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Conserved domains on  [gi|1098637342|ref|XP_018785863|]
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PREDICTED: uncharacterized protein LOC108967075 [Bactrocera latifrons]

Protein Classification

multicopper oxidase( domain architecture ID 13125024)

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

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
CuRO_1_tcLCC2_insect_like cd13858
The first cupredoxin domain of insect laccases similar to laccase 2 in Tribolium castaneum; ...
 360-464 1.98e-72

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: 235.13  E-value: 1.98e-72
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1098637342  360 DGIERSVMVVNRMMPGPSIEVCEGDMIVVDVHNHLLGDSTTIHWHGMHQRNYPYMDGVPHISQCPISPHSTFRYRFRAEN 439
Cdd:cd13858      1 DGVERPVITVNGQLPGPSIEVCEGDTVVVDVKNRLPGESTTIHWHGIHQRGTPYMDGVPMVTQCPILPGQTFRYKFKADP 80

                           90       100
                   ....*....|....*....|....*
gi 1098637342  440 TGTHFWHSHTGMQRGDGVFGALIVR 464
Cdd:cd13858     81 AGTHWYHSHSGTQRADGLFGALIVR 105
CuRO_3_tcLLC2_insect_like cd13905
The third cupredoxin domain of the insect laccases similar to laccase 2 in Tribolium castaneum; ...
 863-1030 5.42e-67

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: 222.56  E-value: 5.42e-67
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1098637342  863 QLNHISLKIPPMALMPERNNVDDSLFCNDTSLAqqgIDCRTDFCNCHHVLQVPLNSVVELIVVDEGFTFDANHPFHLHGN 942
Cdd:cd13905      1 SINGISFVFPSSPLLSQPEDLSDSSSCDFCNVP---SKCCTEPCECTHVIKLPLNSVVEIVLINEGPGPGLSHPFHLHGH 77

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1098637342  943 AFRVVGLERLGSNVTIEMV-------KQLDRYNLLKRNLDRPPIKDTVTIPDGGYTILRFEAYNPGFWLFHCHIEFHAEI 1015
Cdd:cd13905     78 SFYVLGMGFPGYNSTTGEIlsqnwnnKLLDRGGLPGRNLVNPPLKDTVVVPNGGYVVIRFRADNPGYWLLHCHIEFHLLE 157

                          170
                   ....*....|....*
gi 1098637342 1016 GMALIIKVGDNDQMK 1030
Cdd:cd13905    158 GMALVLKVGEPSDPP 172
ascorbase super family cl37259
L-ascorbate oxidase, plant type; Members of this protein family are the copper-containing ...
 360-1039 3.21e-56

L-ascorbate oxidase, plant type; Members of this protein family are the copper-containing enzyme L-ascorbate oxidase (EC 1.10.3.3), also called ascorbase. This family is found in flowering plants, and shows greater sequence similarity to a family of laccases (EC 1.10.3.2) from plants than to other known ascorbate oxidases.


The actual alignment was detected with superfamily member TIGR03388:

Pssm-ID: 274555 [Multi-domain]  Cd Length: 541  Bit Score: 204.60  E-value: 3.21e-56
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1098637342  360 DGIERSVMVVNRMMPGPSIEVCEGDMIVVDVHNHLLGDSTTIHWHGMHQRNYPYMDGVPHISQCPISPHSTFRYRFRAEN 439
Cdd:TIGR03388   16 DCFEKLVIGINGQFPGPTIRAQAGDTIVVELTNKLHTEGVVIHWHGIRQIGTPWADGTAGVTQCAINPGETFIYNFVVDR 95

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1098637342  440 TGTHFWHSHTGMQRGDGVFGALIVRRPRAMEAHGHlYDfdlSEHKMILQDWVHTpgvsifSSHHHSRGDN--------KP 511
Cdd:TIGR03388   96 PGTYFYHGHYGMQRSAGLYGSLIVDVPDGEKEPFH-YD---GEFNLLLSDWWHK------SIHEQEVGLSskpmrwigEP 165

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1098637342  512 VNLLVNGRGRFYYAIwdqakkearTATVNKPNtqddkpvtpsptsttttttpttsttpltfvLNQSEVGGQYDLTPsqie 591
Cdd:TIGR03388  166 QSLLINGRGQFNCSL---------AAKFSSTN------------------------------LPQCNLKGNEQCAP---- 202

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1098637342  592 llqphndtsrnnmrlrnineisrlthvaqqppspsdrsdaepevefdltaqptnvqrtkravddiqlhqmplQIFHVRRG 671
Cdd:TIGR03388  203 ------------------------------------------------------------------------QILHVEPG 210

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1098637342  672 FRYRFRIINAEFLNCpIALSIDNHTLLAIHSDGYDFEPLEVGAMVTYAGERFDFVLNANQSIG-NYWIrfkglmdcsdqf 750
Cdd:TIGR03388  211 KTYRLRIASTTALAA-LNFAIEGHKLTVVEADGNYVEPFTVKDIDIYSGETYSVLLTTDQDPSrNYWI------------ 277

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1098637342  751 tsafqvgilryedasetePSGVLGwQHKADGIELNAMNRGSGHPDSLTAAEMTALPIYDTvpgvdrdalkpVADYKFFVY 830
Cdd:TIGR03388  278 ------------------SVGVRG-RKPNTPPGLTVLNYYPNSPSRLPPTPPPVTPAWDD-----------FDRSKAFSL 327

                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1098637342  831 YDFYAKDNPVfHPSDYYSFNDSLGKTNKL--YTP-QLNHISLKIPP----MALMPERNNVDDSLFCNDTSLAQQGIDCRT 903
Cdd:TIGR03388  328 AIKAAMGSPK-PPETSDRRIVLLNTQNKIngYTKwAINNVSLTLPHtpylGSLKYNLLNAFDQKPPPENYPRDYDIFKPP 406

                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1098637342  904 DFCNC---HHVLQVPLNSVVELIVVDEGfTFDAN----HPFHLHGNAFRVVGLERLGSNVTIEmVKQLdrynllkrNLDR 976
Cdd:TIGR03388  407 PNPNTttgNGIYRLKFNTTVDVILQNAN-TLNGNnsetHPWHLHGHDFWVLGYGEGKFRPGVD-EKSY--------NLKN 476

                          650       660       670       680       690       700
                   ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1098637342  977 PPIKDTVTIPDGGYTILRFEAYNPGFWLFHCHIEFHAEIGMALIIKVGdNDQMKSTPKNFPTC 1039
Cdd:TIGR03388  477 PPLRNTVVIFPYGWTALRFVADNPGVWAFHCHIEPHLHMGMGVVFAEG-VEKVGKLPKEALGC 538
VWC super family cl17735
von Willebrand factor type C domain; The high cutoff was used to prevent overlap with ...
 216-281 3.46e-03

von Willebrand factor type C domain; The high cutoff was used to prevent overlap with pfam00094.


The actual alignment was detected with superfamily member pfam00093:

Pssm-ID: 450195  Cd Length: 57  Bit Score: 36.63  E-value: 3.46e-03
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1098637342  216 CRFNDTVYDLGQTWHsPDGCTMYECAPLpersvvtpMINVFEKTCAPLPLDCPREQVYVKDCCQQC 281
Cdd:pfam00093    1 CVQNGVVYENGETWK-PDLCTICTCDDG--------KVLCDKIICPPLDCPNPRLEIPPGECCPVC 57
 
Name Accession Description Interval E-value
CuRO_1_tcLCC2_insect_like cd13858
The first cupredoxin domain of insect laccases similar to laccase 2 in Tribolium castaneum; ...
 360-464 1.98e-72

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: 235.13  E-value: 1.98e-72
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1098637342  360 DGIERSVMVVNRMMPGPSIEVCEGDMIVVDVHNHLLGDSTTIHWHGMHQRNYPYMDGVPHISQCPISPHSTFRYRFRAEN 439
Cdd:cd13858      1 DGVERPVITVNGQLPGPSIEVCEGDTVVVDVKNRLPGESTTIHWHGIHQRGTPYMDGVPMVTQCPILPGQTFRYKFKADP 80

                           90       100
                   ....*....|....*....|....*
gi 1098637342  440 TGTHFWHSHTGMQRGDGVFGALIVR 464
Cdd:cd13858     81 AGTHWYHSHSGTQRADGLFGALIVR 105
CuRO_3_tcLLC2_insect_like cd13905
The third cupredoxin domain of the insect laccases similar to laccase 2 in Tribolium castaneum; ...
 863-1030 5.42e-67

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: 222.56  E-value: 5.42e-67
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1098637342  863 QLNHISLKIPPMALMPERNNVDDSLFCNDTSLAqqgIDCRTDFCNCHHVLQVPLNSVVELIVVDEGFTFDANHPFHLHGN 942
Cdd:cd13905      1 SINGISFVFPSSPLLSQPEDLSDSSSCDFCNVP---SKCCTEPCECTHVIKLPLNSVVEIVLINEGPGPGLSHPFHLHGH 77

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1098637342  943 AFRVVGLERLGSNVTIEMV-------KQLDRYNLLKRNLDRPPIKDTVTIPDGGYTILRFEAYNPGFWLFHCHIEFHAEI 1015
Cdd:cd13905     78 SFYVLGMGFPGYNSTTGEIlsqnwnnKLLDRGGLPGRNLVNPPLKDTVVVPNGGYVVIRFRADNPGYWLLHCHIEFHLLE 157

                          170
                   ....*....|....*
gi 1098637342 1016 GMALIIKVGDNDQMK 1030
Cdd:cd13905    158 GMALVLKVGEPSDPP 172
ascorbase TIGR03388
L-ascorbate oxidase, plant type; Members of this protein family are the copper-containing ...
 360-1039 3.21e-56

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: 204.60  E-value: 3.21e-56
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1098637342  360 DGIERSVMVVNRMMPGPSIEVCEGDMIVVDVHNHLLGDSTTIHWHGMHQRNYPYMDGVPHISQCPISPHSTFRYRFRAEN 439
Cdd:TIGR03388   16 DCFEKLVIGINGQFPGPTIRAQAGDTIVVELTNKLHTEGVVIHWHGIRQIGTPWADGTAGVTQCAINPGETFIYNFVVDR 95

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1098637342  440 TGTHFWHSHTGMQRGDGVFGALIVRRPRAMEAHGHlYDfdlSEHKMILQDWVHTpgvsifSSHHHSRGDN--------KP 511
Cdd:TIGR03388   96 PGTYFYHGHYGMQRSAGLYGSLIVDVPDGEKEPFH-YD---GEFNLLLSDWWHK------SIHEQEVGLSskpmrwigEP 165

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1098637342  512 VNLLVNGRGRFYYAIwdqakkearTATVNKPNtqddkpvtpsptsttttttpttsttpltfvLNQSEVGGQYDLTPsqie 591
Cdd:TIGR03388  166 QSLLINGRGQFNCSL---------AAKFSSTN------------------------------LPQCNLKGNEQCAP---- 202

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1098637342  592 llqphndtsrnnmrlrnineisrlthvaqqppspsdrsdaepevefdltaqptnvqrtkravddiqlhqmplQIFHVRRG 671
Cdd:TIGR03388  203 ------------------------------------------------------------------------QILHVEPG 210

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1098637342  672 FRYRFRIINAEFLNCpIALSIDNHTLLAIHSDGYDFEPLEVGAMVTYAGERFDFVLNANQSIG-NYWIrfkglmdcsdqf 750
Cdd:TIGR03388  211 KTYRLRIASTTALAA-LNFAIEGHKLTVVEADGNYVEPFTVKDIDIYSGETYSVLLTTDQDPSrNYWI------------ 277

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1098637342  751 tsafqvgilryedasetePSGVLGwQHKADGIELNAMNRGSGHPDSLTAAEMTALPIYDTvpgvdrdalkpVADYKFFVY 830
Cdd:TIGR03388  278 ------------------SVGVRG-RKPNTPPGLTVLNYYPNSPSRLPPTPPPVTPAWDD-----------FDRSKAFSL 327

                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1098637342  831 YDFYAKDNPVfHPSDYYSFNDSLGKTNKL--YTP-QLNHISLKIPP----MALMPERNNVDDSLFCNDTSLAQQGIDCRT 903
Cdd:TIGR03388  328 AIKAAMGSPK-PPETSDRRIVLLNTQNKIngYTKwAINNVSLTLPHtpylGSLKYNLLNAFDQKPPPENYPRDYDIFKPP 406

                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1098637342  904 DFCNC---HHVLQVPLNSVVELIVVDEGfTFDAN----HPFHLHGNAFRVVGLERLGSNVTIEmVKQLdrynllkrNLDR 976
Cdd:TIGR03388  407 PNPNTttgNGIYRLKFNTTVDVILQNAN-TLNGNnsetHPWHLHGHDFWVLGYGEGKFRPGVD-EKSY--------NLKN 476

                          650       660       670       680       690       700
                   ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1098637342  977 PPIKDTVTIPDGGYTILRFEAYNPGFWLFHCHIEFHAEIGMALIIKVGdNDQMKSTPKNFPTC 1039
Cdd:TIGR03388  477 PPLRNTVVIFPYGWTALRFVADNPGVWAFHCHIEPHLHMGMGVVFAEG-VEKVGKLPKEALGC 538
CuRO_2_tcLCC_insect_like cd13884
The second cupredoxin domain of the insect laccases similar to laccase 2 in Tribolium ...
 482-761 6.81e-54

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: 184.74  E-value: 6.81e-54
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1098637342  482 EHKMILQDWVHTPGVSIFSSHHHSRGDNKPVNLLVNGRGRFYYaiwdqakkeartatvnkpntqddkpvtpsptsttttt 561
Cdd:cd13884      1 EHVILIQDWTHELSSERFVGRGHNGGGQPPDSILINGKGRYYD------------------------------------- 43

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1098637342  562 tpttsttpltfvlnqsevggqydltpsqiellqphndtsrnnmrlrnineisrlthvaqqppspsdrsdaepevefdlta 641
Cdd:cd13884        --------------------------------------------------------------------------------

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1098637342  642 qptnvqrtkraVDDIQLHQMPLQIFHVRRGFRYRFRIINAEFLNCPIALSIDNHTLLAIHSDGYDFEPLEVGAMVTYAGE 721
Cdd:cd13884     44 -----------PKTGNTNNTPLEVFTVEQGKRYRFRLINAGATNCPFRVSIDGHTLTVIASDGNDVEPVEVDSIIIYPGE 112

                          250       260       270       280
                   ....*....|....*....|....*....|....*....|
gi 1098637342  722 RFDFVLNANQSIGNYWIRFKGLMDCSdqFTSAFQVGILRY 761
Cdd:cd13884    113 RYDFVLNANQPIGNYWIRARGLEDCD--NRRLQQLAILRY 150
PLN02191 PLN02191
L-ascorbate oxidase
 360-1026 1.13e-50

L-ascorbate oxidase


Pssm-ID: 177843 [Multi-domain]  Cd Length: 574  Bit Score: 189.07  E-value: 1.13e-50
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1098637342  360 DGIERSVMVVNRMMPGPSIEVCEGDMIVVDVHNHLLGDSTTIHWHGMHQRNYPYMDGVPHISQCPISPHSTFRYRFRAEN 439
Cdd:PLN02191    38 DCKEGAVMTVNGQFPGPTIDAVAGDTIVVHLTNKLTTEGLVIHWHGIRQKGSPWADGAAGVTQCAINPGETFTYKFTVEK 117

