NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|346214843|gb|AEO20225|]
View 

laccase I precursor [Trametes sp. Ha1]

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

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

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; ...
 25-149 8.77e-80

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: 244.94  E-value: 8.77e-80
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346214843  25 PTADLTISNAEVSPDGFARQAVVVNNVTPGPLVAGNKGDRFQLNVIDNLTNHTMLKSTSIHWHGFFQKGTNWADGPAFVN 104
Cdd:cd13856    1 PTYTLNIVNTRLAPDGFERSAVLANGQFPGPLITANKGDTFRITVVNQLTDPTMRRSTSIHWHGIFQHGTNYADGPAFVT 80

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*
gi 346214843 105 QCPISSGHSFLYDFQVPDQAGTFWYHSHLSTQYCDGLRGPFVVYD 149
Cdd:cd13856   81 QCPIAPNHSFTYDFTAGDQAGTFWYHSHLSTQYCDGLRGPLVIYD 125
Cupredoxin super family cl19115
Cupredoxin superfamily; Cupredoxins contain type I copper centers and are involved in ...
 165-309 2.80e-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: 239.62  E-value: 2.80e-77
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346214843 165 TVITLADWYHTAAKLGPA----FPLGADATLINGLGRSPSTTAADLAVINVTKGKRYRFRLVSLSCDPNHTFSIDGHDLT 240
Cdd:cd13882    1 TVITLGDWYHTAAPDLLAttagVPPVPDSGTINGKGRFDGGPTSPLAVINVKRGKRYRFRVINISCIPSFTFSIDGHNLT 80

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346214843 241 IIEVDSINSQHLVVDSIQIFAAQRYSFVLNADQDVGNYWIRANPSFGNVGFAGGI-NSAILRYDGADPVE 309
Cdd:cd13882   81 VIEADGVETKPLTVDSVQIYAGQRYSVVVEANQPVDNYWIRAPPTGGTPANNGGQlNRAILRYKGAPEVE 150
CuRO_3_Tv-LCC_like cd13903
The third cupredoxin domain of the fungal laccases similar to Tv-LCC from Trametes Versicolor; ...
 343-491 2.36e-73

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: 229.09  E-value: 2.36e-73
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346214843 343 DKAINMAFNFNGTN--FFINGASFVPPTVPVLLQIISGAQNAQDLLPSGSVYSLPANADIEISFPATAAAPGAPhpFHLH 420
Cdd:cd13903    1 DVNITLTFGLNGTTglFTINGVSYVSPTVPVLLQILSGATSAEDLLPTESTIILPRNKVVEITIPGGAIGGPHP--FHLH 78

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 346214843 421 GHAFAVVRSAGSTVYNYDNPIFRDVVSTGTPaaGDNVTIRFRTDNPGPWFLHCHIDFHLEAGFAVVMAEDI 491
Cdd:cd13903   79 GHAFSVVRSAGSNTYNYVNPVRRDVVSVGTP--GDGVTIRFVTDNPGPWFLHCHIDWHLEAGLAVVFAEDP 147
 
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; ...
 25-149 8.77e-80

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: 244.94  E-value: 8.77e-80
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346214843  25 PTADLTISNAEVSPDGFARQAVVVNNVTPGPLVAGNKGDRFQLNVIDNLTNHTMLKSTSIHWHGFFQKGTNWADGPAFVN 104
Cdd:cd13856    1 PTYTLNIVNTRLAPDGFERSAVLANGQFPGPLITANKGDTFRITVVNQLTDPTMRRSTSIHWHGIFQHGTNYADGPAFVT 80

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*
gi 346214843 105 QCPISSGHSFLYDFQVPDQAGTFWYHSHLSTQYCDGLRGPFVVYD 149
Cdd:cd13856   81 QCPIAPNHSFTYDFTAGDQAGTFWYHSHLSTQYCDGLRGPLVIYD 125
CuRO_2_Tv-LCC_like cd13882
The second cupredoxin domain of the fungal laccases similar to Tv-LCC from Trametes versicolor; ...
 165-309 2.80e-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: 239.62  E-value: 2.80e-77
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346214843 165 TVITLADWYHTAAKLGPA----FPLGADATLINGLGRSPSTTAADLAVINVTKGKRYRFRLVSLSCDPNHTFSIDGHDLT 240
Cdd:cd13882    1 TVITLGDWYHTAAPDLLAttagVPPVPDSGTINGKGRFDGGPTSPLAVINVKRGKRYRFRVINISCIPSFTFSIDGHNLT 80

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346214843 241 IIEVDSINSQHLVVDSIQIFAAQRYSFVLNADQDVGNYWIRANPSFGNVGFAGGI-NSAILRYDGADPVE 309
Cdd:cd13882   81 VIEADGVETKPLTVDSVQIYAGQRYSVVVEANQPVDNYWIRAPPTGGTPANNGGQlNRAILRYKGAPEVE 150
CuRO_3_Tv-LCC_like cd13903
The third cupredoxin domain of the fungal laccases similar to Tv-LCC from Trametes Versicolor; ...
 343-491 2.36e-73

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: 229.09  E-value: 2.36e-73
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346214843 343 DKAINMAFNFNGTN--FFINGASFVPPTVPVLLQIISGAQNAQDLLPSGSVYSLPANADIEISFPATAAAPGAPhpFHLH 420
Cdd:cd13903    1 DVNITLTFGLNGTTglFTINGVSYVSPTVPVLLQILSGATSAEDLLPTESTIILPRNKVVEITIPGGAIGGPHP--FHLH 78

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 346214843 421 GHAFAVVRSAGSTVYNYDNPIFRDVVSTGTPaaGDNVTIRFRTDNPGPWFLHCHIDFHLEAGFAVVMAEDI 491
Cdd:cd13903   79 GHAFSVVRSAGSNTYNYVNPVRRDVVSVGTP--GDGVTIRFVTDNPGPWFLHCHIDWHLEAGLAVVFAEDP 147
ascorbase TIGR03388
L-ascorbate oxidase, plant type; Members of this protein family are the copper-containing ...
 37-496 5.21e-65

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: 220.01  E-value: 5.21e-65
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346214843   37 SPDGFARQAVVVNNVTPGPLVAGNKGDrfqlNVIDNLTNHTMLKSTSIHWHGFFQKGTNWADGPAFVNQCPISSGHSFLY 116
Cdd:TIGR03388  14 SPDCFEKLVIGINGQFPGPTIRAQAGD----TIVVELTNKLHTEGVVIHWHGIRQIGTPWADGTAGVTQCAINPGETFIY 89

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346214843  117 DFQVpDQAGTFWYHSHLSTQYCDGLRGPFVVyDPNDPHASLYDVDNDDTVItLADWYHTAA---KLG----PAFPLG-AD 188
Cdd:TIGR03388  90 NFVV-DRPGTYFYHGHYGMQRSAGLYGSLIV-DVPDGEKEPFHYDGEFNLL-LSDWWHKSIheqEVGlsskPMRWIGePQ 166

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346214843  189 ATLINGLGR-----SPSTTAADLAVINVTK-------------GKRYRFRLVSLSCDPNHTFSIDGHDLTIIEVDSINSQ 250
Cdd:TIGR03388 167 SLLINGRGQfncslAAKFSSTNLPQCNLKGneqcapqilhvepGKTYRLRIASTTALAALNFAIEGHKLTVVEADGNYVE 246

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346214843  251 HLVVDSIQIFAAQRYSFVLNADQDVG-NYWIRANPSFGNVGFAGGInsAILRYDGADPVEPTTTQTTPTKPLNEVDLHPL 329
Cdd:TIGR03388 247 PFTVKDIDIYSGETYSVLLTTDQDPSrNYWISVGVRGRKPNTPPGL--TVLNYYPNSPSRLPPTPPPVTPAWDDFDRSKA 324

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346214843  330 DTMA----PGSPV-AGGVDKAI---NMAFNFNG-TNFFINGASFVPPTVPVLLQIISGAQNAQDLLP------------- 387
Cdd:TIGR03388 325 FSLAikaaMGSPKpPETSDRRIvllNTQNKINGyTKWAINNVSLTLPHTPYLGSLKYNLLNAFDQKPppenyprdydifk 404

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346214843  388 ---------SGSVYSLPANADIEISFPATAAAPGAPHP---FHLHGHAFAVV--------RSAGSTVYNYDNPIFRDVVS 447
Cdd:TIGR03388 405 pppnpntttGNGIYRLKFNTTVDVILQNANTLNGNNSEthpWHLHGHDFWVLgygegkfrPGVDEKSYNLKNPPLRNTVV 484

                         490       500       510       520       530
                  ....*....|....*....|....*....|....*....|....*....|..
gi 346214843  448 T---GTPAagdnvtIRFRTDNPGPWFLHCHIDFHLEAGFAVVMAEDIPDVAS 496
Cdd:TIGR03388 485 IfpyGWTA------LRFVADNPGVWAFHCHIEPHLHMGMGVVFAEGVEKVGK 530
PLN02604 PLN02604
oxidoreductase
 37-496 1.23e-56

oxidoreductase


Pssm-ID: 215324 [Multi-domain]  Cd Length: 566  Bit Score: 198.16  E-value: 1.23e-56
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346214843  37 SPDGFARQAVVVNNVTPGPLVAGNKGDrfqlNVIDNLTNHTMLKSTSIHWHGFFQKGTNWADGPAFVNQCPISSGHSFLY 116
Cdd:PLN02604  37 SPDCFKKLVITINGRSPGPTILAQQGD----TVIVELKNSLLTENVAIHWHGIRQIGTPWFDGTEGVTQCPILPGETFTY 112

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346214843 117 DFQVpDQAGTFWYHSHLSTQYCDGLRGPFVVYDPN---DPHAslYDVDNDdtvITLADWYHT-----AAKLGpAFPLG-- 186
Cdd:PLN02604 113 EFVV-DRPGTYLYHAHYGMQREAGLYGSIRVSLPRgksEPFS--YDYDRS---IILTDWYHKstyeqALGLS-SIPFDwv 185

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346214843 187 --ADATLINGLGR------SPSTTAADLA----------VINVTKGKRYRFRLVSLSCDPNHTFSIDGHDLTIIEVDSIN 248
Cdd:PLN02604 186 gePQSLLIQGKGRyncslvSSPYLKAGVCnatnpecspyVLTVVPGKTYRLRISSLTALSALSFQIEGHNMTVVEADGHY 265

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346214843 249 SQHLVVDSIQIFAAQRYSFVLNADQDVG-NYWIRANPSFGNVGFAGGInsAILRYDGADPVEPTTTQTTPTKPLNEVDLH 327
Cdd:PLN02604 266 VEPFVVKNLFIYSGETYSVLVKADQDPSrNYWVTTSVVSRNNTTPPGL--AIFNYYPNHPRRSPPTVPPSGPLWNDVEPR 343

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346214843 328 PLDTMA---------PGSPVAGGVDKAINMAFNFNGT-NFFINGASFVPPTVPVLLQIISGAQNAQDLLP---------- 387
Cdd:PLN02604 344 LNQSLAikarhgyihPPPLTSDRVIVLLNTQNEVNGYrRWSVNNVSFNLPHTPYLIALKENLTGAFDQTPppegydfany 423

                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346214843 388 -------------SGSVYSLPANADIEISFPATAAAPGAPHP---FHLHGHAFAVV--------RSAGSTVYNYDNPIFR 443
Cdd:PLN02604 424 diyakpnnsnatsSDSIYRLQFNSTVDIILQNANTMNANNSEthpWHLHGHDFWVLgygegkfnMSSDPKKYNLVDPIMK 503

                        490       500       510       520       530
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 346214843 444 DVVST---GTPAagdnvtIRFRTDNPGPWFLHCHIDFHLEAGFAVVMAEDIPDVAS 496
Cdd:PLN02604 504 NTVPVhpyGWTA------LRFRADNPGVWAFHCHIESHFFMGMGVVFEEGIERVGK 553
Cu-oxidase pfam00394
Multicopper oxidase; Many of the proteins in this family contain multiple similar copies of ...
 163-305 1.54e-53

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: 177.51  E-value: 1.54e-53
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346214843  163 DDTVITLADWYHTAAK-----------LGPAFPLGADATLINGlgrspsTTAADLAVINVTKGKRYRFRLVSLSCDPNHT 231
Cdd:pfam00394   1 EDYVITLSDWYHKDAKdlekellasgkAPTDFPPVPDAVLING------KDGASLATLTVTPGKTYRLRIINVALDDSLN 74

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 346214843  232 FSIDGHDLTIIEVDSINSQHLVVDSIQIFAAQRYSFVLNADQDVGNYWIRANPSfgNVGFAGGINSAILRYDGA 305
Cdd:pfam00394  75 FSIEGHKMTVVEVDGVYVNPFTVDSLDIFPGQRYSVLVTANQDPGNYWIVASPN--IPAFDNGTAAAILRYSGA 146
SufI COG2132
Multicopper oxidase with three cupredoxin domains (includes cell division protein FtsP and ...
 24-486 6.46e-48

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: 171.27  E-value: 6.46e-48
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346214843  24 GPTADLTISNAEVS-PDGFARQAVVVNNVTPGPLVAGNKGDRFQLNVIDNLTNHTmlkstSIHWHGFFQKGTNwaDGPAF 102
Cdd:COG2132   13 GREYELTAQPATVElLPGKPTTVWGYNGQYPGPTIRVREGDRVRVRVTNRLPEPT-----TVHWHGLRVPNAM--DGVPG 85

