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Conserved domains on  [gi|1063730442|ref|NP_001330377|]
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laccase 13 [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 ...
 2-484 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: 709.58  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063730442   2 RNPWADGPEYITQCPIQPGGSYTYRFTMEDQEGTLWWHAHSRWLRATVYGALIIRPPLSSPhYPFPViPKREITLLLGEW 81
Cdd:TIGR03389  67 RNGWADGPAYITQCPIQPGQSYVYNFTITGQRGTLWWHAHISWLRATVYGAIVILPKPGVP-YPFPK-PDREVPIILGEW 144

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063730442  82 WDRNPMDVLNLAQFTGAAPNISDAFTINGQPGDLYRCSSQETLRFLVGSGEIVLLRVINSALNQELFFGVANHKLTVVAA 161
Cdd:TIGR03389 145 WNADVEAVINQANQTGGAPNVSDAYTINGHPGPLYNCSSKDTFKLTVEPGKTYLLRIINAALNDELFFAIANHTLTVVEV 224

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063730442 162 DASYTKPFSTNVIMLGPGQTTDVLLTADQPPAHYYMAAHAYNSANAAFDNTTTTAILKYKDASCvtlqaksQARAIPAQL 241
Cdd:TIGR03389 225 DATYTKPFKTKTIVIGPGQTTNVLLTADQSPGRYFMAARPYMDAPGAFDNTTTTAILQYKGTSN-------SAKPILPTL 297

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063730442 242 PGFNDTATAAAFTAQMKSPSK----VKVPLEIDENLFFTVGLGLFNCPTpntQRCQGPNGTRFTASINNVSFVFPKqNSI 317
Cdd:TIGR03389 298 PAYNDTAAATNFSNKLRSLNSaqypANVPVTIDRRLFFTIGLGLDPCPN---NTCQGPNGTRFAASMNNISFVMPT-TAL 373

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063730442 318 MQAYYQGTPtGVFTTDFPPTPPVTFDYTGNVSRGLWQPTRGTKAYKLKFNSQVQIILQDTSIVTTENHPMHLHGYEFYVV 397
Cdd:TIGR03389 374 LQAHYFGIS-GVFTTDFPANPPTKFNYTGTNLPNNLFTTNGTKVVRLKFNSTVELVLQDTSILGSENHPIHLHGYNFFVV 452

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063730442 398 GTGVGNFNPNTDTSSFNLIDPPRRNTIGTPPGGWVAIRFVANNPGAWLMHCHIDSHIFWGLAMVFLVENGEGHLQSVQSP 477
Cdd:TIGR03389 453 GTGFGNFDPKKDPAKFNLVDPPERNTVGVPTGGWAAIRFVADNPGVWFMHCHLEVHTTWGLKMAFLVDNGKGPNQSLLPP 532


                  ....*..
gi 1063730442 478 PLDLPQC 484
Cdd:TIGR03389 533 PSDLPSC 539
 
Name Accession Description Interval E-value
laccase TIGR03389
laccase, plant; Members of this protein family include the copper-containing enzyme laccase ...
 2-484 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: 709.58  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063730442   2 RNPWADGPEYITQCPIQPGGSYTYRFTMEDQEGTLWWHAHSRWLRATVYGALIIRPPLSSPhYPFPViPKREITLLLGEW 81
Cdd:TIGR03389  67 RNGWADGPAYITQCPIQPGQSYVYNFTITGQRGTLWWHAHISWLRATVYGAIVILPKPGVP-YPFPK-PDREVPIILGEW 144

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063730442  82 WDRNPMDVLNLAQFTGAAPNISDAFTINGQPGDLYRCSSQETLRFLVGSGEIVLLRVINSALNQELFFGVANHKLTVVAA 161
Cdd:TIGR03389 145 WNADVEAVINQANQTGGAPNVSDAYTINGHPGPLYNCSSKDTFKLTVEPGKTYLLRIINAALNDELFFAIANHTLTVVEV 224

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063730442 162 DASYTKPFSTNVIMLGPGQTTDVLLTADQPPAHYYMAAHAYNSANAAFDNTTTTAILKYKDASCvtlqaksQARAIPAQL 241
Cdd:TIGR03389 225 DATYTKPFKTKTIVIGPGQTTNVLLTADQSPGRYFMAARPYMDAPGAFDNTTTTAILQYKGTSN-------SAKPILPTL 297

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063730442 242 PGFNDTATAAAFTAQMKSPSK----VKVPLEIDENLFFTVGLGLFNCPTpntQRCQGPNGTRFTASINNVSFVFPKqNSI 317
Cdd:TIGR03389 298 PAYNDTAAATNFSNKLRSLNSaqypANVPVTIDRRLFFTIGLGLDPCPN---NTCQGPNGTRFAASMNNISFVMPT-TAL 373

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063730442 318 MQAYYQGTPtGVFTTDFPPTPPVTFDYTGNVSRGLWQPTRGTKAYKLKFNSQVQIILQDTSIVTTENHPMHLHGYEFYVV 397
Cdd:TIGR03389 374 LQAHYFGIS-GVFTTDFPANPPTKFNYTGTNLPNNLFTTNGTKVVRLKFNSTVELVLQDTSILGSENHPIHLHGYNFFVV 452

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063730442 398 GTGVGNFNPNTDTSSFNLIDPPRRNTIGTPPGGWVAIRFVANNPGAWLMHCHIDSHIFWGLAMVFLVENGEGHLQSVQSP 477
Cdd:TIGR03389 453 GTGFGNFDPKKDPAKFNLVDPPERNTVGVPTGGWAAIRFVADNPGVWFMHCHLEVHTTWGLKMAFLVDNGKGPNQSLLPP 532


                  ....*..
gi 1063730442 478 PLDLPQC 484
Cdd:TIGR03389 533 PSDLPSC 539
CuRO_3_LCC_plant cd13897
The third cupredoxin domain of the plant laccases; Laccase is a blue multicopper oxidase (MCO) ...
 329-467 2.98e-87

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: 263.35  E-value: 2.98e-87
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063730442 329 VFTTDFPPTPPVTFDYTGNVSRGLWQPTRGTKAYKLKFNSQVQIILQDTSIVTTENHPMHLHGYEFYVVGTGVGNFNPNT 408
Cdd:cd13897     1 VYTTDFPDRPPVPFDYTGNAPNENTPTSRGTKVKVLEYGSTVEIVLQGTSLLAAENHPMHLHGFDFYVVGRGFGNFDPST 80

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1063730442 409 DTSSFNLIDPPRRNTIGTPPGGWVAIRFVANNPGAWLMHCHIDSHIFWGLAMVFLVENG 467
Cdd:cd13897    81 DPATFNLVDPPLRNTVGVPRGGWAAIRFVADNPGVWFMHCHFERHTSWGMATVFIVKNG 139
PLN02191 PLN02191
L-ascorbate oxidase
 3-462 3.05e-64

L-ascorbate oxidase


Pssm-ID: 177843 [Multi-domain]  Cd Length: 574  Bit Score: 217.96  E-value: 3.05e-64
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063730442   3 NPWADGPEYITQCPIQPGGSYTYRFTMeDQEGTLWWHAHSRWLRAT-VYGALIIRPPLSSPHYpfpVIPKREITLLLGEW 81
Cdd:PLN02191   89 SPWADGAAGVTQCAINPGETFTYKFTV-EKPGTHFYHGHYGMQRSAgLYGSLIVDVAKGPKER---LRYDGEFNLLLSDW 164

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063730442  82 WDRN-PMDVLNLA----QFTGAAPNIsdafTINGQ-------------PGDLYRCSSQE-------TLRflVGSGEIVLL 136
Cdd:PLN02191  165 WHESiPSQELGLSskpmRWIGEAQSI----LINGRgqfncslaaqfsnGTELPMCTFKEgdqcapqTLR--VEPNKTYRI 238

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063730442 137 RVINSALNQELFFGVANHKLTVVAADASYTKPFSTNVIMLGPGQTTDVLLTADQPPAHYYMAAHAYNSANAafDNTTTTA 216
Cdd:PLN02191  239 RLASTTALASLNLAVQGHKLVVVEADGNYITPFTTDDIDIYSGESYSVLLTTDQDPSQNYYISVGVRGRKP--NTTQALT 316

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063730442 217 ILKYKDASCVTLQAKSqaraiPAQLPGFNDTATAAAFTAQMKSPSKVKVPLEIDENLFFTVglglfncptpNTQRCQgPN 296
Cdd:PLN02191  317 ILNYVTAPASKLPSSP-----PPVTPRWDDFERSKNFSKKIFSAMGSPSPPKKYRKRLILL----------NTQNLI-DG 380

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063730442 297 GTRFtaSINNVSFVFPK-------QNSIMQAYYQGTPTGVFTTDF----PPTPPVTfdytgnvsrglwqpTRGTKAYKLK 365
Cdd:PLN02191  381 YTKW--AINNVSLVTPAtpylgsvKYNLKLGFNRKSPPRSYRMDYdimnPPPFPNT--------------TTGNGIYVFP 444

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063730442 366 FNSQVQIILQDTSI---VTTENHPMHLHGYEFYVVGTGVGNFNPNTDTSSFNLIDPPRRNTIGTPPGGWVAIRFVANNPG 442
Cdd:PLN02191  445 FNVTVDVIIQNANVlkgVVSEIHPWHLHGHDFWVLGYGDGKFKPGIDEKTYNLKNPPLRNTAILYPYGWTAIRFVTDNPG 524

                         490       500
                  ....*....|....*....|
gi 1063730442 443 AWLMHCHIDSHIFWGLAMVF 462
Cdd:PLN02191  525 VWFFHCHIEPHLHMGMGVVF 544
Cu-oxidase_2 pfam07731
Multicopper oxidase; This entry contains many divergent copper oxidase-like domains that are ...
 333-468 1.23e-45

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: 155.67  E-value: 1.23e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063730442 333 DFPPTPPVTFDYT-GNVSRGLWQPT-----RGTKAYKLKFNSQVQIILQDTsivTTENHPMHLHGYEFYVVGTGVGNfNP 406
Cdd:pfam07731   1 DTPPKLPTLLQITsGNFRRNDWAINgllfpPNTNVITLPYGTVVEWVLQNT---TTGVHPFHLHGHSFQVLGRGGGP-WP 76

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1063730442 407 NTDTSSFNLIDPPRRNTIGTPPGGWVAIRFVANNPGAWLMHCHIDSHIFWGLAMVFLVENGE 468
Cdd:pfam07731  77 EEDPKTYNLVDPVRRDTVQVPPGGWVAIRFRADNPGVWLFHCHILWHLDQGMMGQFVVRPGD 138
SufI COG2132
Multicopper oxidase with three cupredoxin domains (includes cell division protein FtsP and ...
 1-453 2.32e-37

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: 142.00  E-value: 2.32e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063730442   1 MRNPWA--DGPEYitqcPIQPGGSYTYRFTMEDQEGTLWWHAHSRwlRATV-------YGALIIRPPLSS-PHYpfpvip 70
Cdd:COG2132    74 LRVPNAmdGVPGD----PIAPGETFTYEFPVPQPAGTYWYHPHTH--GSTAeqvyrglAGALIVEDPEEDlPRY------ 141

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063730442  71 KREITLLLGEWWDRNPMDVLNlAQFTGAAPNISDAFTINGQPGDlyrcssqetlRFLVGSGEIVLLRVINSALNQELFFG 150
Cdd:COG2132   142 DRDIPLVLQDWRLDDDGQLLY-PMDAAMGGRLGDTLLVNGRPNP----------TLEVRPGERVRLRLLNASNARIYRLA 210

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063730442 151 VA-NHKLTVVAADASYT-KPFSTNVIMLGPGQTTDVLLTADQPPAHYYMAAhaynsanAAFDNTTTTAILKykdascVTL 228
Cdd:COG2132   211 LSdGRPFTVIATDGGLLpAPVEVDELLLAPGERADVLVDFSADPGEEVTLA-------NPFEGRSGRALLT------LRV 277

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063730442 229 QAKSQARAIPAQLPGFNDTataaaftaqmkSPSKVKVPLEIDenlfFTVglglfncptpntqrcqGPNGTRFTasINNVS 308
Cdd:COG2132   278 TGAAASAPLPANLAPLPDL-----------EDREAVRTRELV----LTG----------------GMAGYVWT--INGKA 324

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063730442 309 fvfpkqnsimqayyqgtptgvfttdFPPTPPvtfdytgnvsrgLWQPTRGTkAYKLKFNSQvqiilqdtsivTTENHPMH 388
Cdd:COG2132   325 -------------------------FDPDRP------------DLTVKLGE-RERWTLVND-----------TMMPHPFH 355

                         410       420       430       440       450       460
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1063730442 389 LHGYEFYVVGTGvGNFNPntdtssfnliDPPRRNTIGTPPGGWVAIRFVANN-PGAWLMHCHIDSH 453
Cdd:COG2132   356 LHGHQFQVLSRN-GKPPP----------EGGWKDTVLVPPGETVRILFRFDNyPGDWMFHCHILEH 410
 
