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Conserved domains on  [gi|56785438|gb|AAW28934|]
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laccase C, partial [Trametes sp. AH28-2]

Protein Classification

multicopper oxidase( domain architecture ID 10195168)

multicopper oxidase (MCO) that couples the oxidation of a substrate with a four-electron reduction of molecular oxygen to water, and which appears to contain three cupredoxin domains; similar to Trametes villosa laccase-1 that may be involved in lignin degradation and detoxification of lignin-derived products

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
CuRO_1_Tv-LCC_like cd13856
The first cupredoxin domain of fungal laccases similar to Tv-LCC from Trametes versicolor; ...
 29-153 1.34e-83

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: 254.18  E-value: 1.34e-83
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56785438  29 PVTDLTISNENVSPDGFTRAAVVANGKAPGPLITGQKGDRFQINVVNKLSNHTMLKSTSIHWHGFFQKGTNWADGPAFVN 108
Cdd:cd13856   1 PTYTLNIVNTRLAPDGFERSAVLANGQFPGPLITANKGDTFRITVVNQLTDPTMRRSTSIHWHGIFQHGTNYADGPAFVT 80

                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*
gi 56785438 109 QCPIATGHSFLYDFQVPDQAGTFWYHSHLSTQYCDGLRGPFVVYD 153
Cdd:cd13856  81 QCPIAPNHSFTYDFTAGDQAGTFWYHSHLSTQYCDGLRGPLVIYD 125
CuRO_3_Tv-LCC_like cd13903
The third cupredoxin domain of the fungal laccases similar to Tv-LCC from Trametes Versicolor; ...
 348-496 1.40e-79

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: 244.50  E-value: 1.40e-79
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56785438 348 DKAINFAFTFNGTN--FFINGATFQPPTTPVLLQILSGAQDAKDLLPSGDVYALPSDATIELSFPAstGAPGAPHPFHLH 425
Cdd:cd13903   1 DVNITLTFGLNGTTglFTINGVSYVSPTVPVLLQILSGATSAEDLLPTESTIILPRNKVVEITIPG--GAIGGPHPFHLH 78

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 56785438 426 GHTFAVVRSAGSTEYNYDNPIWRDVVSTGTPqaGDNVTIRFRTDNPGPWFLHCHIDFHLEAGFAVVMAEDI 496
Cdd:cd13903  79 GHAFSVVRSAGSNTYNYVNPVRRDVVSVGTP--GDGVTIRFVTDNPGPWFLHCHIDWHLEAGLAVVFAEDP 147
Cupredoxin super family cl19115
Cupredoxin superfamily; Cupredoxins contain type I copper centers and are involved in ...
 169-321 1.58e-77

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.


The actual alignment was detected with superfamily member cd13882:

Pssm-ID: 473140 [Multi-domain]  Cd Length: 159  Bit Score: 240.00  E-value: 1.58e-77
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56785438 169 TVITLADWYHVAAKLGPA----FPPRSDATLINGLGRTSDTPNADLAVITVTTGKRYRFRLISLSCDPAYTFSIDNHDMT 244
Cdd:cd13882   1 TVITLGDWYHTAAPDLLAttagVPPVPDSGTINGKGRFDGGPTSPLAVINVKRGKRYRFRVINISCIPSFTFSIDGHNLT 80

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 56785438 245 IIEADGVNTQQLTVDSLQIFAGQRYSFVLEANQKSGNYWVRANPLFGTTGFAGGI-NSAILRYDDAVPAEPTSEQGTS 321
Cdd:cd13882  81 VIEADGVETKPLTVDSVQIYAGQRYSVVVEANQPVDNYWIRAPPTGGTPANNGGQlNRAILRYKGAPEVEPTTESTAG 158
 
Name Accession Description Interval E-value
CuRO_1_Tv-LCC_like cd13856
The first cupredoxin domain of fungal laccases similar to Tv-LCC from Trametes versicolor; ...
 29-153 1.34e-83

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: 254.18  E-value: 1.34e-83
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56785438  29 PVTDLTISNENVSPDGFTRAAVVANGKAPGPLITGQKGDRFQINVVNKLSNHTMLKSTSIHWHGFFQKGTNWADGPAFVN 108
Cdd:cd13856   1 PTYTLNIVNTRLAPDGFERSAVLANGQFPGPLITANKGDTFRITVVNQLTDPTMRRSTSIHWHGIFQHGTNYADGPAFVT 80

                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*
gi 56785438 109 QCPIATGHSFLYDFQVPDQAGTFWYHSHLSTQYCDGLRGPFVVYD 153
Cdd:cd13856  81 QCPIAPNHSFTYDFTAGDQAGTFWYHSHLSTQYCDGLRGPLVIYD 125
CuRO_3_Tv-LCC_like cd13903
The third cupredoxin domain of the fungal laccases similar to Tv-LCC from Trametes Versicolor; ...
 348-496 1.40e-79

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: 244.50  E-value: 1.40e-79
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56785438 348 DKAINFAFTFNGTN--FFINGATFQPPTTPVLLQILSGAQDAKDLLPSGDVYALPSDATIELSFPAstGAPGAPHPFHLH 425
Cdd:cd13903   1 DVNITLTFGLNGTTglFTINGVSYVSPTVPVLLQILSGATSAEDLLPTESTIILPRNKVVEITIPG--GAIGGPHPFHLH 78

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 56785438 426 GHTFAVVRSAGSTEYNYDNPIWRDVVSTGTPqaGDNVTIRFRTDNPGPWFLHCHIDFHLEAGFAVVMAEDI 496
Cdd:cd13903  79 GHAFSVVRSAGSNTYNYVNPVRRDVVSVGTP--GDGVTIRFVTDNPGPWFLHCHIDWHLEAGLAVVFAEDP 147
CuRO_2_Tv-LCC_like cd13882
The second cupredoxin domain of the fungal laccases similar to Tv-LCC from Trametes versicolor; ...
 169-321 1.58e-77

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: 240.00  E-value: 1.58e-77
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56785438 169 TVITLADWYHVAAKLGPA----FPPRSDATLINGLGRTSDTPNADLAVITVTTGKRYRFRLISLSCDPAYTFSIDNHDMT 244
Cdd:cd13882   1 TVITLGDWYHTAAPDLLAttagVPPVPDSGTINGKGRFDGGPTSPLAVINVKRGKRYRFRVINISCIPSFTFSIDGHNLT 80

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 56785438 245 IIEADGVNTQQLTVDSLQIFAGQRYSFVLEANQKSGNYWVRANPLFGTTGFAGGI-NSAILRYDDAVPAEPTSEQGTS 321
Cdd:cd13882  81 VIEADGVETKPLTVDSVQIYAGQRYSVVVEANQPVDNYWIRAPPTGGTPANNGGQlNRAILRYKGAPEVEPTTESTAG 158
ascorbase TIGR03388
L-ascorbate oxidase, plant type; Members of this protein family are the copper-containing ...
 35-496 6.25e-76

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: 248.51  E-value: 6.25e-76
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56785438    35 ISNENVSPDGFTRAAVVANGKAPGPLITGQKGDRFQINVVNKLsnHTmlKSTSIHWHGFFQKGTNWADGPAFVNQCPIAT 114
Cdd:TIGR03388   8 VEYEFWSPDCFEKLVIGINGQFPGPTIRAQAGDTIVVELTNKL--HT--EGVVIHWHGIRQIGTPWADGTAGVTQCAINP 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56785438   115 GHSFLYDFQVpDQAGTFWYHSHLSTQYCDGLRGPFVVyDPNDPNASLYDVDNDDTVItLADWYHVAA---KLGPAFPP-- 189
Cdd:TIGR03388  84 GETFIYNFVV-DRPGTYFYHGHYGMQRSAGLYGSLIV-DVPDGEKEPFHYDGEFNLL-LSDWWHKSIheqEVGLSSKPmr 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56785438   190 ---RSDATLINGLGR-------TSDTPNADL-----------AVITVTTGKRYRFRLISLSCDPAYTFSIDNHDMTIIEA 248
Cdd:TIGR03388 161 wigEPQSLLINGRGQfncslaaKFSSTNLPQcnlkgneqcapQILHVEPGKTYRLRIASTTALAALNFAIEGHKLTVVEA 240

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56785438   249 DGVNTQQLTVDSLQIFAGQRYSFVLEANQK-SGNYW----VRANPLFGTTGFAgginsaILRYDDAVPAE--PTSEQGT- 320
Cdd:TIGR03388 241 DGNYVEPFTVKDIDIYSGETYSVLLTTDQDpSRNYWisvgVRGRKPNTPPGLT------VLNYYPNSPSRlpPTPPPVTp 314

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56785438   321 ---STKPLKETDLHPLTAMPVPGSAVSGgvDKAINFAFTFNGTNFF----INGATFQPPTTPVLLQILSGAQDAKDLLPS 393
Cdd:TIGR03388 315 awdDFDRSKAFSLAIKAAMGSPKPPETS--DRRIVLLNTQNKINGYtkwaINNVSLTLPHTPYLGSLKYNLLNAFDQKPP 392

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56785438   394 GDVYALPSDATIELSFPASTGAPGA-------------------------PHPFHLHGHTFAVV--------RSAGSTEY 440
Cdd:TIGR03388 393 PENYPRDYDIFKPPPNPNTTTGNGIyrlkfnttvdvilqnantlngnnseTHPWHLHGHDFWVLgygegkfrPGVDEKSY 472

                         490       500       510       520       530
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 56785438   441 NYDNPIWRDVVSTgtpQAGDNVTIRFRTDNPGPWFLHCHIDFHLEAGFAVVMAEDI 496
Cdd:TIGR03388 473 NLKNPPLRNTVVI---FPYGWTALRFVADNPGVWAFHCHIEPHLHMGMGVVFAEGV 525
PLN02604 PLN02604
oxidoreductase
 38-496 2.20e-67

oxidoreductase


Pssm-ID: 215324 [Multi-domain]  Cd Length: 566  Bit Score: 226.66  E-value: 2.20e-67
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56785438   38 ENVSPDGFTRAAVVANGKAPGPLITGQKGDrfqiNVVNKLSNHTMLKSTSIHWHGFFQKGTNWADGPAFVNQCPIATGHS 117
Cdd:PLN02604  34 EYKSPDCFKKLVITINGRSPGPTILAQQGD----TVIVELKNSLLTENVAIHWHGIRQIGTPWFDGTEGVTQCPILPGET 109

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56785438  118 FLYDFQVpDQAGTFWYHSHLSTQYCDGLRGPFVVYDPN-DPNASLYDVDNDdtvITLADWYHVAA---KLGPAFPP---- 189
Cdd:PLN02604 110 FTYEFVV-DRPGTYLYHAHYGMQREAGLYGSIRVSLPRgKSEPFSYDYDRS---IILTDWYHKSTyeqALGLSSIPfdwv 185

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56785438  190 -RSDATLINGLGR----------------TSDTPNADLAVITVTTGKRYRFRLISLSCDPAYTFSIDNHDMTIIEADGVN 252
Cdd:PLN02604 186 gEPQSLLIQGKGRyncslvsspylkagvcNATNPECSPYVLTVVPGKTYRLRISSLTALSALSFQIEGHNMTVVEADGHY 265

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56785438  253 TQQLTVDSLQIFAGQRYSFVLEANQK-SGNYWVRANPLFGTTGFAGGInsAILRYDDAVP--AEPTSEqgtSTKPLKEtD 329
Cdd:PLN02604 266 VEPFVVKNLFIYSGETYSVLVKADQDpSRNYWVTTSVVSRNNTTPPGL--AIFNYYPNHPrrSPPTVP---PSGPLWN-D 339

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56785438  330 LHPLTAMPVPGSAVSGGV-------DKAINFAFTFNGTN----FFINGATFQPPTTPVLLQILSGAQDAKDLLPSG---- 394
Cdd:PLN02604 340 VEPRLNQSLAIKARHGYIhpppltsDRVIVLLNTQNEVNgyrrWSVNNVSFNLPHTPYLIALKENLTGAFDQTPPPegyd 419

                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56785438  395 ----DVYALP-------SDATIELSF---------PASTGAP--GAPHPFHLHGHTFAVV--------RSAGSTEYNYDN 444
Cdd:PLN02604 420 fanyDIYAKPnnsnatsSDSIYRLQFnstvdiilqNANTMNAnnSETHPWHLHGHDFWVLgygegkfnMSSDPKKYNLVD 499

                        490       500       510       520       530
                 ....*....|....*....|....*....|....*....|....*....|..
gi 56785438  445 PIWRDVVSTgtpQAGDNVTIRFRTDNPGPWFLHCHIDFHLEAGFAVVMAEDI 496
Cdd:PLN02604 500 PIMKNTVPV---HPYGWTALRFRADNPGVWAFHCHIESHFFMGMGVVFEEGI 548
SufI COG2132
Multicopper oxidase with three cupredoxin domains (includes cell division protein FtsP and ...
 53-491 2.99e-65

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: 217.11  E-value: 2.99e-65
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56785438  53 NGKAPGPLITGQKGDRFQINVVNKLSNHTmlkstSIHWHGFFQKGTNwaDGPAFVnqcPIATGHSFLYDFQVPDQAGTFW 132
Cdd:COG2132  39 NGQYPGPTIRVREGDRVRVRVTNRLPEPT-----TVHWHGLRVPNAM--DGVPGD---PIAPGETFTYEFPVPQPAGTYW 108

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56785438 133 YHSHL----STQYCDGLRGPFVVYDPNDPnasLYDVDnDDTVITLADW-----YHVAAKLGPAFPPRS-DATLINGlgrt 202
Cdd:COG2132 109 YHPHThgstAEQVYRGLAGALIVEDPEED---LPRYD-RDIPLVLQDWrldddGQLLYPMDAAMGGRLgDTLLVNG---- 180

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56785438 203 sdtpnADLAVITVTTGKRYRFRLISLSCDPAYTFSI-DNHDMTIIEADGVNTQQ-LTVDSLQIFAGQRYSFVLEANQKSG 280
Cdd:COG2132 181 -----RPNPTLEVRPGERVRLRLLNASNARIYRLALsDGRPFTVIATDGGLLPApVEVDELLLAPGERADVLVDFSADPG 255

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56785438 281 NYWVRANPLFGTTGFAGginsAILRYDDAVPAEPTSEQGTSTKPLKETDlhpltampvpgsavsggVDKAINFAFTFN-- 358
Cdd:COG2132 256 EEVTLANPFEGRSGRAL----LTLRVTGAAASAPLPANLAPLPDLEDRE-----------------AVRTRELVLTGGma 314

                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56785438 359 GTNFFINGATFQPptTPVLLQILSGaqdakdllpsgdvyalpsdATIELSFpasTGAPGAPHPFHLHGHTFAVVRSAGST 438
Cdd:COG2132 315 GYVWTINGKAFDP--DRPDLTVKLG-------------------ERERWTL---VNDTMMPHPFHLHGHQFQVLSRNGKP 370