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346214843 103 VnqcPISSGHSFLYDFQVPDQAGTFWYHSHL----STQYCDGLRGPFVVYDPNDPhasLYDVDnDDTVITLADW------ 172
Cdd:COG2132   86 D---PIAPGETFTYEFPVPQPAGTYWYHPHThgstAEQVYRGLAGALIVEDPEED---LPRYD-RDIPLVLQDWrldddg 158

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346214843 173 ---YHTAAKLGPAFPlgaDATLINGlgrspsttaADLAVINVTKGKRYRFRLVSLSCDPNHTFSI-DGHDLTIIEVDSIN 248
Cdd:COG2132  159 qllYPMDAAMGGRLG---DTLLVNG---------RPNPTLEVRPGERVRLRLLNASNARIYRLALsDGRPFTVIATDGGL 226

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346214843 249 -SQHLVVDSIQIFAAQRYSFVLNADQDVGNYWIRANPSFGNVGFAGginsAILRYDGADPVEPTTTQttptkplnevdLH 327
Cdd:COG2132  227 lPAPVEVDELLLAPGERADVLVDFSADPGEEVTLANPFEGRSGRAL----LTLRVTGAAASAPLPAN-----------LA 291

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346214843 328 PLDTMAPGSPVaggVDKAINMAFNFNGTNFFINGASFVPPTVPVLLQIisgaqnaqdllpsGSVYslpanaDIEISfpat 407
Cdd:COG2132  292 PLPDLEDREAV---RTRELVLTGGMAGYVWTINGKAFDPDRPDLTVKL-------------GERE------RWTLV---- 345

                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346214843 408 aAAPGAPHPFHLHGHAFAVVRSAGSTVynyDNPIFRDVVSTGtpaAGDNVTIRFRTDN-PGPWFLHCHIDFHLEAG---- 482
Cdd:COG2132  346 -NDTMMPHPFHLHGHQFQVLSRNGKPP---PEGGWKDTVLVP---PGETVRILFRFDNyPGDWMFHCHILEHEDAGmmgq 418


                 ....
gi 346214843 483 FAVV 486
Cdd:COG2132  419 FEVV 422
Cu-oxidase_3 pfam07732
Multicopper oxidase; This entry contains many divergent copper oxidase-like domains that are ...
 30-152 9.20e-44

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: 150.86  E-value: 9.20e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346214843   30 TISNAEVSPDGFARQAVV-VNNVTPGPLVAGNKGDRFQLNVIDNLTNhtmlkSTSIHWHGFFQKGTNWADGPAFVNQCPI 108
Cdd:pfam07732   1 TVTYGTVSPLGGTRQAVIgVNGQFPGPTIRVREGDTVVVNVTNNLDE-----PTSIHWHGLQQRGTPWMDGVPGVTQCPI 75

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 346214843  109 SSGHSFLYDFQVPDQAGTFWYHSHLSTQYCDGLRGPFVVYDPND 152
Cdd:pfam07732  76 PPGQSFTYRFQVKQQAGTYWYHSHTSGQQAAGLAGAIIIEDRAS 119
Cu-oxidase_2 pfam07731
Multicopper oxidase; This entry contains many divergent copper oxidase-like domains that are ...
 364-493 1.18e-31

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: 118.69  E-value: 1.18e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346214843  364 FVPPTVPVLLQIISGAQ-------NAQDLLPSGSVYSLPANADIEISFPATAAAPGAphpFHLHGHAFAVVRS------- 429
Cdd:pfam07731   1 DTPPKLPTLLQITSGNFrrndwaiNGLLFPPNTNVITLPYGTVVEWVLQNTTTGVHP---FHLHGHSFQVLGRgggpwpe 77

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 346214843  430 AGSTVYNYDNPIFRDVVSTGtpaAGDNVTIRFRTDNPGPWFLHCHIDFHLEAGFAVVMAEDIPD 493
Cdd:pfam07731  78 EDPKTYNLVDPVRRDTVQVP---PGGWVAIRFRADNPGVWLFHCHILWHLDQGMMGQFVVRPGD 138
PLN02354 PLN02354
copper ion binding / oxidoreductase
 36-305 1.56e-27

copper ion binding / oxidoreductase


Pssm-ID: 177987 [Multi-domain]  Cd Length: 552  Bit Score: 116.04  E-value: 1.56e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346214843  36 VSPDGFARQAVVVNNVTPGPLVAGNKGDRFQLNVIDNLtNHTMLkstsIHWHGFFQKGTNWADGPAFVNqCPISSGHSFL 115
Cdd:PLN02354  39 ASPLGVPQQVILINGQFPGPNINSTSNNNIVINVFNNL-DEPFL----LTWSGIQQRKNSWQDGVPGTN-CPIPPGTNFT 112

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346214843 116 YDFQVPDQAGTFWYHSHLSTQYCDGLRGPFVVydpndpHASL-----YDVDNDDTVITLADWY---HTAAK--LGPAFPL 185
Cdd:PLN02354 113 YHFQPKDQIGSYFYYPSTGMHRAAGGFGGLRV------NSRLlipvpYADPEDDYTVLIGDWYtksHTALKkfLDSGRTL 186

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346214843 186 G-ADATLINGlgRSPSTTAADLAVINVTKGKRYRFRLVSLSCDPNHTFSIDGHDLTIIEVDSINSQHLVVDSIQIFAAQR 264
Cdd:PLN02354 187 GrPDGVLING--KSGKGDGKDEPLFTMKPGKTYRYRICNVGLKSSLNFRIQGHKMKLVEMEGSHVLQNDYDSLDVHVGQC 264

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|.
gi 346214843 265 YSFVLNADQDVGNYWIRANPSFGNVGFAGginSAILRYDGA 305
Cdd:PLN02354 265 FSVLVTANQAPKDYYMVASTRFLKKVLTT---TGIIRYEGG 302
 
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; ...
 25-149 8.77e-80

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: 244.94  E-value: 8.77e-80
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346214843  25 PTADLTISNAEVSPDGFARQAVVVNNVTPGPLVAGNKGDRFQLNVIDNLTNHTMLKSTSIHWHGFFQKGTNWADGPAFVN 104
Cdd:cd13856    1 PTYTLNIVNTRLAPDGFERSAVLANGQFPGPLITANKGDTFRITVVNQLTDPTMRRSTSIHWHGIFQHGTNYADGPAFVT 80

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*
gi 346214843 105 QCPISSGHSFLYDFQVPDQAGTFWYHSHLSTQYCDGLRGPFVVYD 149
Cdd:cd13856   81 QCPIAPNHSFTYDFTAGDQAGTFWYHSHLSTQYCDGLRGPLVIYD 125
CuRO_2_Tv-LCC_like cd13882
The second cupredoxin domain of the fungal laccases similar to Tv-LCC from Trametes versicolor; ...
 165-309 2.80e-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: 239.62  E-value: 2.80e-77
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346214843 165 TVITLADWYHTAAKLGPA----FPLGADATLINGLGRSPSTTAADLAVINVTKGKRYRFRLVSLSCDPNHTFSIDGHDLT 240
Cdd:cd13882    1 TVITLGDWYHTAAPDLLAttagVPPVPDSGTINGKGRFDGGPTSPLAVINVKRGKRYRFRVINISCIPSFTFSIDGHNLT 80

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346214843 241 IIEVDSINSQHLVVDSIQIFAAQRYSFVLNADQDVGNYWIRANPSFGNVGFAGGI-NSAILRYDGADPVE 309
Cdd:cd13882   81 VIEADGVETKPLTVDSVQIYAGQRYSVVVEANQPVDNYWIRAPPTGGTPANNGGQlNRAILRYKGAPEVE 150
CuRO_3_Tv-LCC_like cd13903
The third cupredoxin domain of the fungal laccases similar to Tv-LCC from Trametes Versicolor; ...
 343-491 2.36e-73

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: 229.09  E-value: 2.36e-73
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346214843 343 DKAINMAFNFNGTN--FFINGASFVPPTVPVLLQIISGAQNAQDLLPSGSVYSLPANADIEISFPATAAAPGAPhpFHLH 420
Cdd:cd13903    1 DVNITLTFGLNGTTglFTINGVSYVSPTVPVLLQILSGATSAEDLLPTESTIILPRNKVVEITIPGGAIGGPHP--FHLH 78

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 346214843 421 GHAFAVVRSAGSTVYNYDNPIFRDVVSTGTPaaGDNVTIRFRTDNPGPWFLHCHIDFHLEAGFAVVMAEDI 491
Cdd:cd13903   79 GHAFSVVRSAGSNTYNYVNPVRRDVVSVGTP--GDGVTIRFVTDNPGPWFLHCHIDWHLEAGLAVVFAEDP 147
ascorbase TIGR03388
L-ascorbate oxidase, plant type; Members of this protein family are the copper-containing ...
 37-496 5.21e-65

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: 220.01  E-value: 5.21e-65
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346214843   37 SPDGFARQAVVVNNVTPGPLVAGNKGDrfqlNVIDNLTNHTMLKSTSIHWHGFFQKGTNWADGPAFVNQCPISSGHSFLY 116
Cdd:TIGR03388  14 SPDCFEKLVIGINGQFPGPTIRAQAGD----TIVVELTNKLHTEGVVIHWHGIRQIGTPWADGTAGVTQCAINPGETFIY 89

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346214843  117 DFQVpDQAGTFWYHSHLSTQYCDGLRGPFVVyDPNDPHASLYDVDNDDTVItLADWYHTAA---KLG----PAFPLG-AD 188
Cdd:TIGR03388  90 NFVV-DRPGTYFYHGHYGMQRSAGLYGSLIV-DVPDGEKEPFHYDGEFNLL-LSDWWHKSIheqEVGlsskPMRWIGePQ 166

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346214843  189 ATLINGLGR-----SPSTTAADLAVINVTK-------------GKRYRFRLVSLSCDPNHTFSIDGHDLTIIEVDSINSQ 250
Cdd:TIGR03388 167 SLLINGRGQfncslAAKFSSTNLPQCNLKGneqcapqilhvepGKTYRLRIASTTALAALNFAIEGHKLTVVEADGNYVE 246

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346214843  251 HLVVDSIQIFAAQRYSFVLNADQDVG-NYWIRANPSFGNVGFAGGInsAILRYDGADPVEPTTTQTTPTKPLNEVDLHPL 329
Cdd:TIGR03388 247 PFTVKDIDIYSGETYSVLLTTDQDPSrNYWISVGVRGRKPNTPPGL--TVLNYYPNSPSRLPPTPPPVTPAWDDFDRSKA 324

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346214843  330 DTMA----PGSPV-AGGVDKAI---NMAFNFNG-TNFFINGASFVPPTVPVLLQIISGAQNAQDLLP------------- 387
Cdd:TIGR03388 325 FSLAikaaMGSPKpPETSDRRIvllNTQNKINGyTKWAINNVSLTLPHTPYLGSLKYNLLNAFDQKPppenyprdydifk 404

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346214843  388 ---------SGSVYSLPANADIEISFPATAAAPGAPHP---FHLHGHAFAVV--------RSAGSTVYNYDNPIFRDVVS 447
Cdd:TIGR03388 405 pppnpntttGNGIYRLKFNTTVDVILQNANTLNGNNSEthpWHLHGHDFWVLgygegkfrPGVDEKSYNLKNPPLRNTVV 484

                         490       500       510       520       530
                  ....*....|....*....|....*....|....*....|....*....|..
gi 346214843  448 T---GTPAagdnvtIRFRTDNPGPWFLHCHIDFHLEAGFAVVMAEDIPDVAS 496
Cdd:TIGR03388 485 IfpyGWTA------LRFVADNPGVWAFHCHIEPHLHMGMGVVFAEGVEKVGK 530
laccase TIGR03389
laccase, plant; Members of this protein family include the copper-containing enzyme laccase ...
 42-486 1.28e-58

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: 203.05  E-value: 1.28e-58
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346214843   42 ARQAVVVNNVTPGPLVAGNKGDRFQLNVIDNLTNhtmlkSTSIHWHGFFQKGTNWADGPAFVNQCPISSGHSFLYDFQVP 121
Cdd:TIGR03389  21 TKSILTVNGKFPGPTLYAREGDTVIVNVTNNVQY-----NVTIHWHGVRQLRNGWADGPAYITQCPIQPGQSYVYNFTIT 95

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346214843  122 DQAGTFWYHSHLS----TQYcdglrGPFVVYdPNDPHASLYDVDNDDTVITLADWYHT--------AAKLGPAfPLGADA 189
Cdd:TIGR03389  96 GQRGTLWWHAHISwlraTVY-----GAIVIL-PKPGVPYPFPKPDREVPIILGEWWNAdveavinqANQTGGA-PNVSDA 168

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346214843  190 TLINGL-GRSPSTTAADLAVINVTKGKRYRFRLVSLSCDPNHTFSIDGHDLTIIEVDSINSQHLVVDSIQIFAAQRYSFV 268
Cdd:TIGR03389 169 YTINGHpGPLYNCSSKDTFKLTVEPGKTYLLRIINAALNDELFFAIANHTLTVVEVDATYTKPFKTKTIVIGPGQTTNVL 248

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346214843  269 LNADQDVGNYWIRANP-SFGNVGFAGGINSAILRYDGadPVEPTTTQTTPTKPLNEVD--------LHPLDTMAPGSPVA 339
Cdd:TIGR03389 249 LTADQSPGRYFMAARPyMDAPGAFDNTTTTAILQYKG--TSNSAKPILPTLPAYNDTAaatnfsnkLRSLNSAQYPANVP 326