Name Accession Description Interval E-value
laccase TIGR03389
laccase, plant; Members of this protein family include the copper-containing enzyme laccase ...
 2-484 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: 709.58  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063730442   2 RNPWADGPEYITQCPIQPGGSYTYRFTMEDQEGTLWWHAHSRWLRATVYGALIIRPPLSSPhYPFPViPKREITLLLGEW 81
Cdd:TIGR03389  67 RNGWADGPAYITQCPIQPGQSYVYNFTITGQRGTLWWHAHISWLRATVYGAIVILPKPGVP-YPFPK-PDREVPIILGEW 144

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063730442  82 WDRNPMDVLNLAQFTGAAPNISDAFTINGQPGDLYRCSSQETLRFLVGSGEIVLLRVINSALNQELFFGVANHKLTVVAA 161
Cdd:TIGR03389 145 WNADVEAVINQANQTGGAPNVSDAYTINGHPGPLYNCSSKDTFKLTVEPGKTYLLRIINAALNDELFFAIANHTLTVVEV 224

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063730442 162 DASYTKPFSTNVIMLGPGQTTDVLLTADQPPAHYYMAAHAYNSANAAFDNTTTTAILKYKDASCvtlqaksQARAIPAQL 241
Cdd:TIGR03389 225 DATYTKPFKTKTIVIGPGQTTNVLLTADQSPGRYFMAARPYMDAPGAFDNTTTTAILQYKGTSN-------SAKPILPTL 297

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063730442 242 PGFNDTATAAAFTAQMKSPSK----VKVPLEIDENLFFTVGLGLFNCPTpntQRCQGPNGTRFTASINNVSFVFPKqNSI 317
Cdd:TIGR03389 298 PAYNDTAAATNFSNKLRSLNSaqypANVPVTIDRRLFFTIGLGLDPCPN---NTCQGPNGTRFAASMNNISFVMPT-TAL 373

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063730442 318 MQAYYQGTPtGVFTTDFPPTPPVTFDYTGNVSRGLWQPTRGTKAYKLKFNSQVQIILQDTSIVTTENHPMHLHGYEFYVV 397
Cdd:TIGR03389 374 LQAHYFGIS-GVFTTDFPANPPTKFNYTGTNLPNNLFTTNGTKVVRLKFNSTVELVLQDTSILGSENHPIHLHGYNFFVV 452

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063730442 398 GTGVGNFNPNTDTSSFNLIDPPRRNTIGTPPGGWVAIRFVANNPGAWLMHCHIDSHIFWGLAMVFLVENGEGHLQSVQSP 477
Cdd:TIGR03389 453 GTGFGNFDPKKDPAKFNLVDPPERNTVGVPTGGWAAIRFVADNPGVWFMHCHLEVHTTWGLKMAFLVDNGKGPNQSLLPP 532


                  ....*..
gi 1063730442 478 PLDLPQC 484
Cdd:TIGR03389 533 PSDLPSC 539
CuRO_3_LCC_plant cd13897
The third cupredoxin domain of the plant laccases; Laccase is a blue multicopper oxidase (MCO) ...
 329-467 2.98e-87

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: 263.35  E-value: 2.98e-87
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063730442 329 VFTTDFPPTPPVTFDYTGNVSRGLWQPTRGTKAYKLKFNSQVQIILQDTSIVTTENHPMHLHGYEFYVVGTGVGNFNPNT 408
Cdd:cd13897     1 VYTTDFPDRPPVPFDYTGNAPNENTPTSRGTKVKVLEYGSTVEIVLQGTSLLAAENHPMHLHGFDFYVVGRGFGNFDPST 80

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1063730442 409 DTSSFNLIDPPRRNTIGTPPGGWVAIRFVANNPGAWLMHCHIDSHIFWGLAMVFLVENG 467
Cdd:cd13897    81 DPATFNLVDPPLRNTVGVPRGGWAAIRFVADNPGVWFMHCHFERHTSWGMATVFIVKNG 139
CuRO_2_LCC_plant cd13875
The second cupredoxin domain of the plant laccases; Laccase is a blue multi-copper enzyme that ...
 74-220 3.59e-84

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: 255.99  E-value: 3.59e-84
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063730442  74 ITLLLGEWWDRNPMDVLNLAQFTGAAPNISDAFTINGQPGDLYRCSSQETLRFLVGSGEIVLLRVINSALNQELFFGVAN 153
Cdd:cd13875     1 VPIILGEWWNRDVNDVEDQALLTGGGPNISDAYTINGQPGDLYNCSSKDTFVLTVEPGKTYLLRIINAALNEELFFKIAN 80

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1063730442 154 HKLTVVAADASYTKPFSTNVIMLGPGQTTDVLLTADQPPAHYYMAAHAYNSANAA-FDNTTTTAILKY 220
Cdd:cd13875    81 HTLTVVAVDASYTKPFTTDYILIAPGQTTDVLLTADQPPGRYYMAARPYQSAPPVpFDNTTATAILEY 148
ascorbase TIGR03388
L-ascorbate oxidase, plant type; Members of this protein family are the copper-containing ...
 4-462 6.06e-79

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: 255.83  E-value: 6.06e-79
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063730442   4 PWADGPEYITQCPIQPGGSYTYRFTMeDQEGTLWWHAHSRWLR-ATVYGALIIRPPLSSPHyPFPVipKREITLLLGEWW 82
Cdd:TIGR03388  68 PWADGTAGVTQCAINPGETFIYNFVV-DRPGTYFYHGHYGMQRsAGLYGSLIVDVPDGEKE-PFHY--DGEFNLLLSDWW 143

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063730442  83 DRNpmdvlNLAQFTGAApniSDAFTINGQPGDL-------YRCSSQETLR-------------------FLVGSGEIVLL 136
Cdd:TIGR03388 144 HKS-----IHEQEVGLS---SKPMRWIGEPQSLlingrgqFNCSLAAKFSstnlpqcnlkgneqcapqiLHVEPGKTYRL 215

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063730442 137 RVINSALNQELFFGVANHKLTVVAADASYTKPFSTNVIMLGPGQTTDVLLTADQPPAHYYMAAHAYNSANAAfdNTTTTA 216
Cdd:TIGR03388 216 RIASTTALAALNFAIEGHKLTVVEADGNYVEPFTVKDIDIYSGETYSVLLTTDQDPSRNYWISVGVRGRKPN--TPPGLT 293

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063730442 217 ILKYKDAScvtlqAKSQARAIPAQLPGFNDTATAAAFTAQMKS-PSKVKVPLEIDENLFFTvglglfncptpNTQRCQGp 295
Cdd:TIGR03388 294 VLNYYPNS-----PSRLPPTPPPVTPAWDDFDRSKAFSLAIKAaMGSPKPPETSDRRIVLL-----------NTQNKIN- 356

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063730442 296 NGTRFtaSINNVSFVFP--------KQNsIMQAYYQGTPTGVFTTDF----PPTPPVTfdytgnvsrglwqpTRGTKAYK 363
Cdd:TIGR03388 357 GYTKW--AINNVSLTLPhtpylgslKYN-LLNAFDQKPPPENYPRDYdifkPPPNPNT--------------TTGNGIYR 419

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063730442 364 LKFNSQVQIILQDTSIV---TTENHPMHLHGYEFYVVGTGVGNFNPNTDTSSFNLIDPPRRNTIGTPPGGWVAIRFVANN 440
Cdd:TIGR03388 420 LKFNTTVDVILQNANTLngnNSETHPWHLHGHDFWVLGYGEGKFRPGVDEKSYNLKNPPLRNTVVIFPYGWTALRFVADN 499

                         490       500
                  ....*....|....*....|..
gi 1063730442 441 PGAWLMHCHIDSHIFWGLAMVF 462
Cdd:TIGR03388 500 PGVWAFHCHIEPHLHMGMGVVF 521
PLN02191 PLN02191
L-ascorbate oxidase
 3-462 3.05e-64

L-ascorbate oxidase


Pssm-ID: 177843 [Multi-domain]  Cd Length: 574  Bit Score: 217.96  E-value: 3.05e-64
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063730442   3 NPWADGPEYITQCPIQPGGSYTYRFTMeDQEGTLWWHAHSRWLRAT-VYGALIIRPPLSSPHYpfpVIPKREITLLLGEW 81
Cdd:PLN02191   89 SPWADGAAGVTQCAINPGETFTYKFTV-EKPGTHFYHGHYGMQRSAgLYGSLIVDVAKGPKER---LRYDGEFNLLLSDW 164

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063730442  82 WDRN-PMDVLNLA----QFTGAAPNIsdafTINGQ-------------PGDLYRCSSQE-------TLRflVGSGEIVLL 136
Cdd:PLN02191  165 WHESiPSQELGLSskpmRWIGEAQSI----LINGRgqfncslaaqfsnGTELPMCTFKEgdqcapqTLR--VEPNKTYRI 238

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063730442 137 RVINSALNQELFFGVANHKLTVVAADASYTKPFSTNVIMLGPGQTTDVLLTADQPPAHYYMAAHAYNSANAafDNTTTTA 216
Cdd:PLN02191  239 RLASTTALASLNLAVQGHKLVVVEADGNYITPFTTDDIDIYSGESYSVLLTTDQDPSQNYYISVGVRGRKP--NTTQALT 316

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063730442 217 ILKYKDASCVTLQAKSqaraiPAQLPGFNDTATAAAFTAQMKSPSKVKVPLEIDENLFFTVglglfncptpNTQRCQgPN 296
Cdd:PLN02191  317 ILNYVTAPASKLPSSP-----PPVTPRWDDFERSKNFSKKIFSAMGSPSPPKKYRKRLILL----------NTQNLI-DG 380

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063730442 297 GTRFtaSINNVSFVFPK-------QNSIMQAYYQGTPTGVFTTDF----PPTPPVTfdytgnvsrglwqpTRGTKAYKLK 365
Cdd:PLN02191  381 YTKW--AINNVSLVTPAtpylgsvKYNLKLGFNRKSPPRSYRMDYdimnPPPFPNT--------------TTGNGIYVFP 444

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063730442 366 FNSQVQIILQDTSI---VTTENHPMHLHGYEFYVVGTGVGNFNPNTDTSSFNLIDPPRRNTIGTPPGGWVAIRFVANNPG 442
Cdd:PLN02191  445 FNVTVDVIIQNANVlkgVVSEIHPWHLHGHDFWVLGYGDGKFKPGIDEKTYNLKNPPLRNTAILYPYGWTAIRFVTDNPG 524

                         490       500
                  ....*....|....*....|
gi 1063730442 443 AWLMHCHIDSHIFWGLAMVF 462
Cdd:PLN02191  525 VWFFHCHIEPHLHMGMGVVF 544
PLN02604 PLN02604
oxidoreductase
 4-462 3.03e-62

oxidoreductase


Pssm-ID: 215324 [Multi-domain]  Cd Length: 566  Bit Score: 212.41  E-value: 3.03e-62
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063730442   4 PWADGPEYITQCPIQPGGSYTYRFTMeDQEGTLWWHAHSRWLR-ATVYGALIIRPPLSSPHyPFPVIPKREItlLLGEWW 82
Cdd:PLN02604   91 PWFDGTEGVTQCPILPGETFTYEFVV-DRPGTYLYHAHYGMQReAGLYGSIRVSLPRGKSE-PFSYDYDRSI--ILTDWY 166

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063730442  83 DRNPMDvlnlaQFTGAApniSDAFTINGQPGDL-------YRCS---------------SQETLRFL--VGSGEIVLLRV 138
Cdd:PLN02604  167 HKSTYE-----QALGLS---SIPFDWVGEPQSLliqgkgrYNCSlvsspylkagvcnatNPECSPYVltVVPGKTYRLRI 238

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063730442 139 INSALNQELFFGVANHKLTVVAADASYTKPFSTNVIMLGPGQTTDVLLTADQPPAHYYMAAHAYNSANAAfdNTTTTAIL 218
Cdd:PLN02604  239 SSLTALSALSFQIEGHNMTVVEADGHYVEPFVVKNLFIYSGETYSVLVKADQDPSRNYWVTTSVVSRNNT--TPPGLAIF 316

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063730442 219 KYKDAscvtlQAKSQARAIPAQLPGFNDTATAAAFTAQMKSPSK--VKVPLEIDENLFFTvglglfncptpNTQrcQGPN 296
Cdd:PLN02604  317 NYYPN-----HPRRSPPTVPPSGPLWNDVEPRLNQSLAIKARHGyiHPPPLTSDRVIVLL-----------NTQ--NEVN 378

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063730442 297 GTRfTASINNVSFVFPKQNSIMQayYQGTPTGVFTtdfPPTPPVTFDYTGNVSRGLWQPTRGTKA---YKLKFNSQVQII 373
Cdd:PLN02604  379 GYR-RWSVNNVSFNLPHTPYLIA--LKENLTGAFD---QTPPPEGYDFANYDIYAKPNNSNATSSdsiYRLQFNSTVDII 452

