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Conserved domains on  [gi|330254725|gb|AEC09819|]
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laccase 5 [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 ...
27-580 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: 901.41  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330254725   27 KAHHHEFIIQATKVKRLCETHNSITVNGMFPGPMLVVNNGDTLVVKVINRARYNITIHWHGVRQMRTGWADGPEFVTQCP 106
Cdd:TIGR03389   2 EVRHYTFDVQEKNVTRLCSTKSILTVNGKFPGPTLYAREGDTVIVNVTNNVQYNVTIHWHGVRQLRNGWADGPAYITQCP 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330254725  107 IRPGSSYTYRFTIQGQEGTLWWHAHSSWLRATVYGSLLVFPPAGSSYPFTKPHRNVPLLLGEWWDANPVDVLRESIRTGG 186
Cdd:TIGR03389  82 IQPGQSYVYNFTITGQRGTLWWHAHISWLRATVYGAIVILPKPGVPYPFPKPDREVPIILGEWWNADVEAVINQANQTGG 161
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330254725  187 APNNSDAYTINGQPGDLYKCSSQDTTVVPINVGETILLRVINSALNQPLFFTVANHKLTVVGADASYLKPFTTNVIVLGP 266
Cdd:TIGR03389 162 APNVSDAYTINGHPGPLYNCSSKDTFKLTVEPGKTYLLRIINAALNDELFFAIANHTLTVVEVDATYTKPFKTKTIVIGP 241
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330254725  267 GQTTDVLITGDQPPNRYYMAARAYQSAQNApFGNTTTTAILQYKSAPCcgvgggsgtkkgnSFKPIMPILPAYNDTNTVT 346
Cdd:TIGR03389 242 GQTTNVLLTADQSPGRYFMAARPYMDAPGA-FDNTTTTAILQYKGTSN-------------SAKPILPTLPAYNDTAAAT 307
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330254725  347 RFSQSFRSLRR----AEVPTEIDENLFVTIGLGLNNCPKNfrsrRCQGPNGTRFTASMNNVSFALPsNYSLLQAHHHGIP 422
Cdd:TIGR03389 308 NFSNKLRSLNSaqypANVPVTIDRRLFFTIGLGLDPCPNN----TCQGPNGTRFAASMNNISFVMP-TTALLQAHYFGIS 382
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330254725  423 GVFTTDFPAKPPVKFDYTGNNISRSLYQPdRGTKLYKLKYGSRVQIVLQDTGIVTPENHPIHLHGYDFYIIAEGFGNFNP 502
Cdd:TIGR03389 383 GVFTTDFPANPPTKFNYTGTNLPNNLFTT-NGTKVVRLKFNSTVELVLQDTSILGSENHPIHLHGYNFFVVGTGFGNFDP 461
                         490       500       510       520       530       540       550
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 330254725  503 KKDTAKFNLEDPPLRNTVGVPVNGWAVIRFIADNPGVWIMHCHLDAHISWGLAMAFLVENGNGVLQTIEQPPHDLPVC 580
Cdd:TIGR03389 462 KKDPAKFNLVDPPERNTVGVPTGGWAAIRFVADNPGVWFMHCHLEVHTTWGLKMAFLVDNGKGPNQSLLPPPSDLPSC 539
 
Name Accession Description Interval E-value
laccase TIGR03389
laccase, plant; Members of this protein family include the copper-containing enzyme laccase ...
27-580 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: 901.41  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330254725   27 KAHHHEFIIQATKVKRLCETHNSITVNGMFPGPMLVVNNGDTLVVKVINRARYNITIHWHGVRQMRTGWADGPEFVTQCP 106
Cdd:TIGR03389   2 EVRHYTFDVQEKNVTRLCSTKSILTVNGKFPGPTLYAREGDTVIVNVTNNVQYNVTIHWHGVRQLRNGWADGPAYITQCP 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330254725  107 IRPGSSYTYRFTIQGQEGTLWWHAHSSWLRATVYGSLLVFPPAGSSYPFTKPHRNVPLLLGEWWDANPVDVLRESIRTGG 186
Cdd:TIGR03389  82 IQPGQSYVYNFTITGQRGTLWWHAHISWLRATVYGAIVILPKPGVPYPFPKPDREVPIILGEWWNADVEAVINQANQTGG 161
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330254725  187 APNNSDAYTINGQPGDLYKCSSQDTTVVPINVGETILLRVINSALNQPLFFTVANHKLTVVGADASYLKPFTTNVIVLGP 266
Cdd:TIGR03389 162 APNVSDAYTINGHPGPLYNCSSKDTFKLTVEPGKTYLLRIINAALNDELFFAIANHTLTVVEVDATYTKPFKTKTIVIGP 241
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330254725  267 GQTTDVLITGDQPPNRYYMAARAYQSAQNApFGNTTTTAILQYKSAPCcgvgggsgtkkgnSFKPIMPILPAYNDTNTVT 346
Cdd:TIGR03389 242 GQTTNVLLTADQSPGRYFMAARPYMDAPGA-FDNTTTTAILQYKGTSN-------------SAKPILPTLPAYNDTAAAT 307
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330254725  347 RFSQSFRSLRR----AEVPTEIDENLFVTIGLGLNNCPKNfrsrRCQGPNGTRFTASMNNVSFALPsNYSLLQAHHHGIP 422
Cdd:TIGR03389 308 NFSNKLRSLNSaqypANVPVTIDRRLFFTIGLGLDPCPNN----TCQGPNGTRFAASMNNISFVMP-TTALLQAHYFGIS 382
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330254725  423 GVFTTDFPAKPPVKFDYTGNNISRSLYQPdRGTKLYKLKYGSRVQIVLQDTGIVTPENHPIHLHGYDFYIIAEGFGNFNP 502
Cdd:TIGR03389 383 GVFTTDFPANPPTKFNYTGTNLPNNLFTT-NGTKVVRLKFNSTVELVLQDTSILGSENHPIHLHGYNFFVVGTGFGNFDP 461
                         490       500       510       520       530       540       550
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 330254725  503 KKDTAKFNLEDPPLRNTVGVPVNGWAVIRFIADNPGVWIMHCHLDAHISWGLAMAFLVENGNGVLQTIEQPPHDLPVC 580
Cdd:TIGR03389 462 KKDPAKFNLVDPPERNTVGVPTGGWAAIRFVADNPGVWFMHCHLEVHTTWGLKMAFLVDNGKGPNQSLLPPPSDLPSC 539
CuRO_2_LCC_plant cd13875
The second cupredoxin domain of the plant laccases; Laccase is a blue multi-copper enzyme that ...
162-309 5.44e-87

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: 266.00  E-value: 5.44e-87
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330254725 162 VPLLLGEWWDANPVDVLRESIRTGGAPNNSDAYTINGQPGDLYKCSSQDTTVVPINVGETILLRVINSALNQPLFFTVAN 241
Cdd:cd13875    1 VPIILGEWWNRDVNDVEDQALLTGGGPNISDAYTINGQPGDLYNCSSKDTFVLTVEPGKTYLLRIINAALNEELFFKIAN 80
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 330254725 242 HKLTVVGADASYLKPFTTNVIVLGPGQTTDVLITGDQPPNRYYMAARAYQSAQNAPFGNTTTTAILQY 309
Cdd:cd13875   81 HTLTVVAVDASYTKPFTTDYILIAPGQTTDVLLTADQPPGRYYMAARPYQSAPPVPFDNTTATAILEY 148
PLN02604 PLN02604
oxidoreductase
7-558 4.96e-83

oxidoreductase


Pssm-ID: 215324 [Multi-domain]  Cd Length: 566  Bit Score: 270.19  E-value: 4.96e-83
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330254725   7 LLCFISFVAFLLFSSVAEAnKAHHHEFIIQATKVKRLCETHNSITVNGMFPGPMLVVNNGDTLVVKVINR-ARYNITIHW 85
Cdd:PLN02604   4 FLALFFLLFSVLNFPAAEA-RIRRYKWEVKYEYKSPDCFKKLVITINGRSPGPTILAQQGDTVIVELKNSlLTENVAIHW 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330254725  86 HGVRQMRTGWADGPEFVTQCPIRPGSSYTYRFTIQgQEGTLWWHAHSSWLR-ATVYGSLLVFPPAGSSYPFTKPH-RNVp 163
Cdd:PLN02604  83 HGIRQIGTPWFDGTEGVTQCPILPGETFTYEFVVD-RPGTYLYHAHYGMQReAGLYGSIRVSLPRGKSEPFSYDYdRSI- 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330254725 164 lLLGEWW-----------DANPVDVLRES----IRTGGAPNNSDAyTINGQPGDLY-----KCSSQDTTVVPinvGETIL 223
Cdd:PLN02604 161 -ILTDWYhkstyeqalglSSIPFDWVGEPqsllIQGKGRYNCSLV-SSPYLKAGVCnatnpECSPYVLTVVP---GKTYR 235
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330254725 224 LRVINSALNQPLFFTVANHKLTVVGADASYLKPFTTNVIVLGPGQTTDVLITGDQPPNRYYMAARAYQSAQNA-PFGntt 302
Cdd:PLN02604 236 LRISSLTALSALSFQIEGHNMTVVEADGHYVEPFVVKNLFIYSGETYSVLVKADQDPSRNYWVTTSVVSRNNTtPPG--- 312
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330254725 303 tTAILQY------KSAPCcgvgggsgtkkgnsfkpIMPILPAYNDTNtvTRFSQSFR-SLRRAEV--PTEIDENLFVTIg 373
Cdd:PLN02604 313 -LAIFNYypnhprRSPPT-----------------VPPSGPLWNDVE--PRLNQSLAiKARHGYIhpPPLTSDRVIVLL- 371
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330254725 374 lglnncpkNFRSRrcqgPNGTRfTASMNNVSFALPSNYSLLqAHHHGIPGVFTtdfPAKPPVKFDYTGNNISRSLYQPDR 453
Cdd:PLN02604 372 --------NTQNE----VNGYR-RWSVNNVSFNLPHTPYLI-ALKENLTGAFD---QTPPPEGYDFANYDIYAKPNNSNA 434
                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330254725 454 GT--KLYKLKYGSRVQIVLQDTGIVTP---ENHPIHLHGYDFYIIAEGFGNFNPKKDTAKFNLEDPPLRNTVGVPVNGWA 528
Cdd:PLN02604 435 TSsdSIYRLQFNSTVDIILQNANTMNAnnsETHPWHLHGHDFWVLGYGEGKFNMSSDPKKYNLVDPIMKNTVPVHPYGWT 514
                        570       580       590
                 ....*....|....*....|....*....|
gi 330254725 529 VIRFIADNPGVWIMHCHLDAHISWGLAMAF 558
Cdd:PLN02604 515 ALRFRADNPGVWAFHCHIESHFFMGMGVVF 544
Cu-oxidase_3 pfam07732
Multicopper oxidase; This entry contains many divergent copper oxidase-like domains that are ...
35-150 1.03e-49

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: 167.81  E-value: 1.03e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330254725   35 IQATKVKRLCETHNS-ITVNGMFPGPMLVVNNGDTLVVKVINRARYNITIHWHGVRQMRTGWADGPEFVTQCPIRPGSSY 113
Cdd:pfam07732   2 VTYGTVSPLGGTRQAvIGVNGQFPGPTIRVREGDTVVVNVTNNLDEPTSIHWHGLQQRGTPWMDGVPGVTQCPIPPGQSF 81
                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 330254725  114 TYRFTIQGQEGTLWWHAHSSWLRA-TVYGSLLVFPPAG 150
Cdd:pfam07732  82 TYRFQVKQQAGTYWYHSHTSGQQAaGLAGAIIIEDRAS 119
SufI COG2132
Multicopper oxidase with three cupredoxin domains (includes cell division protein FtsP and ...
51-546 4.72e-44

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: 162.03  E-value: 4.72e-44
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330254725  51 TVNGMFPGPMLVVNNGDTLVVKVINRARYNITIHWHGvrqMRTGWA-DGpefVTQCPIRPGSSYTYRFTIQGQEGTLWWH 129
Cdd:COG2132   37 GYNGQYPGPTIRVREGDRVRVRVTNRLPEPTTVHWHG---LRVPNAmDG---VPGDPIAPGETFTYEFPVPQPAGTYWYH 110
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330254725 130 AHSswLRATV-------YGSLLVFPPAGssyPFTKPHRNVPLLLGEWWDANPVDVLR-ESIRTGGAPnnSDAYTINGQPG 201
Cdd:COG2132  111 PHT--HGSTAeqvyrglAGALIVEDPEE---DLPRYDRDIPLVLQDWRLDDDGQLLYpMDAAMGGRL--GDTLLVNGRPN 183
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330254725 202 DlykcssqdttVVPINVGETILLRVINSALNQplFFTVA---NHKLTVVGADASYL-KPFTTNVIVLGPGQTTDVLITGD 277
Cdd:COG2132  184 P----------TLEVRPGERVRLRLLNASNAR--IYRLAlsdGRPFTVIATDGGLLpAPVEVDELLLAPGERADVLVDFS 251
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330254725 278 QPPNRYYMAArayqsaqnAPFGNTTTTAILQYKsapccgVGGGSGTKKgnsfkpimpiLPAYNDTNTvtrfsqsfrSLRR 357
Cdd:COG2132  252 ADPGEEVTLA--------NPFEGRSGRALLTLR------VTGAAASAP----------LPANLAPLP---------DLED 298
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330254725 358 AEVPTEIDENLFVtiglglnncpknfrsrrcqGPNGTRFTasMNNVSFalpsnysllqahhhgipgvfttdfpakppvkf 437
Cdd:COG2132  299 REAVRTRELVLTG-------------------GMAGYVWT--INGKAF-------------------------------- 325
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330254725 438 dytgnnisrslyqpDRGTKLYKLKYGSRVQIVLQDTgivTPENHPIHLHGYDFYIIAEgfgnfNPKKdtakfnLEDPPLR 517
Cdd:COG2132  326 --------------DPDRPDLTVKLGERERWTLVND---TMMPHPFHLHGHQFQVLSR-----NGKP------PPEGGWK 377
                        490       500       510
                 ....*....|....*....|....*....|
gi 330254725 518 NTVGVPVNGWAVIRFIADN-PGVWIMHCHL 546
Cdd:COG2132  378 DTVLVPPGETVRILFRFDNyPGDWMFHCHI 407
 