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1098637342  440 TGTHFWHSHTGMQRGDGVFGALIVRRPRAmEAHGHLYDfdlSEHKMILQDWVH--TPGVSIFSSHHHSRGDNKPVNLLVN 517
Cdd:PLN02191   118 PGTHFYHGHYGMQRSAGLYGSLIVDVAKG-PKERLRYD---GEFNLLLSDWWHesIPSQELGLSSKPMRWIGEAQSILIN 193

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1098637342  518 GRGRFYYAIWDQAKKEArtatvnkpntqdDKPVtpsptsttttttpttsttpLTFvlnqsevggqydltpsqiellqPHN 597
Cdd:PLN02191   194 GRGQFNCSLAAQFSNGT------------ELPM-------------------CTF----------------------KEG 220

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1098637342  598 DtsrnnmrlrnineisrlthvaqqppspsdrsdaepevefdltaqptnvqrtkravddiqlhQMPLQIFHVRRGFRYRFR 677
Cdd:PLN02191   221 D-------------------------------------------------------------QCAPQTLRVEPNKTYRIR 239

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1098637342  678 IINAEFLnCPIALSIDNHTLLAIHSDGYDFEPLEVGAMVTYAGERFDFVLNANQSIG-NYWIRFkGLMDCSDQFTSAFQv 756
Cdd:PLN02191   240 LASTTAL-ASLNLAVQGHKLVVVEADGNYITPFTTDDIDIYSGESYSVLLTTDQDPSqNYYISV-GVRGRKPNTTQALT- 316

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1098637342  757 gILRYEDASETepsgvlgwqhkadgielnamnRGSGHPDSLTaaemtalPIYDTvpgVDRDalkpvadyKFFVYYDFYAK 836
Cdd:PLN02191   317 -ILNYVTAPAS---------------------KLPSSPPPVT-------PRWDD---FERS--------KNFSKKIFSAM 356

                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1098637342  837 DNPvfHPSDYYSFNDSLGKTNKLY-----------------TPQLNHI--------SLKIPPMALMPERNNVDDSLFCND 891
Cdd:PLN02191   357 GSP--SPPKKYRKRLILLNTQNLIdgytkwainnvslvtpaTPYLGSVkynlklgfNRKSPPRSYRMDYDIMNPPPFPNT 434

                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1098637342  892 TSlaQQGIdcrtdfcnchhvLQVPLNSVVELIV----VDEGFTFDAnHPFHLHGNAFRVVGlerLGSNvtiEMVKQLDRY 967
Cdd:PLN02191   435 TT--GNGI------------YVFPFNVTVDVIIqnanVLKGVVSEI-HPWHLHGHDFWVLG---YGDG---KFKPGIDEK 493

                          650       660       670       680       690
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 1098637342  968 NLlkrNLDRPPIKDTVTIPDGGYTILRFEAYNPGFWLFHCHIEFHAEIGMALIIKVGDN 1026
Cdd:PLN02191   494 TY---NLKNPPLRNTAILYPYGWTAIRFVTDNPGVWFFHCHIEPHLHMGMGVVFAEGLN 549
Cu-oxidase_3 pfam07732
Multicopper oxidase; This entry contains many divergent copper oxidase-like domains that are ...
 350-466 1.60e-47

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: 165.11  E-value: 1.60e-47
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1098637342  350 DCERPHCVLGDGIERSVMVVNRMMPGPSIEVCEGDMIVVDVHNHLlGDSTTIHWHGMHQRNYPYMDGVPHISQCPISPHS 429
Cdd:pfam07732    1 TVTYGTVSPLGGTRQAVIGVNGQFPGPTIRVREGDTVVVNVTNNL-DEPTSIHWHGLQQRGTPWMDGVPGVTQCPIPPGQ 79

                           90       100       110
                   ....*....|....*....|....*....|....*...
gi 1098637342  430 TFRYRFRAENT-GTHFWHSHTGMQRGDGVFGALIVRRP 466
Cdd:pfam07732   80 SFTYRFQVKQQaGTYWYHSHTSGQQAAGLAGAIIIEDR 117
SufI COG2132
Multicopper oxidase with three cupredoxin domains (includes cell division protein FtsP and ...
 358-1025 5.29e-35

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: 139.30  E-value: 5.29e-35
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1098637342  358 LGDGIERSVMVVNRMMPGPSIEVCEGDMIVVDVHNHlLGDSTTIHWHGMHQRNypYMDGVPHIsqcPISPHSTFRYRFRA 437
Cdd:COG2132     27 LLPGKPTTVWGYNGQYPGPTIRVREGDRVRVRVTNR-LPEPTTVHWHGLRVPN--AMDGVPGD---PIAPGETFTYEFPV 100

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1098637342  438 ENT-GTHFWHSH----TGMQRGDGVFGALIVRRPramEAHGHLYDFDlseHKMILQDWVHTPGVSIFSSHHHSRGdnkpv 512
Cdd:COG2132    101 PQPaGTYWYHPHthgsTAEQVYRGLAGALIVEDP---EEDLPRYDRD---IPLVLQDWRLDDDGQLLYPMDAAMG----- 169

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1098637342  513 nllvngrGRFYYAIwdqakkeartaTVNkpntqddkpvtpsptsttttttpttsttpltfvlnqsevgGQYDLTpsqiel 592
Cdd:COG2132    170 -------GRLGDTL-----------LVN----------------------------------------GRPNPT------ 185

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1098637342  593 lqphndtsrnnmrlrnineisrlthvaqqppspsdrsdaepevefdltaqptnvqrtkravddiqlhqmplqiFHVRRGF 672
Cdd:COG2132    186 -------------------------------------------------------------------------LEVRPGE 192

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1098637342  673 RYRFRIINA---EFLNcpIALSiDNHTLLAIHSDGYDFE-PLEVGAMVTYAGERFDFVLNANQSIGNYWIrfkgLMDcSD 748
Cdd:COG2132    193 RVRLRLLNAsnaRIYR--LALS-DGRPFTVIATDGGLLPaPVEVDELLLAPGERADVLVDFSADPGEEVT----LAN-PF 264

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1098637342  749 QFTSAFQVGILRYEDASETEPSgvlgwqhkadgielnamnrgsghPDSLTaaemtalpiydTVPGVDRDALKPVADYKFF 828
Cdd:COG2132    265 EGRSGRALLTLRVTGAAASAPL-----------------------PANLA-----------PLPDLEDREAVRTRELVLT 310

                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1098637342  829 VYYDFYAkdnpvfhpsdyYSFNdslgktNKLYTPqlnhislkIPPMalmpernnvddslfcndtslaqqgidcrtdfcnc 908
Cdd:COG2132    311 GGMAGYV-----------WTIN------GKAFDP--------DRPD---------------------------------- 331

                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1098637342  909 hhvLQVPLNSVVELIVVDEGftfDANHPFHLHGNAFRVvgLERLGSNVtiemvkqldrynllkrnlDRPPIKDTVTIPDG 988
Cdd:COG2132    332 ---LTVKLGERERWTLVNDT---MMPHPFHLHGHQFQV--LSRNGKPP------------------PEGGWKDTVLVPPG 385

                          650       660       670
                   ....*....|....*....|....*....|....*....
gi 1098637342  989 G-YTIL-RFEAYnPGFWLFHCHIEFHAEIGMALIIKVGD 1025
Cdd:COG2132    386 EtVRILfRFDNY-PGDWMFHCHILEHEDAGMMGQFEVVP 423
Cu-oxidase_2 pfam07731
Multicopper oxidase; This entry contains many divergent copper oxidase-like domains that are ...
 904-1027 9.18e-32

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: 121.00  E-value: 9.18e-32
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1098637342  904 DFCNCHHVLQVPLNSVVELIVVDEGFTfdaNHPFHLHGNAFRVVGleRLGSNVTIEMVKqldrynllKRNLDRPPIKDTV 983
Cdd:pfam07731   28 LFPPNTNVITLPYGTVVEWVLQNTTTG---VHPFHLHGHSFQVLG--RGGGPWPEEDPK--------TYNLVDPVRRDTV 94

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....
gi 1098637342  984 TIPDGGYTILRFEAYNPGFWLFHCHIEFHAEIGMALIIKVGDND 1027
Cdd:pfam07731   95 QVPPGGWVAIRFRADNPGVWLFHCHILWHLDQGMMGQFVVRPGD 138
Cu-oxidase pfam00394
Multicopper oxidase; Many of the proteins in this family contain multiple similar copies of ...
 662-762 2.10e-18

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: 83.14  E-value: 2.10e-18
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1098637342  662 PLQIFHVRRGFRYRFRIINA---EFLNcpiaLSIDNHTLLAIHSDGYDFEPLEVGAMVTYAGERFDFVLNANQSIGNYWI 738
Cdd:pfam00394   48 SLATLTVTPGKTYRLRIINValdDSLN----FSIEGHKMTVVEVDGVYVNPFTVDSLDIFPGQRYSVLVTANQDPGNYWI 123

                           90       100
                   ....*....|....*....|....
gi 1098637342  739 RFKglMDCSDQFTSAfQVGILRYE 762
Cdd:pfam00394  124 VAS--PNIPAFDNGT-AAAILRYS 144
PLN02354 PLN02354
copper ion binding / oxidoreductase
 361-520 7.33e-17

copper ion binding / oxidoreductase


Pssm-ID: 177987 [Multi-domain]  Cd Length: 552  Bit Score: 85.23  E-value: 7.33e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1098637342  361 GIERSVMVVNRMMPGPSIEVCEGDMIVVDVHNHlLGDSTTIHWHGMHQRNYPYMDGVPHiSQCPISPHSTFRYRFRAENT 440
Cdd:PLN02354    43 GVPQQVILINGQFPGPNINSTSNNNIVINVFNN-LDEPFLLTWSGIQQRKNSWQDGVPG-TNCPIPPGTNFTYHFQPKDQ 120

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1098637342  441 -GTHFWHSHTGMQRGDGVFGALIVrrprameaHGHL-----YDFDLSEHKMILQDWVHTPGVSIFSSHHHSRGDNKPVNL 514
Cdd:PLN02354   121 iGSYFYYPSTGMHRAAGGFGGLRV--------NSRLlipvpYADPEDDYTVLIGDWYTKSHTALKKFLDSGRTLGRPDGV 192


                   ....*.
gi 1098637342  515 LVNGRG 520
Cdd:PLN02354   193 LINGKS 198
VWC pfam00093
von Willebrand factor type C domain; The high cutoff was used to prevent overlap with ...
 216-281 3.46e-03

von Willebrand factor type C domain; The high cutoff was used to prevent overlap with pfam00094.


Pssm-ID: 278520  Cd Length: 57  Bit Score: 36.63  E-value: 3.46e-03
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1098637342  216 CRFNDTVYDLGQTWHsPDGCTMYECAPLpersvvtpMINVFEKTCAPLPLDCPREQVYVKDCCQQC 281
Cdd:pfam00093    1 CVQNGVVYENGETWK-PDLCTICTCDDG--------KVLCDKIICPPLDCPNPRLEIPPGECCPVC 57
 
Name Accession Description Interval E-value
CuRO_1_tcLCC2_insect_like cd13858
The first cupredoxin domain of insect laccases similar to laccase 2 in Tribolium castaneum; ...
 360-464 1.98e-72

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: 235.13  E-value: 1.98e-72
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1098637342  360 DGIERSVMVVNRMMPGPSIEVCEGDMIVVDVHNHLLGDSTTIHWHGMHQRNYPYMDGVPHISQCPISPHSTFRYRFRAEN 439
Cdd:cd13858      1 DGVERPVITVNGQLPGPSIEVCEGDTVVVDVKNRLPGESTTIHWHGIHQRGTPYMDGVPMVTQCPILPGQTFRYKFKADP 80

                           90       100
                   ....*....|....*....|....*
gi 1098637342  440 TGTHFWHSHTGMQRGDGVFGALIVR 464
Cdd:cd13858     81 AGTHWYHSHSGTQRADGLFGALIVR 105
CuRO_3_tcLLC2_insect_like cd13905
The third cupredoxin domain of the insect laccases similar to laccase 2 in Tribolium castaneum; ...
 863-1030 5.42e-67

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: 222.56  E-value: 5.42e-67
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1098637342  863 QLNHISLKIPPMALMPERNNVDDSLFCNDTSLAqqgIDCRTDFCNCHHVLQVPLNSVVELIVVDEGFTFDANHPFHLHGN 942
Cdd:cd13905      1 SINGISFVFPSSPLLSQPEDLSDSSSCDFCNVP---SKCCTEPCECTHVIKLPLNSVVEIVLINEGPGPGLSHPFHLHGH 77

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1098637342  943 AFRVVGLERLGSNVTIEMV-------KQLDRYNLLKRNLDRPPIKDTVTIPDGGYTILRFEAYNPGFWLFHCHIEFHAEI 1015
Cdd:cd13905     78 SFYVLGMGFPGYNSTTGEIlsqnwnnKLLDRGGLPGRNLVNPPLKDTVVVPNGGYVVIRFRADNPGYWLLHCHIEFHLLE 157

                          170
                   ....*....|....*
gi 1098637342 1016 GMALIIKVGDNDQMK 1030
Cdd:cd13905    158 GMALVLKVGEPSDPP 172
ascorbase TIGR03388
L-ascorbate oxidase, plant type; Members of this protein family are the copper-containing ...
 360-1039 3.21e-56

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: 204.60  E-value: 3.21e-56
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1098637342  360 DGIERSVMVVNRMMPGPSIEVCEGDMIVVDVHNHLLGDSTTIHWHGMHQRNYPYMDGVPHISQCPISPHSTFRYRFRAEN 439
Cdd:TIGR03388   16 DCFEKLVIGINGQFPGPTIRAQAGDTIVVELTNKLHTEGVVIHWHGIRQIGTPWADGTAGVTQCAINPGETFIYNFVVDR 95

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1098637342  440 TGTHFWHSHTGMQRGDGVFGALIVRRPRAMEAHGHlYDfdlSEHKMILQDWVHTpgvsifSSHHHSRGDN--------KP 511
Cdd:TIGR03388   96 PGTYFYHGHYGMQRSAGLYGSLIVDVPDGEKEPFH-YD---GEFNLLLSDWWHK------SIHEQEVGLSskpmrwigEP 165

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1098637342  512 VNLLVNGRGRFYYAIwdqakkearTATVNKPNtqddkpvtpsptsttttttpttsttpltfvLNQSEVGGQYDLTPsqie 591
Cdd:TIGR03388  166 QSLLINGRGQFNCSL---------AAKFSSTN------------------------------LPQCNLKGNEQCAP---- 202

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1098637342  592 llqphndtsrnnmrlrnineisrlthvaqqppspsdrsdaepevefdltaqptnvqrtkravddiqlhqmplQIFHVRRG 671
Cdd:TIGR03388  203 ------------------------------------------------------------------------QILHVEPG 210

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1098637342  672 FRYRFRIINAEFLNCpIALSIDNHTLLAIHSDGYDFEPLEVGAMVTYAGERFDFVLNANQSIG-NYWIrfkglmdcsdqf 750
Cdd:TIGR03388  211 KTYRLRIASTTALAA-LNFAIEGHKLTVVEADGNYVEPFTVKDIDIYSGETYSVLLTTDQDPSrNYWI------------ 277

