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Conserved domains on  [gi|558695371|dbj|BAO09156|]
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laccase1a [Agaricus brasiliensis]

Protein Classification

multicopper oxidase( domain architecture ID 10195165)

multicopper oxidase (MCO) that couples the oxidation of a substrate with a four-electron reduction of molecular oxygen to water, and which contains three cupredoxin domains that include one mononuclear and one trinuclear copper center; similar to Trametes villosa laccase-2 that may be involved in lignin degradation and detoxification of lignin-derived products

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
CuRO_2_Tv-LCC_like cd13882
The second cupredoxin domain of the fungal laccases similar to Tv-LCC from Trametes versicolor; ...
 162-325 9.84e-85

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: 258.88  E-value: 9.84e-85
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 558695371 162 TVITLGEWYHVLAPAGNNDffTSGTVPVQDSGLINGKGRFNGGPEVPFAVVNVEKGKRYRFRVIALSCRPFFTFSVDNHN 241
Cdd:cd13882    1 TVITLGDWYHTAAPDLLAT--TAGVPPVPDSGTINGKGRFDGGPTSPLAVINVKRGKRYRFRVINISCIPSFTFSIDGHN 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 558695371 242 ITFMEADGVEHDPVEAQNVDVYAAQRVSVILNANQPIGNYWIRAPPTGGnpaNNPNYNPNLTLAILRYKGAADEEPTTVN 321
Cdd:cd13882   79 LTVIEADGVETKPLTVDSVQIYAGQRYSVVVEANQPVDNYWIRAPPTGG---TPANNGGQLNRAILRYKGAPEVEPTTES 155


                 ....
gi 558695371 322 VPGH 325
Cdd:cd13882  156 TAGI 159
CuRO_1_Tv-LCC_like cd13856
The first cupredoxin domain of fungal laccases similar to Tv-LCC from Trametes versicolor; ...
 22-146 8.17e-79

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: 242.63  E-value: 8.17e-79
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 558695371  22 KTFNFDLVNARLAPDGFERDTVVINGEFPGTLIQVNKGDTVRIPVNNKLTNPLMRRSTSIHWHGFFQARTSAQDGPSFVN 101
Cdd:cd13856    1 PTYTLNIVNTRLAPDGFERSAVLANGQFPGPLITANKGDTFRITVVNQLTDPTMRRSTSIHWHGIFQHGTNYADGPAFVT 80

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*
gi 558695371 102 QCPQPPNTTFTYEFSVANQTGTYWYHSHLSTQYCDGLRGGFIVYD 146
Cdd:cd13856   81 QCPIAPNHSFTYDFTAGDQAGTFWYHSHLSTQYCDGLRGPLVIYD 125
CuRO_3_Tv-LCC_like cd13903
The third cupredoxin domain of the fungal laccases similar to Tv-LCC from Trametes Versicolor; ...
 349-489 9.95e-74

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: 230.24  E-value: 9.95e-74
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 558695371 349 DKHITLNIA-QPHSPFFDINGISYISPTVPVLLQILSGAKKPEDVLPSEQIFFIPKNSLIEVNIPG---AGAHPFHLHGH 424
Cdd:cd13903    1 DVNITLTFGlNGTTGLFTINGVSYVSPTVPVLLQILSGATSAEDLLPTESTIILPRNKVVEITIPGgaiGGPHPFHLHGH 80

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 558695371 425 NFDVVLASNDDTFNFKNPPRRDVYPIN--GGNTTFRFFTDNPGTWFLHCHIDWHLEAGLAIVFAESP 489
Cdd:cd13903   81 AFSVVRSAGSNTYNYVNPVRRDVVSVGtpGDGVTIRFVTDNPGPWFLHCHIDWHLEAGLAVVFAEDP 147
 
Name Accession Description Interval E-value
CuRO_2_Tv-LCC_like cd13882
The second cupredoxin domain of the fungal laccases similar to Tv-LCC from Trametes versicolor; ...
 162-325 9.84e-85

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: 258.88  E-value: 9.84e-85
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 558695371 162 TVITLGEWYHVLAPAGNNDffTSGTVPVQDSGLINGKGRFNGGPEVPFAVVNVEKGKRYRFRVIALSCRPFFTFSVDNHN 241
Cdd:cd13882    1 TVITLGDWYHTAAPDLLAT--TAGVPPVPDSGTINGKGRFDGGPTSPLAVINVKRGKRYRFRVINISCIPSFTFSIDGHN 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 558695371 242 ITFMEADGVEHDPVEAQNVDVYAAQRVSVILNANQPIGNYWIRAPPTGGnpaNNPNYNPNLTLAILRYKGAADEEPTTVN 321
Cdd:cd13882   79 LTVIEADGVETKPLTVDSVQIYAGQRYSVVVEANQPVDNYWIRAPPTGG---TPANNGGQLNRAILRYKGAPEVEPTTES 155


                 ....
gi 558695371 322 VPGH 325
Cdd:cd13882  156 TAGI 159
CuRO_1_Tv-LCC_like cd13856
The first cupredoxin domain of fungal laccases similar to Tv-LCC from Trametes versicolor; ...
 22-146 8.17e-79

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: 242.63  E-value: 8.17e-79
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 558695371  22 KTFNFDLVNARLAPDGFERDTVVINGEFPGTLIQVNKGDTVRIPVNNKLTNPLMRRSTSIHWHGFFQARTSAQDGPSFVN 101
Cdd:cd13856    1 PTYTLNIVNTRLAPDGFERSAVLANGQFPGPLITANKGDTFRITVVNQLTDPTMRRSTSIHWHGIFQHGTNYADGPAFVT 80

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*
gi 558695371 102 QCPQPPNTTFTYEFSVANQTGTYWYHSHLSTQYCDGLRGGFIVYD 146
Cdd:cd13856   81 QCPIAPNHSFTYDFTAGDQAGTFWYHSHLSTQYCDGLRGPLVIYD 125
ascorbase TIGR03388
L-ascorbate oxidase, plant type; Members of this protein family are the copper-containing ...
 21-487 1.25e-75

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


Pssm-ID: 274555 [Multi-domain]  Cd Length: 541  Bit Score: 248.13  E-value: 1.25e-75
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 558695371   21 TKTFNFDLVNARLAPDGFERDTVVINGEFPGTLIQVNKGDTVRIPVNNKLtnplMRRSTSIHWHGFFQARTSAQDGPSFV 100
Cdd:TIGR03388   1 IRHYKWEVEYEFWSPDCFEKLVIGINGQFPGPTIRAQAGDTIVVELTNKL----HTEGVVIHWHGIRQIGTPWADGTAGV 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 558695371  101 NQCPQPPNTTFTYEFSVaNQTGTYWYHSHLSTQYCDGLRGGFIVyDPNDPLADLYDVDDENTVItLGEWYHVLAPAGNND 180
Cdd:TIGR03388  77 TQCAINPGETFIYNFVV-DRPGTYFYHGHYGMQRSAGLYGSLIV-DVPDGEKEPFHYDGEFNLL-LSDWWHKSIHEQEVG 153

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 558695371  181 FftsGTVPVQ-----DSGLINGKGRFN------------------GGPEVPFAVVNVEKGKRYRFRVIALSCRPFFTFSV 237
Cdd:TIGR03388 154 L---SSKPMRwigepQSLLINGRGQFNcslaakfsstnlpqcnlkGNEQCAPQILHVEPGKTYRLRIASTTALAALNFAI 230

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 558695371  238 DNHNITFMEADGVEHDPVEAQNVDVYAAQRVSVILNANQ-PIGNYWI------RAP--PTGgnpannpnynpnltLAILR 308
Cdd:TIGR03388 231 EGHKLTVVEADGNYVEPFTVKDIDIYSGETYSVLLTTDQdPSRNYWIsvgvrgRKPntPPG--------------LTVLN 296

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 558695371  309 YKGA-ADEEPTTVNvPGHKLLDQEMHPIASEGP--GKLGSGPP----DKHI----TLNIAQPHSPfFDINGISYISPTVP 377
Cdd:TIGR03388 297 YYPNsPSRLPPTPP-PVTPAWDDFDRSKAFSLAikAAMGSPKPpetsDRRIvllnTQNKINGYTK-WAINNVSLTLPHTP 374

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 558695371  378 VLLQI---LSGA---KKPEDVLP----------------SEQIFFIPKNSLIEVNIPGAGA--------HPFHLHGHNFD 427
Cdd:TIGR03388 375 YLGSLkynLLNAfdqKPPPENYPrdydifkpppnpntttGNGIYRLKFNTTVDVILQNANTlngnnsetHPWHLHGHDFW 454

                         490       500       510       520       530       540       550
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 558695371  428 VV--------LASNDDTFNFKNPPRRD---VYPIngGNTTFRFFTDNPGTWFLHCHIDWHLEAGLAIVFAE 487
Cdd:TIGR03388 455 VLgygegkfrPGVDEKSYNLKNPPLRNtvvIFPY--GWTALRFVADNPGVWAFHCHIEPHLHMGMGVVFAE 523
CuRO_3_Tv-LCC_like cd13903
The third cupredoxin domain of the fungal laccases similar to Tv-LCC from Trametes Versicolor; ...
 349-489 9.95e-74

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: 230.24  E-value: 9.95e-74
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 558695371 349 DKHITLNIA-QPHSPFFDINGISYISPTVPVLLQILSGAKKPEDVLPSEQIFFIPKNSLIEVNIPG---AGAHPFHLHGH 424
Cdd:cd13903    1 DVNITLTFGlNGTTGLFTINGVSYVSPTVPVLLQILSGATSAEDLLPTESTIILPRNKVVEITIPGgaiGGPHPFHLHGH 80

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 558695371 425 NFDVVLASNDDTFNFKNPPRRDVYPIN--GGNTTFRFFTDNPGTWFLHCHIDWHLEAGLAIVFAESP 489
Cdd:cd13903   81 AFSVVRSAGSNTYNYVNPVRRDVVSVGtpGDGVTIRFVTDNPGPWFLHCHIDWHLEAGLAVVFAEDP 147
PLN02191 PLN02191
L-ascorbate oxidase
 35-487 4.61e-66

L-ascorbate oxidase


Pssm-ID: 177843 [Multi-domain]  Cd Length: 574  Bit Score: 223.74  E-value: 4.61e-66
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 558695371  35 PDGFERDTVVINGEFPGTLIQVNKGDTVRIPVNNKLTNplmrRSTSIHWHGFFQARTSAQDGPSFVNQCPQPPNTTFTYE 114
Cdd:PLN02191  37 PDCKEGAVMTVNGQFPGPTIDAVAGDTIVVHLTNKLTT----EGLVIHWHGIRQKGSPWADGAAGVTQCAINPGETFTYK 112

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 558695371 115 FSVaNQTGTYWYHSHLSTQYCDGLRGGFIVYDPNDPLADLydVDDENTVITLGEWYHVLAPAGNndfFTSGTVPVQ---- 190
Cdd:PLN02191 113 FTV-EKPGTHFYHGHYGMQRSAGLYGSLIVDVAKGPKERL--RYDGEFNLLLSDWWHESIPSQE---LGLSSKPMRwige 186

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 558695371 191 -DSGLINGKGRFN--------GGPEVPFA-----------VVNVEKGKRYRFRVIALSCRPFFTFSVDNHNITFMEADGV 250
Cdd:PLN02191 187 aQSILINGRGQFNcslaaqfsNGTELPMCtfkegdqcapqTLRVEPNKTYRIRLASTTALASLNLAVQGHKLVVVEADGN 266

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 558695371 251 EHDPVEAQNVDVYAAQRVSVILNANQ-PIGNYWI------RAPPTggnpannpnynpNLTLAILRYKGAADEEPTTVNVP 323
Cdd:PLN02191 267 YITPFTTDDIDIYSGESYSVLLTTDQdPSQNYYIsvgvrgRKPNT------------TQALTILNYVTAPASKLPSSPPP 334

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 558695371 324 GHKLLD--QEMHPIASEGPGKLGS-GPPDKH----ITLNIAQPHSPF--FDINGISYISPTVPVLLQILSGAK------- 387
Cdd:PLN02191 335 VTPRWDdfERSKNFSKKIFSAMGSpSPPKKYrkrlILLNTQNLIDGYtkWAINNVSLVTPATPYLGSVKYNLKlgfnrks 414

                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 558695371 388 ------------KP---EDVLPSEQIFFIPKNSLIEVNIPGAGA--------HPFHLHGHNFDVV--------LASNDDT 436
Cdd:PLN02191 415 pprsyrmdydimNPppfPNTTTGNGIYVFPFNVTVDVIIQNANVlkgvvseiHPWHLHGHDFWVLgygdgkfkPGIDEKT 494

                        490       500       510       520       530
                 ....*....|....*....|....*....|....*....|....*....|....
gi 558695371 437 FNFKNPPRRD---VYPIngGNTTFRFFTDNPGTWFLHCHIDWHLEAGLAIVFAE 487
Cdd:PLN02191 495 YNLKNPPLRNtaiLYPY--GWTAIRFVTDNPGVWFFHCHIEPHLHMGMGVVFAE 546
SufI COG2132
Multicopper oxidase with three cupredoxin domains (includes cell division protein FtsP and ...
 14-485 1.20e-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: 173.58  E-value: 1.20e-48
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 558695371  14 ISGALGATKTFNFDLV----NARLAPdGFERDTVVINGEFPGTLIQVNKGDTVRIPVNNKLTNPlmrrsTSIHWHGFfqa 89
Cdd:COG2132    4 IPPLLESGGGREYELTaqpaTVELLP-GKPTTVWGYNGQYPGPTIRVREGDRVRVRVTNRLPEP-----TTVHWHGL--- 74

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 558695371  90 RTS-AQDGpsfVNQCPQPPNTTFTYEFSVANQTGTYWYHSHL----STQYCDGLRGGFIVYDPNDplaDLYDVDDENTVI 164
Cdd:COG2132   75 RVPnAMDG---VPGDPIAPGETFTYEFPVPQPAGTYWYHPHThgstAEQVYRGLAGALIVEDPEE---DLPRYDRDIPLV 148

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 558695371 165 tLGEWyhVLAPAGNNDFFTSGTVP--VQDSGLINGKgrfnggpevPFAVVNVEKGKRYRFRVIALSCRPFFTFSV-DNHN 241
Cdd:COG2132  149 -LQDW--RLDDDGQLLYPMDAAMGgrLGDTLLVNGR---------PNPTLEVRPGERVRLRLLNASNARIYRLALsDGRP 216

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 558695371 242 ITFMEADG--VEHdPVEAQNVDVYAAQRVSVILNANQPIG-NYWIRAPPTGGnpannpnynPNLTLAILRYKGAADEEPt 318
Cdd:COG2132  217 FTVIATDGglLPA-PVEVDELLLAPGERADVLVDFSADPGeEVTLANPFEGR---------SGRALLTLRVTGAAASAP- 285

