value: 2.22e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063710373   6 PIQPGQRYAYRFNITGQEGTLWWHAHAsfLRATV-------YGALVIRPKSGhsyPFPKPHKEVPILFGEWWNTD--VVA 76
Cdd:COG2132    87 PIAPGETFTYEFPVPQPAGTYWYHPHT--HGSTAeqvyrglAGALIVEDPEE---DLPRYDRDIPLVLQDWRLDDdgQLL 161

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063710373  77 LEEAAIATGVPPnnsDAYTINGRPGnlypcskdrmFSLNVVKGKRYLLRIINAA----MNIQLFfkiANHRLTVVAADAV 152
Cdd:COG2132   162 YPMDAAMGGRLG---DTLLVNGRPN----------PTLEVRPGERVRLRLLNASnariYRLALS---DGRPFTVIATDGG 225

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063710373 153 YT-APYVTDVIVIAPGQTIDALLFADQSVDTSYYMAAHPYASAPAvpfpnttTRGVIHYGGASKtgrskpvlMPKLPsff 231
Cdd:COG2132   226 LLpAPVEVDELLLAPGERADVLVDFSADPGEEVTLANPFEGRSGR-------ALLTLRVTGAAA--------SAPLP--- 287

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063710373 232 dtltayrfysnltalvngPHWVPVPRYVDEEMLVTIGLgleacadnttcpKFSASMSNHSFVLPKKlsileavfhdvkgi 311
Cdd:COG2132   288 ------------------ANLAPLPDLEDREAVRTREL------------VLTGGMAGYVWTINGK-------------- 323

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063710373 312 ftadfpdqppvKFDYTNPNVTqtnpgllftqkstsakiLKFNTTVEVVLQNHaliAAESHPMHLHGFNFHVLaqgfgnyd 391
Cdd:COG2132   324 -----------AFDPDRPDLT-----------------VKLGERERWTLVND---TMMPHPFHLHGHQFQVL-------- 364

                         410       420       430       440       450       460
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063710373 392 pSRDRSKLNlvDPQSRNTLAVPVGGWAVIRFTANN-PGAWIFHCHIDVHLPFGLGMIFVV 450
Cdd:COG2132   365 -SRNGKPPP--EGGWKDTVLVPPGETVRILFRFDNyPGDWMFHCHILEHEDAGMMGQFEV 421
 
Name Accession Description Interval E-value
laccase TIGR03389
laccase, plant; Members of this protein family include the copper-containing enzyme laccase ...
 2-453 0e+00

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: 603.27  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063710373   2 ITQCPIQPGQRYAYRFNITGQEGTLWWHAHASFLRATVYGALVIRPKSGHSYPFPKPHKEVPILFGEWWNTDVVALEEAA 81
Cdd:TIGR03389  77 ITQCPIQPGQSYVYNFTITGQRGTLWWHAHISWLRATVYGAIVILPKPGVPYPFPKPDREVPIILGEWWNADVEAVINQA 156

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063710373  82 IATGVPPNNSDAYTINGRPGNLYPCSKDRMFSLNVVKGKRYLLRIINAAMNIQLFFKIANHRLTVVAADAVYTAPYVTDV 161
Cdd:TIGR03389 157 NQTGGAPNVSDAYTINGHPGPLYNCSSKDTFKLTVEPGKTYLLRIINAALNDELFFAIANHTLTVVEVDATYTKPFKTKT 236

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063710373 162 IVIAPGQTIDALLFADQSVDTsYYMAAHPYASAPaVPFPNTTTRGVIHYGGASktGRSKPVlMPKLPSFFDTLTAYRFYS 241
Cdd:TIGR03389 237 IVIGPGQTTNVLLTADQSPGR-YFMAARPYMDAP-GAFDNTTTTAILQYKGTS--NSAKPI-LPTLPAYNDTAAATNFSN 311

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063710373 242 NLTALVNGPHWVPVPRYVDEEMLVTIGLGLEACADNT-TCP---KFSASMSNHSFVLPkKLSILEAVFHDVKGIFTADFP 317
Cdd:TIGR03389 312 KLRSLNSAQYPANVPVTIDRRLFFTIGLGLDPCPNNTcQGPngtRFAASMNNISFVMP-TTALLQAHYFGISGVFTTDFP 390

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063710373 318 DQPPVKFDYTNPNVtqtnPGLLFTQKSTSAKILKFNTTVEVVLQNHALIAAESHPMHLHGFNFHVLAQGFGNYDPSRDRS 397
Cdd:TIGR03389 391 ANPPTKFNYTGTNL----PNNLFTTNGTKVVRLKFNSTVELVLQDTSILGSENHPIHLHGYNFFVVGTGFGNFDPKKDPA 466

                         410       420       430       440       450
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1063710373 398 KLNLVDPQSRNTLAVPVGGWAVIRFTANNPGAWIFHCHIDVHLPFGLGMIFVVKNG 453
Cdd:TIGR03389 467 KFNLVDPPERNTVGVPTGGWAAIRFVADNPGVWFMHCHLEVHTTWGLKMAFLVDNG 522
CuRO_2_LCC_plant cd13875
The second cupredoxin domain of the plant laccases; Laccase is a blue multi-copper enzyme that ...
 62-210 6.13e-91

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: 272.93  E-value: 6.13e-91
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063710373  62 VPILFGEWWNTDVVALEEAAIATGVPPNNSDAYTINGRPGNLYPCSKDRMFSLNVVKGKRYLLRIINAAMNIQLFFKIAN 141
Cdd:cd13875     1 VPIILGEWWNRDVNDVEDQALLTGGGPNISDAYTINGQPGDLYNCSSKDTFVLTVEPGKTYLLRIINAALNEELFFKIAN 80

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1063710373 142 HRLTVVAADAVYTAPYVTDVIVIAPGQTIDALLFADQSVDtSYYMAAHPYASAPAVPFPNTTTRGVIHY 210
Cdd:cd13875    81 HTLTVVAVDASYTKPFTTDYILIAPGQTTDVLLTADQPPG-RYYMAARPYQSAPPVPFDNTTATAILEY 148
CuRO_3_LCC_plant cd13897
The third cupredoxin domain of the plant laccases; Laccase is a blue multicopper oxidase (MCO) ...
 311-453 3.75e-72

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: 224.45  E-value: 3.75e-72
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063710373 311 IFTADFPDQPPVKFDYTNPNVtqtnPGLLFTQKSTSAKILKFNTTVEVVLQNHALIAAESHPMHLHGFNFHVLAQGFGNY 390
Cdd:cd13897     1 VYTTDFPDRPPVPFDYTGNAP----NENTPTSRGTKVKVLEYGSTVEIVLQGTSLLAAENHPMHLHGFDFYVVGRGFGNF 76

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1063710373 391 DPSRDRSKLNLVDPQSRNTLAVPVGGWAVIRFTANNPGAWIFHCHIDVHLPFGLGMIFVVKNG 453
Cdd:cd13897    77 DPSTDPATFNLVDPPLRNTVGVPRGGWAAIRFVADNPGVWFMHCHFERHTSWGMATVFIVKNG 139
ascorbase TIGR03388
L-ascorbate oxidase, plant type; Members of this protein family are the copper-containing ...
 2-448 6.55e-66

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: 221.16  E-value: 6.55e-66
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063710373   2 ITQCPIQPGQRYAYRFnITGQEGTLWWHAHASFLR-ATVYGALVIRPKSGHSYPFPKPHkEVPILFGEWWNTDVVAlEEA 80
Cdd:TIGR03388  76 VTQCAINPGETFIYNF-VVDRPGTYFYHGHYGMQRsAGLYGSLIVDVPDGEKEPFHYDG-EFNLLLSDWWHKSIHE-QEV 152

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063710373  81 AIAT------GVPPNnsdaYTINGR------------PGNLYPCSKDRM-----FSLNVVKGKRYLLRIINAAMNIQLFF 137
Cdd:TIGR03388 153 GLSSkpmrwiGEPQS----LLINGRgqfncslaakfsSTNLPQCNLKGNeqcapQILHVEPGKTYRLRIASTTALAALNF 228

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063710373 138 KIANHRLTVVAADAVYTAPYVTDVIVIAPGQTIDALLFADQSVDTSYYMAAHPYASAPAVPfPNTTtrgVIHYGGASKTg 217
Cdd:TIGR03388 229 AIEGHKLTVVEADGNYVEPFTVKDIDIYSGETYSVLLTTDQDPSRNYWISVGVRGRKPNTP-PGLT---VLNYYPNSPS- 303

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063710373 218 RSKPVLMPKLPSFFDTLTAYRFYSNLTALVNGPhwvPVPRYVDE--EMLVTiglgleacaDNTTCPKFSASMSNHSFVLP 295
Cdd:TIGR03388 304 RLPPTPPPVTPAWDDFDRSKAFSLAIKAAMGSP---KPPETSDRriVLLNT---------QNKINGYTKWAINNVSLTLP 371

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063710373 296 KKLsILEAVFHDVKGIFTADFP-DQPPVKFDYTNPnvtQTNPGllfTQKSTSAKILKFNTTVEVVLQNHALIAA---ESH 371
Cdd:TIGR03388 372 HTP-YLGSLKYNLLNAFDQKPPpENYPRDYDIFKP---PPNPN---TTTGNGIYRLKFNTTVDVILQNANTLNGnnsETH 444

                         410       420       430       440       450       460       470
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1063710373 372 PMHLHGFNFHVLAQGFGNYDPSRDRSKLNLVDPQSRNTLAVPVGGWAVIRFTANNPGAWIFHCHIDVHLPFGLGMIF 448
Cdd:TIGR03388 445 PWHLHGHDFWVLGYGEGKFRPGVDEKSYNLKNPPLRNTVVIFPYGWTALRFVADNPGVWAFHCHIEPHLHMGMGVVF 521
PLN02604 PLN02604
oxidoreductase
 2-448 9.42e-60

oxidoreductase


Pssm-ID: 215324 [Multi-domain]  Cd Length: 566  Bit Score: 205.48  E-value: 9.42e-60
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063710373   2 ITQCPIQPGQRYAYRFnITGQEGTLWWHAHASFLR-ATVYGALVIRPKSGHSYPFPKPHKEvPILFGEWWNTDVValEEA 80
Cdd:PLN02604   99 VTQCPILPGETFTYEF-VVDRPGTYLYHAHYGMQReAGLYGSIRVSLPRGKSEPFSYDYDR-SIILTDWYHKSTY--EQA 174