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063730442 374 LQDTSIVT---TENHPMHLHGYEFYVVGTGVGNFNPNTDTSSFNLIDPPRRNTIGTPPGGWVAIRFVANNPGAWLMHCHI 450
Cdd:PLN02604  453 LQNANTMNannSETHPWHLHGHDFWVLGYGEGKFNMSSDPKKYNLVDPIMKNTVPVHPYGWTALRFRADNPGVWAFHCHI 532

                         490
                  ....*....|..
gi 1063730442 451 DSHIFWGLAMVF 462
Cdd:PLN02604  533 ESHFFMGMGVVF 544
Cu-oxidase_2 pfam07731
Multicopper oxidase; This entry contains many divergent copper oxidase-like domains that are ...
 333-468 1.23e-45

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: 155.67  E-value: 1.23e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063730442 333 DFPPTPPVTFDYT-GNVSRGLWQPT-----RGTKAYKLKFNSQVQIILQDTsivTTENHPMHLHGYEFYVVGTGVGNfNP 406
Cdd:pfam07731   1 DTPPKLPTLLQITsGNFRRNDWAINgllfpPNTNVITLPYGTVVEWVLQNT---TTGVHPFHLHGHSFQVLGRGGGP-WP 76

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1063730442 407 NTDTSSFNLIDPPRRNTIGTPPGGWVAIRFVANNPGAWLMHCHIDSHIFWGLAMVFLVENGE 468
Cdd:pfam07731  77 EEDPKTYNLVDPVRRDTVQVPPGGWVAIRFRADNPGVWLFHCHILWHLDQGMMGQFVVRPGD 138
Cu-oxidase pfam00394
Multicopper oxidase; Many of the proteins in this family contain multiple similar copies of ...
 72-221 4.21e-43

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: 149.39  E-value: 4.21e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063730442  72 REITLLLGEWWDRNPMDVLNLAQFTGAA----PNISDAFTINGQPGdlyrcssQETLRFLVGSGEIVLLRVINSALNQEL 147
Cdd:pfam00394   1 EDYVITLSDWYHKDAKDLEKELLASGKAptdfPPVPDAVLINGKDG-------ASLATLTVTPGKTYRLRIINVALDDSL 73

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1063730442 148 FFGVANHKLTVVAADASYTKPFSTNVIMLGPGQTTDVLLTADQPPAHYYMAAHaynSANAAFDNTTTTAILKYK 221
Cdd:pfam00394  74 NFSIEGHKMTVVEVDGVYVNPFTVDSLDIFPGQRYSVLVTANQDPGNYWIVAS---PNIPAFDNGTAAAILRYS 144
CuRO_3_AAO cd13893
The third cupredoxin domain of plant Ascorbate oxidase; Ascorbate oxidase catalyzes the ...
 362-462 1.99e-37

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: 134.47  E-value: 1.99e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063730442 362 YKLKFNSQVQIILQDTSIVT---TENHPMHLHGYEFYVVGTGVGNFNPNTDTSSFNLIDPPRRNTIGTPPGGWVAIRFVA 438
Cdd:cd13893    41 YPFKGGDVVDVILQNANTNTrnaSEQHPWHLHGHDFWVLGYGLGGFDPAADPSSLNLVNPPMRNTVTIFPYGWTALRFKA 120

                          90       100
                  ....*....|....*....|....
gi 1063730442 439 NNPGAWLMHCHIDSHIFWGLAMVF 462
Cdd:cd13893   121 DNPGVWAFHCHIEWHFHMGMGVVF 144
SufI COG2132
Multicopper oxidase with three cupredoxin domains (includes cell division protein FtsP and ...
 1-453 2.32e-37

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: 142.00  E-value: 2.32e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063730442   1 MRNPWA--DGPEYitqcPIQPGGSYTYRFTMEDQEGTLWWHAHSRwlRATV-------YGALIIRPPLSS-PHYpfpvip 70
Cdd:COG2132    74 LRVPNAmdGVPGD----PIAPGETFTYEFPVPQPAGTYWYHPHTH--GSTAeqvyrglAGALIVEDPEEDlPRY------ 141

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063730442  71 KREITLLLGEWWDRNPMDVLNlAQFTGAAPNISDAFTINGQPGDlyrcssqetlRFLVGSGEIVLLRVINSALNQELFFG 150
Cdd:COG2132   142 DRDIPLVLQDWRLDDDGQLLY-PMDAAMGGRLGDTLLVNGRPNP----------TLEVRPGERVRLRLLNASNARIYRLA 210

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063730442 151 VA-NHKLTVVAADASYT-KPFSTNVIMLGPGQTTDVLLTADQPPAHYYMAAhaynsanAAFDNTTTTAILKykdascVTL 228
Cdd:COG2132   211 LSdGRPFTVIATDGGLLpAPVEVDELLLAPGERADVLVDFSADPGEEVTLA-------NPFEGRSGRALLT------LRV 277

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063730442 229 QAKSQARAIPAQLPGFNDTataaaftaqmkSPSKVKVPLEIDenlfFTVglglfncptpntqrcqGPNGTRFTasINNVS 308
Cdd:COG2132   278 TGAAASAPLPANLAPLPDL-----------EDREAVRTRELV----LTG----------------GMAGYVWT--INGKA 324

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063730442 309 fvfpkqnsimqayyqgtptgvfttdFPPTPPvtfdytgnvsrgLWQPTRGTkAYKLKFNSQvqiilqdtsivTTENHPMH 388
Cdd:COG2132   325 -------------------------FDPDRP------------DLTVKLGE-RERWTLVND-----------TMMPHPFH 355

                         410       420       430       440       450       460
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1063730442 389 LHGYEFYVVGTGvGNFNPntdtssfnliDPPRRNTIGTPPGGWVAIRFVANN-PGAWLMHCHIDSH 453
Cdd:COG2132   356 LHGHQFQVLSRN-GKPPP----------EGGWKDTVLVPPGETVRILFRFDNyPGDWMFHCHILEH 410
CuRO_3_tcLLC2_insect_like cd13905
The third cupredoxin domain of the insect laccases similar to laccase 2 in Tribolium castaneum; ...
 303-464 1.98e-36

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: 132.42  E-value: 1.98e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063730442 303 SINNVSFVFPkqNSIMQayyqgtptgvftTDFPPTPPVTFDYTGNVSRGLWQPT-RGTKAYKLKFNSQVQIILQDTSIVT 381
Cdd:cd13905     1 SINGISFVFP--SSPLL------------SQPEDLSDSSSCDFCNVPSKCCTEPcECTHVIKLPLNSVVEIVLINEGPGP 66

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063730442 382 TENHPMHLHGYEFYVVGTGVGNFNPNTDTSSF----------------NLIDPPRRNTIGTPPGGWVAIRFVANNPGAWL 445
Cdd:cd13905    67 GLSHPFHLHGHSFYVLGMGFPGYNSTTGEILSqnwnnklldrgglpgrNLVNPPLKDTVVVPNGGYVVIRFRADNPGYWL 146

                         170
                  ....*....|....*....
gi 1063730442 446 MHCHIDSHIFWGLAMVFLV 464
Cdd:cd13905   147 LHCHIEFHLLEGMALVLKV 165
CuRO_1_LCC_plant cd13849
The first cupredoxin domain of plant laccases; Laccase is a blue multicopper oxidase (MCO) ...
 1-57 2.04e-36

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: 130.46  E-value: 2.04e-36
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1063730442   1 MRNPWADGPEYITQCPIQPGGSYTYRFTMEDQEGTLWWHAHSRWLRATVYGALIIRP 57
Cdd:cd13849    61 LRSGWADGPAYITQCPIQPGQSYTYRFTVTGQEGTLWWHAHISWLRATVYGAFIIRP 117
CuRO_3_LCC_like cd04207
Cupredoxin domain 3 of laccase-like multicopper oxidases; including laccase, CueO, spore coat ...
 358-462 1.06e-32

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: 121.03  E-value: 1.06e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063730442 358 GTKAYKLKFNSQVQIILQDTSIvTTENHPMHLHGYEFYVVGTGVGNFNPntdtsSFNLIDPPRRNTIGTPPGGWVAIRFV 437
Cdd:cd04207    33 NTDIFSVEAGDVVEIVLINAGN-HDMQHPFHLHGHSFWVLGSGGGPFDA-----PLNLTNPPWRDTVLVPPGGWVVIRFK 106

                          90       100
                  ....*....|....*....|....*
gi 1063730442 438 ANNPGAWLMHCHIDSHIFWGLAMVF 462
Cdd:cd04207   107 ADNPGVWMLHCHILEHEDAGMMTVF 131
ascorbOXfungal TIGR03390
L-ascorbate oxidase, fungal type; This model describes a family of fungal ascorbate oxidases, ...
 4-468 3.58e-32

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: 129.19  E-value: 3.58e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063730442   4 PWADGPEYITQCPIQPGGSYTYRFTME-DQEGTLWWHAHSRWLRATVYGALIIRPPLSSP-HYpfpvipKREITLLLGEW 81
Cdd:TIGR03390  75 PFSDGTPLASQWPIPPGHFFDYEIKPEpGDAGSYFYHSHVGFQAVTAFGPLIVEDCEPPPyKY------DDERILLVSDF 148

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063730442  82 WDRNPMDV---LNLAQFTGaaPNISDAFTINGQPGDL-----YRCSSQETLRFL-VGSGEIVLLRVINSALNQELFFGVA 152
Cdd:TIGR03390 149 FSATDEEIeqgLLSTPFTW--SGETEAVLLNGKSGNKsfyaqINPSGSCMLPVIdVEPGKTYRLRFIGATALSLISLGIE 226

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063730442 153 NHK-LTVVAADASYTKPFSTNVIMLGPGQTTDVLLTAdqppahyymaahaynsanaafdntTTTAILKYKDASCVTLQAK 231
Cdd:TIGR03390 227 DHEnLTIIEADGSYTKPAKIDHLQLGGGQRYSVLFKA------------------------KTEDELCGGDKRQYFIQFE 282

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063730442 232 SQARaiPAQLPGF---NDTATAAAFTAQMKSPSKVKVPLEIDENLFFTV-GLGLFN---CPTPN--TQRCQ-------GP 295
Cdd:TIGR03390 283 TRDR--PKVYRGYavlRYRSDKASKLPSVPETPPLPLPNSTYDWLEYELePLSEENnqdFPTLDevTRRVVidahqnvDP 360

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063730442 296 NGTRFTASINNVSFV--FPKQNSIMQAYYQGTPTgvfttdfpptppvTFDYTGNVSRGLWQPTrgTKAYKLKFNSQVQII 373
Cdd:TIGR03390 361 LNGRVAWLQNGLSWTesVRQTPYLVDIYENGLPA-------------TPNYTAALANYGFDPE--TRAFPAKVGEVLEIV 425

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063730442 374 LQDTSIVTTEN-----HPMHLHGYEFYVVGTGVGNFNPNTDTSSFNLIDPPRRNTI--------GTP--PGGWVAIRFVA 438
Cdd:TIGR03390 426 WQNTGSYTGPNggvdtHPFHAHGRHFYDIGGGDGEYNATANEAKLENYTPVLRDTTmlyryavkVVPgaPAGWRAWRIRV 505

                         490       500       510
                  ....*....|....*....|....*....|
gi 1063730442 439 NNPGAWLMHCHIDSHIFWGLAMVFLVENGE 468
Cdd:TIGR03390 506 TNPGVWMMHCHILQHMVMGMQTVWVFGDAE 535
CuRO_2_LCC_like cd04205
Cupredoxin domain 2 of laccase-like multicopper oxidases; including laccase, CueO, spore coat ...
 74-220 1.06e-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: 113.61  E-value: 1.06e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063730442  74 ITLLLGEWWDRNPMDVLN-LAQFTGAAPNISDAFTINGQPGD----LYRCSSQETLRFLVGSGEIVLLRVINSALNQELF 148
Cdd:cd04205     1 RVLLLSDWYHDSAEDVLAgYMPNSFGNEPVPDSLLINGRGRFncsmAVCNSGCPLPVITVEPGKTYRLRLINAGSFASFN 80

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1063730442 149 FGVANHKLTVVAADASYTKPFSTNVIMLGPGQTTDVLLTADQPPAHYYMAAHAYNSANAAFDNTTTTAILKY 220
Cdd:cd04205    81 FAIDGHNMTVIEVDGGYVEPLEVDNLDLAPGQRYDVLVKADQPPGNYWIRASADGRTFDEGGNPNGTAILRY 152
PLN02991 PLN02991
oxidoreductase
 2-450 5.18e-29

oxidoreductase


Pssm-ID: 215536 [Multi-domain]  Cd Length: 543  Bit Score: 120.12  E-value: 5.18e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063730442   2 RNPWADGPeYITQCPIQPGGSYTYRFTMEDQEGTLWWHAHSRWLRAT-VYGALIIRPPLSSPhYPFPViPKREITLLLGE 80
Cdd:PLN02991   92 RNSYQDGV-YGTTCPIPPGKNYTYALQVKDQIGSFYYFPSLGFHKAAgGFGAIRISSRPLIP-VPFPA-PADDYTVLIGD 168