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 558695371 319 tvnvpghklLDQEMHPIASegpgkLGSGPPDKHITLNIA-QPHSPFFDINGISYiSPTVPvllqilsgakkpedvlpseq 397
Cdd:COG2132  286 ---------LPANLAPLPD-----LEDREAVRTRELVLTgGMAGYVWTINGKAF-DPDRP-------------------- 330

                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 558695371 398 IFFIPKNSLIEVNI--PGAGAHPFHLHGHNFDvVLASNDDTFNFknPPRRDVYPINGGNT-TFRF-FTDNPGTWFLHCHI 473
Cdd:COG2132  331 DLTVKLGERERWTLvnDTMMPHPFHLHGHQFQ-VLSRNGKPPPE--GGWKDTVLVPPGETvRILFrFDNYPGDWMFHCHI 407

                        490
                 ....*....|..
gi 558695371 474 DWHLEAGLAIVF 485
Cdd:COG2132  408 LEHEDAGMMGQF 419
Cu-oxidase pfam00394
Multicopper oxidase; Many of the proteins in this family contain multiple similar copies of ...
 160-312 9.23e-44

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: 151.70  E-value: 9.23e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 558695371  160 ENTVITLGEWYHVLAPAGNNDFFTSG-----TVPVQDSGLINGKgrfnggPEVPFAVVNVEKGKRYRFRVIALSCRPFFT 234
Cdd:pfam00394   1 EDYVITLSDWYHKDAKDLEKELLASGkaptdFPPVPDAVLINGK------DGASLATLTVTPGKTYRLRIINVALDDSLN 74

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 558695371  235 FSVDNHNITFMEADGVEHDPVEAQNVDVYAAQRVSVILNANQPIGNYWIRAPPTGGnpannpNYNPNLTLAILRYKGA 312
Cdd:pfam00394  75 FSIEGHKMTVVEVDGVYVNPFTVDSLDIFPGQRYSVLVTANQDPGNYWIVASPNIP------AFDNGTAAAILRYSGA 146
Cu-oxidase_3 pfam07732
Multicopper oxidase; This entry contains many divergent copper oxidase-like domains that are ...
 34-149 2.68e-41

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: 144.31  E-value: 2.68e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 558695371   34 APDGFERDTVV-INGEFPGTLIQVNKGDTVRIPVNNKLTNPlmrrsTSIHWHGFFQARTSAQDGPSFVNQCPQPPNTTFT 112
Cdd:pfam07732   8 SPLGGTRQAVIgVNGQFPGPTIRVREGDTVVVNVTNNLDEP-----TSIHWHGLQQRGTPWMDGVPGVTQCPIPPGQSFT 82

                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 558695371  113 YEFSVANQTGTYWYHSHLSTQYCDGLRGGFIVYDPND 149
Cdd:pfam07732  83 YRFQVKQQAGTYWYHSHTSGQQAAGLAGAIIIEDRAS 119
Cu-oxidase_2 pfam07731
Multicopper oxidase; This entry contains many divergent copper oxidase-like domains that are ...
 371-491 3.41e-36

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: 131.02  E-value: 3.41e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 558695371  371 YISPTVPVLLQILSGAKKPEDVLPSEQIFF-------IPKNSLIEVNI--PGAGAHPFHLHGHNFDVVLASNDD------ 435
Cdd:pfam07731   1 DTPPKLPTLLQITSGNFRRNDWAINGLLFPpntnvitLPYGTVVEWVLqnTTTGVHPFHLHGHSFQVLGRGGGPwpeedp 80

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 558695371  436 -TFNFKNPPRRDVYPIN-GGNTTFRFFTDNPGTWFLHCHIDWHLEAGLAIVFAESPED 491
Cdd:pfam07731  81 kTYNLVDPVRRDTVQVPpGGWVAIRFRADNPGVWLFHCHILWHLDQGMMGQFVVRPGD 138
PRK10965 PRK10965
multicopper oxidase; Provisional
 45-159 1.14e-10

multicopper oxidase; Provisional


Pssm-ID: 236810 [Multi-domain]  Cd Length: 523  Bit Score: 63.89  E-value: 1.14e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 558695371  45 INGEFPGTLIQVNKGDTVRIPVNNKLTNPlmrrsTSIHWHGFFQartsaqdgPSFVNQCPQ---PPNTTFTYEFSVANQT 121
Cdd:PRK10965  70 YNGNLLGPAVRLQRGKAVTVDITNQLPEE-----TTLHWHGLEV--------PGEVDGGPQgiiAPGGKRTVTFTVDQPA 136

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*
gi 558695371 122 GTYWYHSHL----STQYCDGLRGGFIVYDPND---PLADLYDVDD 159
Cdd:PRK10965 137 ATCWFHPHQhgktGRQVAMGLAGLVLIEDDESlklGLPKQWGVDD 181
 
Name Accession Description Interval E-value
CuRO_2_Tv-LCC_like cd13882
The second cupredoxin domain of the fungal laccases similar to Tv-LCC from Trametes versicolor; ...
 162-325 9.84e-85

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: 258.88  E-value: 9.84e-85
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 558695371 162 TVITLGEWYHVLAPAGNNDffTSGTVPVQDSGLINGKGRFNGGPEVPFAVVNVEKGKRYRFRVIALSCRPFFTFSVDNHN 241
Cdd:cd13882    1 TVITLGDWYHTAAPDLLAT--TAGVPPVPDSGTINGKGRFDGGPTSPLAVINVKRGKRYRFRVINISCIPSFTFSIDGHN 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 558695371 242 ITFMEADGVEHDPVEAQNVDVYAAQRVSVILNANQPIGNYWIRAPPTGGnpaNNPNYNPNLTLAILRYKGAADEEPTTVN 321
Cdd:cd13882   79 LTVIEADGVETKPLTVDSVQIYAGQRYSVVVEANQPVDNYWIRAPPTGG---TPANNGGQLNRAILRYKGAPEVEPTTES 155


                 ....
gi 558695371 322 VPGH 325
Cdd:cd13882  156 TAGI 159
CuRO_1_Tv-LCC_like cd13856
The first cupredoxin domain of fungal laccases similar to Tv-LCC from Trametes versicolor; ...
 22-146 8.17e-79

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: 242.63  E-value: 8.17e-79
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 558695371  22 KTFNFDLVNARLAPDGFERDTVVINGEFPGTLIQVNKGDTVRIPVNNKLTNPLMRRSTSIHWHGFFQARTSAQDGPSFVN 101
Cdd:cd13856    1 PTYTLNIVNTRLAPDGFERSAVLANGQFPGPLITANKGDTFRITVVNQLTDPTMRRSTSIHWHGIFQHGTNYADGPAFVT 80

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*
gi 558695371 102 QCPQPPNTTFTYEFSVANQTGTYWYHSHLSTQYCDGLRGGFIVYD 146
Cdd:cd13856   81 QCPIAPNHSFTYDFTAGDQAGTFWYHSHLSTQYCDGLRGPLVIYD 125
ascorbase TIGR03388
L-ascorbate oxidase, plant type; Members of this protein family are the copper-containing ...
 21-487 1.25e-75

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


Pssm-ID: 274555 [Multi-domain]  Cd Length: 541  Bit Score: 248.13  E-value: 1.25e-75
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 558695371   21 TKTFNFDLVNARLAPDGFERDTVVINGEFPGTLIQVNKGDTVRIPVNNKLtnplMRRSTSIHWHGFFQARTSAQDGPSFV 100
Cdd:TIGR03388   1 IRHYKWEVEYEFWSPDCFEKLVIGINGQFPGPTIRAQAGDTIVVELTNKL----HTEGVVIHWHGIRQIGTPWADGTAGV 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 558695371  101 NQCPQPPNTTFTYEFSVaNQTGTYWYHSHLSTQYCDGLRGGFIVyDPNDPLADLYDVDDENTVItLGEWYHVLAPAGNND 180
Cdd:TIGR03388  77 TQCAINPGETFIYNFVV-DRPGTYFYHGHYGMQRSAGLYGSLIV-DVPDGEKEPFHYDGEFNLL-LSDWWHKSIHEQEVG 153

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 558695371  181 FftsGTVPVQ-----DSGLINGKGRFN------------------GGPEVPFAVVNVEKGKRYRFRVIALSCRPFFTFSV 237
Cdd:TIGR03388 154 L---SSKPMRwigepQSLLINGRGQFNcslaakfsstnlpqcnlkGNEQCAPQILHVEPGKTYRLRIASTTALAALNFAI 230

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 558695371  238 DNHNITFMEADGVEHDPVEAQNVDVYAAQRVSVILNANQ-PIGNYWI------RAP--PTGgnpannpnynpnltLAILR 308
Cdd:TIGR03388 231 EGHKLTVVEADGNYVEPFTVKDIDIYSGETYSVLLTTDQdPSRNYWIsvgvrgRKPntPPG--------------LTVLN 296

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 558695371  309 YKGA-ADEEPTTVNvPGHKLLDQEMHPIASEGP--GKLGSGPP----DKHI----TLNIAQPHSPfFDINGISYISPTVP 377
Cdd:TIGR03388 297 YYPNsPSRLPPTPP-PVTPAWDDFDRSKAFSLAikAAMGSPKPpetsDRRIvllnTQNKINGYTK-WAINNVSLTLPHTP 374

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 558695371  378 VLLQI---LSGA---KKPEDVLP----------------SEQIFFIPKNSLIEVNIPGAGA--------HPFHLHGHNFD 427
Cdd:TIGR03388 375 YLGSLkynLLNAfdqKPPPENYPrdydifkpppnpntttGNGIYRLKFNTTVDVILQNANTlngnnsetHPWHLHGHDFW 454

                         490       500       510       520       530       540       550
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 558695371  428 VV--------LASNDDTFNFKNPPRRD---VYPIngGNTTFRFFTDNPGTWFLHCHIDWHLEAGLAIVFAE 487
Cdd:TIGR03388 455 VLgygegkfrPGVDEKSYNLKNPPLRNtvvIFPY--GWTALRFVADNPGVWAFHCHIEPHLHMGMGVVFAE 523
CuRO_3_Tv-LCC_like cd13903
The third cupredoxin domain of the fungal laccases similar to Tv-LCC from Trametes Versicolor; ...
 349-489 9.95e-74

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: 230.24  E-value: 9.95e-74
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 558695371 349 DKHITLNIA-QPHSPFFDINGISYISPTVPVLLQILSGAKKPEDVLPSEQIFFIPKNSLIEVNIPG---AGAHPFHLHGH 424
Cdd:cd13903    1 DVNITLTFGlNGTTGLFTINGVSYVSPTVPVLLQILSGATSAEDLLPTESTIILPRNKVVEITIPGgaiGGPHPFHLHGH 80

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 558695371 425 NFDVVLASNDDTFNFKNPPRRDVYPIN--GGNTTFRFFTDNPGTWFLHCHIDWHLEAGLAIVFAESP 489
Cdd:cd13903   81 AFSVVRSAGSNTYNYVNPVRRDVVSVGtpGDGVTIRFVTDNPGPWFLHCHIDWHLEAGLAVVFAEDP 147
PLN02191 PLN02191
L-ascorbate oxidase
 35-487 4.61e-66

L-ascorbate oxidase


Pssm-ID: 177843 [Multi-domain]  Cd Length: 574  Bit Score: 223.74  E-value: 4.61e-66
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 558695371  35 PDGFERDTVVINGEFPGTLIQVNKGDTVRIPVNNKLTNplmrRSTSIHWHGFFQARTSAQDGPSFVNQCPQPPNTTFTYE 114
Cdd:PLN02191  37 PDCKEGAVMTVNGQFPGPTIDAVAGDTIVVHLTNKLTT----EGLVIHWHGIRQKGSPWADGAAGVTQCAINPGETFTYK 112

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 558695371 115 FSVaNQTGTYWYHSHLSTQYCDGLRGGFIVYDPNDPLADLydVDDENTVITLGEWYHVLAPAGNndfFTSGTVPVQ---- 190
Cdd:PLN02191 113 FTV-EKPGTHFYHGHYGMQRSAGLYGSLIVDVAKGPKERL--RYDGEFNLLLSDWWHESIPSQE---LGLSSKPMRwige 186

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 558695371 191 -DSGLINGKGRFN--------GGPEVPFA-----------VVNVEKGKRYRFRVIALSCRPFFTFSVDNHNITFMEADGV 250
Cdd:PLN02191 187 aQSILINGRGQFNcslaaqfsNGTELPMCtfkegdqcapqTLRVEPNKTYRIRLASTTALASLNLAVQGHKLVVVEADGN 266

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 558695371 251 EHDPVEAQNVDVYAAQRVSVILNANQ-PIGNYWI------RAPPTggnpannpnynpNLTLAILRYKGAADEEPTTVNVP 323
Cdd:PLN02191 267 YITPFTTDDIDIYSGESYSVLLTTDQdPSQNYYIsvgvrgRKPNT------------TQALTILNYVTAPASKLPSSPPP 334

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 558695371 324 GHKLLD--QEMHPIASEGPGKLGS-GPPDKH----ITLNIAQPHSPF--FDINGISYISPTVPVLLQILSGAK------- 387
Cdd:PLN02191 335 VTPRWDdfERSKNFSKKIFSAMGSpSPPKKYrkrlILLNTQNLIDGYtkWAINNVSLVTPATPYLGSVKYNLKlgfnrks 414

                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 558695371 388 ------------KP---EDVLPSEQIFFIPKNSLIEVNIPGAGA--------HPFHLHGHNFDVV--------LASNDDT 436
Cdd:PLN02191 415 pprsyrmdydimNPppfPNTTTGNGIYVFPFNVTVDVIIQNANVlkgvvseiHPWHLHGHDFWVLgygdgkfkPGIDEKT 494

                        490       500       510       520       530
                 ....*....|....*....|....*....|....*....|....*....|....
gi 558695371 437 FNFKNPPRRD---VYPIngGNTTFRFFTDNPGTWFLHCHIDWHLEAGLAIVFAE 487
Cdd:PLN02191 495 YNLKNPPLRNtaiLYPY--GWTAIRFVTDNPGVWFFHCHIEPHLHMGMGVVFAE 546
laccase TIGR03389
laccase, plant; Members of this protein family include the copper-containing enzyme laccase ...
 43-502 5.11e-62

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: 212.29  E-value: 5.11e-62
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 558695371   43 VVINGEFPGTLIQVNKGDTVRIPVNNKLTNPLmrrstSIHWHGFFQARTSAQDGPSFVNQCPQPPNTTFTYEFSVANQTG 122
Cdd:TIGR03389  25 LTVNGKFPGPTLYAREGDTVIVNVTNNVQYNV-----TIHWHGVRQLRNGWADGPAYITQCPIQPGQSYVYNFTITGQRG 99

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 558695371  123 TYWYHSHLS----TQYcdglrGGFIVYdPNDPLADLYDVDDENTVITLGEWYHVLAPAGNNDFFTSGTVP-VQDSGLING 197
Cdd:TIGR03389 100 TLWWHAHISwlraTVY-----GAIVIL-PKPGVPYPFPKPDREVPIILGEWWNADVEAVINQANQTGGAPnVSDAYTING 173