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063710373  81 AIATGVP---PNNSDAYTINGRpgNLYPCSKDR-----------------MFSLNVVKGKRYLLRIINAAMNIQLFFKIA 140
Cdd:PLN02604  175 LGLSSIPfdwVGEPQSLLIQGK--GRYNCSLVSspylkagvcnatnpecsPYVLTVVPGKTYRLRISSLTALSALSFQIE 252

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063710373 141 NHRLTVVAADAVYTAPYVTDVIVIAPGQTIDALLFADQSVDTSYYMAAHPYASAPAVPfpntTTRGVIHYGgASKTGRSK 220
Cdd:PLN02604  253 GHNMTVVEADGHYVEPFVVKNLFIYSGETYSVLVKADQDPSRNYWVTTSVVSRNNTTP----PGLAIFNYY-PNHPRRSP 327

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063710373 221 PVLMPKLPSFFDTLTayRFYSNLTALVNGPHWVPVPRYVDEemlVTIGLGLEACADNTtcpkFSASMSNHSFVLPKKlSI 300
Cdd:PLN02604  328 PTVPPSGPLWNDVEP--RLNQSLAIKARHGYIHPPPLTSDR---VIVLLNTQNEVNGY----RRWSVNNVSFNLPHT-PY 397

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063710373 301 LEAVFHDVKGIFTadfPDQPPVKFDYTNPNV--TQTNpgllfTQKSTSAKI--LKFNTTVEVVLQNHALIAA---ESHPM 373
Cdd:PLN02604  398 LIALKENLTGAFD---QTPPPEGYDFANYDIyaKPNN-----SNATSSDSIyrLQFNSTVDIILQNANTMNAnnsETHPW 469

                         410       420       430       440       450       460       470
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1063710373 374 HLHGFNFHVLAQGFGNYDPSRDRSKLNLVDPQSRNTLAVPVGGWAVIRFTANNPGAWIFHCHIDVHLPFGLGMIF 448
Cdd:PLN02604  470 HLHGHDFWVLGYGEGKFNMSSDPKKYNLVDPIMKNTVPVHPYGWTALRFRADNPGVWAFHCHIESHFFMGMGVVF 544
PLN02191 PLN02191
L-ascorbate oxidase
 2-449 1.82e-55

L-ascorbate oxidase


Pssm-ID: 177843 [Multi-domain]  Cd Length: 574  Bit Score: 194.08  E-value: 1.82e-55
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063710373   2 ITQCPIQPGQRYAYRFnITGQEGTLWWHAHASFLRAT-VYGALVIRPKSGHSYPFpKPHKEVPILFGEWWNTDVVALEea 80
Cdd:PLN02191   98 VTQCAINPGETFTYKF-TVEKPGTHFYHGHYGMQRSAgLYGSLIVDVAKGPKERL-RYDGEFNLLLSDWWHESIPSQE-- 173

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063710373  81 aIATGVPP----NNSDAYTINGRpgNLYPCSKDRMFS--------------------LNVVKGKRYLLRIINAAMNIQLF 136
Cdd:PLN02191  174 -LGLSSKPmrwiGEAQSILINGR--GQFNCSLAAQFSngtelpmctfkegdqcapqtLRVEPNKTYRIRLASTTALASLN 250

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063710373 137 FKIANHRLTVVAADAVYTAPYVTDVIVIAPGQTIDALLFADQSVDTSYYMAAHPYASAPAVPFPNTttrgVIHY--GGAS 214
Cdd:PLN02191  251 LAVQGHKLVVVEADGNYITPFTTDDIDIYSGESYSVLLTTDQDPSQNYYISVGVRGRKPNTTQALT----ILNYvtAPAS 326

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063710373 215 KTGRSKPvlmPKLPSFFDTLTAYRFYSNLTALVNGPHwvPVPRYVDEEMLvtigLGLEACADNTTcpkfSASMSNHSFVL 294
Cdd:PLN02191  327 KLPSSPP---PVTPRWDDFERSKNFSKKIFSAMGSPS--PPKKYRKRLIL----LNTQNLIDGYT----KWAINNVSLVT 393

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063710373 295 PKKlSILEAVFHDVKGIFTADFPDQP-PVKFDYTNPnvtQTNPGllfTQKSTSAKILKFNTTVEVVLQNHAL---IAAES 370
Cdd:PLN02191  394 PAT-PYLGSVKYNLKLGFNRKSPPRSyRMDYDIMNP---PPFPN---TTTGNGIYVFPFNVTVDVIIQNANVlkgVVSEI 466

                         410       420       430       440       450       460       470
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1063710373 371 HPMHLHGFNFHVLAQGFGNYDPSRDRSKLNLVDPQSRNTLAVPVGGWAVIRFTANNPGAWIFHCHIDVHLPFGLGMIFV 449
Cdd:PLN02191  467 HPWHLHGHDFWVLGYGDGKFKPGIDEKTYNLKNPPLRNTAILYPYGWTAIRFVTDNPGVWFFHCHIEPHLHMGMGVVFA 545
Cu-oxidase pfam00394
Multicopper oxidase; Many of the proteins in this family contain multiple similar copies of ...
 60-213 1.32e-45

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: 155.55  E-value: 1.32e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063710373  60 KEVPILFGEWWNTDVVALEEAAIATGVP----PNNSDAYTINGRPGNLYpcskdrmFSLNVVKGKRYLLRIINAAMNIQL 135
Cdd:pfam00394   1 EDYVITLSDWYHKDAKDLEKELLASGKAptdfPPVPDAVLINGKDGASL-------ATLTVTPGKTYRLRIINVALDDSL 73

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1063710373 136 FFKIANHRLTVVAADAVYTAPYVTDVIVIAPGQTIDALLFADQSVDTsYYMAAHPyasaPAVPFPNTTTRGVIHYGGA 213
Cdd:pfam00394  74 NFSIEGHKMTVVEVDGVYVNPFTVDSLDIFPGQRYSVLVTANQDPGN-YWIVASP----NIPAFDNGTAAAILRYSGA 146
Cu-oxidase_2 pfam07731
Multicopper oxidase; This entry contains many divergent copper oxidase-like domains that are ...
 315-453 2.20e-44

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: 152.20  E-value: 2.20e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063710373 315 DFPDQPPVKFDYTNPNVTQTNP---GLLFTQkSTSAKILKFNTTVEVVLQNHALIaaeSHPMHLHGFNFHVLAQGFGNyD 391
Cdd:pfam07731   1 DTPPKLPTLLQITSGNFRRNDWainGLLFPP-NTNVITLPYGTVVEWVLQNTTTG---VHPFHLHGHSFQVLGRGGGP-W 75

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1063710373 392 PSRDRSKLNLVDPQSRNTLAVPVGGWAVIRFTANNPGAWIFHCHIDVHLPFGLGMIFVVKNG 453
Cdd:pfam07731  76 PEEDPKTYNLVDPVRRDTVQVPPGGWVAIRFRADNPGVWLFHCHILWHLDQGMMGQFVVRPG 137
CuRO_3_tcLLC2_insect_like cd13905
The third cupredoxin domain of the insect laccases similar to laccase 2 in Tribolium castaneum; ...
 350-448 1.71e-34

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: 127.03  E-value: 1.71e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063710373 350 LKFNTTVEVVLQNHALIAAESHPMHLHGFNFHVLAQGFGNYDPS----------------RDRSKLNLVDPQSRNTLAVP 413
Cdd:cd13905    49 LPLNSVVEIVLINEGPGPGLSHPFHLHGHSFYVLGMGFPGYNSTtgeilsqnwnnklldrGGLPGRNLVNPPLKDTVVVP 128

                          90       100       110
                  ....*....|....*....|....*....|....*
gi 1063710373 414 VGGWAVIRFTANNPGAWIFHCHIDVHLPFGLGMIF 448
Cdd:cd13905   129 NGGYVVIRFRADNPGYWLLHCHIEFHLLEGMALVL 163
CuRO_3_AAO cd13893
The third cupredoxin domain of plant Ascorbate oxidase; Ascorbate oxidase catalyzes the ...
 350-449 2.04e-34

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: 126.38  E-value: 2.04e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063710373 350 LKFNTTVEVVLQNHAL---IAAESHPMHLHGFNFHVLAQGFGNYDPSRDRSKLNLVDPQSRNTLAVPVGGWAVIRFTANN 426
Cdd:cd13893    43 FKGGDVVDVILQNANTntrNASEQHPWHLHGHDFWVLGYGLGGFDPAADPSSLNLVNPPMRNTVTIFPYGWTALRFKADN 122

                          90       100
                  ....*....|....*....|...
gi 1063710373 427 PGAWIFHCHIDVHLPFGLGMIFV 449
Cdd:cd13893   123 PGVWAFHCHIEWHFHMGMGVVFA 145
PLN02168 PLN02168
copper ion binding / pectinesterase
 3-430 9.29e-33

copper ion binding / pectinesterase


Pssm-ID: 215113 [Multi-domain]  Cd Length: 545  Bit Score: 130.48  E-value: 9.29e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063710373   3 TQCPIQPGQRYAYRFNITGQEGTLWWHAHASFLRATV-YGALVIRPKSGHSYPFPKPHKEVPILFGEWWNTDVVALeEAA 81
Cdd:PLN02168  100 TNCPILPGTNWTYRFQVKDQIGSYFYFPSLLLQKAAGgYGAIRIYNPELVPVPFPKPDEEYDILIGDWFYADHTVM-RAS 178

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063710373  82 IATGVPPNNSDAYTINGRPGNlypcskDRMFSLNvvKGKRYLLRIINAAMNIQLFFKIANHRLTVVAADAVYTAPYVTDV 161
Cdd:PLN02168  179 LDNGHSLPNPDGILFNGRGPE------ETFFAFE--PGKTYRLRISNVGLKTCLNFRIQDHDMLLVETEGTYVQKRVYSS 250

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063710373 162 IVIAPGQTIDALLFADQS---VDTSYYMaahpYASAPAVPFpNTTTRGVIHYGGASKTGRSKPVLMPKLPSFFDTLT--- 235
Cdd:PLN02168  251 LDIHVGQSYSVLVTAKTDpvgIYRSYYI----VATARFTDA-YLGGVALIRYPNSPLDPVGPLPLAPALHDYFSSVEqal 325