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1098637342  751 tsafqvgilryedasetePSGVLGwQHKADGIELNAMNRGSGHPDSLTAAEMTALPIYDTvpgvdrdalkpVADYKFFVY 830
Cdd:TIGR03388  278 ------------------SVGVRG-RKPNTPPGLTVLNYYPNSPSRLPPTPPPVTPAWDD-----------FDRSKAFSL 327

                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1098637342  831 YDFYAKDNPVfHPSDYYSFNDSLGKTNKL--YTP-QLNHISLKIPP----MALMPERNNVDDSLFCNDTSLAQQGIDCRT 903
Cdd:TIGR03388  328 AIKAAMGSPK-PPETSDRRIVLLNTQNKIngYTKwAINNVSLTLPHtpylGSLKYNLLNAFDQKPPPENYPRDYDIFKPP 406

                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1098637342  904 DFCNC---HHVLQVPLNSVVELIVVDEGfTFDAN----HPFHLHGNAFRVVGLERLGSNVTIEmVKQLdrynllkrNLDR 976
Cdd:TIGR03388  407 PNPNTttgNGIYRLKFNTTVDVILQNAN-TLNGNnsetHPWHLHGHDFWVLGYGEGKFRPGVD-EKSY--------NLKN 476

                          650       660       670       680       690       700
                   ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1098637342  977 PPIKDTVTIPDGGYTILRFEAYNPGFWLFHCHIEFHAEIGMALIIKVGdNDQMKSTPKNFPTC 1039
Cdd:TIGR03388  477 PPLRNTVVIFPYGWTALRFVADNPGVWAFHCHIEPHLHMGMGVVFAEG-VEKVGKLPKEALGC 538
CuRO_2_tcLCC_insect_like cd13884
The second cupredoxin domain of the insect laccases similar to laccase 2 in Tribolium ...
 482-761 6.81e-54

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: 184.74  E-value: 6.81e-54
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1098637342  482 EHKMILQDWVHTPGVSIFSSHHHSRGDNKPVNLLVNGRGRFYYaiwdqakkeartatvnkpntqddkpvtpsptsttttt 561
Cdd:cd13884      1 EHVILIQDWTHELSSERFVGRGHNGGGQPPDSILINGKGRYYD------------------------------------- 43

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1098637342  562 tpttsttpltfvlnqsevggqydltpsqiellqphndtsrnnmrlrnineisrlthvaqqppspsdrsdaepevefdlta 641
Cdd:cd13884        --------------------------------------------------------------------------------

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1098637342  642 qptnvqrtkraVDDIQLHQMPLQIFHVRRGFRYRFRIINAEFLNCPIALSIDNHTLLAIHSDGYDFEPLEVGAMVTYAGE 721
Cdd:cd13884     44 -----------PKTGNTNNTPLEVFTVEQGKRYRFRLINAGATNCPFRVSIDGHTLTVIASDGNDVEPVEVDSIIIYPGE 112

                          250       260       270       280
                   ....*....|....*....|....*....|....*....|
gi 1098637342  722 RFDFVLNANQSIGNYWIRFKGLMDCSdqFTSAFQVGILRY 761
Cdd:cd13884    113 RYDFVLNANQPIGNYWIRARGLEDCD--NRRLQQLAILRY 150
PLN02191 PLN02191
L-ascorbate oxidase
 360-1026 1.13e-50

L-ascorbate oxidase


Pssm-ID: 177843 [Multi-domain]  Cd Length: 574  Bit Score: 189.07  E-value: 1.13e-50
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1098637342  360 DGIERSVMVVNRMMPGPSIEVCEGDMIVVDVHNHLLGDSTTIHWHGMHQRNYPYMDGVPHISQCPISPHSTFRYRFRAEN 439
Cdd:PLN02191    38 DCKEGAVMTVNGQFPGPTIDAVAGDTIVVHLTNKLTTEGLVIHWHGIRQKGSPWADGAAGVTQCAINPGETFTYKFTVEK 117

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1098637342  440 TGTHFWHSHTGMQRGDGVFGALIVRRPRAmEAHGHLYDfdlSEHKMILQDWVH--TPGVSIFSSHHHSRGDNKPVNLLVN 517
Cdd:PLN02191   118 PGTHFYHGHYGMQRSAGLYGSLIVDVAKG-PKERLRYD---GEFNLLLSDWWHesIPSQELGLSSKPMRWIGEAQSILIN 193

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1098637342  518 GRGRFYYAIWDQAKKEArtatvnkpntqdDKPVtpsptsttttttpttsttpLTFvlnqsevggqydltpsqiellqPHN 597
Cdd:PLN02191   194 GRGQFNCSLAAQFSNGT------------ELPM-------------------CTF----------------------KEG 220

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1098637342  598 DtsrnnmrlrnineisrlthvaqqppspsdrsdaepevefdltaqptnvqrtkravddiqlhQMPLQIFHVRRGFRYRFR 677
Cdd:PLN02191   221 D-------------------------------------------------------------QCAPQTLRVEPNKTYRIR 239

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1098637342  678 IINAEFLnCPIALSIDNHTLLAIHSDGYDFEPLEVGAMVTYAGERFDFVLNANQSIG-NYWIRFkGLMDCSDQFTSAFQv 756
Cdd:PLN02191   240 LASTTAL-ASLNLAVQGHKLVVVEADGNYITPFTTDDIDIYSGESYSVLLTTDQDPSqNYYISV-GVRGRKPNTTQALT- 316

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1098637342  757 gILRYEDASETepsgvlgwqhkadgielnamnRGSGHPDSLTaaemtalPIYDTvpgVDRDalkpvadyKFFVYYDFYAK 836
Cdd:PLN02191   317 -ILNYVTAPAS---------------------KLPSSPPPVT-------PRWDD---FERS--------KNFSKKIFSAM 356

                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1098637342  837 DNPvfHPSDYYSFNDSLGKTNKLY-----------------TPQLNHI--------SLKIPPMALMPERNNVDDSLFCND 891
Cdd:PLN02191   357 GSP--SPPKKYRKRLILLNTQNLIdgytkwainnvslvtpaTPYLGSVkynlklgfNRKSPPRSYRMDYDIMNPPPFPNT 434

                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1098637342  892 TSlaQQGIdcrtdfcnchhvLQVPLNSVVELIV----VDEGFTFDAnHPFHLHGNAFRVVGlerLGSNvtiEMVKQLDRY 967
Cdd:PLN02191   435 TT--GNGI------------YVFPFNVTVDVIIqnanVLKGVVSEI-HPWHLHGHDFWVLG---YGDG---KFKPGIDEK 493

                          650       660       670       680       690
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 1098637342  968 NLlkrNLDRPPIKDTVTIPDGGYTILRFEAYNPGFWLFHCHIEFHAEIGMALIIKVGDN 1026
Cdd:PLN02191   494 TY---NLKNPPLRNTAILYPYGWTAIRFVTDNPGVWFFHCHIEPHLHMGMGVVFAEGLN 549
Cu-oxidase_3 pfam07732
Multicopper oxidase; This entry contains many divergent copper oxidase-like domains that are ...
 350-466 1.60e-47

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: 165.11  E-value: 1.60e-47
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1098637342  350 DCERPHCVLGDGIERSVMVVNRMMPGPSIEVCEGDMIVVDVHNHLlGDSTTIHWHGMHQRNYPYMDGVPHISQCPISPHS 429
Cdd:pfam07732    1 TVTYGTVSPLGGTRQAVIGVNGQFPGPTIRVREGDTVVVNVTNNL-DEPTSIHWHGLQQRGTPWMDGVPGVTQCPIPPGQ 79

                           90       100       110
                   ....*....|....*....|....*....|....*...
gi 1098637342  430 TFRYRFRAENT-GTHFWHSHTGMQRGDGVFGALIVRRP 466
Cdd:pfam07732   80 SFTYRFQVKQQaGTYWYHSHTSGQQAAGLAGAIIIEDR 117
laccase TIGR03389
laccase, plant; Members of this protein family include the copper-containing enzyme laccase ...
 364-1039 4.47e-47

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: 177.62  E-value: 4.47e-47
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1098637342  364 RSVMVVNRMMPGPSIEVCEGDMIVVDVHNHLlGDSTTIHWHGMHQRNYPYMDGVPHISQCPISPHSTFRYRFRAE-NTGT 442
Cdd:TIGR03389   22 KSILTVNGKFPGPTLYAREGDTVIVNVTNNV-QYNVTIHWHGVRQLRNGWADGPAYITQCPIQPGQSYVYNFTITgQRGT 100

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1098637342  443 HFWHSHTGMQRGDgVFGALIVRRPRameahGHLYDFDLSEHK--MILQDWvhtpgvsifsshhhsrgdnkpvnllvngrg 520
Cdd:TIGR03389  101 LWWHAHISWLRAT-VYGAIVILPKP-----GVPYPFPKPDREvpIILGEW------------------------------ 144

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1098637342  521 rfyyaiWdqakkeartatvnKPNTQDdkpvtpsptsttttttpttsttpltfVLNQS-EVGGqydltpsqiellqphndt 599
Cdd:TIGR03389  145 ------W-------------NADVEA--------------------------VINQAnQTGG------------------ 161

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1098637342  600 srnnmrlrnineisrlthvaqqPPSPSDRS--DAEPEVEFDLTAQPTNVqrtkravddiqlhqmplqiFHVRRGFRYRFR 677
Cdd:TIGR03389  162 ----------------------APNVSDAYtiNGHPGPLYNCSSKDTFK-------------------LTVEPGKTYLLR 200

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1098637342  678 IINAEfLNCPIALSIDNHTLLAIHSDGYDFEPLEVGAMVTYAGERFDFVLNANQSIGNYWIRFKGLMDCSDQFTSAFQVG 757
Cdd:TIGR03389  201 IINAA-LNDELFFAIANHTLTVVEVDATYTKPFKTKTIVIGPGQTTNVLLTADQSPGRYFMAARPYMDAPGAFDNTTTTA 279

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1098637342  758 ILRYedasetepsgvlgwqhkadgielnamnrgSGHPDSLtAAEMTALPIYDTVPGVDR--DALKPVADYKFFVYYDFYA 835
Cdd:TIGR03389  280 ILQY-----------------------------KGTSNSA-KPILPTLPAYNDTAAATNfsNKLRSLNSAQYPANVPVTI 329

                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1098637342  836 KDNPVFHPS---DYYSFNDSLGKTNKLYTPQLNHISLKIPPMALMPERNNVDDSLFCND------TSLAQQGIDCRTDFC 906
Cdd:TIGR03389  330 DRRLFFTIGlglDPCPNNTCQGPNGTRFAASMNNISFVMPTTALLQAHYFGISGVFTTDfpanppTKFNYTGTNLPNNLF 409

                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1098637342  907 NCH--HVLQVPLNSVVELIVVDEGFTFDANHPFHLHGNAFRVVGlERLGSnvtIEMVKQLDRYNLLKrnldrPPIKDTVT 984
Cdd:TIGR03389  410 TTNgtKVVRLKFNSTVELVLQDTSILGSENHPIHLHGYNFFVVG-TGFGN---FDPKKDPAKFNLVD-----PPERNTVG 480

                          650       660       670       680       690
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 1098637342  985 IPDGGYTILRFEAYNPGFWLFHCHIEFHAEIG--MALIIK--VGDNDQMKSTPKNFPTC 1039
Cdd:TIGR03389  481 VPTGGWAAIRFVADNPGVWFMHCHLEVHTTWGlkMAFLVDngKGPNQSLLPPPSDLPSC 539
CuRO_1_LCC_like cd04206
Cupredoxin domain 1 of laccase-like multicopper oxidases; including laccase, CueO, spore coat ...
 360-464 2.06e-46

Cupredoxin domain 1 of laccase-like multicopper oxidases; including laccase, CueO, spore coat protein A, ascorbate oxidase and similar proteins; Laccase-like multicopper oxidases (MCOs) in this family contain three cupredoxin domains. They are able to couple oxidation of substrates with reduction of dioxygen to water. MCOs are capable of oxidizing a vast range of substrates, varying from aromatic to inorganic compounds such as metals. Although the members of this family have diverse functions, majority of them have three cupredoxin domain repeats. The copper ions are bound in several sites; Type 1, Type 2, and/or Type 3. The ensemble of types 2 and 3 copper is called a trinuclear cluster. MCOs oxidize their substrate by accepting electrons at a mononuclear copper center and transferring them to the active site trinuclear copper center. The cupredoxin domain 1 of 3-domain MCOs contains part the trinuclear copper binding site, which is located at the interface of domains 1 and 3. Also included in this family are cupredoxin domains 1, 3, and 5 of the 6-domain MCO ceruloplasmin and similar proteins.


Pssm-ID: 259869 [Multi-domain]  Cd Length: 120  Bit Score: 162.07  E-value: 2.06e-46
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1098637342  360 DGIERSVMVVNRMMPGPSIEVCEGDMIVVDVHNHLLGDSTTIHWHGMHQRNYPYMDGVPHISQCPISPHSTFRYRFRAEN 439
Cdd:cd04206     15 DGVLRQVITVNGQFPGPTIRVKEGDTVEVTVTNNLPNEPTSIHWHGLRQPGTNDGDGVAGLTQCPIPPGESFTYRFTVDD 94

                           90       100
                   ....*....|....*....|....*.
gi 1098637342  440 T-GTHFWHSHTGMQRGDGVFGALIVR 464
Cdd:cd04206     95 QaGTFWYHSHVGGQRADGLYGPLIVE 120
CuRO_1_Diphenol_Ox cd13857
The first cupredoxin domain of fungal laccase, diphenol oxidase; Diphenol oxidase belongs to ...
 360-463 5.50e-43

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: 152.41  E-value: 5.50e-43
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1098637342  360 DGIERSVMVVNRMMPGPSIEVCEGDMIVVDVHNHLlGDSTTIHWHGMHQRNYPYMDGVPHISQCPISPHSTFRYRFRAEN 439
Cdd:cd13857     15 DGFVRPMLVINGQFPGPLIEANQGDRIVVHVTNEL-DEPTSIHWHGLFQNGTNWMDGTAGITQCPIPPGGSFTYNFTVDG 93

                           90       100
                   ....*....|....*....|....*
gi 1098637342  440 -TGTHFWHSHTGMQRGDGVFGALIV 463
Cdd:cd13857     94 qYGTYWYHSHYSTQYADGLVGPLIV 118
PLN02604 PLN02604
oxidoreductase
 360-1024 6.65e-43

oxidoreductase


Pssm-ID: 215324 [Multi-domain]  Cd Length: 566  Bit Score: 165.80  E-value: 6.65e-43
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1098637342  360 DGIERSVMVVNRMMPGPSIEVCEGDMIVVDVHNHLLGDSTTIHWHGMHQRNYPYMDGVPHISQCPISPHSTFRYRFRAEN 439
Cdd:PLN02604    39 DCFKKLVITINGRSPGPTILAQQGDTVIVELKNSLLTENVAIHWHGIRQIGTPWFDGTEGVTQCPILPGETFTYEFVVDR 118

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1098637342  440 TGTHFWHSHTGMQRGDGVFGALIVRRPRAmEAHGHLYDFDlseHKMILQDWVHTpgvsifSSHHHSRGDN--------KP 511
Cdd:PLN02604   119 PGTYLYHAHYGMQREAGLYGSIRVSLPRG-KSEPFSYDYD---RSIILTDWYHK------STYEQALGLSsipfdwvgEP 188