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 558695371  198 K-GRFNGGPEVPFAVVNVEKGKRYRFRVI--ALSCRPFFTfsVDNHNITFMEADGVEHDPVEAQNVDVYAAQRVSVILNA 274
Cdd:TIGR03389 174 HpGPLYNCSSKDTFKLTVEPGKTYLLRIInaALNDELFFA--IANHTLTVVEVDATYTKPFKTKTIVIGPGQTTNVLLTA 251

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 558695371  275 NQPIGNYWIRAPPtggNPANNPNYNPNLTLAILRYKG----AADEEPTT-------------------------VNVPgh 325
Cdd:TIGR03389 252 DQSPGRYFMAARP---YMDAPGAFDNTTTTAILQYKGtsnsAKPILPTLpayndtaaatnfsnklrslnsaqypANVP-- 326

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 558695371  326 KLLDQEMHPIASEGpgkLGSGPPDKHITLNIAQPHSpffDINGISYISPTVPvLLQI----------------------L 383
Cdd:TIGR03389 327 VTIDRRLFFTIGLG---LDPCPNNTCQGPNGTRFAA---SMNNISFVMPTTA-LLQAhyfgisgvfttdfpanpptkfnY 399

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 558695371  384 SGAKKPEDVLPSE--QIFFIPKNSLIEV-----NIPGAGAHPFHLHGHNFDVV------LASNDDT--FNFKNPPRRDVY 448
Cdd:TIGR03389 400 TGTNLPNNLFTTNgtKVVRLKFNSTVELvlqdtSILGSENHPIHLHGYNFFVVgtgfgnFDPKKDPakFNLVDPPERNTV 479

                         490       500       510       520       530
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 558695371  449 PI-NGGNTTFRFFTDNPGTWFLHCHIDWHLEAGLAIVFAespEDNVSGPQSQITP 502
Cdd:TIGR03389 480 GVpTGGWAAIRFVADNPGVWFMHCHLEVHTTWGLKMAFL---VDNGKGPNQSLLP 531
PLN02604 PLN02604
oxidoreductase
 1-498 7.83e-59

oxidoreductase


Pssm-ID: 215324 [Multi-domain]  Cd Length: 566  Bit Score: 204.32  E-value: 7.83e-59
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 558695371   1 MRLSNAFVLAATCI--SGALGATKTFNFDLVNARLAPDGFERDTVVINGEFPGTLIQVNKGDTVRIpvnnKLTNPLMRRS 78
Cdd:PLN02604   2 MRFLALFFLLFSVLnfPAAEARIRRYKWEVKYEYKSPDCFKKLVITINGRSPGPTILAQQGDTVIV----ELKNSLLTEN 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 558695371  79 TSIHWHGFFQARTSAQDGPSFVNQCPQPPNTTFTYEFsVANQTGTYWYHSHLSTQYCDGLRGGFIVYDPN---DPLAdlY 155
Cdd:PLN02604  78 VAIHWHGIRQIGTPWFDGTEGVTQCPILPGETFTYEF-VVDRPGTYLYHAHYGMQREAGLYGSIRVSLPRgksEPFS--Y 154

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 558695371 156 DVDDEntvITLGEWYHV-----LAPAGNNDFftsGTVPVQDSGLINGKGRFN----------------GGPEVPFAVVNV 214
Cdd:PLN02604 155 DYDRS---IILTDWYHKstyeqALGLSSIPF---DWVGEPQSLLIQGKGRYNcslvsspylkagvcnaTNPECSPYVLTV 228

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 558695371 215 EKGKRYRFRVIALSCRPFFTFSVDNHNITFMEADGVEHDPVEAQNVDVYAAQRVSVILNANQ-PIGNYWI------RAP- 286
Cdd:PLN02604 229 VPGKTYRLRISSLTALSALSFQIEGHNMTVVEADGHYVEPFVVKNLFIYSGETYSVLVKADQdPSRNYWVttsvvsRNNt 308

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 558695371 287 -PTGgnpannpnynpnltLAILR-YKGAADEEPTTVNVPGHKLLDQEMHPIASEG----PGKLGSGPPDKH---ITLNIA 357
Cdd:PLN02604 309 tPPG--------------LAIFNyYPNHPRRSPPTVPPSGPLWNDVEPRLNQSLAikarHGYIHPPPLTSDrviVLLNTQ 374

                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 558695371 358 QPHSPFF--DINGISYISPTVPVLLQI---LSGA------------------KKPEDV--LPSEQIFFIPKNSLIEVNIP 412
Cdd:PLN02604 375 NEVNGYRrwSVNNVSFNLPHTPYLIALkenLTGAfdqtpppegydfanydiyAKPNNSnaTSSDSIYRLQFNSTVDIILQ 454

                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 558695371 413 GAGA--------HPFHLHGHNFdVVLASNDDTFNFKNPPRRD--VYPING--------GNTTFRFFTDNPGTWFLHCHID 474
Cdd:PLN02604 455 NANTmnannsetHPWHLHGHDF-WVLGYGEGKFNMSSDPKKYnlVDPIMKntvpvhpyGWTALRFRADNPGVWAFHCHIE 533

                        570       580
                 ....*....|....*....|....
gi 558695371 475 WHLEAGLAIVFAESPEDNVSGPQS 498
Cdd:PLN02604 534 SHFFMGMGVVFEEGIERVGKLPSS 557
CuRO_1_Diphenol_Ox cd13857
The first cupredoxin domain of fungal laccase, diphenol oxidase; Diphenol oxidase belongs to ...
 22-145 6.54e-51

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: 169.75  E-value: 6.54e-51
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 558695371  22 KTFNFDLVNARLAPDGFERDTVVINGEFPGTLIQVNKGDTVRIPVNNKLTNPlmrrsTSIHWHGFFQARTSAQDGPSFVN 101
Cdd:cd13857    1 REYNFTISEITGAPDGFVRPMLVINGQFPGPLIEANQGDRIVVHVTNELDEP-----TSIHWHGLFQNGTNWMDGTAGIT 75

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....
gi 558695371 102 QCPQPPNTTFTYEFSVANQTGTYWYHSHLSTQYCDGLRGGFIVY 145
Cdd:cd13857   76 QCPIPPGGSFTYNFTVDGQYGTYWYHSHYSTQYADGLVGPLIVH 119
SufI COG2132
Multicopper oxidase with three cupredoxin domains (includes cell division protein FtsP and ...
 14-485 1.20e-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: 173.58  E-value: 1.20e-48
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 558695371  14 ISGALGATKTFNFDLV----NARLAPdGFERDTVVINGEFPGTLIQVNKGDTVRIPVNNKLTNPlmrrsTSIHWHGFfqa 89
Cdd:COG2132    4 IPPLLESGGGREYELTaqpaTVELLP-GKPTTVWGYNGQYPGPTIRVREGDRVRVRVTNRLPEP-----TTVHWHGL--- 74

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 558695371  90 RTS-AQDGpsfVNQCPQPPNTTFTYEFSVANQTGTYWYHSHL----STQYCDGLRGGFIVYDPNDplaDLYDVDDENTVI 164
Cdd:COG2132   75 RVPnAMDG---VPGDPIAPGETFTYEFPVPQPAGTYWYHPHThgstAEQVYRGLAGALIVEDPEE---DLPRYDRDIPLV 148

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 558695371 165 tLGEWyhVLAPAGNNDFFTSGTVP--VQDSGLINGKgrfnggpevPFAVVNVEKGKRYRFRVIALSCRPFFTFSV-DNHN 241
Cdd:COG2132  149 -LQDW--RLDDDGQLLYPMDAAMGgrLGDTLLVNGR---------PNPTLEVRPGERVRLRLLNASNARIYRLALsDGRP 216

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 558695371 242 ITFMEADG--VEHdPVEAQNVDVYAAQRVSVILNANQPIG-NYWIRAPPTGGnpannpnynPNLTLAILRYKGAADEEPt 318
Cdd:COG2132  217 FTVIATDGglLPA-PVEVDELLLAPGERADVLVDFSADPGeEVTLANPFEGR---------SGRALLTLRVTGAAASAP- 285

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 558695371 319 tvnvpghklLDQEMHPIASegpgkLGSGPPDKHITLNIA-QPHSPFFDINGISYiSPTVPvllqilsgakkpedvlpseq 397
Cdd:COG2132  286 ---------LPANLAPLPD-----LEDREAVRTRELVLTgGMAGYVWTINGKAF-DPDRP-------------------- 330

                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 558695371 398 IFFIPKNSLIEVNI--PGAGAHPFHLHGHNFDvVLASNDDTFNFknPPRRDVYPINGGNT-TFRF-FTDNPGTWFLHCHI 473
Cdd:COG2132  331 DLTVKLGERERWTLvnDTMMPHPFHLHGHQFQ-VLSRNGKPPPE--GGWKDTVLVPPGETvRILFrFDNYPGDWMFHCHI 407

                        490
                 ....*....|..
gi 558695371 474 DWHLEAGLAIVF 485
Cdd:COG2132  408 LEHEDAGMMGQF 419
CuRO_1_MaLCC_like cd13854
The first cupredoxin domain of the fungal laccases similar to Ma-LCC from Melanocarpus ...
 19-145 1.51e-44

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


Pssm-ID: 259923 [Multi-domain]  Cd Length: 122  Bit Score: 152.78  E-value: 1.51e-44
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 558695371  19 GATKTFNFDLVNARLAPDGFERDTVVINGEFPGTLIQVNKGDTVRIPVNNKLTNplmrRSTSIHWHGFFQARTSAQDGPS 98
Cdd:cd13854    1 GVTRKYTLTITNSTLAPDGVEKEVMLINGQYPGPLIEANWGDTIEVTVINKLQD----NGTSIHWHGIRQLNTNWQDGVP 76

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*..
gi 558695371  99 FVNQCPQPPNTTFTYEFSvANQTGTYWYHSHLSTQYCDGLRGGFIVY 145
Cdd:cd13854   77 GVTECPIAPGDTRTYRFR-ATQYGTSWYHSHYSAQYGDGVVGPIVIH 122
CuRO_1_LCC_like cd04206
Cupredoxin domain 1 of laccase-like multicopper oxidases; including laccase, CueO, spore coat ...
 22-145 3.35e-44

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: 152.05  E-value: 3.35e-44
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 558695371  22 KTFNFDLVNARLAPDGFERDTVVINGEFPGTLIQVNKGDTVRIPVNNKLTNplmrRSTSIHWHGFFQARTSAQDGPSFVN 101
Cdd:cd04206    1 REYELTITETTVNPDGVLRQVITVNGQFPGPTIRVKEGDTVEVTVTNNLPN----EPTSIHWHGLRQPGTNDGDGVAGLT 76

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....
gi 558695371 102 QCPQPPNTTFTYEFSVANQTGTYWYHSHLSTQYCDGLRGGFIVY 145
Cdd:cd04206   77 QCPIPPGESFTYRFTVDDQAGTFWYHSHVGGQRADGLYGPLIVE 120
Cu-oxidase pfam00394
Multicopper oxidase; Many of the proteins in this family contain multiple similar copies of ...
 160-312 9.23e-44

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: 151.70  E-value: 9.23e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 558695371  160 ENTVITLGEWYHVLAPAGNNDFFTSG-----TVPVQDSGLINGKgrfnggPEVPFAVVNVEKGKRYRFRVIALSCRPFFT 234
Cdd:pfam00394   1 EDYVITLSDWYHKDAKDLEKELLASGkaptdFPPVPDAVLINGK------DGASLATLTVTPGKTYRLRIINVALDDSLN 74

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 558695371  235 FSVDNHNITFMEADGVEHDPVEAQNVDVYAAQRVSVILNANQPIGNYWIRAPPTGGnpannpNYNPNLTLAILRYKGA 312
Cdd:pfam00394  75 FSIEGHKMTVVEVDGVYVNPFTVDSLDIFPGQRYSVLVTANQDPGNYWIVASPNIP------AFDNGTAAAILRYSGA 146
CuRO_1_Fet3p cd13851
The first Cupredoxin domain of multicopper oxidase Fet3P; Fet3p catalyzes the ferroxidase ...
 21-144 1.23e-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: 150.50  E-value: 1.23e-43
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 558695371  21 TKTFNFDLVNArlAPDG-FERDTVVINGEFPGTLIQVNKGDTVRIPVNNKLTNplmrRSTSIHWHGFFQARTSAQDGPSF 99
Cdd:cd13851    2 EFDWNITWVTA--NPDGlFERRVIGINGQWPPPPIEVNKGDTVVIHATNSLGD----QPTSLHFHGLFQNGTNYMDGPVG 75

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*
gi 558695371 100 VNQCPQPPNTTFTYEFSVANQTGTYWYHSHLSTQYCDGLRGGFIV 144
Cdd:cd13851   76 VTQCPIPPGQSFTYEFTVDTQVGTYWYHSHDGGQYPDGLRGPFII 120
Cu-oxidase_3 pfam07732
Multicopper oxidase; This entry contains many divergent copper oxidase-like domains that are ...
 34-149 2.68e-41

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: 144.31  E-value: 2.68e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 558695371   34 APDGFERDTVV-INGEFPGTLIQVNKGDTVRIPVNNKLTNPlmrrsTSIHWHGFFQARTSAQDGPSFVNQCPQPPNTTFT 112
Cdd:pfam07732   8 SPLGGTRQAVIgVNGQFPGPTIRVREGDTVVVNVTNNLDEP-----TSIHWHGLQQRGTPWMDGVPGVTQCPIPPGQSFT 82

                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 558695371  113 YEFSVANQTGTYWYHSHLSTQYCDGLRGGFIVYDPND 149
Cdd:pfam07732  83 YRFQVKQQAGTYWYHSHTSGQQAAGLAGAIIIEDRAS 119
CuRO_1_tcLCC2_insect_like cd13858
The first cupredoxin domain of insect laccases similar to laccase 2 in Tribolium castaneum; ...
 36-144 9.86e-40

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: 139.60  E-value: 9.86e-40
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 558695371  36 DGFERDTVVINGEFPGTLIQVNKGDTVRIPVNNKLTNplmrRSTSIHWHGFFQARTSAQDGPSFVNQCPQPPNTTFTYEF 115
Cdd:cd13858    1 DGVERPVITVNGQLPGPSIEVCEGDTVVVDVKNRLPG----ESTTIHWHGIHQRGTPYMDGVPMVTQCPILPGQTFRYKF 76

                         90       100
                 ....*....|....*....|....*....
gi 558695371 116 SvANQTGTYWYHSHLSTQYCDGLRGGFIV 144
Cdd:cd13858   77 K-ADPAGTHWYHSHSGTQRADGLFGALIV 104
ascorbOXfungal TIGR03390
L-ascorbate oxidase, fungal type; This model describes a family of fungal ascorbate oxidases, ...
 39-485 2.85e-39

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


Pssm-ID: 132431 [Multi-domain]  Cd Length: 538  Bit Score: 149.99  E-value: 2.85e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 558695371   39 ERDTVVINGEFPGTLIQVNKGDTVRIPVNNKLTNplmrRSTSIHWHGFFQARTSAQDGPSFVNQCPQPPNTTFTYEFSVA 118
Cdd:TIGR03390  26 SRYSVVVNGTSPGPEIRLQEGQTTWIRVYNDIPD----NNVTMHWHGLTQRTAPFSDGTPLASQWPIPPGHFFDYEIKPE 101