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063710373 236 AYRFYSNLTALVNGP----HW--VPVPRYV---DEEMLVTiglgleacadnttcPKFSASMSNHSFVLPKKLSILEAVFH 306
Cdd:PLN02168  326 SIRMDLNVGAARSNPqgsyHYgrINVTRTIilhNDVMLSS--------------GKLRYTINGVSFVYPGTPLKLVDHFQ 391

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063710373 307 DVKGIFTADFPDQPPVKfdytnpnvtqtNPGLlftqkSTSAKILKFNTTVEVVLQNhALIAAESHpmHLHGFNFHVLAQG 386
Cdd:PLN02168  392 LNDTIIPGMFPVYPSNK-----------TPTL-----GTSVVDIHYKDFYHIVFQN-PLFSLESY--HIDGYNFFVVGYG 452

                         410       420       430       440
                  ....*....|....*....|....*....|....*....|....
gi 1063710373 387 FGNYDPSRdRSKLNLVDPQSRNTLAVPVGGWAVIRFTANNPGAW 430
Cdd:PLN02168  453 FGAWSESK-KAGYNLVDAVSRSTVQVYPYSWTAILIAMDNQGMW 495
PLN02991 PLN02991
oxidoreductase
 3-430 5.84e-32

oxidoreductase


Pssm-ID: 215536 [Multi-domain]  Cd Length: 543  Bit Score: 128.21  E-value: 5.84e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063710373   3 TQCPIQPGQRYAYRFNITGQEGTLWWHAHASFLRATV-YGALVIRPKSGHSYPFPKPHKEVPILFGEWWNTDVVALEeAA 81
Cdd:PLN02991  102 TTCPIPPGKNYTYALQVKDQIGSFYYFPSLGFHKAAGgFGAIRISSRPLIPVPFPAPADDYTVLIGDWYKTNHKDLR-AQ 180

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063710373  82 IATGVPPNNSDAYTINGRPGNLypcskdrmfSLNVVKGKRYLLRIINAAMNIQLFFKIANHRLTVVAADAVYTAPYVTDV 161
Cdd:PLN02991  181 LDNGGKLPLPDGILINGRGSGA---------TLNIEPGKTYRLRISNVGLQNSLNFRIQNHTMKLVEVEGTHTIQTPFSS 251

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063710373 162 IVIAPGQTIDALLFADQSVDTSYYMAAHPYASAPavpfpnTTTRGVIHYGGAsktgrSKPVLMP------KLPSFFDTLT 235
Cdd:PLN02991  252 LDVHVGQSYSVLITADQPAKDYYIVVSSRFTSKI------LITTGVLHYSNS-----AGPVSGPipdgpiQLSWSFDQAR 320

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063710373 236 AYRfySNLTAlvNGPHWVPVPRYVDEEMLVTIGLGLEACADNTTcPKFSASMSNHSFvLPKKLSILEAVFHDVKGIFT-A 314
Cdd:PLN02991  321 AIK--TNLTA--SGPRPNPQGSYHYGKINITRTIRLANSAGNIE-GKQRYAVNSASF-YPADTPLKLADYFKIAGVYNpG 394

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063710373 315 DFPDQPPVKFDYTNPNVTQTNpgllftqkstsakilkFNTTVEVVLQNHALIAaesHPMHLHGFNFHVLAQGFGNYDPSr 394
Cdd:PLN02991  395 SIPDQPTNGAIFPVTSVMQTD----------------YKAFVEIVFENWEDIV---QTWHLDGYSFYVVGMELGKWSAA- 454

                         410       420       430
                  ....*....|....*....|....*....|....*.
gi 1063710373 395 DRSKLNLVDPQSRNTLAVPVGGWAVIRFTANNPGAW 430
Cdd:PLN02991  455 SRKVYNLNDAVSRCTVQVYPRSWTAIYVSLDNVGMW 490
SufI COG2132
Multicopper oxidase with three cupredoxin domains (includes cell division protein FtsP and ...
 6-450 2.22e-31

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: 125.05  E-value: 2.22e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063710373   6 PIQPGQRYAYRFNITGQEGTLWWHAHAsfLRATV-------YGALVIRPKSGhsyPFPKPHKEVPILFGEWWNTD--VVA 76
Cdd:COG2132    87 PIAPGETFTYEFPVPQPAGTYWYHPHT--HGSTAeqvyrglAGALIVEDPEE---DLPRYDRDIPLVLQDWRLDDdgQLL 161

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063710373  77 LEEAAIATGVPPnnsDAYTINGRPGnlypcskdrmFSLNVVKGKRYLLRIINAA----MNIQLFfkiANHRLTVVAADAV 152
Cdd:COG2132   162 YPMDAAMGGRLG---DTLLVNGRPN----------PTLEVRPGERVRLRLLNASnariYRLALS---DGRPFTVIATDGG 225

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063710373 153 YT-APYVTDVIVIAPGQTIDALLFADQSVDTSYYMAAHPYASAPAvpfpnttTRGVIHYGGASKtgrskpvlMPKLPsff 231
Cdd:COG2132   226 LLpAPVEVDELLLAPGERADVLVDFSADPGEEVTLANPFEGRSGR-------ALLTLRVTGAAA--------SAPLP--- 287

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063710373 232 dtltayrfysnltalvngPHWVPVPRYVDEEMLVTIGLgleacadnttcpKFSASMSNHSFVLPKKlsileavfhdvkgi 311
Cdd:COG2132   288 ------------------ANLAPLPDLEDREAVRTREL------------VLTGGMAGYVWTINGK-------------- 323

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063710373 312 ftadfpdqppvKFDYTNPNVTqtnpgllftqkstsakiLKFNTTVEVVLQNHaliAAESHPMHLHGFNFHVLaqgfgnyd 391
Cdd:COG2132   324 -----------AFDPDRPDLT-----------------VKLGERERWTLVND---TMMPHPFHLHGHQFQVL-------- 364

                         410       420       430       440       450       460
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063710373 392 pSRDRSKLNlvDPQSRNTLAVPVGGWAVIRFTANN-PGAWIFHCHIDVHLPFGLGMIFVV 450
Cdd:COG2132   365 -SRNGKPPP--EGGWKDTVLVPPGETVRILFRFDNyPGDWMFHCHILEHEDAGMMGQFEV 421
PLN02354 PLN02354
copper ion binding / oxidoreductase
 3-430 1.18e-29

copper ion binding / oxidoreductase


Pssm-ID: 177987 [Multi-domain]  Cd Length: 552  Bit Score: 121.82  E-value: 1.18e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063710373   3 TQCPIQPGQRYAYRFNITGQEGTLWWHAHASFLRAT-VYGALVIRPKSGHSYPFPKPHKEVPILFGEWWNTDVVALE--- 78
Cdd:PLN02354  101 TNCPIPPGTNFTYHFQPKDQIGSYFYYPSTGMHRAAgGFGGLRVNSRLLIPVPYADPEDDYTVLIGDWYTKSHTALKkfl 180

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063710373  79 EAAIATGVPpnnsDAYTINGRPGNLyPCSKDRMFSLNvvKGKRYLLRIINAAMNIQLFFKIANHRLTVVAADAVYTAPYV 158
Cdd:PLN02354  181 DSGRTLGRP----DGVLINGKSGKG-DGKDEPLFTMK--PGKTYRYRICNVGLKSSLNFRIQGHKMKLVEMEGSHVLQND 253

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063710373 159 TDVIVIAPGQTIDALLFADQsVDTSYYMAAhpyasapAVPFPNT--TTRGVIHYGGASKTGRSKpvlMPKLPSFFD-TLT 235
Cdd:PLN02354  254 YDSLDVHVGQCFSVLVTANQ-APKDYYMVA-------STRFLKKvlTTTGIIRYEGGKGPASPE---LPEAPVGWAwSLN 322

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063710373 236 AYR-FYSNLTALVNGPHWVPVPRYVDEEMLVTIGLGLEAcadNTTCPKFSASMSNHSFVLPKKLSILEAVFHDVKGIFTA 314
Cdd:PLN02354  323 QFRsFRWNLTASAARPNPQGSYHYGKINITRTIKLVNSA---SKVDGKLRYALNGVSHVDPETPLKLAEYFGVADKVFKY 399

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063710373 315 D-FPDQPPVKFD--YTNPNVTQtnpgllftqkstsakiLKFNTTVEVVLQNHaliAAESHPMHLHGFNFHVLAQGFGNYD 391
Cdd:PLN02354  400 DtIKDNPPAKITkiKIQPNVLN----------------ITFRTFVEIIFENH---EKSMQSWHLDGYSFFAVAVEPGTWT 460

                         410       420       430
                  ....*....|....*....|....*....|....*....
gi 1063710373 392 PSRdRSKLNLVDPQSRNTLAVPVGGWAVIRFTANNPGAW 430
Cdd:PLN02354  461 PEK-RKNYNLLDAVSRHTVQVYPKSWAAILLTFDNAGMW 498
CuRO_2_LCC_like cd04205
Cupredoxin domain 2 of laccase-like multicopper oxidases; including laccase, CueO, spore coat ...
 62-210 1.75e-29

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: 112.84  E-value: 1.75e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063710373  62 VPILFGEWWNTDVVALEEAAIAT--GVPPNnSDAYTINGRPgnLYPCSKDRMFS------LNVVKGKRYLLRIINAAMNI 133
Cdd:cd04205     1 RVLLLSDWYHDSAEDVLAGYMPNsfGNEPV-PDSLLINGRG--RFNCSMAVCNSgcplpvITVEPGKTYRLRLINAGSFA 77

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1063710373 134 QLFFKIANHRLTVVAADAVYTAPYVTDVIVIAPGQTIDALLFADQSVDTsYYMAAHPYASAPAvPFPNTTTRGVIHY 210
Cdd:cd04205    78 SFNFAIDGHNMTVIEVDGGYVEPLEVDNLDLAPGQRYDVLVKADQPPGN-YWIRASADGRTFD-EGGNPNGTAILRY 152
PLN02835 PLN02835
oxidoreductase
 3-430 7.50e-29

oxidoreductase


Pssm-ID: 178429 [Multi-domain]  Cd Length: 539  Bit Score: 119.31  E-value: 7.50e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063710373   3 TQCPIQPGQRYAYRFNITGQEGTLWWHAHASFLRATV-YGALVIRPKSGHSYPFPKPHKEVPILFGEWWNTDVVALEeAA 81
Cdd:PLN02835  103 TNCPIPPNSNYTYKFQTKDQIGTFTYFPSTLFHKAAGgFGAINVYERPRIPIPFPLPDGDFTLLVGDWYKTSHKTLQ-QR 181