                       410       420       430       440       450
                ....*....|....*....|....*....|....*....|....*....|....*...
gi 56785438 439 EynyDNPIWRDVVSTGtpqAGDNVTIRFRTDN-PGPWFLHCHIDFHLEAG----FAVV 491
Cdd:COG2132 371 P---PEGGWKDTVLVP---PGETVRILFRFDNyPGDWMFHCHILEHEDAGmmgqFEVV 422
Cu-oxidase pfam00394
Multicopper oxidase; Many of the proteins in this family contain multiple similar copies of ...
 167-307 1.72e-55

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: 182.13  E-value: 1.72e-55
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56785438   167 DDTVITLADWYHVAAK-----------LGPAFPPRSDATLINGlgrtsdTPNADLAVITVTTGKRYRFRLISLSCDPAYT 235
Cdd:pfam00394   1 EDYVITLSDWYHKDAKdlekellasgkAPTDFPPVPDAVLING------KDGASLATLTVTPGKTYRLRIINVALDDSLN 74

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 56785438   236 FSIDNHDMTIIEADGVNTQQLTVDSLQIFAGQRYSFVLEANQKSGNYWVRANPLfgTTGFAGGINSAILRYD 307
Cdd:pfam00394  75 FSIEGHKMTVVEVDGVYVNPFTVDSLDIFPGQRYSVLVTANQDPGNYWIVASPN--IPAFDNGTAAAILRYS 144
Cu-oxidase_3 pfam07732
Multicopper oxidase; This entry contains many divergent copper oxidase-like domains that are ...
 34-156 3.07e-48

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: 162.41  E-value: 3.07e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56785438    34 TISNENVSPDGFTRAAVVA-NGKAPGPLITGQKGDRFQINVVNKLSNhtmlkSTSIHWHGFFQKGTNWADGPAFVNQCPI 112
Cdd:pfam07732   1 TVTYGTVSPLGGTRQAVIGvNGQFPGPTIRVREGDTVVVNVTNNLDE-----PTSIHWHGLQQRGTPWMDGVPGVTQCPI 75

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 56785438   113 ATGHSFLYDFQVPDQAGTFWYHSHLSTQYCDGLRGPFVVYDPND 156
Cdd:pfam07732  76 PPGQSFTYRFQVKQQAGTYWYHSHTSGQQAAGLAGAIIIEDRAS 119
Cu-oxidase_2 pfam07731
Multicopper oxidase; This entry contains many divergent copper oxidase-like domains that are ...
 371-498 6.53e-37

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: 132.94  E-value: 6.53e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56785438   371 PPTTPVLLQILSGAQDAKDLLPSG-------DVYALPSDATIELSFPASTGAPgapHPFHLHGHTFAVVRS-------AG 436
Cdd:pfam07731   3 PPKLPTLLQITSGNFRRNDWAINGllfppntNVITLPYGTVVEWVLQNTTTGV---HPFHLHGHSFQVLGRgggpwpeED 79

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 56785438   437 STEYNYDNPIWRDVVSTGtpqAGDNVTIRFRTDNPGPWFLHCHIDFHLEAGFAVVMAEDIPD 498
Cdd:pfam07731  80 PKTYNLVDPVRRDTVQVP---PGGWVAIRFRADNPGVWLFHCHILWHLDQGMMGQFVVRPGD 138
PLN02354 PLN02354
copper ion binding / oxidoreductase
 40-314 6.16e-32

copper ion binding / oxidoreductase


Pssm-ID: 177987 [Multi-domain]  Cd Length: 552  Bit Score: 128.75  E-value: 6.16e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56785438   40 VSPDGFTRAAVVANGKAPGPLITGQKGDRFQINVVNKLsNHTMLkstsIHWHGFFQKGTNWADGPAFVNqCPIATGHSFL 119
Cdd:PLN02354  39 ASPLGVPQQVILINGQFPGPNINSTSNNNIVINVFNNL-DEPFL----LTWSGIQQRKNSWQDGVPGTN-CPIPPGTNFT 112

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56785438  120 YDFQVPDQAGTFWYHSHLSTQYCDGLRGPFVVydpndpNASL-----YDVDNDDTVITLADWY---HVAAK--------L 183
Cdd:PLN02354 113 YHFQPKDQIGSYFYYPSTGMHRAAGGFGGLRV------NSRLlipvpYADPEDDYTVLIGDWYtksHTALKkfldsgrtL 186

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56785438  184 GpafppRSDATLINGLGRTSDTPNADLavITVTTGKRYRFRLISLSCDPAYTFSIDNHDMTIIEADGVNTQQLTVDSLQI 263
Cdd:PLN02354 187 G-----RPDGVLINGKSGKGDGKDEPL--FTMKPGKTYRYRICNVGLKSSLNFRIQGHKMKLVEMEGSHVLQNDYDSLDV 259

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|..
gi 56785438  264 FAGQRYSFVLEANQKSGNYWVRANPLFGTTGFAGginSAILRYDDA-VPAEP 314
Cdd:PLN02354 260 HVGQCFSVLVTANQAPKDYYMVASTRFLKKVLTT---TGIIRYEGGkGPASP 308
 
Name Accession Description Interval E-value
CuRO_1_Tv-LCC_like cd13856
The first cupredoxin domain of fungal laccases similar to Tv-LCC from Trametes versicolor; ...
 29-153 1.34e-83

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: 254.18  E-value: 1.34e-83
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56785438  29 PVTDLTISNENVSPDGFTRAAVVANGKAPGPLITGQKGDRFQINVVNKLSNHTMLKSTSIHWHGFFQKGTNWADGPAFVN 108
Cdd:cd13856   1 PTYTLNIVNTRLAPDGFERSAVLANGQFPGPLITANKGDTFRITVVNQLTDPTMRRSTSIHWHGIFQHGTNYADGPAFVT 80

                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*
gi 56785438 109 QCPIATGHSFLYDFQVPDQAGTFWYHSHLSTQYCDGLRGPFVVYD 153
Cdd:cd13856  81 QCPIAPNHSFTYDFTAGDQAGTFWYHSHLSTQYCDGLRGPLVIYD 125
CuRO_3_Tv-LCC_like cd13903
The third cupredoxin domain of the fungal laccases similar to Tv-LCC from Trametes Versicolor; ...
 348-496 1.40e-79

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: 244.50  E-value: 1.40e-79
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56785438 348 DKAINFAFTFNGTN--FFINGATFQPPTTPVLLQILSGAQDAKDLLPSGDVYALPSDATIELSFPAstGAPGAPHPFHLH 425
Cdd:cd13903   1 DVNITLTFGLNGTTglFTINGVSYVSPTVPVLLQILSGATSAEDLLPTESTIILPRNKVVEITIPG--GAIGGPHPFHLH 78

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 56785438 426 GHTFAVVRSAGSTEYNYDNPIWRDVVSTGTPqaGDNVTIRFRTDNPGPWFLHCHIDFHLEAGFAVVMAEDI 496
Cdd:cd13903  79 GHAFSVVRSAGSNTYNYVNPVRRDVVSVGTP--GDGVTIRFVTDNPGPWFLHCHIDWHLEAGLAVVFAEDP 147
CuRO_2_Tv-LCC_like cd13882
The second cupredoxin domain of the fungal laccases similar to Tv-LCC from Trametes versicolor; ...
 169-321 1.58e-77

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: 240.00  E-value: 1.58e-77
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56785438 169 TVITLADWYHVAAKLGPA----FPPRSDATLINGLGRTSDTPNADLAVITVTTGKRYRFRLISLSCDPAYTFSIDNHDMT 244
Cdd:cd13882   1 TVITLGDWYHTAAPDLLAttagVPPVPDSGTINGKGRFDGGPTSPLAVINVKRGKRYRFRVINISCIPSFTFSIDGHNLT 80

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 56785438 245 IIEADGVNTQQLTVDSLQIFAGQRYSFVLEANQKSGNYWVRANPLFGTTGFAGGI-NSAILRYDDAVPAEPTSEQGTS 321
Cdd:cd13882  81 VIEADGVETKPLTVDSVQIYAGQRYSVVVEANQPVDNYWIRAPPTGGTPANNGGQlNRAILRYKGAPEVEPTTESTAG 158
ascorbase TIGR03388
L-ascorbate oxidase, plant type; Members of this protein family are the copper-containing ...
 35-496 6.25e-76

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: 248.51  E-value: 6.25e-76
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56785438    35 ISNENVSPDGFTRAAVVANGKAPGPLITGQKGDRFQINVVNKLsnHTmlKSTSIHWHGFFQKGTNWADGPAFVNQCPIAT 114
Cdd:TIGR03388   8 VEYEFWSPDCFEKLVIGINGQFPGPTIRAQAGDTIVVELTNKL--HT--EGVVIHWHGIRQIGTPWADGTAGVTQCAINP 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56785438   115 GHSFLYDFQVpDQAGTFWYHSHLSTQYCDGLRGPFVVyDPNDPNASLYDVDNDDTVItLADWYHVAA---KLGPAFPP-- 189
Cdd:TIGR03388  84 GETFIYNFVV-DRPGTYFYHGHYGMQRSAGLYGSLIV-DVPDGEKEPFHYDGEFNLL-LSDWWHKSIheqEVGLSSKPmr 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56785438   190 ---RSDATLINGLGR-------TSDTPNADL-----------AVITVTTGKRYRFRLISLSCDPAYTFSIDNHDMTIIEA 248
Cdd:TIGR03388 161 wigEPQSLLINGRGQfncslaaKFSSTNLPQcnlkgneqcapQILHVEPGKTYRLRIASTTALAALNFAIEGHKLTVVEA 240

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56785438   249 DGVNTQQLTVDSLQIFAGQRYSFVLEANQK-SGNYW----VRANPLFGTTGFAgginsaILRYDDAVPAE--PTSEQGT- 320
Cdd:TIGR03388 241 DGNYVEPFTVKDIDIYSGETYSVLLTTDQDpSRNYWisvgVRGRKPNTPPGLT------VLNYYPNSPSRlpPTPPPVTp 314

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56785438   321 ---STKPLKETDLHPLTAMPVPGSAVSGgvDKAINFAFTFNGTNFF----INGATFQPPTTPVLLQILSGAQDAKDLLPS 393
Cdd:TIGR03388 315 awdDFDRSKAFSLAIKAAMGSPKPPETS--DRRIVLLNTQNKINGYtkwaINNVSLTLPHTPYLGSLKYNLLNAFDQKPP 392

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56785438   394 GDVYALPSDATIELSFPASTGAPGA-------------------------PHPFHLHGHTFAVV--------RSAGSTEY 440
Cdd:TIGR03388 393 PENYPRDYDIFKPPPNPNTTTGNGIyrlkfnttvdvilqnantlngnnseTHPWHLHGHDFWVLgygegkfrPGVDEKSY 472

                         490       500       510       520       530
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 56785438   441 NYDNPIWRDVVSTgtpQAGDNVTIRFRTDNPGPWFLHCHIDFHLEAGFAVVMAEDI 496
Cdd:TIGR03388 473 NLKNPPLRNTVVI---FPYGWTALRFVADNPGVWAFHCHIEPHLHMGMGVVFAEGV 525
laccase TIGR03389
laccase, plant; Members of this protein family include the copper-containing enzyme laccase ...
 46-491 1.61e-68

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: 228.85  E-value: 1.61e-68
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56785438    46 TRAAVVANGKAPGPLITGQKGDRFQINVVNKLSNhtmlkSTSIHWHGFFQKGTNWADGPAFVNQCPIATGHSFLYDFQVP 125
Cdd:TIGR03389  21 TKSILTVNGKFPGPTLYAREGDTVIVNVTNNVQY-----NVTIHWHGVRQLRNGWADGPAYITQCPIQPGQSYVYNFTIT 95

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56785438   126 DQAGTFWYHSHLS----TQYcdglrGPFVVYdPNDPNASLYDVDNDDTVITLADWY-----HV---AAKLGPAfPPRSDA 193
Cdd:TIGR03389  96 GQRGTLWWHAHISwlraTVY-----GAIVIL-PKPGVPYPFPKPDREVPIILGEWWnadveAVinqANQTGGA-PNVSDA 168

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56785438   194 TLINGL-GRTSDTPNADLAVITVTTGKRYRFRLISLSCDPAYTFSIDNHDMTIIEADGVNTQQLTVDSLQIFAGQRYSFV 272
Cdd:TIGR03389 169 YTINGHpGPLYNCSSKDTFKLTVEPGKTYLLRIINAALNDELFFAIANHTLTVVEVDATYTKPFKTKTIVIGPGQTTNVL 248

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56785438   273 LEANQKSGNYWVRANPLFGTTG-FAGGINSAILRYDDAVPAEPTSEqgTSTKPLKETD--------LHPLTAMPVPGSaV 343
Cdd:TIGR03389 249 LTADQSPGRYFMAARPYMDAPGaFDNTTTTAILQYKGTSNSAKPIL--PTLPAYNDTAaatnfsnkLRSLNSAQYPAN-V 325

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56785438   344 SGGVDKaiNFAFTF---------------NGTNFF--INGATFQPPTTPvLLQI----------------------LSGA 384
Cdd:TIGR03389 326 PVTIDR--RLFFTIglgldpcpnntcqgpNGTRFAasMNNISFVMPTTA-LLQAhyfgisgvfttdfpanpptkfnYTGT 402

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56785438   385 QDAKDLLPSG--DVYALPSDATIELSFPASTGAPGAPHPFHLHGHTFAVV--------RSAGSTEYNYDNPIWRDVVstG 454
Cdd:TIGR03389 403 NLPNNLFTTNgtKVVRLKFNSTVELVLQDTSILGSENHPIHLHGYNFFVVgtgfgnfdPKKDPAKFNLVDPPERNTV--G 480

                         490       500       510
                  ....*....|....*....|....*....|....*..
gi 56785438   455 TPQAGdNVTIRFRTDNPGPWFLHCHIDFHLEAGFAVV 491
Cdd:TIGR03389 481 VPTGG-WAAIRFVADNPGVWFMHCHLEVHTTWGLKMA 516
PLN02604 PLN02604
oxidoreductase
 38-496 2.20e-67

oxidoreductase


Pssm-ID: 215324 [Multi-domain]  Cd Length: 566  Bit Score: 226.66  E-value: 2.20e-67
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56785438   38 ENVSPDGFTRAAVVANGKAPGPLITGQKGDrfqiNVVNKLSNHTMLKSTSIHWHGFFQKGTNWADGPAFVNQCPIATGHS 117
Cdd:PLN02604  34 EYKSPDCFKKLVITINGRSPGPTILAQQGD----TVIVELKNSLLTENVAIHWHGIRQIGTPWFDGTEGVTQCPILPGET 109

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56785438  118 FLYDFQVpDQAGTFWYHSHLSTQYCDGLRGPFVVYDPN-DPNASLYDVDNDdtvITLADWYHVAA---KLGPAFPP---- 189
Cdd:PLN02604 110 FTYEFVV-DRPGTYLYHAHYGMQREAGLYGSIRVSLPRgKSEPFSYDYDRS---IILTDWYHKSTyeqALGLSSIPfdwv 185