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063730442  81 WWDRNPMDVLNLAQFTGAAPnISDAFTINGQpgdlyrcSSQETLRflVGSGEIVLLRVINSALNQELFFGVANHKLTVVA 160
Cdd:PLN02991  169 WYKTNHKDLRAQLDNGGKLP-LPDGILINGR-------GSGATLN--IEPGKTYRLRISNVGLQNSLNFRIQNHTMKLVE 238

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063730442 161 ADASYT--KPFSTNVIMLgpGQTTDVLLTADQPPAHYYMAAHAYNSANAafdnTTTTAILKYKDAscvtlqaksqARAIP 238
Cdd:PLN02991  239 VEGTHTiqTPFSSLDVHV--GQSYSVLITADQPAKDYYIVVSSRFTSKI----LITTGVLHYSNS----------AGPVS 302

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063730442 239 AQLPgfndtataaaftaqmksPSKVKVPLEIDENLFFTVGLGLfNCPTPNTQ---RCQGPNGTRFTASINNVSFVFPKQN 315
Cdd:PLN02991  303 GPIP-----------------DGPIQLSWSFDQARAIKTNLTA-SGPRPNPQgsyHYGKINITRTIRLANSAGNIEGKQR 364

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063730442 316 simqayYQGTPTGVFTTDFPPTPPVTFDYTGNVSRGLW--QPTRG-----TKAYKLKFNSQVQIILQDTS-IVTTenhpM 387
Cdd:PLN02991  365 ------YAVNSASFYPADTPLKLADYFKIAGVYNPGSIpdQPTNGaifpvTSVMQTDYKAFVEIVFENWEdIVQT----W 434

                         410       420       430       440       450       460
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1063730442 388 HLHGYEFYVVGTGVGNFNPNTdTSSFNLIDPPRRNTIGTPPGGWVAIRFVANNPGAWLMHCHI 450
Cdd:PLN02991  435 HLDGYSFYVVGMELGKWSAAS-RKVYNLNDAVSRCTVQVYPRSWTAIYVSLDNVGMWNLRSEL 496
CuRO_3_MCO_like_4 cd13910
The third cupredoxin domain of uncharacterized multicopper oxidase; Multicopper Oxidases (MCOs) ...
 384-464 5.84e-29

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: 112.00  E-value: 5.84e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063730442 384 NHPMHLHGYEFYVVGTGVGNFN----PNTDTSSFNLIDPPRRNTIGTPPGGWVAIRFVANNPGAWLMHCHIDSHIFWGLA 459
Cdd:cd13910    82 DHPFHLHGHKFWVLGSGDGRYGgggyTAPDGTSLNTTNPLRRDTVSVPGFGWAVLRFVADNPGLWAFHCHILWHMAAGML 161


                  ....*
gi 1063730442 460 MVFLV 464
Cdd:cd13910   162 MQFAV 166
CuRO_3_Abr2_like cd13898
The third cupredoxin domain of a group of fungal Laccases similar to Abr2 from Aspergillus ...
 363-463 7.45e-29

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: 111.58  E-value: 7.45e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063730442 363 KLKFNSQVQIILQDTSIVTTEnHPMHLHGYEFYVVGTGVGNFNPNT-------DTSSFNLIDPPRRNTIGTPPGG----W 431
Cdd:cd13898    52 STKNGTWVDLIFQVTGPPQPP-HPIHKHGNKAFVIGTGTGPFNWSSvaeaaeaAPENFNLVNPPLRDTFTTPPSTegpsW 130

                          90       100       110
                  ....*....|....*....|....*....|..
gi 1063730442 432 VAIRFVANNPGAWLMHCHIDSHIFWGLAMVFL 463
Cdd:cd13898   131 LVIRYHVVNPGAWLLHCHIQSHLAGGMAVVLL 162
CuRO_3_MaLCC_like cd13901
The third cupredoxin domain of the fungal laccases similar to Ma-LCC from Melanocarpus ...
 367-463 9.30e-29

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: 111.16  E-value: 9.30e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063730442 367 NSQVQIILQDTSIVtteNHPMHLHGYEFYVVGTGVGNFNpnTDTSSFNLIDPPRRNTIGTPPGGWVAIRFVANNPGAWLM 446
Cdd:cd13901    66 NKWVYIVIQNNSPL---PHPIHLHGHDFYILAQGTGTFD--DDGTILNLNNPPRRDVAMLPAGGYLVIAFKTDNPGAWLM 140

                          90
                  ....*....|....*..
gi 1063730442 447 HCHIDSHIFWGLAMVFL 463
Cdd:cd13901   141 HCHIAWHASGGLALQFL 157
PLN02168 PLN02168
copper ion binding / pectinesterase
 2-444 9.52e-29

copper ion binding / pectinesterase


Pssm-ID: 215113 [Multi-domain]  Cd Length: 545  Bit Score: 119.31  E-value: 9.52e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063730442   2 RNPWADGPEYiTQCPIQPGGSYTYRFTMEDQEGTLWWHAHSRWLRAT-VYGALIIRPPLSSPhYPFPViPKREITLLLGE 80
Cdd:PLN02168   90 KNSWQDGVRG-TNCPILPGTNWTYRFQVKDQIGSYFYFPSLLLQKAAgGYGAIRIYNPELVP-VPFPK-PDEEYDILIGD 166

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063730442  81 WWDRNPMDVLNLAQFTGAAPNiSDAFTINGQpgdlyrcSSQETLrFLVGSGEIVLLRVINSALNQELFFGVANHKLTVVA 160
Cdd:PLN02168  167 WFYADHTVMRASLDNGHSLPN-PDGILFNGR-------GPEETF-FAFEPGKTYRLRISNVGLKTCLNFRIQDHDMLLVE 237

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063730442 161 ADASYTKPFSTNVIMLGPGQTTDVLLTADQPPAHYYMAAHAYNSANAAFDNTTTTAILKYKDAScvtLQAKSQARAIPAQ 240
Cdd:PLN02168  238 TEGTYVQKRVYSSLDIHVGQSYSVLVTAKTDPVGIYRSYYIVATARFTDAYLGGVALIRYPNSP---LDPVGPLPLAPAL 314

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063730442 241 LPGFndtataaaftaqmkspSKVKVPLEIDENLffTVGLGLfncPTPNTQRCQGP-NGTR--------------FTASIN 305
Cdd:PLN02168  315 HDYF----------------SSVEQALSIRMDL--NVGAAR---SNPQGSYHYGRiNVTRtiilhndvmlssgkLRYTIN 373

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063730442 306 NVSFVFPKQNSIMQAYYQGTPTgVFTTDFPPTPpvtfdytGNVSrglwqPTRGTKAYKLKFNSQVQIILQDTsivTTENH 385
Cdd:PLN02168  374 GVSFVYPGTPLKLVDHFQLNDT-IIPGMFPVYP-------SNKT-----PTLGTSVVDIHYKDFYHIVFQNP---LFSLE 437

                         410       420       430       440       450
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1063730442 386 PMHLHGYEFYVVGTGVGNFNPNTdTSSFNLIDPPRRNTIGTPPGGWVAIRFVANNPGAW 444
Cdd:PLN02168  438 SYHIDGYNFFVVGYGFGAWSESK-KAGYNLVDAVSRSTVQVYPYSWTAILIAMDNQGMW 495
CuRO_3_Fet3p cd13899
The third Cupredoxin domain of multicopper oxidase Fet3p; Fet3p catalyzes the ferroxidase ...
 302-464 7.14e-28

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: 108.88  E-value: 7.14e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063730442 302 ASINNVSFVFPKQNSIMQAYYQGtptgvfttDFPPTPPVtfdYTGNvsrglwqptrgTKAYKLKFNSQVQIIL--QDTSi 379
Cdd:cd13899    20 AAFNNITYVSPKVPTLYTALSMG--------DDALDPAI---YGPQ-----------TNAFVLNHGEVVELVVnnWDAG- 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063730442 380 vtteNHPMHLHGYEFYVV--GTGVGNFNPNTDTSSFNlIDPPRRNTIGTPPGGWVAIRFVANNPGAWLMHCHIDSHIFWG 457
Cdd:cd13899    77 ----KHPFHLHGHKFQVVqrSPDVASDDPNPPINEFP-ENPMRRDTVMVPPGGSVVIRFRADNPGVWFFHCHIEWHLEAG 151


                  ....*..
gi 1063730442 458 LAMVFLV 464
Cdd:cd13899   152 LAATFIE 158
CuRO_3_Tv-LCC_like cd13903
The third cupredoxin domain of the fungal laccases similar to Tv-LCC from Trametes Versicolor; ...
 270-462 1.09e-26

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: 105.05  E-value: 1.09e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063730442 270 DENLFFTVGLGlfncptpntqrcqgPNGTRFTasINNVSFVFPKQNSIMQayyqgTPTGV-FTTDFPPTppvtfdytGNV 348
Cdd:cd13903     1 DVNITLTFGLN--------------GTTGLFT--INGVSYVSPTVPVLLQ-----ILSGAtSAEDLLPT--------EST 51

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063730442 349 srglwqptrgtkaYKLKFNSQVQIILQDTSIVttENHPMHLHGYEFYVVGTGvgnfnpntDTSSFNLIDPPRRNTIGT-P 427
Cdd:cd13903    52 -------------IILPRNKVVEITIPGGAIG--GPHPFHLHGHAFSVVRSA--------GSNTYNYVNPVRRDVVSVgT 108

                         170       180       190
                  ....*....|....*....|....*....|....*
gi 1063730442 428 PGGWVAIRFVANNPGAWLMHCHIDSHIFWGLAMVF 462
Cdd:cd13903   109 PGDGVTIRFVTDNPGPWFLHCHIDWHLEAGLAVVF 143
PLN02835 PLN02835
oxidoreductase
 2-484 1.27e-26

oxidoreductase


Pssm-ID: 178429 [Multi-domain]  Cd Length: 539  Bit Score: 112.76  E-value: 1.27e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063730442   2 RNPWADGPeYITQCPIQPGGSYTYRFTMEDQEGTLWWHAHSRWLRAT-VYGALII--RPPLSsphYPFPViPKREITLLL 78
Cdd:PLN02835   93 KNSWQDGV-LGTNCPIPPNSNYTYKFQTKDQIGTFTYFPSTLFHKAAgGFGAINVyeRPRIP---IPFPL-PDGDFTLLV 167

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063730442  79 GEWWDRNpMDVLNLAQFTGAAPNISDAFTINGQpgdlyrcsSQETlrFLVGSGEIVLLRVINSALNQELFFGVANHKLTV 158
Cdd:PLN02835  168 GDWYKTS-HKTLQQRLDSGKVLPFPDGVLINGQ--------TQST--FSGDQGKTYMFRISNVGLSTSLNFRIQGHTMKL 236

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063730442 159 VAADASYTKPFSTNVIMLGPGQTTDVLLTADQPPAHYYMAAhaynSANAAFDNTTTTAILKYKDascvtlqAKSQARAIP 238
Cdd:PLN02835  237 VEVEGSHTIQNIYDSLDVHVGQSVAVLVTLNQSPKDYYIVA----STRFTRQILTATAVLHYSN-------SRTPASGPL 305

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063730442 239 AQLPGFndtataaAFTAQMKSPSKVKVPLEIDENLFFTVGLGLFNCPTPN-----TQRCQGPNGTRFTAsINNVSFVfPK 313
Cdd:PLN02835  306 PALPSG-------ELHWSMRQARTYRWNLTASAARPNPQGSFHYGKITPTktivlANSAPLINGKQRYA-VNGVSYV-NS 376

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063730442 314 QNSIMQAYYQGTPtGVFTTDFPPTPPvtfdytgnvSRGlwQPTRGTKAYKLKFNSQVQIILQDTSIVTtenHPMHLHGYE 393
Cdd:PLN02835  377 DTPLKLADYFGIP-GVFSVNSIQSLP---------SGG--PAFVATSVMQTSLHDFLEVVFQNNEKTM---QSWHLDGYD 441

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063730442 394 FYVVGTGVGNFNPNTdTSSFNLIDPPRRNTIGTPPGGWVAIRFVANNPGAWLMHCHIDSHIFWGLAMVFLVENGEGHLQS 473
Cdd:PLN02835  442 FWVVGYGSGQWTPAK-RSLYNLVDALTRHTAQVYPKSWTTILVSLDNQGMWNMRSAIWERQYLGQQFYLRVWNQVHSLAN 520