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063710373  82 IATGVPPNNSDAYTINGRPGNLYpcSKDrmfslnvvKGKRYLLRIINAAMNIQLFFKIANHRLTVVAADAVYTAPYVTDV 161
Cdd:PLN02835  182 LDSGKVLPFPDGVLINGQTQSTF--SGD--------QGKTYMFRISNVGLSTSLNFRIQGHTMKLVEVEGSHTIQNIYDS 251

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063710373 162 IVIAPGQTIDALLFADQSVDTSYYMAAHPYASApavpfpNTTTRGVIHYGGaSKTGRSKPVlmPKLPSF---FDTLTAYR 238
Cdd:PLN02835  252 LDVHVGQSVAVLVTLNQSPKDYYIVASTRFTRQ------ILTATAVLHYSN-SRTPASGPL--PALPSGelhWSMRQART 322

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063710373 239 FYSNLTALVNGPHWVPVPRYVDEEMLVTIGLGLEACADNTtcpKFSASMSNHSFV---LPKKLsileAVFHDVKGIFTAD 315
Cdd:PLN02835  323 YRWNLTASAARPNPQGSFHYGKITPTKTIVLANSAPLING---KQRYAVNGVSYVnsdTPLKL----ADYFGIPGVFSVN 395

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063710373 316 -FPDQPPVKFDYTNPNVTQTNpgllftqkstsakilkFNTTVEVVLQNHaliAAESHPMHLHGFNFHVLAQGFGNYDPSR 394
Cdd:PLN02835  396 sIQSLPSGGPAFVATSVMQTS----------------LHDFLEVVFQNN---EKTMQSWHLDGYDFWVVGYGSGQWTPAK 456

                         410       420       430
                  ....*....|....*....|....*....|....*.
gi 1063710373 395 dRSKLNLVDPQSRNTLAVPVGGWAVIRFTANNPGAW 430
Cdd:PLN02835  457 -RSLYNLVDALTRHTAQVYPKSWTTILVSLDNQGMW 491
CuRO_3_LCC_like cd04207
Cupredoxin domain 3 of laccase-like multicopper oxidases; including laccase, CueO, spore coat ...
 350-449 1.58e-28

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: 109.47  E-value: 1.58e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063710373 350 LKFNTTVEVVLQNhALIAAESHPMHLHGFNFHVLAQGFGNYDPSrdrskLNLVDPQSRNTLAVPVGGWAVIRFTANNPGA 429
Cdd:cd04207    39 VEAGDVVEIVLIN-AGNHDMQHPFHLHGHSFWVLGSGGGPFDAP-----LNLTNPPWRDTVLVPPGGWVVIRFKADNPGV 112

                          90       100
                  ....*....|....*....|
gi 1063710373 430 WIFHCHIDVHLPFGLGMIFV 449
Cdd:cd04207   113 WMLHCHILEHEDAGMMTVFE 132
CuRO_3_MaLCC_like cd13901
The third cupredoxin domain of the fungal laccases similar to Ma-LCC from Melanocarpus ...
 353-449 5.32e-28

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: 108.85  E-value: 5.32e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063710373 353 NTTVEVVLQNHALIAaesHPMHLHGFNFHVLAQGFGNYDPsrDRSKLNLVDPQSRNTLAVPVGGWAVIRFTANNPGAWIF 432
Cdd:cd13901    66 NKWVYIVIQNNSPLP---HPIHLHGHDFYILAQGTGTFDD--DGTILNLNNPPRRDVAMLPAGGYLVIAFKTDNPGAWLM 140

                          90
                  ....*....|....*..
gi 1063710373 433 HCHIDVHLPFGLGMIFV 449
Cdd:cd13901   141 HCHIAWHASGGLALQFL 157
CuRO_2_MaLCC_like cd13880
The second cupredoxin domain of the fungal laccases similar to Ma-LCC from Melanocarpus ...
 63-216 5.57e-28

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: 109.26  E-value: 5.57e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063710373  63 PILFGEWWNTDVVALEEAAIATGVPPNnSDAYTINGRpgNLYPCSKDRM--FSLNVVKGKRYLLRIINAAMNIQLFFKIA 140
Cdd:cd13880     3 PVLLTDWYHRSAFELFSEELPTGGPPP-MDNILINGK--GKFPCSTGAGsyFETTFTPGKKYRLRLINTGVDTTFRFSID 79

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1063710373 141 NHRLTVVAADAVYTAPYVTDVIVIAPGQTIDALLFADQSVDTSYYMAAHPYASAPAVPFPNTTTRGVIHYGGASKT 216
Cdd:cd13880    80 GHNLTVIAADFVPIVPYTTDSLNIGIGQRYDVIVEANQDPVGNYWIRAEPATGCSGTNNNPDNRTGILRYDGASPT 155
CuRO_3_Fet3p cd13899
The third Cupredoxin domain of multicopper oxidase Fet3p; Fet3p catalyzes the ferroxidase ...
 344-450 1.04e-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: 108.11  E-value: 1.04e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063710373 344 STSAKILKFNTTVEVVLQNHAliaAESHPMHLHGFNFHVLAQGF---GNYDPSRDRSklNLVDPQSRNTLAVPVGGWAVI 420
Cdd:cd13899    54 QTNAFVLNHGEVVELVVNNWD---AGKHPFHLHGHKFQVVQRSPdvaSDDPNPPINE--FPENPMRRDTVMVPPGGSVVI 128

                          90       100       110
                  ....*....|....*....|....*....|
gi 1063710373 421 RFTANNPGAWIFHCHIDVHLPFGLGMIFVV 450
Cdd:cd13899   129 RFRADNPGVWFFHCHIEWHLEAGLAATFIE 158
CuRO_3_MCO_like_4 cd13910
The third cupredoxin domain of uncharacterized multicopper oxidase; Multicopper Oxidases (MCOs) ...
 355-450 1.58e-27

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: 107.77  E-value: 1.58e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063710373 355 TVEVVLQNhalIAAESHPMHLHGFNFHVLAQGFGNYD----PSRDRSKLNLVDPQSRNTLAVPVGGWAVIRFTANNPGAW 430
Cdd:cd13910    70 VVDLVINN---LDDGDHPFHLHGHKFWVLGSGDGRYGgggyTAPDGTSLNTTNPLRRDTVSVPGFGWAVLRFVADNPGLW 146

                          90       100
                  ....*....|....*....|
gi 1063710373 431 IFHCHIDVHLPFGLGMIFVV 450
Cdd:cd13910   147 AFHCHILWHMAAGMLMQFAV 166
CuRO_1_LCC_plant cd13849
The first cupredoxin domain of plant laccases; Laccase is a blue multicopper oxidase (MCO) ...
 1-47 5.83e-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: 104.65  E-value: 5.83e-27
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*..
gi 1063710373   1 MITQCPIQPGQRYAYRFNITGQEGTLWWHAHASFLRATVYGALVIRP 47
Cdd:cd13849    71 YITQCPIQPGQSYTYRFTVTGQEGTLWWHAHISWLRATVYGAFIIRP 117
PLN00044 PLN00044
multi-copper oxidase-related protein; Provisional
 3-430 8.23e-27

multi-copper oxidase-related protein; Provisional


Pssm-ID: 165622 [Multi-domain]  Cd Length: 596  Bit Score: 113.61  E-value: 8.23e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063710373   3 TQCPIQPGQRYAYRFNITGQEGTLWWHAHASFLRATV-YGALVIRPKSGHSYPFPKPHK-EVPILFGEWWNTDVVALEEA 80
Cdd:PLN00044  103 TNCAIPAGWNWTYQFQVKDQVGSFFYAPSTALHRAAGgYGAITINNRDVIPIPFGFPDGgDITLFIADWYARDHRALRRA 182

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063710373  81 aIATGVPPNNSDAYTING-----------RPGNLYPcskdrmfSLNVVKGKRYLLRIINAAMNIQLFFKIANHRLTVVAA 149
Cdd:PLN00044  183 -LDAGDLLGAPDGVLINAfgpyqyndslvPPGITYE-------RINVDPGKTYRFRVHNVGVATSLNFRIQGHNLLLVEA 254

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063710373 150 DAVYTAPYVTDVIVIAPGQTIDALLFADQSVDTSYYMAAHPyASAPAVPFPNTTTRGVIHYGGaSKTGRSKPvlMPKLP- 228
Cdd:PLN00044  255 EGSYTSQQNYTNLDIHVGQSYSFLLTMDQNASTDYYVVASA-RFVDAAVVDKLTGVAILHYSN-SQGPASGP--LPDAPd 330

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063710373 229 ----SFFDTLTAYRFYSNLTAlvNGPHWVPVPRYVDEEMLVTIGLGLEACADNTTCPKFSASMSNHSFVLPKKLSILEAV 304
Cdd:PLN00044  331 dqydTAFSINQARSIRWNVTA--SGARPNPQGSFHYGDITVTDVYLLQSMAPELIDGKLRATLNEISYIAPSTPLMLAQI 408

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063710373 305 FhDVKGIFTADFPDQPPVKFdytnPNVtqtnpgllftqkSTSAKILKFNTTVEVVLQNHaliAAESHPMHLHGFNFHVLA 384
Cdd:PLN00044  409 F-NVPGVFKLDFPNHPMNRL----PKL------------DTSIINGTYKGFMEIIFQNN---ATNVQSYHLDGYAFFVVG 468

                         410       420       430       440
                  ....*....|....*....|....*....|....*....|....*.
gi 1063710373 385 QGFGNYDpSRDRSKLNLVDPQSRNTLAVPVGGWAVIRFTANNPGAW 430
Cdd:PLN00044  469 MDYGLWT-DNSRGTYNKWDGVARSTIQVFPGAWTAILVFLDNAGIW 513
CuRO_2_Tv-LCC_like cd13882
The second cupredoxin domain of the fungal laccases similar to Tv-LCC from Trametes versicolor; ...
 64-213 9.88e-27

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: 105.57  E-value: 9.88e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063710373  64 ILFGEWWNTDVVALEeaAIATGVPPNnSDAYTINGRpGNLYPCSKDRMFSLNVVKGKRYLLRIINAAMNIQLFFKIANHR 143
Cdd:cd13882     3 ITLGDWYHTAAPDLL--ATTAGVPPV-PDSGTINGK-GRFDGGPTSPLAVINVKRGKRYRFRVINISCIPSFTFSIDGHN 78