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346214843  340 GGVDK----AINMAFN---------FNGTNFF--INGASFVPPTVPVL---LQIISG-----------------AQNAQD 384
Cdd:TIGR03389 327 VTIDRrlffTIGLGLDpcpnntcqgPNGTRFAasMNNISFVMPTTALLqahYFGISGvfttdfpanpptkfnytGTNLPN 406

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346214843  385 LL--PSGS-VYSLPANADIEISFPATAAAPGAPHPFHLHGHAFAVVrsaGSTVYNYD-----------NPIFRDVVstGT 450
Cdd:TIGR03389 407 NLftTNGTkVVRLKFNSTVELVLQDTSILGSENHPIHLHGYNFFVV---GTGFGNFDpkkdpakfnlvDPPERNTV--GV 481

                         490       500       510
                  ....*....|....*....|....*....|....*.
gi 346214843  451 PAAGdNVTIRFRTDNPGPWFLHCHIDFHLEAGFAVV 486
Cdd:TIGR03389 482 PTGG-WAAIRFVADNPGVWFMHCHLEVHTTWGLKMA 516
PLN02604 PLN02604
oxidoreductase
 37-496 1.23e-56

oxidoreductase


Pssm-ID: 215324 [Multi-domain]  Cd Length: 566  Bit Score: 198.16  E-value: 1.23e-56
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346214843  37 SPDGFARQAVVVNNVTPGPLVAGNKGDrfqlNVIDNLTNHTMLKSTSIHWHGFFQKGTNWADGPAFVNQCPISSGHSFLY 116
Cdd:PLN02604  37 SPDCFKKLVITINGRSPGPTILAQQGD----TVIVELKNSLLTENVAIHWHGIRQIGTPWFDGTEGVTQCPILPGETFTY 112

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346214843 117 DFQVpDQAGTFWYHSHLSTQYCDGLRGPFVVYDPN---DPHAslYDVDNDdtvITLADWYHT-----AAKLGpAFPLG-- 186
Cdd:PLN02604 113 EFVV-DRPGTYLYHAHYGMQREAGLYGSIRVSLPRgksEPFS--YDYDRS---IILTDWYHKstyeqALGLS-SIPFDwv 185

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346214843 187 --ADATLINGLGR------SPSTTAADLA----------VINVTKGKRYRFRLVSLSCDPNHTFSIDGHDLTIIEVDSIN 248
Cdd:PLN02604 186 gePQSLLIQGKGRyncslvSSPYLKAGVCnatnpecspyVLTVVPGKTYRLRISSLTALSALSFQIEGHNMTVVEADGHY 265

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346214843 249 SQHLVVDSIQIFAAQRYSFVLNADQDVG-NYWIRANPSFGNVGFAGGInsAILRYDGADPVEPTTTQTTPTKPLNEVDLH 327
Cdd:PLN02604 266 VEPFVVKNLFIYSGETYSVLVKADQDPSrNYWVTTSVVSRNNTTPPGL--AIFNYYPNHPRRSPPTVPPSGPLWNDVEPR 343

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346214843 328 PLDTMA---------PGSPVAGGVDKAINMAFNFNGT-NFFINGASFVPPTVPVLLQIISGAQNAQDLLP---------- 387
Cdd:PLN02604 344 LNQSLAikarhgyihPPPLTSDRVIVLLNTQNEVNGYrRWSVNNVSFNLPHTPYLIALKENLTGAFDQTPppegydfany 423

                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346214843 388 -------------SGSVYSLPANADIEISFPATAAAPGAPHP---FHLHGHAFAVV--------RSAGSTVYNYDNPIFR 443
Cdd:PLN02604 424 diyakpnnsnatsSDSIYRLQFNSTVDIILQNANTMNANNSEthpWHLHGHDFWVLgygegkfnMSSDPKKYNLVDPIMK 503

                        490       500       510       520       530
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 346214843 444 DVVST---GTPAagdnvtIRFRTDNPGPWFLHCHIDFHLEAGFAVVMAEDIPDVAS 496
Cdd:PLN02604 504 NTVPVhpyGWTA------LRFRADNPGVWAFHCHIESHFFMGMGVVFEEGIERVGK 553
PLN02191 PLN02191
L-ascorbate oxidase
 37-504 1.47e-53

L-ascorbate oxidase


Pssm-ID: 177843 [Multi-domain]  Cd Length: 574  Bit Score: 190.22  E-value: 1.47e-53
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346214843  37 SPDGFARQAVVVNNVTPGPLVAGNKGDRFQLNVIDNLTNHTMLkstsIHWHGFFQKGTNWADGPAFVNQCPISSGHSFLY 116
Cdd:PLN02191  36 WPDCKEGAVMTVNGQFPGPTIDAVAGDTIVVHLTNKLTTEGLV----IHWHGIRQKGSPWADGAAGVTQCAINPGETFTY 111

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346214843 117 DFQVpDQAGTFWYHSHLSTQYCDGLRGPFVVYDPNDPHASL-YDVDNDdtvITLADWYHTAAklgPAFPLG--------- 186
Cdd:PLN02191 112 KFTV-EKPGTHFYHGHYGMQRSAGLYGSLIVDVAKGPKERLrYDGEFN---LLLSDWWHESI---PSQELGlsskpmrwi 184

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346214843 187 --ADATLINGLGRSPSTTAADLA-------------------VINVTKGKRYRFRLVSLSCDPNHTFSIDGHDLTIIEVD 245
Cdd:PLN02191 185 geAQSILINGRGQFNCSLAAQFSngtelpmctfkegdqcapqTLRVEPNKTYRIRLASTTALASLNLAVQGHKLVVVEAD 264

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346214843 246 SINSQHLVVDSIQIFAAQRYSFVLNADQDVG-NYWIranpSFGNVGFAGGINSA--ILRYDGADPVEPTTTQTTPTKPLN 322
Cdd:PLN02191 265 GNYITPFTTDDIDIYSGESYSVLLTTDQDPSqNYYI----SVGVRGRKPNTTQAltILNYVTAPASKLPSSPPPVTPRWD 340

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346214843 323 EVDLHP------LDTMAPGSPVAGGVDKAI--NMAFNFNG-TNFFINGASFVPPTVPVLLQIISGAQNAQDL-------- 385
Cdd:PLN02191 341 DFERSKnfskkiFSAMGSPSPPKKYRKRLIllNTQNLIDGyTKWAINNVSLVTPATPYLGSVKYNLKLGFNRkspprsyr 420

                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346214843 386 -------------LPSGS-VYSLPANADIEISFPATAAAPGAPHP---FHLHGHAFAVV--------RSAGSTVYNYDNP 440
Cdd:PLN02191 421 mdydimnpppfpnTTTGNgIYVFPFNVTVDVIIQNANVLKGVVSEihpWHLHGHDFWVLgygdgkfkPGIDEKTYNLKNP 500

                        490       500       510       520       530       540       550
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 346214843 441 IFRDVV---STGTPAagdnvtIRFRTDNPGPWFLHCHIDFHLEAGFAVVMAE------DIPDVASANPVPQAW 504
Cdd:PLN02191 501 PLRNTAilyPYGWTA------IRFVTDNPGVWFFHCHIEPHLHMGMGVVFAEglnrigKIPDEALGCGLTKQF 567
Cu-oxidase pfam00394
Multicopper oxidase; Many of the proteins in this family contain multiple similar copies of ...
 163-305 1.54e-53

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: 177.51  E-value: 1.54e-53
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346214843  163 DDTVITLADWYHTAAK-----------LGPAFPLGADATLINGlgrspsTTAADLAVINVTKGKRYRFRLVSLSCDPNHT 231
Cdd:pfam00394   1 EDYVITLSDWYHKDAKdlekellasgkAPTDFPPVPDAVLING------KDGASLATLTVTPGKTYRLRIINVALDDSLN 74

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 346214843  232 FSIDGHDLTIIEVDSINSQHLVVDSIQIFAAQRYSFVLNADQDVGNYWIRANPSfgNVGFAGGINSAILRYDGA 305
Cdd:pfam00394  75 FSIEGHKMTVVEVDGVYVNPFTVDSLDIFPGQRYSVLVTANQDPGNYWIVASPN--IPAFDNGTAAAILRYSGA 146
CuRO_1_Diphenol_Ox cd13857
The first cupredoxin domain of fungal laccase, diphenol oxidase; Diphenol oxidase belongs to ...
 28-148 3.46e-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: 167.82  E-value: 3.46e-50
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346214843  28 DLTISNAEVSPDGFARQAVVVNNVTPGPLVAGNKGDRFQLNVIDNLTNhtmlkSTSIHWHGFFQKGTNWADGPAFVNQCP 107
Cdd:cd13857    4 NFTISEITGAPDGFVRPMLVINGQFPGPLIEANQGDRIVVHVTNELDE-----PTSIHWHGLFQNGTNWMDGTAGITQCP 78

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|.
gi 346214843 108 ISSGHSFLYDFQVPDQAGTFWYHSHLSTQYCDGLRGPFVVY 148
Cdd:cd13857   79 IPPGGSFTYNFTVDGQYGTYWYHSHYSTQYADGLVGPLIVH 119
SufI COG2132
Multicopper oxidase with three cupredoxin domains (includes cell division protein FtsP and ...
 24-486 6.46e-48

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: 171.27  E-value: 6.46e-48
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346214843  24 GPTADLTISNAEVS-PDGFARQAVVVNNVTPGPLVAGNKGDRFQLNVIDNLTNHTmlkstSIHWHGFFQKGTNwaDGPAF 102
Cdd:COG2132   13 GREYELTAQPATVElLPGKPTTVWGYNGQYPGPTIRVREGDRVRVRVTNRLPEPT-----TVHWHGLRVPNAM--DGVPG 85

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346214843 103 VnqcPISSGHSFLYDFQVPDQAGTFWYHSHL----STQYCDGLRGPFVVYDPNDPhasLYDVDnDDTVITLADW------ 172
Cdd:COG2132   86 D---PIAPGETFTYEFPVPQPAGTYWYHPHThgstAEQVYRGLAGALIVEDPEED---LPRYD-RDIPLVLQDWrldddg 158

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346214843 173 ---YHTAAKLGPAFPlgaDATLINGlgrspsttaADLAVINVTKGKRYRFRLVSLSCDPNHTFSI-DGHDLTIIEVDSIN 248
Cdd:COG2132  159 qllYPMDAAMGGRLG---DTLLVNG---------RPNPTLEVRPGERVRLRLLNASNARIYRLALsDGRPFTVIATDGGL 226

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346214843 249 -SQHLVVDSIQIFAAQRYSFVLNADQDVGNYWIRANPSFGNVGFAGginsAILRYDGADPVEPTTTQttptkplnevdLH 327
Cdd:COG2132  227 lPAPVEVDELLLAPGERADVLVDFSADPGEEVTLANPFEGRSGRAL----LTLRVTGAAASAPLPAN-----------LA 291

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346214843 328 PLDTMAPGSPVaggVDKAINMAFNFNGTNFFINGASFVPPTVPVLLQIisgaqnaqdllpsGSVYslpanaDIEISfpat 407
Cdd:COG2132  292 PLPDLEDREAV---RTRELVLTGGMAGYVWTINGKAFDPDRPDLTVKL-------------GERE------RWTLV---- 345

                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346214843 408 aAAPGAPHPFHLHGHAFAVVRSAGSTVynyDNPIFRDVVSTGtpaAGDNVTIRFRTDN-PGPWFLHCHIDFHLEAG---- 482
Cdd:COG2132  346 -NDTMMPHPFHLHGHQFQVLSRNGKPP---PEGGWKDTVLVP---PGETVRILFRFDNyPGDWMFHCHILEHEDAGmmgq 418


                 ....
gi 346214843 483 FAVV 486
Cdd:COG2132  419 FEVV 422
CuRO_1_LCC_like cd04206
Cupredoxin domain 1 of laccase-like multicopper oxidases; including laccase, CueO, spore coat ...
 25-148 2.71e-47

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: 160.14  E-value: 2.71e-47
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346214843  25 PTADLTISNAEVSPDGFARQAVVVNNVTPGPLVAGNKGDRFQLNVIDNLTNhtmlKSTSIHWHGFFQKGTNWADGPAFVN 104
Cdd:cd04206    1 REYELTITETTVNPDGVLRQVITVNGQFPGPTIRVKEGDTVEVTVTNNLPN----EPTSIHWHGLRQPGTNDGDGVAGLT 76

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....
gi 346214843 105 QCPISSGHSFLYDFQVPDQAGTFWYHSHLSTQYCDGLRGPFVVY 148
Cdd:cd04206   77 QCPIPPGESFTYRFTVDDQAGTFWYHSHVGGQRADGLYGPLIVE 120
Cu-oxidase_3 pfam07732
Multicopper oxidase; This entry contains many divergent copper oxidase-like domains that are ...
 30-152 9.20e-44

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: 150.86  E-value: 9.20e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346214843   30 TISNAEVSPDGFARQAVV-VNNVTPGPLVAGNKGDRFQLNVIDNLTNhtmlkSTSIHWHGFFQKGTNWADGPAFVNQCPI 108
Cdd:pfam07732   1 TVTYGTVSPLGGTRQAVIgVNGQFPGPTIRVREGDTVVVNVTNNLDE-----PTSIHWHGLQQRGTPWMDGVPGVTQCPI 75