Name Accession Description Interval E-value
laccase TIGR03389
laccase, plant; Members of this protein family include the copper-containing enzyme laccase ...
27-580 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: 901.41  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330254725   27 KAHHHEFIIQATKVKRLCETHNSITVNGMFPGPMLVVNNGDTLVVKVINRARYNITIHWHGVRQMRTGWADGPEFVTQCP 106
Cdd:TIGR03389   2 EVRHYTFDVQEKNVTRLCSTKSILTVNGKFPGPTLYAREGDTVIVNVTNNVQYNVTIHWHGVRQLRNGWADGPAYITQCP 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330254725  107 IRPGSSYTYRFTIQGQEGTLWWHAHSSWLRATVYGSLLVFPPAGSSYPFTKPHRNVPLLLGEWWDANPVDVLRESIRTGG 186
Cdd:TIGR03389  82 IQPGQSYVYNFTITGQRGTLWWHAHISWLRATVYGAIVILPKPGVPYPFPKPDREVPIILGEWWNADVEAVINQANQTGG 161
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330254725  187 APNNSDAYTINGQPGDLYKCSSQDTTVVPINVGETILLRVINSALNQPLFFTVANHKLTVVGADASYLKPFTTNVIVLGP 266
Cdd:TIGR03389 162 APNVSDAYTINGHPGPLYNCSSKDTFKLTVEPGKTYLLRIINAALNDELFFAIANHTLTVVEVDATYTKPFKTKTIVIGP 241
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330254725  267 GQTTDVLITGDQPPNRYYMAARAYQSAQNApFGNTTTTAILQYKSAPCcgvgggsgtkkgnSFKPIMPILPAYNDTNTVT 346
Cdd:TIGR03389 242 GQTTNVLLTADQSPGRYFMAARPYMDAPGA-FDNTTTTAILQYKGTSN-------------SAKPILPTLPAYNDTAAAT 307
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330254725  347 RFSQSFRSLRR----AEVPTEIDENLFVTIGLGLNNCPKNfrsrRCQGPNGTRFTASMNNVSFALPsNYSLLQAHHHGIP 422
Cdd:TIGR03389 308 NFSNKLRSLNSaqypANVPVTIDRRLFFTIGLGLDPCPNN----TCQGPNGTRFAASMNNISFVMP-TTALLQAHYFGIS 382
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330254725  423 GVFTTDFPAKPPVKFDYTGNNISRSLYQPdRGTKLYKLKYGSRVQIVLQDTGIVTPENHPIHLHGYDFYIIAEGFGNFNP 502
Cdd:TIGR03389 383 GVFTTDFPANPPTKFNYTGTNLPNNLFTT-NGTKVVRLKFNSTVELVLQDTSILGSENHPIHLHGYNFFVVGTGFGNFDP 461
                         490       500       510       520       530       540       550
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 330254725  503 KKDTAKFNLEDPPLRNTVGVPVNGWAVIRFIADNPGVWIMHCHLDAHISWGLAMAFLVENGNGVLQTIEQPPHDLPVC 580
Cdd:TIGR03389 462 KKDPAKFNLVDPPERNTVGVPTGGWAAIRFVADNPGVWFMHCHLEVHTTWGLKMAFLVDNGKGPNQSLLPPPSDLPSC 539
ascorbase TIGR03388
L-ascorbate oxidase, plant type; Members of this protein family are the copper-containing ...
44-558 3.84e-96

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: 303.60  E-value: 3.84e-96
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330254725   44 CETHNSITVNGMFPGPMLVVNNGDTLVVKVINR-ARYNITIHWHGVRQMRTGWADGPEFVTQCPIRPGSSYTYRFTIQgQ 122
Cdd:TIGR03388  17 CFEKLVIGINGQFPGPTIRAQAGDTIVVELTNKlHTEGVVIHWHGIRQIGTPWADGTAGVTQCAINPGETFIYNFVVD-R 95
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330254725  123 EGTLWWHAHSSWLR-ATVYGSLLVFPPAGSSYPFTKPH-RNvpLLLGEWWD----ANPVDVLRESIRTGGAP-------- 188
Cdd:TIGR03388  96 PGTYFYHGHYGMQRsAGLYGSLIVDVPDGEKEPFHYDGeFN--LLLSDWWHksihEQEVGLSSKPMRWIGEPqsllingr 173
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330254725  189 ------NNSDAYTINGQPGDLY---KCSSQDTTVVPinvGETILLRVIN----SALNqplfFTVANHKLTVVGADASYLK 255
Cdd:TIGR03388 174 gqfncsLAAKFSSTNLPQCNLKgneQCAPQILHVEP---GKTYRLRIASttalAALN----FAIEGHKLTVVEADGNYVE 246
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330254725  256 PFTTNVIVLGPGQTTDVLITGDQPPNRYYMAARAYQSAQNApfgNTTTTAILQYKSAPccgvgggsgTKKGNSFKPimPI 335
Cdd:TIGR03388 247 PFTVKDIDIYSGETYSVLLTTDQDPSRNYWISVGVRGRKPN---TPPGLTVLNYYPNS---------PSRLPPTPP--PV 312
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330254725  336 LPAYNDTNTVTRFSQSFRSLRRA-EVPTEIDENLFVtiglgLNNcpknfrsrrcQGPNGTRFTASMNNVSFALPSNySLL 414
Cdd:TIGR03388 313 TPAWDDFDRSKAFSLAIKAAMGSpKPPETSDRRIVL-----LNT----------QNKINGYTKWAINNVSLTLPHT-PYL 376
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330254725  415 QAHHHGIPGVFTTDFP-----------AKPPVKFDYTGNNIsrslyqpdrgtklYKLKYGSRVQIVLQDTGIV---TPEN 480
Cdd:TIGR03388 377 GSLKYNLLNAFDQKPPpenyprdydifKPPPNPNTTTGNGI-------------YRLKFNTTVDVILQNANTLngnNSET 443
                         490       500       510       520       530       540       550
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 330254725  481 HPIHLHGYDFYIIAEGFGNFNPKKDTAKFNLEDPPLRNTVGVPVNGWAVIRFIADNPGVWIMHCHLDAHISWGLAMAF 558
Cdd:TIGR03388 444 HPWHLHGHDFWVLGYGEGKFRPGVDEKSYNLKNPPLRNTVVIFPYGWTALRFVADNPGVWAFHCHIEPHLHMGMGVVF 521
CuRO_2_LCC_plant cd13875
The second cupredoxin domain of the plant laccases; Laccase is a blue multi-copper enzyme that ...
162-309 5.44e-87

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: 266.00  E-value: 5.44e-87
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330254725 162 VPLLLGEWWDANPVDVLRESIRTGGAPNNSDAYTINGQPGDLYKCSSQDTTVVPINVGETILLRVINSALNQPLFFTVAN 241
Cdd:cd13875    1 VPIILGEWWNRDVNDVEDQALLTGGGPNISDAYTINGQPGDLYNCSSKDTFVLTVEPGKTYLLRIINAALNEELFFKIAN 80
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 330254725 242 HKLTVVGADASYLKPFTTNVIVLGPGQTTDVLITGDQPPNRYYMAARAYQSAQNAPFGNTTTTAILQY 309
Cdd:cd13875   81 HTLTVVAVDASYTKPFTTDYILIAPGQTTDVLLTADQPPGRYYMAARPYQSAPPVPFDNTTATAILEY 148
CuRO_3_LCC_plant cd13897
The third cupredoxin domain of the plant laccases; Laccase is a blue multicopper oxidase (MCO) ...
424-563 5.02e-84

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: 257.96  E-value: 5.02e-84
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330254725 424 VFTTDFPAKPPVKFDYTGNNiSRSLYQPDRGTKLYKLKYGSRVQIVLQDTGIVTPENHPIHLHGYDFYIIAEGFGNFNPK 503
Cdd:cd13897    1 VYTTDFPDRPPVPFDYTGNA-PNENTPTSRGTKVKVLEYGSTVEIVLQGTSLLAAENHPMHLHGFDFYVVGRGFGNFDPS 79
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 330254725 504 KDTAKFNLEDPPLRNTVGVPVNGWAVIRFIADNPGVWIMHCHLDAHISWGLAMAFLVENG 563
Cdd:cd13897   80 TDPATFNLVDPPLRNTVGVPRGGWAAIRFVADNPGVWFMHCHFERHTSWGMATVFIVKNG 139
PLN02604 PLN02604
oxidoreductase
7-558 4.96e-83

oxidoreductase


Pssm-ID: 215324 [Multi-domain]  Cd Length: 566  Bit Score: 270.19  E-value: 4.96e-83
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330254725   7 LLCFISFVAFLLFSSVAEAnKAHHHEFIIQATKVKRLCETHNSITVNGMFPGPMLVVNNGDTLVVKVINR-ARYNITIHW 85
Cdd:PLN02604   4 FLALFFLLFSVLNFPAAEA-RIRRYKWEVKYEYKSPDCFKKLVITINGRSPGPTILAQQGDTVIVELKNSlLTENVAIHW 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330254725  86 HGVRQMRTGWADGPEFVTQCPIRPGSSYTYRFTIQgQEGTLWWHAHSSWLR-ATVYGSLLVFPPAGSSYPFTKPH-RNVp 163
Cdd:PLN02604  83 HGIRQIGTPWFDGTEGVTQCPILPGETFTYEFVVD-RPGTYLYHAHYGMQReAGLYGSIRVSLPRGKSEPFSYDYdRSI- 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330254725 164 lLLGEWW-----------DANPVDVLRES----IRTGGAPNNSDAyTINGQPGDLY-----KCSSQDTTVVPinvGETIL 223
Cdd:PLN02604 161 -ILTDWYhkstyeqalglSSIPFDWVGEPqsllIQGKGRYNCSLV-SSPYLKAGVCnatnpECSPYVLTVVP---GKTYR 235
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330254725 224 LRVINSALNQPLFFTVANHKLTVVGADASYLKPFTTNVIVLGPGQTTDVLITGDQPPNRYYMAARAYQSAQNA-PFGntt 302
Cdd:PLN02604 236 LRISSLTALSALSFQIEGHNMTVVEADGHYVEPFVVKNLFIYSGETYSVLVKADQDPSRNYWVTTSVVSRNNTtPPG--- 312
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330254725 303 tTAILQY------KSAPCcgvgggsgtkkgnsfkpIMPILPAYNDTNtvTRFSQSFR-SLRRAEV--PTEIDENLFVTIg 373
Cdd:PLN02604 313 -LAIFNYypnhprRSPPT-----------------VPPSGPLWNDVE--PRLNQSLAiKARHGYIhpPPLTSDRVIVLL- 371
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330254725 374 lglnncpkNFRSRrcqgPNGTRfTASMNNVSFALPSNYSLLqAHHHGIPGVFTtdfPAKPPVKFDYTGNNISRSLYQPDR 453
Cdd:PLN02604 372 --------NTQNE----VNGYR-RWSVNNVSFNLPHTPYLI-ALKENLTGAFD---QTPPPEGYDFANYDIYAKPNNSNA 434
                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330254725 454 GT--KLYKLKYGSRVQIVLQDTGIVTP---ENHPIHLHGYDFYIIAEGFGNFNPKKDTAKFNLEDPPLRNTVGVPVNGWA 528
Cdd:PLN02604 435 TSsdSIYRLQFNSTVDIILQNANTMNAnnsETHPWHLHGHDFWVLGYGEGKFNMSSDPKKYNLVDPIMKNTVPVHPYGWT 514
                        570       580       590
                 ....*....|....*....|....*....|
gi 330254725 529 VIRFIADNPGVWIMHCHLDAHISWGLAMAF 558
Cdd:PLN02604 515 ALRFRADNPGVWAFHCHIESHFFMGMGVVF 544
PLN02191 PLN02191
L-ascorbate oxidase
10-558 9.19e-83

L-ascorbate oxidase


Pssm-ID: 177843 [Multi-domain]  Cd Length: 574  Bit Score: 269.96  E-value: 9.19e-83
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330254725  10 FISFVAFLLFSSVAEANKAHHHEfiIQATKVKRLCETHNSITVNGMFPGPMLVVNNGDTLVVKVINR-ARYNITIHWHGV 88
Cdd:PLN02191   7 WIVTVVAVLTHTASAAVREYTWE--VEYKYWWPDCKEGAVMTVNGQFPGPTIDAVAGDTIVVHLTNKlTTEGLVIHWHGI 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330254725  89 RQMRTGWADGPEFVTQCPIRPGSSYTYRFTIQgQEGTLWWHAHSSWLRAT-VYGSLLVFPPAGSSYPFtKPHRNVPLLLG 167
Cdd:PLN02191  85 RQKGSPWADGAAGVTQCAINPGETFTYKFTVE-KPGTHFYHGHYGMQRSAgLYGSLIVDVAKGPKERL-RYDGEFNLLLS 162
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330254725 168 EWW-----------DANPVDVLRES----IRTGGAPNNSDAYTING---------QPGDlyKCSSQDTTVVPinvGETIL 223
Cdd:PLN02191 163 DWWhesipsqelglSSKPMRWIGEAqsilINGRGQFNCSLAAQFSNgtelpmctfKEGD--QCAPQTLRVEP---NKTYR 237
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330254725 224 LRVINSALNQPLFFTVANHKLTVVGADASYLKPFTTNVIVLGPGQTTDVLITGDQ-PPNRYYMAARAYQSAQNAPFGNTt 302
Cdd:PLN02191 238 IRLASTTALASLNLAVQGHKLVVVEADGNYITPFTTDDIDIYSGESYSVLLTTDQdPSQNYYISVGVRGRKPNTTQALT- 316
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330254725 303 ttaILQYKSAPccgvgggsgTKKGNSFKPimPILPAYNDTNTVTRFSQSFRSLRRAEVPTEIDENLFVTigLGLNNCPKN 382
Cdd:PLN02191 317 ---ILNYVTAP---------ASKLPSSPP--PVTPRWDDFERSKNFSKKIFSAMGSPSPPKKYRKRLIL--LNTQNLIDG 380
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330254725 383 FrsrrcqgpngTRFtaSMNNVSFALPSNySLLQAHHHGIPGVFTTDFPAKPpVKFDYtgnNISRSLYQPD--RGTKLYKL 460
Cdd:PLN02191 381 Y----------TKW--AINNVSLVTPAT-PYLGSVKYNLKLGFNRKSPPRS-YRMDY---DIMNPPPFPNttTGNGIYVF 443
                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330254725 461 KYGSRVQIVLQDTGI---VTPENHPIHLHGYDFYIIAEGFGNFNPKKDTAKFNLEDPPLRNTVGVPVNGWAVIRFIADNP 537
Cdd:PLN02191 444 PFNVTVDVIIQNANVlkgVVSEIHPWHLHGHDFWVLGYGDGKFKPGIDEKTYNLKNPPLRNTAILYPYGWTAIRFVTDNP 523
                        570       580
                 ....*....|....*....|.
gi 330254725 538 GVWIMHCHLDAHISWGLAMAF 558
Cdd:PLN02191 524 GVWFFHCHIEPHLHMGMGVVF 544
CuRO_1_LCC_plant cd13849
The first cupredoxin domain of plant laccases; Laccase is a blue multicopper oxidase (MCO) ...
31-147 1.18e-69

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: 220.21  E-value: 1.18e-69
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330254725  31 HEFIIQATKVKRLCETHNSITVNGMFPGPMLVVNNGDTLVVKVINRARYNITIHWHGVRQMRTGWADGPEFVTQCPIRPG 110
Cdd:cd13849    1 YTFVVQEKNVTRLCSTKSILTVNGQFPGPTIRVHEGDTVVVNVTNRSPYNITIHWHGIRQLRSGWADGPAYITQCPIQPG 80
                         90       100       110
                 ....*....|....*....|....*....|....*..
gi 330254725 111 SSYTYRFTIQGQEGTLWWHAHSSWLRATVYGSLLVFP 147
Cdd:cd13849   81 QSYTYRFTVTGQEGTLWWHAHISWLRATVYGAFIIRP 117
Cu-oxidase_3 pfam07732
Multicopper oxidase; This entry contains many divergent copper oxidase-like domains that are ...
35-150 1.03e-49