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063710373 144 LTVVAADAVYTAPYVTDVIVIAPGQTIDALLFADQSVDTsYYMAAHPYASAPAVPfPNTTTRGVIHYGGA 213
Cdd:cd13882    79 LTVIEADGVETKPLTVDSVQIYAGQRYSVVVEANQPVDN-YWIRAPPTGGTPANN-GGQLNRAILRYKGA 146
PLN02792 PLN02792
oxidoreductase
 3-430 2.43e-26

oxidoreductase


Pssm-ID: 178389 [Multi-domain]  Cd Length: 536  Bit Score: 111.99  E-value: 2.43e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063710373   3 TQCPIQPGQRYAYRFNITGQEGTLWWHAHASFLRATV-YGALVIRPKSGHSYPFPKPHKEVPILFGEWWNTDVVALEEAA 81
Cdd:PLN02792   90 TTCPIPPGKNYTYDFQVKDQVGSYFYFPSLAVQKAAGgYGSLRIYSLPRIPVPFPEPAGDFTFLIGDWYRRNHTTLKKIL 169

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063710373  82 IATGVPPNNSDAYTINGRpgnlypcSKDRMFSLNVVKGKRYLLRIINAAMNIQLFFKIANHRLTVVAADAVYTAPYVTDV 161
Cdd:PLN02792  170 DGGRKLPLMPDGVMINGQ-------GVSYVYSITVDKGKTYRFRISNVGLQTSLNFEILGHQLKLIEVEGTHTVQSMYTS 242

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063710373 162 IVIAPGQTIDALLFADQSVDTSYYMAAHPYASAPAVpfpnttTRGVIHYGGaSKTGRSKPVLMPKLPSF-FDTLTAYRFY 240
Cdd:PLN02792  243 LDIHVGQTYSVLVTMDQPPQNYSIVVSTRFIAAKVL------VSSTLHYSN-SKGHKIIHARQPDPDDLeWSIKQAQSIR 315

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063710373 241 SNLTAlvNGPHWVPVPRYVDEEMLVTIGLGLEACADNTTcPKFSASMSNHSFVlPKKLSILEAVFHDVKGIF-TADFPDQ 319
Cdd:PLN02792  316 TNLTA--SGPRTNPQGSYHYGKMKISRTLILESSAALVK-RKQRYAINGVSFV-PSDTPLKLADHFKIKGVFkVGSIPDK 391

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063710373 320 PpvkfdytnpnvtQTNPGLlftQKSTSAKILKFNTTVEVVLQNHALIAaesHPMHLHGFNFHVLAQGFGNYDPSrDRSKL 399
Cdd:PLN02792  392 P------------RRGGGM---RLDTSVMGAHHNAFLEIIFQNREKIV---QSYHLDGYNFWVVGINKGIWSRA-SRREY 452

                         410       420       430
                  ....*....|....*....|....*....|.
gi 1063710373 400 NLVDPQSRNTLAVPVGGWAVIRFTANNPGAW 430
Cdd:PLN02792  453 NLKDAISRSTTQVYPESWTAVYVALDNVGMW 483
ascorbOXfungal TIGR03390
L-ascorbate oxidase, fungal type; This model describes a family of fungal ascorbate oxidases, ...
 1-452 3.76e-25

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: 108.39  E-value: 3.76e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063710373   1 MITQCPIQPGQRYAYRFNIT-GQEGTLWWHAHASFLRATVYGALVIRPKSGHSYPFpkpHKEVPILFGEWWNTDVVALEE 79
Cdd:TIGR03390  82 LASQWPIPPGHFFDYEIKPEpGDAGSYFYHSHVGFQAVTAFGPLIVEDCEPPPYKY---DDERILLVSDFFSATDEEIEQ 158

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063710373  80 AAIATG-VPPNNSDAYTINGRPGNL------YPCSKDRMFSLNVVKGKRYLLRIINAAMNIQLFFKIANHR-LTVVAADA 151
Cdd:TIGR03390 159 GLLSTPfTWSGETEAVLLNGKSGNKsfyaqiNPSGSCMLPVIDVEPGKTYRLRFIGATALSLISLGIEDHEnLTIIEADG 238

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063710373 152 VYTAPYVTDVIVIAPGQTIDALLFAD-----QSVDTSYYMAAHPYASAPAVpfpnTTTRGVIHYGGasktgrSKPVLMPK 226
Cdd:TIGR03390 239 SYTKPAKIDHLQLGGGQRYSVLFKAKtedelCGGDKRQYFIQFETRDRPKV----YRGYAVLRYRS------DKASKLPS 308

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063710373 227 LPSffdtltayrfysnltalvngPHWVPVPRYVDEEMLVTI-GLGLEAcadNTTCPKFSA-----SMSNHSFVLPKKLSI 300
Cdd:TIGR03390 309 VPE--------------------TPPLPLPNSTYDWLEYELePLSEEN---NQDFPTLDEvtrrvVIDAHQNVDPLNGRV 365

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063710373 301 LEAVFHDVkgiFTADFPDQPPVKFDYTN-----PNVTQTNPGLLFtQKSTSAKILKFNTTVEVVLQNHALI-----AAES 370
Cdd:TIGR03390 366 AWLQNGLS---WTESVRQTPYLVDIYENglpatPNYTAALANYGF-DPETRAFPAKVGEVLEIVWQNTGSYtgpngGVDT 441

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063710373 371 HPMHLHGFNFHVLAQGFGNYDPSRDRSKLNLVDPQSRNT-----LAVPV-----GGWAVIRFTANNPGAWIFHCHIDVHL 440
Cdd:TIGR03390 442 HPFHAHGRHFYDIGGGDGEYNATANEAKLENYTPVLRDTtmlyrYAVKVvpgapAGWRAWRIRVTNPGVWMMHCHILQHM 521

                         490
                  ....*....|..
gi 1063710373 441 PFGLGMIFVVKN 452
Cdd:TIGR03390 522 VMGMQTVWVFGD 533
CuRO_3_Diphenol_Ox cd13904
The third cupredoxin domain of fungal laccase, diphenol oxidase; Diphenol oxidase belongs to ...
 344-449 1.07e-23

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: 96.98  E-value: 1.07e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063710373 344 STSAKILKFNT--TVEVVLQNhaLIAAESHPMHLHGFNFHVLAQGFGNYDPSR-DRSKLNLVDPQSRNTLAVPVGGWAVI 420
Cdd:cd13904    51 SSEVASVTFPTdgWYDIVINN--LDPAIDHPYHLHGVDFHIVARGSGTLTLEQlANVQYNTTNPLRRDTIVIPGGSWAVL 128

                          90       100       110
                  ....*....|....*....|....*....|
gi 1063710373 421 RFTANNPGAWIFHCHIDVHLPFG-LGMIFV 449
Cdd:cd13904   129 RIPADNPGVWALHCHIGWHLAAGfAGVVVV 158
CuRO_3_Tv-LCC_like cd13903
The third cupredoxin domain of the fungal laccases similar to Tv-LCC from Trametes Versicolor; ...
 334-449 5.04e-23

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: 94.65  E-value: 5.04e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063710373 334 TNPGLLFTQKSTSakILKFNTTVEVVLqnHALIAAESHPMHLHGFNFHVLaQGFGNYDPsrdrsklNLVDPQSRNTLAV- 412
Cdd:cd13903    40 TSAEDLLPTESTI--ILPRNKVVEITI--PGGAIGGPHPFHLHGHAFSVV-RSAGSNTY-------NYVNPVRRDVVSVg 107

                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 1063710373 413 PVGGWAVIRFTANNPGAWIFHCHIDVHLPFGLGMIFV 449
Cdd:cd13903   108 TPGDGVTIRFVTDNPGPWFLHCHIDWHLEAGLAVVFA 144
CuRO_3_Abr2_like cd13898
The third cupredoxin domain of a group of fungal Laccases similar to Abr2 from Aspergillus ...
 309-448 4.22e-22

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: 92.71  E-value: 4.22e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063710373 309 KGIFTADFPDQPPVKFDYTNPNVTQTNPGLlftqkSTsakilKFNTTVEVVLQNHALIAAeSHPMHLHGFNFHVLAQGFG 388
Cdd:cd13898    22 TELYPLDEEAYPPLLFLPDPATALDSALTI-----ST-----KNGTWVDLIFQVTGPPQP-PHPIHKHGNKAFVIGTGTG 90

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1063710373 389 NYDPS-------RDRSKLNLVDPQSR---NTLAVPVGG-WAVIRFTANNPGAWIFHCHIDVHLPFGLGMIF 448
Cdd:cd13898    91 PFNWSsvaeaaeAAPENFNLVNPPLRdtfTTPPSTEGPsWLVIRYHVVNPGAWLLHCHIQSHLAGGMAVVL 161
CuRO_2_MCO_like_1 cd13886
The second cupredoxin domain of uncharacterized multicopper oxidase; Multicopper Oxidases ...
 64-211 3.45e-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 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: 84.25  E-value: 3.45e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063710373  64 ILFGEWWNTDVVALEEAAIATGVPPN--NSDAYTINGRpgNLYPCSKDRM-----------FSLNVVKGKRYLLRIINAA 130
Cdd:cd13886     3 VMVNDYYHDPSSVLLARYLAPGNEGDepVPDNGLINGI--GQFDCASATYkiyccasngtyYNFTLEPNKTYRLRLINAG 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063710373 131 MNIQLFFKIANHRLTVVAADAVYTAPYVTDVIVIAPGQTIDALLFADQSVDTSYYMAAH--PYASAPAVPFPNTTTRGVI 208
Cdd:cd13886    81 SFADFTFSVDGHPLTVIEADGTLVEPVEVHSITISVAQRYSVILTTNQPTGGNFWMRAElnTDCFTYDNPNLDPDVRAIV 160


                  ...
gi 1063710373 209 HYG 211
Cdd:cd13886   161 SYT 163
Cu-oxidase_3 pfam07732
Multicopper oxidase; This entry contains many divergent copper oxidase-like domains that are ...
 1-50 6.76e-19

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: 82.29  E-value: 6.76e-19
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1063710373   1 MITQCPIQPGQRYAYRFNITGQEGTLWWHAHASFLR-ATVYGALVIRPKSG 50
Cdd:pfam07732  69 GVTQCPIPPGQSFTYRFQVKQQAGTYWYHSHTSGQQaAGLAGAIIIEDRAS 119
CuRO_2_Fet3p_like cd13877
The second Cupredoxin domain of multicopper oxidase Fet3P; Fet3p catalyzes the ferroxidase ...
 110-186 9.57e-18