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 558695371  119 -NQTGTYWYHSHLSTQYCDGlRGGFIVYDPNDPladLYDVDDENTVItLGEWYhvlapAGNNDFFTSG--TVPVQDSG-- 193
Cdd:TIGR03390 102 pGDAGSYFYHSHVGFQAVTA-FGPLIVEDCEPP---PYKYDDERILL-VSDFF-----SATDEEIEQGllSTPFTWSGet 171

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 558695371  194 ---LINGKGR-------FNGGPEVPFAVVNVEKGKRYRFRVIALSCRPFFTFSVDNH-NITFMEADGVEHDPVEAQNVDV 262
Cdd:TIGR03390 172 eavLLNGKSGnksfyaqINPSGSCMLPVIDVEPGKTYRLRFIGATALSLISLGIEDHeNLTIIEADGSYTKPAKIDHLQL 251

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 558695371  263 YAAQRVSVILNA--NQPIG-----NYWI----RAPPTggnpannpnynPNLTLAILRYKgaADEEPTTVNVPGHKL---- 327
Cdd:TIGR03390 252 GGGQRYSVLFKAktEDELCggdkrQYFIqfetRDRPK-----------VYRGYAVLRYR--SDKASKLPSVPETPPlplp 318

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 558695371  328 ------LDQEMHPIASE-GPGKLGSGPPDKHITLNIAQPHSPFFD-----INGISYIS--PTVPVLLQILSGAkkpEDVL 393
Cdd:TIGR03390 319 nstydwLEYELEPLSEEnNQDFPTLDEVTRRVVIDAHQNVDPLNGrvawlQNGLSWTEsvRQTPYLVDIYENG---LPAT 395

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 558695371  394 PSEQ-------------IFFIPKNSLIEVNIPGAGA----------HPFHLHG-HNFDvvLASNDDTFN-------FKN- 441
Cdd:TIGR03390 396 PNYTaalanygfdpetrAFPAKVGEVLEIVWQNTGSytgpnggvdtHPFHAHGrHFYD--IGGGDGEYNataneakLENy 473

                         490       500       510       520       530
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 558695371  442 -PPRRDV-----YPING------GNTTFRFFTDNPGTWFLHCHIDWHLEAGLAIVF 485
Cdd:TIGR03390 474 tPVLRDTtmlyrYAVKVvpgapaGWRAWRIRVTNPGVWMMHCHILQHMVMGMQTVW 529
CuRO_2_tcLCC_insect_like cd13884
The second cupredoxin domain of the insect laccases similar to laccase 2 in Tribolium ...
 163-309 1.13e-36

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: 132.74  E-value: 1.13e-36
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 558695371 163 VITLGEWYHVLAPAGNNDFFTSGTVPVQDSGLINGKGRFNGG-----PEVPFAVVNVEKGKRYRFRVI---ALSCrPFfT 234
Cdd:cd13884    3 VILIQDWTHELSSERFVGRGHNGGGQPPDSILINGKGRYYDPktgntNNTPLEVFTVEQGKRYRFRLInagATNC-PF-R 80

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 558695371 235 FSVDNHNITFMEADG--VEhdPVEAQNVDVYAAQRVSVILNANQPIGNYWIRAPPTGGNPANNPNynpnlTLAILRY 309
Cdd:cd13884   81 VSIDGHTLTVIASDGndVE--PVEVDSIIIYPGERYDFVLNANQPIGNYWIRARGLEDCDNRRLQ-----QLAILRY 150
Cu-oxidase_2 pfam07731
Multicopper oxidase; This entry contains many divergent copper oxidase-like domains that are ...
 371-491 3.41e-36

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: 131.02  E-value: 3.41e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 558695371  371 YISPTVPVLLQILSGAKKPEDVLPSEQIFF-------IPKNSLIEVNI--PGAGAHPFHLHGHNFDVVLASNDD------ 435
Cdd:pfam07731   1 DTPPKLPTLLQITSGNFRRNDWAINGLLFPpntnvitLPYGTVVEWVLqnTTTGVHPFHLHGHSFQVLGRGGGPwpeedp 80

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 558695371  436 -TFNFKNPPRRDVYPIN-GGNTTFRFFTDNPGTWFLHCHIDWHLEAGLAIVFAESPED 491
Cdd:pfam07731  81 kTYNLVDPVRRDTVQVPpGGWVAIRFRADNPGVWLFHCHILWHLDQGMMGQFVVRPGD 138
CuRO_3_Fet3p cd13899
The third Cupredoxin domain of multicopper oxidase Fet3p; Fet3p catalyzes the ferroxidase ...
 366-489 2.46e-35

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: 129.68  E-value: 2.46e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 558695371 366 INGISYISPTVPVLLQILSG---AKKPEDVLPSEQIFFIPKNSLIE--VNIPGAGAHPFHLHGHNFDVVLASNDDTFNFK 440
Cdd:cd13899   22 FNNITYVSPKVPTLYTALSMgddALDPAIYGPQTNAFVLNHGEVVElvVNNWDAGKHPFHLHGHKFQVVQRSPDVASDDP 101

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 558695371 441 NPP---------RRD-VYPINGGNTTFRFFTDNPGTWFLHCHIDWHLEAGLAIVFAESP 489
Cdd:cd13899  102 NPPinefpenpmRRDtVMVPPGGSVVIRFRADNPGVWFFHCHIEWHLEAGLAATFIEAP 160
CuRO_2_LCC_like cd04205
Cupredoxin domain 2 of laccase-like multicopper oxidases; including laccase, CueO, spore coat ...
 163-309 3.23e-35

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: 129.02  E-value: 3.23e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 558695371 163 VITLGEWYH-----VLAPAGNNDFftsGTVPVQDSGLINGKGRFN-----GGPEVPFAVVNVEKGKRYRFRVIALSCRPF 232
Cdd:cd04205    2 VLLLSDWYHdsaedVLAGYMPNSF---GNEPVPDSLLINGRGRFNcsmavCNSGCPLPVITVEPGKTYRLRLINAGSFAS 78

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 558695371 233 FTFSVDNHNITFMEADGVEHDPVEAQNVDVYAAQRVSVILNANQPIGNYWIRAPPTGGNPANNPNYNpnlTLAILRY 309
Cdd:cd04205   79 FNFAIDGHNMTVIEVDGGYVEPLEVDNLDLAPGQRYDVLVKADQPPGNYWIRASADGRTFDEGGNPN---GTAILRY 152
CuRO_2_MCO_like_1 cd13886
The second cupredoxin domain of uncharacterized multicopper oxidase; Multicopper Oxidases ...
 163-285 3.77e-32

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


Pssm-ID: 259953 [Multi-domain]  Cd Length: 163  Bit Score: 120.84  E-value: 3.77e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 558695371 163 VITLGEWYH-----VLAPAGNNDffTSGTVPVQDSGLINGKGRFNGGPE----------VPFAVVNVEKGKRYRFRVIAL 227
Cdd:cd13886    2 VVMVNDYYHdpssvLLARYLAPG--NEGDEPVPDNGLINGIGQFDCASAtykiyccasnGTYYNFTLEPNKTYRLRLINA 79

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 558695371 228 SCRPFFTFSVDNHNITFMEADGVEHDPVEAQNVDVYAAQRVSVILNANQP-IGNYWIRA 285
Cdd:cd13886   80 GSFADFTFSVDGHPLTVIEADGTLVEPVEVHSITISVAQRYSVILTTNQPtGGNFWMRA 138
CuRO_1_Abr2_like cd13850
The first cupredoxin domain of a group of fungal Laccases similar to Abr2 from Aspergillus ...
 24-144 2.54e-30

The first cupredoxin domain of a group of fungal Laccases similar to Abr2 from Aspergillus fumigatus; Abr2 is involved in conidial pigment biosynthesis in Aspergillus fumigatus. Laccase is a blue multi-copper enzyme that catalyzes the oxidation of a variety aromatic - notably phenolic and inorganic substances coupled to the reduction of molecular oxygen to water. Laccase has been implicated in a wide spectrum of biological activities and, in particular, plays a key role in morphogenesis, development and lignin metabolism in fungi and plants. Like other related multicopper oxidases (MCOs), laccase is composed of three cupredoxin domains that include one mononuclear and one trinuclear copper center. The copper ions are bound in several sites: Type 1, Type 2, and/or Type 3. The ensemble of types 2 and 3 copper is called a trinuclear cluster. MCOs oxidize their substrate by accepting electrons at a mononuclear copper center and transferring them to the active site trinuclear copper center. The cupredoxin domain 1 of 3-domain MCOs contains part the trinuclear copper binding site, which is located at the interface of domains 1 and 3.


Pssm-ID: 259919 [Multi-domain]  Cd Length: 117  Bit Score: 114.32  E-value: 2.54e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 558695371  24 FNFDLVNARLAPDGFERDTVVINGEFPGTLIQVNKGDTVRIPVNNKLTNPlmrrsTSIHWHGFFQARTSAQDGPSFVNQC 103
Cdd:cd13850    1 FTLTVTEGSPDGDGGEREVILINGQFPGPPIILDEGDEVEILVTNNLPVN-----TTIHFHGILQRGTPWSDGVPGVTQW 75

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|.
gi 558695371 104 PQPPNTTFTYEFSVANQTGTYWYHSHLSTQYCDGLRGGFIV 144
Cdd:cd13850   76 PIQPGGSFTYRWKAEDQYGLYWYHSHYRGYYMDGLYGPIYI 116
CuRO_3_tcLLC2_insect_like cd13905
The third cupredoxin domain of the insect laccases similar to laccase 2 in Tribolium castaneum; ...
 366-488 4.53e-28

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: 110.08  E-value: 4.53e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 558695371 366 INGISYISPTVPVLLQilsgakkPEDVLPSEQIFF-------------------IPKNSLIE---VNI-PGAG-AHPFHL 421
Cdd:cd13905    2 INGISFVFPSSPLLSQ-------PEDLSDSSSCDFcnvpskcctepcecthvikLPLNSVVEivlINEgPGPGlSHPFHL 74

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 558695371 422 HGHNFDVV----LASNDDTF--------------------NFKNPPRRDVYPI-NGGNTTFRFFTDNPGTWFLHCHIDWH 476
Cdd:cd13905   75 HGHSFYVLgmgfPGYNSTTGeilsqnwnnklldrgglpgrNLVNPPLKDTVVVpNGGYVVIRFRADNPGYWLLHCHIEFH 154

                        170
                 ....*....|..
gi 558695371 477 LEAGLAIVFAES 488
Cdd:cd13905  155 LLEGMALVLKVG 166
CuRO_1_AAO cd13845
The first cupredoxin domain of plant Ascorbate oxidase; Ascorbate oxidase catalyzes the ...
 34-147 5.03e-28

The first cupredoxin domain of plant Ascorbate oxidase; Ascorbate oxidase catalyzes the oxidation of ascorbic acid to dehydroascorbic acid. This multicopper oxidase (MCO) is found in cucurbitaceous plants such as pumpkin, cucumber, and melon. It can detect levels of ascorbic acid and eliminate it. The biological function of ascorbate oxidase is still not clear. Ascorbate oxidase belongs to MCO family which couple oxidation of substrates with reduction of dioxygen to water. MCOs are capable of oxidizing a vast range of substrates, varying from aromatic compounds to inorganic compounds such as metals. Although the members of this family have diverse functions, majority of them have three cupredoxin domain repeats. The copper ions are bound in several sites: Type 1, Type 2, and/or Type 3. The ensemble of types 2 and 3 copper is called a trinuclear cluster. MCOs oxidize their substrate by accepting electrons at a mononuclear copper center and transferring them to the active site trinuclear copper center. The cupredoxin domain 1 of 3-domain MCOs contains part the trinuclear copper binding site, which is located at the interface of domains 1 and 3.


Pssm-ID: 259914 [Multi-domain]  Cd Length: 120  Bit Score: 108.30  E-value: 5.03e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 558695371  34 APDGFERDTVVINGEFPGTLIQVNKGDTVRIpvnnKLTNPLMRRSTSIHWHGFFQARTSAQDGPSFVNQCPQPPNTTFTY 113
Cdd:cd13845   13 APDCVEKLVIGINGQFPGPTIRATAGDTIVV----ELENKLPTEGVAIHWHGIRQRGTPWADGTASVSQCPINPGETFTY 88

                         90       100       110
                 ....*....|....*....|....*....|....
gi 558695371 114 EFsVANQTGTYWYHSHLSTQYCDGLRGGFIVyDP 147
Cdd:cd13845   89 QF-VVDRPGTYFYHGHYGMQRSAGLYGSLIV-DP 120
PLN02792 PLN02792
oxidoreductase
 19-283 5.17e-28

oxidoreductase


Pssm-ID: 178389 [Multi-domain]  Cd Length: 536  Bit Score: 117.39  E-value: 5.17e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 558695371  19 GATKTFNFDLVNARLAPDGFERDTVVINGEFPGTLIQVNKGDTVRIPVNNKLTNPLMrrstsIHWHGFFQARTSAQDGpS 98
Cdd:PLN02792  14 DDTLFYNWRVTYGNISLLTLPRRGILINGQFPGPEIRSLTNDNLVINVHNDLDEPFL-----LSWNGVHMRKNSYQDG-V 87

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 558695371  99 FVNQCPQPPNTTFTYEFSVANQTGTYWYHSHLSTQYCDGLRGGFIVYD-PNDPLAdlYDVDDENTVITLGEWYHVLAPAG 177
Cdd:PLN02792  88 YGTTCPIPPGKNYTYDFQVKDQVGSYFYFPSLAVQKAAGGYGSLRIYSlPRIPVP--FPEPAGDFTFLIGDWYRRNHTTL 165

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 558695371 178 NNDFFTSGTVPVQDSG-LINGKGRFNggpevpFAVVNVEKGKRYRFRVIALSCRPFFTFSVDNHNITFMEADGVEHDPVE 256
Cdd:PLN02792 166 KKILDGGRKLPLMPDGvMINGQGVSY------VYSITVDKGKTYRFRISNVGLQTSLNFEILGHQLKLIEVEGTHTVQSM 239

                        250       260
                 ....*....|....*....|....*..
gi 558695371 257 AQNVDVYAAQRVSVILNANQPIGNYWI 283
Cdd:PLN02792 240 YTSLDIHVGQTYSVLVTMDQPPQNYSI 266
PLN02354 PLN02354
copper ion binding / oxidoreductase
 1-312 2.75e-27

copper ion binding / oxidoreductase


Pssm-ID: 177987 [Multi-domain]  Cd Length: 552  Bit Score: 115.27  E-value: 2.75e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 558695371   1 MRLSNAFVLAATCISGALGATKTFNFDLVN---ARLAPDGFERDTVVINGEFPGTLIQVNKGDTVRIPVNNKLTNPLMrr 77
Cdd:PLN02354   4 GRLLAVLLCLAAAVALVVRAEDPYFFFTWNvtyGTASPLGVPQQVILINGQFPGPNINSTSNNNIVINVFNNLDEPFL-- 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 558695371  78 stsIHWHGFFQARTSAQDGPSFVNqCPQPPNTTFTYEFSVANQTGTYWYHSHLSTQYCDGLRGGFIVYD------PNDpl 151
Cdd:PLN02354  82 ---LTWSGIQQRKNSWQDGVPGTN-CPIPPGTNFTYHFQPKDQIGSYFYYPSTGMHRAAGGFGGLRVNSrllipvPYA-- 155