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: 167.81  E-value: 1.03e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330254725   35 IQATKVKRLCETHNS-ITVNGMFPGPMLVVNNGDTLVVKVINRARYNITIHWHGVRQMRTGWADGPEFVTQCPIRPGSSY 113
Cdd:pfam07732   2 VTYGTVSPLGGTRQAvIGVNGQFPGPTIRVREGDTVVVNVTNNLDEPTSIHWHGLQQRGTPWMDGVPGVTQCPIPPGQSF 81
                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 330254725  114 TYRFTIQGQEGTLWWHAHSSWLRA-TVYGSLLVFPPAG 150
Cdd:pfam07732  82 TYRFQVKQQAGTYWYHSHTSGQQAaGLAGAIIIEDRAS 119
Cu-oxidase_2 pfam07731
Multicopper oxidase; This entry contains many divergent copper oxidase-like domains that are ...
428-564 1.90e-46

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: 159.52  E-value: 1.90e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330254725  428 DFPAKPPVKFDYTGNNISRSLYQP-----DRGTKLYKLKYGSRVQIVLQDTgivTPENHPIHLHGYDFYIIAEGFGNfNP 502
Cdd:pfam07731   1 DTPPKLPTLLQITSGNFRRNDWAIngllfPPNTNVITLPYGTVVEWVLQNT---TTGVHPFHLHGHSFQVLGRGGGP-WP 76
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 330254725  503 KKDTAKFNLEDPPLRNTVGVPVNGWAVIRFIADNPGVWIMHCHLDAHISWGLAMAFLVENGN 564
Cdd:pfam07731  77 EEDPKTYNLVDPVRRDTVQVPPGGWVAIRFRADNPGVWLFHCHILWHLDQGMMGQFVVRPGD 138
PLN02168 PLN02168
copper ion binding / pectinesterase
1-540 2.53e-45

copper ion binding / pectinesterase


Pssm-ID: 215113 [Multi-domain]  Cd Length: 545  Bit Score: 168.23  E-value: 2.53e-45
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330254725   1 MDVTKSLLCFISFVAFLLFSSVAEANK-----AHHHEFIIQATKvkrlcethNSITVNGMFPGPMLVVNNGDTLVVKVIN 75
Cdd:PLN02168   2 RHVFVEVFVLISLVILELSYAFAPIVSyqwvvSYSQRFILGGNK--------QVIVINDMFPGPLLNATANDVINVNIFN 73
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330254725  76 RARYNITIHWHGVRQMRTGWADGPEfVTQCPIRPGSSYTYRFTIQGQEGTLWWHAHSSWLRAT-VYGSLLVFPPAGSSYP 154
Cdd:PLN02168  74 NLTEPFLMTWNGLQLRKNSWQDGVR-GTNCPILPGTNWTYRFQVKDQIGSYFYFPSLLLQKAAgGYGAIRIYNPELVPVP 152
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330254725 155 FTKPHRNVPLLLGEWWDANPVDvLRESIRTGGAPNNSDAYTINGQpgdlykcsSQDTTVVPINVGETILLRVINSALNQP 234
Cdd:PLN02168 153 FPKPDEEYDILIGDWFYADHTV-MRASLDNGHSLPNPDGILFNGR--------GPEETFFAFEPGKTYRLRISNVGLKTC 223
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330254725 235 LFFTVANHKLTVVGADASYLKPFTTNVIVLGPGQTTDVLITGDQPPNRYYMAARAYQSAQ--NAPFGNtttTAILQYKSA 312
Cdd:PLN02168 224 LNFRIQDHDMLLVETEGTYVQKRVYSSLDIHVGQSYSVLVTAKTDPVGIYRSYYIVATARftDAYLGG---VALIRYPNS 300
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330254725 313 PCCGVGGGsgtkkgnsfkpimPILPAYNDTNTVTrfsQSFRSLRRAEVPTEIDENLFVTIGLGLNNCPKNFRSRRCQGPN 392
Cdd:PLN02168 301 PLDPVGPL-------------PLAPALHDYFSSV---EQALSIRMDLNVGAARSNPQGSYHYGRINVTRTIILHNDVMLS 364
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330254725 393 GTRFTASMNNVSFALPSNYSLLQAHHHGIPGVFTTDFPakppvkfDYTGNNIsrslyqPDRGTKLYKLKYGSRVQIVLQD 472
Cdd:PLN02168 365 SGKLRYTINGVSFVYPGTPLKLVDHFQLNDTIIPGMFP-------VYPSNKT------PTLGTSVVDIHYKDFYHIVFQN 431
                        490       500       510       520       530       540
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 330254725 473 TgivTPENHPIHLHGYDFYIIAEGFGNFNPKKdTAKFNLEDPPLRNTVGVPVNGWAVIRFIADNPGVW 540
Cdd:PLN02168 432 P---LFSLESYHIDGYNFFVVGYGFGAWSESK-KAGYNLVDAVSRSTVQVYPYSWTAILIAMDNQGMW 495
SufI COG2132
Multicopper oxidase with three cupredoxin domains (includes cell division protein FtsP and ...
51-546 4.72e-44

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: 162.03  E-value: 4.72e-44
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330254725  51 TVNGMFPGPMLVVNNGDTLVVKVINRARYNITIHWHGvrqMRTGWA-DGpefVTQCPIRPGSSYTYRFTIQGQEGTLWWH 129
Cdd:COG2132   37 GYNGQYPGPTIRVREGDRVRVRVTNRLPEPTTVHWHG---LRVPNAmDG---VPGDPIAPGETFTYEFPVPQPAGTYWYH 110
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330254725 130 AHSswLRATV-------YGSLLVFPPAGssyPFTKPHRNVPLLLGEWWDANPVDVLR-ESIRTGGAPnnSDAYTINGQPG 201
Cdd:COG2132  111 PHT--HGSTAeqvyrglAGALIVEDPEE---DLPRYDRDIPLVLQDWRLDDDGQLLYpMDAAMGGRL--GDTLLVNGRPN 183
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330254725 202 DlykcssqdttVVPINVGETILLRVINSALNQplFFTVA---NHKLTVVGADASYL-KPFTTNVIVLGPGQTTDVLITGD 277
Cdd:COG2132  184 P----------TLEVRPGERVRLRLLNASNAR--IYRLAlsdGRPFTVIATDGGLLpAPVEVDELLLAPGERADVLVDFS 251
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330254725 278 QPPNRYYMAArayqsaqnAPFGNTTTTAILQYKsapccgVGGGSGTKKgnsfkpimpiLPAYNDTNTvtrfsqsfrSLRR 357
Cdd:COG2132  252 ADPGEEVTLA--------NPFEGRSGRALLTLR------VTGAAASAP----------LPANLAPLP---------DLED 298
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330254725 358 AEVPTEIDENLFVtiglglnncpknfrsrrcqGPNGTRFTasMNNVSFalpsnysllqahhhgipgvfttdfpakppvkf 437
Cdd:COG2132  299 REAVRTRELVLTG-------------------GMAGYVWT--INGKAF-------------------------------- 325
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330254725 438 dytgnnisrslyqpDRGTKLYKLKYGSRVQIVLQDTgivTPENHPIHLHGYDFYIIAEgfgnfNPKKdtakfnLEDPPLR 517
Cdd:COG2132  326 --------------DPDRPDLTVKLGERERWTLVND---TMMPHPFHLHGHQFQVLSR-----NGKP------PPEGGWK 377
                        490       500       510
                 ....*....|....*....|....*....|
gi 330254725 518 NTVGVPVNGWAVIRFIADN-PGVWIMHCHL 546
Cdd:COG2132  378 DTVLVPPGETVRILFRFDNyPGDWMFHCHI 407
PLN02835 PLN02835
oxidoreductase
50-542 5.90e-41

oxidoreductase


Pssm-ID: 178429 [Multi-domain]  Cd Length: 539  Bit Score: 155.90  E-value: 5.90e-41
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330254725  50 ITVNGMFPGPMLVVNNGDTLVVKVINRARYNITIHWHGVRQMRTGWADGPeFVTQCPIRPGSSYTYRFTIQGQEGTLWWH 129
Cdd:PLN02835  51 ILINGQFPGPRLDVVTNDNIILNLINKLDQPFLLTWNGIKQRKNSWQDGV-LGTNCPIPPNSNYTYKFQTKDQIGTFTYF 129
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330254725 130 AHSSWLRAT-VYGSLLVFPPAGSSYPFTKPHRNVPLLLGEWWDANPvDVLRESIRTGGAPNNSDAYTINGQPgdlYKCSS 208
Cdd:PLN02835 130 PSTLFHKAAgGFGAINVYERPRIPIPFPLPDGDFTLLVGDWYKTSH-KTLQQRLDSGKVLPFPDGVLINGQT---QSTFS 205
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330254725 209 QDTtvvpinvGETILLRVINSALNQPLFFTVANHKLTVVGADASYLKPFTTNVIVLGPGQTTDVLITGDQPPNRYYMAAR 288
Cdd:PLN02835 206 GDQ-------GKTYMFRISNVGLSTSLNFRIQGHTMKLVEVEGSHTIQNIYDSLDVHVGQSVAVLVTLNQSPKDYYIVAS 278
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330254725 289 AYQSAQnapfgNTTTTAILQYKsapccgvgggsgtkkgNSFKPIMPILPAYNDTNTVTRFSQSfRSLRRAEVPTEIDENL 368
Cdd:PLN02835 279 TRFTRQ-----ILTATAVLHYS----------------NSRTPASGPLPALPSGELHWSMRQA-RTYRWNLTASAARPNP 336
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330254725 369 FVTIGLGLNNCPKNFR-SRRCQGPNGTRFTAsMNNVSFaLPSNYSLLQAHHHGIPGVFTTDFPAKPPvkfdytgnnisrS 447
Cdd:PLN02835 337 QGSFHYGKITPTKTIVlANSAPLINGKQRYA-VNGVSY-VNSDTPLKLADYFGIPGVFSVNSIQSLP------------S 402
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330254725 448 LYQPDRGTKLYKLKYGSRVQIVLQDTgivtpEN--HPIHLHGYDFYIIAEGFGNFNPKKDTAkFNLEDPPLRNTVGVPVN 525
Cdd:PLN02835 403 GGPAFVATSVMQTSLHDFLEVVFQNN-----EKtmQSWHLDGYDFWVVGYGSGQWTPAKRSL-YNLVDALTRHTAQVYPK 476
                        490
                 ....*....|....*..
gi 330254725 526 GWAVIRFIADNPGVWIM 542
Cdd:PLN02835 477 SWTTILVSLDNQGMWNM 493
Cu-oxidase pfam00394
Multicopper oxidase; Many of the proteins in this family contain multiple similar copies of ...
160-312 3.77e-40

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: 142.84  E-value: 3.77e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330254725  160 RNVPLLLGEWWDANPVDVLRESIRTG----GAPNNSDAYTINGQPGdlykcssQDTTVVPINVGETILLRVINSALNQPL 235
Cdd:pfam00394   1 EDYVITLSDWYHKDAKDLEKELLASGkaptDFPPVPDAVLINGKDG-------ASLATLTVTPGKTYRLRIINVALDDSL 73
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 330254725  236 FFTVANHKLTVVGADASYLKPFTTNVIVLGPGQTTDVLITGDQPPNRYYMAArayqSAQNAPFGNTTTTAILQYKSA 312
Cdd:pfam00394  74 NFSIEGHKMTVVEVDGVYVNPFTVDSLDIFPGQRYSVLVTANQDPGNYWIVA----SPNIPAFDNGTAAAILRYSGA 146
CuRO_1_LCC_like cd04206
Cupredoxin domain 1 of laccase-like multicopper oxidases; including laccase, CueO, spore coat ...
29-145 1.54e-39

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: 140.50  E-value: 1.54e-39
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330254725  29 HHHEFIIQATKVKRLCETHNSITVNGMFPGPMLVVNNGDTLVVKVINR-ARYNITIHWHGVRQMRTGWADGPEFVTQCPI 107
Cdd:cd04206    1 REYELTITETTVNPDGVLRQVITVNGQFPGPTIRVKEGDTVEVTVTNNlPNEPTSIHWHGLRQPGTNDGDGVAGLTQCPI 80
                         90       100       110
                 ....*....|....*....|....*....|....*....
gi 330254725 108 RPGSSYTYRFTIQGQEGTLWWHAHSSWLRA-TVYGSLLV 145
Cdd:cd04206   81 PPGESFTYRFTVDDQAGTFWYHSHVGGQRAdGLYGPLIV 119
ascorbOXfungal TIGR03390
L-ascorbate oxidase, fungal type; This model describes a family of fungal ascorbate oxidases, ...
27-562 1.69e-39

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: 151.53  E-value: 1.69e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330254725   27 KAHHHEF----IIQAT--KVKRLCETHNSITVNGMFPGPMLVVNNGDTLVVKVINR-ARYNITIHWHGVRQMRTGWADGP 99
Cdd:TIGR03390   1 VVHDDSFqpdhILRVTsdNIKIACSSRYSVVVNGTSPGPEIRLQEGQTTWIRVYNDiPDNNVTMHWHGLTQRTAPFSDGT 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330254725  100 EFVTQCPIRPGSSYTYRFTIQ-GQEGTLWWHAHSSWLRATVYGSLLVFPPAGSSYPFTKphrNVPLLLGEWWDANPVDVL 178
Cdd:TIGR03390  81 PLASQWPIPPGHFFDYEIKPEpGDAGSYFYHSHVGFQAVTAFGPLIVEDCEPPPYKYDD---ERILLVSDFFSATDEEIE 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330254725  179 RESIRTGGA-PNNSDAYTINGQPGDLYKCSSQDTT------VVPINVGETILLRVIN-SALNQPLFFTVANHKLTVVGAD 250
Cdd:TIGR03390 158 QGLLSTPFTwSGETEAVLLNGKSGNKSFYAQINPSgscmlpVIDVEPGKTYRLRFIGaTALSLISLGIEDHENLTIIEAD 237
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330254725  251 ASYLKPFTTNVIVLGPGQTTDVLIT---------GDQppNRYYMaaRAYQSAQNAPFgntTTTAILQYKSapccgvgggs 321
Cdd:TIGR03390 238 GSYTKPAKIDHLQLGGGQRYSVLFKaktedelcgGDK--RQYFI--QFETRDRPKVY---RGYAVLRYRS---------- 300
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330254725  322 gtKKGNSFKPI--MPILPAYNDTNTVTRFS-QSFRSLRRAEVPTEIDENLFVTIGLGLNNCPKNFRSRRCQgpNGTRFTA 398
Cdd:TIGR03390 301 --DKASKLPSVpeTPPLPLPNSTYDWLEYElEPLSEENNQDFPTLDEVTRRVVIDAHQNVDPLNGRVAWLQ--NGLSWTE 376
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330254725  399 SMNNVSFalpsnysLLQAHHHGIpgvfttdfPAKPPVKFDYTGNNIsrslyqpDRGTKLYKLKYGSRVQIVLQDTGIVTP 478
Cdd:TIGR03390 377 SVRQTPY-------LVDIYENGL--------PATPNYTAALANYGF-------DPETRAFPAKVGEVLEIVWQNTGSYTG 434
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330254725  479 EN-----HPIHLHGYDFYIIAEGFGNFNPKKDTAKFNLEDPPLRNTV-----------GVPvNGWAVIRFIADNPGVWIM 542
Cdd:TIGR03390 435 PNggvdtHPFHAHGRHFYDIGGGDGEYNATANEAKLENYTPVLRDTTmlyryavkvvpGAP-AGWRAWRIRVTNPGVWMM 513
                         570       580
                  ....*....|....*....|
gi 330254725  543 HCHLDAHISWGLAMAFLVEN 562
Cdd:TIGR03390 514 HCHILQHMVMGMQTVWVFGD 533
PLN02991 PLN02991
oxidoreductase
16-546 8.39e-39