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56785438  190 -RSDATLINGLGR----------------TSDTPNADLAVITVTTGKRYRFRLISLSCDPAYTFSIDNHDMTIIEADGVN 252
Cdd:PLN02604 186 gEPQSLLIQGKGRyncslvsspylkagvcNATNPECSPYVLTVVPGKTYRLRISSLTALSALSFQIEGHNMTVVEADGHY 265

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56785438  253 TQQLTVDSLQIFAGQRYSFVLEANQK-SGNYWVRANPLFGTTGFAGGInsAILRYDDAVP--AEPTSEqgtSTKPLKEtD 329
Cdd:PLN02604 266 VEPFVVKNLFIYSGETYSVLVKADQDpSRNYWVTTSVVSRNNTTPPGL--AIFNYYPNHPrrSPPTVP---PSGPLWN-D 339

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56785438  330 LHPLTAMPVPGSAVSGGV-------DKAINFAFTFNGTN----FFINGATFQPPTTPVLLQILSGAQDAKDLLPSG---- 394
Cdd:PLN02604 340 VEPRLNQSLAIKARHGYIhpppltsDRVIVLLNTQNEVNgyrrWSVNNVSFNLPHTPYLIALKENLTGAFDQTPPPegyd 419

                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56785438  395 ----DVYALP-------SDATIELSF---------PASTGAP--GAPHPFHLHGHTFAVV--------RSAGSTEYNYDN 444
Cdd:PLN02604 420 fanyDIYAKPnnsnatsSDSIYRLQFnstvdiilqNANTMNAnnSETHPWHLHGHDFWVLgygegkfnMSSDPKKYNLVD 499

                        490       500       510       520       530
                 ....*....|....*....|....*....|....*....|....*....|..
gi 56785438  445 PIWRDVVSTgtpQAGDNVTIRFRTDNPGPWFLHCHIDFHLEAGFAVVMAEDI 496
Cdd:PLN02604 500 PIMKNTVPV---HPYGWTALRFRADNPGVWAFHCHIESHFFMGMGVVFEEGI 548
SufI COG2132
Multicopper oxidase with three cupredoxin domains (includes cell division protein FtsP and ...
 53-491 2.99e-65

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: 217.11  E-value: 2.99e-65
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56785438  53 NGKAPGPLITGQKGDRFQINVVNKLSNHTmlkstSIHWHGFFQKGTNwaDGPAFVnqcPIATGHSFLYDFQVPDQAGTFW 132
Cdd:COG2132  39 NGQYPGPTIRVREGDRVRVRVTNRLPEPT-----TVHWHGLRVPNAM--DGVPGD---PIAPGETFTYEFPVPQPAGTYW 108

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56785438 133 YHSHL----STQYCDGLRGPFVVYDPNDPnasLYDVDnDDTVITLADW-----YHVAAKLGPAFPPRS-DATLINGlgrt 202
Cdd:COG2132 109 YHPHThgstAEQVYRGLAGALIVEDPEED---LPRYD-RDIPLVLQDWrldddGQLLYPMDAAMGGRLgDTLLVNG---- 180

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56785438 203 sdtpnADLAVITVTTGKRYRFRLISLSCDPAYTFSI-DNHDMTIIEADGVNTQQ-LTVDSLQIFAGQRYSFVLEANQKSG 280
Cdd:COG2132 181 -----RPNPTLEVRPGERVRLRLLNASNARIYRLALsDGRPFTVIATDGGLLPApVEVDELLLAPGERADVLVDFSADPG 255

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56785438 281 NYWVRANPLFGTTGFAGginsAILRYDDAVPAEPTSEQGTSTKPLKETDlhpltampvpgsavsggVDKAINFAFTFN-- 358
Cdd:COG2132 256 EEVTLANPFEGRSGRAL----LTLRVTGAAASAPLPANLAPLPDLEDRE-----------------AVRTRELVLTGGma 314

                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56785438 359 GTNFFINGATFQPptTPVLLQILSGaqdakdllpsgdvyalpsdATIELSFpasTGAPGAPHPFHLHGHTFAVVRSAGST 438
Cdd:COG2132 315 GYVWTINGKAFDP--DRPDLTVKLG-------------------ERERWTL---VNDTMMPHPFHLHGHQFQVLSRNGKP 370

                       410       420       430       440       450
                ....*....|....*....|....*....|....*....|....*....|....*...
gi 56785438 439 EynyDNPIWRDVVSTGtpqAGDNVTIRFRTDN-PGPWFLHCHIDFHLEAG----FAVV 491
Cdd:COG2132 371 P---PEGGWKDTVLVP---PGETVRILFRFDNyPGDWMFHCHILEHEDAGmmgqFEVV 422
PLN02191 PLN02191
L-ascorbate oxidase
 41-501 1.07e-63

L-ascorbate oxidase


Pssm-ID: 177843 [Multi-domain]  Cd Length: 574  Bit Score: 217.19  E-value: 1.07e-63
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56785438   41 SPDGFTRAAVVANGKAPGPLITGQKGDRFQINVVNKLSNHTMLkstsIHWHGFFQKGTNWADGPAFVNQCPIATGHSFLY 120
Cdd:PLN02191  36 WPDCKEGAVMTVNGQFPGPTIDAVAGDTIVVHLTNKLTTEGLV----IHWHGIRQKGSPWADGAAGVTQCAINPGETFTY 111

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56785438  121 DFQVpDQAGTFWYHSHLSTQYCDGLRGPFVVYDPNDPNASL-YDVDNDdtvITLADWYHV---AAKLGPAFPP-----RS 191
Cdd:PLN02191 112 KFTV-EKPGTHFYHGHYGMQRSAGLYGSLIVDVAKGPKERLrYDGEFN---LLLSDWWHEsipSQELGLSSKPmrwigEA 187

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56785438  192 DATLINGLGR------TSDTPNADLAVIT-------------VTTGKRYRFRLISLSCDPAYTFSIDNHDMTIIEADGVN 252
Cdd:PLN02191 188 QSILINGRGQfncslaAQFSNGTELPMCTfkegdqcapqtlrVEPNKTYRIRLASTTALASLNLAVQGHKLVVVEADGNY 267

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56785438  253 TQQLTVDSLQIFAGQRYSFVLEANQ-KSGNYWVRAnplfGTTGFAGGINSA--ILRYDDAVPAEPTSEQGTSTKPLKETD 329
Cdd:PLN02191 268 ITPFTTDDIDIYSGESYSVLLTTDQdPSQNYYISV----GVRGRKPNTTQAltILNYVTAPASKLPSSPPPVTPRWDDFE 343

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56785438  330 LHP------LTAMPVPgSAVSGGVDKAI--NFAFTFNG-TNFFINGATFQPPTTPVLLQILSGAQDAKDLLPSGDVYALP 400
Cdd:PLN02191 344 RSKnfskkiFSAMGSP-SPPKKYRKRLIllNTQNLIDGyTKWAINNVSLVTPATPYLGSVKYNLKLGFNRKSPPRSYRMD 422

                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56785438  401 SDATIELSFPASTGAPG-------------------------APHPFHLHGHTFAVVR------SAGSTE--YNYDNPIW 447
Cdd:PLN02191 423 YDIMNPPPFPNTTTGNGiyvfpfnvtvdviiqnanvlkgvvsEIHPWHLHGHDFWVLGygdgkfKPGIDEktYNLKNPPL 502

                        490       500       510       520       530       540
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 56785438  448 RDVVSTgTPQAGdnVTIRFRTDNPGPWFLHCHIDFHLEAGFAVVMAE------DIPDTKL 501
Cdd:PLN02191 503 RNTAIL-YPYGW--TAIRFVTDNPGVWFFHCHIEPHLHMGMGVVFAEglnrigKIPDEAL 559
Cu-oxidase pfam00394
Multicopper oxidase; Many of the proteins in this family contain multiple similar copies of ...
 167-307 1.72e-55

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: 182.13  E-value: 1.72e-55
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56785438   167 DDTVITLADWYHVAAK-----------LGPAFPPRSDATLINGlgrtsdTPNADLAVITVTTGKRYRFRLISLSCDPAYT 235
Cdd:pfam00394   1 EDYVITLSDWYHKDAKdlekellasgkAPTDFPPVPDAVLING------KDGASLATLTVTPGKTYRLRIINVALDDSLN 74

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 56785438   236 FSIDNHDMTIIEADGVNTQQLTVDSLQIFAGQRYSFVLEANQKSGNYWVRANPLfgTTGFAGGINSAILRYD 307
Cdd:pfam00394  75 FSIEGHKMTVVEVDGVYVNPFTVDSLDIFPGQRYSVLVTANQDPGNYWIVASPN--IPAFDNGTAAAILRYS 144
CuRO_1_Diphenol_Ox cd13857
The first cupredoxin domain of fungal laccase, diphenol oxidase; Diphenol oxidase belongs to ...
 32-152 4.50e-50

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: 167.05  E-value: 4.50e-50
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56785438  32 DLTISNENVSPDGFTRAAVVANGKAPGPLITGQKGDRFQINVVNKLSNhtmlkSTSIHWHGFFQKGTNWADGPAFVNQCP 111
Cdd:cd13857   4 NFTISEITGAPDGFVRPMLVINGQFPGPLIEANQGDRIVVHVTNELDE-----PTSIHWHGLFQNGTNWMDGTAGITQCP 78

                        90       100       110       120
                ....*....|....*....|....*....|....*....|.
gi 56785438 112 IATGHSFLYDFQVPDQAGTFWYHSHLSTQYCDGLRGPFVVY 152
Cdd:cd13857  79 IPPGGSFTYNFTVDGQYGTYWYHSHYSTQYADGLVGPLIVH 119
CuRO_1_LCC_like cd04206
Cupredoxin domain 1 of laccase-like multicopper oxidases; including laccase, CueO, spore coat ...
 32-152 2.97e-49

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: 164.77  E-value: 2.97e-49
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56785438  32 DLTISNENVSPDGFTRAAVVANGKAPGPLITGQKGDRFQINVVNKLSNhtmlKSTSIHWHGFFQKGTNWADGPAFVNQCP 111
Cdd:cd04206   4 ELTITETTVNPDGVLRQVITVNGQFPGPTIRVKEGDTVEVTVTNNLPN----EPTSIHWHGLRQPGTNDGDGVAGLTQCP 79

                        90       100       110       120
                ....*....|....*....|....*....|....*....|.
gi 56785438 112 IATGHSFLYDFQVPDQAGTFWYHSHLSTQYCDGLRGPFVVY 152
Cdd:cd04206  80 IPPGESFTYRFTVDDQAGTFWYHSHVGGQRADGLYGPLIVE 120
ascorbOXfungal TIGR03390
L-ascorbate oxidase, fungal type; This model describes a family of fungal ascorbate oxidases, ...
 33-496 5.55e-49

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: 176.57  E-value: 5.55e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56785438    33 LTISNENVSPDGFTRAAVVANGKAPGPLITGQKGDRFQINVVNKLSNhtmlKSTSIHWHGFFQKGTNWADGPAFVNQCPI 112
Cdd:TIGR03390  13 LRVTSDNIKIACSSRYSVVVNGTSPGPEIRLQEGQTTWIRVYNDIPD----NNVTMHWHGLTQRTAPFSDGTPLASQWPI 88

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56785438   113 ATGHSFLYDFQV-PDQAGTFWYHSHLSTQYCDGlRGPFVVYDPNDPNaslYDVDnDDTVITLADWYH------VAAKLGP 185
Cdd:TIGR03390  89 PPGHFFDYEIKPePGDAGSYFYHSHVGFQAVTA-FGPLIVEDCEPPP---YKYD-DERILLVSDFFSatdeeiEQGLLST 163

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56785438   186 AF--PPRSDATLINGLGR-------TSDTPNADLAVITVTTGKRYRFRLISLSCDPAYTFSIDNHD-MTIIEADGVNTQQ 255
Cdd:TIGR03390 164 PFtwSGETEAVLLNGKSGnksfyaqINPSGSCMLPVIDVEPGKTYRLRFIGATALSLISLGIEDHEnLTIIEADGSYTKP 243

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56785438   256 LTVDSLQIFAGQRYSFVLEANQ----KSGN---YWVRANPLFGTTGFAGginSAILRYDD-------AVPAEPTSEQGTS 321
Cdd:TIGR03390 244 AKIDHLQLGGGQRYSVLFKAKTedelCGGDkrqYFIQFETRDRPKVYRG---YAVLRYRSdkasklpSVPETPPLPLPNS 320

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56785438   322 TKPLKETDLHPLTAMPVPGSAVSGGVDKAI------NFAFTFNGTNFFINGATFQP--PTTPVLLQILSGAQDA-----K 388
Cdd:TIGR03390 321 TYDWLEYELEPLSEENNQDFPTLDEVTRRVvidahqNVDPLNGRVAWLQNGLSWTEsvRQTPYLVDIYENGLPAtpnytA 400

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56785438   389 DLLPSG---DVYALPS--DATIELSF---PASTGAPGA--PHPFHLHGHTFAVVRSaGSTEYNYD---------NPIWRD 449
Cdd:TIGR03390 401 ALANYGfdpETRAFPAkvGEVLEIVWqntGSYTGPNGGvdTHPFHAHGRHFYDIGG-GDGEYNATaneaklenyTPVLRD 479

                         490       500       510       520       530
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 56785438   450 VV------STGTPQAGDN-VTIRFRTDNPGPWFLHCHIDFHLEAGFAVVM----AEDI 496
Cdd:TIGR03390 480 TTmlyryaVKVVPGAPAGwRAWRIRVTNPGVWMMHCHILQHMVMGMQTVWvfgdAEDI 537
Cu-oxidase_3 pfam07732
Multicopper oxidase; This entry contains many divergent copper oxidase-like domains that are ...
 34-156 3.07e-48

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: 162.41  E-value: 3.07e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56785438    34 TISNENVSPDGFTRAAVVA-NGKAPGPLITGQKGDRFQINVVNKLSNhtmlkSTSIHWHGFFQKGTNWADGPAFVNQCPI 112
Cdd:pfam07732   1 TVTYGTVSPLGGTRQAVIGvNGQFPGPTIRVREGDTVVVNVTNNLDE-----PTSIHWHGLQQRGTPWMDGVPGVTQCPI 75

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 56785438   113 ATGHSFLYDFQVPDQAGTFWYHSHLSTQYCDGLRGPFVVYDPND 156
Cdd:pfam07732  76 PPGQSFTYRFQVKQQAGTYWYHSHTSGQQAAGLAGAIIIEDRAS 119
CuRO_1_Fet3p cd13851
The first Cupredoxin domain of multicopper oxidase Fet3P; Fet3p catalyzes the ferroxidase ...
 32-151 8.04e-46

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: 155.89  E-value: 8.04e-46
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56785438  32 DLTISNENVSPDG-FTRAAVVANGKAPGPLITGQKGDRFQINVVNKLSNhtmlKSTSIHWHGFFQKGTNWADGPAFVNQC 110
Cdd:cd13851   4 DWNITWVTANPDGlFERRVIGINGQWPPPPIEVNKGDTVVIHATNSLGD----QPTSLHFHGLFQNGTNYMDGPVGVTQC 79