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 558695371 152 adlyDVDDENTVItLGEWY---H-VLApagnnDFFTSG-TVPVQDSGLINGKGRFNGGPEVPfaVVNVEKGKRYRFRVIA 226
Cdd:PLN02354 156 ----DPEDDYTVL-IGDWYtksHtALK-----KFLDSGrTLGRPDGVLINGKSGKGDGKDEP--LFTMKPGKTYRYRICN 223

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 558695371 227 LSCRPFFTFSVDNHNITFMEADGvEHdpvEAQNV----DVYAAQRVSVILNANQPIGNYWIRApptggnpANNPNYNPNL 302
Cdd:PLN02354 224 VGLKSSLNFRIQGHKMKLVEMEG-SH---VLQNDydslDVHVGQCFSVLVTANQAPKDYYMVA-------STRFLKKVLT 292

                        330
                 ....*....|
gi 558695371 303 TLAILRYKGA 312
Cdd:PLN02354 293 TTGIIRYEGG 302
PLN02991 PLN02991
oxidoreductase
 22-283 4.14e-27

oxidoreductase


Pssm-ID: 215536 [Multi-domain]  Cd Length: 543  Bit Score: 114.73  E-value: 4.14e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 558695371  22 KTFNFDLVNARLAPDGFERDTVVINGEFPGTLIQVNKGDTVRIPVNNKLTNPLMrrstsIHWHGFFQARTSAQDGpSFVN 101
Cdd:PLN02991  29 RFFEWHVTYGNISPLGVAQQGILINGKFPGPDIISVTNDNLIINVFNHLDEPFL-----ISWSGIRNWRNSYQDG-VYGT 102

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 558695371 102 QCPQPPNTTFTYEFSVANQTGTYWYHSHLSTQYCDGLRGGF-IVYDPNDPLADLYDVDDENTVItlGEWYHVLAPAGNND 180
Cdd:PLN02991 103 TCPIPPGKNYTYALQVKDQIGSFYYFPSLGFHKAAGGFGAIrISSRPLIPVPFPAPADDYTVLI--GDWYKTNHKDLRAQ 180

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 558695371 181 FFTSGTVPVQDSGLINGKGrfNGgpevpfAVVNVEKGKRYRFRVIALSCRPFFTFSVDNHNITFMEADGVEHDPVEAQNV 260
Cdd:PLN02991 181 LDNGGKLPLPDGILINGRG--SG------ATLNIEPGKTYRLRISNVGLQNSLNFRIQNHTMKLVEVEGTHTIQTPFSSL 252

                        250       260
                 ....*....|....*....|...
gi 558695371 261 DVYAAQRVSVILNANQPIGNYWI 283
Cdd:PLN02991 253 DVHVGQSYSVLITADQPAKDYYI 275
CuRO_3_MaLCC_like cd13901
The third cupredoxin domain of the fungal laccases similar to Ma-LCC from Melanocarpus ...
 347-483 1.10e-26

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: 105.77  E-value: 1.10e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 558695371 347 PPDKHITLNIAQPHSPFFD--INGIS-YISPTVPVLLQILSGAKKPEDvlPSEQIFFIPKNS-----LIEVNIPGAgaHP 418
Cdd:cd13901    7 SPTQTLTIDLGPNATGVFLwtLNGSSfRVDWNDPTLLLVADGNTSTFP--PEWNVIELPKANkwvyiVIQNNSPLP--HP 82

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 558695371 419 FHLHGHNFdVVLA-------SNDDTFNFKNPPRRDVY--PINGGnTTFRFFTDNPGTWFLHCHIDWHLEAGLAI 483
Cdd:cd13901   83 IHLHGHDF-YILAqgtgtfdDDGTILNLNNPPRRDVAmlPAGGY-LVIAFKTDNPGAWLMHCHIAWHASGGLAL 154
CuRO_2_MaLCC_like cd13880
The second cupredoxin domain of the fungal laccases similar to Ma-LCC from Melanocarpus ...
 163-319 1.11e-26

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: 105.79  E-value: 1.11e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 558695371 163 VITLGEWYHVLAPAGNNDFFTSGTVPVQDSGLINGKGRFNGGPEVP-FAVVNVEKGKRYRFRVIALSCRPFFTFSVDNHN 241
Cdd:cd13880    3 PVLLTDWYHRSAFELFSEELPTGGPPPMDNILINGKGKFPCSTGAGsYFETTFTPGKKYRLRLINTGVDTTFRFSIDGHN 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 558695371 242 ITFMEADGVehdPVEAQNVDVYA---AQRVSVILNANQ-PIGNYWIRAPPTGGNPANNPNYNPnlTLAILRYKGAADEEP 317
Cdd:cd13880   83 LTVIAADFV---PIVPYTTDSLNigiGQRYDVIVEANQdPVGNYWIRAEPATGCSGTNNNPDN--RTGILRYDGASPTLD 157


                 ..
gi 558695371 318 TT 319
Cdd:cd13880  158 PS 159
PLN02168 PLN02168
copper ion binding / pectinesterase
 9-502 4.42e-26

copper ion binding / pectinesterase


Pssm-ID: 215113 [Multi-domain]  Cd Length: 545  Bit Score: 111.61  E-value: 4.42e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 558695371   9 LAATCISGALGATKTFNFDLVNARLAPDGFERDTVVINGEFPGTLIQVNKGDTVRIPVNNKLTNPLMrrstsIHWHGFFQ 88
Cdd:PLN02168  14 LVILELSYAFAPIVSYQWVVSYSQRFILGGNKQVIVINDMFPGPLLNATANDVINVNIFNNLTEPFL-----MTWNGLQL 88

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 558695371  89 ARTSAQDGPSFVNqCPQPPNTTFTYEFSVANQTGTYWYHSHLSTQYCDGLRGGFIVYDPnDPLADLYDVDDENTVITLGE 168
Cdd:PLN02168  89 RKNSWQDGVRGTN-CPILPGTNWTYRFQVKDQIGSYFYFPSLLLQKAAGGYGAIRIYNP-ELVPVPFPKPDEEYDILIGD 166

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 558695371 169 WYHVLAPAGNNDFFTSGTVPVQDSGLINGKgrfngGPEVPFavVNVEKGKRYRFRVIALSCRPFFTFSVDNHNITFMEAD 248
Cdd:PLN02168 167 WFYADHTVMRASLDNGHSLPNPDGILFNGR-----GPEETF--FAFEPGKTYRLRISNVGLKTCLNFRIQDHDMLLVETE 239

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 558695371 249 GVEHDPVEAQNVDVYAAQRVSVILNA-NQPIG---NYWIRApptggnpANNPNYNPNLTLAILRYKGaADEEPTTVNVPG 324
Cdd:PLN02168 240 GTYVQKRVYSSLDIHVGQSYSVLVTAkTDPVGiyrSYYIVA-------TARFTDAYLGGVALIRYPN-SPLDPVGPLPLA 311

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 558695371 325 HKLLD-----QEMHPIA-----------SEGPGKLGSGPPDKHITLNIAQPHSP---FFDINGISYISPTVPvlLQILSG 385
Cdd:PLN02168 312 PALHDyfssvEQALSIRmdlnvgaarsnPQGSYHYGRINVTRTIILHNDVMLSSgklRYTINGVSFVYPGTP--LKLVDH 389

                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 558695371 386 AKKPEDVLPSeqIFFI-PKN-------SLIEVNI----------PGAGAHPFHLHGHNFDVV-------LASNDDTFNFK 440
Cdd:PLN02168 390 FQLNDTIIPG--MFPVyPSNktptlgtSVVDIHYkdfyhivfqnPLFSLESYHIDGYNFFVVgygfgawSESKKAGYNLV 467

                        490       500       510       520       530       540
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 558695371 441 NPPRRD---VYPIngGNTTFRFFTDNPGTWFLHCHI--DWHLEAGLAI-VFAESPEDNVSGPQSQITP 502
Cdd:PLN02168 468 DAVSRStvqVYPY--SWTAILIAMDNQGMWNVRSQKaeQWYLGQELYMrVKGEGEEDPSTIPVRDENP 533
PLN02835 PLN02835
oxidoreductase
 8-285 1.61e-25

oxidoreductase


Pssm-ID: 178429 [Multi-domain]  Cd Length: 539  Bit Score: 110.06  E-value: 1.61e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 558695371   8 VLAATCISGALGATKTFNFDLVNARLAPDGFERDTVVINGEFPGTLIQVNKGDTVRIPVNNKLTNPLMrrstsIHWHGFF 87
Cdd:PLN02835  16 VLSSVSLVNGEDPYKYYTWTVTYGTISPLGVPQQVILINGQFPGPRLDVVTNDNIILNLINKLDQPFL-----LTWNGIK 90

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 558695371  88 QARTSAQDGPSFVNqCPQPPNTTFTYEFSVANQTGTYWYHSHLSTQYCDGLRGGFIVYD-PNDPLAdlYDVDDENTVITL 166
Cdd:PLN02835  91 QRKNSWQDGVLGTN-CPIPPNSNYTYKFQTKDQIGTFTYFPSTLFHKAAGGFGAINVYErPRIPIP--FPLPDGDFTLLV 167

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 558695371 167 GEWYHVLAPAGNNDFFTSGTVPVQDSGLINGK--GRFNGgpevpfavvnvEKGKRYRFRVIALSCRPFFTFSVDNHNITF 244
Cdd:PLN02835 168 GDWYKTSHKTLQQRLDSGKVLPFPDGVLINGQtqSTFSG-----------DQGKTYMFRISNVGLSTSLNFRIQGHTMKL 236

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|.
gi 558695371 245 MEADGVEHDPVEAQNVDVYAAQRVSVILNANQPIGNYWIRA 285
Cdd:PLN02835 237 VEVEGSHTIQNIYDSLDVHVGQSVAVLVTLNQSPKDYYIVA 277
CuRO_3_MCO_like_4 cd13910
The third cupredoxin domain of uncharacterized multicopper oxidase; Multicopper Oxidases (MCOs) ...
 366-487 2.35e-25

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


Pssm-ID: 259977 [Multi-domain]  Cd Length: 166  Bit Score: 102.37  E-value: 2.35e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 558695371 366 INGISYIS-PTVPVLLQILSGAKKPEDVLPSEQIFFiPKNSLIeVNIPGA-------------GAHPFHLHGHNFDVVLA 431
Cdd:cd13910   20 FNGTSWRPlPGPATLLLALDADNAEEVAAGNGLSTF-DGNQLV-ITVDDIdkvvdlvinnlddGDHPFHLHGHKFWVLGS 97

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 558695371 432 SN------------DDTFNFKNPPRRDVYPING-GNTTFRFFTDNPGTWFLHCHIDWHLEAGLAIVFAE 487
Cdd:cd13910   98 GDgryggggytapdGTSLNTTNPLRRDTVSVPGfGWAVLRFVADNPGLWAFHCHILWHMAAGMLMQFAV 166
CuRO_1_2dMco_1 cd13860
The first cupredoxin domain of bacteria two domain multicopper oxidase; This subfamily ...
 46-144 6.19e-25

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: 99.58  E-value: 6.19e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 558695371  46 NGEFPGTLIQVNKGDTVRIPVNNKLTNPlmrrsTSIHWHGFfqARTSAQDGPSFVNQCPQPPNTTFTYEFsVANQTGTYW 125
Cdd:cd13860   26 NGSVPGPTIEVTEGDRVRILVTNELPEP-----TTVHWHGL--PVPNGMDGVPGITQPPIQPGETFTYEF-TAKQAGTYM 97

                         90       100
                 ....*....|....*....|.
gi 558695371 126 YHSHLSTQYCD--GLRGGFIV 144
Cdd:cd13860   98 YHSHVDEAKQEdmGLYGAFIV 118
CuRO_1_LCC_plant cd13849
The first cupredoxin domain of plant laccases; Laccase is a blue multicopper oxidase (MCO) ...
 24-146 1.47e-24

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: 98.49  E-value: 1.47e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 558695371  24 FNFDLVNARLAPDGFERDTVVINGEFPGTLIQVNKGDTVRIPVNNKLTNPLmrrstSIHWHGFFQARTSAQDGPSFVNQC 103
Cdd:cd13849    1 YTFVVQEKNVTRLCSTKSILTVNGQFPGPTIRVHEGDTVVVNVTNRSPYNI-----TIHWHGIRQLRSGWADGPAYITQC 75

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*..
gi 558695371 104 PQPPNTTFTYEFSVANQTGTYWYHSHLS----TQYcdglrGGFIVYD 146
Cdd:cd13849   76 PIQPGQSYTYRFTVTGQEGTLWWHAHISwlraTVY-----GAFIIRP 117
CuRO_3_LCC_like cd04207
Cupredoxin domain 3 of laccase-like multicopper oxidases; including laccase, CueO, spore coat ...
 349-486 1.64e-24

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: 98.69  E-value: 1.64e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 558695371 349 DKHITLNIAQPHSPFFD----INGISYisptvpvllqilsgakkpEDVLPSEQIFFIPKNSLIEVNIPGAGA----HPFH 420
Cdd:cd04207    1 DRTRRLVLSQTGAPDGTtrwvINGMPF------------------KEGDANTDIFSVEAGDVVEIVLINAGNhdmqHPFH 62

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 558695371 421 LHGHNFDVV---LASNDDTFNFKNPPRRDVYPIN-GGNTTFRFFTDNPGTWFLHCHIDWHLEAGLAIVFA 486
Cdd:cd04207   63 LHGHSFWVLgsgGGPFDAPLNLTNPPWRDTVLVPpGGWVVIRFKADNPGVWMLHCHILEHEDAGMMTVFE 132
CuRO_1_CopA cd13848
The first cupredoxin domain of CopA copper resistance protein family; CopA is a multicopper ...
 36-144 5.20e-24

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: 96.58  E-value: 5.20e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 558695371  36 DGFERDTVVINGEFPGTLIQVNKGDTVRIPVNNKLTNPlmrrsTSIHWHGFFQARTsaQDGPSFVNQCPQPPNTTFTYEF 115
Cdd:cd13848   15 GGKEGEAITVNGQVPGPLLRFKEGDDATIRVHNRLDED-----TSIHWHGLLLPND--MDGVPGLSFPGIKPGETFTYRF 87