oxidoreductase


Pssm-ID: 215536 [Multi-domain]  Cd Length: 543  Bit Score: 149.78  E-value: 8.39e-39
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330254725  16 FLLFSSVAEANKAHHHEFIIQATKVKRLCETHNSITVNGMFPGPMLVVNNGDTLVVKVINRARYNITIHWHGVRQMRTGW 95
Cdd:PLN02991  16 LFLISFVAAEDPYRFFEWHVTYGNISPLGVAQQGILINGKFPGPDIISVTNDNLIINVFNHLDEPFLISWSGIRNWRNSY 95
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330254725  96 ADGPeFVTQCPIRPGSSYTYRFTIQGQEGTLWWHAHSSWLRATV-YGSLLVFPPAGSSYPFTKPHRNVPLLLGEWWDANP 174
Cdd:PLN02991  96 QDGV-YGTTCPIPPGKNYTYALQVKDQIGSFYYFPSLGFHKAAGgFGAIRISSRPLIPVPFPAPADDYTVLIGDWYKTNH 174
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330254725 175 VDvLRESIRTGGAPNNSDAYTINGQpgdlykcSSQDTtvVPINVGETILLRVINSALNQPLFFTVANHKLTVVGADASYL 254
Cdd:PLN02991 175 KD-LRAQLDNGGKLPLPDGILINGR-------GSGAT--LNIEPGKTYRLRISNVGLQNSLNFRIQNHTMKLVEVEGTHT 244
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330254725 255 --KPFTTnvIVLGPGQTTDVLITGDQPPNRYYMAARAYQSAQNapfgnTTTTAILQYKsapccgvgggsgtkkgNSFKPI 332
Cdd:PLN02991 245 iqTPFSS--LDVHVGQSYSVLITADQPAKDYYIVVSSRFTSKI-----LITTGVLHYS----------------NSAGPV 301
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330254725 333 MPILPayndtNTVTRFSQSF---RSLRRAEVPTEIDENLFVTIGLGLNNCPKNFRSRRCQGPNGTRFTASMNNVSFaLPS 409
Cdd:PLN02991 302 SGPIP-----DGPIQLSWSFdqaRAIKTNLTASGPRPNPQGSYHYGKINITRTIRLANSAGNIEGKQRYAVNSASF-YPA 375
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330254725 410 NYSLLQAHHHGIPGVFTtdfPAKPPVKFDYTGNNISRSLYQPDrgtklyklkYGSRVQIVLQDTGIVTpenHPIHLHGYD 489
Cdd:PLN02991 376 DTPLKLADYFKIAGVYN---PGSIPDQPTNGAIFPVTSVMQTD---------YKAFVEIVFENWEDIV---QTWHLDGYS 440
                        490       500       510       520       530
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 330254725 490 FYIIAEGFGNFNPKKDTAkFNLEDPPLRNTVGVPVNGWAVIRFIADNPGVWIMHCHL 546
Cdd:PLN02991 441 FYVVGMELGKWSAASRKV-YNLNDAVSRCTVQVYPRSWTAIYVSLDNVGMWNLRSEL 496
copper_res_A TIGR01480
copper-resistance protein, CopA family; This model represents the CopA copper resistance ...
49-561 6.13e-38

copper-resistance protein, CopA family; This model represents the CopA copper resistance protein family. CopA is related to laccase (benzenediol:oxygen oxidoreductase) and L-ascorbate oxidase, both copper-containing enzymes. Most members have a typical TAT (twin-arginine translocation) signal sequence with an Arg-Arg pair. Twin-arginine translocation is observed for a large number of periplasmic proteins that cross the inner membrane with metal-containing cofactors already bound. The combination of copper-binding sites and TAT translocation motif suggests a mechansism of resistance by packaging and export. [Cellular processes, Detoxification, Transport and binding proteins, Cations and iron carrying compounds]


Pssm-ID: 273649 [Multi-domain]  Cd Length: 587  Bit Score: 148.10  E-value: 6.13e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330254725   49 SITVNGMFPGPMLVVNNGDTLVVKVINRARYNITIHWHGV---RQMrtgwaDGPEFVTQCPIRPGSSYTYRFTIQgQEGT 125
Cdd:TIGR01480  66 AITVNGSIPGPLLRWREGDTVRLRVTNTLPEDTSIHWHGIllpFQM-----DGVPGVSFAGIAPGETFTYRFPVR-QSGT 139
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330254725  126 LWWHAHSSWL-RATVYGSLLVFPPAGSSYPFTKPHrnvPLLLGEWWDANPVDVLRESIRTGGAPNnsdayTINGQPGDLY 204
Cdd:TIGR01480 140 YWYHSHSGFQeQAGLYGPLIIDPAEPDPVRADREH---VVLLSDWTDLDPAALFRKLKVMAGHDN-----YYKRTVADFF 211
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330254725  205 KCSSQD-------------------TTVVPINV----------------------GETILLRVINSALNQPLFFTVANHK 243
Cdd:TIGR01480 212 RDVRNDglkqtladrkmwgqmrmtpTDLADVNGstytylmngttpagnwtglfrpGEKVRLRFINGSAMTYFDVRIPGLK 291
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330254725  244 LTVVGADASYLKPFTTNVIVLGPGQTTDVLI--TGD-------QPPNRYYMA--ARAYQSAQNAPFGNTTTTAILQYKSA 312
Cdd:TIGR01480 292 LTVVAVDGQYVHPVSVDEFRIAPAETFDVIVepTGDdaftifaQDSDRTGYArgTLAVRLGLTAPVPALDPRPLLTMKDM 371
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330254725  313 PCCGVGGGS-GTKKGNSFKPIMPILPAYNDTNTVTRFSQSFRSLRRAEVPTEidenlfvtIGLGLNNCPKNFRSRRCQGP 391
Cdd:TIGR01480 372 GMGGMHHGMdHSKMSMGGMPGMDMSMRAQSNAPMDHSQMAMDASPKHPASEP--------LNPLVDMIVDMPMDRMDDPG 443
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330254725  392 NGTRftasmNNvsfalpSNYSLLQAHHHGIPGVFTTDFPAKpPVKFDYTGN---------NISRSLYQPDRgtklykLKY 462
Cdd:TIGR01480 444 IGLR-----DN------GRRVLTYADLHSLFPPPDGRAPGR-EIELHLTGNmerfawsfdGEAFGLKTPLR------FNY 505
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330254725  463 GSRVQIVLQDTGIVTpenHPIHLHGYdFYIIAEGFGNFNPKKdtakfnledpplrNTVGVPVNGWAVIRFIADNPGVWIM 542
Cdd:TIGR01480 506 GERLRVVLVNDTMMA---HPIHLHGM-WSELEDGQGEFQVRK-------------HTVDVPPGGKRSFRVTADALGRWAY 568
                         570
                  ....*....|....*....
gi 330254725  543 HCHLDAHISWGLAMAFLVE 561
Cdd:TIGR01480 569 HCHMLLHMEAGMFREVTVR 587
CuRO_3_tcLLC2_insect_like cd13905
The third cupredoxin domain of the insect laccases similar to laccase 2 in Tribolium castaneum; ...
399-560 3.11e-37

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: 135.89  E-value: 3.11e-37
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330254725 399 SMNNVSFALPSnySLLQahhhgipgvftTDFPAKPPVKFDYTGNNISRSLYQPDRGTKLYKLKYGSRVQIVLQDTGIVTP 478
Cdd:cd13905    1 SINGISFVFPS--SPLL-----------SQPEDLSDSSSCDFCNVPSKCCTEPCECTHVIKLPLNSVVEIVLINEGPGPG 67
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330254725 479 ENHPIHLHGYDFYIIAEGFGNFNPKKDTAKF----------------NLEDPPLRNTVGVPVNGWAVIRFIADNPGVWIM 542
Cdd:cd13905   68 LSHPFHLHGHSFYVLGMGFPGYNSTTGEILSqnwnnklldrgglpgrNLVNPPLKDTVVVPNGGYVVIRFRADNPGYWLL 147
                        170
                 ....*....|....*...
gi 330254725 543 HCHLDAHISWGLAMAFLV 560
Cdd:cd13905  148 HCHIEFHLLEGMALVLKV 165
CuRO_1_tcLCC2_insect_like cd13858
The first cupredoxin domain of insect laccases similar to laccase 2 in Tribolium castaneum; ...
50-145 2.11e-36

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: 131.12  E-value: 2.11e-36
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330254725  50 ITVNGMFPGPMLVVNNGDTLVVKVINRARYN-ITIHWHGVRQMRTGWADGPEFVTQCPIRPGSSYTYRFTIQgQEGTLWW 128
Cdd:cd13858    8 ITVNGQLPGPSIEVCEGDTVVVDVKNRLPGEsTTIHWHGIHQRGTPYMDGVPMVTQCPILPGQTFRYKFKAD-PAGTHWY 86
                         90
                 ....*....|....*...
gi 330254725 129 HAHSSWLRA-TVYGSLLV 145
Cdd:cd13858   87 HSHSGTQRAdGLFGALIV 104
CuRO_1_Diphenol_Ox cd13857
The first cupredoxin domain of fungal laccase, diphenol oxidase; Diphenol oxidase belongs to ...
50-145 6.45e-36

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: 130.46  E-value: 6.45e-36
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330254725  50 ITVNGMFPGPMLVVNNGDTLVVKVINRARYNITIHWHGVRQMRTGWADGPEFVTQCPIRPGSSYTYRFTIQGQEGTLWWH 129
Cdd:cd13857   22 LVINGQFPGPLIEANQGDRIVVHVTNELDEPTSIHWHGLFQNGTNWMDGTAGITQCPIPPGGSFTYNFTVDGQYGTYWYH 101
                         90
                 ....*....|....*..
gi 330254725 130 AHSSWLRAT-VYGSLLV 145
Cdd:cd13857  102 SHYSTQYADgLVGPLIV 118
CuRO_3_AAO cd13893
The third cupredoxin domain of plant Ascorbate oxidase; Ascorbate oxidase catalyzes the ...
457-558 1.88e-35

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: 130.62  E-value: 1.88e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330254725 457 LYKLKYGSRVQIVLQDTGIVTP---ENHPIHLHGYDFYIIAEGFGNFNPKKDTAKFNLEDPPLRNTVGVPVNGWAVIRFI 533
Cdd:cd13893   40 VYPFKGGDVVDVILQNANTNTRnasEQHPWHLHGHDFWVLGYGLGGFDPAADPSSLNLVNPPMRNTVTIFPYGWTALRFK 119
                         90       100
                 ....*....|....*....|....*
gi 330254725 534 ADNPGVWIMHCHLDAHISWGLAMAF 558
Cdd:cd13893  120 ADNPGVWAFHCHIEWHFHMGMGVVF 144
CuRO_3_LCC_like cd04207
Cupredoxin domain 3 of laccase-like multicopper oxidases; including laccase, CueO, spore coat ...
442-558 2.19e-34

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: 126.81  E-value: 2.19e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330254725 442 NNISRSLYQPDRGTklYKLKYGSRVQIVLQDTGIvTPENHPIHLHGYDFYIIAEGFGNFNpkkdtAKFNLEDPPLRNTVG 521
Cdd:cd04207   23 NGMPFKEGDANTDI--FSVEAGDVVEIVLINAGN-HDMQHPFHLHGHSFWVLGSGGGPFD-----APLNLTNPPWRDTVL 94
                         90       100       110
                 ....*....|....*....|....*....|....*..
gi 330254725 522 VPVNGWAVIRFIADNPGVWIMHCHLDAHISWGLAMAF 558
Cdd:cd04207   95 VPPGGWVVIRFKADNPGVWMLHCHILEHEDAGMMTVF 131
PLN02354 PLN02354
copper ion binding / oxidoreductase
7-540 2.63e-32

copper ion binding / oxidoreductase


Pssm-ID: 177987 [Multi-domain]  Cd Length: 552  Bit Score: 131.07  E-value: 2.63e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330254725   7 LLCFISFVAFLlfssVAEANKAHHHEFIIQATKVKRLCETHNSITVNGMFPGPMLVVNNGDTLVVKVINRARYNITIHWH 86
Cdd:PLN02354  10 LLCLAAAVALV----VRAEDPYFFFTWNVTYGTASPLGVPQQVILINGQFPGPNINSTSNNNIVINVFNNLDEPFLLTWS 85
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330254725  87 GVRQMRTGWADGPEFvTQCPIRPGSSYTYRFTIQGQEGTLWWHAHSSWLRAT-VYGSLLVFPPAGSSYPFTKPHRNVPLL 165
Cdd:PLN02354  86 GIQQRKNSWQDGVPG-TNCPIPPGTNFTYHFQPKDQIGSYFYYPSTGMHRAAgGFGGLRVNSRLLIPVPYADPEDDYTVL 164
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330254725 166 LGEWWDANPVdVLRESIRTGGAPNNSDAYTINGQPGdlyKCSSQDTTVVPINVGETILLRVINSALNQPLFFTVANHKLT 245
Cdd:PLN02354 165 IGDWYTKSHT-ALKKFLDSGRTLGRPDGVLINGKSG---KGDGKDEPLFTMKPGKTYRYRICNVGLKSSLNFRIQGHKMK 240
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330254725 246 VVGADASYLKPFTTNVIVLGPGQTTDVLITGDQPPNRYYMAA--RAYQSAQnapfgntTTTAILQYKsapccgvgGGSGt 323
Cdd:PLN02354 241 LVEMEGSHVLQNDYDSLDVHVGQCFSVLVTANQAPKDYYMVAstRFLKKVL-------TTTGIIRYE--------GGKG- 304
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330254725 324 kkgnsfkPIMPILPAyNDTNTVTRFSQsFRSLRRAEVPTEIDENLFVTIGLGLNNCPKNFRSRRCQGPNGTRFTASMNNV 403
Cdd:PLN02354 305 -------PASPELPE-APVGWAWSLNQ-FRSFRWNLTASAARPNPQGSYHYGKINITRTIKLVNSASKVDGKLRYALNGV 375
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330254725 404 SFALPSNYSLLQAHHHGIPGVFTTD-FPAKPPVKfdytgnnISRSLYQPDrgtkLYKLKYGSRVQIVLqdtgivtpENH- 481
Cdd:PLN02354 376 SHVDPETPLKLAEYFGVADKVFKYDtIKDNPPAK-------ITKIKIQPN----VLNITFRTFVEIIF--------ENHe 436
                        490       500       510       520       530       540
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 330254725 482 ----PIHLHGYDFYIIAEGFGNFNPKKdTAKFNLEDPPLRNTVGVPVNGWAVIRFIADNPGVW 540
Cdd:PLN02354 437 ksmqSWHLDGYSFFAVAVEPGTWTPEK-RKNYNLLDAVSRHTVQVYPKSWAAILLTFDNAGMW 498
PLN00044 PLN00044
multi-copper oxidase-related protein; Provisional
50-540 3.04e-32