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 346214843  109 SSGHSFLYDFQVPDQAGTFWYHSHLSTQYCDGLRGPFVVYDPND 152
Cdd:pfam07732  76 PPGQSFTYRFQVKQQAGTYWYHSHTSGQQAAGLAGAIIIEDRAS 119
CuRO_1_Fet3p cd13851
The first Cupredoxin domain of multicopper oxidase Fet3P; Fet3p catalyzes the ferroxidase ...
 28-147 5.20e-43

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: 148.95  E-value: 5.20e-43
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346214843  28 DLTISNAEVSPDG-FARQAVVVNNVTPGPLVAGNKGDRFQLNVIDNLTNhtmlKSTSIHWHGFFQKGTNWADGPAFVNQC 106
Cdd:cd13851    4 DWNITWVTANPDGlFERRVIGINGQWPPPPIEVNKGDTVVIHATNSLGD----QPTSLHFHGLFQNGTNYMDGPVGVTQC 79

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|.
gi 346214843 107 PISSGHSFLYDFQVPDQAGTFWYHSHLSTQYCDGLRGPFVV 147
Cdd:cd13851   80 PIPPGQSFTYEFTVDTQVGTYWYHSHDGGQYPDGLRGPFII 120
CuRO_1_MaLCC_like cd13854
The first cupredoxin domain of the fungal laccases similar to Ma-LCC from Melanocarpus ...
 28-148 9.88e-42

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


Pssm-ID: 259923 [Multi-domain]  Cd Length: 122  Bit Score: 145.46  E-value: 9.88e-42
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346214843  28 DLTISNAEVSPDGFARQAVVVNNVTPGPLVAGNKGDRFQLNVIDNLTNHtmlkSTSIHWHGFFQKGTNWADGPAFVNQCP 107
Cdd:cd13854    7 TLTITNSTLAPDGVEKEVMLINGQYPGPLIEANWGDTIEVTVINKLQDN----GTSIHWHGIRQLNTNWQDGVPGVTECP 82

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|.
gi 346214843 108 ISSGHSFLYDFQVpDQAGTFWYHSHLSTQYCDGLRGPFVVY 148
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; ...
 39-147 1.56e-37

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: 133.43  E-value: 1.56e-37
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346214843  39 DGFARQAVVVNNVTPGPLVAGNKGDRfqlnVIDNLTNHTMLKSTSIHWHGFFQKGTNWADGPAFVNQCPISSGHSFLYDF 118
Cdd:cd13858    1 DGVERPVITVNGQLPGPSIEVCEGDT----VVVDVKNRLPGESTTIHWHGIHQRGTPYMDGVPMVTQCPILPGQTFRYKF 76

                         90       100
                 ....*....|....*....|....*....
gi 346214843 119 QVpDQAGTFWYHSHLSTQYCDGLRGPFVV 147
Cdd:cd13858   77 KA-DPAGTHWYHSHSGTQRADGLFGALIV 104
ascorbOXfungal TIGR03390
L-ascorbate oxidase, fungal type; This model describes a family of fungal ascorbate oxidases, ...
 29-491 5.69e-37

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: 143.44  E-value: 5.69e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346214843   29 LTISNAEVSPDGFARQAVVVNNVTPGPLVAGNKGDRFQLNVIDNLTNhtmlKSTSIHWHGFFQKGTNWADGPAFVNQCPI 108
Cdd:TIGR03390  13 LRVTSDNIKIACSSRYSVVVNGTSPGPEIRLQEGQTTWIRVYNDIPD----NNVTMHWHGLTQRTAPFSDGTPLASQWPI 88

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346214843  109 SSGHSFLYDFQV-PDQAGTFWYHSHLSTQYCDGlRGPFVVYDPNDPHaslYDVDnDDTVITLADWYHTAAK------LGP 181
Cdd:TIGR03390  89 PPGHFFDYEIKPePGDAGSYFYHSHVGFQAVTA-FGPLIVEDCEPPP---YKYD-DERILLVSDFFSATDEeieqglLST 163

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346214843  182 AF--PLGADATLINGLGRSPSTTAAD-------LAVINVTKGKRYRFRLVSLSCDPNHTFSIDGHD-LTIIEVDSINSQH 251
Cdd:TIGR03390 164 PFtwSGETEAVLLNGKSGNKSFYAQInpsgscmLPVIDVEPGKTYRLRFIGATALSLISLGIEDHEnLTIIEADGSYTKP 243

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346214843  252 LVVDSIQIFAAQRYSFVLNA-------DQDVGNYWI----RANPSFGNvGFagginsAILRY--DGADPVEPTTTQTTPT 318
Cdd:TIGR03390 244 AKIDHLQLGGGQRYSVLFKAktedelcGGDKRQYFIqfetRDRPKVYR-GY------AVLRYrsDKASKLPSVPETPPLP 316

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346214843  319 KPLN-----EVDLHPLDTMA-PGSPVAGGVDK--AINMAFNFNGTN----FFINGASFVP--PTVPVLLQIisgAQNAQD 384
Cdd:TIGR03390 317 LPNStydwlEYELEPLSEENnQDFPTLDEVTRrvVIDAHQNVDPLNgrvaWLQNGLSWTEsvRQTPYLVDI---YENGLP 393

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346214843  385 LLPS-----------GSVYSLPANAD--IEISFPATAAAPGAPHP-----FHLHGHAFAVVRSaGSTVYNYD-------- 438
Cdd:TIGR03390 394 ATPNytaalanygfdPETRAFPAKVGevLEIVWQNTGSYTGPNGGvdthpFHAHGRHFYDIGG-GDGEYNATaneaklen 472

                         490       500       510       520       530       540
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 346214843  439 -NPIFRDV---------VSTGTPAAGDnvTIRFRTDNPGPWFLHCHIDFHLEAGFAVVM----AEDI 491
Cdd:TIGR03390 473 yTPVLRDTtmlyryavkVVPGAPAGWR--AWRIRVTNPGVWMMHCHILQHMVMGMQTVWvfgdAEDI 537
CuRO_2_tcLCC_insect_like cd13884
The second cupredoxin domain of the insect laccases similar to laccase 2 in Tribolium ...
 166-302 4.55e-35

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: 128.50  E-value: 4.55e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346214843 166 VITLADWYHTAA------KLGPAFPLGADATLINGLGRSPS-----TTAADLAVINVTKGKRYRFRLVSLSCDpNHTF-- 232
Cdd:cd13884    3 VILIQDWTHELSserfvgRGHNGGGQPPDSILINGKGRYYDpktgnTNNTPLEVFTVEQGKRYRFRLINAGAT-NCPFrv 81

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346214843 233 SIDGHDLTIIEVDSINSQHLVVDSIQIFAAQRYSFVLNADQDVGNYWIRANpSFGNVGFAGGINSAILRY 302
Cdd:cd13884   82 SIDGHTLTVIASDGNDVEPVEVDSIIIYPGERYDFVLNANQPIGNYWIRAR-GLEDCDNRRLQQLAILRY 150
CuRO_2_LCC_like cd04205
Cupredoxin domain 2 of laccase-like multicopper oxidases; including laccase, CueO, spore coat ...
 166-302 2.90e-33

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: 123.62  E-value: 2.90e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346214843 166 VITLADWYHTAAKLGPAF--------PLGADATLINGLGRSPSTTAAD-----LAVINVTKGKRYRFRLVSLSCDPNHTF 232
Cdd:cd04205    2 VLLLSDWYHDSAEDVLAGympnsfgnEPVPDSLLINGRGRFNCSMAVCnsgcpLPVITVEPGKTYRLRLINAGSFASFNF 81

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 346214843 233 SIDGHDLTIIEVDSINSQHLVVDSIQIFAAQRYSFVLNADQDVGNYWIRANPSFGNVGFAGGIN-SAILRY 302
Cdd:cd04205   82 AIDGHNMTVIEVDGGYVEPLEVDNLDLAPGQRYDVLVKADQPPGNYWIRASADGRTFDEGGNPNgTAILRY 152
PLN02792 PLN02792
oxidoreductase
 28-471 1.34e-32

oxidoreductase


Pssm-ID: 178389 [Multi-domain]  Cd Length: 536  Bit Score: 130.87  E-value: 1.34e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346214843  28 DLTISNAEVSPDGFARQAVVVNNVTPGPLVAGNKGDRFQLNVIDNLTNHTMLKstsihWHGFFQKGTNWADGpAFVNQCP 107
Cdd:PLN02792  20 NWRVTYGNISLLTLPRRGILINGQFPGPEIRSLTNDNLVINVHNDLDEPFLLS-----WNGVHMRKNSYQDG-VYGTTCP 93

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346214843 108 ISSGHSFLYDFQVPDQAGTFWYHSHLSTQYCDGLRGPFVVYD-PNDPHAslYDVDNDDTVITLADWY---HTAAKL---- 179
Cdd:PLN02792  94 IPPGKNYTYDFQVKDQVGSYFYFPSLAVQKAAGGYGSLRIYSlPRIPVP--FPEPAGDFTFLIGDWYrrnHTTLKKildg 171

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346214843 180 GPAFPLGADATLINGLGRSPSTTaadlavINVTKGKRYRFRLVSLSCDPNHTFSIDGHDLTIIEVDSINSQHLVVDSIQI 259
Cdd:PLN02792 172 GRKLPLMPDGVMINGQGVSYVYS------ITVDKGKTYRFRISNVGLQTSLNFEILGHQLKLIEVEGTHTVQSMYTSLDI 245

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346214843 260 FAAQRYSFVLNADQDVGNYWIRANPSFGN--------VGFAGGINSAILRYDGADPVEPTTTQTTPTKPLNEVDLHPLDT 331
Cdd:PLN02792 246 HVGQTYSVLVTMDQPPQNYSIVVSTRFIAakvlvsstLHYSNSKGHKIIHARQPDPDDLEWSIKQAQSIRTNLTASGPRT 325

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346214843 332 MAPGSPVAGGVDKAINMAFNFNGT------NFFINGASFVPPTVPVLLqiiSGAQNAQDLLPSGSVYSLPA--------- 396
Cdd:PLN02792 326 NPQGSYHYGKMKISRTLILESSAAlvkrkqRYAINGVSFVPSDTPLKL---ADHFKIKGVFKVGSIPDKPRrgggmrldt 402

                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346214843 397 -------NADIEISFpatAAAPGAPHPFHLHGHAFAVV-------RSAGSTVYNydnpiFRDVVSTGT----PAAGDNVT 458
Cdd:PLN02792 403 svmgahhNAFLEIIF---QNREKIVQSYHLDGYNFWVVginkgiwSRASRREYN-----LKDAISRSTtqvyPESWTAVY 474

                        490
                 ....*....|...
gi 346214843 459 IRFrtDNPGPWFL 471
Cdd:PLN02792 475 VAL--DNVGMWNL 485
CuRO_1_Abr2_like cd13850
The first cupredoxin domain of a group of fungal Laccases similar to Abr2 from Aspergillus ...
 28-147 4.09e-32

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: 119.32  E-value: 4.09e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346214843  28 DLTISNAEVSPDGFARQAVVVNNVTPGPLVAGNKGDRFQLNVIDNLTnhtmlKSTSIHWHGFFQKGTNWADGPAFVNQCP 107
Cdd:cd13850    2 TLTVTEGSPDGDGGEREVILINGQFPGPPIILDEGDEVEILVTNNLP-----VNTTIHFHGILQRGTPWSDGVPGVTQWP 76

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|
gi 346214843 108 ISSGHSFLYDFQVPDQAGTFWYHSHLSTQYCDGLRGPFVV 147
Cdd:cd13850   77 IQPGGSFTYRWKAEDQYGLYWYHSHYRGYYMDGLYGPIYI 116
Cu-oxidase_2 pfam07731
Multicopper oxidase; This entry contains many divergent copper oxidase-like domains that are ...
 364-493 1.18e-31

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: 118.69  E-value: 1.18e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346214843  364 FVPPTVPVLLQIISGAQ-------NAQDLLPSGSVYSLPANADIEISFPATAAAPGAphpFHLHGHAFAVVRS------- 429
Cdd:pfam07731   1 DTPPKLPTLLQITSGNFrrndwaiNGLLFPPNTNVITLPYGTVVEWVLQNTTTGVHP---FHLHGHSFQVLGRgggpwpe 77

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 346214843  430 AGSTVYNYDNPIFRDVVSTGtpaAGDNVTIRFRTDNPGPWFLHCHIDFHLEAGFAVVMAEDIPD 493
Cdd:pfam07731  78 EDPKTYNLVDPVRRDTVQVP---PGGWVAIRFRADNPGVWLFHCHILWHLDQGMMGQFVVRPGD 138
CuRO_1_AAO cd13845
The first cupredoxin domain of plant Ascorbate oxidase; Ascorbate oxidase catalyzes the ...
 37-150 1.00e-29

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: 112.92  E-value: 1.00e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346214843  37 SPDGFARQAVVVNNVTPGPLVAGNKGDrfqlNVIDNLTNHTMLKSTSIHWHGFFQKGTNWADGPAFVNQCPISSGHSFLY 116
Cdd:cd13845   13 APDCVEKLVIGINGQFPGPTIRATAGD----TIVVELENKLPTEGVAIHWHGIRQRGTPWADGTASVSQCPINPGETFTY 88

                         90       100       110
                 ....*....|....*....|....*....|....
gi 346214843 117 DFQVpDQAGTFWYHSHLSTQYCDGLRGPFVVyDP 150
Cdd:cd13845   89 QFVV-DRPGTYFYHGHYGMQRSAGLYGSLIV-DP 120
CuRO_2_MaLCC_like cd13880
The second cupredoxin domain of the fungal laccases similar to Ma-LCC from Melanocarpus ...
 166-307 7.85e-28

The second cupredoxin domain of the fungal laccases similar to Ma-LCC from Melanocarpus albomyces; The subfamily of fungal laccases includes Ma-LCC and similar proteins. Ma-LCC is a multicopper oxidase (MCO) from Melanocarpus albomyces. Its crystal structure contains all four coppers at the mono- and trinuclear copper centers. Laccase is a blue multi-copper enzyme that catalyzes the oxidation of a variety aromatic - notably phenolic and inorganic substances coupled to the reduction of molecular oxygen to water. It has been implicated in a wide spectrum of biological activities and, in particular, plays a key role in morphogenesis, development and lignin metabolism in fungi and plants. Laccase is composed of three cupredoxin domains that include one mononuclear and one trinuclear copper center. The copper ions are bound in several sites: Type 1, Type 2, and/or Type 3. The ensemble of types 2 and 3 copper is called a trinuclear cluster. MCOs oxidize their substrate by accepting electrons at a mononuclear copper center and transferring them to the active site trinuclear copper center. The cupredoxin domain 2 of 3-domain MCOs has lost the ability to bind copper.