                         90       100
                 ....*....|....*....|....*....
gi 558695371 116 SVAnQTGTYWYHSHLSTQYCDGLRGGFIV 144
Cdd:cd13848   88 PVR-QSGTYWYHSHSGLQEQTGLYGPIII 115
copper_res_A TIGR01480
copper-resistance protein, CopA family; This model represents the CopA copper resistance ...
 36-481 6.37e-24

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


Pssm-ID: 273649 [Multi-domain]  Cd Length: 587  Bit Score: 105.35  E-value: 6.37e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 558695371   36 DGFERDTVVINGEFPGTLIQVNKGDTVRIPVNNKLtnPLMrrsTSIHWHGFFQArtSAQDGPSFVNQCPQPPNTTFTYEF 115
Cdd:TIGR01480  60 TGRARPAITVNGSIPGPLLRWREGDTVRLRVTNTL--PED---TSIHWHGILLP--FQMDGVPGVSFAGIAPGETFTYRF 132

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 558695371  116 SVaNQTGTYWYHSHLSTQYCDGLRGGFIVyDPNDPlaDLYDVDDENTVItLGEW-----------YHVLAPAGNN----- 179
Cdd:TIGR01480 133 PV-RQSGTYWYHSHSGFQEQAGLYGPLII-DPAEP--DPVRADREHVVL-LSDWtdldpaalfrkLKVMAGHDNYykrtv 207

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 558695371  180 -DFFTSGTVPVQDSGLINGK--GRFNGGPeVPFAVVN--------------------VEKGKRYRFRVIALSCRPFFTFS 236
Cdd:TIGR01480 208 aDFFRDVRNDGLKQTLADRKmwGQMRMTP-TDLADVNgstytylmngttpagnwtglFRPGEKVRLRFINGSAMTYFDVR 286

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 558695371  237 VDNHNITFMEADGVEHDPVEAQNVDVYAAQRVSVILnanQPIGN--YWIRAPPTG--GNPANNPNYNPNLTLAIlrykGA 312
Cdd:TIGR01480 287 IPGLKLTVVAVDGQYVHPVSVDEFRIAPAETFDVIV---EPTGDdaFTIFAQDSDrtGYARGTLAVRLGLTAPV----PA 359

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 558695371  313 ADEEP-TTVNVPGHKLLDQEMHPIASEGPGKLG--------SGPPDKH--ITLNIAQPHSPFFDIN-GISYISPTVPVLL 380
Cdd:TIGR01480 360 LDPRPlLTMKDMGMGGMHHGMDHSKMSMGGMPGmdmsmraqSNAPMDHsqMAMDASPKHPASEPLNpLVDMIVDMPMDRM 439

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 558695371  381 ----QILSGAKKPEDVLPSEQIFFIPKNSL-----IEVNIPG------------------------------------AG 415
Cdd:TIGR01480 440 ddpgIGLRDNGRRVLTYADLHSLFPPPDGRapgreIELHLTGnmerfawsfdgeafglktplrfnygerlrvvlvndtMM 519

                         490       500       510       520       530       540
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 558695371  416 AHPFHLHGHNFDVVlasnDDTFNFKnpPRRDVYPIN-GGNTTFRFFTDNPGTWFLHCHIDWHLEAGL 481
Cdd:TIGR01480 520 AHPIHLHGMWSELE----DGQGEFQ--VRKHTVDVPpGGKRSFRVTADALGRWAYHCHMLLHMEAGM 580
CuRO_3_AAO cd13893
The third cupredoxin domain of plant Ascorbate oxidase; Ascorbate oxidase catalyzes the ...
 348-490 1.31e-23

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: 97.11  E-value: 1.31e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 558695371 348 PDKHITLNIAQPHSPFF---DINGISYISPTVPVLLQILSGAKKPEDVLpseQIFFIPKNSLIEVNipgAGAHPFHLHGH 424
Cdd:cd13893    1 ATRTLLLLNTQNLINGQlrwAINNVSYVPPPTPYLAALPVYPFKGGDVV---DVILQNANTNTRNA---SEQHPWHLHGH 74

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 558695371 425 NFDVVL--------ASNDDTFNFKNPPRRDVYPI-NGGNTTFRFFTDNPGTWFLHCHIDWHLEAGLAIVFAESPE 490
Cdd:cd13893   75 DFWVLGyglggfdpAADPSSLNLVNPPMRNTVTIfPYGWTALRFKADNPGVWAFHCHIEWHFHMGMGVVFAEGVE 149
PLN00044 PLN00044
multi-copper oxidase-related protein; Provisional
 39-494 5.36e-22

multi-copper oxidase-related protein; Provisional


Pssm-ID: 165622 [Multi-domain]  Cd Length: 596  Bit Score: 99.74  E-value: 5.36e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 558695371  39 ERDTVVINGEFPGTLIQVNKGDTVRIPVNNKLTNPLMrrstsIHWHGFFQARTSAQDGPSFVNqCPQPPNTTFTYEFSVA 118
Cdd:PLN00044  47 KQEAIGINGQFPGPALNVTTNWNLVVNVRNALDEPLL-----LTWHGVQQRKSAWQDGVGGTN-CAIPAGWNWTYQFQVK 120

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 558695371 119 NQTGTYWYHSHLSTQYCDGLRGGFIVYDPND-----PLADLYDVddentVITLGEWYHVLAPAGNNDFFTSGTVPVQDSG 193
Cdd:PLN00044 121 DQVGSFFYAPSTALHRAAGGYGAITINNRDVipipfGFPDGGDI-----TLFIADWYARDHRALRRALDAGDLLGAPDGV 195

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 558695371 194 LINGKG--RFNGG---PEVPFAVVNVEKGKRYRFRVIALSCRPFFTFSVDNHNITFMEADGVEHDPVEAQNVDVYAAQRV 268
Cdd:PLN00044 196 LINAFGpyQYNDSlvpPGITYERINVDPGKTYRFRVHNVGVATSLNFRIQGHNLLLVEAEGSYTSQQNYTNLDIHVGQSY 275

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 558695371 269 SVILNANQPIG-NYWIRApptgGNPANNPNYNPNLT-LAILRYKGAADEEPTTVNVPGHKLLDQEMH---------PIAS 337
Cdd:PLN00044 276 SFLLTMDQNAStDYYVVA----SARFVDAAVVDKLTgVAILHYSNSQGPASGPLPDAPDDQYDTAFSinqarsirwNVTA 351

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 558695371 338 EG--PGKLGS-GPPDKHIT-LNIAQPHSPFF-------DINGISYISPTVPVLL-QILSGAKKPEDVLPSEQIFFIPK-- 403
Cdd:PLN00044 352 SGarPNPQGSfHYGDITVTdVYLLQSMAPELidgklraTLNEISYIAPSTPLMLaQIFNVPGVFKLDFPNHPMNRLPKld 431

                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 558695371 404 NSLIEVNIPG----------AGAHPFHLHGHNFDVV-------LASNDDTFN-FKNPPRRDVYPINGGNTTFRFFTDNPG 465
Cdd:PLN00044 432 TSIINGTYKGfmeiifqnnaTNVQSYHLDGYAFFVVgmdyglwTDNSRGTYNkWDGVARSTIQVFPGAWTAILVFLDNAG 511

                        490       500       510
                 ....*....|....*....|....*....|...
gi 558695371 466 TWFLHC-HID-WHL--EAGLAIVfaeSPEDNVS 494
Cdd:PLN00044 512 IWNLRVeNLDaWYLgqEVYINVV---NPEDNSN 541
CuRO_2_Diphenol_Ox cd13883
The second cupredoxin domain of fungal laccase, diphenol oxidase; Diphenol oxidase belongs to ...
 163-310 7.87e-22

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: 92.40  E-value: 7.87e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 558695371 163 VITLGEWYH---------VLAPAGnndFFTSGTVPVQDSGLINGKGRFN--------GGPEVPFAVVNVEKGKRYRFRVI 225
Cdd:cd13883    2 VLFISDWYHdqsevivagLLSPQG---YKGSPAAPSPDSALINGIGQFNcsaadpgtCCTQTSPPEIQVEAGKRTRFRLI 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 558695371 226 ALSCRPFFTFSVDNHNITFMEADGVE-HDPVEAQNVDVYAAQRVSVILNANQP-IGN-YWIRAppTGGNPANNPNYNPNL 302
Cdd:cd13883   79 NAGSHAMFRFSVDNHTLNVVEADDTPvYGPTVVHRIPIHNGQRYSVIIDTTSGkAGDsFWLRA--RMATDCFAWDLQQQT 156


                 ....*...
gi 558695371 303 TLAILRYK 310
Cdd:cd13883  157 GKAILRYV 164
CuRO_1_CumA_like cd13861
The first cupredoxin domain of CumA like multicopper oxidase; This multicopper oxidase (MCO) ...
 31-144 1.14e-21

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: 90.37  E-value: 1.14e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 558695371  31 ARLAPDGFERDTVVINGEFPGTLIQVNKGDTVRIPVNNKLTNPlmrrsTSIHWHGFfqARTSAQDGPSFVNQCPQPPNTT 110
Cdd:cd13861   11 ELLDLGGPTTRTWGYNGQVPGPELRVRQGDTLRVRLTNRLPEP-----TTIHWHGL--RLPNAMDGVPGLTQPPVPPGES 83

                         90       100       110
                 ....*....|....*....|....*....|....*.
gi 558695371 111 FTYEFSVANqTGTYWYHSHLSTQYC--DGLRGGFIV 144
Cdd:cd13861   84 FTYEFTPPD-AGTYWYHPHVGSQEQldRGLYGPLIV 118
CuRO_3_Diphenol_Ox cd13904
The third cupredoxin domain of fungal laccase, diphenol oxidase; Diphenol oxidase belongs to ...
 364-486 2.62e-21

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: 90.43  E-value: 2.62e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 558695371 364 FDINGISYIS-PTVPVLLQILSGAKKPED-------VLPSEQIFfipknSLIEVNIPGAGAHPFHLHGHNFDVV------ 429
Cdd:cd13904   22 FFVNNVTWTNyIYQPLLHQVASGGGGTLNssevasvTFPTDGWY-----DIVINNLDPAIDHPYHLHGVDFHIVargsgt 96

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 558695371 430 --LASNDD-TFNFKNPPRRDVYPINGGN-TTFRFFTDNPGTWFLHCHIDWHLEAGLAIVFA 486
Cdd:cd13904   97 ltLEQLANvQYNTTNPLRRDTIVIPGGSwAVLRIPADNPGVWALHCHIGWHLAAGFAGVVV 157
CuRO_3_LCC_plant cd13897
The third cupredoxin domain of the plant laccases; Laccase is a blue multicopper oxidase (MCO) ...
 401-485 3.36e-20

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: 86.93  E-value: 3.36e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 558695371 401 IPKNSLIEV-----NIPGAGAHPFHLHGHNFDVV--------LASNDDTFNFKNPPRRDVYPI-NGGNTTFRFFTDNPGT 466
Cdd:cd13897   36 LEYGSTVEIvlqgtSLLAAENHPMHLHGFDFYVVgrgfgnfdPSTDPATFNLVDPPLRNTVGVpRGGWAAIRFVADNPGV 115

                         90
                 ....*....|....*....
gi 558695371 467 WFLHCHIDWHLEAGLAIVF 485
Cdd:cd13897  116 WFMHCHFERHTSWGMATVF 134
CuRO_D1_2dMcoN_like cd13859
The first cupredoxin domain of bacterial two domain multicopper oxidase McoN and similar ...
 27-140 3.40e-20

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


Pssm-ID: 259928 [Multi-domain]  Cd Length: 122  Bit Score: 86.38  E-value: 3.40e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 558695371  27 DLVNARLAPDgFERDTVVINGEFPGTLIQVNKGDTVRIPVNNKLTNPlmrrsTSIHWHGFFQARTSAQDGPSFVNQCPQP 106
Cdd:cd13859    8 DETVITVVPG-LDFKTFAFNGQVPGPLIHVKEGDDLVVHVTNNTTLP-----HTIHWHGVLQMGSWKMDGVPGVTQPAIE 81

                         90       100       110
                 ....*....|....*....|....*....|....
gi 558695371 107 PNTTFTYEFSvANQTGTYWYHSHLSTQYCDGLRG 140
Cdd:cd13859   82 PGESFTYKFK-AERPGTLWYHCHVNVNEHVGMRG 114
CuRO_1_AAO_like_2 cd13847
The first cupredoxin domain of Ascorbate oxidase homologs; This family includes fungal ...
 32-146 7.39e-20

The first cupredoxin domain of Ascorbate oxidase homologs; This family includes fungal proteins with similarity to ascorbate oxidase. Ascorbate oxidase catalyzes the oxidation of ascorbic acid to dehydroascorbic acid. It can detect levels of ascorbic acid and eliminate it. The biological function of ascorbate oxidase is still not clear. Ascorbate oxidase belongs to multicopper oxidase (MCO) family which couple oxidation of substrates with reduction of dioxygen to water. MCOs are capable of oxidizing a vast range of substrates, varying from aromatic compounds to inorganic compounds such as metals. Although the members of this family have diverse functions, majority of them have three cupredoxin domain repeats. The copper ions are bound in several sites: Type 1, Type 2, and/or Type 3. The ensemble of types 2 and 3 copper is called a trinuclear cluster. MCOs oxidize their substrate by accepting electrons at a mononuclear copper center and transferring them to the active site trinuclear copper center. The cupredoxin domain 1 of 3-domain MCOs contains part the trinuclear copper binding site, which is located at the interface of domains 1 and 3.