multi-copper oxidase-related protein; Provisional


Pssm-ID: 165622 [Multi-domain]  Cd Length: 596  Bit Score: 131.32  E-value: 3.04e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330254725  50 ITVNGMFPGPMLVVNNGDTLVVKVINRARYNITIHWHGVRQMRTGWADGPeFVTQCPIRPGSSYTYRFTIQGQEGTLWWH 129
Cdd:PLN00044  51 IGINGQFPGPALNVTTNWNLVVNVRNALDEPLLLTWHGVQQRKSAWQDGV-GGTNCAIPAGWNWTYQFQVKDQVGSFFYA 129
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330254725 130 AHSSWLRAT-VYGSLLVFPPAGSSYPFTKPHR-NVPLLLGEWWDANPVDvLRESIRTGGAPNNSDAYTINGQPGDLYkcs 207
Cdd:PLN00044 130 PSTALHRAAgGYGAITINNRDVIPIPFGFPDGgDITLFIADWYARDHRA-LRRALDAGDLLGAPDGVLINAFGPYQY--- 205
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330254725 208 sqDTTVVP-------INV--GETILLRVINSALNQPLFFTVANHKLTVVGADASYLKPFTTNVIVLGPGQTTDVLITGDQ 278
Cdd:PLN00044 206 --NDSLVPpgityerINVdpGKTYRFRVHNVGVATSLNFRIQGHNLLLVEAEGSYTSQQNYTNLDIHVGQSYSFLLTMDQ 283
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330254725 279 PPNRYYMAARAYQSAQNAPFGNTTTTAILQYKsapccgvgggsgtkkgNSFKPIMPILPAYNDTNTVTRFS-QSFRSLRR 357
Cdd:PLN00044 284 NASTDYYVVASARFVDAAVVDKLTGVAILHYS----------------NSQGPASGPLPDAPDDQYDTAFSiNQARSIRW 347
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330254725 358 AEVPTEIDENLFVTIGLGLNNCPKNF--RSRRCQGPNGtRFTASMNNVSFALPSNySLLQAHHHGIPGVFTTDFPAKPPV 435
Cdd:PLN00044 348 NVTASGARPNPQGSFHYGDITVTDVYllQSMAPELIDG-KLRATLNEISYIAPST-PLMLAQIFNVPGVFKLDFPNHPMN 425
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330254725 436 KFdytgnnisrslyqPDRGTKLYKLKYGSRVQIVLQDTGIVTpenHPIHLHGYDFYIIAEGFGNFNpKKDTAKFNLEDPP 515
Cdd:PLN00044 426 RL-------------PKLDTSIINGTYKGFMEIIFQNNATNV---QSYHLDGYAFFVVGMDYGLWT-DNSRGTYNKWDGV 488
                        490       500
                 ....*....|....*....|....*
gi 330254725 516 LRNTVGVPVNGWAVIRFIADNPGVW 540
Cdd:PLN00044 489 ARSTIQVFPGAWTAILVFLDNAGIW 513
CuRO_1_Tv-LCC_like cd13856
The first cupredoxin domain of fungal laccases similar to Tv-LCC from Trametes versicolor; ...
30-133 4.47e-32

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: 120.13  E-value: 4.47e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330254725  30 HHEFIIQATKVKRLCETHNSITVNGMFPGPMLVVNNGDTLVVKVINR-----ARYNITIHWHGVRQMRTGWADGPEFVTQ 104
Cdd:cd13856    2 TYTLNIVNTRLAPDGFERSAVLANGQFPGPLITANKGDTFRITVVNQltdptMRRSTSIHWHGIFQHGTNYADGPAFVTQ 81
                         90       100
                 ....*....|....*....|....*....
gi 330254725 105 CPIRPGSSYTYRFTIQGQEGTLWWHAHSS 133
Cdd:cd13856   82 CPIAPNHSFTYDFTAGDQAGTFWYHSHLS 110
CuRO_1_MaLCC_like cd13854
The first cupredoxin domain of the fungal laccases similar to Ma-LCC from Melanocarpus ...
48-133 5.27e-31

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: 116.96  E-value: 5.27e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330254725  48 NSITVNGMFPGPMLVVNNGDTLVVKVINRARYNIT-IHWHGVRQMRTGWADGPEFVTQCPIRPGSSYTYRFTIQgQEGTL 126
Cdd:cd13854   23 EVMLINGQYPGPLIEANWGDTIEVTVINKLQDNGTsIHWHGIRQLNTNWQDGVPGVTECPIAPGDTRTYRFRAT-QYGTS 101

                 ....*..
gi 330254725 127 WWHAHSS 133
Cdd:cd13854  102 WYHSHYS 108
CuRO_1_Abr2_like cd13850
The first cupredoxin domain of a group of fungal Laccases similar to Abr2 from Aspergillus ...
50-131 1.34e-30

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: 115.47  E-value: 1.34e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330254725  50 ITVNGMFPGPMLVVNNGDTLVVKVINRARYNITIHWHGVRQMRTGWADGPEFVTQCPIRPGSSYTYRFTIQGQEGTLWWH 129
Cdd:cd13850   20 ILINGQFPGPPIILDEGDEVEILVTNNLPVNTTIHFHGILQRGTPWSDGVPGVTQWPIQPGGSFTYRWKAEDQYGLYWYH 99

                 ..
gi 330254725 130 AH 131
Cdd:cd13850  100 SH 101
PLN02792 PLN02792
oxidoreductase
50-540 1.36e-29

oxidoreductase


Pssm-ID: 178389 [Multi-domain]  Cd Length: 536  Bit Score: 122.78  E-value: 1.36e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330254725  50 ITVNGMFPGPMLVVNNGDTLVVKVINRARYNITIHWHGVRQMRTGWADGPeFVTQCPIRPGSSYTYRFTIQGQEGTLWWH 129
Cdd:PLN02792  38 ILINGQFPGPEIRSLTNDNLVINVHNDLDEPFLLSWNGVHMRKNSYQDGV-YGTTCPIPPGKNYTYDFQVKDQVGSYFYF 116
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330254725 130 AHSSWLRAT-VYGSLLVFPPAGSSYPFTKPHRNVPLLLGEWWDANPVDVlrESIRTGG--APNNSDAYTINGQpGDLYKC 206
Cdd:PLN02792 117 PSLAVQKAAgGYGSLRIYSLPRIPVPFPEPAGDFTFLIGDWYRRNHTTL--KKILDGGrkLPLMPDGVMINGQ-GVSYVY 193
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330254725 207 SsqdttvVPINVGETILLRVINSALNQPLFFTVANHKLTVVGADASYLKPFTTNVIVLGPGQTTDVLITGDQPPNRYYMA 286
Cdd:PLN02792 194 S------ITVDKGKTYRFRISNVGLQTSLNFEILGHQLKLIEVEGTHTVQSMYTSLDIHVGQTYSVLVTMDQPPQNYSIV 267
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330254725 287 ARAYQSAQNAPFGNTtttaiLQYKSApccgvgggsgtkKGNsfKPIMPILPAYNDTNTVTRFSQSFRSLRRAEVP----- 361
Cdd:PLN02792 268 VSTRFIAAKVLVSST-----LHYSNS------------KGH--KIIHARQPDPDDLEWSIKQAQSIRTNLTASGPrtnpq 328
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330254725 362 -------TEIDENLFVTIGLGLnncpknfrSRRCQgpngtRFtaSMNNVSFaLPSNYSLLQAHHHGIPGVFTT-DFPAKP 433
Cdd:PLN02792 329 gsyhygkMKISRTLILESSAAL--------VKRKQ-----RY--AINGVSF-VPSDTPLKLADHFKIKGVFKVgSIPDKP 392
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330254725 434 pvkfdYTGNNISRSlyqpdrgTKLYKLKYGSRVQIVLQDTGIVTpenHPIHLHGYDFYIIAEGFGNFNpKKDTAKFNLED 513
Cdd:PLN02792 393 -----RRGGGMRLD-------TSVMGAHHNAFLEIIFQNREKIV---QSYHLDGYNFWVVGINKGIWS-RASRREYNLKD 456
                        490       500
                 ....*....|....*....|....*..
gi 330254725 514 PPLRNTVGVPVNGWAVIRFIADNPGVW 540
Cdd:PLN02792 457 AISRSTTQVYPESWTAVYVALDNVGMW 483
CuRO_3_MaLCC_like cd13901
The third cupredoxin domain of the fungal laccases similar to Ma-LCC from Melanocarpus ...
466-559 7.17e-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: 112.32  E-value: 7.17e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330254725 466 VQIVLQDTgivTPENHPIHLHGYDFYIIAEGFGNFNPkkDTAKFNLEDPPLRNTVGVPVNGWAVIRFIADNPGVWIMHCH 545
Cdd:cd13901   69 VYIVIQNN---SPLPHPIHLHGHDFYILAQGTGTFDD--DGTILNLNNPPRRDVAMLPAGGYLVIAFKTDNPGAWLMHCH 143
                         90
                 ....*....|....
gi 330254725 546 LDAHISWGLAMAFL 559
Cdd:cd13901  144 IAWHASGGLALQFL 157
CuRO_1_AAO cd13845
The first cupredoxin domain of plant Ascorbate oxidase; Ascorbate oxidase catalyzes the ...
50-147 1.95e-28

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: 109.84  E-value: 1.95e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330254725  50 ITVNGMFPGPMLVVNNGDTLVVKVINR-ARYNITIHWHGVRQMRTGWADGPEFVTQCPIRPGSSYTYRFTIQgQEGTLWW 128
Cdd:cd13845   22 IGINGQFPGPTIRATAGDTIVVELENKlPTEGVAIHWHGIRQRGTPWADGTASVSQCPINPGETFTYQFVVD-RPGTYFY 100
                         90       100
                 ....*....|....*....|
gi 330254725 129 HAHSSWLR-ATVYGSLLVFP 147
Cdd:cd13845  101 HGHYGMQRsAGLYGSLIVDP 120
CuRO_2_LCC_like cd04205
Cupredoxin domain 2 of laccase-like multicopper oxidases; including laccase, CueO, spore coat ...
162-309 3.55e-28

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: 110.14  E-value: 3.55e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330254725 162 VPLLLGEWWDANPVDVLRE-SIRTGGAPNNSDAYTINGQPGD----LYKCSSQDTTVVPINVGETILLRVINSALNQPLF 236
Cdd:cd04205    1 RVLLLSDWYHDSAEDVLAGyMPNSFGNEPVPDSLLINGRGRFncsmAVCNSGCPLPVITVEPGKTYRLRLINAGSFASFN 80
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 330254725 237 FTVANHKLTVVGADASYLKPFTTNVIVLGPGQTTDVLITGDQPPNRYYMAARAYqSAQNAPFGNTTTTAILQY 309
Cdd:cd04205   81 FAIDGHNMTVIEVDGGYVEPLEVDNLDLAPGQRYDVLVKADQPPGNYWIRASAD-GRTFDEGGNPNGTAILRY 152
CuRO_1_Fet3p cd13851
The first Cupredoxin domain of multicopper oxidase Fet3P; Fet3p catalyzes the ferroxidase ...
50-133 7.73e-28

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: 108.12  E-value: 7.73e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330254725  50 ITVNGMFPGPMLVVNNGDTLVVKVINR-ARYNITIHWHGVRQMRTGWADGPEFVTQCPIRPGSSYTYRFTIQGQEGTLWW 128
Cdd:cd13851   23 IGINGQWPPPPIEVNKGDTVVIHATNSlGDQPTSLHFHGLFQNGTNYMDGPVGVTQCPIPPGQSFTYEFTVDTQVGTYWY 102

                 ....*
gi 330254725 129 HAHSS 133
Cdd:cd13851  103 HSHDG 107
CuRO_3_MCO_like_4 cd13910
The third cupredoxin domain of uncharacterized multicopper oxidase; Multicopper Oxidases (MCOs) ...
466-560 1.20e-27

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


Pssm-ID: 259977 [Multi-domain]  Cd Length: 166  Bit Score: 108.92  E-value: 1.20e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330254725 466 VQIVLQ--DTGivtpeNHPIHLHGYDFYIIAEGFGNFN----PKKDTAKFNLEDPPLRNTVGVPVNGWAVIRFIADNPGV 539
Cdd:cd13910   71 VDLVINnlDDG-----DHPFHLHGHKFWVLGSGDGRYGgggyTAPDGTSLNTTNPLRRDTVSVPGFGWAVLRFVADNPGL 145
                         90       100
                 ....*....|....*....|.
gi 330254725 540 WIMHCHLDAHISWGLAMAFLV 560
Cdd:cd13910  146 WAFHCHILWHMAAGMLMQFAV 166
CuRO_3_Diphenol_Ox cd13904
The third cupredoxin domain of fungal laccase, diphenol oxidase; Diphenol oxidase belongs to ...
468-560 1.38e-25

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: 102.76  E-value: 1.38e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330254725 468 IVLQ--DTGIvtpeNHPIHLHGYDFYIIAEGFGNFNPKK-DTAKFNLEDPPLRNTVGVPVNGWAVIRFIADNPGVWIMHC 544
Cdd:cd13904   67 IVINnlDPAI----DHPYHLHGVDFHIVARGSGTLTLEQlANVQYNTTNPLRRDTIVIPGGSWAVLRIPADNPGVWALHC 142
                         90
                 ....*....|....*.
gi 330254725 545 HLDAHISWGLAMAFLV 560
Cdd:cd13904  143 HIGWHLAAGFAGVVVV 158
CuRO_3_Abr2_like cd13898
The third cupredoxin domain of a group of fungal Laccases similar to Abr2 from Aspergillus ...
461-559 2.85e-25

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: 102.34  E-value: 2.85e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330254725 461 KYGSRVQIVLQDTGIVTPEnHPIHLHGYDFYIIAEGFGNFN-------PKKDTAKFNLEDPPLRNTVGVPV----NGWAV 529
Cdd:cd13898   54 KNGTWVDLIFQVTGPPQPP-HPIHKHGNKAFVIGTGTGPFNwssvaeaAEAAPENFNLVNPPLRDTFTTPPstegPSWLV 132
                         90       100       110
                 ....*....|....*....|....*....|
gi 330254725 530 IRFIADNPGVWIMHCHLDAHISWGLAMAFL 559
Cdd:cd13898  133 IRYHVVNPGAWLLHCHIQSHLAGGMAVVLL 162
CuRO_3_Fet3p cd13899
The third Cupredoxin domain of multicopper oxidase Fet3p; Fet3p catalyzes the ferroxidase ...
460-561 4.63e-23

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: 95.78  E-value: 4.63e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330254725 460 LKYGSRVQIVL--QDTGivtpeNHPIHLHGYDFYIIAEGFGNFNPKKD--TAKFNlEDPPLRNTVGVPVNGWAVIRFIAD 535
Cdd:cd13899   60 LNHGEVVELVVnnWDAG-----KHPFHLHGHKFQVVQRSPDVASDDPNppINEFP-ENPMRRDTVMVPPGGSVVIRFRAD 133
                         90       100
                 ....*....|....*....|....*.
gi 330254725 536 NPGVWIMHCHLDAHISWGLAmAFLVE 561
Cdd:cd13899  134 NPGVWFFHCHIEWHLEAGLA-ATFIE 158
CuRO_1_CopA cd13848
The first cupredoxin domain of CopA copper resistance protein family; CopA is a multicopper ...
50-145 5.27e-22