Pssm-ID: 259947 [Multi-domain]  Cd Length: 167  Bit Score: 109.26  E-value: 7.85e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346214843 166 VITLADWYH--------TAAKLGPAFPlgADATLINGLGRSP-STTAADLAVINVTKGKRYRFRLVSLSCDPNHTFSIDG 236
Cdd:cd13880    3 PVLLTDWYHrsafelfsEELPTGGPPP--MDNILINGKGKFPcSTGAGSYFETTFTPGKKYRLRLINTGVDTTFRFSIDG 80

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 346214843 237 HDLTIIEVDSINSQHLVVDSIQIFAAQRYSFVLNADQD-VGNYWIRANPSFGNVGFAGGINS--AILRYDGADP 307
Cdd:cd13880   81 HNLTVIAADFVPIVPYTTDSLNIGIGQRYDVIVEANQDpVGNYWIRAEPATGCSGTNNNPDNrtGILRYDGASP 154
CuRO_1_LCC_plant cd13849
The first cupredoxin domain of plant laccases; Laccase is a blue multicopper oxidase (MCO) ...
 28-149 8.59e-28

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: 107.35  E-value: 8.59e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346214843  28 DLTISNAEVSPDGFARQAVVVNNVTPGPLVAGNKGDRFQLNVIDNLtnhtmLKSTSIHWHGFFQKGTNWADGPAFVNQCP 107
Cdd:cd13849    2 TFVVQEKNVTRLCSTKSILTVNGQFPGPTIRVHEGDTVVVNVTNRS-----PYNITIHWHGIRQLRSGWADGPAYITQCP 76

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*.
gi 346214843 108 ISSGHSFLYDFQVPDQAGTFWYHSHLS----TQYcdglrGPFVVYD 149
Cdd:cd13849   77 IQPGQSYTYRFTVTGQEGTLWWHAHISwlraTVY-----GAFIIRP 117
CuRO_2_MCO_like_1 cd13886
The second cupredoxin domain of uncharacterized multicopper oxidase; Multicopper Oxidases ...
 166-282 1.22e-27

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: 108.51  E-value: 1.22e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346214843 166 VITLADWYHTAAKLGPAFPLGA---------DATLINGLGR----------SPSTTAADLAVINVTKGKRYRFRLVSLSC 226
Cdd:cd13886    2 VVMVNDYYHDPSSVLLARYLAPgnegdepvpDNGLINGIGQfdcasatykiYCCASNGTYYNFTLEPNKTYRLRLINAGS 81

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 346214843 227 DPNHTFSIDGHDLTIIEVDSINSQHLVVDSIQIFAAQRYSFVLNADQ-DVGNYWIRA 282
Cdd:cd13886   82 FADFTFSVDGHPLTVIEADGTLVEPVEVHSITISVAQRYSVILTTNQpTGGNFWMRA 138
PLN02354 PLN02354
copper ion binding / oxidoreductase
 36-305 1.56e-27

copper ion binding / oxidoreductase


Pssm-ID: 177987 [Multi-domain]  Cd Length: 552  Bit Score: 116.04  E-value: 1.56e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346214843  36 VSPDGFARQAVVVNNVTPGPLVAGNKGDRFQLNVIDNLtNHTMLkstsIHWHGFFQKGTNWADGPAFVNqCPISSGHSFL 115
Cdd:PLN02354  39 ASPLGVPQQVILINGQFPGPNINSTSNNNIVINVFNNL-DEPFL----LTWSGIQQRKNSWQDGVPGTN-CPIPPGTNFT 112

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346214843 116 YDFQVPDQAGTFWYHSHLSTQYCDGLRGPFVVydpndpHASL-----YDVDNDDTVITLADWY---HTAAK--LGPAFPL 185
Cdd:PLN02354 113 YHFQPKDQIGSYFYYPSTGMHRAAGGFGGLRV------NSRLlipvpYADPEDDYTVLIGDWYtksHTALKkfLDSGRTL 186

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346214843 186 G-ADATLINGlgRSPSTTAADLAVINVTKGKRYRFRLVSLSCDPNHTFSIDGHDLTIIEVDSINSQHLVVDSIQIFAAQR 264
Cdd:PLN02354 187 GrPDGVLING--KSGKGDGKDEPLFTMKPGKTYRYRICNVGLKSSLNFRIQGHKMKLVEMEGSHVLQNDYDSLDVHVGQC 264

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|.
gi 346214843 265 YSFVLNADQDVGNYWIRANPSFGNVGFAGginSAILRYDGA 305
Cdd:PLN02354 265 FSVLVTANQAPKDYYMVASTRFLKKVLTT---TGIIRYEGG 302
PLN02168 PLN02168
copper ion binding / pectinesterase
 28-306 3.72e-27

copper ion binding / pectinesterase


Pssm-ID: 215113 [Multi-domain]  Cd Length: 545  Bit Score: 115.07  E-value: 3.72e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346214843  28 DLTISNAEVSPDGFARQAVVVNNVTPGPLVAGNKGDRFQLNVIDNLTNHTMLKstsihWHGFFQKGTNWADGPAFVNqCP 107
Cdd:PLN02168  30 QWVVSYSQRFILGGNKQVIVINDMFPGPLLNATANDVINVNIFNNLTEPFLMT-----WNGLQLRKNSWQDGVRGTN-CP 103

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346214843 108 ISSGHSFLYDFQVPDQAGTFWYHSHLSTQYCDGLRGPFVVYDPN-------DPHASlYDvdnddtvITLADWY---HTAA 177
Cdd:PLN02168 104 ILPGTNWTYRFQVKDQIGSYFYFPSLLLQKAAGGYGAIRIYNPElvpvpfpKPDEE-YD-------ILIGDWFyadHTVM 175

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346214843 178 KL----GPAFPlGADATLINglGRSPSTTaadlaVINVTKGKRYRFRLVSLSCDPNHTFSIDGHDLTIIEVDSINSQHLV 253
Cdd:PLN02168 176 RAsldnGHSLP-NPDGILFN--GRGPEET-----FFAFEPGKTYRLRISNVGLKTCLNFRIQDHDMLLVETEGTYVQKRV 247

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 346214843 254 VDSIQIFAAQRYSFVLNADQD-VG---NYWIRANPSFGNvGFAGGInsAILRYDGAD 306
Cdd:PLN02168 248 YSSLDIHVGQSYSVLVTAKTDpVGiyrSYYIVATARFTD-AYLGGV--ALIRYPNSP 301
PLN02991 PLN02991
oxidoreductase
 31-475 4.05e-26

oxidoreductase


Pssm-ID: 215536 [Multi-domain]  Cd Length: 543  Bit Score: 111.65  E-value: 4.05e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346214843  31 ISNAEVSPDGFARQAVVVNNVTPGPLVAGNKGDRFQLNVIDNLTNHTMLKSTSI-HWHGFFQKGTnwadgpaFVNQCPIS 109
Cdd:PLN02991  35 VTYGNISPLGVAQQGILINGKFPGPDIISVTNDNLIINVFNHLDEPFLISWSGIrNWRNSYQDGV-------YGTTCPIP 107

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346214843 110 SGHSFLYDFQVPDQAGTFWYHSHLSTQYCDGLRGPFVVYD-PNDPHAslYDVDNDDTVITLADWYHT-----AAKL--GP 181
Cdd:PLN02991 108 PGKNYTYALQVKDQIGSFYYFPSLGFHKAAGGFGAIRISSrPLIPVP--FPAPADDYTVLIGDWYKTnhkdlRAQLdnGG 185

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346214843 182 AFPLgADATLINGLGRSpsttaadlAVINVTKGKRYRFRLVSLSCDPNHTFSIDGHDLTIIEVDSINSQHLVVDSIQIFA 261
Cdd:PLN02991 186 KLPL-PDGILINGRGSG--------ATLNIEPGKTYRLRISNVGLQNSLNFRIQNHTMKLVEVEGTHTIQTPFSSLDVHV 256

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346214843 262 AQRYSFVLNADQDVGNYWIRANPSFGNVGFaggINSAILRY-DGADPVEPTTTQTTPTKPLNEVDLHPLDTMAPGS---P 337
Cdd:PLN02991 257 GQSYSVLITADQPAKDYYIVVSSRFTSKIL---ITTGVLHYsNSAGPVSGPIPDGPIQLSWSFDQARAIKTNLTASgprP 333

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346214843 338 VAGG--------VDKAINMAFNFNGTN----FFINGASFVPPTVPVLLQ---IISGAQNAQD---------LLPSGSVYS 393
Cdd:PLN02991 334 NPQGsyhygkinITRTIRLANSAGNIEgkqrYAVNSASFYPADTPLKLAdyfKIAGVYNPGSipdqptngaIFPVTSVMQ 413

                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346214843 394 LPANADIEISFpatAAAPGAPHPFHLHGHAFAVV-------RSAGSTVYNYDNPIFRDVVSTgTPAAGDNVTIRFrtDNP 466
Cdd:PLN02991 414 TDYKAFVEIVF---ENWEDIVQTWHLDGYSFYVVgmelgkwSAASRKVYNLNDAVSRCTVQV-YPRSWTAIYVSL--DNV 487


                 ....*....
gi 346214843 467 GPWFLHCHI 475
Cdd:PLN02991 488 GMWNLRSEL 496
CuRO_3_Fet3p cd13899
The third Cupredoxin domain of multicopper oxidase Fet3p; Fet3p catalyzes the ferroxidase ...
 346-490 1.16e-25

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: 102.72  E-value: 1.16e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346214843 346 INMAFNFNGTN-FFINGASFVPPTVPVLLQIISGAQNAQD---LLPSGSVYSLPANADIEIsfpATAAAPGAPHPFHLHG 421
Cdd:cd13899    8 VDFDTFDDGVNrAAFNNITYVSPKVPTLYTALSMGDDALDpaiYGPQTNAFVLNHGEVVEL---VVNNWDAGKHPFHLHG 84

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 346214843 422 HAFAVV-RSAGSTVY--------NYDNPIFRDVVSTgtPAAGdNVTIRFRTDNPGPWFLHCHIDFHLEAGFAVVMAED 490
Cdd:cd13899   85 HKFQVVqRSPDVASDdpnppineFPENPMRRDTVMV--PPGG-SVVIRFRADNPGVWFFHCHIEWHLEAGLAATFIEA 159
PLN02835 PLN02835
oxidoreductase
 30-286 9.43e-23

oxidoreductase


Pssm-ID: 178429 [Multi-domain]  Cd Length: 539  Bit Score: 101.59  E-value: 9.43e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346214843  30 TISNAEVSPDGFARQAVVVNNVTPGPLVAGNKGDRFQLNVIDNLTNHTMLKstsihWHGFFQKGTNWADGPAFVNqCPIS 109
Cdd:PLN02835  35 TVTYGTISPLGVPQQVILINGQFPGPRLDVVTNDNIILNLINKLDQPFLLT-----WNGIKQRKNSWQDGVLGTN-CPIP 108

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346214843 110 SGHSFLYDFQVPDQAGTFWYHSHLSTQYCDGLRGPFVVYD-PNDPHAslYDVDNDDTVITLADWYHTAAKL-------GP 181
Cdd:PLN02835 109 PNSNYTYKFQTKDQIGTFTYFPSTLFHKAAGGFGAINVYErPRIPIP--FPLPDGDFTLLVGDWYKTSHKTlqqrldsGK 186

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346214843 182 AFPLgADATLINGlgRSPSTTAADlavinvtKGKRYRFRLVSLSCDPNHTFSIDGHDLTIIEVDSINSQHLVVDSIQIFA 261
Cdd:PLN02835 187 VLPF-PDGVLING--QTQSTFSGD-------QGKTYMFRISNVGLSTSLNFRIQGHTMKLVEVEGSHTIQNIYDSLDVHV 256

                        250       260
                 ....*....|....*....|....*
gi 346214843 262 AQRYSFVLNADQDVGNYWIRANPSF 286
Cdd:PLN02835 257 GQSVAVLVTLNQSPKDYYIVASTRF 281
CuRO_3_LCC_like cd04207
Cupredoxin domain 3 of laccase-like multicopper oxidases; including laccase, CueO, spore coat ...
 343-488 1.47e-22