Pssm-ID: 259916 [Multi-domain]  Cd Length: 117  Bit Score: 85.27  E-value: 7.39e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 558695371  32 RLAPDGF-ERDTVVINGEFPGTLIQVNKGDTVRIPVNNKLTNplmrRSTSIHWHGFFQARTSAQDGPSFVNQCPQPPNTT 110
Cdd:cd13847    6 RVSCDPFgPRPSTLINGSFPGPELRVQEGQHLWVRVYNDLEA----GNTTMHFHGLSQYMSPFSDGTPLASQWPIPPGKF 81

                         90       100       110
                 ....*....|....*....|....*....|....*..
gi 558695371 111 FTYEFSV-ANQTGTYWYHSHLSTQYCDGlRGGFIVYD 146
Cdd:cd13847   82 FDYEFPLeAGDAGTYYYHSHVGFQSVTA-YGALIVED 117
CuRO_1_MCO_like_2 cd13864
The second cupredoxin domain of uncharacterized multicopper oxidase; Multicopper Oxidases ...
 51-144 5.30e-19

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


Pssm-ID: 259932 [Multi-domain]  Cd Length: 139  Bit Score: 83.35  E-value: 5.30e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 558695371  51 GTLIQVNKGDTVRIPVNNKLTNPLMRR-------STSIHWHGFFQARTSAQ-----DGPSFVNQCPQPPNTTFTYEFSVA 118
Cdd:cd13864   31 GPTIRVKSGDTLNLLVTNHLCNEQELSkiwqdycPTSIHFHGLVLENFGKQlanlvDGVPGLTQYPIGVGESYWYNFTIP 110

                         90       100
                 ....*....|....*....|....*..
gi 558695371 119 NQT-GTYWYHSHLSTQYCDGLRGGFIV 144
Cdd:cd13864  111 EDTcGTFWYHSHSSVQYGDGLRGVFIV 137
CuRO_1_AAO_like_1 cd13846
The first cupredoxin domain of plant Ascorbate oxidase homologs; This subfamily is composed of ...
 22-144 1.03e-18

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: 81.68  E-value: 1.03e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 558695371  22 KTFNFDLVNARLAPDGFERDTVVINGEFPGTLIQVNKGDTVRIPVNNKLTNPLMrrstsIHWHGFFQARTSAQDGPSFVN 101
Cdd:cd13846    1 SFFDWNVSYITASPLGVPQQVIAINGQFPGPTINVTTNDNVVVNVFNSLDEPLL-----LTWNGIQQRRNSWQDGVLGTN 75

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|...
gi 558695371 102 qCPQPPNTTFTYEFSVANQTGTYWYHSHLSTQYCDGLRGGFIV 144
Cdd:cd13846   76 -CPIPPGWNWTYKFQVKDQIGSFFYFPSLHFQRAAGGFGGIRV 117
CuRO_2_Fet3p_like cd13877
The second Cupredoxin domain of multicopper oxidase Fet3P; Fet3p catalyzes the ferroxidase ...
 163-281 1.07e-18

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: 82.60  E-value: 1.07e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 558695371 163 VITLGEWYHVLAPAGNNDFFTS----GTVPVQDSGLINGKGRFNggpevpfavVNVEKGKRYRFRVI---ALSCrpfFTF 235
Cdd:cd13877    4 TLTLSDWYHDQSPDLLRDFLSPynptGAEPIPDSSLFNDTQNAT---------INFEPGKTYLLRIInmgAFAS---QYF 71

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*..
gi 558695371 236 SVDNHNITFMEADGVEHDPVEAQNVDVYAAQRVSVILNA-NQPIGNY 281
Cdd:cd13877   72 HIEGHDMTIIEVDGVYVKPYPVDTLYIAVGQRYSVLVKAkNDTDRNY 118
CuRO_1_LCC_like_3 cd13865
The second cupredoxin domain of uncharacterized multicopper oxidase; Multicopper Oxidases ...
 45-146 8.12e-18

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: 79.28  E-value: 8.12e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 558695371  45 INGEFPGTLIQVNKGDTVRIPVNNKLTNPlmrrsTSIHWHGffQARTSAQDGPSFVNQCPQPPNTTFTYEFSVaNQTGTY 124
Cdd:cd13865   22 IRQPDGTEGLRLTEGDRFDVELENRLDEP-----TTIHWHG--LIPPNLQDGVPDVTQPPIPPGQSQRYDFPL-VQPGTF 93

                         90       100
                 ....*....|....*....|..
gi 558695371 125 WYHSHLSTQYCDGLRGGFIVYD 146
Cdd:cd13865   94 WMHSHYGLQEQKLLAAPLIIRS 115
CuRO_3_Abr2_like cd13898
The third cupredoxin domain of a group of fungal Laccases similar to Abr2 from Aspergillus ...
 349-487 2.32e-17

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: 79.61  E-value: 2.32e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 558695371 349 DKHITLNIAQPHSPF-FDINGISYISPT---VPVLLQILSgakkPEDVLPSEQIFFIPKNS----LIEVNIPGAGAHPFH 420
Cdd:cd13898    1 DQTLILTLGRVGSAYsWTLNGTELYPLDeeaYPPLLFLPD----PATALDSALTISTKNGTwvdlIFQVTGPPQPPHPIH 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 558695371 421 LHGHNFDVV---------------LASNDDTFNFKNPPRRDVYPINGGNTT-----FRFFTDNPGTWFLHCHIDWHLEAG 480
Cdd:cd13898   77 KHGNKAFVIgtgtgpfnwssvaeaAEAAPENFNLVNPPLRDTFTTPPSTEGpswlvIRYHVVNPGAWLLHCHIQSHLAGG 156


                 ....*..
gi 558695371 481 LAIVFAE 487
Cdd:cd13898  157 MAVVLLD 163
CuRO_3_CopA cd13896
The third cupredoxin domain of CopA copper resistance protein family; CopA is a multicopper ...
 416-485 1.34e-16

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: 75.76  E-value: 1.34e-16
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 558695371 416 AHPFHLHGHNFDVVlasNDDTFNfknPPRRDVYPINGGNT-TFRFFTDNPGTWFLHCHIDWHLEAGLAIVF 485
Cdd:cd13896   49 AHPMHLHGHFFQVE---NGNGEY---GPRKDTVLVPPGETvSVDFDADNPGRWAFHCHNLYHMEAGMMRVV 113
CuRO_1_McoP_like cd13852
The first cupredoxin domain of multicopper oxidase McoP and similar proteins; This family ...
 45-147 1.36e-16

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: 75.79  E-value: 1.36e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 558695371  45 INGEFPGTLIQVNKGDTVRIPVNNKLTNPlmrrsTSIHWHGFFQArtSAQDG-PSFVnqcpQPPNTTFTYEFSVANQTGT 123
Cdd:cd13852   18 LPDSYLGPILRLRKGQKVRITFKNNLPEP-----TIIHWHGLHVP--AAMDGhPRYA----IDPGETYVYEFEVLNRAGT 86

                         90       100
                 ....*....|....*....|....*...
gi 558695371 124 YWYHSH----LSTQYCDGLRGGFIVYDP 147
Cdd:cd13852   87 YWYHPHphglTAKQVYRGLAGLFLVTDE 114
CuRO_2_AAO cd13871
The second cupredoxin domain of plant Ascorbate oxidase; Ascorbate oxidase catalyzes the ...
 192-309 1.56e-16

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: 77.20  E-value: 1.56e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 558695371 192 SGLINGKGRFN------GGPEVPFAVVN------------VEKGKRYRFRVIALSCRPFFTFSVDNHNITFMEADGVEHD 253
Cdd:cd13871   36 SLLIEGRGRYNcslapaYPSSLPSPVCNksnpqcapfilhVSPGKTYRLRIASVTALSSLNFIIEGHNLTVVEADGNYVQ 115

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 558695371 254 PVEAQNVDVYAAQRVSVILNANQ-PIGNYWI------RAP--PTGgnpannpnynpnltLAILRY 309
Cdd:cd13871  116 PFEVSNLDIYSGETYSVLVTADQdPSRNYWVsvnvrgRRPntPPG--------------LAILNY 166
CuRO_1_CueO_FtsP cd04232
The first Cupredoxin domain of the multicopper oxidase CueO, the cell division protein FtsP, ...
 41-146 2.98e-15

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: 72.22  E-value: 2.98e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 558695371  41 DTVVINGEFPGTLIQVNKGDTVRIPVNNKLTnplmrRSTSIHWHGFfQARTSAQDGPsfvnQCPQPPNTTFTYEFSVANQ 120
Cdd:cd04232   21 ATWGYNGSYLGPTIRVKKGDTVRINVTNNLD-----EETTVHWHGL-HVPGEMDGGP----HQPIAPGQTWSPTFTIDQP 90

                         90       100       110
                 ....*....|....*....|....*....|
gi 558695371 121 TGTYWYHSHL--ST--QYCDGLRGGFIVYD 146
Cdd:cd04232   91 AATLWYHPHThgKTaeQVYRGLAGLFIIED 120
CuRO_2_LCC_plant cd13875
The second cupredoxin domain of the plant laccases; Laccase is a blue multi-copper enzyme that ...
 163-309 2.23e-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: 70.32  E-value: 2.23e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 558695371 163 VITLGEWYHVLAPAGNNDFFTSGTVP-VQDSGLINGK-GRFNGGPEVPFAVVNVEKGKRYRFRVI--ALSCRPFFTfsVD 238
Cdd:cd13875    2 PIILGEWWNRDVNDVEDQALLTGGGPnISDAYTINGQpGDLYNCSSKDTFVLTVEPGKTYLLRIInaALNEELFFK--IA 79

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 558695371 239 NHNITFMEADGVEHDPVEAQNVDVYAAQRVSVILNANQPIGNYWIRAPPTggNPANNPNYNPNLTLAILRY 309
Cdd:cd13875   80 NHTLTVVAVDASYTKPFTTDYILIAPGQTTDVLLTADQPPGRYYMAARPY--QSAPPVPFDNTTATAILEY 148
CuRO_1_McoC_like cd13855
The first cupredoxin domain of a multicopper oxidase McoC and similar proteins; This family ...
 46-144 3.55e-14

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: 69.04  E-value: 3.55e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 558695371  46 NGEFPGTLIQVNKGDTVRIPVNNKLTNPlmrrsTSIHWHGFFQArtSAQDG-PSfvnqCPQPPNTTFTYEFSV-ANQTGT 123
Cdd:cd13855   27 NGSVPGPLIEVFEGDTVEITFRNRLPEP-----TTVHWHGLPVP--PDQDGnPH----DPVAPGNDRVYRFTLpQDSAGT 95

                         90       100
                 ....*....|....*....|....*
gi 558695371 124 YWYHSH----LSTQYCDGLRGGFIV 144
Cdd:cd13855   96 YWYHPHphghTAEQVYRGLAGAFVV 120
CuRO_2_Abr2_like cd13876
The second cupredoxin domain of a group of fungal Laccases similar to Abr2 from Aspergillus ...
 163-310 4.77e-13

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: 66.46  E-value: 4.77e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 558695371 163 VITLGEWYHVLAPAGNNDFFTSGTVPV-QDSGLINGKGRfnggpeVPFAVVNVEKGKRYR-FRVIALSCRPFFTFSVDNH 240
Cdd:cd13876    2 PIILSDWRHLTSEEYWKIMRASGIEPFcYDSILINGKGR------VYCLIVIVDPGERWVsLNFINAGGFHTLAFSIDEH 75

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 558695371 241 NITFMEADGVEHDPVEAQNVDVYAAQRVSVILNANQPIGNYWIRAPPTGGNPANNpnynpnlTLAILRYK 310
Cdd:cd13876   76 PMWVYAVDGGYIEPQLVDAISITNGERYSVLVKLDKPPGDYTIRVASTGAPQVIS-------GYAILRYK 138
CuRO_1_Tth-MCO_like cd13853
The first cupredoxin domain of the bacterial laccases similar to Tth-MCO from Thermus ...
 23-144 2.79e-12

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


Pssm-ID: 259922 [Multi-domain]  Cd Length: 139  Bit Score: 64.20  E-value: 2.79e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 558695371  23 TFNFDLVNARLAPDGFERDTvvINGEFPGTLIQVNKGDTVRIPVNNKLTNPLMRR------------STSIHWHGFFQAR 90
Cdd:cd13853    5 TLTVEYGRVTLAGLPVTLRT--YNGSIPGPTLRVRPGDTLRITLKNDLPPEGAANeapapntphcpnTTNLHFHGLHVSP 82

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 558695371  91 TSAQDGPsFVNqcpQPPNTTFTYEFSVANQ--TGTYWYHSHL----STQYCDGLRGGFIV 144
Cdd:cd13853   83 TGNSDNV-FLT---IAPGESFTYEYDIPADhpPGTYWYHPHLhgstALQVAGGMAGALVV 138
CuRO_1_2DMCO_NIR_like cd11024
The cupredoxin domain 1 of a two-domain laccase related to nitrite reductase; The two-domain ...
 46-148 1.04e-11

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: 61.90  E-value: 1.04e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 558695371  46 NGEFPGTLIQVNKGDTVRIPVNNKLTNPlmrrsTSIHWHGffqARTSAQDGPSFVnqcPQPPNTTFTYEFsVANQTGTYW 125
Cdd:cd11024   27 NGTVPGPTLRATEGDLVRIHFINTGDHP-----HTIHFHG---IHDAAMDGTGLG---PIMPGESFTYEF-VAEPAGTHL 94

                         90       100
                 ....*....|....*....|....*.
gi 558695371 126 YHSH---LSTQYCDGLRGGFIVyDPN 148
Cdd:cd11024   95 YHCHvqpLKEHIAMGLYGAFIV-DPK 119
CuRO_3_MCO_like_3 cd13909
The third cupredoxin domain of uncharacterized multicopper oxidase; Multicopper Oxidases (MCOs) ...
 416-481 2.11e-11

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


Pssm-ID: 259976 [Multi-domain]  Cd Length: 137  Bit Score: 61.77  E-value: 2.11e-11
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 558695371 416 AHPFHLHGHNFDVVLAsnddtfNFKNPPRRDVYPINGGNTT-FRFFTDNPGTWFLHCHIDWHLEAGL 481
Cdd:cd13909   70 PHGMHLHGHHFRAILP------NGALGPWRDTLLMDRGETReIAFVADNPGDWLLHCHMLEHAAAGM 130
CuRO_3_CumA_like cd13906
The third cupredoxin domain of CumA like multicopper oxidase; This multicopper oxidase (MCO) ...
 417-485 5.88e-11

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


Pssm-ID: 259973 [Multi-domain]  Cd Length: 138  Bit Score: 60.48  E-value: 5.88e-11
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 558695371 417 HPFHLHGHNFdVVLASNDDTFNFknPPRRDVYPINGGNTT-FRFFTDNPGTWFLHCHIDWHLEAGLAIVF 485
Cdd:cd13906   69 HPMHLHGHFF-RVLSRNGRPVPE--PFWRDTVLLGPKETVdIAFVADNPGDWMFHCHILEHQETGMMGVI 135
PRK10965 PRK10965
multicopper oxidase; Provisional
 45-159 1.14e-10

multicopper oxidase; Provisional


Pssm-ID: 236810 [Multi-domain]  Cd Length: 523  Bit Score: 63.89  E-value: 1.14e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 558695371  45 INGEFPGTLIQVNKGDTVRIPVNNKLTNPlmrrsTSIHWHGFFQartsaqdgPSFVNQCPQ---PPNTTFTYEFSVANQT 121
Cdd:PRK10965  70 YNGNLLGPAVRLQRGKAVTVDITNQLPEE-----TTLHWHGLEV--------PGEVDGGPQgiiAPGGKRTVTFTVDQPA 136

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*
gi 558695371 122 GTYWYHSHL----STQYCDGLRGGFIVYDPND---PLADLYDVDD 159
Cdd:PRK10965 137 ATCWFHPHQhgktGRQVAMGLAGLVLIEDDESlklGLPKQWGVDD 181
CuRO_2_AAO_like_1 cd13872
The second cupredoxin domain of plant pollen multicopper oxidase homologous to ascorbate ...
 159-287 5.66e-10

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: 57.41  E-value: 5.66e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 558695371 159 DENTVItLGEWYHVLAPAGNNDFFTSGTVPVQDSGLINGKGRFNGGpeVPFAVVNVEKGKRYRFRVIALSCRPFFTFSVD 238
Cdd:cd13872    1 DEYTVL-IGDWYKTDHKTLRQSLDKGRTLGRPDGILINGKGPYGYG--ANETSFTVEPGKTYRLRISNVGLRTSLNFRIQ 77