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: 91.19  E-value: 5.27e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330254725  50 ITVNGMFPGPMLVVNNGDTLVVKVINRARYNITIHWHGV---RQMrtgwaDGPEFVTQCPIRPGSSYTYRFTIQgQEGTL 126
Cdd:cd13848   22 ITVNGQVPGPLLRFKEGDDATIRVHNRLDEDTSIHWHGLllpNDM-----DGVPGLSFPGIKPGETFTYRFPVR-QSGTY 95
                         90       100
                 ....*....|....*....|
gi 330254725 127 WWHAHSSWLRAT-VYGSLLV 145
Cdd:cd13848   96 WYHSHSGLQEQTgLYGPIII 115
CuRO_3_Tv-LCC_like cd13903
The third cupredoxin domain of the fungal laccases similar to Tv-LCC from Trametes Versicolor; ...
391-558 2.39e-20

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: 87.72  E-value: 2.39e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330254725 391 PNGTRFTasMNNVSFALPSNYSLLQAhhhgIPGvfttdfpAKPPVKFDYTGNnisrslyqpdrgtkLYKLKYGSRVQIVL 470
Cdd:cd13903   12 GTTGLFT--INGVSYVSPTVPVLLQI----LSG-------ATSAEDLLPTES--------------TIILPRNKVVEITI 64
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330254725 471 QDTGIVTPenHPIHLHGYDFYIIaEGFGNFNPkkdtakfNLEDPPLRNTVGVPVNG-WAVIRFIADNPGVWIMHCHLDAH 549
Cdd:cd13903   65 PGGAIGGP--HPFHLHGHAFSVV-RSAGSNTY-------NYVNPVRRDVVSVGTPGdGVTIRFVTDNPGPWFLHCHIDWH 134

                 ....*....
gi 330254725 550 ISWGLAMAF 558
Cdd:cd13903  135 LEAGLAVVF 143
CuRO_D1_2dMcoN_like cd13859
The first cupredoxin domain of bacterial two domain multicopper oxidase McoN and similar ...
53-131 4.87e-20

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: 85.99  E-value: 4.87e-20
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 330254725  53 NGMFPGPMLVVNNGDTLVVKVINRARYNITIHWHGVRQMRTGWADGPEFVTQCPIRPGSSYTYRFTIQgQEGTLWWHAH 131
Cdd:cd13859   26 NGQVPGPLIHVKEGDDLVVHVTNNTTLPHTIHWHGVLQMGSWKMDGVPGVTQPAIEPGESFTYKFKAE-RPGTLWYHCH 103
CuRO_1_2dMco_1 cd13860
The first cupredoxin domain of bacteria two domain multicopper oxidase; This subfamily ...
32-131 1.50e-19

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: 84.56  E-value: 1.50e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330254725  32 EFIIQATKVKRlcETHNSITV-----NGMFPGPMLVVNNGDTLVVKVINRARYNITIHWHGVR---QMrtgwaDGPEFVT 103
Cdd:cd13860    2 VFHLVAEPVKW--EIAPGVKVeawgyNGSVPGPTIEVTEGDRVRILVTNELPEPTTVHWHGLPvpnGM-----DGVPGIT 74
                         90       100
                 ....*....|....*....|....*...
gi 330254725 104 QCPIRPGSSYTYRFTIQgQEGTLWWHAH 131
Cdd:cd13860   75 QPPIQPGETFTYEFTAK-QAGTYMYHSH 101
CuRO_1_AAO_like_2 cd13847
The first cupredoxin domain of Ascorbate oxidase homologs; This family includes fungal ...
44-145 7.41e-19

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: 82.58  E-value: 7.41e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330254725  44 CETHNSITVNGMFPGPMLVVNNGDTLVVKVINR-ARYNITIHWHGVRQMRTGWADGPEFVTQCPIRPGSSYTYRFTIQ-G 121
Cdd:cd13847   12 FGPRPSTLINGSFPGPELRVQEGQHLWVRVYNDlEAGNTTMHFHGLSQYMSPFSDGTPLASQWPIPPGKFFDYEFPLEaG 91
                         90       100
                 ....*....|....*....|....
gi 330254725 122 QEGTLWWHAHSSWLRATVYGSLLV 145
Cdd:cd13847   92 DAGTYYYHSHVGFQSVTAYGALIV 115
CuRO_1_CumA_like cd13861
The first cupredoxin domain of CumA like multicopper oxidase; This multicopper oxidase (MCO) ...
53-145 1.61e-18

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: 81.51  E-value: 1.61e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330254725  53 NGMFPGPMLVVNNGDTLVVKVINRARYNITIHWHGVR---QMrtgwaDGPEFVTQCPIRPGSSYTYRFTIQgQEGTLWWH 129
Cdd:cd13861   26 NGQVPGPELRVRQGDTLRVRLTNRLPEPTTIHWHGLRlpnAM-----DGVPGLTQPPVPPGESFTYEFTPP-DAGTYWYH 99
                         90
                 ....*....|....*....
gi 330254725 130 AH---SSWLRATVYGSLLV 145
Cdd:cd13861  100 PHvgsQEQLDRGLYGPLIV 118
CuRO_2_Tv-LCC_like cd13882
The second cupredoxin domain of the fungal laccases similar to Tv-LCC from Trametes versicolor; ...
164-313 2.34e-18

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: 82.46  E-value: 2.34e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330254725 164 LLLGEWWDANPVDVLRESIRTggaPNNSDAYTING----QPGDlykcsSQDTTVVPINVGETILLRVINSALNQPLFFTV 239
Cdd:cd13882    3 ITLGDWYHTAAPDLLATTAGV---PPVPDSGTINGkgrfDGGP-----TSPLAVINVKRGKRYRFRVINISCIPSFTFSI 74
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 330254725 240 ANHKLTVVGADASYLKPFTTNVIVLGPGQTTDVLITGDQPPNRYYMaaRAYQSAQNAPF-GNTTTTAILQYKSAP 313
Cdd:cd13882   75 DGHNLTVIEADGVETKPLTVDSVQIYAGQRYSVVVEANQPVDNYWI--RAPPTGGTPANnGGQLNRAILRYKGAP 147
CuRO_3_AAO_like_2 cd13895
The third cupredoxin domain of Ascorbate oxidase homologs; This family includes fungal ...
452-559 1.24e-17

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: 81.21  E-value: 1.24e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330254725 452 DRGTKLYKLKYGSRVQIVLQDTGIVTP--ENHPIHLHGYDFYIIAEGFGNFNP--KKDTAKFNLEDPPLRNTV------- 520
Cdd:cd13895   62 DPETNTFPAKLGEVLDIVWQNTASPTGglDAHPWHAHGAHYYDLGSGLGTYSAtaLANEEKLRGYNPIRRDTTmlyrygg 141
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*
gi 330254725 521 -GVP-----VNGWAVIRFIADNPGVWIMHCHLDAHISWGLAMAFL 559
Cdd:cd13895  142 kGYYpppgtGSGWRAWRLRVDDPGVWMLHCHILQHMIMGMQTVWV 186
CuRO_3_CopA cd13896
The third cupredoxin domain of CopA copper resistance protein family; CopA is a multicopper ...
459-560 1.92e-17

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


Pssm-ID: 259963 [Multi-domain]  Cd Length: 115  Bit Score: 78.45  E-value: 1.92e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330254725 459 KLKYGSRVQIVLQDTgivTPENHPIHLHGYDFYIIAEGfGNFNPKKDTakfnledpplrntVGVPVNGWAVIRFIADNPG 538
Cdd:cd13896   31 RVREGERVRIVFVND---TMMAHPMHLHGHFFQVENGN-GEYGPRKDT-------------VLVPPGETVSVDFDADNPG 93
                         90       100
                 ....*....|....*....|..
gi 330254725 539 VWIMHCHLDAHISWGLAMAFLV 560
Cdd:cd13896   94 RWAFHCHNLYHMEAGMMRVVEY 115
CuRO_2_MaLCC_like cd13880
The second cupredoxin domain of the fungal laccases similar to Ma-LCC from Melanocarpus ...
163-313 6.45e-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: 78.45  E-value: 6.45e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330254725 163 PLLLGEWWDANPVDVLRESIRTGGAPNnSDAYTINGQ---PGDLYKCSSQDTTVVPinvGETILLRVINSALNQPLFFTV 239
Cdd:cd13880    3 PVLLTDWYHRSAFELFSEELPTGGPPP-MDNILINGKgkfPCSTGAGSYFETTFTP---GKKYRLRLINTGVDTTFRFSI 78
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 330254725 240 ANHKLTVVGADASYLKPFTTNVIVLGPGQTTDVLITGDQPPNR-YYMAARaYQSAQNAP-FGNTTTTAILQYKSAP 313
Cdd:cd13880   79 DGHNLTVIAADFVPIVPYTTDSLNIGIGQRYDVIVEANQDPVGnYWIRAE-PATGCSGTnNNPDNRTGILRYDGAS 153
CuRO_1_AAO_like_1 cd13846
The first cupredoxin domain of plant Ascorbate oxidase homologs; This subfamily is composed of ...
50-145 7.37e-17

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: 76.68  E-value: 7.37e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330254725  50 ITVNGMFPGPMLVVNNGDTLVVKVINRARYNITIHWHGVRQMRTGWADGpEFVTQCPIRPGSSYTYRFTIQGQEGTLWWH 129
Cdd:cd13846   22 IAINGQFPGPTINVTTNDNVVVNVFNSLDEPLLLTWNGIQQRRNSWQDG-VLGTNCPIPPGWNWTYKFQVKDQIGSFFYF 100
                         90
                 ....*....|....*..
gi 330254725 130 AHSSWLRAT-VYGSLLV 145
Cdd:cd13846  101 PSLHFQRAAgGFGGIRV 117
CuRO_D2_2dMcoN_like cd04202
The second cupredoxin domain of bacterial two domain multicopper oxidase McoN and similar ...
454-556 5.65e-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: 74.98  E-value: 5.65e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330254725 454 GTKLYKLKYGSRVQIVLQDTGivtPENHPIHLHGYDFYIIAEGfGNFNPKkdtakfnlEDPPLRNTVGVPVNGWAVIRFI 533
Cdd:cd04202   39 ATPPLVVKEGDRVRIRLINLS---MDHHPMHLHGHFFLVTATD-GGPIPG--------SAPWPKDTLNVAPGERYDIEFV 106
                         90       100
                 ....*....|....*....|...
gi 330254725 534 ADNPGVWIMHCHLDAHISWGLAM 556
Cdd:cd04202  107 ADNPGDWMFHCHKLHHAMNGMGG 129
CuRO_2_tcLCC_insect_like cd13884
The second cupredoxin domain of the insect laccases similar to laccase 2 in Tribolium ...
164-309 1.15e-15

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: 74.19  E-value: 1.15e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330254725 164 LLLGEWWDANPVDVLrESIRTGGAPNNSDAYTINGQpGDLYKCSSQDTTVVP---INV--GETILLRVINSA-LNQPLFF 237
Cdd:cd13884    4 ILIQDWTHELSSERF-VGRGHNGGGQPPDSILINGK-GRYYDPKTGNTNNTPlevFTVeqGKRYRFRLINAGaTNCPFRV 81
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 330254725 238 TVANHKLTVVGADASYLKPFTTNVIVLGPGQTTDVLITGDQPPNRYYMAARAYQSAQNApfgNTTTTAILQY 309
Cdd:cd13884   82 SIDGHTLTVIASDGNDVEPVEVDSIIIYPGERYDFVLNANQPIGNYWIRARGLEDCDNR---RLQQLAILRY 150
CuRO_2_MCO_like_1 cd13886
The second cupredoxin domain of uncharacterized multicopper oxidase; Multicopper Oxidases ...
159-309 9.32e-14

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: 69.22  E-value: 9.32e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330254725 159 HRNVPLLLGEWWdanpvdvlreSIRTGGAPNNSDAYTINGQ-----PGDLYK--CSSQDTTVVPINV--GETILLRVINS 229
Cdd:cd13886   10 HDPSSVLLARYL----------APGNEGDEPVPDNGLINGIgqfdcASATYKiyCCASNGTYYNFTLepNKTYRLRLINA 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330254725 230 ALNQPLFFTVANHKLTVVGADASYLKPFTTNVIVLGPGQTTDVLITGDQP-PNRYYMAARAYQS--AQNAPFGNTTTTAI 306
Cdd:cd13886   80 GSFADFTFSVDGHPLTVIEADGTLVEPVEVHSITISVAQRYSVILTTNQPtGGNFWMRAELNTDcfTYDNPNLDPDVRAI 159

                 ...
gi 330254725 307 LQY 309
Cdd:cd13886  160 VSY 162
CuRO_2_AAO cd13871
The second cupredoxin domain of plant Ascorbate oxidase; Ascorbate oxidase catalyzes the ...
213-309 4.44e-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: 67.57  E-value: 4.44e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330254725 213 VVPINVGETILLRVINSALNQPLFFTVANHKLTVVGADASYLKPFTTNVIVLGPGQTTDVLITGDQPPNRYYMAARAYQS 292
Cdd:cd13871   73 ILHVSPGKTYRLRIASVTALSSLNFIIEGHNLTVVEADGNYVQPFEVSNLDIYSGETYSVLVTADQDPSRNYWVSVNVRG 152
                         90
                 ....*....|....*...
gi 330254725 293 AQ-NAPFGntttTAILQY 309
Cdd:cd13871  153 RRpNTPPG----LAILNY 166
CuRO_2_AAO_like_1 cd13872
The second cupredoxin domain of plant pollen multicopper oxidase homologous to ascorbate ...
164-309 1.16e-12

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: 65.50  E-value: 1.16e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330254725 164 LLLGEWWDANpVDVLRESIRTGGAPNNSDAYTINGQPGDLYKCSSQDTTVVPinvGETILLRVINSALNQPLFFTVANHK 243
Cdd:cd13872    5 VLIGDWYKTD-HKTLRQSLDKGRTLGRPDGILINGKGPYGYGANETSFTVEP---GKTYRLRISNVGLRTSLNFRIQGHK 80
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 330254725 244 LTVVGADASYLKPFTTNVIVLGPGQTTDVLITGDQPPNRYYMAArayqsaqNAPFGNT--TTTAILQY 309
Cdd:cd13872   81 MLLVETEGSYTAQNTYDSLDVHVGQSYSVLVTADQSPKDYYIVA-------SSRFLSPelTGVAILHY 141
CuRO_3_AAO_like_1 cd13894
The third cupredoxin domain of plant Ascorbate oxidase homologs; This subfamily is composed of ...
416-540 5.53e-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: 62.83  E-value: 5.53e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330254725 416 AHHHGIPGVFTTDFPAKPPVKfdytgnnisrslYQPDRGTKLYKLKYGSRVQIVLQDtgivtPEN--HPIHLHGYDFYII 493
Cdd:cd13894    9 ADYFKIKGVFQLDSIPDPPTR------------KTPYLGTSVINGTYRGFIEIVFQN-----NEDtvQSWHLDGYSFFVV 71
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*..
gi 330254725 494 AEGFGNFNPKKdTAKFNLEDPPLRNTVGVPVNGWAVIRFIADNPGVW 540
Cdd:cd13894   72 GMGFGDWTPEK-RKSYNLLDAVSRSTTQVYPGSWTAILLELDNVGMW 117
CuRO_1_LCC_like_3 cd13865
The second cupredoxin domain of uncharacterized multicopper oxidase; Multicopper Oxidases ...
49-131 6.51e-12