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1098637342  512 VNLLVNGRGRFyyaiwdqakkeaRTATVNKPNTQDDkpvtpsptsttttttpttsttpltfVLNQSevggqydltpsqie 591
Cdd:PLN02604   189 QSLLIQGKGRY------------NCSLVSSPYLKAG-------------------------VCNAT-------------- 217

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1098637342  592 llqphndtsrnnmrlrnineisrlthvaqqppspsdrsdaEPEVE-FDLTAQPtnvqrtkravddiqlhqmplqifhvrr 670
Cdd:PLN02604   218 ----------------------------------------NPECSpYVLTVVP--------------------------- 230

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1098637342  671 GFRYRFRIINAEFLNcpiALS--IDNHTLLAIHSDGYDFEPLEVGAMVTYAGERFDFVLNANQ-SIGNYWIRfkglmdcs 747
Cdd:PLN02604   231 GKTYRLRISSLTALS---ALSfqIEGHNMTVVEADGHYVEPFVVKNLFIYSGETYSVLVKADQdPSRNYWVT-------- 299

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1098637342  748 dqfTSAFQvgilryedASETEPSGvlgwqhkadgieLNAMNRGSGHPDSLTAAEMTALPIY-DTVPGVDRD-ALKPVADY 825
Cdd:PLN02604   300 ---TSVVS--------RNNTTPPG------------LAIFNYYPNHPRRSPPTVPPSGPLWnDVEPRLNQSlAIKARHGY 356

                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1098637342  826 KFfvyydfyakdnPVFHPSD-YYSFNDSLGKTNKLYTPQLNHISLKIPPMA-LMPERNNVDDSLfcnDTSLAQQGIDCR- 902
Cdd:PLN02604   357 IH-----------PPPLTSDrVIVLLNTQNEVNGYRRWSVNNVSFNLPHTPyLIALKENLTGAF---DQTPPPEGYDFAn 422

                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1098637342  903 ---------TDFCNCHHVLQVPLNSVVELIVVDEGfTFDAN----HPFHLHGNAFRVVGLERlgsnVTIEMVKQLDRYNL 969
Cdd:PLN02604   423 ydiyakpnnSNATSSDSIYRLQFNSTVDIILQNAN-TMNANnsetHPWHLHGHDFWVLGYGE----GKFNMSSDPKKYNL 497

                          650       660       670       680       690
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 1098637342  970 LKrnldrPPIKDTVTIPDGGYTILRFEAYNPGFWLFHCHIEFHAEIGMALIIKVG 1024
Cdd:PLN02604   498 VD-----PIMKNTVPVHPYGWTALRFRADNPGVWAFHCHIESHFFMGMGVVFEEG 547
CuRO_1_MaLCC_like cd13854
The first cupredoxin domain of the fungal laccases similar to Ma-LCC from Melanocarpus ...
 360-463 7.25e-42

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: 149.31  E-value: 7.25e-42
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1098637342  360 DGIERSVMVVNRMMPGPSIEVCEGDMIVVDVHNHLLGDSTTIHWHGMHQRNYPYMDGVPHISQCPISPHSTFRYRFRAEN 439
Cdd:cd13854     18 DGVEKEVMLINGQYPGPLIEANWGDTIEVTVINKLQDNGTSIHWHGIRQLNTNWQDGVPGVTECPIAPGDTRTYRFRATQ 97

                           90       100
                   ....*....|....*....|....
gi 1098637342  440 TGTHFWHSHTGMQRGDGVFGALIV 463
Cdd:cd13854     98 YGTSWYHSHYSAQYGDGVVGPIVI 121
CuRO_1_AAO cd13845
The first cupredoxin domain of plant Ascorbate oxidase; Ascorbate oxidase catalyzes the ...
 354-463 2.03e-36

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: 133.73  E-value: 2.03e-36
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1098637342  354 PHCVlgdgiERSVMVVNRMMPGPSIEVCEGDMIVVDVHNHLLGDSTTIHWHGMHQRNYPYMDGVPHISQCPISPHSTFRY 433
Cdd:cd13845     14 PDCV-----EKLVIGINGQFPGPTIRATAGDTIVVELENKLPTEGVAIHWHGIRQRGTPWADGTASVSQCPINPGETFTY 88

                           90       100       110
                   ....*....|....*....|....*....|
gi 1098637342  434 RFRAENTGTHFWHSHTGMQRGDGVFGALIV 463
Cdd:cd13845     89 QFVVDRPGTYFYHGHYGMQRSAGLYGSLIV 118
SufI COG2132
Multicopper oxidase with three cupredoxin domains (includes cell division protein FtsP and ...
 358-1025 5.29e-35

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: 139.30  E-value: 5.29e-35
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1098637342  358 LGDGIERSVMVVNRMMPGPSIEVCEGDMIVVDVHNHlLGDSTTIHWHGMHQRNypYMDGVPHIsqcPISPHSTFRYRFRA 437
Cdd:COG2132     27 LLPGKPTTVWGYNGQYPGPTIRVREGDRVRVRVTNR-LPEPTTVHWHGLRVPN--AMDGVPGD---PIAPGETFTYEFPV 100

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1098637342  438 ENT-GTHFWHSH----TGMQRGDGVFGALIVRRPramEAHGHLYDFDlseHKMILQDWVHTPGVSIFSSHHHSRGdnkpv 512
Cdd:COG2132    101 PQPaGTYWYHPHthgsTAEQVYRGLAGALIVEDP---EEDLPRYDRD---IPLVLQDWRLDDDGQLLYPMDAAMG----- 169

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1098637342  513 nllvngrGRFYYAIwdqakkeartaTVNkpntqddkpvtpsptsttttttpttsttpltfvlnqsevgGQYDLTpsqiel 592
Cdd:COG2132    170 -------GRLGDTL-----------LVN----------------------------------------GRPNPT------ 185

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1098637342  593 lqphndtsrnnmrlrnineisrlthvaqqppspsdrsdaepevefdltaqptnvqrtkravddiqlhqmplqiFHVRRGF 672
Cdd:COG2132    186 -------------------------------------------------------------------------LEVRPGE 192

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1098637342  673 RYRFRIINA---EFLNcpIALSiDNHTLLAIHSDGYDFE-PLEVGAMVTYAGERFDFVLNANQSIGNYWIrfkgLMDcSD 748
Cdd:COG2132    193 RVRLRLLNAsnaRIYR--LALS-DGRPFTVIATDGGLLPaPVEVDELLLAPGERADVLVDFSADPGEEVT----LAN-PF 264

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1098637342  749 QFTSAFQVGILRYEDASETEPSgvlgwqhkadgielnamnrgsghPDSLTaaemtalpiydTVPGVDRDALKPVADYKFF 828
Cdd:COG2132    265 EGRSGRALLTLRVTGAAASAPL-----------------------PANLA-----------PLPDLEDREAVRTRELVLT 310

                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1098637342  829 VYYDFYAkdnpvfhpsdyYSFNdslgktNKLYTPqlnhislkIPPMalmpernnvddslfcndtslaqqgidcrtdfcnc 908
Cdd:COG2132    311 GGMAGYV-----------WTIN------GKAFDP--------DRPD---------------------------------- 331

                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1098637342  909 hhvLQVPLNSVVELIVVDEGftfDANHPFHLHGNAFRVvgLERLGSNVtiemvkqldrynllkrnlDRPPIKDTVTIPDG 988
Cdd:COG2132    332 ---LTVKLGERERWTLVNDT---MMPHPFHLHGHQFQV--LSRNGKPP------------------PEGGWKDTVLVPPG 385

                          650       660       670
                   ....*....|....*....|....*....|....*....
gi 1098637342  989 G-YTIL-RFEAYnPGFWLFHCHIEFHAEIGMALIIKVGD 1025
Cdd:COG2132    386 EtVRILfRFDNY-PGDWMFHCHILEHEDAGMMGQFEVVP 423
CuRO_1_Abr2_like cd13850
The first cupredoxin domain of a group of fungal Laccases similar to Abr2 from Aspergillus ...
 359-464 1.71e-34

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: 127.80  E-value: 1.71e-34
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1098637342  359 GDGIERSVMVVNRMMPGPSIEVCEGDMIVVDVHNHLlGDSTTIHWHGMHQRNYPYMDGVPHISQCPISPHSTFRYRFRAE 438
Cdd:cd13850     12 GDGGEREVILINGQFPGPPIILDEGDEVEILVTNNL-PVNTTIHFHGILQRGTPWSDGVPGVTQWPIQPGGSFTYRWKAE 90

                           90       100
                   ....*....|....*....|....*..
gi 1098637342  439 N-TGTHFWHSHTGMQRGDGVFGALIVR 464
Cdd:cd13850     91 DqYGLYWYHSHYRGYYMDGLYGPIYIR 117
Cu-oxidase_2 pfam07731
Multicopper oxidase; This entry contains many divergent copper oxidase-like domains that are ...
 904-1027 9.18e-32

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: 121.00  E-value: 9.18e-32
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1098637342  904 DFCNCHHVLQVPLNSVVELIVVDEGFTfdaNHPFHLHGNAFRVVGleRLGSNVTIEMVKqldrynllKRNLDRPPIKDTV 983
Cdd:pfam07731   28 LFPPNTNVITLPYGTVVEWVLQNTTTG---VHPFHLHGHSFQVLG--RGGGPWPEEDPK--------TYNLVDPVRRDTV 94

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....
gi 1098637342  984 TIPDGGYTILRFEAYNPGFWLFHCHIEFHAEIGMALIIKVGDND 1027
Cdd:pfam07731   95 QVPPGGWVAIRFRADNPGVWLFHCHILWHLDQGMMGQFVVRPGD 138
CuRO_1_Fet3p cd13851
The first Cupredoxin domain of multicopper oxidase Fet3P; Fet3p catalyzes the ferroxidase ...
 360-463 2.19e-31

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: 119.29  E-value: 2.19e-31
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1098637342  360 DGI-ERSVMVVNRMMPGPSIEVCEGDMIVVDVHNHLLGDSTTIHWHGMHQRNYPYMDGVPHISQCPISPHSTFRYRFRA- 437
Cdd:cd13851     15 DGLfERRVIGINGQWPPPPIEVNKGDTVVIHATNSLGDQPTSLHFHGLFQNGTNYMDGPVGVTQCPIPPGQSFTYEFTVd 94

                           90       100
                   ....*....|....*....|....*.
gi 1098637342  438 ENTGTHFWHSHTGMQRGDGVFGALIV 463
Cdd:cd13851     95 TQVGTYWYHSHDGGQYPDGLRGPFII 120
CuRO_1_CopA cd13848
The first cupredoxin domain of CopA copper resistance protein family; CopA is a multicopper ...
 360-463 1.44e-29

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: 113.91  E-value: 1.44e-29
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1098637342  360 DGIERSVMVVNRMMPGPSIEVCEGDMIVVDVHNHLlGDSTTIHWHGMHqrnYPY-MDGVPHISQCPISPHSTFRYRFRAE 438
Cdd:cd13848     15 GGKEGEAITVNGQVPGPLLRFKEGDDATIRVHNRL-DEDTSIHWHGLL---LPNdMDGVPGLSFPGIKPGETFTYRFPVR 90

                           90       100
                   ....*....|....*....|....*
gi 1098637342  439 NTGTHFWHSHTGMQRGDGVFGALIV 463
Cdd:cd13848     91 QSGTYWYHSHSGLQEQTGLYGPIII 115
CuRO_1_Tv-LCC_like cd13856
The first cupredoxin domain of fungal laccases similar to Tv-LCC from Trametes versicolor; ...
 360-463 1.54e-29

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: 113.97  E-value: 1.54e-29
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1098637342  360 DGIERSVMVVNRMMPGPSIEVCEGDMIVVDVHNHLLGD----STTIHWHGMHQRNYPYMDGVPHISQCPISPHSTFRYRF 435
Cdd:cd13856     15 DGFERSAVLANGQFPGPLITANKGDTFRITVVNQLTDPtmrrSTSIHWHGIFQHGTNYADGPAFVTQCPIAPNHSFTYDF 94

                           90       100
                   ....*....|....*....|....*....
gi 1098637342  436 RAEN-TGTHFWHSHTGMQRGDGVFGALIV 463
Cdd:cd13856     95 TAGDqAGTFWYHSHLSTQYCDGLRGPLVI 123
CuRO_1_CumA_like cd13861
The first cupredoxin domain of CumA like multicopper oxidase; This multicopper oxidase (MCO) ...
 359-464 6.64e-28

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: 109.25  E-value: 6.64e-28
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1098637342  359 GDGIERSVMVVNRMMPGPSIEVCEGDMIVVDVHNHLlGDSTTIHWHGMHQRNYpyMDGVPHISQCPISPHSTFRYRFRAE 438
Cdd:cd13861     15 LGGPTTRTWGYNGQVPGPELRVRQGDTLRVRLTNRL-PEPTTIHWHGLRLPNA--MDGVPGLTQPPVPPGESFTYEFTPP 91

                           90       100
                   ....*....|....*....|....*...
gi 1098637342  439 NTGTHFWHSHTGM--QRGDGVFGALIVR 464
Cdd:cd13861     92 DAGTYWYHPHVGSqeQLDRGLYGPLIVE 119
CuRO_3_LCC_like cd04207
Cupredoxin domain 3 of laccase-like multicopper oxidases; including laccase, CueO, spore coat ...
 903-1021 1.73e-27

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: 108.32  E-value: 1.73e-27
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1098637342  903 TDFCNCHHVLQVPLNSVVELIVVDEGfTFDANHPFHLHGNAFRVVGLERLGSNVTIemvkqldrynllkrNLDRPPIKDT 982
Cdd:cd04207     28 KEGDANTDIFSVEAGDVVEIVLINAG-NHDMQHPFHLHGHSFWVLGSGGGPFDAPL--------------NLTNPPWRDT 92

                           90       100       110
                   ....*....|....*....|....*....|....*....
gi 1098637342  983 VTIPDGGYTILRFEAYNPGFWLFHCHIEFHAEIGMALII 1021
Cdd:cd04207     93 VLVPPGGWVVIRFKADNPGVWMLHCHILEHEDAGMMTVF 131
CuRO_1_2dMco_1 cd13860
The first cupredoxin domain of bacteria two domain multicopper oxidase; This subfamily ...
 370-464 6.23e-27

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: 106.51  E-value: 6.23e-27
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1098637342  370 NRMMPGPSIEVCEGDMIVVDVHNHLlGDSTTIHWHGMHQRNYpyMDGVPHISQCPISPHSTFRYRFRAENTGTHFWHSHT 449
Cdd:cd13860     26 NGSVPGPTIEVTEGDRVRILVTNEL-PEPTTVHWHGLPVPNG--MDGVPGITQPPIQPGETFTYEFTAKQAGTYMYHSHV 102

                           90
                   ....*....|....*..
gi 1098637342  450 GMQRGD--GVFGALIVR 464
Cdd:cd13860    103 DEAKQEdmGLYGAFIVH 119
CuRO_1_LCC_plant cd13849
The first cupredoxin domain of plant laccases; Laccase is a blue multicopper oxidase (MCO) ...
 363-464 7.09e-27

The first cupredoxin domain of plant laccases; Laccase is a blue multicopper oxidase (MCO) which catalyzes the oxidation of a variety aromatic - notably phenolic and inorganic substances coupled to the reduction of molecular oxygen to water. Laccase has been implicated in a wide spectrum of biological activities and, in particular, plays a key role in morphogenesis, development and lignin metabolism. Plants usually express multiple laccase genes, but their precise physiological/biochemical roles remain largely unclear. MCOs are capable of oxidizing a vast range of substrates, varying from aromatic compounds to inorganic compounds such as metals. Although the members of this family have diverse functions, majority of them have three cupredoxin domain repeats. The copper ions are bound in several sites: Type 1, Type 2, and/or Type 3. The ensemble of types 2 and 3 copper is called a trinuclear cluster. MCOs oxidize their substrate by accepting electrons at a mononuclear copper center and transferring them to the active site trinuclear copper center. The cupredoxin domain 1 of 3-domain MCOs contains part the trinuclear copper binding site, which is located at the interface of domains 1 and 3.