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: 79.90  E-value: 9.57e-18
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1063710373 110 RMFSLNVVKGKRYLLRIINAAMNIQLFFKIANHRLTVVAADAVYTAPYVTDVIVIAPGQTIDALLFADQSVDTSYYM 186
Cdd:cd13877    44 QNATINFEPGKTYLLRIINMGAFASQYFHIEGHDMTIIEVDGVYVKPYPVDTLYIAVGQRYSVLVKAKNDTDRNYAI 120
CuRO_2_tcLCC_insect_like cd13884
The second cupredoxin domain of the insect laccases similar to laccase 2 in Tribolium ...
 61-210 5.71e-17

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: 77.66  E-value: 5.71e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063710373  61 EVPILFGEWWNTDVVALEEAaIATGVPPNNSDAYTINGRpGNLYPCSKD-----RMFSLNVVKGKRYLLRIINAAMNIQL 135
Cdd:cd13884     1 EHVILIQDWTHELSSERFVG-RGHNGGGQPPDSILINGK-GRYYDPKTGntnntPLEVFTVEQGKRYRFRLINAGATNCP 78

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1063710373 136 F-FKIANHRLTVVAADAVYTAPYVTDVIVIAPGQTIDALLFADQSVDtSYYMAAHPYASApavPFPNTTTRGVIHY 210
Cdd:cd13884    79 FrVSIDGHTLTVIASDGNDVEPVEVDSIIIYPGERYDFVLNANQPIG-NYWIRARGLEDC---DNRRLQQLAILRY 150
CuRO_3_AAO_like_2 cd13895
The third cupredoxin domain of Ascorbate oxidase homologs; This family includes fungal ...
 351-449 5.89e-16

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: 75.82  E-value: 5.89e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063710373 351 KFNTTVEVVLQNHALIAA--ESHPMHLHGFNFHVLAQGFGNYDPSRDRS--KLNLVDPQSRNTLAV-------------P 413
Cdd:cd13895    71 KLGEVLDIVWQNTASPTGglDAHPWHAHGAHYYDLGSGLGTYSATALANeeKLRGYNPIRRDTTMLyryggkgyypppgT 150

                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 1063710373 414 VGGWAVIRFTANNPGAWIFHCHIDVHLPFGLGMIFV 449
Cdd:cd13895   151 GSGWRAWRLRVDDPGVWMLHCHILQHMIMGMQTVWV 186
CuRO_3_CopA cd13896
The third cupredoxin domain of CopA copper resistance protein family; CopA is a multicopper ...
 356-450 8.30e-16

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: 73.44  E-value: 8.30e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063710373 356 VEVVLQNHALIAaesHPMHLHGFNFHVLAqGFGNYDPSRDrsklnlvdpqsrnTLAVPVGGWAVIRFTANNPGAWIFHCH 435
Cdd:cd13896    38 VRIVFVNDTMMA---HPMHLHGHFFQVEN-GNGEYGPRKD-------------TVLVPPGETVSVDFDADNPGRWAFHCH 100

                          90
                  ....*....|....*
gi 1063710373 436 IDVHLpfGLGMIFVV 450
Cdd:cd13896   101 NLYHM--EAGMMRVV 113
CuRO_D2_2dMcoN_like cd04202
The second cupredoxin domain of bacterial two domain multicopper oxidase McoN and similar ...
 368-439 1.10e-15

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: 73.83  E-value: 1.10e-15
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1063710373 368 AESHPMHLHGFNFHVLAQGFGNYDPSrdrsklnlvDPQSRNTLAVPVGGWAVIRFTANNPGAWIFHCHIDVH 439
Cdd:cd04202    60 MDHHPMHLHGHFFLVTATDGGPIPGS---------APWPKDTLNVAPGERYDIEFVADNPGDWMFHCHKLHH 122
CuRO_2_AAO_like_1 cd13872
The second cupredoxin domain of plant pollen multicopper oxidase homologous to ascorbate ...
 61-210 1.62e-15

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: 73.21  E-value: 1.62e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063710373  61 EVPILFGEWWNTDVVALEeAAIATGVPPNNSDAYTINGRPGNLYPCSKDrmfSLNVVKGKRYLLRIINAAMNIQLFFKIA 140
Cdd:cd13872     2 EYTVLIGDWYKTDHKTLR-QSLDKGRTLGRPDGILINGKGPYGYGANET---SFTVEPGKTYRLRISNVGLRTSLNFRIQ 77

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063710373 141 NHRLTVVAADAVYTAPYVTDVIVIAPGQTIDALLFADQSvDTSYYMAAHPYASAPAVpfpntTTRGVIHY 210
Cdd:cd13872    78 GHKMLLVETEGSYTAQNTYDSLDVHVGQSYSVLVTADQS-PKDYYIVASSRFLSPEL-----TGVAILHY 141
CuRO_2_AAO cd13871
The second cupredoxin domain of plant Ascorbate oxidase; Ascorbate oxidase catalyzes the ...
 61-198 1.05e-14

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: 71.81  E-value: 1.05e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063710373  61 EVPILFGEWWNTDV----VALEEAAIA-TGVPpnnsDAYTINGR-----------PGNLYP--CSKDR----MFSLNVVK 118
Cdd:cd13871     3 ELNILLSDWWHKSIyeqeTGLSSKPFRwVGEP----QSLLIEGRgryncslapayPSSLPSpvCNKSNpqcaPFILHVSP 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063710373 119 GKRYLLRIINAAMNIQLFFKIANHRLTVVAADAVYTAPYVTDVIVIAPGQTIDALLFADQSVDTSYYMAAHPYASAPAVP 198
Cdd:cd13871    79 GKTYRLRIASVTALSSLNFIIEGHNLTVVEADGNYVQPFEVSNLDIYSGETYSVLVTADQDPSRNYWVSVNVRGRRPNTP 158
CuRO_1_tcLCC2_insect_like cd13858
The first cupredoxin domain of insect laccases similar to laccase 2 in Tribolium castaneum; ...
 1-46 1.92e-14

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: 69.10  E-value: 1.92e-14
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*..
gi 1063710373   1 MITQCPIQPGQRYAYRFnITGQEGTLWWHAHASFLRA-TVYGALVIR 46
Cdd:cd13858    60 MVTQCPILPGQTFRYKF-KADPAGTHWYHSHSGTQRAdGLFGALIVR 105
CuRO_3_AAO_like_1 cd13894
The third cupredoxin domain of plant Ascorbate oxidase homologs; This subfamily is composed of ...
 295-430 5.24e-14

The third 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 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. This subfamily does not harbor T1 copper or trinuclear copper binding sites.


Pssm-ID: 259961 [Multi-domain]  Cd Length: 123  Bit Score: 68.61  E-value: 5.24e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063710373 295 PKKLsileAVFHDVKGIFTADFPDQPPVKFD-YTNPNVTQTNpgllftqkstsakilkFNTTVEVVLQNHaLIAAEShpM 373
Cdd:cd13894     5 PLKL----ADYFKIKGVFQLDSIPDPPTRKTpYLGTSVINGT----------------YRGFIEIVFQNN-EDTVQS--W 61

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1063710373 374 HLHGFNFHVLAQGFGNYDPSRdRSKLNLVDPQSRNTLAVPVGGWAVIRFTANNPGAW 430
Cdd:cd13894    62 HLDGYSFFVVGMGFGDWTPEK-RKSYNLLDAVSRSTTQVYPGSWTAILLELDNVGMW 117
CuRO_1_LCC_like cd04206
Cupredoxin domain 1 of laccase-like multicopper oxidases; including laccase, CueO, spore coat ...
 2-46 8.72e-14

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: 67.70  E-value: 8.72e-14
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*.
gi 1063710373   2 ITQCPIQPGQRYAYRFNITGQEGTLWWHAHASFLRA-TVYGALVIR 46
Cdd:cd04206    75 LTQCPIPPGESFTYRFTVDDQAGTFWYHSHVGGQRAdGLYGPLIVE 120
CuRO_1_Diphenol_Ox cd13857
The first cupredoxin domain of fungal laccase, diphenol oxidase; Diphenol oxidase belongs to ...
 2-45 9.10e-14

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: 67.67  E-value: 9.10e-14
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*
gi 1063710373   2 ITQCPIQPGQRYAYRFNITGQEGTLWWHAHASFLRAT-VYGALVI 45
Cdd:cd13857    74 ITQCPIPPGGSFTYNFTVDGQYGTYWYHSHYSTQYADgLVGPLIV 118
CuRO_2_AAO_like_2 cd13873
The second cupredoxin domain of plant Ascorbate oxidase homologs; This family includes plant ...
 61-174 3.39e-11

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: 61.53  E-value: 3.39e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063710373  61 EVPILFGEWWNTDVVALEEAAIATG-VPPNNSDAYTINGRPGN------LYPCSKD-RMFSLNVVKGKRYLLRIINAAMN 132
Cdd:cd13873     2 ERILLFSDYFPKTDSTIETGLTATPfVWPGEPNALLVNGKSGGtcnksaTEGCTTScHPPVIDVEPGKTYRFRFIGATAL 81

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|...
gi 1063710373 133 IQLFFKIANH-RLTVVAADAVYTAPYVTDVIVIAPGQTIDALL 174
Cdd:cd13873    82 SFVSLGIEGHdNLTIIEADGSYTKPAETDHLQLGSGQRYSFLL 124
CuRO_3_CumA_like cd13906
The third cupredoxin domain of CumA like multicopper oxidase; This multicopper oxidase (MCO) ...
 371-444 1.45e-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: 58.93  E-value: 1.45e-10
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1063710373 371 HPMHLHGFNFHVLaqgfgnydpSRDRSKLNLvdPQSRNTLAVPVGGWAVIRFTANNPGAWIFHCHIDVHLPFGL 444
Cdd:cd13906    69 HPMHLHGHFFRVL---------SRNGRPVPE--PFWRDTVLLGPKETVDIAFVADNPGDWMFHCHILEHQETGM 131
CuRO_2_Diphenol_Ox cd13883
The second cupredoxin domain of fungal laccase, diphenol oxidase; Diphenol oxidase belongs to ...
 114-210 2.19e-10