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: 62.33  E-value: 6.51e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330254725  49 SITVNG----------MFPGPMLVVNNGDTLVVKVINRARYNITIHWHG----VRQmrtgwaDGPEFVTQCPIRPGSSYT 114
Cdd:cd13865    9 TIEVNGkaatvygirqPDGTEGLRLTEGDRFDVELENRLDEPTTIHWHGlippNLQ------DGVPDVTQPPIPPGQSQR 82
                         90
                 ....*....|....*..
gi 330254725 115 YRFTIqGQEGTLWWHAH 131
Cdd:cd13865   83 YDFPL-VQPGTFWMHSH 98
CuRO_1_2DMCO_NIR_like cd11024
The cupredoxin domain 1 of a two-domain laccase related to nitrite reductase; The two-domain ...
51-148 8.91e-12

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


Pssm-ID: 259910 [Multi-domain]  Cd Length: 119  Bit Score: 62.29  E-value: 8.91e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330254725  51 TVNGMFPGPMLVVNNGDTLVVKVINRARYNITIHWHGVR---QMRTGWAdgpefvtqcPIRPGSSYTYRFtIQGQEGTLW 127
Cdd:cd11024   25 TYNGTVPGPTLRATEGDLVRIHFINTGDHPHTIHFHGIHdaaMDGTGLG---------PIMPGESFTYEF-VAEPAGTHL 94
                         90       100
                 ....*....|....*....|....*
gi 330254725 128 WHAHSSWLRATV----YGSLLVFPP 148
Cdd:cd11024   95 YHCHVQPLKEHIamglYGAFIVDPK 119
CuRO_1_McoC_like cd13855
The first cupredoxin domain of a multicopper oxidase McoC and similar proteins; This family ...
51-131 9.67e-12

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


Pssm-ID: 259924 [Multi-domain]  Cd Length: 121  Bit Score: 62.11  E-value: 9.67e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330254725  51 TVNGMFPGPMLVVNNGDTLVVKVINRARYNITIHWHGVRQMRTgwADGPefvTQCPIRPGSSYTYRFTI-QGQEGTLWWH 129
Cdd:cd13855   25 AYNGSVPGPLIEVFEGDTVEITFRNRLPEPTTVHWHGLPVPPD--QDGN---PHDPVAPGNDRVYRFTLpQDSAGTYWYH 99

                 ..
gi 330254725 130 AH 131
Cdd:cd13855  100 PH 101
CuRO_2_Fet3p_like cd13877
The second Cupredoxin domain of multicopper oxidase Fet3P; Fet3p catalyzes the ferroxidase ...
164-284 1.17e-11

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: 62.57  E-value: 1.17e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330254725 164 LLLGEWWDANPVDVLRESIR---TGGAPNNSDAYTINGqpgdlykcsSQDTTVvPINVGETILLRVINSALNQPLFFTVA 240
Cdd:cd13877    5 LTLSDWYHDQSPDLLRDFLSpynPTGAEPIPDSSLFND---------TQNATI-NFEPGKTYLLRIINMGAFASQYFHIE 74
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....
gi 330254725 241 NHKLTVVGADASYLKPFTTNVIVLGPGQTTDVLITGDQPPNRYY 284
Cdd:cd13877   75 GHDMTIIEVDGVYVKPYPVDTLYIAVGQRYSVLVKAKNDTDRNY 118
CuRO_1_CueO_FtsP cd04232
The first Cupredoxin domain of the multicopper oxidase CueO, the cell division protein FtsP, ...
52-131 1.48e-11

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


Pssm-ID: 259894 [Multi-domain]  Cd Length: 120  Bit Score: 61.82  E-value: 1.48e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330254725  52 VNGMFPGPMLVVNNGDTLVVKVINRARYNITIHWHGVRQmrTGWADG-PefvtQCPIRPGSSYTYRFTIQGQEGTLWWHA 130
Cdd:cd04232   25 YNGSYLGPTIRVKKGDTVRINVTNNLDEETTVHWHGLHV--PGEMDGgP----HQPIAPGQTWSPTFTIDQPAATLWYHP 98

                 .
gi 330254725 131 H 131
Cdd:cd04232   99 H 99
CuRO_2_Abr2_like cd13876
The second cupredoxin domain of a group of fungal Laccases similar to Abr2 from Aspergillus ...
163-310 1.86e-11

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: 61.84  E-value: 1.86e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330254725 163 PLLLGEWWDANPVDVLRESIRTGGAPNNSDAYTINGQpGDLYkCssqdTTVVPINVGETILLRVINSALNQPLFFTVANH 242
Cdd:cd13876    2 PIILSDWRHLTSEEYWKIMRASGIEPFCYDSILINGK-GRVY-C----LIVIVDPGERWVSLNFINAGGFHTLAFSIDEH 75
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 330254725 243 KLTVVGADASYLKPFTTNVIVLGPGQTTDVLITGDQPPNRYYMAARAYQSAQnapfgNTTTTAILQYK 310
Cdd:cd13876   76 PMWVYAVDGGYIEPQLVDAISITNGERYSVLVKLDKPPGDYTIRVASTGAPQ-----VISGYAILRYK 138
CuRO_3_CumA_like cd13906
The third cupredoxin domain of CumA like multicopper oxidase; This multicopper oxidase (MCO) ...
476-559 7.50e-11

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: 60.09  E-value: 7.50e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330254725 476 VTPENHPIHLHGYDFYIIAEgfgnfNPKKdtakfnLEDPPLRNTVGVPVNGWAVIRFIADNPGVWIMHCHLDAHISWGLa 555
Cdd:cd13906   64 ETAFLHPMHLHGHFFRVLSR-----NGRP------VPEPFWRDTVLLGPKETVDIAFVADNPGDWMFHCHILEHQETGM- 131

                 ....
gi 330254725 556 MAFL 559
Cdd:cd13906  132 MGVI 135
CuRO_3_MCO_like_3 cd13909
The third cupredoxin domain of uncharacterized multicopper oxidase; Multicopper Oxidases (MCOs) ...
450-560 1.02e-10

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


Pssm-ID: 259976 [Multi-domain]  Cd Length: 137  Bit Score: 59.84  E-value: 1.02e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330254725 450 QPDRG-TKLYKLKYGSRVQI-VLQDTGIvtpeNHPIHLHGYDFYIIAEgfgNFNPkkdtakfnledPPLRNTVGVPVNGW 527
Cdd:cd13909   42 VAGRPdDPLLEARRGETVRIeMVNNTGF----PHGMHLHGHHFRAILP---NGAL-----------GPWRDTLLMDRGET 103
                         90       100       110
                 ....*....|....*....|....*....|...
gi 330254725 528 AVIRFIADNPGVWIMHCHLDAHISWGLAMAFLV 560
Cdd:cd13909  104 REIAFVADNPGDWLLHCHMLEHAAAGMMSWFRV 136
CuRO_2_CopA cd13874
The second cupredoxin domain of CopA copper resistance protein family; CopA is a multicopper ...
192-275 1.17e-10

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: 58.84  E-value: 1.17e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330254725 192 DAYTINGQPgdlykcsSQDTTVVPINVGETILLRVINSALNQPLFFTVANHKLTVVGADASYLKPFTTNVIVLGPGQTTD 271
Cdd:cd13874   12 DTYLINGKP-------PEDNWTGLFKPGERVRLRFINAAASTYFDVRIPGGKMTVVAADGQDVRPVEVDEFRIGVAETYD 84

                 ....
gi 330254725 272 VLIT 275
Cdd:cd13874   85 VIVT 88
CuRO_1_MCO_like_2 cd13864
The second cupredoxin domain of uncharacterized multicopper oxidase; Multicopper Oxidases ...
58-133 2.14e-10

The second cupredoxin domain of uncharacterized multicopper oxidase; Multicopper Oxidases (MCOs) are multi-domain enzymes that are able to couple oxidation of substrates with reduction of dioxygen to water. MCOs 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: 59.09  E-value: 2.14e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330254725  58 GPMLVVNNGDTLVVKVIN------------RARYNITIHWHGVRQMRTGWA-----DGPEFVTQCPIRPGSSYTYRFTI- 119
Cdd:cd13864   31 GPTIRVKSGDTLNLLVTNhlcneqelskiwQDYCPTSIHFHGLVLENFGKQlanlvDGVPGLTQYPIGVGESYWYNFTIp 110
                         90
                 ....*....|....
gi 330254725 120 QGQEGTLWWHAHSS 133
Cdd:cd13864  111 EDTCGTFWYHSHSS 124
CuRO_2_McoC_like cd13881
The second cupredoxin domain of a multicopper oxidase McoC and similar proteins; This family ...
183-291 3.93e-10

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: 58.39  E-value: 3.93e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330254725 183 RTGGAPNNSDAYTINGQPGDLYKCSSQDTTVVPINVGETILLRVINSALNQPLFFTVANHKLTVVGADASYL-KPFTTNV 261
Cdd:cd13881   13 GDGQLAEPSAADWMFGREGDLVLVNGQLNPTITVRPGEVQRWRIVNAASARYFRLALDGHKFRLIGTDGGLLeAPREVDE 92
                         90       100       110
                 ....*....|....*....|....*....|
gi 330254725 262 IVLGPGQTTDVLITGDQPPNRYYMAARAYQ 291
Cdd:cd13881   93 LLLAPGERAEVLVTAGEPGGRLVLLALPYD 122
CuRO_1_Tth-MCO_like cd13853
The first cupredoxin domain of the bacterial laccases similar to Tth-MCO from Thermus ...
51-131 4.13e-10

The first cupredoxin domain of the bacterial laccases similar to Tth-MCO from Thermus Thermophilus; The subfamily of bacterial laccases includes Tth-MCO and similar proteins. Tth-MCO is a hyperthermophilic multicopper oxidase (MCO) from thermus thermophilus HB27. Laccase is a blue multi-copper enzyme that catalyzes the oxidation of a variety aromatic - notably phenolic and inorganic substances coupled to the reduction of molecular oxygen to water. It has been implicated in a wide spectrum of biological activities and, in particular, plays a key role in morphogenesis, development and lignin metabolism in fungi and plants. Although MCOs have diverse functions, majority of them have three cupredoxin domain repeats that include one mononuclear and one trinuclear copper center. The copper ions are bound in several sites: Type 1, Type 2, and/or Type 3. The ensemble of types 2 and 3 copper is called a trinuclear cluster. MCOs oxidize their substrate by accepting electrons at a mononuclear copper center and transferring them to the active site trinuclear copper center. The cupredoxin domain 1 of 3-domain MCOs contains part the trinuclear copper binding site, which is located at the interface of domains 1 and 3.


Pssm-ID: 259922 [Multi-domain]  Cd Length: 139  Bit Score: 58.03  E-value: 4.13e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330254725  51 TVNGMFPGPMLVVNNGDTLVVKVINR----------------ARYNIT-IHWHGVRQMRTGWADGPeFVTqcpIRPGSSY 113
Cdd:cd13853   24 TYNGSIPGPTLRVRPGDTLRITLKNDlppegaaneapapntpHCPNTTnLHFHGLHVSPTGNSDNV-FLT---IAPGESF 99
                         90       100
                 ....*....|....*....|
gi 330254725 114 TYRFTIQGQE--GTLWWHAH 131
Cdd:cd13853  100 TYEYDIPADHppGTYWYHPH 119
CuRO_2_Diphenol_Ox cd13883
The second cupredoxin domain of fungal laccase, diphenol oxidase; Diphenol oxidase belongs to ...
164-310 7.19e-10

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


Pssm-ID: 259950 [Multi-domain]  Cd Length: 164  Bit Score: 58.12  E-value: 7.19e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330254725 164 LLLGEWWDANPVDVLRESIRTGG-----APNNSDAYTINGQ-------PGDLYKCSSQDTTVVPINVGETILLRVINSAL 231
Cdd:cd13883    3 LFISDWYHDQSEVIVAGLLSPQGykgspAAPSPDSALINGIgqfncsaADPGTCCTQTSPPEIQVEAGKRTRFRLINAGS 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330254725 232 NQPLFFTVANHKLTVVGADAS-YLKPFTTNVIVLGPGQTTDVLITGDQ--PPNRYYMAARAYQSAQNAPFGNTTTTAILQ 308
Cdd:cd13883   83 HAMFRFSVDNHTLNVVEADDTpVYGPTVVHRIPIHNGQRYSVIIDTTSgkAGDSFWLRARMATDCFAWDLQQQTGKAILR 162

                 ..
gi 330254725 309 YK 310
Cdd:cd13883  163 YV 164
CuRO_3_McoC_like cd13902
The third cupredoxin domain of a multicopper oxidase McoC and similar proteins; This family ...
481-559 8.55e-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: 56.64  E-value: 8.55e-10
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 330254725 481 HPIHLHGYDFYIIAEgfgNFNPKKDtakfnlEDPPLRNTVGVPVNGWAVIRFIADNPGVWIMHCHLDAHISWGLaMAFL 559
Cdd:cd13902   55 HPFHLHGTQFQVLEI---DGNPQKP------EYRAWKDTVNLPPGEAVRIATRQDDPGMWMYHCHILEHEDAGM-MGML 123
CuRO_1_McoP_like cd13852
The first cupredoxin domain of multicopper oxidase McoP and similar proteins; This family ...
58-143 5.20e-09

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: 54.22  E-value: 5.20e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330254725  58 GPMLVVNNGDTLVVKVINRARYNITIHWHGvrqMRTGWA-DG-PEFVtqcpIRPGSSYTYRFTIQGQEGTLWWHAHSSWL 135
Cdd:cd13852   24 GPILRLRKGQKVRITFKNNLPEPTIIHWHG---LHVPAAmDGhPRYA----IDPGETYVYEFEVLNRAGTYWYHPHPHGL 96

                 ....*....
gi 330254725 136 RAT-VYGSL 143
Cdd:cd13852   97 TAKqVYRGL 105
PRK10965 PRK10965
multicopper oxidase; Provisional
52-131 2.37e-08

multicopper oxidase; Provisional


Pssm-ID: 236810 [Multi-domain]  Cd Length: 523  Bit Score: 56.57  E-value: 2.37e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330254725  52 VNGMFPGPMLVVNNGDTLVVKVINRARYNITIHWHGVRQmrTGWAD-GPefvtQCPIRPGSSYTYRFTIQGQEGTLWWHA 130
Cdd:PRK10965  70 YNGNLLGPAVRLQRGKAVTVDITNQLPEETTLHWHGLEV--PGEVDgGP----QGIIAPGGKRTVTFTVDQPAATCWFHP 143

                 .
gi 330254725 131 H 131
Cdd:PRK10965 144 H 144
CuRO_2_CopA_like_1 cd13870
The second cupredoxin domain of CopA copper resistance protein like family; The members of ...
194-278 4.48e-08