                         490
                  ....*....|.
gi 1063730442 474 VQSPPLDLPQC 484
Cdd:PLN02835  521 EYDIPDNALLC 531
PLN02354 PLN02354
copper ion binding / oxidoreductase
 2-444 1.12e-25

copper ion binding / oxidoreductase


Pssm-ID: 177987 [Multi-domain]  Cd Length: 552  Bit Score: 110.27  E-value: 1.12e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063730442   2 RNPWADGPEYiTQCPIQPGGSYTYRFTMEDQEGTLWWHAHSRWLRAT-VYGALIIRPPLSSPhYPFPViPKREITLLLGE 80
Cdd:PLN02354   91 KNSWQDGVPG-TNCPIPPGTNFTYHFQPKDQIGSYFYYPSTGMHRAAgGFGGLRVNSRLLIP-VPYAD-PEDDYTVLIGD 167

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063730442  81 WWDRnpmDVLNLAQFTGAAPNIS--DAFTINGQPGDLYrcSSQETLrFLVGSGEIVLLRVINSALNQELFFGVANHKLTV 158
Cdd:PLN02354  168 WYTK---SHTALKKFLDSGRTLGrpDGVLINGKSGKGD--GKDEPL-FTMKPGKTYRYRICNVGLKSSLNFRIQGHKMKL 241

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063730442 159 VAADASYTKPFSTNVIMLGPGQTTDVLLTADQPPAHYYMAAhaynSANAAFDNTTTTAILKYKDascvtlqAKSQAraiP 238
Cdd:PLN02354  242 VEMEGSHVLQNDYDSLDVHVGQCFSVLVTANQAPKDYYMVA----STRFLKKVLTTTGIIRYEG-------GKGPA---S 307

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063730442 239 AQLPgfndtataaaftaqmKSPSKVKVPLeideNLFFTVGLGLF-NCPTPNTQ-----------------RCQGPNGTRF 300
Cdd:PLN02354  308 PELP---------------EAPVGWAWSL----NQFRSFRWNLTaSAARPNPQgsyhygkinitrtiklvNSASKVDGKL 368

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063730442 301 TASINNVSFVFPkQNSIMQAYYQGTPTGVFT----TDFPPTPPVTFDYTGNVSRglwqptrgtkaykLKFNSQVQIILqd 376
Cdd:PLN02354  369 RYALNGVSHVDP-ETPLKLAEYFGVADKVFKydtiKDNPPAKITKIKIQPNVLN-------------ITFRTFVEIIF-- 432

                         410       420       430       440       450       460       470
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1063730442 377 tsivttENH-----PMHLHGYEFYVVGTGVGNFNPNTdTSSFNLIDPPRRNTIGTPPGGWVAIRFVANNPGAW 444
Cdd:PLN02354  433 ------ENHeksmqSWHLDGYSFFAVAVEPGTWTPEK-RKNYNLLDAVSRHTVQVYPKSWAAILLTFDNAGMW 498
Cu-oxidase_3 pfam07732
Multicopper oxidase; This entry contains many divergent copper oxidase-like domains that are ...
 2-60 7.29e-25

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: 98.86  E-value: 7.29e-25
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063730442   2 RNPWADGPEYITQCPIQPGGSYTYRFTMEDQEGTLWWHAHSRWLRA-TVYGALIIRPPLS 60
Cdd:pfam07732  60 GTPWMDGVPGVTQCPIPPGQSFTYRFQVKQQAGTYWYHSHTSGQQAaGLAGAIIIEDRAS 119
PLN00044 PLN00044
multi-copper oxidase-related protein; Provisional
 2-444 7.86e-25

multi-copper oxidase-related protein; Provisional


Pssm-ID: 165622 [Multi-domain]  Cd Length: 596  Bit Score: 107.83  E-value: 7.86e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063730442   2 RNPWADGPEYiTQCPIQPGGSYTYRFTMEDQEGTLWWHAHSRWLRATV-YGALIIRPPLSSPhYPFPVIPKREITLLLGE 80
Cdd:PLN00044   93 KSAWQDGVGG-TNCAIPAGWNWTYQFQVKDQVGSFFYAPSTALHRAAGgYGAITINNRDVIP-IPFGFPDGGDITLFIAD 170

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063730442  81 WWDRNPMDvLNLAQFTGAAPNISDAFTING-----------QPGDLYRcssqetlRFLVGSGEIVLLRVINSALNQELFF 149
Cdd:PLN00044  171 WYARDHRA-LRRALDAGDLLGAPDGVLINAfgpyqyndslvPPGITYE-------RINVDPGKTYRFRVHNVGVATSLNF 242

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063730442 150 GVANHKLTVVAADASYTKPFSTNVIMLGPGQTTDVLLTADQ-PPAHYYMAAHAYNSANAAFDNTTTTAILKYKDascvtl 228
Cdd:PLN00044  243 RIQGHNLLLVEAEGSYTSQQNYTNLDIHVGQSYSFLLTMDQnASTDYYVVASARFVDAAVVDKLTGVAILHYSN------ 316

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063730442 229 qakSQARAIPAQLPGFNDTATAAAFTAQMKSPSKVKVPLEIDENLFFTVGLGLFNCPTPNTQRCQGPN--GTRFTASINN 306
Cdd:PLN00044  317 ---SQGPASGPLPDAPDDQYDTAFSINQARSIRWNVTASGARPNPQGSFHYGDITVTDVYLLQSMAPEliDGKLRATLNE 393

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063730442 307 VSFVFPkQNSIMQAYYQGTPtGVFTTDFPPTPpvtfdytgnVSRglwQPTRGTKAYKLKFNSQVQIILQDTSivtTENHP 386
Cdd:PLN00044  394 ISYIAP-STPLMLAQIFNVP-GVFKLDFPNHP---------MNR---LPKLDTSIINGTYKGFMEIIFQNNA---TNVQS 456

                         410       420       430       440       450
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1063730442 387 MHLHGYEFYVVGTGVGNFNPNTdTSSFNLIDPPRRNTIGTPPGGWVAIRFVANNPGAW 444
Cdd:PLN00044  457 YHLDGYAFFVVGMDYGLWTDNS-RGTYNKWDGVARSTIQVFPGAWTAILVFLDNAGIW 513
PLN02792 PLN02792
oxidoreductase
 2-444 2.19e-24

oxidoreductase


Pssm-ID: 178389 [Multi-domain]  Cd Length: 536  Bit Score: 106.22  E-value: 2.19e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063730442   2 RNPWADGPeYITQCPIQPGGSYTYRFTMEDQEGTLWWHAHSRWLRAT-VYGALIIrppLSSPHYPFPVI-PKREITLLLG 79
Cdd:PLN02792   80 KNSYQDGV-YGTTCPIPPGKNYTYDFQVKDQVGSYFYFPSLAVQKAAgGYGSLRI---YSLPRIPVPFPePAGDFTFLIG 155

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063730442  80 EWWDRNPMDVLNLAQFTGAAPNISDAFTINGQpGDLYRCSsqetlrFLVGSGEIVLLRVINSALNQELFFGVANHKLTVV 159
Cdd:PLN02792  156 DWYRRNHTTLKKILDGGRKLPLMPDGVMINGQ-GVSYVYS------ITVDKGKTYRFRISNVGLQTSLNFEILGHQLKLI 228

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063730442 160 AADASYTKPFSTNVIMLGPGQTTDVLLTADQPPAHY-------YMAAHAYNSANAAFDNTTTTAILKYK--DASCVTLQA 230
Cdd:PLN02792  229 EVEGTHTVQSMYTSLDIHVGQTYSVLVTMDQPPQNYsivvstrFIAAKVLVSSTLHYSNSKGHKIIHARqpDPDDLEWSI 308

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063730442 231 KsQARAIPAQLPGFNDTATAAAFTAQMKspskvkvpLEIDENLFFTVGLGLfncptpnTQRCQgpngtRFtaSINNVSFV 310
Cdd:PLN02792  309 K-QAQSIRTNLTASGPRTNPQGSYHYGK--------MKISRTLILESSAAL-------VKRKQ-----RY--AINGVSFV 365

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063730442 311 FPKQNSIMQAYYQgtPTGVFTTDFPPTppvtfdytgnvsrglwQPTRG------TKAYKLKFNSQVQIILQDTSIVTten 384
Cdd:PLN02792  366 PSDTPLKLADHFK--IKGVFKVGSIPD----------------KPRRGggmrldTSVMGAHHNAFLEIIFQNREKIV--- 424

                         410       420       430       440       450       460
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063730442 385 HPMHLHGYEFYVVGTGVGNFNpNTDTSSFNLIDPPRRNTIGTPPGGWVAIRFVANNPGAW 444
Cdd:PLN02792  425 QSYHLDGYNFWVVGINKGIWS-RASRREYNLKDAISRSTTQVYPESWTAVYVALDNVGMW 483
CuRO_3_Diphenol_Ox cd13904
The third cupredoxin domain of fungal laccase, diphenol oxidase; Diphenol oxidase belongs to ...
 384-463 4.44e-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: 95.44  E-value: 4.44e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063730442 384 NHPMHLHGYEFYVVGTGVGNFNP-NTDTSSFNLIDPPRRNTIGTPPGGWVAIRFVANNPGAWLMHCHIDshifWGLAMVF 462
Cdd:cd13904    77 DHPYHLHGVDFHIVARGSGTLTLeQLANVQYNTTNPLRRDTIVIPGGSWAVLRIPADNPGVWALHCHIG----WHLAAGF 152


                  .
gi 1063730442 463 L 463
Cdd:cd13904   153 A 153
CuRO_3_AAO_like_2 cd13895
The third cupredoxin domain of Ascorbate oxidase homologs; This family includes fungal ...
 343-463 9.08e-22

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: 92.38  E-value: 9.08e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063730442 343 DYTGNVSRGLWQPTrgTKAYKLKFNSQVQIILQDTSIVT--TENHPMHLHGYEFYVVGTGVGNFNPNTDTSSFNLI--DP 418
Cdd:cd13895    51 DYEAALANGGFDPE--TNTFPAKLGEVLDIVWQNTASPTggLDAHPWHAHGAHYYDLGSGLGTYSATALANEEKLRgyNP 128

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1063730442 419 PRRNT-----------IGTP--PGGWVAIRFVANNPGAWLMHCHIDSHIFWGLAMVFL 463
Cdd:cd13895   129 IRRDTtmlyryggkgyYPPPgtGSGWRAWRLRVDDPGVWMLHCHILQHMIMGMQTVWV 186
CuRO_1_LCC_like cd04206
Cupredoxin domain 1 of laccase-like multicopper oxidases; including laccase, CueO, spore coat ...
 3-56 4.07e-19

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: 83.10  E-value: 4.07e-19
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1063730442   3 NPWADGPEYITQCPIQPGGSYTYRFTMEDQEGTLWWHAHSRWLRA-TVYGALIIR 56
Cdd:cd04206    66 TNDGDGVAGLTQCPIPPGESFTYRFTVDDQAGTFWYHSHVGGQRAdGLYGPLIVE 120
CuRO_1_tcLCC2_insect_like cd13858
The first cupredoxin domain of insect laccases similar to laccase 2 in Tribolium castaneum; ...
 2-56 1.75e-18

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: 80.66  E-value: 1.75e-18
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1063730442   2 RNPWADGPEYITQCPIQPGGSYTYRFTMeDQEGTLWWHAHSRWLRA-TVYGALIIR 56
Cdd:cd13858    51 GTPYMDGVPMVTQCPILPGQTFRYKFKA-DPAGTHWYHSHSGTQRAdGLFGALIVR 105
CuRO_3_CopA cd13896
The third cupredoxin domain of CopA copper resistance protein family; CopA is a multicopper ...
 340-464 2.40e-18

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: 80.38  E-value: 2.40e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063730442 340 VTFDYTGNVSRGLWqpTRGTKAY------KLKFNSQVQIILQDTsivTTENHPMHLHGYEFYVVgtgvgnfNPNTDTSsf 413
Cdd:cd13896     4 IELHLTGNMERYVW--TINGKAYpdadplRVREGERVRIVFVND---TMMAHPMHLHGHFFQVE-------NGNGEYG-- 69

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1063730442 414 nlidpPRRNTIGTPPGGWVAIRFVANNPGAWLMHCHIDSHIFWGLAMVFLV 464
Cdd:cd13896    70 -----PRKDTVLVPPGETVSVDFDADNPGRWAFHCHNLYHMEAGMMRVVEY 115
CuRO_2_MaLCC_like cd13880
The second cupredoxin domain of the fungal laccases similar to Ma-LCC from Melanocarpus ...
 75-224 2.34e-17

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: 79.22  E-value: 2.34e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063730442  75 TLLLGEWWDRNPMDVLNLAQFTGAAPnISDAFTINGQpGDlYRCSSQETLRFLVG--SGEIVLLRVINSALNQELFFGVA 152
Cdd:cd13880     3 PVLLTDWYHRSAFELFSEELPTGGPP-PMDNILINGK-GK-FPCSTGAGSYFETTftPGKKYRLRLINTGVDTTFRFSID 79

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1063730442 153 NHKLTVVAADASYTKPFSTNVIMLGPGQTTDVLLTADQPPA-HYYM-AAHAYNSANAAFDNTTTTAILKYKDAS 224
Cdd:cd13880    80 GHNLTVIAADFVPIVPYTTDSLNIGIGQRYDVIVEANQDPVgNYWIrAEPATGCSGTNNNPDNRTGILRYDGAS 153
CuRO_2_Tv-LCC_like cd13882
The second cupredoxin domain of the fungal laccases similar to Tv-LCC from Trametes versicolor; ...
 76-223 3.79e-17