                        90       100       110       120
                ....*....|....*....|....*....|....*....|.
gi 56785438 111 PIATGHSFLYDFQVPDQAGTFWYHSHLSTQYCDGLRGPFVV 151
Cdd:cd13851  80 PIPPGQSFTYEFTVDTQVGTYWYHSHDGGQYPDGLRGPFII 120
CuRO_1_MaLCC_like cd13854
The first cupredoxin domain of the fungal laccases similar to Ma-LCC from Melanocarpus ...
 32-152 6.10e-44

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: 150.86  E-value: 6.10e-44
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56785438  32 DLTISNENVSPDGFTRAAVVANGKAPGPLITGQKGDRFQINVVNKLSNHtmlkSTSIHWHGFFQKGTNWADGPAFVNQCP 111
Cdd:cd13854   7 TLTITNSTLAPDGVEKEVMLINGQYPGPLIEANWGDTIEVTVINKLQDN----GTSIHWHGIRQLNTNWQDGVPGVTECP 82

                        90       100       110       120
                ....*....|....*....|....*....|....*....|.
gi 56785438 112 IATGHSFLYDFQVpDQAGTFWYHSHLSTQYCDGLRGPFVVY 152
Cdd:cd13854  83 IAPGDTRTYRFRA-TQYGTSWYHSHYSAQYGDGVVGPIVIH 122
CuRO_1_tcLCC2_insect_like cd13858
The first cupredoxin domain of insect laccases similar to laccase 2 in Tribolium castaneum; ...
 43-151 2.82e-42

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: 145.76  E-value: 2.82e-42
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56785438  43 DGFTRAAVVANGKAPGPLITGQKGDRFQINVVNKLSNHtmlkSTSIHWHGFFQKGTNWADGPAFVNQCPIATGHSFLYDF 122
Cdd:cd13858   1 DGVERPVITVNGQLPGPSIEVCEGDTVVVDVKNRLPGE----STTIHWHGIHQRGTPYMDGVPMVTQCPILPGQTFRYKF 76

                        90       100
                ....*....|....*....|....*....
gi 56785438 123 QVpDQAGTFWYHSHLSTQYCDGLRGPFVV 151
Cdd:cd13858  77 KA-DPAGTHWYHSHSGTQRADGLFGALIV 104
CuRO_2_tcLCC_insect_like cd13884
The second cupredoxin domain of the insect laccases similar to laccase 2 in Tribolium ...
 170-306 1.09e-41

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: 145.84  E-value: 1.09e-41
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56785438 170 VITLADWYH------VAAKLGPAFPPRSDATLINGLGR-----TSDTPNADLAVITVTTGKRYRFRLIS---LSCdpAYT 235
Cdd:cd13884   3 VILIQDWTHelsserFVGRGHNGGGQPPDSILINGKGRyydpkTGNTNNTPLEVFTVEQGKRYRFRLINagaTNC--PFR 80

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 56785438 236 FSIDNHDMTIIEADGVNTQQLTVDSLQIFAGQRYSFVLEANQKSGNYWVRANPLfGTTGFAGGINSAILRY 306
Cdd:cd13884  81 VSIDGHTLTVIASDGNDVEPVEVDSIIIYPGERYDFVLNANQPIGNYWIRARGL-EDCDNRRLQQLAILRY 150
CuRO_2_LCC_like cd04205
Cupredoxin domain 2 of laccase-like multicopper oxidases; including laccase, CueO, spore coat ...
 170-306 1.67e-38

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: 137.49  E-value: 1.67e-38
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56785438 170 VITLADWYHVAAKLGPAF--------PPRSDATLINGLGR-----TSDTPNADLAVITVTTGKRYRFRLISLSCDPAYTF 236
Cdd:cd04205   2 VLLLSDWYHDSAEDVLAGympnsfgnEPVPDSLLINGRGRfncsmAVCNSGCPLPVITVEPGKTYRLRLINAGSFASFNF 81

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 56785438 237 SIDNHDMTIIEADGVNTQQLTVDSLQIFAGQRYSFVLEANQKSGNYWVRANPLFGT-TGFAGGINSAILRY 306
Cdd:cd04205  82 AIDGHNMTVIEVDGGYVEPLEVDNLDLAPGQRYDVLVKADQPPGNYWIRASADGRTfDEGGNPNGTAILRY 152
CuRO_2_MaLCC_like cd13880
The second cupredoxin domain of the fungal laccases similar to Ma-LCC from Melanocarpus ...
 170-322 2.12e-37

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: 135.07  E-value: 2.12e-37
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56785438 170 VITLADWYH------VAAKLGPAFPPRSDATLINGLGR-TSDTPNADLAVITVTTGKRYRFRLISLSCDPAYTFSIDNHD 242
Cdd:cd13880   3 PVLLTDWYHrsafelFSEELPTGGPPPMDNILINGKGKfPCSTGAGSYFETTFTPGKKYRLRLINTGVDTTFRFSIDGHN 82

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56785438 243 MTIIEADGVNTQQLTVDSLQIFAGQRYSFVLEANQ-KSGNYWVRANPLfgtTGFAGGINS-----AILRYDDAVPAEPTS 316
Cdd:cd13880  83 LTVIAADFVPIVPYTTDSLNIGIGQRYDVIVEANQdPVGNYWIRAEPA---TGCSGTNNNpdnrtGILRYDGASPTLDPS 159


                ....*.
gi 56785438 317 EQGTST 322
Cdd:cd13880 160 STANVT 165
PLN02792 PLN02792
oxidoreductase
 39-476 2.34e-37

oxidoreductase


Pssm-ID: 178389 [Multi-domain]  Cd Length: 536  Bit Score: 144.35  E-value: 2.34e-37
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56785438   39 NVSPDGFTRAAVVANGKAPGPLITGQKGDRFQINVVNKLSNHTMLKstsihWHGFFQKGTNWADGpAFVNQCPIATGHSF 118
Cdd:PLN02792  27 NISLLTLPRRGILINGQFPGPEIRSLTNDNLVINVHNDLDEPFLLS-----WNGVHMRKNSYQDG-VYGTTCPIPPGKNY 100

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56785438  119 LYDFQVPDQAGTFWYHSHLSTQYCDGLRGPFVVYD-PNDPNAslYDVDNDDTVITLADWY---HVAAKL----GPAFPPR 190
Cdd:PLN02792 101 TYDFQVKDQVGSYFYFPSLAVQKAAGGYGSLRIYSlPRIPVP--FPEPAGDFTFLIGDWYrrnHTTLKKildgGRKLPLM 178

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56785438  191 SDATLINGLGRTSdtpnadLAVITVTTGKRYRFRLISLSCDPAYTFSIDNHDMTIIEADGVNTQQLTVDSLQIFAGQRYS 270
Cdd:PLN02792 179 PDGVMINGQGVSY------VYSITVDKGKTYRFRISNVGLQTSLNFEILGHQLKLIEVEGTHTVQSMYTSLDIHVGQTYS 252

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56785438  271 FVLEANQKSGNY-------WVRANPLFGTT---GFAGGINSAILRYDDAVPAEPTSEQGTSTKplkeTDLHPLTAMPVP- 339
Cdd:PLN02792 253 VLVTMDQPPQNYsivvstrFIAAKVLVSSTlhySNSKGHKIIHARQPDPDDLEWSIKQAQSIR----TNLTASGPRTNPq 328

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56785438  340 GSAVSGGVDKAINF------AFTFNGTNFFINGATFQPPTTPVLlqiLSGAQDAKDLLPSGDVYALPSDATielSFPAST 413
Cdd:PLN02792 329 GSYHYGKMKISRTLilessaALVKRKQRYAINGVSFVPSDTPLK---LADHFKIKGVFKVGSIPDKPRRGG---GMRLDT 402

                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56785438  414 GAPGAPH----------------PFHLHGHTFAVV-------RSAGSTEYNYdnpiwRDVVSTGTPQAGDN--VTIRFRT 468
Cdd:PLN02792 403 SVMGAHHnafleiifqnrekivqSYHLDGYNFWVVginkgiwSRASRREYNL-----KDAISRSTTQVYPEswTAVYVAL 477


                 ....*...
gi 56785438  469 DNPGPWFL 476
Cdd:PLN02792 478 DNVGMWNL 485
Cu-oxidase_2 pfam07731
Multicopper oxidase; This entry contains many divergent copper oxidase-like domains that are ...
 371-498 6.53e-37

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: 132.94  E-value: 6.53e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56785438   371 PPTTPVLLQILSGAQDAKDLLPSG-------DVYALPSDATIELSFPASTGAPgapHPFHLHGHTFAVVRS-------AG 436
Cdd:pfam07731   3 PPKLPTLLQITSGNFRRNDWAINGllfppntNVITLPYGTVVEWVLQNTTTGV---HPFHLHGHSFQVLGRgggpwpeED 79

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 56785438   437 STEYNYDNPIWRDVVSTGtpqAGDNVTIRFRTDNPGPWFLHCHIDFHLEAGFAVVMAEDIPD 498
Cdd:pfam07731  80 PKTYNLVDPVRRDTVQVP---PGGWVAIRFRADNPGVWLFHCHILWHLDQGMMGQFVVRPGD 138
CuRO_1_Abr2_like cd13850
The first cupredoxin domain of a group of fungal Laccases similar to Abr2 from Aspergillus ...
 32-151 4.36e-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: 124.33  E-value: 4.36e-34
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56785438  32 DLTISNENVSPDGFTRAAVVANGKAPGPLITGQKGDRFQINVVNKLSnhtmlKSTSIHWHGFFQKGTNWADGPAFVNQCP 111
Cdd:cd13850   2 TLTVTEGSPDGDGGEREVILINGQFPGPPIILDEGDEVEILVTNNLP-----VNTTIHFHGILQRGTPWSDGVPGVTQWP 76

                        90       100       110       120
                ....*....|....*....|....*....|....*....|
gi 56785438 112 IATGHSFLYDFQVPDQAGTFWYHSHLSTQYCDGLRGPFVV 151
Cdd:cd13850  77 IQPGGSFTYRWKAEDQYGLYWYHSHYRGYYMDGLYGPIYI 116
CuRO_3_Fet3p cd13899
The third Cupredoxin domain of multicopper oxidase Fet3p; Fet3p catalyzes the ferroxidase ...
 351-495 3.47e-32

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: 120.82  E-value: 3.47e-32
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56785438 351 INFAFTFNGTN-FFINGATFQPPTTPVLLQILSGAQDAKD---LLPSGDVYALPSDATIELS-FPASTGapgaPHPFHLH 425
Cdd:cd13899   8 VDFDTFDDGVNrAAFNNITYVSPKVPTLYTALSMGDDALDpaiYGPQTNAFVLNHGEVVELVvNNWDAG----KHPFHLH 83

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 56785438 426 GHTFAVV-RSAGSTEY--------NYDNPIWRDVVSTgtpQAGDNVTIRFRTDNPGPWFLHCHIDFHLEAGFAVVMAED 495
Cdd:cd13899  84 GHKFQVVqRSPDVASDdpnppineFPENPMRRDTVMV---PPGGSVVIRFRADNPGVWFFHCHIEWHLEAGLAATFIEA 159
CuRO_1_LCC_plant cd13849
The first cupredoxin domain of plant laccases; Laccase is a blue multicopper oxidase (MCO) ...
 32-153 3.78e-32

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: 119.29  E-value: 3.78e-32
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56785438  32 DLTISNENVSPDGFTRAAVVANGKAPGPLITGQKGDRFQINVVNKlSNHTMlkstSIHWHGFFQKGTNWADGPAFVNQCP 111
Cdd:cd13849   2 TFVVQEKNVTRLCSTKSILTVNGQFPGPTIRVHEGDTVVVNVTNR-SPYNI----TIHWHGIRQLRSGWADGPAYITQCP 76

                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*.
gi 56785438 112 IATGHSFLYDFQVPDQAGTFWYHSHLS----TQYcdglrGPFVVYD 153
Cdd:cd13849  77 IQPGQSYTYRFTVTGQEGTLWWHAHISwlraTVY-----GAFIIRP 117
PLN02168 PLN02168
copper ion binding / pectinesterase
 10-378 4.69e-32

copper ion binding / pectinesterase


Pssm-ID: 215113 [Multi-domain]  Cd Length: 545  Bit Score: 129.33  E-value: 4.69e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56785438   10 FASLAVVVSLALNTLA-GIGPVT--DLTISNENVSPDGFTRAAVVANGKAPGPLITGQKGDRFQINVVNKLSNHTMLKst 86
Cdd:PLN02168   5 FVEVFVLISLVILELSyAFAPIVsyQWVVSYSQRFILGGNKQVIVINDMFPGPLLNATANDVINVNIFNNLTEPFLMT-- 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56785438   87 sihWHGFFQKGTNWADGPAFVNqCPIATGHSFLYDFQVPDQAGTFWYHSHLSTQYCDGLRGPFVVYDPNDPNASLYDVDN 166
Cdd:PLN02168  83 ---WNGLQLRKNSWQDGVRGTN-CPILPGTNWTYRFQVKDQIGSYFYFPSLLLQKAAGGYGAIRIYNPELVPVPFPKPDE 158

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56785438  167 DDTVItLADWYHVAAKLGPAFP------PRSDATLINGLGrtsdtPNAdlAVITVTTGKRYRFRLISLSCDPAYTFSIDN 240
Cdd:PLN02168 159 EYDIL-IGDWFYADHTVMRASLdnghslPNPDGILFNGRG-----PEE--TFFAFEPGKTYRLRISNVGLKTCLNFRIQD 230

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56785438  241 HDMTIIEADGVNTQQLTVDSLQIFAGQRYSFVLEA-NQKSG---NYWVRANPLFgTTGFAGGInsAILRYDDA------- 309
Cdd:PLN02168 231 HDMLLVETEGTYVQKRVYSSLDIHVGQSYSVLVTAkTDPVGiyrSYYIVATARF-TDAYLGGV--ALIRYPNSpldpvgp 307

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56785438  310 VPAEPTS-------EQGTSTKplkeTDLHPLTAMPVPGSAVSGG---VDKAI---NFAFTFNGT-NFFINGATFQPPTTP 375
Cdd:PLN02168 308 LPLAPALhdyfssvEQALSIR----MDLNVGAARSNPQGSYHYGrinVTRTIilhNDVMLSSGKlRYTINGVSFVYPGTP 383


                 ...
gi 56785438  376 VLL 378
Cdd:PLN02168 384 LKL 386
CuRO_2_MCO_like_1 cd13886
The second cupredoxin domain of uncharacterized multicopper oxidase; Multicopper Oxidases ...
 170-307 5.77e-32

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: 120.07  E-value: 5.77e-32
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56785438 170 VITLADWYH-VAAKLGPAFPPRS--------DATLINGLGR----------TSDTPNADLAVITVTTGKRYRFRLISLSC 230
Cdd:cd13886   2 VVMVNDYYHdPSSVLLARYLAPGnegdepvpDNGLINGIGQfdcasatykiYCCASNGTYYNFTLEPNKTYRLRLINAGS 81