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: 51.56  E-value: 4.48e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330254725 194 YTINGQPGDlykcssqDTTVVPINVGETILLRVINSALNQPLFFTVANHKLTVVGADASYLKPFTTNVIVLGPGQTTDVL 273
Cdd:cd13870   18 YLINGRPPE-------DPAVFTARPGDRLRLRLINAAGDTAFRVALAGHRLTVTHTDGFPVEPVEVDALLIGMGERYDAI 90

                 ....*
gi 330254725 274 ITGDQ 278
Cdd:cd13870   91 VTANN 95
CuRO_3_MCO_like_2 cd13908
The third cupredoxin domain of uncharacterized multicopper oxidase; Multicopper Oxidases (MCOs) ...
436-558 1.50e-07

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


Pssm-ID: 259975 [Multi-domain]  Cd Length: 122  Bit Score: 50.14  E-value: 1.50e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330254725 436 KFD-YTGNNISRSLYQPdrgtkLYKLKYGSRVQIVLQDTgivTPENHPIHLHGYDFYIIAEGfgnfnpKKDTAKFnledp 514
Cdd:cd13908   17 GFNlWTINGKSYPDEDP-----PLVVQQGRRYRLVFRNA---SDDAHPMHLHRHTFEVTRID------GKPTSGL----- 77
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....
gi 330254725 515 pLRNTVGVPVNGWAVIRFIADNPGVWIMHCHLDAHISWGLAMAF 558
Cdd:cd13908   78 -RKDVVMLGGYQRVEVDFVADNPGLTLFHCHQQLHMDYGFMALF 120
CuRO_1_MCO_like_1 cd13862
The first cupredoxin domain of uncharacterized multicopper oxidase; Multicopper Oxidases (MCOs) ...
49-131 1.75e-07

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


Pssm-ID: 259931 [Multi-domain]  Cd Length: 123  Bit Score: 50.21  E-value: 1.75e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330254725  49 SITVNGMFPGPMLVVNNGDTLVVKVINRARYNITIHWHGvrQMRTGWADGPEFVTQCPIRPGSSYTYRFTiQGQEGTLWW 128
Cdd:cd13862   22 TLGYNGQVPGPLLRMRQGVSVTVDVFNDTDIPEYVHWHG--LPLPADVDGAMEEGTPSVPPHGHRRYRMT-PRPAGFRWY 98

                 ...
gi 330254725 129 HAH 131
Cdd:cd13862   99 HTH 101
CuRO_2_CumA_like cd13885
The second cupredoxin domain of CumA like multicopper oxidase; This multicopper oxidase (MCO) ...
160-282 1.24e-06

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: 47.71  E-value: 1.24e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330254725 160 RNVPLLLGEWW---DANPV---DVLRESIRTGGAPNnsdAYTINGQPgdlykcsSQDTTVVPinvGETILLRVINSAlnQ 233
Cdd:cd13885    1 RDLVWVLDDWRldpDGQAVpgfGTPHDAAHAGRIGN---LYTINGRV-------QPDFTVRA---GERVRLRLINAA--N 65
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|...
gi 330254725 234 PLFFTV--ANHKLTVVGADASYLKPFTTN--VIVLGPGQTTDVLITGDQPPNR 282
Cdd:cd13885   66 ARVFALkfPGHEARVIALDGQPAEPFVARngAVVLAPGMRIDLVIDAPQAAGT 118
CuRO_2_MCO_like_2 cd13887
The second cupredoxin domain of uncharacterized multicopper oxidase; Multicopper Oxidases ...
210-275 2.23e-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: 46.55  E-value: 2.23e-06
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 330254725 210 DTTVVPINVGETILLRVINSALNQPLFFTVANHKLTVVGADASYLKPFTTNVIVLGPGQTTDVLIT 275
Cdd:cd13887   22 DPEVVRVEPGGRVRLRVINGSTATNFHIDLGDLKGTLIAVDGNPVQPVEGRRFPLATAQRLDLLVT 87
CuRO_1_CuNIR_like cd04201
Cupredoxin domain 1 of Copper-containing nitrite reductase and two-domain laccase; ...
51-147 3.57e-06

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


Pssm-ID: 259864 [Multi-domain]  Cd Length: 120  Bit Score: 46.33  E-value: 3.57e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330254725  51 TVNGMFPGPMLVVNNGDTLVVKVINRARYNI--TIHWHGVrqmrTGwADGPEFVTQcpIRPGSSYTYRFTIQgQEGTLWW 128
Cdd:cd04201   25 TFDGDIPGPMLRVREGDTVELHFSNNPSSTMphNIDFHAA----TG-AGGGAGATF--IAPGETSTFSFKAT-QPGLYVY 96
                         90       100
                 ....*....|....*....|...
gi 330254725 129 HAHSSWLRATV----YGSLLVFP 147
Cdd:cd04201   97 HCAVAPVPMHIangmYGLILVEP 119
CuRO_1_CuNIR cd11020
Cupredoxin domain 1 of Copper-containing nitrite reductase; Copper-containing nitrite ...
46-118 1.72e-05

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: 44.12  E-value: 1.72e-05
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 330254725  46 THNSITVNGMFPGPMLVVNNGDTLVVKVINRARYNIT--IHWHGVrqmrTGwADGPEFVTqcpIRPGSSYTYRFT 118
Cdd:cd11020   20 TYTAWTFNGQVPGPVIRVREGDTVELTLTNPGTNTMPhsIDFHAA----TG-PGGGEFTT---IAPGETKTFSFK 86
CuRO_2_AAO_like_2 cd13873
The second cupredoxin domain of plant Ascorbate oxidase homologs; This family includes plant ...
162-273 2.11e-05

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: 44.97  E-value: 2.11e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330254725 162 VPLLLGEWWDANpvDVLRESIRTGG---APNNSDAYTINGQPG------DLYKCSSQDTTVVpINV--GETILLRVI-NS 229
Cdd:cd13873    3 RILLFSDYFPKT--DSTIETGLTATpfvWPGEPNALLVNGKSGgtcnksATEGCTTSCHPPV-IDVepGKTYRFRFIgAT 79
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*
gi 330254725 230 ALNqPLFFTVANH-KLTVVGADASYLKPFTTNVIVLGPGQTTDVL 273
Cdd:cd13873   80 ALS-FVSLGIEGHdNLTIIEADGSYTKPAETDHLQLGSGQRYSFL 123
CuRO_3_Tth-MCO_like cd13900
The third cupredoxin domain of the bacterial laccases similar to Tth-MCO from Thermus ...
477-549 2.16e-05

The third cupredoxin domain of the bacterial laccases similar to Tth-MCO from Thermus Thermophilus; The subfamily of bacterial laccases includes Tth-MCO and similar proteins. Tth-MCO is a hyperthermophilic multicopper oxidase (MCO) from thermus thermophilus HB27. Laccase is a blue multi-copper enzyme that catalyzes the oxidation of a variety aromatic - notably phenolic and inorganic substances coupled to the reduction of molecular oxygen to water. It has been implicated in a wide spectrum of biological activities and, in particular, plays a key role in morphogenesis, development and lignin metabolism in fungi and plants. Although MCOs have diverse functions, majority of them have three cupredoxin domain repeats that include one mononuclear and one trinuclear copper center. The copper ions are bound in several sites: Type 1, Type 2, and/or Type 3. The ensemble of types 2 and 3 copper is called a trinuclear cluster. MCOs oxidize their substrate by accepting electrons at a mononuclear copper center and transferring them to the active site trinuclear copper center. The cupredoxin domain 3 of 3-domain MCOs contains the Type 1 (T1) copper binding site and part the trinuclear copper binding site, which is located at the interface of domains 1 and 3.


Pssm-ID: 259967 [Multi-domain]  Cd Length: 123  Bit Score: 44.16  E-value: 2.16e-05
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 330254725 477 TPENHPIHLHGYDFYIIAegfgnFNPKKdtakfnLEDPPLRNTVGVPVNGWAVIR--FIaDNPGVWIMHCHLDAH 549
Cdd:cd13900   50 SGEDHPFHIHVNPFQVVS-----INGKP------GLPPVWRDTVNVPAGGSVTIRtrFR-DFTGEFVLHCHILDH 112
CuRO_3_MCO_like_1 cd13907
The third cupredoxin domain of uncharacterized multicopper oxidase; Multicopper Oxidases (MCOs) ...
481-561 3.23e-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: 44.40  E-value: 3.23e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330254725 481 HPIHLHGYDFYIIAEGFG-NFNPKKDTAKFNLEDPPLRNTVGV-PVNGWAVIRFIADNPGVWIMHCHLDAHISWGLAMAF 558
Cdd:cd13907   72 HPIHLHGVQFQVLERSVGpKDRAYWATVKDGFIDEGWKDTVLVmPGERVRIIKPFDDYKGLFLYHCHNLEHEDMGMMRNF 151

                 ...
gi 330254725 559 LVE 561
Cdd:cd13907  152 LVE 154
CuRO_D2_2dMcoN_like cd04202
The second cupredoxin domain of bacterial two domain multicopper oxidase McoN and similar ...
164-279 3.34e-05

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


Pssm-ID: 259865 [Multi-domain]  Cd Length: 138  Bit Score: 43.78  E-value: 3.34e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330254725 164 LLLGEWwdanPVDVLRESIRTGGAPNNsdAYTINGQPGDlykcssqDTTVVPINVGETILLRVIN-SALNQPlfFTVANH 242
Cdd:cd04202    6 LVLQEW----FVDPGTTPMPPEGMDFN--YFTINGKSFP-------ATPPLVVKEGDRVRIRLINlSMDHHP--MHLHGH 70
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|
gi 330254725 243 KLTVVGADASYLK---PFTTNVIVLGPGQTTDVLITGDQP 279
Cdd:cd04202   71 FFLVTATDGGPIPgsaPWPKDTLNVAPGERYDIEFVADNP 110
CuRO_1_Ceruloplasmin_like_1 cd04229
cupredoxin domain of ceruloplasmin homologs; Uncharacterized subfamily of ceruloplasmin ...
58-145 1.46e-04

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


Pssm-ID: 259891 [Multi-domain]  Cd Length: 175  Bit Score: 42.79  E-value: 1.46e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330254725  58 GPMLVVNNGDTLVVKVINR-ARYNITIHWHGVRQmrtgWADGPEFVTQC--PIRPGSSYTYRFTIQGQEG--------TL 126
Cdd:cd04229   73 GPVIRAEVGDTIKVVFKNNlDEFPVNMHPHGGLY----SKDNEGTTDGAgdVVAPGETYTYRWIVPEDAGpgpgdpssRL 148
                         90       100
                 ....*....|....*....|...
gi 330254725 127 WW-HAHSSWLRAT---VYGSLLV 145
Cdd:cd04229  149 WLyHSHVDVFAHTnagLVGPIIV 171
CuRO_3_ceruloplasmin cd04224
The third cupredoxin domain of Ceruloplasmin; Ceruloplasmin is a multicopper oxidase essential ...
58-119 1.87e-04

The third 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 third cupredoxin domain of ceruloplasmin.


Pssm-ID: 259886 [Multi-domain]  Cd Length: 197  Bit Score: 42.85  E-value: 1.87e-04
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 330254725  58 GPMLVVNNGDTLVVKVINRARYNITIHWHGVRQMR----TGWADGPEFvTQCPIRPGSSYTYRFTI 119
Cdd:cd04224   82 GPVIRAEVGDTIKVTFRNKASRPFSIQPHGVFYEKnyegAMYRDGDPS-PGSHVSPGETFTYEWTV 146
CuRO_1_ceruloplasmin cd04222
The first cupredoxin domain of Ceruloplasmin; Ceruloplasmin is a multicopper oxidase essential ...
56-131 6.06e-04

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


Pssm-ID: 259884 [Multi-domain]  Cd Length: 183  Bit Score: 41.25  E-value: 6.06e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330254725  56 FPGPMLVVNNGDTLVVKVINRARYNITIHWHGVRQMRTG----WADGPEFVTQC--PIRPGSSYTYRFTIQGQEG----- 124
Cdd:cd04222   73 FLGPILKAEVGDVIVVHLKNFASRPYSLHPHGVFYNKENegalYPDNTSGFEKAddAVPPGGSYTYTWTVPEEQAptkad 152
                         90
                 ....*....|.
gi 330254725 125 ----TLWWHAH 131
Cdd:cd04222  153 anclTRIYHSH 163
CuRO_1_CuNIR cd11020
Cupredoxin domain 1 of Copper-containing nitrite reductase; Copper-containing nitrite ...
514-561 1.08e-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: 39.12  E-value: 1.08e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|.
gi 330254725 514 PPLRNTVGVPVNGWAVIRFIADNPGVWIMHC---HLDAHISWGLAMAFLVE 561
Cdd:cd11020   67 PGGGEFTTIAPGETKTFSFKALYPGVFMYHCataPVLMHIANGMYGAIIVE 117
CuRO_3_BOD cd13889
The third cupredoxin domain of Bilirubin oxidase (BOD); Bilirubin oxidase (BOD) catalyzes the ...
481-545 2.95e-03

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


Pssm-ID: 259956 [Multi-domain]  Cd Length: 124  Bit Score: 38.06  E-value: 2.95e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 330254725 481 HPIHLHGYDFYIIAEGfGNFNP-------KKDTakFNLEDpplRNTVGVpvngwaVIRFiADNPGVWIMHCH 545
Cdd:cd13889   51 HPIHIHLEDFQILSRN-GGSRAvppyergRKDV--VYLGP---GEEVRV------LMRF-RPFRGKYMMHCH 109
CuRO_2_ceruloplasmin_like_2 cd11023
cupredoxin domain of ceruloplasmin homologs; Uncharacterized subfamily of ceruloplasmin ...
529-560 4.27e-03

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


Pssm-ID: 259909 [Multi-domain]  Cd Length: 118  Bit Score: 37.59  E-value: 4.27e-03
                         10        20        30
                 ....*....|....*....|....*....|..
gi 330254725 529 VIRFIADNPGVWIMHCHLDAHISWGLAMAFLV 560
Cdd:cd11023   87 VADMTAADVGTWLLHCHVHDHYMAGMMTQFAV 118
CuRO_1_ceruloplasmin_like cd04199
Cupredoxin domains 1, 3, and 5 of ceruloplasmin and similar proteins; This family includes the ...
58-124 4.29e-03

Cupredoxin domains 1, 3, and 5 of ceruloplasmin and similar proteins; This family includes the first, third, and fifth cupredoxin domains of ceruloplasmin and similar proteins including the first, third and fifth cupredoxin domains of unprocessed coagulation factors V and VIII. Ceruloplasmin (ferroxidase) is a multicopper oxidase essential for normal iron homeostasis. It functions in copper transport, amine oxidation 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: 259862 [Multi-domain]  Cd Length: 177  Bit Score: 38.54  E-value: 4.29e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 330254725  58 GPMLVVNNGDTLVVKVINRARYNITIHWHGV------RQMRTGWADGPEFVTQCPIRPGSSYTYRFTIQGQEG 124
Cdd:cd04199   69 GPTIRAEVGDTIKVHFKNKASRPYSIHPHGVsyekdsEGASYSDQTGPDEKKDDAVAPGETYTYVWIVTEESG 141
 
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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