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: 78.60  E-value: 3.79e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063730442  76 LLLGEWWDRNPMDVLNLaqfTGAAPNISDAFTING----QPGDlyrcssQETLRFL-VGSGEIVLLRVINSALNQELFFG 150
Cdd:cd13882     3 ITLGDWYHTAAPDLLAT---TAGVPPVPDSGTINGkgrfDGGP------TSPLAVInVKRGKRYRFRVINISCIPSFTFS 73

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1063730442 151 VANHKLTVVAADASYTKPFSTNVIMLGPGQTTDVLLTADQPPAHYYMAAHAYNSANAAFDNTTTTAILKYKDA 223
Cdd:cd13882    74 IDGHNLTVIEADGVETKPLTVDSVQIYAGQRYSVVVEANQPVDNYWIRAPPTGGTPANNGGQLNRAILRYKGA 146
CuRO_1_Diphenol_Ox cd13857
The first cupredoxin domain of fungal laccase, diphenol oxidase; Diphenol oxidase belongs to ...
 4-55 4.86e-17

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: 76.91  E-value: 4.86e-17
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1063730442   4 PWADGPEYITQCPIQPGGSYTYRFTMEDQEGTLWWHAHSRWLRAT-VYGALII 55
Cdd:cd13857    66 NWMDGTAGITQCPIPPGGSFTYNFTVDGQYGTYWYHSHYSTQYADgLVGPLIV 118
CuRO_D2_2dMcoN_like cd04202
The second cupredoxin domain of bacterial two domain multicopper oxidase McoN and similar ...
 380-454 1.30e-16

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: 76.52  E-value: 1.30e-16
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1063730442 380 VTTENHPMHLHGYEFYVVGTGvGNFNPNTDtssfnlidPPRRNTIGTPPGGWVAIRFVANNPGAWLMHCHIDSHI 454
Cdd:cd04202    58 LSMDHHPMHLHGHFFLVTATD-GGPIPGSA--------PWPKDTLNVAPGERYDIEFVADNPGDWMFHCHKLHHA 123
CuRO_2_Abr2_like cd13876
The second cupredoxin domain of a group of fungal Laccases similar to Abr2 from Aspergillus ...
 76-221 1.82e-15

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: 73.01  E-value: 1.82e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063730442  76 LLLGEWWDRNPMDVLNLAQFTGAAPNISDAFTINGQpgdlyrcSSQETLRFLVGSGE-IVLLRVINSALNQELFFGVANH 154
Cdd:cd13876     3 IILSDWRHLTSEEYWKIMRASGIEPFCYDSILINGK-------GRVYCLIVIVDPGErWVSLNFINAGGFHTLAFSIDEH 75

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1063730442 155 KLTVVAADASYTKPFSTNVIMLGPGQTTDVLLTADQPPAHYYMAAHaynsANAAFDNTTTTAILKYK 221
Cdd:cd13876    76 PMWVYAVDGGYIEPQLVDAISITNGERYSVLVKLDKPPGDYTIRVA----STGAPQVISGYAILRYK 138
CuRO_1_Abr2_like cd13850
The first cupredoxin domain of a group of fungal Laccases similar to Abr2 from Aspergillus ...
 4-56 5.00e-15

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: 71.17  E-value: 5.00e-15
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1063730442   4 PWADGPEYITQCPIQPGGSYTYRFTMEDQEGTLWWHAHSRWLRAT-VYGALIIR 56
Cdd:cd13850    64 PWSDGVPGVTQWPIQPGGSFTYRWKAEDQYGLYWYHSHYRGYYMDgLYGPIYIR 117
CuRO_1_Tv-LCC_like cd13856
The first cupredoxin domain of fungal laccases similar to Tv-LCC from Trametes versicolor; ...
 2-41 5.37e-14

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: 68.52  E-value: 5.37e-14
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|
gi 1063730442   2 RNPWADGPEYITQCPIQPGGSYTYRFTMEDQEGTLWWHAH 41
Cdd:cd13856    69 GTNYADGPAFVTQCPIAPNHSFTYDFTAGDQAGTFWYHSH 108
CuRO_2_AAO_like_1 cd13872
The second cupredoxin domain of plant pollen multicopper oxidase homologous to ascorbate ...
 73-220 1.23e-13

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: 67.81  E-value: 1.23e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063730442  73 EITLLLGEWWDrnpMDVLNLAQF--TGAAPNISDAFTINGQPGdlYRCSSQETLrFLVGSGEIVLLRVINSALNQELFFG 150
Cdd:cd13872     2 EYTVLIGDWYK---TDHKTLRQSldKGRTLGRPDGILINGKGP--YGYGANETS-FTVEPGKTYRLRISNVGLRTSLNFR 75

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1063730442 151 VANHKLTVVAADASYTKPFSTNVIMLGPGQTTDVLLTADQPPAHYYMAahaynsANAAFDNT--TTTAILKY 220
Cdd:cd13872    76 IQGHKMLLVETEGSYTAQNTYDSLDVHVGQSYSVLVTADQSPKDYYIV------ASSRFLSPelTGVAILHY 141
CuRO_2_AAO cd13871
The second cupredoxin domain of plant Ascorbate oxidase; Ascorbate oxidase catalyzes the ...
 73-220 2.21e-13

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


Pssm-ID: 259939 [Multi-domain]  Cd Length: 166  Bit Score: 67.95  E-value: 2.21e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063730442  73 EITLLLGEWWDRNPMDvlnlaQFTGAApniSDAFTINGQPGDL-------YRCS-----------------SQETLRFL- 127
Cdd:cd13871     3 ELNILLSDWWHKSIYE-----QETGLS---SKPFRWVGEPQSLliegrgrYNCSlapaypsslpspvcnksNPQCAPFIl 74

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063730442 128 -VGSGEIVLLRVINSALNQELFFGVANHKLTVVAADASYTKPFSTNVIMLGPGQTTDVLLTADQPPAHYYMAAHAYNSAN 206
Cdd:cd13871    75 hVSPGKTYRLRIASVTALSSLNFIIEGHNLTVVEADGNYVQPFEVSNLDIYSGETYSVLVTADQDPSRNYWVSVNVRGRR 154

                         170
                  ....*....|....
gi 1063730442 207 AAfdNTTTTAILKY 220
Cdd:cd13871   155 PN--TPPGLAILNY 166
CuRO_1_Fet3p cd13851
The first Cupredoxin domain of multicopper oxidase Fet3P; Fet3p catalyzes the ferroxidase ...
 4-43 4.90e-13

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: 65.75  E-value: 4.90e-13
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|
gi 1063730442   4 PWADGPEYITQCPIQPGGSYTYRFTMEDQEGTLWWHAHSR 43
Cdd:cd13851    68 NYMDGPVGVTQCPIPPGQSFTYEFTVDTQVGTYWYHSHDG 107
CuRO_1_AAO cd13845
The first cupredoxin domain of plant Ascorbate oxidase; Ascorbate oxidase catalyzes the ...
 3-57 6.59e-13

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: 65.16  E-value: 6.59e-13
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1063730442   3 NPWADGPEYITQCPIQPGGSYTYRFTMeDQEGTLWWHAHSRWLR-ATVYGALIIRP 57
Cdd:cd13845    66 TPWADGTASVSQCPINPGETFTYQFVV-DRPGTYFYHGHYGMQRsAGLYGSLIVDP 120
CuRO_2_tcLCC_insect_like cd13884
The second cupredoxin domain of the insect laccases similar to laccase 2 in Tribolium ...
 73-220 1.04e-12

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: 65.72  E-value: 1.04e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063730442  73 EITLLLGEWWDRNPMDVLnLAQFTGAAPNISDAFTINGQpGDLYRCSSQETL-----RFLVGSGEIVLLRVINSA-LNQE 146
Cdd:cd13884     1 EHVILIQDWTHELSSERF-VGRGHNGGGQPPDSILINGK-GRYYDPKTGNTNntpleVFTVEQGKRYRFRLINAGaTNCP 78

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1063730442 147 LFFGVANHKLTVVAADASYTKPFSTNVIMLGPGQTTDVLLTADQPPAHYYMAAHAYNSANaaFDNTTTTAILKY 220
Cdd:cd13884    79 FRVSIDGHTLTVIASDGNDVEPVEVDSIIIYPGERYDFVLNANQPIGNYWIRARGLEDCD--NRRLQQLAILRY 150
CuRO_3_AAO_like_1 cd13894
The third cupredoxin domain of plant Ascorbate oxidase homologs; This subfamily is composed of ...
 327-444 1.35e-12

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: 64.37  E-value: 1.35e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063730442 327 TGVFTTDFPPTPPvTFDytgnvsrglwQPTRGTKAYKLKFNSQVQIILQ--DTSIvttenHPMHLHGYEFYVVGTGVGNF 404
Cdd:cd13894    15 KGVFQLDSIPDPP-TRK----------TPYLGTSVINGTYRGFIEIVFQnnEDTV-----QSWHLDGYSFFVVGMGFGDW 78

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 1063730442 405 NPNTdTSSFNLIDPPRRNTIGTPPGGWVAIRFVANNPGAW 444
Cdd:cd13894    79 TPEK-RKSYNLLDAVSRSTTQVYPGSWTAILLELDNVGMW 117
CuRO_3_CumA_like cd13906
The third cupredoxin domain of CumA like multicopper oxidase; This multicopper oxidase (MCO) ...
 374-464 1.83e-12

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: 64.71  E-value: 1.83e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063730442 374 LQDTSIVTTEN-----HPMHLHGYEFYVVG-TGVgnfnpntdtssfNLIDPPRRNTIGTPPGGWVAIRFVANNPGAWLMH 447
Cdd:cd13906    53 RGRSYVLRLVNetaflHPMHLHGHFFRVLSrNGR------------PVPEPFWRDTVLLGPKETVDIAFVADNPGDWMFH 120

                          90
                  ....*....|....*..
gi 1063730442 448 CHIDSHIFWGLAMVFLV 464
Cdd:cd13906   121 CHILEHQETGMMGVIRV 137
CuRO_2_Fet3p_like cd13877
The second Cupredoxin domain of multicopper oxidase Fet3P; Fet3p catalyzes the ferroxidase ...
 73-189 2.70e-12

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: 64.50  E-value: 2.70e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063730442  73 EITLLLGEWWDrNPMDVL-----NLAQFTGAAPnISDAFTINGqpgdlyrcSSQETLRFlvGSGEIVLLRVINSALNQEL 147
Cdd:cd13877     2 EVTLTLSDWYH-DQSPDLlrdflSPYNPTGAEP-IPDSSLFND--------TQNATINF--EPGKTYLLRIINMGAFASQ 69

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 1063730442 148 FFGVANHKLTVVAADASYTKPFSTNVIMLGPGQTTDVLLTAD 189
Cdd:cd13877    70 YFHIEGHDMTIIEVDGVYVKPYPVDTLYIAVGQRYSVLVKAK 111
CuRO_3_MCO_like_3 cd13909
The third cupredoxin domain of uncharacterized multicopper oxidase; Multicopper Oxidases (MCOs) ...
 385-453 8.27e-12

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: 62.54  E-value: 8.27e-12
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1063730442 385 HPMHLHGYEFYVVGTgvgNFNPntdtssfnlidPPRRNTIGTPPGGWVAIRFVANNPGAWLMHCHIDSH 453
Cdd:cd13909    71 HGMHLHGHHFRAILP---NGAL-----------GPWRDTLLMDRGETREIAFVADNPGDWLLHCHMLEH 125
CuRO_2_CumA_like cd13885
The second cupredoxin domain of CumA like multicopper oxidase; This multicopper oxidase (MCO) ...
 72-193 4.48e-11

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: 60.42  E-value: 4.48e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063730442  72 REITLLLGEW----------WDRNPMDvlnlAQFTGAAPNISdafTINGQPgdlyrcssqeTLRFLVGSGEIVLLRVINS 141
Cdd:cd13885     1 RDLVWVLDDWrldpdgqavpGFGTPHD----AAHAGRIGNLY---TINGRV----------QPDFTVRAGERVRLRLINA 63

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1063730442 142 ALNQELFFGVANHKLTVVAADASYTKPF--STNVIMLGPGQTTDVLLTADQPPA 193
Cdd:cd13885    64 ANARVFALKFPGHEARVIALDGQPAEPFvaRNGAVVLAPGMRIDLVIDAPQAAG 117
CuRO_2_MCO_like_1 cd13886
The second cupredoxin domain of uncharacterized multicopper oxidase; Multicopper Oxidases ...
 103-220 5.60e-11

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: 60.75  E-value: 5.60e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063730442 103 SDAFTINGQPGDLYRcssqetlrflvgsgeivlLRVINSALNQELFFGVANHKLTVVAADASYTKPFSTNVIMLGPGQTT 182
Cdd:cd13886    59 GTYYNFTLEPNKTYR------------------LRLINAGSFADFTFSVDGHPLTVIEADGTLVEPVEVHSITISVAQRY 120

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
gi 1063730442 183 DVLLTADQP-PAHYYMAAH------AYNSANAafdNTTTTAILKY 220
Cdd:cd13886   121 SVILTTNQPtGGNFWMRAElntdcfTYDNPNL---DPDVRAIVSY 162
CuRO_3_MCO_like_2 cd13908
The third cupredoxin domain of uncharacterized multicopper oxidase; Multicopper Oxidases (MCOs) ...
 381-462 6.60e-11

The third cupredoxin domain of uncharacterized multicopper oxidase; Multicopper Oxidases (MCOs) are multi-domain enzymes that are able to couple oxidation of substrates with reduction of dioxygen to water. MCOs oxidize their substrate by accepting electrons at a mononuclear copper centre and transferring them to a trinuclear copper centre which binds a dioxygen. The dioxygen, following the transfer of four electrons, is reduced to two molecules of water. These MCOs are capable of oxidizing a vast range of substrates, varying from aromatic to inorganic compounds such as metals. This subfamily of MCOs is composed of three cupredoxin domains. The cupredoxin domain 3 of 3-domain MCOs contains the Type 1 (T1) copper binding site and part the trinuclear copper binding site, which is located at the interface of domains 1 and 3.