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: 93.29  E-value: 1.47e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346214843 343 DKAINMAFNFNG-----TNFFINGASFVPptvpvllqiisgaqnaqdLLPSGSVYSLPANADIEISFPATAAAPGAPHpF 417
Cdd:cd04207    1 DRTRRLVLSQTGapdgtTRWVINGMPFKE------------------GDANTDIFSVEAGDVVEIVLINAGNHDMQHP-F 61

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 346214843 418 HLHGHAFAVVRSAG---STVYNYDNPIFRDVVSTGtpaAGDNVTIRFRTDNPGPWFLHCHIDFHLEAGFAVVMA 488
Cdd:cd04207   62 HLHGHSFWVLGSGGgpfDAPLNLTNPPWRDTVLVP---PGGWVVIRFKADNPGVWMLHCHILEHEDAGMMTVFE 132
CuRO_1_CumA_like cd13861
The first cupredoxin domain of CumA like multicopper oxidase; This multicopper oxidase (MCO) ...
 26-147 3.20e-22

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: 91.91  E-value: 3.20e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346214843  26 TADLTISNAEVSPDGFARQAVVV-NNVTPGPLVAGNKGDRFQLNvidnLTNHtMLKSTSIHWHGFfqKGTNWADGPAFVN 104
Cdd:cd13861    2 EYTLTAAPAELLDLGGPTTRTWGyNGQVPGPELRVRQGDTLRVR----LTNR-LPEPTTIHWHGL--RLPNAMDGVPGLT 74

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*
gi 346214843 105 QCPISSGHSFLYDFQVPDqAGTFWYHSHLSTQYC--DGLRGPFVV 147
Cdd:cd13861   75 QPPVPPGESFTYEFTPPD-AGTYWYHPHVGSQEQldRGLYGPLIV 118
CuRO_1_CopA cd13848
The first cupredoxin domain of CopA copper resistance protein family; CopA is a multicopper ...
 26-147 3.57e-22

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


Pssm-ID: 259917 [Multi-domain]  Cd Length: 116  Bit Score: 91.57  E-value: 3.57e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346214843  26 TADLTISNAEVSPDGFARQAVVVNNVTPGPLVAGNKGDRFQLNVidnlTNHTMlKSTSIHWHGFFQKGTnwADGPAFVNQ 105
Cdd:cd13848    2 EYDLVIAETPVNIGGKEGEAITVNGQVPGPLLRFKEGDDATIRV----HNRLD-EDTSIHWHGLLLPND--MDGVPGLSF 74

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|..
gi 346214843 106 CPISSGHSFLYDFQVpDQAGTFWYHSHLSTQYCDGLRGPFVV 147
Cdd:cd13848   75 PGIKPGETFTYRFPV-RQSGTYWYHSHSGLQEQTGLYGPIII 115
CuRO_1_MCO_like_2 cd13864
The second cupredoxin domain of uncharacterized multicopper oxidase; Multicopper Oxidases ...
 27-147 5.93e-22

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: 91.83  E-value: 5.93e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346214843  27 ADLTISNAEVSPDGFARQAVVVN--NVTPGPLVAGNKGDRFQLNVIDNLTNHTMLK-------STSIHWHG-----FFQK 92
Cdd:cd13864    2 TLLIILRISVEYNKDGKQIISINgsNDTIGPTIRVKSGDTLNLLVTNHLCNEQELSkiwqdycPTSIHFHGlvlenFGKQ 81

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 346214843  93 GTNWADGPAFVNQCPISSGHSFLYDFQVPDQA-GTFWYHSHLSTQYCDGLRGPFVV 147
Cdd:cd13864   82 LANLVDGVPGLTQYPIGVGESYWYNFTIPEDTcGTFWYHSHSSVQYGDGLRGVFIV 137
CuRO_3_tcLLC2_insect_like cd13905
The third cupredoxin domain of the insect laccases similar to laccase 2 in Tribolium castaneum; ...
 359-487 9.00e-22

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: 92.36  E-value: 9.00e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346214843 359 INGASFVPPTVPVLLQ-------IISGAQNAQDLLPSGS-----VYSLPANADIEISFPATAAAPGAPHPFHLHGHAFAV 426
Cdd:cd13905    2 INGISFVFPSSPLLSQpedlsdsSSCDFCNVPSKCCTEPcecthVIKLPLNSVVEIVLINEGPGPGLSHPFHLHGHSFYV 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346214843 427 V------------------------RSAGSTVYNYDNPIFRDVVStgTPAAGdNVTIRFRTDNPGPWFLHCHIDFHLEAG 482
Cdd:cd13905   82 LgmgfpgynsttgeilsqnwnnkllDRGGLPGRNLVNPPLKDTVV--VPNGG-YVVIRFRADNPGYWLLHCHIEFHLLEG 158


                 ....*
gi 346214843 483 FAVVM 487
Cdd:cd13905  159 MALVL 163
CuRO_D1_2dMcoN_like cd13859
The first cupredoxin domain of bacterial two domain multicopper oxidase McoN and similar ...
 49-143 2.94e-21

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: 89.07  E-value: 2.94e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346214843  49 NNVTPGPLVAGNKGDRFQLNVidnlTNHTMLKSTsIHWHGFFQKGTNWADGPAFVNQCPISSGHSFLYDFQVpDQAGTFW 128
Cdd:cd13859   26 NGQVPGPLIHVKEGDDLVVHV----TNNTTLPHT-IHWHGVLQMGSWKMDGVPGVTQPAIEPGESFTYKFKA-ERPGTLW 99

                         90
                 ....*....|....*
gi 346214843 129 YHSHLSTQYCDGLRG 143
Cdd:cd13859  100 YHCHVNVNEHVGMRG 114
PLN00044 PLN00044
multi-copper oxidase-related protein; Provisional
 43-305 1.00e-20

multi-copper oxidase-related protein; Provisional


Pssm-ID: 165622 [Multi-domain]  Cd Length: 596  Bit Score: 95.50  E-value: 1.00e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346214843  43 RQAVVVNNVTPGPLVAGNKGDRFQLNVIDNLTNHTMLKstsihWHGFFQKGTNWADGPAFVNqCPISSGHSFLYDFQVPD 122
Cdd:PLN00044  48 QEAIGINGQFPGPALNVTTNWNLVVNVRNALDEPLLLT-----WHGVQQRKSAWQDGVGGTN-CAIPAGWNWTYQFQVKD 121

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346214843 123 QAGTFWYHSHLSTQYCDGLRGPFVVYDPNDPHASLYDVDNDDTVITLADWY---HTAAK--LGPAFPLGA-DATLINGLG 196
Cdd:PLN00044 122 QVGSFFYAPSTALHRAAGGYGAITINNRDVIPIPFGFPDGGDITLFIADWYardHRALRraLDAGDLLGApDGVLINAFG 201

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346214843 197 -----RSPSTTAADLAVINVTKGKRYRFRLVSLSCDPNHTFSIDGHDLTIIEVDSINSQHLVVDSIQIFAAQRYSFVLNA 271
Cdd:PLN00044 202 pyqynDSLVPPGITYERINVDPGKTYRFRVHNVGVATSLNFRIQGHNLLLVEAEGSYTSQQNYTNLDIHVGQSYSFLLTM 281

                        250       260       270
                 ....*....|....*....|....*....|....*.
gi 346214843 272 DQDVG-NYWIRANPSFGNVGFAGGINS-AILRYDGA 305
Cdd:PLN00044 282 DQNAStDYYVVASARFVDAAVVDKLTGvAILHYSNS 317
CuRO_2_Diphenol_Ox cd13883
The second cupredoxin domain of fungal laccase, diphenol oxidase; Diphenol oxidase belongs to ...
 166-303 2.75e-20

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: 87.78  E-value: 2.75e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346214843 166 VITLADWYHTAAKL------------GPAFPLGADATLINGLGRSPSTTAAD--------LAVINVTKGKRYRFRLVSLS 225
Cdd:cd13883    2 VLFISDWYHDQSEVivagllspqgykGSPAAPSPDSALINGIGQFNCSAADPgtcctqtsPPEIQVEAGKRTRFRLINAG 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346214843 226 CDPNHTFSIDGHDLTIIEVDSIN-SQHLVVDSIQIFAAQRYSFVLNADQD-VGN-YWIRANPSFGNVGFAG--GINSAIL 300
Cdd:cd13883   82 SHAMFRFSVDNHTLNVVEADDTPvYGPTVVHRIPIHNGQRYSVIIDTTSGkAGDsFWLRARMATDCFAWDLqqQTGKAIL 161


                 ...
gi 346214843 301 RYD 303
Cdd:cd13883  162 RYV 164
CuRO_2_Fet3p_like cd13877
The second Cupredoxin domain of multicopper oxidase Fet3P; Fet3p catalyzes the ferroxidase ...
 163-283 7.36e-20

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: 86.07  E-value: 7.36e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346214843 163 DDTVITLADWYH------TAAKLGPAFPLGA----DATLINGlGRSPSttaadlavINVTKGKRYRFRLVSLSCDPNHTF 232
Cdd:cd13877    1 EEVTLTLSDWYHdqspdlLRDFLSPYNPTGAepipDSSLFND-TQNAT--------INFEPGKTYLLRIINMGAFASQYF 71

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|..
gi 346214843 233 SIDGHDLTIIEVDSINSQHLVVDSIQIFAAQRYSFVLNA-DQDVGNYWIRAN 283
Cdd:cd13877   72 HIEGHDMTIIEVDGVYVKPYPVDTLYIAVGQRYSVLVKAkNDTDRNYAIING 123
CuRO_1_2dMco_1 cd13860
The first cupredoxin domain of bacteria two domain multicopper oxidase; This subfamily ...
 49-147 5.30e-19

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


Pssm-ID: 259929 [Multi-domain]  Cd Length: 119  Bit Score: 82.63  E-value: 5.30e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346214843  49 NNVTPGPLVAGNKGDRFQLNVIDNLTNHTmlkstSIHWHGFFQKgtNWADGPAFVNQCPISSGHSFLYDFQVpDQAGTFW 128
Cdd:cd13860   26 NGSVPGPTIEVTEGDRVRILVTNELPEPT-----TVHWHGLPVP--NGMDGVPGITQPPIQPGETFTYEFTA-KQAGTYM 97

                         90       100
                 ....*....|....*....|.
gi 346214843 129 YHSHLSTQYCD--GLRGPFVV 147
Cdd:cd13860   98 YHSHVDEAKQEdmGLYGAFIV 118
CuRO_1_AAO_like_2 cd13847
The first cupredoxin domain of Ascorbate oxidase homologs; This family includes fungal ...
 25-149 2.57e-18

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: 80.65  E-value: 2.57e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346214843  25 PTADLTISNAEVSPdgfaRQAVVVNNVTPGPLVAGNKGDRFQLNVIDNLTNhtmlKSTSIHWHGFFQKGTNWADGPAFVN 104
Cdd:cd13847    1 PDATLRVSCDPFGP----RPSTLINGSFPGPELRVQEGQHLWVRVYNDLEA----GNTTMHFHGLSQYMSPFSDGTPLAS 72

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*.
gi 346214843 105 QCPISSGHSFLYDFQV-PDQAGTFWYHSHLSTQYCDGlRGPFVVYD 149
Cdd:cd13847   73 QWPIPPGKFFDYEFPLeAGDAGTYYYHSHVGFQSVTA-YGALIVED 117
CuRO_1_LCC_like_3 cd13865
The second cupredoxin domain of uncharacterized multicopper oxidase; Multicopper Oxidases ...
 60-149 1.54e-17

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: 78.51  E-value: 1.54e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346214843  60 NKGDRFQLNVIDNLTnhtmlKSTSIHWHGffQKGTNWADGPAFVNQCPISSGHSFLYDFQVpDQAGTFWYHSHLSTQYCD 139
Cdd:cd13865   34 TEGDRFDVELENRLD-----EPTTIHWHG--LIPPNLQDGVPDVTQPPIPPGQSQRYDFPL-VQPGTFWMHSHYGLQEQK 105

                         90
                 ....*....|
gi 346214843 140 GLRGPFVVYD 149
Cdd:cd13865  106 LLAAPLIIRS 115
CuRO_3_MCO_like_4 cd13910
The third cupredoxin domain of uncharacterized multicopper oxidase; Multicopper Oxidases (MCOs) ...
 358-489 8.30e-17

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: 78.11  E-value: 8.30e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346214843 358 FINGASFVP-PTVPVLLQII--------SGAQNAQDLLPSGSVYSLPANA---DIEISfpataAAPGAPHPFHLHGHAFA 425
Cdd:cd13910   19 FFNGTSWRPlPGPATLLLALdadnaeevAAGNGLSTFDGNQLVITVDDIDkvvDLVIN-----NLDDGDHPFHLHGHKFW 93

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 346214843 426 VVRS------------AGSTVYNYDNPIFRDVVSTgtPAAGdNVTIRFRTDNPGPWFLHCHIDFHLEAGFAVVMAE 489
Cdd:cd13910   94 VLGSgdgryggggytaPDGTSLNTTNPLRRDTVSV--PGFG-WAVLRFVADNPGLWAFHCHILWHMAAGMLMQFAV 166
CuRO_3_LCC_plant cd13897
The third cupredoxin domain of the plant laccases; Laccase is a blue multicopper oxidase (MCO) ...
 390-486 1.88e-16

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: 76.14  E-value: 1.88e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346214843 390 SVYSLPANADIEISFPATAAAPGAPHPFHLHGHAFAVV--------RSAGSTVYNYDNPIFRDVVstGTPAAGdNVTIRF 461
Cdd:cd13897   32 KVKVLEYGSTVEIVLQGTSLLAAENHPMHLHGFDFYVVgrgfgnfdPSTDPATFNLVDPPLRNTV--GVPRGG-WAAIRF 108