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56785438 231 DPAYTFSIDNHDMTIIEADGVNTQQLTVDSLQIFAGQRYSFVLEANQ-KSGNYWVRA----------NPLFGTTgfaggi 299
Cdd:cd13886  82 FADFTFSVDGHPLTVIEADGTLVEPVEVHSITISVAQRYSVILTTNQpTGGNFWMRAelntdcftydNPNLDPD------ 155


                ....*...
gi 56785438 300 NSAILRYD 307
Cdd:cd13886 156 VRAIVSYT 163
PLN02354 PLN02354
copper ion binding / oxidoreductase
 40-314 6.16e-32

copper ion binding / oxidoreductase


Pssm-ID: 177987 [Multi-domain]  Cd Length: 552  Bit Score: 128.75  E-value: 6.16e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56785438   40 VSPDGFTRAAVVANGKAPGPLITGQKGDRFQINVVNKLsNHTMLkstsIHWHGFFQKGTNWADGPAFVNqCPIATGHSFL 119
Cdd:PLN02354  39 ASPLGVPQQVILINGQFPGPNINSTSNNNIVINVFNNL-DEPFL----LTWSGIQQRKNSWQDGVPGTN-CPIPPGTNFT 112

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56785438  120 YDFQVPDQAGTFWYHSHLSTQYCDGLRGPFVVydpndpNASL-----YDVDNDDTVITLADWY---HVAAK--------L 183
Cdd:PLN02354 113 YHFQPKDQIGSYFYYPSTGMHRAAGGFGGLRV------NSRLlipvpYADPEDDYTVLIGDWYtksHTALKkfldsgrtL 186

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56785438  184 GpafppRSDATLINGLGRTSDTPNADLavITVTTGKRYRFRLISLSCDPAYTFSIDNHDMTIIEADGVNTQQLTVDSLQI 263
Cdd:PLN02354 187 G-----RPDGVLINGKSGKGDGKDEPL--FTMKPGKTYRYRICNVGLKSSLNFRIQGHKMKLVEMEGSHVLQNDYDSLDV 259

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|..
gi 56785438  264 FAGQRYSFVLEANQKSGNYWVRANPLFGTTGFAGginSAILRYDDA-VPAEP 314
Cdd:PLN02354 260 HVGQCFSVLVTANQAPKDYYMVASTRFLKKVLTT---TGIIRYEGGkGPASP 308
CuRO_1_AAO cd13845
The first cupredoxin domain of plant Ascorbate oxidase; Ascorbate oxidase catalyzes the ...
 38-154 2.69e-31

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: 116.78  E-value: 2.69e-31
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56785438  38 ENVSPDGFTRAAVVANGKAPGPLITGQKGDrfqiNVVNKLSNHTMLKSTSIHWHGFFQKGTNWADGPAFVNQCPIATGHS 117
Cdd:cd13845  10 MFWAPDCVEKLVIGINGQFPGPTIRATAGD----TIVVELENKLPTEGVAIHWHGIRQRGTPWADGTASVSQCPINPGET 85

                        90       100       110
                ....*....|....*....|....*....|....*..
gi 56785438 118 FLYDFQVpDQAGTFWYHSHLSTQYCDGLRGPFVVyDP 154
Cdd:cd13845  86 FTYQFVV-DRPGTYFYHGHYGMQRSAGLYGSLIV-DP 120
CuRO_3_LCC_like cd04207
Cupredoxin domain 3 of laccase-like multicopper oxidases; including laccase, CueO, spore coat ...
 348-493 1.91e-29

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: 112.17  E-value: 1.91e-29
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56785438 348 DKAINFAFTFNG-----TNFFINGATFqppttpvllqilsgaqdaKDLLPSGDVYALPSDATIELSFPaSTGAPGAPHPF 422
Cdd:cd04207   1 DRTRRLVLSQTGapdgtTRWVINGMPF------------------KEGDANTDIFSVEAGDVVEIVLI-NAGNHDMQHPF 61

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 56785438 423 HLHGHTFAVVRSAG---STEYNYDNPIWRDVVSTGtpqAGDNVTIRFRTDNPGPWFLHCHIDFHLEAGFAVVMA 493
Cdd:cd04207  62 HLHGHSFWVLGSGGgpfDAPLNLTNPPWRDTVLVP---PGGWVVIRFKADNPGVWMLHCHILEHEDAGMMTVFE 132
PLN02991 PLN02991
oxidoreductase
 39-480 4.95e-29

oxidoreductase


Pssm-ID: 215536 [Multi-domain]  Cd Length: 543  Bit Score: 120.12  E-value: 4.95e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56785438   39 NVSPDGFTRAAVVANGKAPGPLITGQKGDRFQINVVNKLSNHTMLKSTSI-HWHGFFQKGTnwadgpaFVNQCPIATGHS 117
Cdd:PLN02991  39 NISPLGVAQQGILINGKFPGPDIISVTNDNLIINVFNHLDEPFLISWSGIrNWRNSYQDGV-------YGTTCPIPPGKN 111

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56785438  118 FLYDFQVPDQAGTFWYHSHLSTQYCDGLRGPFVVYD-PNDPNAslYDVDNDDTVITLADWYH-----VAAKLGPAFP-PR 190
Cdd:PLN02991 112 YTYALQVKDQIGSFYYFPSLGFHKAAGGFGAIRISSrPLIPVP--FPAPADDYTVLIGDWYKtnhkdLRAQLDNGGKlPL 189

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56785438  191 SDATLINGLGRTsdtpnadlAVITVTTGKRYRFRLISLSCDPAYTFSIDNHDMTIIEADGVNTQQLTVDSLQIFAGQRYS 270
Cdd:PLN02991 190 PDGILINGRGSG--------ATLNIEPGKTYRLRISNVGLQNSLNFRIQNHTMKLVEVEGTHTIQTPFSSLDVHVGQSYS 261

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56785438  271 FVLEANQKSGNYWVRANPLFGTTGFaggINSAILRYDDA-------VPAEPTS-----EQGTSTKplkeTDLHPLTAMPV 338
Cdd:PLN02991 262 VLITADQPAKDYYIVVSSRFTSKIL---ITTGVLHYSNSagpvsgpIPDGPIQlswsfDQARAIK----TNLTASGPRPN 334

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56785438  339 PGSAVSGG---VDKAINFAFTFNGTN----FFINGATFQPPTTPVLL-----------------QILSGAqdakdLLPSG 394
Cdd:PLN02991 335 PQGSYHYGkinITRTIRLANSAGNIEgkqrYAVNSASFYPADTPLKLadyfkiagvynpgsipdQPTNGA-----IFPVT 409

                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56785438  395 DVYALPSDATIELSFPASTgapGAPHPFHLHGHTFAVV-------RSAGSTEYNYDNPIWRDVVSTgTPQAGDNVTIRFr 467
Cdd:PLN02991 410 SVMQTDYKAFVEIVFENWE---DIVQTWHLDGYSFYVVgmelgkwSAASRKVYNLNDAVSRCTVQV-YPRSWTAIYVSL- 484

                        490
                 ....*....|...
gi 56785438  468 tDNPGPWFLHCHI 480
Cdd:PLN02991 485 -DNVGMWNLRSEL 496
PLN02835 PLN02835
oxidoreductase
 2-474 7.58e-27

oxidoreductase


Pssm-ID: 178429 [Multi-domain]  Cd Length: 539  Bit Score: 113.91  E-value: 7.58e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56785438    2 NGLRLLPSFASLAVVVSLALNTLAGIGPVTDLTISNENVSPDGFTRAAVVANGKAPGPLITGQKGDRFQINVVNKLSNHT 81
Cdd:PLN02835   3 SAVNLHLLLGVLAVLSSVSLVNGEDPYKYYTWTVTYGTISPLGVPQQVILINGQFPGPRLDVVTNDNIILNLINKLDQPF 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56785438   82 MLKstsihWHGFFQKGTNWADGPAFVNqCPIATGHSFLYDFQVPDQAGTFWYHSHLSTQYCDGLRGPFVVYD-PNDPNAs 160
Cdd:PLN02835  83 LLT-----WNGIKQRKNSWQDGVLGTN-CPIPPNSNYTYKFQTKDQIGTFTYFPSTLFHKAAGGFGAINVYErPRIPIP- 155

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56785438  161 lYDVDNDDTVITLADWYHVAAKLGPAFP------PRSDATLINGlgRTSDTPNADlavitvtTGKRYRFRLISLSCDPAY 234
Cdd:PLN02835 156 -FPLPDGDFTLLVGDWYKTSHKTLQQRLdsgkvlPFPDGVLING--QTQSTFSGD-------QGKTYMFRISNVGLSTSL 225

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56785438  235 TFSIDNHDMTIIEADGVNTQQLTVDSLQIFAGQRYSFVLEANQKSGNYWVRANPLFGTTGFAGginSAILRYDDA----- 309
Cdd:PLN02835 226 NFRIQGHTMKLVEVEGSHTIQNIYDSLDVHVGQSVAVLVTLNQSPKDYYIVASTRFTRQILTA---TAVLHYSNSrtpas 302

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56785438  310 --VPAEPTSEQGTSTKPLK--ETDLHPLTAMPVP-GSAVSGGVDKAINFAFT-----FNGTN-FFINGATFQPPTTPVLL 378
Cdd:PLN02835 303 gpLPALPSGELHWSMRQARtyRWNLTASAARPNPqGSFHYGKITPTKTIVLAnsaplINGKQrYAVNGVSYVNSDTPLKL 382

                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56785438  379 QILSGaqdAKDLLPSGDVYALPSDATielSFPASTGAPGAPHPF---------------HLHGHTFAVV-------RSAG 436
Cdd:PLN02835 383 ADYFG---IPGVFSVNSIQSLPSGGP---AFVATSVMQTSLHDFlevvfqnnektmqswHLDGYDFWVVgygsgqwTPAK 456

                        490       500       510
                 ....*....|....*....|....*....|....*...
gi 56785438  437 STEYNYDNPIWRDVVSTgTPQAGdnVTIRFRTDNPGPW 474
Cdd:PLN02835 457 RSLYNLVDALTRHTAQV-YPKSW--TTILVSLDNQGMW 491
CuRO_2_Diphenol_Ox cd13883
The second cupredoxin domain of fungal laccase, diphenol oxidase; Diphenol oxidase belongs to ...
 170-307 1.07e-25

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: 102.80  E-value: 1.07e-25
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56785438 170 VITLADWYH------VAAKL------GPAFPPRSDATLINGLGRT--SDTPNA------DLAVITVTTGKRYRFRLISLS 229
Cdd:cd13883   2 VLFISDWYHdqseviVAGLLspqgykGSPAAPSPDSALINGIGQFncSAADPGtcctqtSPPEIQVEAGKRTRFRLINAG 81

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56785438 230 CDPAYTFSIDNHDMTIIEADGVNTQQ-LTVDSLQIFAGQRYSFVLEANQKS-GN-YWVRANplFGTTGFAGG----INSA 302
Cdd:cd13883  82 SHAMFRFSVDNHTLNVVEADDTPVYGpTVVHRIPIHNGQRYSVIIDTTSGKaGDsFWLRAR--MATDCFAWDlqqqTGKA 159


                ....*
gi 56785438 303 ILRYD 307
Cdd:cd13883 160 ILRYV 164
CuRO_3_tcLLC2_insect_like cd13905
The third cupredoxin domain of the insect laccases similar to laccase 2 in Tribolium castaneum; ...
 364-492 1.12e-25

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: 103.14  E-value: 1.12e-25
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56785438 364 INGATFQPPTTPVLLQ---ILSGAQDAKDLLPSGDVYA---------LPSDATIELSFPASTGAPGAPHPFHLHGHTFAV 431
Cdd:cd13905   2 INGISFVFPSSPLLSQpedLSDSSSCDFCNVPSKCCTEpcecthvikLPLNSVVEIVLINEGPGPGLSHPFHLHGHSFYV 81

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56785438 432 VRSaGSTEY-------------------------NYDNPIWRDVVSTgtpQAGDNVTIRFRTDNPGPWFLHCHIDFHLEA 486
Cdd:cd13905  82 LGM-GFPGYnsttgeilsqnwnnklldrgglpgrNLVNPPLKDTVVV---PNGGYVVIRFRADNPGYWLLHCHIEFHLLE 157


                ....*.
gi 56785438 487 GFAVVM 492
Cdd:cd13905 158 GMALVL 163
CuRO_1_CumA_like cd13861
The first cupredoxin domain of CumA like multicopper oxidase; This multicopper oxidase (MCO) ...
 32-151 1.35e-25

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: 101.16  E-value: 1.35e-25
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56785438  32 DLTISNENVSPDGFTRAAVVA-NGKAPGPLITGQKGDRFQINVVNKLSnhtmlKSTSIHWHGFfqKGTNWADGPAFVNQC 110
Cdd:cd13861   4 TLTAAPAELLDLGGPTTRTWGyNGQVPGPELRVRQGDTLRVRLTNRLP-----EPTTIHWHGL--RLPNAMDGVPGLTQP 76

                        90       100       110       120
                ....*....|....*....|....*....|....*....|...
gi 56785438 111 PIATGHSFLYDFQVPDqAGTFWYHSHLSTQYC--DGLRGPFVV 151
Cdd:cd13861  77 PVPPGESFTYEFTPPD-AGTYWYHPHVGSQEQldRGLYGPLIV 118
PLN00044 PLN00044
multi-copper oxidase-related protein; Provisional
 49-327 4.59e-25

multi-copper oxidase-related protein; Provisional


Pssm-ID: 165622 [Multi-domain]  Cd Length: 596  Bit Score: 108.60  E-value: 4.59e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56785438   49 AVVANGKAPGPLITGQKGDRFQINVVNKLSNHTMLKstsihWHGFFQKGTNWADGPAFVNqCPIATGHSFLYDFQVPDQA 128
Cdd:PLN00044  50 AIGINGQFPGPALNVTTNWNLVVNVRNALDEPLLLT-----WHGVQQRKSAWQDGVGGTN-CAIPAGWNWTYQFQVKDQV 123

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56785438  129 GTFWYHSHLSTQYCDGLRGPFVVYDPNDPNASLYDVDNDDTVITLADWY---HVAAKLG-----PAFPPrsDATLINGLG 200
Cdd:PLN00044 124 GSFFYAPSTALHRAAGGYGAITINNRDVIPIPFGFPDGGDITLFIADWYardHRALRRAldagdLLGAP--DGVLINAFG 201

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56785438  201 --RTSDT---PNADLAVITVTTGKRYRFRLISLSCDPAYTFSIDNHDMTIIEADGVNTQQLTVDSLQIFAGQRYSFVLEA 275
Cdd:PLN00044 202 pyQYNDSlvpPGITYERINVDPGKTYRFRVHNVGVATSLNFRIQGHNLLLVEAEGSYTSQQNYTNLDIHVGQSYSFLLTM 281