Pssm-ID: 259975 [Multi-domain]  Cd Length: 122  Bit Score: 59.77  E-value: 6.60e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063730442 381 TTENHPMHLHGYEFYVVGTGvgnfnpNTDTSSFnlidppRRNTIGTPPGGWVAIRFVANNPGAWLMHCHIDSHIFWGLAM 460
Cdd:cd13908    51 SDDAHPMHLHRHTFEVTRID------GKPTSGL------RKDVVMLGGYQRVEVDFVADNPGLTLFHCHQQLHMDYGFMA 118


                  ..
gi 1063730442 461 VF 462
Cdd:cd13908   119 LF 120
CuRO_1_MaLCC_like cd13854
The first cupredoxin domain of the fungal laccases similar to Ma-LCC from Melanocarpus ...
 3-55 1.07e-10

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: 59.18  E-value: 1.07e-10
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1063730442   3 NPWADGPEYITQCPIQPGGSYTYRFTMeDQEGTLWWHAH-SRWLRATVYGALII 55
Cdd:cd13854    69 TNWQDGVPGVTECPIAPGDTRTYRFRA-TQYGTSWYHSHySAQYGDGVVGPIVI 121
CuRO_1_CopA cd13848
The first cupredoxin domain of CopA copper resistance protein family; CopA is a multicopper ...
 7-55 3.83e-10

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: 57.29  E-value: 3.83e-10
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|
gi 1063730442   7 DGPEYITQCPIQPGGSYTYRFTMEdQEGTLWWHAHSRWLRAT-VYGALII 55
Cdd:cd13848    67 DGVPGLSFPGIKPGETFTYRFPVR-QSGTYWYHSHSGLQEQTgLYGPIII 115
CuRO_3_McoC_like cd13902
The third cupredoxin domain of a multicopper oxidase McoC and similar proteins; This family ...
 385-453 5.62e-10

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: 57.02  E-value: 5.62e-10
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1063730442 385 HPMHLHGYEFYVVGTGVGNFNPntdtssfnlidPPR--RNTIGTPPGGWVAIRFVANNPGAWLMHCHIDSH 453
Cdd:cd13902    55 HPFHLHGTQFQVLEIDGNPQKP-----------EYRawKDTVNLPPGEAVRIATRQDDPGMWMYHCHILEH 114
CuRO_1_2dMco_1 cd13860
The first cupredoxin domain of bacteria two domain multicopper oxidase; This subfamily ...
 7-56 1.53e-08

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: 52.58  E-value: 1.53e-08
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1063730442   7 DGPEYITQCPIQPGGSYTYRFTMEdQEGTLWWHAH---SRWLRATVYGALIIR 56
Cdd:cd13860    68 DGVPGITQPPIQPGETFTYEFTAK-QAGTYMYHSHvdeAKQEDMGLYGAFIVH 119
CuRO_2_Diphenol_Ox cd13883
The second cupredoxin domain of fungal laccase, diphenol oxidase; Diphenol oxidase belongs to ...
 97-221 3.11e-08

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: 53.11  E-value: 3.11e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063730442  97 GAAPNISDAFTINGQ-------PGDLYRCSSQETLRFLVGSGEIVLLRVINSALNQELFFGVANHKLTVVAADAS-YTKP 168
Cdd:cd13883    29 SPAAPSPDSALINGIgqfncsaADPGTCCTQTSPPEIQVEAGKRTRFRLINAGSHAMFRFSVDNHTLNVVEADDTpVYGP 108

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1063730442 169 FSTNVIMLGPGQTTDVLLTADQPPA--HYYM-AAHAYNSANAAFDNTTTTAILKYK 221
Cdd:cd13883   109 TVVHRIPIHNGQRYSVIIDTTSGKAgdSFWLrARMATDCFAWDLQQQTGKAILRYV 164
CuRO_2_CopA cd13874
The second cupredoxin domain of CopA copper resistance protein family; CopA is a multicopper ...
 85-187 3.41e-08

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: 51.53  E-value: 3.41e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063730442  85 NPMDvlnLAQFTGaapnisDAFTINGQPGdlyrcSSQETLRFLVGsgEIVLLRVINSALNQELFFGVANHKLTVVAADAS 164
Cdd:cd13874     2 DPMD---ISDVYY------DTYLINGKPP-----EDNWTGLFKPG--ERVRLRFINAAASTYFDVRIPGGKMTVVAADGQ 65

                          90       100
                  ....*....|....*....|...
gi 1063730442 165 YTKPFSTNVIMLGPGQTTDVLLT 187
Cdd:cd13874    66 DVRPVEVDEFRIGVAETYDVIVT 88
CuRO_1_CumA_like cd13861
The first cupredoxin domain of CumA like multicopper oxidase; This multicopper oxidase (MCO) ...
 7-56 2.93e-07

The first cupredoxin domain of CumA like multicopper oxidase; This multicopper oxidase (MCO) subfamily includes CumA from Pseudomonas putida, which is involved in the oxidation of Mn(II). However, the cumA gene has been identified in a variety of bacterial species, including both Mn(II)-oxidizing and non-Mn(II)-oxidizing strains. Thus, the proteins in this family may catalyze the oxidation of other substrates. MCO catalyzes the oxidation of a variety aromatic - notably phenolic and inorganic substances coupled to the reduction of molecular oxygen to water and has been implicated in a wide spectrum of biological activities and, in particular, plays a key role in morphogenesis, development and lignin metabolism. Although MCOs have diverse functions, majority of them have three cupredoxin domain repeats that include one mononuclear and one trinuclear copper center. The copper ions are bound in several sites: Type 1, Type 2, and/or Type 3. The ensemble of types 2 and 3 copper is called a trinuclear cluster. MCOs oxidize their substrate by accepting electrons at a mononuclear copper center and transferring them to the active site trinuclear copper center. The cupredoxin domain 1 of 3-domain MCOs contains part the trinuclear copper binding site, which is located at the interface of domains 1 and 3.


Pssm-ID: 259930 [Multi-domain]  Cd Length: 119  Bit Score: 49.16  E-value: 2.93e-07
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1063730442   7 DGPEYITQCPIQPGGSYTYRFTMEDQeGTLWWHAHSR---WLRATVYGALIIR 56
Cdd:cd13861    68 DGVPGLTQPPVPPGESFTYEFTPPDA-GTYWYHPHVGsqeQLDRGLYGPLIVE 119
CuRO_2_AAO_like_2 cd13873
The second cupredoxin domain of plant Ascorbate oxidase homologs; This family includes plant ...
 73-188 3.73e-07

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


Pssm-ID: 259941 [Multi-domain]  Cd Length: 161  Bit Score: 49.98  E-value: 3.73e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063730442  73 EITLLLGEWW---DRNPMDVLNLAQFTgaAPNISDAFTINGQPG------DLYRCSSQETLRFL-VGSGEIVLLRVI-NS 141
Cdd:cd13873     2 ERILLFSDYFpktDSTIETGLTATPFV--WPGEPNALLVNGKSGgtcnksATEGCTTSCHPPVIdVEPGKTYRFRFIgAT 79

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*...
gi 1063730442 142 ALNQeLFFGVANH-KLTVVAADASYTKPFSTNVIMLGPGQTTDVLLTA 188
Cdd:cd13873    80 ALSF-VSLGIEGHdNLTIIEADGSYTKPAETDHLQLGSGQRYSFLLKT 126
CuRO_2_CopA_like_1 cd13870
The second cupredoxin domain of CopA copper resistance protein like family; The members of ...
 126-190 4.29e-07

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: 48.48  E-value: 4.29e-07
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1063730442 126 FLVGSGEIVLLRVINSALNQELFFGVANHKLTVVAADASYTKPFSTNVIMLGPGQTTDVLLTADQ 190
Cdd:cd13870    31 FTARPGDRLRLRLINAAGDTAFRVALAGHRLTVTHTDGFPVEPVEVDALLIGMGERYDAIVTANN 95
CuRO_1_LCC_like_3 cd13865
The second cupredoxin domain of uncharacterized multicopper oxidase; Multicopper Oxidases ...
 4-41 3.11e-06

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: 46.15  E-value: 3.11e-06
                          10        20        30
                  ....*....|....*....|....*....|....*....
gi 1063730442   4 PWA-DGPEYITQCPIQPGGSYTYRFTMeDQEGTLWWHAH 41
Cdd:cd13865    61 PNLqDGVPDVTQPPIPPGQSQRYDFPL-VQPGTFWMHSH 98
CuRO_D1_2dMcoN_like cd13859
The first cupredoxin domain of bacterial two domain multicopper oxidase McoN and similar ...
 2-41 5.84e-06

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: 45.55  E-value: 5.84e-06
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|.
gi 1063730442   2 RNPW-ADGPEYITQCPIQPGGSYTYRFTMeDQEGTLWWHAH 41
Cdd:cd13859    64 MGSWkMDGVPGVTQPAIEPGESFTYKFKA-ERPGTLWYHCH 103
CuRO_1_MCO_like_2 cd13864
The second cupredoxin domain of uncharacterized multicopper oxidase; Multicopper Oxidases ...
 7-42 6.77e-06

The second cupredoxin domain of uncharacterized multicopper oxidase; Multicopper Oxidases (MCOs) are multi-domain enzymes that are able to couple oxidation of substrates with reduction of dioxygen to water. MCOs oxidize their substrate by accepting electrons at a mononuclear copper centre and transferring them to a trinuclear copper centre which binds a dioxygen. The dioxygen, following the transfer of four electrons, is reduced to two molecules of water. These MCOs are capable of oxidizing a vast range of substrates, varying from aromatic to inorganic compounds such as metals. This subfamily of MCOs is composed of three cupredoxin domains. The cupredoxin domain 1 of 3-domain MCOs contains part the trinuclear copper binding site, which is located at the interface of domains 1 and 3.