Pssm-ID: 259918 [Multi-domain]  Cd Length: 117  Bit Score: 106.19  E-value: 7.09e-27
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1098637342  363 ERSVMVVNRMMPGPSIEVCEGDMIVVDVHNHLLGDsTTIHWHGMHQRNYPYMDGVPHISQCPISPHSTFRYRFR-AENTG 441
Cdd:cd13849     16 TKSILTVNGQFPGPTIRVHEGDTVVVNVTNRSPYN-ITIHWHGIRQLRSGWADGPAYITQCPIQPGQSYTYRFTvTGQEG 94

                           90       100
                   ....*....|....*....|...
gi 1098637342  442 THFWHSHTGMQRGDgVFGALIVR 464
Cdd:cd13849     95 TLWWHAHISWLRAT-VYGAFIIR 116
CuRO_2_Tv-LCC_like cd13882
The second cupredoxin domain of the fungal laccases similar to Tv-LCC from Trametes versicolor; ...
 660-769 4.57e-26

The second cupredoxin domain of the fungal laccases similar to Tv-LCC from Trametes versicolor; This subfamily of fungal laccases includes Tv-LCC from Trametes versicolor and Rs-LCC2 from plant pathogenic fungus Rhizoctonia solani. Laccase is a blue multi-copper enzyme that catalyzes the oxidation of a variety aromatic - notably phenolic and inorganic substances coupled to the reduction of molecular oxygen to water. It has been implicated in a wide spectrum of biological activities and, in particular, plays a key role in morphogenesis, development and lignin metabolism. Laccase is a multicopper oxidase (MCO) composed of three cupredoxin domains that include one mononuclear and one trinuclear copper center. The copper ions are bound in several sites: Type 1, Type 2, and/or Type 3. The ensemble of types 2 and 3 copper is called a trinuclear cluster. MCOs oxidize their substrate by accepting electrons at a mononuclear copper center and transferring them to the active site trinuclear copper center. The cupredoxin domain 2 of 3-domain MCOs has lost the ability to bind copper.


Pssm-ID: 259949 [Multi-domain]  Cd Length: 159  Bit Score: 105.57  E-value: 4.57e-26
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1098637342  660 QMPLQIFHVRRGFRYRFRIINAEFLNCpIALSIDNHTLLAIHSDGYDFEPLEVGAMVTYAGERFDFVLNANQSIGNYWIR 739
Cdd:cd13882     43 TSPLAVINVKRGKRYRFRVINISCIPS-FTFSIDGHNLTVIEADGVETKPLTVDSVQIYAGQRYSVVVEANQPVDNYWIR 121

                           90       100       110
                   ....*....|....*....|....*....|....*....
gi 1098637342  740 ---------FKGlmdcsDQFTSAfqvgILRYEDASETEP 769
Cdd:cd13882    122 apptggtpaNNG-----GQLNRA----ILRYKGAPEVEP 151
CuRO_D1_2dMcoN_like cd13859
The first cupredoxin domain of bacterial two domain multicopper oxidase McoN and similar ...
 357-463 6.46e-26

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: 103.71  E-value: 6.46e-26
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1098637342  357 VLGDGIERSVMVVNRMMPGPSIEVCEGDMIVVDVHNhllgDST---TIHWHGMHQRNYPYMDGVPHISQCPISPHSTFRY 433
Cdd:cd13859     13 TVVPGLDFKTFAFNGQVPGPLIHVKEGDDLVVHVTN----NTTlphTIHWHGVLQMGSWKMDGVPGVTQPAIEPGESFTY 88

                           90       100       110
                   ....*....|....*....|....*....|....*.
gi 1098637342  434 RFRAENTGTHFWH------SHTGMQrgdGVFGALIV 463
Cdd:cd13859     89 KFKAERPGTLWYHchvnvnEHVGMR---GMWGPLIV 121
ascorbOXfungal TIGR03390
L-ascorbate oxidase, fungal type; This model describes a family of fungal ascorbate oxidases, ...
 363-1030 2.60e-25

L-ascorbate oxidase, fungal type; This model describes a family of fungal ascorbate oxidases, within a larger family of multicopper oxidases that also includes plant ascorbate oxidases (TIGR03388), plant laccases and laccase-like proteins (TIGR03389), and related proteins. The member from Acremonium sp. HI-25 is characterized.


Pssm-ID: 132431 [Multi-domain]  Cd Length: 538  Bit Score: 111.86  E-value: 2.60e-25
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1098637342  363 ERSVMVVNRMMPGPSIEVCEGDMIVVDVHNHLLGDSTTIHWHGMHQRNYPYMDGVPHISQCPISPHSTFRYRFRAE--NT 440
Cdd:TIGR03390   26 SRYSVVVNGTSPGPEIRLQEGQTTWIRVYNDIPDNNVTMHWHGLTQRTAPFSDGTPLASQWPIPPGHFFDYEIKPEpgDA 105

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1098637342  441 GTHFWHSHTGMQrGDGVFGALIVRRPRAMEahghlYDFDlSEHKMILQDwvhtpgvsifsshHHSRGDNKPVNLLVngrg 520
Cdd:TIGR03390  106 GSYFYHSHVGFQ-AVTAFGPLIVEDCEPPP-----YKYD-DERILLVSD-------------FFSATDEEIEQGLL---- 161

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1098637342  521 rfyyAIWDQAKKEARTATVNkpntqddkpvtpsptsttttttpttsttpltfvlnqsevgGQydltpsqiellqphndtS 600
Cdd:TIGR03390  162 ----STPFTWSGETEAVLLN----------------------------------------GK-----------------S 180

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1098637342  601 RNnmrlrnineisrLTHVAQQPPSPSDRsdaepevefdltaqptnvqrtkravddiqlhqmpLQIFHVRRGFRYRFRIIN 680
Cdd:TIGR03390  181 GN------------KSFYAQINPSGSCM----------------------------------LPVIDVEPGKTYRLRFIG 214

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1098637342  681 AEFLNCpIALSIDNHTLLA-IHSDGYDFEPLEVGAMVTYAGERFDFVLNANQSIG-------NYWIRFKGLmDCSDQFTS 752
Cdd:TIGR03390  215 ATALSL-ISLGIEDHENLTiIEADGSYTKPAKIDHLQLGGGQRYSVLFKAKTEDElcggdkrQYFIQFETR-DRPKVYRG 292

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1098637342  753 afqVGILRYedasetepsgvlgwqhkadgielnamnRGSGHPDSLTAAEMTALPIYDTVPGVDRDALKPVADykffvyyd 832
Cdd:TIGR03390  293 ---YAVLRY---------------------------RSDKASKLPSVPETPPLPLPNSTYDWLEYELEPLSE-------- 334

                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1098637342  833 fyaKDNPVFHPSDYYS------FNDSLGKTNKLYTPQLNHISL-----KIPPMALMPER-NNVDDSLfcnDTSLAQQGID 900
Cdd:TIGR03390  335 ---ENNQDFPTLDEVTrrvvidAHQNVDPLNGRVAWLQNGLSWtesvrQTPYLVDIYENgLPATPNY---TAALANYGFD 408

                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1098637342  901 CRTdfcnchHVLQVPLNSVVELIVVDEGFTFDAN-----HPFHLHGNAFRVVGLERLGSNVTiEMVKQLDRYNLLKR--- 972
Cdd:TIGR03390  409 PET------RAFPAKVGEVLEIVWQNTGSYTGPNggvdtHPFHAHGRHFYDIGGGDGEYNAT-ANEAKLENYTPVLRdtt 481

                          650       660       670       680       690
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 1098637342  973 NLDRPPIKDTVTIPdGGYTILRFEAYNPGFWLFHCHIEFHAEIGMALIIKVGDNDQMK 1030
Cdd:TIGR03390  482 MLYRYAVKVVPGAP-AGWRAWRIRVTNPGVWMMHCHILQHMVMGMQTVWVFGDAEDIV 538
CuRO_3_MCO_like_4 cd13910
The third cupredoxin domain of uncharacterized multicopper oxidase; Multicopper Oxidases (MCOs) ...
 911-1019 3.60e-25

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: 103.14  E-value: 3.60e-25
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1098637342  911 VLQVP-LNSVVELIV--VDEGftfdaNHPFHLHGNAFRVVGLERLGSNVTIEmvkQLDRYNLLkrNLDRPPIKDTVTIPD 987
Cdd:cd13910     61 VITVDdIDKVVDLVInnLDDG-----DHPFHLHGHKFWVLGSGDGRYGGGGY---TAPDGTSL--NTTNPLRRDTVSVPG 130

                           90       100       110
                   ....*....|....*....|....*....|..
gi 1098637342  988 GGYTILRFEAYNPGFWLFHCHIEFHAEIGMAL 1019
Cdd:cd13910    131 FGWAVLRFVADNPGLWAFHCHILWHMAAGMLM 162
CuRO_1_AAO_like_2 cd13847
The first cupredoxin domain of Ascorbate oxidase homologs; This family includes fungal ...
 364-463 1.72e-24

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: 99.53  E-value: 1.72e-24
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1098637342  364 RSVMVVNRMMPGPSIEVCEGDMIVVDVHNHLLGDSTTIHWHGMHQRNYPYMDGVPHISQCPISPHSTFRYRFR--AENTG 441
Cdd:cd13847     15 RPSTLINGSFPGPELRVQEGQHLWVRVYNDLEAGNTTMHFHGLSQYMSPFSDGTPLASQWPIPPGKFFDYEFPleAGDAG 94

                           90       100
                   ....*....|....*....|..
gi 1098637342  442 THFWHSHTGMQRGDGvFGALIV 463
Cdd:cd13847     95 TYYYHSHVGFQSVTA-YGALIV 115
CuRO_3_Fet3p cd13899
The third Cupredoxin domain of multicopper oxidase Fet3p; Fet3p catalyzes the ferroxidase ...
 914-1021 7.61e-24

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: 98.87  E-value: 7.61e-24
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1098637342  914 VPLNSVVELIVvdegFTFDA-NHPFHLHGNAFRVVGLERLGSNVtiemvkqlDRYNLLKRNLDRPPIKDTVTIPDGGYTI 992
Cdd:cd13899     60 LNHGEVVELVV----NNWDAgKHPFHLHGHKFQVVQRSPDVASD--------DPNPPINEFPENPMRRDTVMVPPGGSVV 127

                           90       100
                   ....*....|....*....|....*....
gi 1098637342  993 LRFEAYNPGFWLFHCHIEFHAEIGMALII 1021
Cdd:cd13899    128 IRFRADNPGVWFFHCHIEWHLEAGLAATF 156
CuRO_3_Tv-LCC_like cd13903
The third cupredoxin domain of the fungal laccases similar to Tv-LCC from Trametes Versicolor; ...
 903-1021 2.35e-23

The third cupredoxin domain of the fungal laccases similar to Tv-LCC from Trametes Versicolor; This subfamily of fungal laccases includes Tv-LCC from Trametes versicolor and Rs-LCC2 from plant pathogenic fungus Rhizoctonia solani. Laccase is a blue multi-copper enzyme that catalyzes the oxidation of a variety aromatic - notably phenolic and inorganic substances coupled to the reduction of molecular oxygen to water. It has been implicated in a wide spectrum of biological activities and, in particular, plays a key role in morphogenesis, development and lignin metabolism. Although MCOs have diverse functions, majority of them have three cupredoxin domain repeats that include one mononuclear and one trinuclear copper center. The copper ions are bound in several sites: Type 1, Type 2, and/or Type 3. The ensemble of types 2 and 3 copper is called a trinuclear cluster. MCOs oxidize their substrate by accepting electrons at a mononuclear copper center and transferring them to the active site trinuclear copper center. The cupredoxin domain 3 of 3-domain MCOs contains the Type 1 (T1) copper binding site and part the trinuclear copper binding site, which is located at the interface of domains 1 and 3.


Pssm-ID: 259970 [Multi-domain]  Cd Length: 147  Bit Score: 97.35  E-value: 2.35e-23
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1098637342  903 TDFCNCHHVLQVPLNSVVELIVvdEGFTFDANHPFHLHGNAFRVVglERLGSNVTiemvkqldrynllkrNLDRPPIKDT 982
Cdd:cd13903     43 EDLLPTESTIILPRNKVVEITI--PGGAIGGPHPFHLHGHAFSVV--RSAGSNTY---------------NYVNPVRRDV 103

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|
gi 1098637342  983 VTI-PDGGYTILRFEAYNPGFWLFHCHIEFHAEIGMALII 1021
Cdd:cd13903    104 VSVgTPGDGVTIRFVTDNPGPWFLHCHIDWHLEAGLAVVF 143
CuRO_3_LCC_plant cd13897
The third cupredoxin domain of the plant laccases; Laccase is a blue multicopper oxidase (MCO) ...
 911-1024 7.42e-23

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: 95.40  E-value: 7.42e-23
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1098637342  911 VLQVPLNSVVELIVVDEGFTFDANHPFHLHGNAFRVVGlERLGsnvTIEMVKQLDRYNLLKrnldrPPIKDTVTIPDGGY 990
Cdd:cd13897     33 VKVLEYGSTVEIVLQGTSLLAAENHPMHLHGFDFYVVG-RGFG---NFDPSTDPATFNLVD-----PPLRNTVGVPRGGW 103

                           90       100       110
                   ....*....|....*....|....*....|....*.
gi 1098637342  991 TILRFEAYNPGFWLFHCHIEFHAEIGM--ALIIKVG 1024
Cdd:cd13897    104 AAIRFVADNPGVWFMHCHFERHTSWGMatVFIVKNG 139
CuRO_2_LCC_like cd04205
Cupredoxin domain 2 of laccase-like multicopper oxidases; including laccase, CueO, spore coat ...
 662-761 6.34e-21

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: 90.50  E-value: 6.34e-21
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1098637342  662 PLQIFHVRRGFRYRFRIINAEfLNCPIALSIDNHTLLAIHSDGYDFEPLEVGAMVTYAGERFDFVLNANQSIGNYWIRFK 741
Cdd:cd04205     54 PLPVITVEPGKTYRLRLINAG-SFASFNFAIDGHNMTVIEVDGGYVEPLEVDNLDLAPGQRYDVLVKADQPPGNYWIRAS 132

                           90       100
                   ....*....|....*....|
gi 1098637342  742 GLMDCSDQFTSAFQVGILRY 761
Cdd:cd04205    133 ADGRTFDEGGNPNGTAILRY 152
CuRO_1_LCC_like_3 cd13865
The second cupredoxin domain of uncharacterized multicopper oxidase; Multicopper Oxidases ...
 360-465 1.70e-20