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: 59.28  E-value: 2.19e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063710373 114 LNVVKGKRYLLRIINAAMNIQLFFKIANHRLTVVAADA--VYTAPYVTDVIvIAPGQTIDALLFADQ-SVDTSYYMAAHP 190
Cdd:cd13883    65 IQVEAGKRTRFRLINAGSHAMFRFSVDNHTLNVVEADDtpVYGPTVVHRIP-IHNGQRYSVIIDTTSgKAGDSFWLRARM 143

                          90       100
                  ....*....|....*....|
gi 1063710373 191 YASAPAVPFPNTTTRGVIHY 210
Cdd:cd13883   144 ATDCFAWDLQQQTGKAILRY 163
CuRO_3_MCO_like_3 cd13909
The third cupredoxin domain of uncharacterized multicopper oxidase; Multicopper Oxidases (MCOs) ...
 371-450 3.30e-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: 259976 [Multi-domain]  Cd Length: 137  Bit Score: 57.91  E-value: 3.30e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063710373 371 HPMHLHGFNFHVLAQGfGNYDPSRDrsklnlvdpqsrnTLAVPVGGWAVIRFTANNPGAWIFHCHIDVHLPFGLGMIFVV 450
Cdd:cd13909    71 HGMHLHGHHFRAILPN-GALGPWRD-------------TLLMDRGETREIAFVADNPGDWLLHCHMLEHAAAGMMSWFRV 136
CuRO_3_McoC_like cd13902
The third cupredoxin domain of a multicopper oxidase McoC and similar proteins; This family ...
 371-449 1.62e-09

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: 55.87  E-value: 1.62e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063710373 371 HPMHLHGFNFHVLAQgfgNYDPSRDRSKLNlvdpqsRNTLAVPVGGWAVIRFTANNPGAWIFHCHIDVHLPFG-LGMIFV 449
Cdd:cd13902    55 HPFHLHGTQFQVLEI---DGNPQKPEYRAW------KDTVNLPPGEAVRIATRQDDPGMWMYHCHILEHEDAGmMGMLHV 125
CuRO_1_Fet3p cd13851
The first Cupredoxin domain of multicopper oxidase Fet3P; Fet3p catalyzes the ferroxidase ...
 1-31 2.01e-09

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: 55.35  E-value: 2.01e-09
                          10        20        30
                  ....*....|....*....|....*....|.
gi 1063710373   1 MITQCPIQPGQRYAYRFNITGQEGTLWWHAH 31
Cdd:cd13851    75 GVTQCPIPPGQSFTYEFTVDTQVGTYWYHSH 105
CuRO_1_Abr2_like cd13850
The first cupredoxin domain of a group of fungal Laccases similar to Abr2 from Aspergillus ...
 2-46 2.82e-09

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: 54.61  E-value: 2.82e-09
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*....
gi 1063710373   2 ITQCPIQPGQRYAYRFNITGQEGTLWWHAHasfLRAT----VYGALVIR 46
Cdd:cd13850    72 VTQWPIQPGGSFTYRWKAEDQYGLYWYHSH---YRGYymdgLYGPIYIR 117
CuRO_2_CopA_like_1 cd13870
The second cupredoxin domain of CopA copper resistance protein like family; The members of ...
 94-180 4.18e-09

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: 54.26  E-value: 4.18e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063710373  94 YTINGRPgnlypcsKDRMFSLNVVKGKRYLLRIINAAMNIQLFFKIANHRLTVVAADAVYTAPYVTDVIVIAPGQTIDAL 173
Cdd:cd13870    18 YLINGRP-------PEDPAVFTARPGDRLRLRLINAAGDTAFRVALAGHRLTVTHTDGFPVEPVEVDALLIGMGERYDAI 90


                  ....*..
gi 1063710373 174 LFADQSV 180
Cdd:cd13870    91 VTANNGI 97
CuRO_2_CumA_like cd13885
The second cupredoxin domain of CumA like multicopper oxidase; This multicopper oxidase (MCO) ...
 94-196 1.29e-08

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: 53.10  E-value: 1.29e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063710373  94 YTINGRPgnlyPCSkdrmfsLNVVKGKRYLLRIINAAmNIQLF-FKIANHRLTVVAADAVYTAPYVTD--VIVIAPGQTI 170
Cdd:cd13885    38 YTINGRV----QPD------FTVRAGERVRLRLINAA-NARVFaLKFPGHEARVIALDGQPAEPFVARngAVVLAPGMRI 106

                          90       100
                  ....*....|....*....|....*.
gi 1063710373 171 DALLFADQSVDTSYYMAAHPYASAPA 196
Cdd:cd13885   107 DLVIDAPQAAGTRFAVLDHDGRRAAP 132
CuRO_2_Abr2_like cd13876
The second cupredoxin domain of a group of fungal Laccases similar to Abr2 from Aspergillus ...
 63-178 1.51e-08

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: 53.36  E-value: 1.51e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063710373  63 PILFGEWWNTDVVALEEAAIATGVPPNNSDAYTINGrpgnlypcsKDRMFSLNVV--KGKRYL-LRIINAAMNIQLFFKI 139
Cdd:cd13876     2 PIILSDWRHLTSEEYWKIMRASGIEPFCYDSILING---------KGRVYCLIVIvdPGERWVsLNFINAGGFHTLAFSI 72

                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 1063710373 140 ANHRLTVVAADAVYTAPYVTDVIVIAPGQTIDALLFADQ 178
Cdd:cd13876    73 DEHPMWVYAVDGGYIEPQLVDAISITNGERYSVLVKLDK 111
CuRO_1_MaLCC_like cd13854
The first cupredoxin domain of the fungal laccases similar to Ma-LCC from Melanocarpus ...
 2-45 4.97e-08

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: 51.47  E-value: 4.97e-08
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*
gi 1063710373   2 ITQCPIQPGQRYAYRFNITgQEGTLWWHAHASFLRAT-VYGALVI 45
Cdd:cd13854    78 VTECPIAPGDTRTYRFRAT-QYGTSWYHSHYSAQYGDgVVGPIVI 121
CuRO_1_Tv-LCC_like cd13856
The first cupredoxin domain of fungal laccases similar to Tv-LCC from Trametes versicolor; ...
 1-45 8.29e-08

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: 50.80  E-value: 8.29e-08
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|
gi 1063710373   1 MITQCPIQPGQRYAYRFNITGQEGTLWWHAHASF-----LRatvyGALVI 45
Cdd:cd13856    78 FVTQCPIAPNHSFTYDFTAGDQAGTFWYHSHLSTqycdgLR----GPLVI 123
CuRO_3_MCO_like_2 cd13908
The third cupredoxin domain of uncharacterized multicopper oxidase; Multicopper Oxidases (MCOs) ...
 369-448 1.47e-07

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: 50.14  E-value: 1.47e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063710373 369 ESHPMHLHGFNFHVlAQGFGNydpsrdrsklnlvdPQS---RNTLAVPVGGWAVIRFTANNPGAWIFHCHIDVHLPFGLG 445
Cdd:cd13908    53 DAHPMHLHRHTFEV-TRIDGK--------------PTSglrKDVVMLGGYQRVEVDFVADNPGLTLFHCHQQLHMDYGFM 117


                  ...
gi 1063710373 446 MIF 448
Cdd:cd13908   118 ALF 120
CuRO_2_CopA cd13874
The second cupredoxin domain of CopA copper resistance protein family; CopA is a multicopper ...
 92-189 1.66e-07

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: 49.60  E-value: 1.66e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063710373  92 DAYTINGRPgnlypcsKDRMFSLNVVKGKRYLLRIINAAMNIQLFFKIANHRLTVVAADAVYTAPYVTDVIVIAPGQTID 171
Cdd:cd13874    12 DTYLINGKP-------PEDNWTGLFKPGERVRLRFINAAASTYFDVRIPGGKMTVVAADGQDVRPVEVDEFRIGVAETYD 84

                          90       100
                  ....*....|....*....|....*...
gi 1063710373 172 AL----------LFAdQSVDTSYYMAAH 189
Cdd:cd13874    85 VIvtipengaytIRA-TSQDRSGYASGT 111
CuRO_2_McoC_like cd13881
The second cupredoxin domain of a multicopper oxidase McoC and similar proteins; This family ...
 85-191 2.26e-06

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: 47.22  E-value: 2.26e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063710373  85 GVPPNNSDAYTINGRPGNLYPCSKDRMFSLNVVKGKRYLLRIINAAMNIqlFFKIA--NHRLTVVAADA-VYTAPYVTDV 161
Cdd:cd13881    15 GQLAEPSAADWMFGREGDLVLVNGQLNPTITVRPGEVQRWRIVNAASAR--YFRLAldGHKFRLIGTDGgLLEAPREVDE 92

                          90       100       110
                  ....*....|....*....|....*....|
gi 1063710373 162 IVIAPGQTIDALLFADQSvDTSYYMAAHPY 191
Cdd:cd13881    93 LLLAPGERAEVLVTAGEP-GGRLVLLALPY 121
CuRO_1_AAO_like_2 cd13847
The first cupredoxin domain of Ascorbate oxidase homologs; This family includes fungal ...
 1-45 8.05e-06

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: 44.83  E-value: 8.05e-06
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*.
gi 1063710373   1 MITQCPIQPGQRYAYRFNIT-GQEGTLWWHAHASFLRATVYGALVI 45
Cdd:cd13847    70 LASQWPIPPGKFFDYEFPLEaGDAGTYYYHSHVGFQSVTAYGALIV 115
CuRO_3_Tth-MCO_like cd13900
The third cupredoxin domain of the bacterial laccases similar to Tth-MCO from Thermus ...
 350-451 1.50e-05

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: 44.16  E-value: 1.50e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063710373 350 LKFNTTVEVVLQNHAliaAESHPMHLHGFNFHVLAqgfGNYDPSRDrsklnlvdPQSRNTLAVPVGGWAVIR-----FTa 424
Cdd:cd13900    36 VRLGTVEEWTLINTS---GEDHPFHIHVNPFQVVS---INGKPGLP--------PVWRDTVNVPAGGSVTIRtrfrdFT- 100

                          90       100       110
                  ....*....|....*....|....*....|.
gi 1063710373 425 nnpGAWIFHCHI----DvhlpfgLGMIFVVK 451
Cdd:cd13900   101 ---GEFVLHCHIldheD------QGMMQVVE 122
CuRO_1_CopA cd13848
The first cupredoxin domain of CopA copper resistance protein family; CopA is a multicopper ...
 2-45 1.71e-05