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....
gi 56785438  276 NQK-SGNYWVRANPLFGTTGFAGGINS-AILRYDDAvpaeptseQGTSTKPLKE 327
Cdd:PLN00044 282 DQNaSTDYYVVASARFVDAAVVDKLTGvAILHYSNS--------QGPASGPLPD 327
CuRO_2_Fet3p_like cd13877
The second Cupredoxin domain of multicopper oxidase Fet3P; Fet3p catalyzes the ferroxidase ...
 167-282 7.89e-25

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: 99.93  E-value: 7.89e-25
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56785438 167 DDTVITLADWYH-VAAKLGPAF---------PPRSDATLINglgrtsDTPNAdlaVITVTTGKRYRFRLISLSCDPAYTF 236
Cdd:cd13877   1 EEVTLTLSDWYHdQSPDLLRDFlspynptgaEPIPDSSLFN------DTQNA---TINFEPGKTYLLRIINMGAFASQYF 71

                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*..
gi 56785438 237 SIDNHDMTIIEADGVNTQQLTVDSLQIFAGQRYSFVLEA-NQKSGNY 282
Cdd:cd13877  72 HIEGHDMTIIEVDGVYVKPYPVDTLYIAVGQRYSVLVKAkNDTDRNY 118
CuRO_1_2dMco_1 cd13860
The first cupredoxin domain of bacteria two domain multicopper oxidase; This subfamily ...
 53-151 7.81e-24

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


Pssm-ID: 259929 [Multi-domain]  Cd Length: 119  Bit Score: 96.11  E-value: 7.81e-24
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56785438  53 NGKAPGPLITGQKGDRFQINVVNKLSNHtmlksTSIHWHGFFQKgtNWADGPAFVNQCPIATGHSFLYDFQVpDQAGTFW 132
Cdd:cd13860  26 NGSVPGPTIEVTEGDRVRILVTNELPEP-----TTVHWHGLPVP--NGMDGVPGITQPPIQPGETFTYEFTA-KQAGTYM 97

                        90       100
                ....*....|....*....|.
gi 56785438 133 YHSHLSTQYCD--GLRGPFVV 151
Cdd:cd13860  98 YHSHVDEAKQEdmGLYGAFIV 118
CuRO_3_Diphenol_Ox cd13904
The third cupredoxin domain of fungal laccase, diphenol oxidase; Diphenol oxidase belongs to ...
 362-491 4.78e-23

The third cupredoxin domain of fungal laccase, diphenol oxidase; Diphenol oxidase belongs to the laccase family. It catalyzes the initial steps in melanin biosynthesis from diphenols. Melanin is one of the virulence factors of infectious fungi. In the pathogenesis of C. neoformans, melanin pigments have been shown to protect the fungal cells from oxidative and microbicidal activities of host defense systems. Laccase is a blue multicopper oxidase (MCO) which catalyzes the oxidation of a variety aromatic - notably phenolic and inorganic substances coupled to the reduction of molecular oxygen to water. It has been implicated in a wide spectrum of biological activities and, in particular, plays a key role in morphogenesis, development and lignin metabolism. Although MCOs have diverse functions, majority of them have three cupredoxin domain repeats that include one mononuclear and one trinuclear copper center. The copper ions are bound in several sites: Type 1, Type 2, and/or Type 3. The ensemble of types 2 and 3 copper is called a trinuclear cluster. MCOs oxidize their substrate by accepting electrons at a mononuclear copper center and transferring them to the active site trinuclear copper center. The cupredoxin domain 3 of 3-domain MCOs contains the Type 1 (T1) copper binding site and part the trinuclear copper binding site, which is located at the interface of domains 1 and 3.


Pssm-ID: 259971 [Multi-domain]  Cd Length: 158  Bit Score: 95.44  E-value: 4.78e-23
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56785438 362 FFINGATFQP-PTTPVLLQILSGAQDAkdllpsgdvyaLPSDATIELSFPASTGA--------PGAPHPFHLHGHTFAVV 432
Cdd:cd13904  22 FFVNNVTWTNyIYQPLLHQVASGGGGT-----------LNSSEVASVTFPTDGWYdivinnldPAIDHPYHLHGVDFHIV 90

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 56785438 433 ---------RSAGSTEYNYDNPIWRDVVstgTPQAGDNVTIRFRTDNPGPWFLHCHIDFHLEAGFAVV 491
Cdd:cd13904  91 argsgtltlEQLANVQYNTTNPLRRDTI---VIPGGSWAVLRIPADNPGVWALHCHIGWHLAAGFAGV 155
CuRO_D1_2dMcoN_like cd13859
The first cupredoxin domain of bacterial two domain multicopper oxidase McoN and similar ...
 53-147 5.20e-23

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: 94.08  E-value: 5.20e-23
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56785438  53 NGKAPGPLITGQKGDRFQINVvnklSNHTMLKSTsIHWHGFFQKGTNWADGPAFVNQCPIATGHSFLYDFQVpDQAGTFW 132
Cdd:cd13859  26 NGQVPGPLIHVKEGDDLVVHV----TNNTTLPHT-IHWHGVLQMGSWKMDGVPGVTQPAIEPGESFTYKFKA-ERPGTLW 99

                        90
                ....*....|....*
gi 56785438 133 YHSHLSTQYCDGLRG 147
Cdd:cd13859 100 YHCHVNVNEHVGMRG 114
CuRO_1_CopA cd13848
The first cupredoxin domain of CopA copper resistance protein family; CopA is a multicopper ...
 32-151 6.98e-23

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: 93.50  E-value: 6.98e-23
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56785438  32 DLTISNENVSPDGFTRAAVVANGKAPGPLITGQKGDRFQINVVNKLSnhtmlKSTSIHWHGFFQKGTnwADGPAFVNQCP 111
Cdd:cd13848   4 DLVIAETPVNIGGKEGEAITVNGQVPGPLLRFKEGDDATIRVHNRLD-----EDTSIHWHGLLLPND--MDGVPGLSFPG 76

                        90       100       110       120
                ....*....|....*....|....*....|....*....|
gi 56785438 112 IATGHSFLYDFQVpDQAGTFWYHSHLSTQYCDGLRGPFVV 151
Cdd:cd13848  77 IKPGETFTYRFPV-RQSGTYWYHSHSGLQEQTGLYGPIII 115
CuRO_3_MaLCC_like cd13901
The third cupredoxin domain of the fungal laccases similar to Ma-LCC from Melanocarpus ...
 347-490 1.77e-22

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: 93.83  E-value: 1.77e-22
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56785438 347 VDKAINFAFTFNGTNFF---INGATFQPP-TTPVLLQILSGaqDAKDLLPSGDVYALPSDAT-----IElsfpastGAPG 417
Cdd:cd13901   8 PTQTLTIDLGPNATGVFlwtLNGSSFRVDwNDPTLLLVADG--NTSTFPPEWNVIELPKANKwvyivIQ-------NNSP 78

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56785438 418 APHPFHLHGHTFAVVrSAGSTEY-------NYDNPIWRDVVstgTPQAGDNVTIRFRTDNPGPWFLHCHIDFHLEAGFAV 490
Cdd:cd13901  79 LPHPIHLHGHDFYIL-AQGTGTFdddgtilNLNNPPRRDVA---MLPAGGYLVIAFKTDNPGAWLMHCHIAWHASGGLAL 154
CuRO_3_MCO_like_4 cd13910
The third cupredoxin domain of uncharacterized multicopper oxidase; Multicopper Oxidases (MCOs) ...
 363-494 4.28e-22

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: 92.74  E-value: 4.28e-22
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56785438 363 FINGATFQP-PTTPVLLQILSGAQDAKDLLPSGDVYALPSDATIELSFPAST----------GApgapHPFHLHGHTFAV 431
Cdd:cd13910  19 FFNGTSWRPlPGPATLLLALDADNAEEVAAGNGLSTFDGNQLVITVDDIDKVvdlvinnlddGD----HPFHLHGHKFWV 94

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 56785438 432 VRS------------AGSTEYNYDNPIWRDVVSTgtpQAGDNVTIRFRTDNPGPWFLHCHIDFHLEAGFAVVMAE 494
Cdd:cd13910  95 LGSgdgryggggytaPDGTSLNTTNPLRRDTVSV---PGFGWAVLRFVADNPGLWAFHCHILWHMAAGMLMQFAV 166
CuRO_2_AAO_like_2 cd13873
The second cupredoxin domain of plant Ascorbate oxidase homologs; This family includes plant ...
 167-306 4.22e-21

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: 90.04  E-value: 4.22e-21
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56785438 167 DDTVITLADWYHVA-------AKLGP-AFPPRSDATLINGLGRTSDTPNA--------DLAVITVTTGKRYRFRLISLSC 230
Cdd:cd13873   1 EERILLFSDYFPKTdstietgLTATPfVWPGEPNALLVNGKSGGTCNKSAtegcttscHPPVIDVEPGKTYRFRFIGATA 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56785438 231 DPAYTFSIDNHD-MTIIEADGVNTQQLTVDSLQIFAGQRYSFVL--------EANQKSgNYWVRANPLFGTTGFAGginS 301
Cdd:cd13873  81 LSFVSLGIEGHDnLTIIEADGSYTKPAETDHLQLGSGQRYSFLLktksleelAALNKT-TFWIQIETRWRPTNDTG---Y 156


                ....*
gi 56785438 302 AILRY 306
Cdd:cd13873 157 AVLRY 161
CuRO_1_MCO_like_2 cd13864
The second cupredoxin domain of uncharacterized multicopper oxidase; Multicopper Oxidases ...
 31-151 5.11e-21

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: 89.13  E-value: 5.11e-21
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56785438  31 TDLTISNENVSPDGFTRAAVVANGKAP--GPLITGQKGDRFQINVVNKLSNHTMLK-------STSIHWHG-----FFQK 96
Cdd:cd13864   2 TLLIILRISVEYNKDGKQIISINGSNDtiGPTIRVKSGDTLNLLVTNHLCNEQELSkiwqdycPTSIHFHGlvlenFGKQ 81

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*.
gi 56785438  97 GTNWADGPAFVNQCPIATGHSFLYDFQVPDQA-GTFWYHSHLSTQYCDGLRGPFVV 151
Cdd:cd13864  82 LANLVDGVPGLTQYPIGVGESYWYNFTIPEDTcGTFWYHSHSSVQYGDGLRGVFIV 137
CuRO_1_AAO_like_2 cd13847
The first cupredoxin domain of Ascorbate oxidase homologs; This family includes fungal ...
 33-153 1.26e-20

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: 87.20  E-value: 1.26e-20
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56785438  33 LTISNENVSPdgftRAAVVANGKAPGPLITGQKGDRFQINVVNKLSNhtmlKSTSIHWHGFFQKGTNWADGPAFVNQCPI 112
Cdd:cd13847   5 LRVSCDPFGP----RPSTLINGSFPGPELRVQEGQHLWVRVYNDLEA----GNTTMHFHGLSQYMSPFSDGTPLASQWPI 76

                        90       100       110       120
                ....*....|....*....|....*....|....*....|..
gi 56785438 113 ATGHSFLYDFQV-PDQAGTFWYHSHLSTQYCDGlRGPFVVYD 153
Cdd:cd13847  77 PPGKFFDYEFPLeAGDAGTYYYHSHVGFQSVTA-YGALIVED 117
CuRO_2_AAO_like_1 cd13872
The second cupredoxin domain of plant pollen multicopper oxidase homologous to ascorbate ...
 167-306 4.99e-20

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


Pssm-ID: 259940 [Multi-domain]  Cd Length: 141  Bit Score: 86.30  E-value: 4.99e-20
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56785438 167 DDTVITLADWYHVAAKL------GPAFPPRSDATLINGLGRTSDtpNADLAVITVTTGKRYRFRLISLSCDPAYTFSIDN 240
Cdd:cd13872   1 DEYTVLIGDWYKTDHKTlrqsldKGRTLGRPDGILINGKGPYGY--GANETSFTVEPGKTYRLRISNVGLRTSLNFRIQG 78

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 56785438 241 HDMTIIEADGVNTQQLTVDSLQIFAGQRYSFVLEANQKSGNYWVRANPLFGTTGFAGginSAILRY 306
Cdd:cd13872  79 HKMLLVETEGSYTAQNTYDSLDVHVGQSYSVLVTADQSPKDYYIVASSRFLSPELTG---VAILHY 141
CuRO_1_LCC_like_3 cd13865
The second cupredoxin domain of uncharacterized multicopper oxidase; Multicopper Oxidases ...
 31-153 1.74e-19

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


Pssm-ID: 259933 [Multi-domain]  Cd Length: 115  Bit Score: 83.90  E-value: 1.74e-19
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56785438  31 TDLTISNENVSPDGftRAAVV--ANGKAPGPLITGQKGDRFQINVVNKLSnhtmlKSTSIHWHGffQKGTNWADGPAFVN 108
Cdd:cd13865   1 TVLTVASRTIEVNG--KAATVygIRQPDGTEGLRLTEGDRFDVELENRLD-----EPTTIHWHG--LIPPNLQDGVPDVT 71

                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*
gi 56785438 109 QCPIATGHSFLYDFQVpDQAGTFWYHSHLSTQYCDGLRGPFVVYD 153
Cdd:cd13865  72 QPPIPPGQSQRYDFPL-VQPGTFWMHSHYGLQEQKLLAAPLIIRS 115
CuRO_2_AAO cd13871
The second cupredoxin domain of plant Ascorbate oxidase; Ascorbate oxidase catalyzes the ...
 171-287 5.71e-19

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: 84.13  E-value: 5.71e-19
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56785438 171 ITLADWYHVA---AKLGPAFPP-----RSDATLINGLGR----------------TSDTPNADLA--VITVTTGKRYRFR 224
Cdd:cd13871   6 ILLSDWWHKSiyeQETGLSSKPfrwvgEPQSLLIEGRGRyncslapaypsslpspVCNKSNPQCApfILHVSPGKTYRLR 85

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 56785438 225 LISLSCDPAYTFSIDNHDMTIIEADGVNTQQLTVDSLQIFAGQRYSFVLEANQK-SGNYWVRAN 287
Cdd:cd13871  86 IASVTALSSLNFIIEGHNLTVVEADGNYVQPFEVSNLDIYSGETYSVLVTADQDpSRNYWVSVN 149
CuRO_3_LCC_plant cd13897
The third cupredoxin domain of the plant laccases; Laccase is a blue multicopper oxidase (MCO) ...
 396-491 1.19e-18

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: 82.31  E-value: 1.19e-18
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56785438 396 VYALPSDATIELSFPASTGAPGAPHPFHLHGHTFAVV--------RSAGSTEYNYDNPIWRDVVstGTPQAGdNVTIRFR 467
Cdd:cd13897  33 VKVLEYGSTVEIVLQGTSLLAAENHPMHLHGFDFYVVgrgfgnfdPSTDPATFNLVDPPLRNTV--GVPRGG-WAAIRFV 109