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: 87.75  E-value: 1.70e-20
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1098637342  360 DGIERSVMVVNRMMPGPSIEVCEGDMIVVDVHNHLlGDSTTIHWHGMhqrNYPY-MDGVPHISQCPISPHSTFRYRFRAE 438
Cdd:cd13865     13 NGKAATVYGIRQPDGTEGLRLTEGDRFDVELENRL-DEPTTIHWHGL---IPPNlQDGVPDVTQPPIPPGQSQRYDFPLV 88

                           90       100
                   ....*....|....*....|....*..
gi 1098637342  439 NTGTHFWHSHTGMQRGDGVFGALIVRR 465
Cdd:cd13865     89 QPGTFWMHSHYGLQEQKLLAAPLIIRS 115
CuRO_1_AAO_like_1 cd13846
The first cupredoxin domain of plant Ascorbate oxidase homologs; This subfamily is composed of ...
 361-463 2.11e-20

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: 87.85  E-value: 2.11e-20
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1098637342  361 GIERSVMVVNRMMPGPSIEVCEGDMIVVDVHNHlLGDSTTIHWHGMHQRNYPYMDGVPHiSQCPISPHSTFRYRFRAENT 440
Cdd:cd13846     16 GVPQQVIAINGQFPGPTINVTTNDNVVVNVFNS-LDEPLLLTWNGIQQRRNSWQDGVLG-TNCPIPPGWNWTYKFQVKDQ 93

                           90       100
                   ....*....|....*....|....
gi 1098637342  441 -GTHFWHSHTGMQRGDGVFGALIV 463
Cdd:cd13846     94 iGSFFYFPSLHFQRAAGGFGGIRV 117
CuRO_3_AAO cd13893
The third cupredoxin domain of plant Ascorbate oxidase; Ascorbate oxidase catalyzes the ...
 917-1024 2.36e-19

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: 85.93  E-value: 2.36e-19
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1098637342  917 NSVVELIVVDEGF---TFDANHPFHLHGNAFRVVGLErLGSNVTIEMVKQLdrynllkrNLDRPPIKDTVTIPDGGYTIL 993
Cdd:cd13893     46 GDVVDVILQNANTntrNASEQHPWHLHGHDFWVLGYG-LGGFDPAADPSSL--------NLVNPPMRNTVTIFPYGWTAL 116

                           90       100       110
                   ....*....|....*....|....*....|.
gi 1098637342  994 RFEAYNPGFWLFHCHIEFHAEIGMALIIKVG 1024
Cdd:cd13893    117 RFKADNPGVWAFHCHIEWHFHMGMGVVFAEG 147
Cu-oxidase pfam00394
Multicopper oxidase; Many of the proteins in this family contain multiple similar copies of ...
 662-762 2.10e-18

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: 83.14  E-value: 2.10e-18
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1098637342  662 PLQIFHVRRGFRYRFRIINA---EFLNcpiaLSIDNHTLLAIHSDGYDFEPLEVGAMVTYAGERFDFVLNANQSIGNYWI 738
Cdd:pfam00394   48 SLATLTVTPGKTYRLRIINValdDSLN----FSIEGHKMTVVEVDGVYVNPFTVDSLDIFPGQRYSVLVTANQDPGNYWI 123

                           90       100
                   ....*....|....*....|....
gi 1098637342  739 RFKglMDCSDQFTSAfQVGILRYE 762
Cdd:pfam00394  124 VAS--PNIPAFDNGT-AAAILRYS 144
CuRO_3_MaLCC_like cd13901
The third cupredoxin domain of the fungal laccases similar to Ma-LCC from Melanocarpus ...
 910-1019 3.90e-18

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: 82.66  E-value: 3.90e-18
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1098637342  910 HVLQVP-LNSVVELIVVDegfTFDANHPFHLHGNAFRVVGLerlGSNVTIEMVKQLdrynllkrNLDRPPIKDTVTIPDG 988
Cdd:cd13901     58 NVIELPkANKWVYIVIQN---NSPLPHPIHLHGHDFYILAQ---GTGTFDDDGTIL--------NLNNPPRRDVAMLPAG 123

                           90       100       110
                   ....*....|....*....|....*....|.
gi 1098637342  989 GYTILRFEAYNPGFWLFHCHIEFHAEIGMAL 1019
Cdd:cd13901    124 GYLVIAFKTDNPGAWLMHCHIAWHASGGLAL 154
CuRO_3_Diphenol_Ox cd13904
The third cupredoxin domain of fungal laccase, diphenol oxidase; Diphenol oxidase belongs to ...
 934-1021 3.16e-17

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: 80.03  E-value: 3.16e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1098637342  934 NHPFHLHGNAFRVVGLerlGSNvtiemvkQLDRYNL--LKRNLDRPPIKDTVTIPDGGYTILRFEAYNPGFWLFHCHIEF 1011
Cdd:cd13904     77 DHPYHLHGVDFHIVAR---GSG-------TLTLEQLanVQYNTTNPLRRDTIVIPGGSWAVLRIPADNPGVWALHCHIGW 146

                           90
                   ....*....|.
gi 1098637342 1012 HAEIG-MALII 1021
Cdd:cd13904    147 HLAAGfAGVVV 157
PLN02354 PLN02354
copper ion binding / oxidoreductase
 361-520 7.33e-17

copper ion binding / oxidoreductase


Pssm-ID: 177987 [Multi-domain]  Cd Length: 552  Bit Score: 85.23  E-value: 7.33e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1098637342  361 GIERSVMVVNRMMPGPSIEVCEGDMIVVDVHNHlLGDSTTIHWHGMHQRNYPYMDGVPHiSQCPISPHSTFRYRFRAENT 440
Cdd:PLN02354    43 GVPQQVILINGQFPGPNINSTSNNNIVINVFNN-LDEPFLLTWSGIQQRKNSWQDGVPG-TNCPIPPGTNFTYHFQPKDQ 120

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1098637342  441 -GTHFWHSHTGMQRGDGVFGALIVrrprameaHGHL-----YDFDLSEHKMILQDWVHTPGVSIFSSHHHSRGDNKPVNL 514
Cdd:PLN02354   121 iGSYFYYPSTGMHRAAGGFGGLRV--------NSRLlipvpYADPEDDYTVLIGDWYTKSHTALKKFLDSGRTLGRPDGV 192


                   ....*.
gi 1098637342  515 LVNGRG 520
Cdd:PLN02354   193 LINGKS 198
CuRO_3_Abr2_like cd13898
The third cupredoxin domain of a group of fungal Laccases similar to Abr2 from Aspergillus ...
 911-1021 3.27e-16

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: 77.30  E-value: 3.27e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1098637342  911 VLQVPLNSVVELIVVDEGFtFDANHPFHLHGNAFRVVGLerlGSNV-TIEMVKQLDRYNLLKRNLDRPPIKDTVTIP--- 986
Cdd:cd13898     50 TISTKNGTWVDLIFQVTGP-PQPPHPIHKHGNKAFVIGT---GTGPfNWSSVAEAAEAAPENFNLVNPPLRDTFTTPpst 125

                           90       100       110
                   ....*....|....*....|....*....|....*.
gi 1098637342  987 -DGGYTILRFEAYNPGFWLFHCHIEFHAEIGMALII 1021
Cdd:cd13898    126 eGPSWLVIRYHVVNPGAWLLHCHIQSHLAGGMAVVL 161
CuRO_2_MaLCC_like cd13880
The second cupredoxin domain of the fungal laccases similar to Ma-LCC from Melanocarpus ...
 666-770 1.01e-14

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: 73.05  E-value: 1.01e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1098637342  666 FHVRRGFRYRFRIINAEFLNcPIALSIDNHTLLAIhsdGYDF---EPLEVGAMVTYAGERFDFVLNANQS-IGNYWIRFK 741
Cdd:cd13880     53 TTFTPGKKYRLRLINTGVDT-TFRFSIDGHNLTVI---AADFvpiVPYTTDSLNIGIGQRYDVIVEANQDpVGNYWIRAE 128

                           90       100       110
                   ....*....|....*....|....*....|
gi 1098637342  742 GLMDCSDQ-FTSAFQVGILRYEDASETEPS 770
Cdd:cd13880    129 PATGCSGTnNNPDNRTGILRYDGASPTLDP 158
PLN02168 PLN02168
copper ion binding / pectinesterase
 361-520 2.52e-14

copper ion binding / pectinesterase


Pssm-ID: 215113 [Multi-domain]  Cd Length: 545  Bit Score: 77.32  E-value: 2.52e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1098637342  361 GIERSVMVVNRMMPGPSIEVCEGDMIVVDVHNHlLGDSTTIHWHGMHQRNYPYMDGVPHiSQCPISPHSTFRYRFRAENT 440
Cdd:PLN02168    42 GGNKQVIVINDMFPGPLLNATANDVINVNIFNN-LTEPFLMTWNGLQLRKNSWQDGVRG-TNCPILPGTNWTYRFQVKDQ 119

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1098637342  441 -GTHFWHSHTGMQRGDGVFGALIVRRPRAM-----EAHGhlydfdlsEHKMILQDWVHTPGVSIFSSHHHSRGDNKPVNL 514
Cdd:PLN02168   120 iGSYFYFPSLLLQKAAGGYGAIRIYNPELVpvpfpKPDE--------EYDILIGDWFYADHTVMRASLDNGHSLPNPDGI 191


                   ....*.
gi 1098637342  515 LVNGRG 520
Cdd:PLN02168   192 LFNGRG 197
CuRO_2_MCO_like_1 cd13886
The second cupredoxin domain of uncharacterized multicopper oxidase; Multicopper Oxidases ...
 666-762 1.36e-13

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: 69.61  E-value: 1.36e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1098637342  666 FHVRRGFRYRFRIINAEFLnCPIALSIDNHTLLAIHSDGYDFEPLEVGAMVTYAGERFDFVLNANQS-IGNYWIRFKGLM 744
Cdd:cd13886     64 FTLEPNKTYRLRLINAGSF-ADFTFSVDGHPLTVIEADGTLVEPVEVHSITISVAQRYSVILTTNQPtGGNFWMRAELNT 142

                           90       100
                   ....*....|....*....|..
gi 1098637342  745 DC----SDQFtSAFQVGILRYE 762
Cdd:cd13886    143 DCftydNPNL-DPDVRAIVSYT 163
CuRO_1_McoC_like cd13855
The first cupredoxin domain of a multicopper oxidase McoC and similar proteins; This family ...
 358-464 1.42e-13

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: 68.27  E-value: 1.42e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1098637342  358 LGDGIERSVMVVNRMMPGPSIEVCEGDMIVVDVHNHlLGDSTTIHWHGMHQRnyPYMDGVPHIsqcPISPHSTFRYRFR- 436
Cdd:cd13855     15 LLPGKPTEFWAYNGSVPGPLIEVFEGDTVEITFRNR-LPEPTTVHWHGLPVP--PDQDGNPHD---PVAPGNDRVYRFTl 88

                           90       100       110
                   ....*....|....*....|....*....|...
gi 1098637342  437 -AENTGTHFWHSH----TGMQRGDGVFGALIVR 464
Cdd:cd13855     89 pQDSAGTYWYHPHphghTAEQVYRGLAGAFVVK 121
CuRO_3_CopA cd13896
The third cupredoxin domain of CopA copper resistance protein family; CopA is a multicopper ...
 934-1023 1.61e-13

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: 68.05  E-value: 1.61e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1098637342  934 NHPFHLHGNAFRVVGLerlgsnvtiemvkqldrynllkrNLDRPPIKDTVTIPDGGYTILRFEAYNPGFWLFHCHIEFHA 1013
Cdd:cd13896     49 AHPMHLHGHFFQVENG-----------------------NGEYGPRKDTVLVPPGETVSVDFDADNPGRWAFHCHNLYHM 105

                           90
                   ....*....|
gi 1098637342 1014 EIGMALIIKV 1023
Cdd:cd13896    106 EAGMMRVVEY 115
CuRO_1_MCO_like_2 cd13864
The second cupredoxin domain of uncharacterized multicopper oxidase; Multicopper Oxidases ...
 375-463 2.19e-13

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: 68.33  E-value: 2.19e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1098637342  375 GPSIEVCEGDMIVVDVHNHLLGD-----------STTIHWHGMHQRNYPYM-----DGVPHISQCPISPHSTFRYRFR-A 437
Cdd:cd13864     31 GPTIRVKSGDTLNLLVTNHLCNEqelskiwqdycPTSIHFHGLVLENFGKQlanlvDGVPGLTQYPIGVGESYWYNFTiP 110

                           90       100
                   ....*....|....*....|....*..
gi 1098637342  438 ENT-GTHFWHSHTGMQRGDGVFGALIV 463
Cdd:cd13864    111 EDTcGTFWYHSHSSVQYGDGLRGVFIV 137
CuRO_1_2DMCO_NIR_like cd11024
The cupredoxin domain 1 of a two-domain laccase related to nitrite reductase; The two-domain ...
 370-463 3.47e-13

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: 67.30  E-value: 3.47e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1098637342  370 NRMMPGPSIEVCEGDMIVVDVHNhLLGDSTTIHWHGMHqrnYPYMDGvphISQCPISPHSTFRYRFRAENTGTHFWHSH- 448
Cdd:cd11024     27 NGTVPGPTLRATEGDLVRIHFIN-TGDHPHTIHFHGIH---DAAMDG---TGLGPIMPGESFTYEFVAEPAGTHLYHCHv 99

                           90
                   ....*....|....*..
gi 1098637342  449 --TGMQRGDGVFGALIV 463
Cdd:cd11024    100 qpLKEHIAMGLYGAFIV 116
PLN02792 PLN02792
oxidoreductase
 360-467 9.97e-13

oxidoreductase


Pssm-ID: 178389 [Multi-domain]  Cd Length: 536  Bit Score: 71.93  E-value: 9.97e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1098637342  360 DGIERSVMVVNRMMPGPSIEVCEGDMIVVDVHNHlLGDSTTIHWHGMHQRNYPYMDGVpHISQCPISPHSTFRYRFRAEN 439
Cdd:PLN02792    31 LTLPRRGILINGQFPGPEIRSLTNDNLVINVHND-LDEPFLLSWNGVHMRKNSYQDGV-YGTTCPIPPGKNYTYDFQVKD 108

                           90       100       110
                   ....*....|....*....|....*....|
gi 1098637342  440 -TGTHFWHSHTGMQRGDGVFGAL-IVRRPR 467
Cdd:PLN02792   109 qVGSYFYFPSLAVQKAAGGYGSLrIYSLPR 138
CuRO_3_CumA_like cd13906
The third cupredoxin domain of CumA like multicopper oxidase; This multicopper oxidase (MCO) ...
 935-1024 1.76e-12

The third cupredoxin domain of CumA like multicopper oxidase; This multicopper oxidase (MCO) subfamily includes CumA from Pseudomonas putida, which is involved in the oxidation of Mn(II). However, the cumA gene has been identified in a variety of bacterial species, including both Mn(II)-oxidizing and non-Mn(II)-oxidizing strains. Thus, the proteins in this family may catalyze the oxidation of other substrates. MCO catalyzes the oxidation of a variety aromatic - notably phenolic and inorganic substances coupled to the reduction of molecular oxygen to water and has been implicated in a wide spectrum of biological activities and, in particular, plays a key role in morphogenesis, development and lignin metabolism. Although MCOs have diverse functions, majority of them have three cupredoxin domain repeats that include one mononuclear and one trinuclear copper center. The copper ions are bound in several sites: Type 1, Type 2, and/or Type 3. The ensemble of types 2 and 3 copper is called a trinuclear cluster. MCOs oxidize their substrate by accepting electrons at a mononuclear copper center and transferring them to the active site trinuclear copper center. The cupredoxin domain 3 of 3-domain MCOs contains the Type 1 (T1) copper binding site and part the trinuclear copper binding site, which is located at the interface of domains 1 and 3.