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: 43.81  E-value: 1.71e-05
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*
gi 1063710373   2 ITQCPIQPGQRYAYRFNITgQEGTLWWHAHASFLRAT-VYGALVI 45
Cdd:cd13848    72 LSFPGIKPGETFTYRFPVR-QSGTYWYHSHSGLQEQTgLYGPIII 115
CuRO_2_MCO_like_2 cd13887
The second cupredoxin domain of uncharacterized multicopper oxidase; Multicopper Oxidases ...
 116-174 2.68e-05

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: 43.47  E-value: 2.68e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1063710373 116 VVKGKRYLLRIINAAMNIQLFFKIANHRLTVVAADAVYTAPYVTDVIVIAPGQTIDALL 174
Cdd:cd13887    28 VEPGGRVRLRVINGSTATNFHIDLGDLKGTLIAVDGNPVQPVEGRRFPLATAQRLDLLV 86
CuRO_D2_2dMcoN_like cd04202
The second cupredoxin domain of bacterial two domain multicopper oxidase McoN and similar ...
 59-177 2.99e-05

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: 43.78  E-value: 2.99e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063710373  59 HKEVPILFGEWwntdvvALEEAAIATGVPPNNSDAYTINGRPgnlYPcskdRMFSLNVVKGKRYLLRIINAAMNIQLFfK 138
Cdd:cd04202     1 DRDYTLVLQEW------FVDPGTTPMPPEGMDFNYFTINGKS---FP----ATPPLVVKEGDRVRIRLINLSMDHHPM-H 66

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 1063710373 139 IANHRLTVVAADAVY---TAPYVTDVIVIAPGQTIDALLFAD 177
Cdd:cd04202    67 LHGHFFLVTATDGGPipgSAPWPKDTLNVAPGERYDIEFVAD 108
CuRO_1_2dMco_1 cd13860
The first cupredoxin domain of bacteria two domain multicopper oxidase; This subfamily ...
 2-46 5.81e-05

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: 42.57  E-value: 5.81e-05
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*...
gi 1063710373   2 ITQCPIQPGQRYAYRFNITgQEGTLWWHAHASFLR---ATVYGALVIR 46
Cdd:cd13860    73 ITQPPIQPGETFTYEFTAK-QAGTYMYHSHVDEAKqedMGLYGAFIVH 119
CuRO_1_AAO cd13845
The first cupredoxin domain of plant Ascorbate oxidase; Ascorbate oxidase catalyzes the ...
 2-47 5.87e-05

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: 42.43  E-value: 5.87e-05
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*..
gi 1063710373   2 ITQCPIQPGQRYAYRFnITGQEGTLWWHAHASFLR-ATVYGALVIRP 47
Cdd:cd13845    75 VSQCPINPGETFTYQF-VVDRPGTYFYHGHYGMQRsAGLYGSLIVDP 120
CuRO_1_LCC_like_3 cd13865
The second cupredoxin domain of uncharacterized multicopper oxidase; Multicopper Oxidases ...
 2-47 1.63e-04

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: 41.14  E-value: 1.63e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*..
gi 1063710373   2 ITQCPIQPGQRYAYRFNItGQEGTLWWHAHASFLRATVYGA-LVIRP 47
Cdd:cd13865    70 VTQPPIPPGQSQRYDFPL-VQPGTFWMHSHYGLQEQKLLAApLIIRS 115
Cupredoxin cd00920
Cupredoxin superfamily; Cupredoxins contain type I copper centers and are involved in ...
 335-448 2.91e-04

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: 40.29  E-value: 2.91e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063710373 335 NPGLLFTQKSTSAKIlkfNTTVEVVLQNHAliaAESHPMHLHGFNFHVLAQGFGNydpsrdrsklnlvDPQSRNTLAVPV 414
Cdd:cd00920    15 NGVLLFGPPVLVVPV---GDTVRVQFVNKL---GENHSVTIAGFGVPVVAMAGGA-------------NPGLVNTLVIGP 75

                          90       100       110
                  ....*....|....*....|....*....|....*
gi 1063710373 415 GGWAVIRFTANNPGAWIFHCHIDVHL-PFGLGMIF 448
Cdd:cd00920    76 GESAEVTFTTDQAGVYWFYCTIPGHNhAGMVGTIN 110
CuRO_3_McoP_like cd13888
The third cupredoxin domain of multicopper oxidase McoP and similar proteins; This subfamily ...
 349-451 5.26e-04

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: 40.24  E-value: 5.26e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063710373 349 ILKFNTTVEVV-LQNHAliAAESHPMHLHGFNFHVLAQGFG---NYDPSRDRSKLNLVDPQSRNTLAVPVGGWA--VIRF 422
Cdd:cd13888    31 VERVGGTVEIWeLVNDA--ASMPHPMHIHGFQFQVLERSDSppqVAELAVAPSGRTATDLGWKDTVLVWPGETVriAVDF 108

                          90       100       110
                  ....*....|....*....|....*....|.
gi 1063710373 423 TANNPGA--WIFHCHIDVHLPFGLGMIFVVK 451
Cdd:cd13888   109 THDYPGDqlYLLHCHNLEHEDDGMMVNVRVP 139
CuRO_1_CuNIR cd11020
Cupredoxin domain 1 of Copper-containing nitrite reductase; Copper-containing nitrite ...
 355-449 6.63e-04

Cupredoxin domain 1 of Copper-containing nitrite reductase; Copper-containing nitrite reductase (CuNIR), which catalyzes the reduction of NO2- to NO, is the key enzyme in the denitrification process in denitrifying bacteria. CuNIR contains at least one type 1 copper center and a type 2 copper center, which serves as the active site of the enzyme. A histidine, bound to the Type 2 Cu center, is responsible for binding and reducing nitrite. A Cys-His bridge plays an important role in facilitating rapid electron transfer from the type 1 center to the type 2 center. A reduced type I blue copper protein (pseudoazurin) was found to be a specific electron transfer donor for the copper-containing NIR in bacteria Alcaligenes faecalis.


Pssm-ID: 259906 [Multi-domain]  Cd Length: 119  Bit Score: 39.50  E-value: 6.63e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063710373 355 TVEVVLQNHaliaaESHPMHlHGFNFHVlAQGfgnydpsrdrsklnlvdPQSRNTLAVPVGGWAVIRFTANNPGAWIFHC 434
Cdd:cd11020    42 TVELTLTNP-----GTNTMP-HSIDFHA-ATG-----------------PGGGEFTTIAPGETKTFSFKALYPGVFMYHC 97

                          90
                  ....*....|....*....
gi 1063710373 435 ---HIDVHLPFGL-GMIFV 449
Cdd:cd11020    98 ataPVLMHIANGMyGAIIV 116
CuRO_3_MCO_like_2 cd13908
The third cupredoxin domain of uncharacterized multicopper oxidase; Multicopper Oxidases (MCOs) ...
 89-182 1.12e-03

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: 38.97  E-value: 1.12e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063710373  89 NNSDAYTINGRPgnlYPcSKDRMFSLNvvKGKRYLLRIINAAMNIQLFfKIANHRLTVVAADAVYTAPYVTDVIVIAPGQ 168
Cdd:cd13908    16 GGFNLWTINGKS---YP-DEDPPLVVQ--QGRRYRLVFRNASDDAHPM-HLHRHTFEVTRIDGKPTSGLRKDVVMLGGYQ 88

                          90
                  ....*....|....
gi 1063710373 169 TIDALLFADQSVDT 182
Cdd:cd13908    89 RVEVDFVADNPGLT 102
CuRO_1_McoP_like cd13852
The first cupredoxin domain of multicopper oxidase McoP and similar proteins; This family ...
 7-43 1.19e-03

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: 38.42  E-value: 1.19e-03
                          10        20        30
                  ....*....|....*....|....*....|....*...
gi 1063710373   7 IQPGQRYAYRFNITGQEGTLWWHAHASFLRAT-VYGAL 43
Cdd:cd13852    68 IDPGETYVYEFEVLNRAGTYWYHPHPHGLTAKqVYRGL 105
CuRO_3_MCO_like_5 cd13911
The third cupredoxin domain of uncharacterized multicopper oxidase; Multicopper Oxidases (MCOs) ...
 324-435 1.55e-03

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: 38.30  E-value: 1.55e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063710373 324 FDYTNPNVTQTNPGLLFTQKSTSAKIlKFNTTVEVVLQnhaliAAESHPMHLHGFNFHVLAQGFGNYDPSrdrsklnlvD 403
Cdd:cd13911     8 FAGDGQGDMWTVNGKVFDPDHIAARP-RLGTTEIWVFS-----SDGRHPVHLHGAHFQVVSRTGGRPGEW---------D 72

                          90       100       110
                  ....*....|....*....|....*....|....
gi 1063710373 404 PQSRNTLAVPVGGWA--VIRFTANNpGAWIFHCH 435
Cdd:cd13911    73 AGWKDTVLLRPRESVtvIIRFDGYR-GRYVFHCH 105
CuRO_3_MCO_like_1 cd13907
The third cupredoxin domain of uncharacterized multicopper oxidase; Multicopper Oxidases (MCOs) ...
 371-435 3.77e-03

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: 37.85  E-value: 3.77e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1063710373 371 HPMHLHGFNFHVLAQGFGNYDPSRDRS-KLNLVDPQSRNT-LAVPVGGWAVIRFTANNPGAWIFHCH 435
Cdd:cd13907    72 HPIHLHGVQFQVLERSVGPKDRAYWATvKDGFIDEGWKDTvLVMPGERVRIIKPFDDYKGLFLYHCH 138
CuRO_1_AAO_like_1 cd13846
The first cupredoxin domain of plant Ascorbate oxidase homologs; This subfamily is composed of ...
 3-45 6.28e-03

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: 36.62  E-value: 6.28e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....
gi 1063710373   3 TQCPIQPGQRYAYRFNITGQEGTLWWHAHASFLRAT-VYGALVI 45
Cdd:cd13846    74 TNCPIPPGWNWTYKFQVKDQIGSFFYFPSLHFQRAAgGFGGIRV 117
CuRO_D1_2dMcoN_like cd13859
The first cupredoxin domain of bacterial two domain multicopper oxidase McoN and similar ...
 2-31 8.40e-03

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: 36.30  E-value: 8.40e-03
                          10        20        30
                  ....*....|....*....|....*....|
gi 1063710373   2 ITQCPIQPGQRYAYRFnITGQEGTLWWHAH 31
Cdd:cd13859    75 VTQPAIEPGESFTYKF-KAERPGTLWYHCH 103
 
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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