                         90       100
                 ....*....|....*....|....*
gi 346214843 462 RTDNPGPWFLHCHIDFHLEAGFAVV 486
Cdd:cd13897  109 VADNPGVWFMHCHFERHTSWGMATV 133
CuRO_2_AAO_like_2 cd13873
The second cupredoxin domain of plant Ascorbate oxidase homologs; This family includes plant ...
 163-302 3.31e-16

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: 76.17  E-value: 3.31e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346214843 163 DDTVITLADWYH-------TAAKLGP-AFPLGADATLINGLG--------RSPSTTAADLAVINVTKGKRYRFRLVSLSC 226
Cdd:cd13873    1 EERILLFSDYFPktdstieTGLTATPfVWPGEPNALLVNGKSggtcnksaTEGCTTSCHPPVIDVEPGKTYRFRFIGATA 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346214843 227 DPNHTFSIDGHD-LTIIEVDSINSQHLVVDSIQIFAAQRYSFVLN-------ADQDVGNYWIRA-------NPSFgnvgf 291
Cdd:cd13873   81 LSFVSLGIEGHDnLTIIEADGSYTKPAETDHLQLGSGQRYSFLLKtksleelAALNKTTFWIQIetrwrptNDTG----- 155

                        170
                 ....*....|.
gi 346214843 292 agginSAILRY 302
Cdd:cd13873  156 -----YAVLRY 161
CuRO_3_Diphenol_Ox cd13904
The third cupredoxin domain of fungal laccase, diphenol oxidase; Diphenol oxidase belongs to ...
 357-486 3.52e-16

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: 75.79  E-value: 3.52e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346214843 357 FFINGASFVP-PTVPVLLQIISGAQ---NAQDLlpSGSVYSLPANADIEIsfpaTAAAPGAPHPFHLHGHAFAVV----- 427
Cdd:cd13904   22 FFVNNVTWTNyIYQPLLHQVASGGGgtlNSSEV--ASVTFPTDGWYDIVI----NNLDPAIDHPYHLHGVDFHIVargsg 95

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 346214843 428 ----RSAGSTVYNYDNPIFRDVVSTGtpaAGDNVTIRFRTDNPGPWFLHCHIDFHLEAGFAVV 486
Cdd:cd13904   96 tltlEQLANVQYNTTNPLRRDTIVIP---GGSWAVLRIPADNPGVWALHCHIGWHLAAGFAGV 155
CuRO_3_MaLCC_like cd13901
The third cupredoxin domain of the fungal laccases similar to Ma-LCC from Melanocarpus ...
 342-485 4.16e-16

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: 75.72  E-value: 4.16e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346214843 342 VDKAINMAFNFNGTNFF---INGASF-VPPTVPVLLQIISGaqNAQDLLPSGSVYSLPANAD-----IEisfpataAAPG 412
Cdd:cd13901    8 PTQTLTIDLGPNATGVFlwtLNGSSFrVDWNDPTLLLVADG--NTSTFPPEWNVIELPKANKwvyivIQ-------NNSP 78

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 346214843 413 APHPFHLHGHAFAVVRSA------GSTVYNYDNPIFRDVVSTgtPAAGDNVtIRFRTDNPGPWFLHCHIDFHLEAGFAV 485
Cdd:cd13901   79 LPHPIHLHGHDFYILAQGtgtfddDGTILNLNNPPRRDVAML--PAGGYLV-IAFKTDNPGAWLMHCHIAWHASGGLAL 154
CuRO_3_AAO cd13893
The third cupredoxin domain of plant Ascorbate oxidase; Ascorbate oxidase catalyzes the ...
 359-495 5.60e-15

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: 72.45  E-value: 5.60e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346214843 359 INGASFVPPTVPVLLQIisgaqnaqdllpsgSVYSLPANADIEISFPATAAAPGAPHP---FHLHGHAFAVV-------- 427
Cdd:cd13893   22 INNVSYVPPPTPYLAAL--------------PVYPFKGGDVVDVILQNANTNTRNASEqhpWHLHGHDFWVLgyglggfd 87

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 346214843 428 RSAGSTVYNYDNPIFRDVVSTgtpAAGDNVTIRFRTDNPGPWFLHCHIDFHLEAGFAVVMAEDIPDVA 495
Cdd:cd13893   88 PAADPSSLNLVNPPMRNTVTI---FPYGWTALRFKADNPGVWAFHCHIEWHFHMGMGVVFAEGVERVG 152
CuRO_2_AAO cd13871
The second cupredoxin domain of plant Ascorbate oxidase; Ascorbate oxidase catalyzes the ...
 167-283 1.43e-14

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


Pssm-ID: 259939 [Multi-domain]  Cd Length: 166  Bit Score: 71.42  E-value: 1.43e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346214843 167 ITLADWYH-------TAAKLGPAFPLGADAT-LINGLGR--------SPST--------TAADLA--VINVTKGKRYRFR 220
Cdd:cd13871    6 ILLSDWWHksiyeqeTGLSSKPFRWVGEPQSlLIEGRGRyncslapaYPSSlpspvcnkSNPQCApfILHVSPGKTYRLR 85

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 346214843 221 LVSLSCDPNHTFSIDGHDLTIIEVDSINSQHLVVDSIQIFAAQRYSFVLNADQDVG-NYWIRAN 283
Cdd:cd13871   86 IASVTALSSLNFIIEGHNLTVVEADGNYVQPFEVSNLDIYSGETYSVLVTADQDPSrNYWVSVN 149
CuRO_1_AAO_like_1 cd13846
The first cupredoxin domain of plant Ascorbate oxidase homologs; This subfamily is composed of ...
 28-147 2.06e-14

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: 69.74  E-value: 2.06e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346214843  28 DLTISNAEVSPDGFARQAVVVNNVTPGPLVAGNKGDRFQLNVIDNLtNHTMLkstsIHWHGFFQKGTNWADGPAFVNqCP 107
Cdd:cd13846    4 DWNVSYITASPLGVPQQVIAINGQFPGPTINVTTNDNVVVNVFNSL-DEPLL----LTWNGIQQRRNSWQDGVLGTN-CP 77

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|
gi 346214843 108 ISSGHSFLYDFQVPDQAGTFWYHSHLSTQYCDGLRGPFVV 147
Cdd:cd13846   78 IPPGWNWTYKFQVKDQIGSFFYFPSLHFQRAAGGFGGIRV 117
CuRO_1_McoP_like cd13852
The first cupredoxin domain of multicopper oxidase McoP and similar proteins; This family ...
 54-150 2.47e-14

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: 69.24  E-value: 2.47e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346214843  54 GPLVAGNKGDRFQLNVIDNLTNHTMlkstsIHWHGFFqkgTNWA-DG-PAFVnqcpISSGHSFLYDFQVPDQAGTFWYHS 131
Cdd:cd13852   24 GPILRLRKGQKVRITFKNNLPEPTI-----IHWHGLH---VPAAmDGhPRYA----IDPGETYVYEFEVLNRAGTYWYHP 91

                         90       100
                 ....*....|....*....|...
gi 346214843 132 H----LSTQYCDGLRGPFVVYDP 150
Cdd:cd13852   92 HphglTAKQVYRGLAGLFLVTDE 114
CuRO_2_LCC_plant cd13875
The second cupredoxin domain of the plant laccases; Laccase is a blue multi-copper enzyme that ...
 166-302 7.87e-14

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: 68.78  E-value: 7.87e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346214843 166 VITLADWYHT-------AAKLGPAFPLGADATLINGL-GRSPSTTAADLAVINVTKGKRYRFRLVSLSCDPNHTFSIDGH 237
Cdd:cd13875    2 PIILGEWWNRdvndvedQALLTGGGPNISDAYTINGQpGDLYNCSSKDTFVLTVEPGKTYLLRIINAALNEELFFKIANH 81

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 346214843 238 DLTIIEVDSINSQHLVVDSIQIFAAQRYSFVLNADQDVGNYWIRANP--SFGNVGFAGGINSAILRY 302
Cdd:cd13875   82 TLTVVAVDASYTKPFTTDYILIAPGQTTDVLLTADQPPGRYYMAARPyqSAPPVPFDNTTATAILEY 148
CuRO_3_CopA cd13896
The third cupredoxin domain of CopA copper resistance protein family; CopA is a multicopper ...
 418-482 1.15e-13

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


Pssm-ID: 259963 [Multi-domain]  Cd Length: 115  Bit Score: 67.28  E-value: 1.15e-13
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 346214843 418 HLHGHAFAVVRSAGSTvynydnPIFRDVVSTgtpAAGDNVTIRFRTDNPGPWFLHCHIDFHLEAG 482
Cdd:cd13896   53 HLHGHFFQVENGNGEY------GPRKDTVLV---PPGETVSVDFDADNPGRWAFHCHNLYHMEAG 108
CuRO_2_AAO_like_1 cd13872
The second cupredoxin domain of plant pollen multicopper oxidase homologous to ascorbate ...
 163-302 1.55e-13

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


Pssm-ID: 259940 [Multi-domain]  Cd Length: 141  Bit Score: 67.81  E-value: 1.55e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346214843 163 DDTVITLADWY---HTAAK--LGPAFPLGA-DATLINGLGrsPSTTAADLAVINVTKGKRYRFRLVSLSCDPNHTFSIDG 236
Cdd:cd13872    1 DEYTVLIGDWYktdHKTLRqsLDKGRTLGRpDGILINGKG--PYGYGANETSFTVEPGKTYRLRISNVGLRTSLNFRIQG 78

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 346214843 237 HDLTIIEVDSINSQHLVVDSIQIFAAQRYSFVLNADQDVGNYWIRANPSFGNVGFAGginSAILRY 302
Cdd:cd13872   79 HKMLLVETEGSYTAQNTYDSLDVHVGQSYSVLVTADQSPKDYYIVASSRFLSPELTG---VAILHY 141
CuRO_1_McoC_like cd13855
The first cupredoxin domain of a multicopper oxidase McoC and similar proteins; This family ...
 49-147 5.80e-13

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


Pssm-ID: 259924 [Multi-domain]  Cd Length: 121  Bit Score: 65.57  E-value: 5.80e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346214843  49 NNVTPGPLVAGNKGDRFQLNVIDNLTnhtmlKSTSIHWHGFfqKGTNWADGPAfvnQCPISSGHSFLYDFQVP-DQAGTF 127
Cdd:cd13855   27 NGSVPGPLIEVFEGDTVEITFRNRLP-----EPTTVHWHGL--PVPPDQDGNP---HDPVAPGNDRVYRFTLPqDSAGTY 96

                         90       100
                 ....*....|....*....|....
gi 346214843 128 WYHSH----LSTQYCDGLRGPFVV 147
Cdd:cd13855   97 WYHPHphghTAEQVYRGLAGAFVV 120
CuRO_2_Abr2_like cd13876
The second cupredoxin domain of a group of fungal Laccases similar to Abr2 from Aspergillus ...
 166-302 1.41e-12

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: 64.92  E-value: 1.41e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346214843 166 VITLADWYH----------TAAKLGPAFplgADATLINGLGRspsttaADLAVINVTKGKRYR-FRLVSLSCDPNHTFSI 234
Cdd:cd13876    2 PIILSDWRHltseeywkimRASGIEPFC---YDSILINGKGR------VYCLIVIVDPGERWVsLNFINAGGFHTLAFSI 72

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 346214843 235 DGHDLTIIEVDS--INSQhlVVDSIQIFAAQRYSFVLNADQDVGNYWIRANpsfgNVGFAGGINS-AILRY 302
Cdd:cd13876   73 DEHPMWVYAVDGgyIEPQ--LVDAISITNGERYSVLVKLDKPPGDYTIRVA----STGAPQVISGyAILRY 137
CuRO_3_CumA_like cd13906
The third cupredoxin domain of CumA like multicopper oxidase; This multicopper oxidase (MCO) ...
 418-482 6.80e-12

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


Pssm-ID: 259973 [Multi-domain]  Cd Length: 138  Bit Score: 63.17  E-value: 6.80e-12
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 346214843 418 HLHGHAFAVVRSAGSTVynyDNPIFRDVVSTGtpaAGDNVTIRFRTDNPGPWFLHCHIDFHLEAG 482
Cdd:cd13906   72 HLHGHFFRVLSRNGRPV---PEPFWRDTVLLG---PKETVDIAFVADNPGDWMFHCHILEHQETG 130
CuRO_3_Abr2_like cd13898
The third cupredoxin domain of a group of fungal Laccases similar to Abr2 from Aspergillus ...
 417-489 2.71e-11

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: 61.89  E-value: 2.71e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346214843 417 FHLHG-HAFAVVRSAG----STV----------YNYDNPIFRD-VVSTGTPAAGDNVTIRFRTDNPGPWFLHCHIDFHLE 480
Cdd:cd13898   75 IHKHGnKAFVIGTGTGpfnwSSVaeaaeaapenFNLVNPPLRDtFTTPPSTEGPSWLVIRYHVVNPGAWLLHCHIQSHLA 154


                 ....*....
gi 346214843 481 AGFAVVMAE 489
Cdd:cd13898  155 GGMAVVLLD 163
CuRO_1_CueO_FtsP cd04232
The first Cupredoxin domain of the multicopper oxidase CueO, the cell division protein FtsP, ...
 54-149 2.72e-10