Pssm-ID: 259973 [Multi-domain]  Cd Length: 138  Bit Score: 65.87  E-value: 1.76e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1098637342  935 HPFHLHGNAFRVvglerLGSNvtiemvkqldrynllKRNLDRPPIKDTVTIPDGGYTILRFEAYNPGFWLFHCHIEFHAE 1014
Cdd:cd13906     69 HPMHLHGHFFRV-----LSRN---------------GRPVPEPFWRDTVLLGPKETVDIAFVADNPGDWMFHCHILEHQE 128

                           90
                   ....*....|
gi 1098637342 1015 IGMALIIKVG 1024
Cdd:cd13906    129 TGMMGVIRVA 138
CuRO_3_McoC_like cd13902
The third cupredoxin domain of a multicopper oxidase McoC and similar proteins; This family ...
 930-1023 2.21e-12

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: 65.11  E-value: 2.21e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1098637342  930 TFDANHPFHLHGNAFRVVGlerlgsnvtIEMVKQLDRYnllkrnldrPPIKDTVTIPDGGYTILRFEAYNPGFWLFHCHI 1009
Cdd:cd13902     50 TSHMDHPFHLHGTQFQVLE---------IDGNPQKPEY---------RAWKDTVNLPPGEAVRIATRQDDPGMWMYHCHI 111

                           90
                   ....*....|....
gi 1098637342 1010 EFHAEIGMALIIKV 1023
Cdd:cd13902    112 LEHEDAGMMGMLHV 125
PLN02835 PLN02835
oxidoreductase
 361-467 8.33e-12

oxidoreductase


Pssm-ID: 178429 [Multi-domain]  Cd Length: 539  Bit Score: 69.23  E-value: 8.33e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1098637342  361 GIERSVMVVNRMMPGPSIEVCEGDMIVVDVHNHLlGDSTTIHWHGMHQRNYPYMDGVPHiSQCPISPHSTFRYRFRAENT 440
Cdd:PLN02835    45 GVPQQVILINGQFPGPRLDVVTNDNIILNLINKL-DQPFLLTWNGIKQRKNSWQDGVLG-TNCPIPPNSNYTYKFQTKDQ 122

                           90       100
                   ....*....|....*....|....*....
gi 1098637342  441 -GTHFWHSHTGMQRGDGVFGAL-IVRRPR 467
Cdd:PLN02835   123 iGTFTYFPSTLFHKAAGGFGAInVYERPR 151
CuRO_1_Tth-MCO_like cd13853
The first cupredoxin domain of the bacterial laccases similar to Tth-MCO from Thermus ...
 370-464 9.89e-12

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: 63.43  E-value: 9.89e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1098637342  370 NRMMPGPSIEVCEGDMIVVDVHNHL----------------LGDSTTIHWHGMHQRNYPYMDGVpHISqcpISPHSTFRY 433
Cdd:cd13853     26 NGSIPGPTLRVRPGDTLRITLKNDLppegaaneapapntphCPNTTNLHFHGLHVSPTGNSDNV-FLT---IAPGESFTY 101

                           90       100       110
                   ....*....|....*....|....*....|....*...
gi 1098637342  434 RFR-AEN--TGTHFWHSH----TGMQRGDGVFGALIVR 464
Cdd:cd13853    102 EYDiPADhpPGTYWYHPHlhgsTALQVAGGMAGALVVE 139
CuRO_1_CueO_FtsP cd04232
The first Cupredoxin domain of the multicopper oxidase CueO, the cell division protein FtsP, ...
 375-464 1.25e-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: 62.59  E-value: 1.25e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1098637342  375 GPSIEVCEGDMIVVDVHNHLlGDSTTIHWHGMHQRnyPYMDGVPHisQcPISPHSTFRYRFRAEN-TGTHFWHSH----T 449
Cdd:cd04232     31 GPTIRVKKGDTVRINVTNNL-DEETTVHWHGLHVP--GEMDGGPH--Q-PIAPGQTWSPTFTIDQpAATLWYHPHthgkT 104

                           90
                   ....*....|....*
gi 1098637342  450 GMQRGDGVFGALIVR 464
Cdd:cd04232    105 AEQVYRGLAGLFIIE 119
CuRO_D2_2dMcoN_like cd04202
The second cupredoxin domain of bacterial two domain multicopper oxidase McoN and similar ...
 934-1018 2.90e-11

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: 62.27  E-value: 2.90e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1098637342  934 NHPFHLHGNAFRVVGleRLGSNVTiemvkqldrynllkrnLDRPPIKDTVTIPDGG-YTILrFEAYNPGFWLFHCHIEFH 1012
Cdd:cd04202     62 HHPMHLHGHFFLVTA--TDGGPIP----------------GSAPWPKDTLNVAPGErYDIE-FVADNPGDWMFHCHKLHH 122


                   ....*.
gi 1098637342 1013 AEIGMA 1018
Cdd:cd04202    123 AMNGMG 128
CuRO_3_AAO_like_2 cd13895
The third cupredoxin domain of Ascorbate oxidase homologs; This family includes fungal ...
 891-1018 6.29e-11

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: 62.72  E-value: 6.29e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1098637342  891 DTSLAQQGIDCRTdfcnchHVLQVPLNSVVELIVVDEGF---TFDAnHPFHLHGNAFRVVGlERLG--SNVTIEMVKQLD 965
Cdd:cd13895     53 EAALANGGFDPET------NTFPAKLGEVLDIVWQNTASptgGLDA-HPWHAHGAHYYDLG-SGLGtySATALANEEKLR 124

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 1098637342  966 RYNLLKR---NLDRPPIKDTVTIPD--GGYTILRFEAYNPGFWLFHCHIEFHAEIGMA 1018
Cdd:cd13895    125 GYNPIRRdttMLYRYGGKGYYPPPGtgSGWRAWRLRVDDPGVWMLHCHILQHMIMGMQ 182
CuRO_3_Tth-MCO_like cd13900
The third cupredoxin domain of the bacterial laccases similar to Tth-MCO from Thermus ...
 913-1023 1.24e-10

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: 59.95  E-value: 1.24e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1098637342  913 QVPLNSVVELIVVDEGftfDANHPFHLHGNAFRVVglERLGsnvtiemvkqldrynllkRNLDRPPIKDTVTIPDGGYTI 992
Cdd:cd13900     35 TVRLGTVEEWTLINTS---GEDHPFHIHVNPFQVV--SING------------------KPGLPPVWRDTVNVPAGGSVT 91

                           90       100       110
                   ....*....|....*....|....*....|...
gi 1098637342  993 LR--FEAYnPGFWLFHCHIEFHAEIGMALIIKV 1023
Cdd:cd13900     92 IRtrFRDF-TGEFVLHCHILDHEDQGMMQVVEI 123
CuRO_3_MCO_like_3 cd13909
The third cupredoxin domain of uncharacterized multicopper oxidase; Multicopper Oxidases (MCOs) ...
 935-1023 1.68e-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: 60.23  E-value: 1.68e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1098637342  935 HPFHLHGNAFRVVGlerlgsnvtiemvkqldrynllkRNLDRPPIKDTVTIPDGGYTILRFEAYNPGFWLFHCHIEFHAE 1014
Cdd:cd13909     71 HGMHLHGHHFRAIL-----------------------PNGALGPWRDTLLMDRGETREIAFVADNPGDWLLHCHMLEHAA 127


                   ....*....
gi 1098637342 1015 IGMALIIKV 1023
Cdd:cd13909    128 AGMMSWFRV 136
CuRO_1_MCO_like_1 cd13862
The first cupredoxin domain of uncharacterized multicopper oxidase; Multicopper Oxidases (MCOs) ...
 370-463 2.82e-10

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: 59.07  E-value: 2.82e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1098637342  370 NRMMPGPSIEVCEGDMIVVDVHNhLLGDSTTIHWHGMHQRnyPYMDGVPHISQCPISPHSTFRYRFRAENTGTHFWHSHT 449
Cdd:cd13862     26 NGQVPGPLLRMRQGVSVTVDVFN-DTDIPEYVHWHGLPLP--ADVDGAMEEGTPSVPPHGHRRYRMTPRPAGFRWYHTHV 102

                           90       100
                   ....*....|....*....|.
gi 1098637342  450 gMQRGD-------GVFGALIV 463
Cdd:cd13862    103 -MTMDDltrgqysGLFGFVYI 122
CuRO_1_McoP_like cd13852
The first cupredoxin domain of multicopper oxidase McoP and similar proteins; This family ...
 375-463 8.38e-10

The first cupredoxin domain of multicopper oxidase McoP and similar proteins; This family includes archaeal and bacterial multicopper oxidases (MCOs), represented by the extremely thermostable McoP from the hyperthermophilic archaeon Pyrobaculum aerophilum. McoP is an efficient metallo-oxidase that catalyzes the oxidation of cuprous and ferrous ions. It is noteworthy that McoP has three-fold higher catalytic efficiency when using nitrous oxide as the electron acceptor than when using dioxygen, the typical oxidizing substrate of MCOs. McoP may function as a novel archaeal nitrous oxide reductase that is probably involved in the denitrification pathway in archaea. Although MCOs have diverse functions, majority of them have three cupredoxin domain repeats that include one mononuclear and one trinuclear copper center. The copper ions are bound in several sites: Type 1, Type 2, and/or Type 3. The ensemble of types 2 and 3 copper is called a trinuclear cluster. MCOs oxidize their substrate by accepting electrons at a mononuclear copper center and transferring them to the active site trinuclear copper center. The cupredoxin domain 1 of 3-domain MCOs contains part the trinuclear copper binding site, which is located at the interface of domains 1 and 3.


Pssm-ID: 259921 [Multi-domain]  Cd Length: 114  Bit Score: 57.30  E-value: 8.38e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1098637342  375 GPSIEVCEGDMIVVDVHNHLlGDSTTIHWHGMHQRnyPYMDGVPHISqcpISPHSTFRYRFRAEN-TGTHFWHSH----T 449
Cdd:cd13852     24 GPILRLRKGQKVRITFKNNL-PEPTIIHWHGLHVP--AAMDGHPRYA---IDPGETYVYEFEVLNrAGTYWYHPHphglT 97

                           90
                   ....*....|....
gi 1098637342  450 GMQRGDGVFGALIV 463
Cdd:cd13852     98 AKQVYRGLAGLFLV 111
PLN00044 PLN00044
multi-copper oxidase-related protein; Provisional
 358-463 9.86e-10

multi-copper oxidase-related protein; Provisional


Pssm-ID: 165622 [Multi-domain]  Cd Length: 596  Bit Score: 62.76  E-value: 9.86e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1098637342  358 LGDGIERSVMVVNRMMPGPSIEVCEGDMIVVDVHNHLlGDSTTIHWHGMHQRNYPYMDGVPHiSQCPISPHSTFRYRFRA 437
Cdd:PLN00044    42 LGGVKKQEAIGINGQFPGPALNVTTNWNLVVNVRNAL-DEPLLLTWHGVQQRKSAWQDGVGG-TNCAIPAGWNWTYQFQV 119

                           90       100
                   ....*....|....*....|....*..
gi 1098637342  438 EN-TGTHFWHSHTGMQRGDGVFGALIV 463
Cdd:PLN00044   120 KDqVGSFFYAPSTALHRAAGGYGAITI 146
CuRO_2_AAO cd13871
The second cupredoxin domain of plant Ascorbate oxidase; Ascorbate oxidase catalyzes the ...
 665-738 1.23e-09

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: 58.32  E-value: 1.23e-09
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1098637342  665 IFHVRRGFRYRFRIINAEFLNCpIALSIDNHTLLAIHSDGYDFEPLEVGAMVTYAGERFDFVLNANQSIG-NYWI 738
Cdd:cd13871     73 ILHVSPGKTYRLRIASVTALSS-LNFIIEGHNLTVVEADGNYVQPFEVSNLDIYSGETYSVLVTADQDPSrNYWV 146
PLN02991 PLN02991
oxidoreductase
 361-520 1.94e-09

oxidoreductase


Pssm-ID: 215536 [Multi-domain]  Cd Length: 543  Bit Score: 61.57  E-value: 1.94e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1098637342  361 GIERSVMVVNRMMPGPSIEVCEGDMIVVDVHNHlLGDSTTIHWHGMHQRNYPYMDGVpHISQCPISPHSTFRYRFRAENT 440
Cdd:PLN02991    44 GVAQQGILINGKFPGPDIISVTNDNLIINVFNH-LDEPFLISWSGIRNWRNSYQDGV-YGTTCPIPPGKNYTYALQVKDQ 121

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1098637342  441 -GTHFWHSHTGMQRGDGVFGAL-IVRRPRAMEAhghlYDFDLSEHKMILQDWVHTpgvsifsSHHHSRG--DNK-----P 511
Cdd:PLN02991   122 iGSFYYFPSLGFHKAAGGFGAIrISSRPLIPVP----FPAPADDYTVLIGDWYKT-------NHKDLRAqlDNGgklplP 190


                   ....*....
gi 1098637342  512 VNLLVNGRG 520
Cdd:PLN02991   191 DGILINGRG 199
CuRO_1_CuNIR_like cd04201
Cupredoxin domain 1 of Copper-containing nitrite reductase and two-domain laccase; ...
 358-463 4.11e-09

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: 55.57  E-value: 4.11e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1098637342  358 LGDGIERSVMVVNRMMPGPSIEVCEGDMIVVDVHNHllGDST---TIHWHGMHQrnyPYMDGvphiSQCPISPHSTFRYR 434
Cdd:cd04201     15 LDDGVEYRYWTFDGDIPGPMLRVREGDTVELHFSNN--PSSTmphNIDFHAATG---AGGGA----GATFIAPGETSTFS 85

                           90       100       110
                   ....*....|....*....|....*....|..
gi 1098637342  435 FRAENTGTHFWHSHTG---MQRGDGVFGALIV 463
Cdd:cd04201     86 FKATQPGLYVYHCAVApvpMHIANGMYGLILV 117
CuRO_3_CueO_FtsP cd13890
The third Cupredoxin domain of the multicopper oxidase CueO, the cell division protein FtsP, ...
 935-1017 2.22e-08

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


Pssm-ID: 259957 [Multi-domain]  Cd Length: 124  Bit Score: 53.41  E-value: 2.22e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1098637342  935 HPFHLHGNAFRVvglerlgsnvtiemvkqldrynlLKRNlDRPP------IKDTVTIPDGGYT--ILRFE--AYNPGFWL 1004
Cdd:cd13890     50 HPFHIHGVQFRI-----------------------LSRN-GQPPppneagWKDTVWVPPGETVriLVKFDhyADPTGPFM 105

                           90
                   ....*....|...
gi 1098637342 1005 FHCHIEFHAEIGM 1017
Cdd:cd13890    106 YHCHILEHEDNGM 118
CuRO_2_CopA_like_1 cd13870
The second cupredoxin domain of CopA copper resistance protein like family; The members of ...
 664-733 2.72e-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: 53.11  E-value: 2.72e-08
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1098637342  664 QIFHVRRGFRYRFRIINAE----FlncpiALSIDNHTLLAIHSDGYDFEPLEVGAMVTYAGERFDFVLNANQSI 733
Cdd:cd13870     29 AVFTARPGDRLRLRLINAAgdtaF-----RVALAGHRLTVTHTDGFPVEPVEVDALLIGMGERYDAIVTANNGI 97
CuRO_3_MCO_like_2 cd13908
The third cupredoxin domain of uncharacterized multicopper oxidase; Multicopper Oxidases (MCOs) ...
 932-1023 3.89e-08