Pssm-ID: 259932 [Multi-domain]  Cd Length: 139  Bit Score: 45.60  E-value: 6.77e-06
                          10        20        30
                  ....*....|....*....|....*....|....*..
gi 1063730442   7 DGPEYITQCPIQPGGSYTYRFTM-EDQEGTLWWHAHS 42
Cdd:cd13864    87 DGVPGLTQYPIGVGESYWYNFTIpEDTCGTFWYHSHS 123
CuRO_2_McoC_like cd13881
The second cupredoxin domain of a multicopper oxidase McoC and similar proteins; This family ...
 95-203 7.32e-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: 45.68  E-value: 7.32e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063730442  95 FTGAAPNISDAFtiNGQPGDLYRCSSQETLRFLVGSGEIVLLRVINSALNQELFFGVANHKLTVVAADAS-YTKPFSTNV 173
Cdd:cd13881    15 GQLAEPSAADWM--FGREGDLVLVNGQLNPTITVRPGEVQRWRIVNAASARYFRLALDGHKFRLIGTDGGlLEAPREVDE 92

                          90       100       110
                  ....*....|....*....|....*....|
gi 1063730442 174 IMLGPGQTTDVLLTADQPPAHYYMAAHAYN 203
Cdd:cd13881    93 LLLAPGERAEVLVTAGEPGGRLVLLALPYD 122
CuRO_2_MCO_like_2 cd13887
The second cupredoxin domain of uncharacterized multicopper oxidase; Multicopper Oxidases ...
 128-187 7.42e-06

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: 45.01  E-value: 7.42e-06
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063730442 128 VGSGEIVLLRVINSALNQELFFGVANHKLTVVAADASYTKPFSTNVIMLGPGQTTDVLLT 187
Cdd:cd13887    28 VEPGGRVRLRVINGSTATNFHIDLGDLKGTLIAVDGNPVQPVEGRRFPLATAQRLDLLVT 87
CuRO_1_AAO_like_2 cd13847
The first cupredoxin domain of Ascorbate oxidase homologs; This family includes fungal ...
 4-55 8.09e-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: 8.09e-06
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1063730442   4 PWADGPEYITQCPIQPGGSYTYRFTME-DQEGTLWWHAHSRWLRATVYGALII 55
Cdd:cd13847    63 PFSDGTPLASQWPIPPGKFFDYEFPLEaGDAGTYYYHSHVGFQSVTAYGALIV 115
CuRO_3_MCO_like_1 cd13907
The third cupredoxin domain of uncharacterized multicopper oxidase; Multicopper Oxidases (MCOs) ...
 385-465 1.08e-05

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: 45.55  E-value: 1.08e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063730442 385 HPMHLHGYEFYVVG-TGVGNFNPNTDTSSFNLIDPPRRNTIGTPPGGWVAI--RFvANNPGAWLMHCHIDSHIFWGLAMV 461
Cdd:cd13907    72 HPIHLHGVQFQVLErSVGPKDRAYWATVKDGFIDEGWKDTVLVMPGERVRIikPF-DDYKGLFLYHCHNLEHEDMGMMRN 150


                  ....
gi 1063730442 462 FLVE 465
Cdd:cd13907   151 FLVE 154
CuRO_1_AAO_like_1 cd13846
The first cupredoxin domain of plant Ascorbate oxidase homologs; This subfamily is composed of ...
 2-55 1.11e-05

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: 44.71  E-value: 1.11e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1063730442   2 RNPWADGPeYITQCPIQPGGSYTYRFTMEDQEGTLWWHAHSRWLRAT-VYGALII 55
Cdd:cd13846    64 RNSWQDGV-LGTNCPIPPGWNWTYKFQVKDQIGSFFYFPSLHFQRAAgGFGGIRV 117
CuRO_6_ceruloplasmin cd11012
The sixth cupredoxin domain of Ceruloplasmin; Ceruloplasmin is a multicopper oxidase essential ...
 385-464 1.58e-05

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


Pssm-ID: 259898 [Multi-domain]  Cd Length: 145  Bit Score: 44.86  E-value: 1.58e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063730442 385 HPMHLHGYEFYVVGTGVGNfnpntdTSSFNLIdpprrntigtpPGGWVAIRFVANNPGAWLMHCHIDSHIFWGLAMVFLV 464
Cdd:cd11012    82 HTAHFHGHSFDYKHRGVYR------SDVFDLF-----------PGTFQTVEMIPRTPGTWLLHCHVTDHIHAGMETTYTV 144
CuRO_2_ceruloplasmin_like_2 cd11023
cupredoxin domain of ceruloplasmin homologs; Uncharacterized subfamily of ceruloplasmin ...
 388-464 1.52e-04

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


Pssm-ID: 259909 [Multi-domain]  Cd Length: 118  Bit Score: 41.44  E-value: 1.52e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1063730442 388 HLHGYefyvvGTGVGNFNPNTDTSSFnLIDPPRRNTIGT-PPGGWVAIRFVANNPGAWLMHCHIDSHIFWGLAMVFLV 464
Cdd:cd11023    47 HLVAY-----GNEVDFHTPHWHGQTV-EADKSRRTDVAElMPASMRVADMTAADVGTWLLHCHVHDHYMAGMMTQFAV 118
CuRO_3_CotA_like cd13891
The third Cupredoxin domain of bacterial laccases including CotA, a bacterial endospore coat ...
 381-453 7.50e-04

The third Cupredoxin domain of bacterial laccases including CotA, a bacterial endospore coat component; CotA protein is an abundant component of the outer coat layer in bacterial endospore coat and is required for spore resistance against hydrogen peroxide and UV light. CotA belongs to the laccase-like multicopper oxidase (MCO) family, which are able to couple oxidation of substrates with reduction of dioxygen to water. MCOs are capable of oxidizing a vast range of substrates, varying from aromatic compounds to inorganic compounds such as metals. Although the members of this family have diverse functions, majority of them have three cupredoxin domain repeats. The copper ions are bound in several sites: Type 1, Type 2, and/or Type 3. The ensemble of types 2 and 3 copper is called a trinuclear cluster. MCOs oxidize their substrate by accepting electrons at a mononuclear copper center and transferring them to the active site trinuclear copper center. The cupredoxin domain 3 of 3-domain MCOs contains the Type 1 (T1) copper binding site and part the trinuclear copper binding site, which is located at the interface of domains 1 and 3.


Pssm-ID: 259958 [Multi-domain]  Cd Length: 143  Bit Score: 39.97  E-value: 7.50e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063730442 381 TTENHPMHLHGYEFYVVGTGVGNFNPNTDTSSFNLIDPPR---------RNTIGTPPGGWVAI--RFvANNPGAWLMHCH 449
Cdd:cd13891    50 TPDAHPIHLHLVQFQVLDRQPFDVDEYNATGEIYYTGPPRppapnergwKDTVRAYPGEVTRIivRF-DGPEGGYVWHCH 128


                  ....
gi 1063730442 450 IDSH 453
Cdd:cd13891   129 ILEH 132
CuRO_D2_2dMcoN_like cd04202
The second cupredoxin domain of bacterial two domain multicopper oxidase McoN and similar ...
 72-191 8.77e-04

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: 39.54  E-value: 8.77e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063730442  72 REITLLLGEW---WDRNPMDvlnlaqFTGAAPNIsdaFTINGQ--PGDlyrcssqETLRflVGSGEIVLLRVINsalnqe 146
Cdd:cd04202     2 RDYTLVLQEWfvdPGTTPMP------PEGMDFNY---FTINGKsfPAT-------PPLV--VKEGDRVRIRLIN------ 57

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1063730442 147 lfFGVANHKL-------TVVAAD---ASYTKPFSTNVIMLGPGQTTDVLLTADQP 191
Cdd:cd04202    58 --LSMDHHPMhlhghffLVTATDggpIPGSAPWPKDTLNVAPGERYDIEFVADNP 110
CuRO_1_2DMCO_NIR_like cd11024
The cupredoxin domain 1 of a two-domain laccase related to nitrite reductase; The two-domain ...
 413-465 1.63e-03

The cupredoxin domain 1 of a two-domain laccase related to nitrite reductase; The two-domain laccase (small laccase) in this family differs significantly from all laccases. It resembles the two domain nitrite reductase in both sequence and structure. It consists of two cupredoxin domains and forms trimers and hence resembles the quaternary structure of nitrite reductases more than that of large laccases. There are three trinuclear copper clusters in the enzyme localized between domains 1 and 2 of each pair of neighbor chains. Three copper ions of type 1 lie close to one another near the surface of the central part of the trimer, and, effectively, a trimeric substrate binding site is formed in their vicinity. Laccase is a blue multi-copper enzyme that catalyzes the oxidation of a variety of organic substrates coupled to the reduction of molecular oxygen to water. It displays broad substrate specificity, catalyzing the oxidation of a wide variety of aromatic, notably phenolic, and inorganic substances. Laccase has been implicated in a wide spectrum of biological activities.


Pssm-ID: 259910 [Multi-domain]  Cd Length: 119  Bit Score: 38.41  E-value: 1.63e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1063730442 413 FNLIDPPRRNTIGT---PPGGWVAIRFVANNPGAWLMHCHID---SHIFWGLAMVFLVE 465
Cdd:cd11024    59 FHGIHDAAMDGTGLgpiMPGESFTYEFVAEPAGTHLYHCHVQplkEHIAMGLYGAFIVD 117
CuRO_1_McoP_like cd13852
The first cupredoxin domain of multicopper oxidase McoP and similar proteins; This family ...
 1-53 1.80e-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: 38.04  E-value: 1.80e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1063730442   1 MRNPWA-DG-PEYItqcpIQPGGSYTYRFTMEDQEGTLWWHAHSRWLRAT-VYGAL 53
Cdd:cd13852    54 LHVPAAmDGhPRYA----IDPGETYVYEFEVLNRAGTYWYHPHPHGLTAKqVYRGL 105
CuRO_3_Tth-MCO_like cd13900
The third cupredoxin domain of the bacterial laccases similar to Tth-MCO from Thermus ...
 381-453 1.82e-03

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: 38.38  E-value: 1.82e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1063730442 381 TTENHPMHLHGYEFYVVGTGvgnfNPNTDtssfnliDPPRRNTIGTPPGGWVAIR--FVaNNPGAWLMHCHIDSH 453
Cdd:cd13900    50 SGEDHPFHIHVNPFQVVSIN----GKPGL-------PPVWRDTVNVPAGGSVTIRtrFR-DFTGEFVLHCHILDH 112
CuRO_1_CuNIR cd11020
Cupredoxin domain 1 of Copper-containing nitrite reductase; Copper-containing nitrite ...
 426-465 2.06e-03

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: 37.96  E-value: 2.06e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|...
gi 1063730442 426 TPPGGWVAIRFVANNPGAWLMHC---HIDSHIFWGLAMVFLVE 465
Cdd:cd11020    75 IAPGETKTFSFKALYPGVFMYHCataPVLMHIANGMYGAIIVE 117
CuRO_2_ceruloplasmin_like cd04200
Cupredoxin domains 2, 4, and 6 of ceruloplasmin and similar proteins; This family includes the ...
 381-464 2.29e-03

Cupredoxin domains 2, 4, and 6 of ceruloplasmin and similar proteins; This family includes the second, fourth and sixth cupredoxin domains of ceruloplasmin and similar proteins, including the second, fourth, and sixth cupredoxin domains of unprocessed coagulation factors V and VIII. Ceruloplasmin (ferroxidase) is a multicopper oxidase essential for normal iron homeostasis. Ceruloplasmin also functions in copper transport, amine oxidase and as an antioxidant preventing free radicals in serum. The protein has 6 cupredoxin domains and exhibits internal sequence homology that appears to have evolved from the triplication of a sequence unit composed of two tandem cupredoxin domains. Human Factor VIII facilitates blood clotting by acting as a cofactor for factor IXa Factor VIII and IXa forms a complex in the presence of Ca+2 and phospholipids that converts factor X to the activated form Xa.


Pssm-ID: 259863 [Multi-domain]  Cd Length: 141  Bit Score: 38.55  E-value: 2.29e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063730442 381 TTENHPMHLHGYEFYVVGTgvgnfnpntdtssfnlidppRRNTIGTPPGGWVAIRFVANNPGAWLMHCHIDSHIFWGLAM 460
Cdd:cd04200    78 EVDVHSIHFHGQTFLYKGY--------------------RIDTLTLFPATFETVEMVPSNPGTWLLHCHNSDHRHAGMQA 137


                  ....
gi 1063730442 461 VFLV 464
Cdd:cd04200   138 YFLV 141
CuRO_1_McoC_like cd13855
The first cupredoxin domain of a multicopper oxidase McoC and similar proteins; This family ...
 16-41 7.19e-03

The first cupredoxin domain of a multicopper oxidase McoC and similar proteins; This family includes bacteria multicopper oxidases (MCOs) represented by McoC from pathogenic bacterium Campylobacter jejuni. McoC is a periplasmic multicopper oxidase, which has been characterized to be associated with copper homeostasis. McoC may also function to protect against oxidative stress as it may convert metallic ions into their less toxic form. MCOs are multi-domain enzymes that are able to couple oxidation of substrates with reduction of dioxygen to water. They are capable of oxidizing a vast range of substrates, varying from aromatic compunds to inorganic compounds such as metals. Most MCOs have three cupredoxin domain repeats that include one mononuclear and one trinuclear copper center. The copper ions are bound in several sites: Type 1, Type 2, and/or Type 3. The ensemble of types 2 and 3 copper is called a trinuclear cluster. MCOs oxidize their substrate by accepting electrons at a mononuclear copper center and transferring them to the active site trinuclear copper center. The cupredoxin domain 1 of 3-domain MCOs contains part the trinuclear copper binding site, which is located at the interface of domains 1 and 3.


Pssm-ID: 259924 [Multi-domain]  Cd Length: 121  Bit Score: 36.68  E-value: 7.19e-03
                          10        20
                  ....*....|....*....|....*..
gi 1063730442  16 PIQPGGSYTYRFTM-EDQEGTLWWHAH 41
Cdd:cd13855    75 PVAPGNDRVYRFTLpQDSAGTYWYHPH 101
CuRO_3_MCO_like_5 cd13911
The third cupredoxin domain of uncharacterized multicopper oxidase; Multicopper Oxidases (MCOs) ...
 381-453 9.63e-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: 35.98  E-value: 9.63e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1063730442 381 TTENHPMHLHGYEFYVVGTGVGNFNPNtdtssfnliDPPRRNTIGTPPGG--WVAIRFVANNpGAWLMHCHIDSH 453
Cdd:cd13911    45 SDGRHPVHLHGAHFQVVSRTGGRPGEW---------DAGWKDTVLLRPREsvTVIIRFDGYR-GRYVFHCHNLEH 109
 
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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