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: 57.97  E-value: 2.72e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346214843  54 GPLVAGNKGDRFQLNVIDNLTnhtmlKSTSIHWHGFFQKGTnwADGPAfvnQCPISSGHSFLYDFQVPDQAGTFWYHSHL 133
Cdd:cd04232   31 GPTIRVKKGDTVRINVTNNLD-----EETTVHWHGLHVPGE--MDGGP---HQPIAPGQTWSPTFTIDQPAATLWYHPHT 100

                         90       100
                 ....*....|....*....|
gi 346214843 134 --ST--QYCDGLRGPFVVYD 149
Cdd:cd04232  101 hgKTaeQVYRGLAGLFIIED 120
CuRO_1_Tth-MCO_like cd13853
The first cupredoxin domain of the bacterial laccases similar to Tth-MCO from Thermus ...
 26-147 5.14e-10

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


Pssm-ID: 259922 [Multi-domain]  Cd Length: 139  Bit Score: 57.65  E-value: 5.14e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346214843  26 TADLTISNAEV--SPDGFARQAVvvNNVTPGPLVAGNKGDRFQLNVIDNLTNHTMLK------------STSIHWHGFFQ 91
Cdd:cd13853    3 EVTLTVEYGRVtlAGLPVTLRTY--NGSIPGPTLRVRPGDTLRITLKNDLPPEGAANeapapntphcpnTTNLHFHGLHV 80

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 346214843  92 KGTNWADGPaFVNqcpISSGHSFLYDFQVPDQ--AGTFWYHSHL----STQYCDGLRGPFVV 147
Cdd:cd13853   81 SPTGNSDNV-FLT---IAPGESFTYEYDIPADhpPGTYWYHPHLhgstALQVAGGMAGALVV 138
CuRO_3_MCO_like_2 cd13908
The third cupredoxin domain of uncharacterized multicopper oxidase; Multicopper Oxidases (MCOs) ...
 418-483 1.42e-09

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: 55.92  E-value: 1.42e-09
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 346214843 418 HLHGHAFAVVRSAGSTVYNydnpIFRDVVSTGtpaAGDNVTIRFRTDNPGPWFLHCHIDFHLEAGF 483
Cdd:cd13908   58 HLHRHTFEVTRIDGKPTSG----LRKDVVMLG---GYQRVEVDFVADNPGLTLFHCHQQLHMDYGF 116
CuRO_3_MCO_like_3 cd13909
The third cupredoxin domain of uncharacterized multicopper oxidase; Multicopper Oxidases (MCOs) ...
 418-482 2.48e-09

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: 55.60  E-value: 2.48e-09
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 346214843 418 HLHGHAFAVVRSagstvyNYDNPIFRDVVSTgtpAAGDNVTIRFRTDNPGPWFLHCHIDFHLEAG 482
Cdd:cd13909   74 HLHGHHFRAILP------NGALGPWRDTLLM---DRGETREIAFVADNPGDWLLHCHMLEHAAAG 129
CuRO_3_McoC_like cd13902
The third cupredoxin domain of a multicopper oxidase McoC and similar proteins; This family ...
 417-482 5.54e-09

The third cupredoxin domain of a multicopper oxidase McoC and similar proteins; This family includes bacteria multicopper oxidases (MCOs) represented by McoC from pathogenic bacterium Campylobacter jejuni. McoC is a periplasmic multicopper oxidase, which has been characterized to be associated with copper homeostasis. McoC may also function to protect against oxidative stress as it may convert metallic ions into their less toxic form. MCOs are multi-domain enzymes that are able to couple oxidation of substrates with reduction of dioxygen to water. They are capable of oxidizing a vast range of substrates, varying from aromatic compunds to inorganic compounds such as metals. Most MCOs have three cupredoxin domain repeats that include one mononuclear and one trinuclear copper center. The copper ions are bound in several sites: Type 1, Type 2, and/or Type 3. The ensemble of types 2 and 3 copper is called a trinuclear cluster. MCOs oxidize their substrate by accepting electrons at a mononuclear copper center and transferring them to the active site trinuclear copper center. The cupredoxin domain 3 of 3-domain MCOs contains the Type 1 (T1) copper binding site and part the trinuclear copper binding site, which is located at the interface of domains 1 and 3.


Pssm-ID: 259969 [Multi-domain]  Cd Length: 125  Bit Score: 54.33  E-value: 5.54e-09
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 346214843 417 FHLHGHAFAVVRSAGSTVyNYDNPIFRDVVSTgtpAAGDNVTIRFRTDNPGPWFLHCHIDFHLEAG 482
Cdd:cd13902   57 FHLHGTQFQVLEIDGNPQ-KPEYRAWKDTVNL---PPGEAVRIATRQDDPGMWMYHCHILEHEDAG 118
CuRO_D2_2dMcoN_like cd04202
The second cupredoxin domain of bacterial two domain multicopper oxidase McoN and similar ...
 417-478 3.24e-08

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: 52.26  E-value: 3.24e-08
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 346214843 417 FHLHGHAFAVVRSAGSTVYNyDNPIFRDVVSTGTpaaGDNVTIRFRTDNPGPWFLHCHIDFH 478
Cdd:cd04202   65 MHLHGHFFLVTATDGGPIPG-SAPWPKDTLNVAP---GERYDIEFVADNPGDWMFHCHKLHH 122
CuRO_1_2DMCO_NIR_like cd11024
The cupredoxin domain 1 of a two-domain laccase related to nitrite reductase; The two-domain ...
 49-151 5.57e-08

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: 51.12  E-value: 5.57e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346214843  49 NNVTPGPLVAGNKGDRFQLNVIdNLTNHtmlkSTSIHWHGffqKGTNWADGPAFVnqcPISSGHSFLYDFqVPDQAGTFW 128
Cdd:cd11024   27 NGTVPGPTLRATEGDLVRIHFI-NTGDH----PHTIHFHG---IHDAAMDGTGLG---PIMPGESFTYEF-VAEPAGTHL 94

                         90       100
                 ....*....|....*....|....*.
gi 346214843 129 YHSH---LSTQYCDGLRGPFVVyDPN 151
Cdd:cd11024   95 YHCHvqpLKEHIAMGLYGAFIV-DPK 119
CuRO_2_CopA_like_1 cd13870
The second cupredoxin domain of CopA copper resistance protein like family; The members of ...
 180-273 4.65e-07

The second cupredoxin domain of CopA copper resistance protein like family; The members of this family are copper resistance protein (CopA) homologs. CopA is multicopper oxidase (MCO) related to laccase and L-ascorbate oxidase, both copper-containing enzymes. CopA is involved in copper resistance in bacteria. CopA mutant causes a loss of function, including copper tolerance and oxidase activity, and copA transcription is inducible in the presence of copper. Although MCOs have diverse functions, majority of them have three cupredoxin domain repeats that include one mononuclear and one trinuclear copper center. The copper ions are bound in several sites: Type 1, Type 2, and/or Type 3. The ensemble of types 2 and 3 copper is called a trinuclear cluster. MCOs oxidize their substrate by accepting electrons at a mononuclear copper center and transferring them to the active site trinuclear copper center. The cupredoxin domain 2 of 3-domain MCOs has lost the ability to bind copper.


Pssm-ID: 259938 [Multi-domain]  Cd Length: 117  Bit Score: 48.48  E-value: 4.65e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346214843 180 GPAFPLGADAT-------LINGlgRSPsttaADLAVINVTKGKRYRFRLVSLSCDPNHTFSIDGHDLTIIEVDSINSQHL 252
Cdd:cd13870    1 TPSGPLGGDAGdvrypyyLING--RPP----EDPAVFTARPGDRLRLRLINAAGDTAFRVALAGHRLTVTHTDGFPVEPV 74

                         90       100
                 ....*....|....*....|.
gi 346214843 253 VVDSIQIFAAQRYSFVLNADQ 273
Cdd:cd13870   75 EVDALLIGMGERYDAIVTANN 95
CuRO_1_MCO_like_1 cd13862
The first cupredoxin domain of uncharacterized multicopper oxidase; Multicopper Oxidases (MCOs) ...
 49-147 1.61e-06

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: 47.13  E-value: 1.61e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346214843  49 NNVTPGPLVAGNKGDRFQLNVIdNLTNHTmlksTSIHWHGFFQKGTnwADGPAFVNQCPISSGHSFLYDFqVPDQAGTFW 128
Cdd:cd13862   26 NGQVPGPLLRMRQGVSVTVDVF-NDTDIP----EYVHWHGLPLPAD--VDGAMEEGTPSVPPHGHRRYRM-TPRPAGFRW 97

                         90       100
                 ....*....|....*....|....*.
gi 346214843 129 YHSHLST-------QYcDGLRGPFVV 147
Cdd:cd13862   98 YHTHVMTmddltrgQY-SGLFGFVYI 122
CuRO_3_AAO_like_2 cd13895
The third cupredoxin domain of Ascorbate oxidase homologs; This family includes fungal ...
 417-487 2.54e-05

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: 45.00  E-value: 2.54e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346214843 417 FHLHGHAFAVVRSaGSTVYNYD-----------NPIFRDVV------STGTPAAGDNVT----IRFRTDNPGPWFLHCHI 475
Cdd:cd13895   95 WHAHGAHYYDLGS-GLGTYSATalaneeklrgyNPIRRDTTmlyrygGKGYYPPPGTGSgwraWRLRVDDPGVWMLHCHI 173

                         90
                 ....*....|..
gi 346214843 476 DFHLEAGFAVVM 487
Cdd:cd13895  174 LQHMIMGMQTVW 185
PRK10965 PRK10965
multicopper oxidase; Provisional
 48-152 6.85e-05

multicopper oxidase; Provisional


Pssm-ID: 236810 [Multi-domain]  Cd Length: 523  Bit Score: 45.40  E-value: 6.85e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346214843  48 VNNVTPGPLVAGNKGDRFQLNVidnlTNHtMLKSTSIHWHGFFQKGTnwADG-PafvnQCPISSGHSFLYDFQVPDQAGT 126
Cdd:PRK10965  70 YNGNLLGPAVRLQRGKAVTVDI----TNQ-LPEETTLHWHGLEVPGE--VDGgP----QGIIAPGGKRTVTFTVDQPAAT 138

                         90       100       110
                 ....*....|....*....|....*....|
gi 346214843 127 FWYHSHL----STQYCDGLRGPFVVYDPND 152
Cdd:PRK10965 139 CWFHPHQhgktGRQVAMGLAGLVLIEDDES 168
CuRO_1_Ceruloplasmin_like_1 cd04229
cupredoxin domain of ceruloplasmin homologs; Uncharacterized subfamily of ceruloplasmin ...
 54-149 8.05e-05

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: 43.56  E-value: 8.05e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346214843  54 GPLVAGNKGDRFQLNVIDNLTNHTMlkstSIHWHG-FFQKGtnwADGPAFVNQCPISSGHSFLYDFQVPDQAG------- 125
Cdd:cd04229   73 GPVIRAEVGDTIKVVFKNNLDEFPV----NMHPHGgLYSKD---NEGTTDGAGDVVAPGETYTYRWIVPEDAGpgpgdps 145

                         90       100
                 ....*....|....*....|....*...
gi 346214843 126 --TFWYHSHLSTQYCD--GLRGPFVVYD 149
Cdd:cd04229  146 srLWLYHSHVDVFAHTnaGLVGPIIVTS 173
CuRO_3_Tth-MCO_like cd13900
The third cupredoxin domain of the bacterial laccases similar to Tth-MCO from Thermus ...
 351-482 8.10e-05

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


Pssm-ID: 259967 [Multi-domain]  Cd Length: 123  Bit Score: 42.23  E-value: 8.10e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346214843 351 NFNGTNFFINGASFVPPTVPVLLQiisgaQNAQD--LLPSGSVYSLPanadieisfpataaapgaphpFHLHGHAFAVVR 428
Cdd:cd13900   14 PGGGGAFTINGKPFDPDRPDRTVR-----LGTVEewTLINTSGEDHP---------------------FHIHVNPFQVVS 67

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 346214843 429 SAGSTvynYDNPIFRDVVSTgtpAAGDNVTIRFR-TDNPGPWFLHCHIDFHLEAG 482
Cdd:cd13900   68 INGKP---GLPPVWRDTVNV---PAGGSVTIRTRfRDFTGEFVLHCHILDHEDQG 116
CuRO_6_ceruloplasmin cd11012
The sixth cupredoxin domain of Ceruloplasmin; Ceruloplasmin is a multicopper oxidase essential ...
 418-485 2.93e-04

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: 41.39  E-value: 2.93e-04
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 346214843 418 HLHGHAFAVVRSAgstvynydnpIFRDVVSTGTPAAGDNVTIRFRtdNPGPWFLHCHIDFHLEAGFAV 485
Cdd:cd11012   85 HFHGHSFDYKHRG----------VYRSDVFDLFPGTFQTVEMIPR--TPGTWLLHCHVTDHIHAGMET 140
CuRO_2_MCO_like_2 cd13887
The second cupredoxin domain of uncharacterized multicopper oxidase; Multicopper Oxidases ...
 202-264 2.05e-03

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: 38.07  E-value: 2.05e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 346214843 202 TAADLAVINVTKGKRYRFRLVSLSCDPNHTFSIDGHDLTIIEVDSINSQHLVVDSIQIFAAQR 264
Cdd:cd13887   19 TLDDPEVVRVEPGGRVRLRVINGSTATNFHIDLGDLKGTLIAVDGNPVQPVEGRRFPLATAQR 81
 
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.
Help | Disclaimer | Write to the Help Desk
NCBI | NLM | NIH