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


Pssm-ID: 259975 [Multi-domain]  Cd Length: 122  Bit Score: 52.84  E-value: 3.89e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1098637342  932 DANHPFHLHGNAFRVVgleRLGSNVTIEMvkqldrynllkrnldrppIKDTVTIPDGGYTILRFEAYNPGFWLFHCHIEF 1011
Cdd:cd13908     52 DDAHPMHLHRHTFEVT---RIDGKPTSGL------------------RKDVVMLGGYQRVEVDFVADNPGLTLFHCHQQL 110

                           90
                   ....*....|..
gi 1098637342 1012 HAEIGMALIIKV 1023
Cdd:cd13908    111 HMDYGFMALFKY 122
CuRO_2_Diphenol_Ox cd13883
The second cupredoxin domain of fungal laccase, diphenol oxidase; Diphenol oxidase belongs to ...
 644-761 6.70e-08

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


Pssm-ID: 259950 [Multi-domain]  Cd Length: 164  Bit Score: 53.11  E-value: 6.70e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1098637342  644 TNVQRTKRAVddiQLHQMPLQIFHVRRGFRYRFRIINAEfLNCPIALSIDNHTLLAIHSDGYD-FEPLEVGAMVTYAGER 722
Cdd:cd13883     46 FNCSAADPGT---CCTQTSPPEIQVEAGKRTRFRLINAG-SHAMFRFSVDNHTLNVVEADDTPvYGPTVVHRIPIHNGQR 121

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....
gi 1098637342  723 FDFVLNANQ-SIGN-YWIRfkGLMDCSDQFTSAFQV---GILRY 761
Cdd:cd13883    122 YSVIIDTTSgKAGDsFWLR--ARMATDCFAWDLQQQtgkAILRY 163
CuRO_1_CuNIR cd11020
Cupredoxin domain 1 of Copper-containing nitrite reductase; Copper-containing nitrite ...
 357-463 8.06e-07

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: 49.13  E-value: 8.06e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1098637342  357 VLGDGIERSVMVVNRMMPGPSIEVCEGDMIVVDVHNHllGDSTTIHWHGMHQRNYPymdGVPHISQcpISPHSTFRYRFR 436
Cdd:cd11020     14 EIAPGVTYTAWTFNGQVPGPVIRVREGDTVELTLTNP--GTNTMPHSIDFHAATGP---GGGEFTT--IAPGETKTFSFK 86

                           90       100       110
                   ....*....|....*....|....*....|
gi 1098637342  437 AENTGTHFWH---SHTGMQRGDGVFGALIV 463
Cdd:cd11020     87 ALYPGVFMYHcatAPVLMHIANGMYGAIIV 116
PRK10965 PRK10965
multicopper oxidase; Provisional
 369-464 2.15e-06

multicopper oxidase; Provisional


Pssm-ID: 236810 [Multi-domain]  Cd Length: 523  Bit Score: 51.56  E-value: 2.15e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1098637342  369 VNRMMPGPSIEVCEGDMIVVDVHNHLlGDSTTIHWHGMHqrnYP-YMDGVPHisqCPISPHSTFRYRFRAENTGTHFW-- 445
Cdd:PRK10965    70 YNGNLLGPAVRLQRGKAVTVDITNQL-PEETTLHWHGLE---VPgEVDGGPQ---GIIAPGGKRTVTFTVDQPAATCWfh 142

                           90       100
                   ....*....|....*....|..
gi 1098637342  446 ---HSHTGMQRGDGVFGALIVR 464
Cdd:PRK10965   143 phqHGKTGRQVAMGLAGLVLIE 164
CuRO_3_CotA_like cd13891
The third Cupredoxin domain of bacterial laccases including CotA, a bacterial endospore coat ...
 932-1029 1.83e-05

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


Pssm-ID: 259958 [Multi-domain]  Cd Length: 143  Bit Score: 45.75  E-value: 1.83e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1098637342  932 DANHPFHLHGNAFRVVGLERLGsnvtiemVKQLDRYNLLKRNLD-RPPI------KDTVTIPDGGYT--ILRFEAYNPGF 1002
Cdd:cd13891     51 PDAHPIHLHLVQFQVLDRQPFD-------VDEYNATGEIYYTGPpRPPApnergwKDTVRAYPGEVTriIVRFDGPEGGY 123

                           90       100
                   ....*....|....*....|....*..
gi 1098637342 1003 wLFHCHIEFHaEigmaliikvgDNDQM 1029
Cdd:cd13891    124 -VWHCHILEH-E----------DNEMM 138
CuRO_2_LCC_plant cd13875
The second cupredoxin domain of the plant laccases; Laccase is a blue multi-copper enzyme that ...
 668-761 2.14e-05

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: 45.67  E-value: 2.14e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1098637342  668 VRRGFRYRFRIINAEfLNCPIALSIDNHTLLAIHSDGYDFEPLEVGAMVTYAGERFDFVLNANQSIGNYWIRFKGLMDCS 747
Cdd:cd13875     55 VEPGKTYLLRIINAA-LNEELFFKIANHTLTVVAVDASYTKPFTTDYILIAPGQTTDVLLTADQPPGRYYMAARPYQSAP 133

                           90
                   ....*....|....*
gi 1098637342  748 D-QFTSAFQVGILRY 761
Cdd:cd13875    134 PvPFDNTTATAILEY 148
CuRO_2_AAO_like_2 cd13873
The second cupredoxin domain of plant Ascorbate oxidase homologs; This family includes plant ...
 663-761 3.20e-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: 45.36  E-value: 3.20e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1098637342  663 LQIFHVRRGFRYRFRIINAEFLNcPIALSIDNH-TLLAIHSDGYDFEPLEVGAMVTYAGERFDFVL---------NANQS 732
Cdd:cd13873     60 PPVIDVEPGKTYRFRFIGATALS-FVSLGIEGHdNLTIIEADGSYTKPAETDHLQLGSGQRYSFLLktksleelaALNKT 138

                           90       100
                   ....*....|....*....|....*....
gi 1098637342  733 igNYWIRFKGLmDCSDQFTSAFqvgILRY 761
Cdd:cd13873    139 --TFWIQIETR-WRPTNDTGYA---VLRY 161
CuRO_2_McoC_like cd13881
The second cupredoxin domain of a multicopper oxidase McoC and similar proteins; This family ...
 667-736 5.17e-05

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: 44.52  E-value: 5.17e-05
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1098637342  667 HVRRGFRYRFRIINA---EFLNcpiaLSIDNHTLLAIHSDGYDFE-PLEVGAMVTYAGERFDFVLNANQSIGNY 736
Cdd:cd13881     45 TVRPGEVQRWRIVNAasaRYFR----LALDGHKFRLIGTDGGLLEaPREVDELLLAPGERAEVLVTAGEPGGRL 114
CuRO_3_MCO_like_1 cd13907
The third cupredoxin domain of uncharacterized multicopper oxidase; Multicopper Oxidases (MCOs) ...
 935-1017 1.12e-04

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


Pssm-ID: 259974 [Multi-domain]  Cd Length: 154  Bit Score: 43.62  E-value: 1.12e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1098637342  935 HPFHLHGNAFRVVGLERLGsnvtiemvKQLDRYNLLKRNLDRPPIKDTVTIPDGGYT--ILRFEAYnPGFWLFHCHIEFH 1012
Cdd:cd13907     72 HPIHLHGVQFQVLERSVGP--------KDRAYWATVKDGFIDEGWKDTVLVMPGERVriIKPFDDY-KGLFLYHCHNLEH 142


                   ....*
gi 1098637342 1013 AEIGM 1017
Cdd:cd13907    143 EDMGM 147
CuRO_2_Fet3p_like cd13877
The second Cupredoxin domain of multicopper oxidase Fet3P; Fet3p catalyzes the ferroxidase ...
 666-745 1.34e-04

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: 43.31  E-value: 1.34e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1098637342  666 FHVRRGFRYRFRIINAEFLNCPIaLSIDNHTLLAIHSDGYDFEPLEVGAMVTYAGERFDFVLNA-NQSIGNYwiRFKGLM 744
Cdd:cd13877     48 INFEPGKTYLLRIINMGAFASQY-FHIEGHDMTIIEVDGVYVKPYPVDTLYIAVGQRYSVLVKAkNDTDRNY--AIINGM 124


                   .
gi 1098637342  745 D 745
Cdd:cd13877    125 D 125
CuRO_3_McoP_like cd13888
The third cupredoxin domain of multicopper oxidase McoP and similar proteins; This subfamily ...
 935-1023 2.45e-04

The third cupredoxin domain of multicopper oxidase McoP and similar proteins; This subfamily includes archaeal and bacterial multicopper oxidases (MCOs), represented by the extremely thermostable McoP from the hyperthermophilic archaeon Pyrobaculum aerophilum. McoP is an efficient metallo-oxidase that catalyzes the oxidation of cuprous and ferrous ions. It is noteworthy that McoP has three-fold higher catalytic efficiency when using nitrous oxide as electron acceptor than when using dioxygen, the typical oxidizing substrate of multicopper oxidases. McoP may function as a novel archaeal nitrous oxide reductase that is probably involved in the denitrification pathway in archaea. Members of this subfamily contain three cupredoxin domain repeats. The copper ions are bound in several sites; Type 1, Type 2, and/or Type 3. The ensemble of types 2 and 3 copper is called a trinuclear cluster. MCOs oxidize their substrate by accepting electrons at a mononuclear copper center and transferring them to the active site trinuclear copper center. The cupredoxin domain 3 of 3-domain MCOs contains the Type 1 (T1) copper binding site and part the trinuclear copper binding site, which is located at the interface of domains 1 and 3.


Pssm-ID: 259955 [Multi-domain]  Cd Length: 139  Bit Score: 42.55  E-value: 2.45e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1098637342  935 HPFHLHGNAFRVvgLERLGSNVtieMVKQLDRYNLLKRNLDRpPIKDTVTI-PdgGYTI---LRFEAYNPG--FWLFHCH 1008
Cdd:cd13888     52 HPMHIHGFQFQV--LERSDSPP---QVAELAVAPSGRTATDL-GWKDTVLVwP--GETVriaVDFTHDYPGdqLYLLHCH 123

                           90
                   ....*....|....*
gi 1098637342 1009 IEFHAEIGMALIIKV 1023
Cdd:cd13888    124 NLEHEDDGMMVNVRV 138
CuRO_2_Abr2_like cd13876
The second cupredoxin domain of a group of fungal Laccases similar to Abr2 from Aspergillus ...
 676-762 3.90e-04

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: 41.80  E-value: 3.90e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1098637342  676 FRIINAEFLNcPIALSIDNHTLLAIHSDGYDFEPLEVGAMVTYAGERFDFVLNANQSIGNYWIRFKGlmdcsdqfTSAFQ 755
Cdd:cd13876     57 LNFINAGGFH-TLAFSIDEHPMWVYAVDGGYIEPQLVDAISITNGERYSVLVKLDKPPGDYTIRVAS--------TGAPQ 127

                           90
                   ....*....|.
gi 1098637342  756 V----GILRYE 762
Cdd:cd13876    128 VisgyAILRYK 138
Cupredoxin cd00920
Cupredoxin superfamily; Cupredoxins contain type I copper centers and are involved in ...
 911-1022 4.36e-04

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


Pssm-ID: 259860 [Multi-domain]  Cd Length: 110  Bit Score: 41.06  E-value: 4.36e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1098637342  911 VLQVPLNSVVELIVVdegFTFDANHPFHLHGNAFRVVGLerlgsnvtiemvkqldrynllkRNLDRPPIKDTVTIPDGGY 990
Cdd:cd00920     24 VLVVPVGDTVRVQFV---NKLGENHSVTIAGFGVPVVAM----------------------AGGANPGLVNTLVIGPGES 78

                           90       100       110
                   ....*....|....*....|....*....|..
gi 1098637342  991 TILRFEAYNPGFWLFHCHIEFHAEIGMALIIK 1022
Cdd:cd00920     79 AEVTFTTDQAGVYWFYCTIPGHNHAGMVGTIN 110
CuRO_1_2DMCO_NIR_like_2 cd14449
The cupredoxin domain 1 of a two-domain laccase related to nitrite reductase; The two-domain ...
 373-465 7.75e-04

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. 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. This subfamily has lost the type 1 (T1) copper binding site in domain 1 that is present in other two-domain laccases.


Pssm-ID: 259991 [Multi-domain]  Cd Length: 135  Bit Score: 40.71  E-value: 7.75e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1098637342  373 MPGPSIEVCEGDMIVVDVHNHlLGDSTTIHWHGMhqrNYPYMDGVPHISQCPISPHSTFRYRFR------------AENT 440
Cdd:cd14449     27 VPGPVIEVREGDTLKILFRNT-LDVPASLHPHGV---DYTTASDGTGMNASIVAPGDTRIYTWRthggyrradgswAEGT 102

                           90       100       110
                   ....*....|....*....|....*....|..
gi 1098637342  441 -GTHFWHSHT-GMQRGD-----GVFGALIVRR 465
Cdd:cd14449    103 aGYWHYHDHVfGTEHGTeglsrGLYGALIVRR 134
CuRO_2_CotA_like cd13868
The second Cupredoxin domain of bacterial laccases including CotA, a bacterial endospore coat ...
 673-734 1.09e-03

The second Cupredoxin domain of bacterial laccases including CotA, a bacterial endospore coat component; CotA protein is an abundant component of the outer coat layer in bacterial endospore coat and it is required for spore resistance against hydrogen peroxide and UV light. Laccase is composed of three cupredoxin-like domains and includes one mononuclear and one trinuclear copper center. It is a member of the multicopper oxidase (MCO) family, which couples the oxidation of a substrate with a four-electron reduction of molecular oxygen to water. MCOs oxidize their substrate by accepting electrons at a mononuclear copper center and transferring them to the active site trinuclear copper center. The cupredoxin domain 2 of 3-domain MCOs has lost the ability to bind copper.


Pssm-ID: 259936 [Multi-domain]  Cd Length: 155  Bit Score: 40.69  E-value: 1.09e-03
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1098637342  673 RYRFRIIN---AEFLNcpiaLSIDNHTLLAIH---SD-GYDFEPLEVGAMVTYAGERFDFVLNANQSIG 734
Cdd:cd13868     58 RYRFRILNgsnARFYN----LSLSNGDGLPFWqigTDgGFLPKPVPLDSLLIGPAERADVIVDFSDYAG 122
VWC pfam00093
von Willebrand factor type C domain; The high cutoff was used to prevent overlap with ...
 216-281 3.46e-03

von Willebrand factor type C domain; The high cutoff was used to prevent overlap with pfam00094.


Pssm-ID: 278520  Cd Length: 57  Bit Score: 36.63  E-value: 3.46e-03
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1098637342  216 CRFNDTVYDLGQTWHsPDGCTMYECAPLpersvvtpMINVFEKTCAPLPLDCPREQVYVKDCCQQC 281
Cdd:pfam00093    1 CVQNGVVYENGETWK-PDLCTICTCDDG--------KVLCDKIICPPLDCPNPRLEIPPGECCPVC 57
 
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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