                        90       100
                ....*....|....*....|....
gi 56785438 468 TDNPGPWFLHCHIDFHLEAGFAVV 491
Cdd:cd13897 110 ADNPGVWFMHCHFERHTSWGMATV 133
CuRO_2_Abr2_like cd13876
The second cupredoxin domain of a group of fungal Laccases similar to Abr2 from Aspergillus ...
 170-306 1.94e-18

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: 81.48  E-value: 1.94e-18
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56785438 170 VITLADWYH----------VAAKLGPAFpprSDATLINGLGRTSdtpnadLAVITVTTGKRYR-FRLISLSCDPAYTFSI 238
Cdd:cd13876   2 PIILSDWRHltseeywkimRASGIEPFC---YDSILINGKGRVY------CLIVIVDPGERWVsLNFINAGGFHTLAFSI 72

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 56785438 239 DNHDMTIIEADG--VNTQQltVDSLQIFAGQRYSFVLEANQKSGNYWVRANplfgTTGFAGGINS-AILRY 306
Cdd:cd13876  73 DEHPMWVYAVDGgyIEPQL--VDAISITNGERYSVLVKLDKPPGDYTIRVA----STGAPQVISGyAILRY 137
CuRO_3_AAO cd13893
The third cupredoxin domain of plant Ascorbate oxidase; Ascorbate oxidase catalyzes the ...
 364-496 2.29e-18

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: 82.08  E-value: 2.29e-18
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56785438 364 INGATFQPPTTPVLLQilsgaqdakdlLPsgdVYALPSDATIEL---SFPASTGAPGAPHPFHLHGHTFAVV-------- 432
Cdd:cd13893  22 INNVSYVPPPTPYLAA-----------LP---VYPFKGGDVVDVilqNANTNTRNASEQHPWHLHGHDFWVLgyglggfd 87

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 56785438 433 RSAGSTEYNYDNPIWRDVVSTgtPQAGdNVTIRFRTDNPGPWFLHCHIDFHLEAGFAVVMAEDI 496
Cdd:cd13893  88 PAADPSSLNLVNPPMRNTVTI--FPYG-WTALRFKADNPGVWAFHCHIEWHFHMGMGVVFAEGV 148
CuRO_2_LCC_plant cd13875
The second cupredoxin domain of the plant laccases; Laccase is a blue multi-copper enzyme that ...
 170-306 2.64e-18

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: 81.49  E-value: 2.64e-18
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56785438 170 VITLADWY--HV-----AAKLGPAFPPRSDATLINGL-GRTSDTPNADLAVITVTTGKRYRFRLISLSCDPAYTFSIDNH 241
Cdd:cd13875   2 PIILGEWWnrDVndvedQALLTGGGPNISDAYTINGQpGDLYNCSSKDTFVLTVEPGKTYLLRIINAALNEELFFKIANH 81

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 56785438 242 DMTIIEADGVNTQQLTVDSLQIFAGQRYSFVLEANQKSGNYWVRANPLFgtTGFAGGINS----AILRY 306
Cdd:cd13875  82 TLTVVAVDASYTKPFTTDYILIAPGQTTDVLLTADQPPGRYYMAARPYQ--SAPPVPFDNttatAILEY 148
CuRO_3_CopA cd13896
The third cupredoxin domain of CopA copper resistance protein family; CopA is a multicopper ...
 419-487 3.96e-17

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


Pssm-ID: 259963 [Multi-domain]  Cd Length: 115  Bit Score: 77.30  E-value: 3.96e-17
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 56785438 419 PHPFHLHGHTFAVVRSAGSTeynydNPIwRDVVSTgtpQAGDNVTIRFRTDNPGPWFLHCHIDFHLEAG 487
Cdd:cd13896  49 AHPMHLHGHFFQVENGNGEY-----GPR-KDTVLV---PPGETVSVDFDADNPGRWAFHCHNLYHMEAG 108
CuRO_1_McoP_like cd13852
The first cupredoxin domain of multicopper oxidase McoP and similar proteins; This family ...
 58-154 4.24e-17

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: 76.94  E-value: 4.24e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56785438  58 GPLITGQKGDRFQINVVNKLSNHTMlkstsIHWHGFFqkgTNWA-DG-PAFVnqcpIATGHSFLYDFQVPDQAGTFWYHS 135
Cdd:cd13852  24 GPILRLRKGQKVRITFKNNLPEPTI-----IHWHGLH---VPAAmDGhPRYA----IDPGETYVYEFEVLNRAGTYWYHP 91

                        90       100
                ....*....|....*....|...
gi 56785438 136 H----LSTQYCDGLRGPFVVYDP 154
Cdd:cd13852  92 HphglTAKQVYRGLAGLFLVTDE 114
CuRO_1_McoC_like cd13855
The first cupredoxin domain of a multicopper oxidase McoC and similar proteins; This family ...
 53-151 2.49e-16

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: 75.20  E-value: 2.49e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56785438  53 NGKAPGPLITGQKGDRFQINVVNKLSnhtmlKSTSIHWHGFfqKGTNWADGPAfvnQCPIATGHSFLYDFQVP-DQAGTF 131
Cdd:cd13855  27 NGSVPGPLIEVFEGDTVEITFRNRLP-----EPTTVHWHGL--PVPPDQDGNP---HDPVAPGNDRVYRFTLPqDSAGTY 96

                        90       100
                ....*....|....*....|....
gi 56785438 132 WYHSH----LSTQYCDGLRGPFVV 151
Cdd:cd13855  97 WYHPHphghTAEQVYRGLAGAFVV 120
CuRO_3_Abr2_like cd13898
The third cupredoxin domain of a group of fungal Laccases similar to Abr2 from Aspergillus ...
 413-494 6.54e-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: 75.37  E-value: 6.54e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56785438 413 TGAPGAPHPFHLHG-HTFAVVRSAG--------------STEYNYDNPIWRD-VVSTGTPQAGDNVTIRFRTDNPGPWFL 476
Cdd:cd13898  66 TGPPQPPHPIHKHGnKAFVIGTGTGpfnwssvaeaaeaaPENFNLVNPPLRDtFTTPPSTEGPSWLVIRYHVVNPGAWLL 145

                        90
                ....*....|....*...
gi 56785438 477 HCHIDFHLEAGFAVVMAE 494
Cdd:cd13898 146 HCHIQSHLAGGMAVVLLD 163
CuRO_1_AAO_like_1 cd13846
The first cupredoxin domain of plant Ascorbate oxidase homologs; This subfamily is composed of ...
 32-151 8.97e-16

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: 73.60  E-value: 8.97e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56785438  32 DLTISNENVSPDGFTRAAVVANGKAPGPLITGQKGDRFQINVVNKLsNHTMLkstsIHWHGFFQKGTNWADGPAFVNqCP 111
Cdd:cd13846   4 DWNVSYITASPLGVPQQVIAINGQFPGPTINVTTNDNVVVNVFNSL-DEPLL----LTWNGIQQRRNSWQDGVLGTN-CP 77

                        90       100       110       120
                ....*....|....*....|....*....|....*....|
gi 56785438 112 IATGHSFLYDFQVPDQAGTFWYHSHLSTQYCDGLRGPFVV 151
Cdd:cd13846  78 IPPGWNWTYKFQVKDQIGSFFYFPSLHFQRAAGGFGGIRV 117
CuRO_3_CumA_like cd13906
The third cupredoxin domain of CumA like multicopper oxidase; This multicopper oxidase (MCO) ...
 419-487 1.31e-14

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: 70.88  E-value: 1.31e-14
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 56785438 419 PHPFHLHGHTFAVVRSAGSTEynyDNPIWRDVVSTGtpqAGDNVTIRFRTDNPGPWFLHCHIDFHLEAG 487
Cdd:cd13906  68 LHPMHLHGHFFRVLSRNGRPV---PEPFWRDTVLLG---PKETVDIAFVADNPGDWMFHCHILEHQETG 130
CuRO_1_Tth-MCO_like cd13853
The first cupredoxin domain of the bacterial laccases similar to Tth-MCO from Thermus ...
 30-151 1.80e-14

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: 70.36  E-value: 1.80e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56785438  30 VTDLTISNENVSPDGFTRAAVVANGKAPGPLITGQKGDRFQINVVNKLSNHTMLK------------STSIHWHGFFQKG 97
Cdd:cd13853   3 EVTLTVEYGRVTLAGLPVTLRTYNGSIPGPTLRVRPGDTLRITLKNDLPPEGAANeapapntphcpnTTNLHFHGLHVSP 82

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|
gi 56785438  98 TNWADGPaFVNqcpIATGHSFLYDFQVPDQ--AGTFWYHSHL----STQYCDGLRGPFVV 151
Cdd:cd13853  83 TGNSDNV-FLT---IAPGESFTYEYDIPADhpPGTYWYHPHLhgstALQVAGGMAGALVV 138
CuRO_3_McoC_like cd13902
The third cupredoxin domain of a multicopper oxidase McoC and similar proteins; This family ...
 420-487 9.50e-14

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: 67.81  E-value: 9.50e-14
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 56785438 420 HPFHLHGHTFAVVRSAGST---EYnydnPIWRDVVSTgtPQaGDNVTIRFRTDNPGPWFLHCHIDFHLEAG 487
Cdd:cd13902  55 HPFHLHGTQFQVLEIDGNPqkpEY----RAWKDTVNL--PP-GEAVRIATRQDDPGMWMYHCHILEHEDAG 118
CuRO_3_MCO_like_3 cd13909
The third cupredoxin domain of uncharacterized multicopper oxidase; Multicopper Oxidases (MCOs) ...
 404-487 1.98e-13

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: 67.16  E-value: 1.98e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56785438 404 TIELSFPASTGAPgapHPFHLHGHTFAVVrsagstEYNYDNPIWRDVVSTgtpQAGDNVTIRFRTDNPGPWFLHCHIDFH 483
Cdd:cd13909  58 TVRIEMVNNTGFP---HGMHLHGHHFRAI------LPNGALGPWRDTLLM---DRGETREIAFVADNPGDWLLHCHMLEH 125


                ....
gi 56785438 484 LEAG 487
Cdd:cd13909 126 AAAG 129
CuRO_3_MCO_like_2 cd13908
The third cupredoxin domain of uncharacterized multicopper oxidase; Multicopper Oxidases (MCOs) ...
 420-488 1.79e-12

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


Pssm-ID: 259975 [Multi-domain]  Cd Length: 122  Bit Score: 64.01  E-value: 1.79e-12
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 56785438 420 HPFHLHGHTFAVVRSAGsteyNYDNPIWRDVVSTGtpqAGDNVTIRFRTDNPGPWFLHCHIDFHLEAGF 488
Cdd:cd13908  55 HPMHLHRHTFEVTRIDG----KPTSGLRKDVVMLG---GYQRVEVDFVADNPGLTLFHCHQQLHMDYGF 116
CuRO_1_CueO_FtsP cd04232
The first Cupredoxin domain of the multicopper oxidase CueO, the cell division protein FtsP, ...
 53-153 5.94e-12

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: 5.94e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56785438  53 NGKAPGPLITGQKGDRFQINVVNKLSnhtmlKSTSIHWHGFFQKGTnwADGPAfvnQCPIATGHSFLYDFQVPDQAGTFW 132
Cdd:cd04232  26 NGSYLGPTIRVKKGDTVRINVTNNLD-----EETTVHWHGLHVPGE--MDGGP---HQPIAPGQTWSPTFTIDQPAATLW 95

                        90       100
                ....*....|....*....|....*
gi 56785438 133 YHSHL--ST--QYCDGLRGPFVVYD 153
Cdd:cd04232  96 YHPHThgKTaeQVYRGLAGLFIIED 120
CuRO_2_CopA_like_1 cd13870
The second cupredoxin domain of CopA copper resistance protein like family; The members of ...
 195-306 7.15e-12

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: 62.35  E-value: 7.15e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56785438 195 LINGlgrtsdTPNADLAVITVTTGKRYRFRLISLSCDPAYTFSIDNHDMTIIEADGVNTQQLTVDSLQIFAGQRYSFVLE 274
Cdd:cd13870  19 LING------RPPEDPAVFTARPGDRLRLRLINAAGDTAFRVALAGHRLTVTHTDGFPVEPVEVDALLIGMGERYDAIVT 92

                        90       100       110
                ....*....|....*....|....*....|..
gi 56785438 275 ANQksGNYWVRANPlFGTTGFAgginSAILRY 306
Cdd:cd13870  93 ANN--GIWPLVALP-EGKDGQA----RAVLRY 117
CuRO_D2_2dMcoN_like cd04202
The second cupredoxin domain of bacterial two domain multicopper oxidase McoN and similar ...
 420-483 9.63e-12

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: 62.66  E-value: 9.63e-12
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 56785438 420 HPFHLHGHTFAVVRSAGSTEYNyDNPIWRDVVSTGTPQAGDnvtIRFRTDNPGPWFLHCHIDFH 483
Cdd:cd04202  63 HPMHLHGHFFLVTATDGGPIPG-SAPWPKDTLNVAPGERYD---IEFVADNPGDWMFHCHKLHH 122
CuRO_3_Tth-MCO_like cd13900
The third cupredoxin domain of the bacterial laccases similar to Tth-MCO from Thermus ...
 351-487 1.20e-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: 58.80  E-value: 1.20e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56785438 351 INFAFTF---NGTNFFINGATFQPPTTPVLLQIlsgaqdakdllpsGDVyalpSDATIElsfpaSTGapGAPHPFHLHGH 427
Cdd:cd13900   6 LVFSEGMspgGGGAFTINGKPFDPDRPDRTVRL-------------GTV----EEWTLI-----NTS--GEDHPFHIHVN 61

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 56785438 428 TFAVVRSAGSTeynYDNPIWRDVVSTgtpQAGDNVTIRFR-TDNPGPWFLHCHIDFHLEAG 487
Cdd:cd13900  62 PFQVVSINGKP---GLPPVWRDTVNV---PAGGSVTIRTRfRDFTGEFVLHCHILDHEDQG 116
CuRO_1_2DMCO_NIR_like cd11024
The cupredoxin domain 1 of a two-domain laccase related to nitrite reductase; The two-domain ...
 53-155 2.93e-10

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: 57.67  E-value: 2.93e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56785438  53 NGKAPGPLITGQKGDRFQINVVNKlSNHtmlkSTSIHWHGffqKGTNWADGPAFVnqcPIATGHSFLYDFqVPDQAGTFW 132
Cdd:cd11024  27 NGTVPGPTLRATEGDLVRIHFINT-GDH----PHTIHFHG---IHDAAMDGTGLG---PIMPGESFTYEF-VAEPAGTHL 94

                        90       100
                ....*....|....*....|....*.
gi 56785438 133 YHSH---LSTQYCDGLRGPFVVyDPN 155
Cdd:cd11024  95 YHCHvqpLKEHIAMGLYGAFIV-DPK 119
CuRO_1_MCO_like_1 cd13862
The first cupredoxin domain of uncharacterized multicopper oxidase; Multicopper Oxidases (MCOs) ...
 27-151 6.61e-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: 56.76  E-value: 6.61e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56785438  27 IGPVTDLTISNENVSPDGFtraavvaNGKAPGPLITGQKGDRFQINVVNKLSNhtmlkSTSIHWHGFFQKGTnwADGPAF 106
Cdd:cd13862   7 IAPVTVELAPGRTISTLGY-------NGQVPGPLLRMRQGVSVTVDVFNDTDI-----PEYVHWHGLPLPAD--VDGAME 72

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|..
gi 56785438 107 VNQCPIATGHSFLYDFqVPDQAGTFWYHSHLST-------QYcDGLRGPFVV 151
Cdd:cd13862  73 EGTPSVPPHGHRRYRM-TPRPAGFRWYHTHVMTmddltrgQY-SGLFGFVYI 122
PRK10965 PRK10965
multicopper oxidase; Provisional
 53-156 5.01e-08

multicopper oxidase; Provisional


Pssm-ID: 236810 [Multi-domain]  Cd Length: 523  Bit Score: 55.42  E-value: 5.01e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56785438   53 NGKAPGPLITGQKGDRFQINVVNKLSnhtmlKSTSIHWHGFFQKGTnwADG-PafvnQCPIATGHSFLYDFQVPDQAGTF 131
Cdd:PRK10965  71 NGNLLGPAVRLQRGKAVTVDITNQLP-----EETTLHWHGLEVPGE--VDGgP----QGIIAPGGKRTVTFTVDQPAATC 139

                         90       100
                 ....*....|....*....|....*....
gi 56785438  132 WYHSHL----STQYCDGLRGPFVVYDPND 156
Cdd:PRK10965 140 WFHPHQhgktGRQVAMGLAGLVLIEDDES 168
CuRO_3_AAO_like_2 cd13895
The third cupredoxin domain of Ascorbate oxidase homologs; This family includes fungal ...
 359-492 2.05e-07

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: 51.16  E-value: 2.05e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56785438 359 GTNFFINGATFQ--PPTTPVLLQILsgaQDAKDLLPSgdvYALPS-----DATIElSFPA-----------STGAPGA-- 418
Cdd:cd13895  18 GVLWAQNGLTWTetLPSVPYLVQLY---EYGTSLLPD---YEAALanggfDPETN-TFPAklgevldivwqNTASPTGgl 90

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56785438 419 -PHPFHLHGHTFAVVRSaGSTEYNYD-----------NPIWRDVV------STGTPQAGDNVT----IRFRTDNPGPWFL 476
Cdd:cd13895  91 dAHPWHAHGAHYYDLGS-GLGTYSATalaneeklrgyNPIRRDTTmlyrygGKGYYPPPGTGSgwraWRLRVDDPGVWML 169

                       170
                ....*....|....*.
gi 56785438 477 HCHIDFHLEAGFAVVM 492
Cdd:cd13895 170 HCHILQHMIMGMQTVW 185
CuRO_1_Ceruloplasmin_like_1 cd04229
cupredoxin domain of ceruloplasmin homologs; Uncharacterized subfamily of ceruloplasmin ...
 58-153 2.49e-06

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


Pssm-ID: 259891 [Multi-domain]  Cd Length: 175  Bit Score: 47.80  E-value: 2.49e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56785438  58 GPLITGQKGDRFQINVVNKLSNHTMlkstSIHWHG-FFQKGtnwADGPAFVNQCPIATGHSFLYDFQVPDQAG------- 129
Cdd:cd04229  73 GPVIRAEVGDTIKVVFKNNLDEFPV----NMHPHGgLYSKD---NEGTTDGAGDVVAPGETYTYRWIVPEDAGpgpgdps 145

                        90       100
                ....*....|....*....|....*...
gi 56785438 130 --TFWYHSHLSTQYCD--GLRGPFVVYD 153
Cdd:cd04229 146 srLWLYHSHVDVFAHTnaGLVGPIIVTS 173
CuRO_2_MCO_like_2 cd13887
The second cupredoxin domain of uncharacterized multicopper oxidase; Multicopper Oxidases ...
 192-268 8.42e-06

The second cupredoxin domain of uncharacterized multicopper oxidase; Multicopper Oxidases (MCOs) are multi-domain enzymes that are able to couple oxidation of substrates with reduction of dioxygen to water. MCOs oxidise their substrate by accepting electrons at a mononuclear copper centre and transferring them to a trinuclear copper centre which binds a dioxygen. The dioxygen, following the transfer of four electrons, is reduced to two molecules of water. These MCOs are capable of oxidizing a vast range of substrates, varying from aromatic to inorganic compounds such as metals. This family of MCOs is composed of three cupredoxin domains that include one mononuclear and one trinuclear copper center. The copper ions are bound in several sites: Type 1, Type 2, and/or Type 3. The ensemble of types 2 and 3 copper is called a trinuclear cluster. MCOs oxidize their substrate by accepting electrons at a mononuclear copper center and transferring them to the active site trinuclear copper center. The cupredoxin domain 2 of 3-domain MCOs has lost the ability to bind copper.


Pssm-ID: 259954 [Multi-domain]  Cd Length: 114  Bit Score: 45.01  E-value: 8.42e-06
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 56785438 192 DATLINGlgRTSDTPNadlaVITVTTGKRYRFRLISLSCDPAYTFSIDNHDMTIIEADGVNTQQLTVDSLQIFAGQR 268
Cdd:cd13887  11 DAFLAND--RTLDDPE----VVRVEPGGRVRLRVINGSTATNFHIDLGDLKGTLIAVDGNPVQPVEGRRFPLATAQR 81
CuRO_3_CueO_FtsP cd13890
The third Cupredoxin domain of the multicopper oxidase CueO, the cell division protein FtsP, ...
 413-487 1.38e-05

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


Pssm-ID: 259957 [Multi-domain]  Cd Length: 124  Bit Score: 44.55  E-value: 1.38e-05
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 56785438 413 TGAPGAPHPFHLHGHTFAVVRSAGSTEYNYDNPiWRDVVSTGtpqAGDNVTI--RFR--TDNPGPWFLHCHIDFHLEAG 487
Cdd:cd13890  43 TNTDGMPHPFHIHGVQFRILSRNGQPPPPNEAG-WKDTVWVP---PGETVRIlvKFDhyADPTGPFMYHCHILEHEDNG 117
CuRO_6_ceruloplasmin cd11012
The sixth cupredoxin domain of Ceruloplasmin; Ceruloplasmin is a multicopper oxidase essential ...
 420-490 1.86e-05

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


Pssm-ID: 259898 [Multi-domain]  Cd Length: 145  Bit Score: 44.47  E-value: 1.86e-05
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 56785438 420 HPFHLHGHTFAVVRSAGSTEYNYDnpiwrdvVSTGTPQagdnvTIRFRTDNPGPWFLHCHIDFHLEAGFAV 490
Cdd:cd11012  82 HTAHFHGHSFDYKHRGVYRSDVFD-------LFPGTFQ-----TVEMIPRTPGTWLLHCHVTDHIHAGMET 140
CuRO_3_MCO_like_1 cd13907
The third cupredoxin domain of uncharacterized multicopper oxidase; Multicopper Oxidases (MCOs) ...
 351-487 2.42e-05

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


Pssm-ID: 259974 [Multi-domain]  Cd Length: 154  Bit Score: 44.40  E-value: 2.42e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56785438 351 INFAFTFNGTNFFINGATFqppttpvllqilsgaqDAKDLLPSGDVyALPSDATIELSFPASTGAPGA------------ 418
Cdd:cd13907   4 RTIKLSMQHMEWTINGRSF----------------EMDDVTPDETV-KLNTTEVWEIINDLGGMGGGGgmmggggmmmgg 66

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56785438 419 ----PHPFHLHGHTFAVV-RSAGSTEYNYDNPI--------WRDVVSTgTPqaGDNVTI--RFRtDNPGPWFLHCHIDFH 483
Cdd:cd13907  67 mmamPHPIHLHGVQFQVLeRSVGPKDRAYWATVkdgfidegWKDTVLV-MP--GERVRIikPFD-DYKGLFLYHCHNLEH 142


                ....
gi 56785438 484 LEAG 487
Cdd:cd13907 143 EDMG 146
CuRO_1_CuNIR cd11020
Cupredoxin domain 1 of Copper-containing nitrite reductase; Copper-containing nitrite ...
 43-134 4.41e-05

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


Pssm-ID: 259906 [Multi-domain]  Cd Length: 119  Bit Score: 42.97  E-value: 4.41e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56785438  43 DGFTRAAVVANGKAPGPLITGQKGDRFQINVVNKLSNhTMLKSTSIHwhgffqkgtnWADGPAFVNQCPIATGHSFLYDF 122
Cdd:cd11020  17 PGVTYTAWTFNGQVPGPVIRVREGDTVELTLTNPGTN-TMPHSIDFH----------AATGPGGGEFTTIAPGETKTFSF 85

                        90
                ....*....|..
gi 56785438 123 qVPDQAGTFWYH 134
Cdd:cd11020  86 -KALYPGVFMYH 96
CuRO_3_MCO_like_5 cd13911
The third cupredoxin domain of uncharacterized multicopper oxidase; Multicopper Oxidases (MCOs) ...
 419-487 6.00e-05

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


Pssm-ID: 259978 [Multi-domain]  Cd Length: 119  Bit Score: 42.53  E-value: 6.00e-05
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56785438 419 PHPFHLHGHTFAVVRSAGSTEYNYDNPiWRDVVSTGtpqAGDNVTIRFRTDN-PGPWFLHCHIDFHLEAG 487
Cdd:cd13911  48 RHPVHLHGAHFQVVSRTGGRPGEWDAG-WKDTVLLR---PRESVTVIIRFDGyRGRYVFHCHNLEHEDMG 113
CuRO_2_CopA cd13874
The second cupredoxin domain of CopA copper resistance protein family; CopA is a multicopper ...
 192-298 8.96e-05

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


Pssm-ID: 259942 [Multi-domain]  Cd Length: 112  Bit Score: 41.90  E-value: 8.96e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56785438 192 DATLINGLgrtsdtPNADLAVITVTTGKRYRFRLISLSCDPAYTFSIDNHDMTIIEADGVNTQQLTVDSLQIFAGQRYSF 271
Cdd:cd13874  12 DTYLINGK------PPEDNWTGLFKPGERVRLRFINAAASTYFDVRIPGGKMTVVAADGQDVRPVEVDEFRIGVAETYDV 85

                        90       100
                ....*....|....*....|....*..
gi 56785438 272 VLEAnQKSGNYWVRANPLfGTTGFAGG 298
Cdd:cd13874  86 IVTI-PENGAYTIRATSQ-DRSGYASG 110
CuRO_1_CuNIR_like cd04201
Cupredoxin domain 1 of Copper-containing nitrite reductase and two-domain laccase; ...
 43-151 2.51e-04

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: 40.94  E-value: 2.51e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56785438  43 DGFTRAAVVANGKAPGPLITGQKGDRFQINVVNKLSNhTMLKstSIHWHGFFQKGTNWADGpafvnqcPIATGHSFLYDF 122
Cdd:cd04201  17 DGVEYRYWTFDGDIPGPMLRVREGDTVELHFSNNPSS-TMPH--NIDFHAATGAGGGAGAT-------FIAPGETSTFSF 86

                        90       100       110
                ....*....|....*....|....*....|..
gi 56785438 123 QVPdQAGTFWYHSH---LSTQYCDGLRGPFVV 151
Cdd:cd04201  87 KAT-QPGLYVYHCAvapVPMHIANGMYGLILV 117
CuRO_3_BOD cd13889
The third cupredoxin domain of Bilirubin oxidase (BOD); Bilirubin oxidase (BOD) catalyzes the ...
 413-483 3.86e-04

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


Pssm-ID: 259956 [Multi-domain]  Cd Length: 124  Bit Score: 40.37  E-value: 3.86e-04
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 56785438 413 TGAPGAPHPFHLHGHTFAVVRSAGSTE--YNYDnPIWRDVVSTGtpqAGDNVTIRFR-TDNPGPWFLHCHIDFH 483
Cdd:cd13889  44 NGGGGWSHPIHIHLEDFQILSRNGGSRavPPYE-RGRKDVVYLG---PGEEVRVLMRfRPFRGKYMMHCHNLVH 113
CuRO_3_McoP_like cd13888
The third cupredoxin domain of multicopper oxidase McoP and similar proteins; This subfamily ...
 353-490 5.20e-04

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


Pssm-ID: 259955 [Multi-domain]  Cd Length: 139  Bit Score: 40.24  E-value: 5.20e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56785438 353 FAFTFNGTNFFINGATFQPPTTPVLLQILSGAQDakdllpsgdVYALPSDATielsfpastgapGAPHPFHLHGHTFAVV 432
Cdd:cd13888   6 IHLSMGRMQWTINGETWADDPDAFPVERVGGTVE---------IWELVNDAA------------SMPHPMHIHGFQFQVL 64

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 56785438 433 RSAGSTEYNYDNPI-----------WRDVVSTGtPQAGDNVTIRFRTDNPGP--WFLHCHIDFHLEAGFAV 490
Cdd:cd13888  65 ERSDSPPQVAELAVapsgrtatdlgWKDTVLVW-PGETVRIAVDFTHDYPGDqlYLLHCHNLEHEDDGMMV 134
CuRO_2_CumA_like cd13885
The second cupredoxin domain of CumA like multicopper oxidase; This multicopper oxidase (MCO) ...
 168-280 7.81e-03

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


Pssm-ID: 259952 [Multi-domain]  Cd Length: 132  Bit Score: 36.54  E-value: 7.81e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56785438 168 DTVITLADWyHV--AAKLGPAFPPRSDATLINGLGRTSdTPNADL-AVITVTTGKRYRFRLISLSCDPAYTFSIDNHDMT 244
Cdd:cd13885   2 DLVWVLDDW-RLdpDGQAVPGFGTPHDAAHAGRIGNLY-TINGRVqPDFTVRAGERVRLRLINAANARVFALKFPGHEAR 79

                        90       100       110
                ....*....|....*....|....*....|....*...
gi 56785438 245 IIEADGVNTQQLTVDSLQIF--AGQRYSFVLEANQKSG 280
Cdd:cd13885  80 VIALDGQPAEPFVARNGAVVlaPGMRIDLVIDAPQAAG 117
CuRO_2_McoC_like cd13881
The second cupredoxin domain of a multicopper oxidase McoC and similar proteins; This family ...
 166-288 8.15e-03

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: 36.82  E-value: 8.15e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56785438 166 NDDTVITLADWyhvaakLGPAFPPRSDATLINGLGRtsdtPnadlaVITVTTGKRYRFRLISLSCDPAYTFSIDNHDMTI 245
Cdd:cd13881  12 DGDGQLAEPSA------ADWMFGREGDLVLVNGQLN----P-----TITVRPGEVQRWRIVNAASARYFRLALDGHKFRL 76

                        90       100       110       120
                ....*....|....*....|....*....|....*....|....
gi 56785438 246 IEADG-VNTQQLTVDSLQIFAGQRYSFVLEANQKSGNYWVRANP 288
Cdd:cd13881  77 IGTDGgLLEAPREVDELLLAPGERAEVLVTAGEPGGRLVLLALP 120
 
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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