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|...
gi 558695371 239 NHNITFMEADGvehdPVEAQNV----DVYAAQRVSVILNANQPIGNYWIRAPP 287
Cdd:cd13872   78 GHKMLLVETEG----SYTAQNTydslDVHVGQSYSVLVTADQSPKDYYIVASS 126
CuRO_2_AAO_like_2 cd13873
The second cupredoxin domain of plant Ascorbate oxidase homologs; This family includes plant ...
 151-284 6.71e-10

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: 58.07  E-value: 6.71e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 558695371 151 LADLYDVDDENTVITLgewyhVLAPagnndFFTSGTVpvqDSGLINGKGRFNGGPEVPF--------AVVNVEKGKRYRF 222
Cdd:cd13873    7 FSDYFPKTDSTIETGL-----TATP-----FVWPGEP---NALLVNGKSGGTCNKSATEgcttschpPVIDVEPGKTYRF 73

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 558695371 223 RVI---ALScrpFFTFSVDNH-NITFMEADGVEHDPVEAQNVDVYAAQRVSVIL---------NANQpiGNYWIR 284
Cdd:cd13873   74 RFIgatALS---FVSLGIEGHdNLTIIEADGSYTKPAETDHLQLGSGQRYSFLLktksleelaALNK--TTFWIQ 143
CuRO_3_McoC_like cd13902
The third cupredoxin domain of a multicopper oxidase McoC and similar proteins; This family ...
 417-481 7.49e-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: 53.94  E-value: 7.49e-09
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 558695371 417 HPFHLHGHNFDVVlASNDDTFnfKNPPR--RDVypIN---GGNTTFRFFTDNPGTWFLHCHIDWHLEAGL 481
Cdd:cd13902   55 HPFHLHGTQFQVL-EIDGNPQ--KPEYRawKDT--VNlppGEAVRIATRQDDPGMWMYHCHILEHEDAGM 119
CuRO_1_MCO_like_1 cd13862
The first cupredoxin domain of uncharacterized multicopper oxidase; Multicopper Oxidases (MCOs) ...
 29-129 2.44e-08

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: 52.52  E-value: 2.44e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 558695371  29 VNARLAPdGFERDTVVINGEFPGTLIQVNKGDTVRIPVNNKLTNPlmrrsTSIHWHGFFQArtSAQDGPSFVNQCPQPPN 108
Cdd:cd13862   10 VTVELAP-GRTISTLGYNGQVPGPLLRMRQGVSVTVDVFNDTDIP-----EYVHWHGLPLP--ADVDGAMEEGTPSVPPH 81

                         90       100
                 ....*....|....*....|.
gi 558695371 109 TTFTYEFsVANQTGTYWYHSH 129
Cdd:cd13862   82 GHRRYRM-TPRPAGFRWYHTH 101
CuRO_3_AAO_like_2 cd13895
The third cupredoxin domain of Ascorbate oxidase homologs; This family includes fungal ...
 413-485 5.62e-08

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: 52.70  E-value: 5.62e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 558695371 413 GAGAHPFHLHG-HNFDvvLASNDDTFNFK-----------NPPRRD---VYPI-----------NGGNTTFRFFTDNPGT 466
Cdd:cd13895   89 GLDAHPWHAHGaHYYD--LGSGLGTYSATalaneeklrgyNPIRRDttmLYRYggkgyypppgtGSGWRAWRLRVDDPGV 166

                         90
                 ....*....|....*....
gi 558695371 467 WFLHCHIDWHLEAGLAIVF 485
Cdd:cd13895  167 WMLHCHILQHMIMGMQTVW 185
CuRO_1_CuNIR_like cd04201
Cupredoxin domain 1 of Copper-containing nitrite reductase and two-domain laccase; ...
 46-144 8.76e-08

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


Pssm-ID: 259864 [Multi-domain]  Cd Length: 120  Bit Score: 50.57  E-value: 8.76e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 558695371  46 NGEFPGTLIQVNKGDTVRIPVNNkltNPLMRRSTSIHWHGFFQARTSAqdGPSFVNqcpqpPNTTFTYEFSvANQTGTYW 125
Cdd:cd04201   27 DGDIPGPMLRVREGDTVELHFSN---NPSSTMPHNIDFHAATGAGGGA--GATFIA-----PGETSTFSFK-ATQPGLYV 95

                         90       100
                 ....*....|....*....|..
gi 558695371 126 YHSH---LSTQYCDGLRGGFIV 144
Cdd:cd04201   96 YHCAvapVPMHIANGMYGLILV 117
CuRO_3_MCO_like_2 cd13908
The third cupredoxin domain of uncharacterized multicopper oxidase; Multicopper Oxidases (MCOs) ...
 416-485 1.07e-07

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


Pssm-ID: 259975 [Multi-domain]  Cd Length: 122  Bit Score: 50.53  E-value: 1.07e-07
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 558695371 416 AHPFHLHGHNFDVVLASNDDTFNFknppRRDVYPINGGNTT-FRFFTDNPGTWFLHCHIDWHLEAGLAIVF 485
Cdd:cd13908   54 AHPMHLHRHTFEVTRIDGKPTSGL----RKDVVMLGGYQRVeVDFVADNPGLTLFHCHQQLHMDYGFMALF 120
CuRO_D2_2dMcoN_like cd04202
The second cupredoxin domain of bacterial two domain multicopper oxidase McoN and similar ...
 413-476 2.70e-07

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: 49.94  E-value: 2.70e-07
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 558695371 413 GAGAHPFHLHGHNFdVVLASN-----------DDTFNFKNPPRRDVYpinggnttfrFFTDNPGTWFLHCHIDWH 476
Cdd:cd04202   59 SMDHHPMHLHGHFF-LVTATDggpipgsapwpKDTLNVAPGERYDIE----------FVADNPGDWMFHCHKLHH 122
CuRO_6_ceruloplasmin cd11012
The sixth cupredoxin domain of Ceruloplasmin; Ceruloplasmin is a multicopper oxidase essential ...
 417-485 1.03e-06

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: 48.33  E-value: 1.03e-06
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 558695371 417 HPFHLHGHNFDVVLASnddTFnfknppRRDVYPINGGN-TTFRFFTDNPGTWFLHCHIDWHLEAGLAIVF 485
Cdd:cd11012   82 HTAHFHGHSFDYKHRG---VY------RSDVFDLFPGTfQTVEMIPRTPGTWLLHCHVTDHIHAGMETTY 142
Cupredoxin cd00920
Cupredoxin superfamily; Cupredoxins contain type I copper centers and are involved in ...
 401-485 3.78e-06

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


Pssm-ID: 259860 [Multi-domain]  Cd Length: 110  Bit Score: 45.68  E-value: 3.78e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 558695371 401 IPKNSLIEVNI--PGAGAHPFHLHGHNFDVVLASNDDTFNFKNPPrrDVYPinGGNTTFRFFTDNPGTWFLHCHIDWHLE 478
Cdd:cd00920   27 VPVGDTVRVQFvnKLGENHSVTIAGFGVPVVAMAGGANPGLVNTL--VIGP--GESAEVTFTTDQAGVYWFYCTIPGHNH 102


                 ....*..
gi 558695371 479 AGLAIVF 485
Cdd:cd00920  103 AGMVGTI 109
CuRO_2_CopA_like_1 cd13870
The second cupredoxin domain of CopA copper resistance protein like family; The members of ...
 194-289 6.08e-06

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: 45.40  E-value: 6.08e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 558695371 194 LINGKGrfnggPEVPfAVVNVEKGKRYRFRVIALSCRPFFTFSVDNHNITFMEADGVEHDPVEAQNVDVYAAQRVSVILN 273
Cdd:cd13870   19 LINGRP-----PEDP-AVFTARPGDRLRLRLINAAGDTAFRVALAGHRLTVTHTDGFPVEPVEVDALLIGMGERYDAIVT 92

                         90
                 ....*....|....*.
gi 558695371 274 ANQpiGNYWIRAPPTG 289
Cdd:cd13870   93 ANN--GIWPLVALPEG 106
CuRO_2_MCO_like_2 cd13887
The second cupredoxin domain of uncharacterized multicopper oxidase; Multicopper Oxidases ...
 211-272 6.13e-06

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


Pssm-ID: 259954 [Multi-domain]  Cd Length: 114  Bit Score: 45.39  E-value: 6.13e-06
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 558695371 211 VVNVEKGKRYRFRVIALSCRPFFTFSVDNHNITFMEADGVEHDPVEAQNVDVYAAQRVSVIL 272
Cdd:cd13887   25 VVRVEPGGRVRLRVINGSTATNFHIDLGDLKGTLIAVDGNPVQPVEGRRFPLATAQRLDLLV 86
CuRO_1_Ceruloplasmin_like_1 cd04229
cupredoxin domain of ceruloplasmin homologs; Uncharacterized subfamily of ceruloplasmin ...
 51-146 1.61e-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: 45.49  E-value: 1.61e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 558695371  51 GTLIQVNKGDTVRIPVNNKLTNPlmrrSTSIHWHGFFQARtsAQDGPSFVNQCPQPPNTTFTYEFSVANQTG-------- 122
Cdd:cd04229   73 GPVIRAEVGDTIKVVFKNNLDEF----PVNMHPHGGLYSK--DNEGTTDGAGDVVAPGETYTYRWIVPEDAGpgpgdpss 146

                         90       100
                 ....*....|....*....|....*..
gi 558695371 123 -TYWYHSHLSTQYCD--GLRGGFIVYD 146
Cdd:cd04229  147 rLWLYHSHVDVFAHTnaGLVGPIIVTS 173
CuRO_1_CuNIR cd11020
Cupredoxin domain 1 of Copper-containing nitrite reductase; Copper-containing nitrite ...
 46-127 1.82e-05

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


Pssm-ID: 259906 [Multi-domain]  Cd Length: 119  Bit Score: 44.12  E-value: 1.82e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 558695371  46 NGEFPGTLIQVNKGDTVRIPVNNKLTNPLMRrstSIHWHGffqARTSAQDGPSFVNqcpqpPNTTFTYEFsVANQTGTYW 125
Cdd:cd11020   27 NGQVPGPVIRVREGDTVELTLTNPGTNTMPH---SIDFHA---ATGPGGGEFTTIA-----PGETKTFSF-KALYPGVFM 94


                 ..
gi 558695371 126 YH 127
Cdd:cd11020   95 YH 96
CuRO_3_CueO_FtsP cd13890
The third Cupredoxin domain of the multicopper oxidase CueO, the cell division protein FtsP, ...
 408-480 3.56e-05

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


Pssm-ID: 259957 [Multi-domain]  Cd Length: 124  Bit Score: 43.39  E-value: 3.56e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 558695371 408 EVNIPGAGAHPFHLHGHNFdVVLASNDdtfnfKNPP-----RRDVYPINGGNTT-----FRFFTDNPGTWFLHCHIDWHL 477
Cdd:cd13890   41 EVTNTDGMPHPFHIHGVQF-RILSRNG-----QPPPpneagWKDTVWVPPGETVrilvkFDHYADPTGPFMYHCHILEHE 114


                 ...
gi 558695371 478 EAG 480
Cdd:cd13890  115 DNG 117
CuRO_3_Tth-MCO_like cd13900
The third cupredoxin domain of the bacterial laccases similar to Tth-MCO from Thermus ...
 413-473 5.25e-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: 43.00  E-value: 5.25e-05
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 558695371 413 GAGAHPFHLHGHNFDVVLASND--------DTFNFKNpprrdvypinGGNTTFRF-FTDNPGTWFLHCHI 473
Cdd:cd13900   50 SGEDHPFHIHVNPFQVVSINGKpglppvwrDTVNVPA----------GGSVTIRTrFRDFTGEFVLHCHI 109
CuRO_2_ceruloplasmin_like cd04200
Cupredoxin domains 2, 4, and 6 of ceruloplasmin and similar proteins; This family includes the ...
 417-485 1.34e-04

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


Pssm-ID: 259863 [Multi-domain]  Cd Length: 141  Bit Score: 42.01  E-value: 1.34e-04
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 558695371 417 HPFHLHGHNFDVvlasnddtfnfkNPPRRDVYPI-NGGNTTFRFFTDNPGTWFLHCHIDWHLEAGLAIVF 485
Cdd:cd04200   82 HSIHFHGQTFLY------------KGYRIDTLTLfPATFETVEMVPSNPGTWLLHCHNSDHRHAGMQAYF 139
CuRO_1_ceruloplasmin_like cd04199
Cupredoxin domains 1, 3, and 5 of ceruloplasmin and similar proteins; This family includes the ...
 51-129 1.41e-04

Cupredoxin domains 1, 3, and 5 of ceruloplasmin and similar proteins; This family includes the first, third, and fifth cupredoxin domains of ceruloplasmin and similar proteins including the first, third and fifth cupredoxin domains of unprocessed coagulation factors V and VIII. Ceruloplasmin (ferroxidase) is a multicopper oxidase essential for normal iron homeostasis. It functions in copper transport, amine oxidation and as an antioxidant preventing free radicals in serum. The protein has 6 cupredoxin domains and exhibits internal sequence homology that appears to have evolved from the triplication of a sequence unit composed of two tandem cupredoxin domains. Human Factor VIII facilitates blood clotting by acting as a cofactor for factor IXa. Factor VIII and IXa forms a complex in the presence of Ca+2 and phospholipids that converts factor X to the activated form Xa.


Pssm-ID: 259862 [Multi-domain]  Cd Length: 177  Bit Score: 42.78  E-value: 1.41e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 558695371  51 GTLIQVNKGDTVRIPVNNKLTNPLmrrstSIHWHGF------FQARTSAQDGPSFVNQCPQPPNTTFTYEFSVANQTG-- 122
Cdd:cd04199   69 GPTIRAEVGDTIKVHFKNKASRPY-----SIHPHGVsyekdsEGASYSDQTGPDEKKDDAVAPGETYTYVWIVTEESGpt 143

                         90
                 ....*....|....
gi 558695371 123 -------TYWYHSH 129
Cdd:cd04199  144 kgdpaclTWAYYSH 157
CuRO_1_2DMCO_NIR_like_2 cd14449
The cupredoxin domain 1 of a two-domain laccase related to nitrite reductase; The two-domain ...
 50-129 3.11e-04

The cupredoxin domain 1 of a two-domain laccase related to nitrite reductase; The two-domain laccase (small laccase) in this family differs significantly from all laccases. It resembles the two domain nitrite reductase in both sequence and structure. It consists of two cupredoxin domains and forms trimers, and hence resembles the quaternary structure of nitrite reductases more than that of large laccases. There are three trinuclear copper clusters in the enzyme localized between domains 1 and 2 of each pair of neighbor chains. Laccase is a blue multi-copper enzyme that catalyzes the oxidation of a variety of organic substrates coupled to the reduction of molecular oxygen to water. It displays broad substrate specificity, catalyzing the oxidation of a wide variety of aromatic, notably phenolic, and inorganic substances. Laccase has been implicated in a wide spectrum of biological activities. This subfamily has lost the type 1 (T1) copper binding site in domain 1 that is present in other two-domain laccases.


Pssm-ID: 259991 [Multi-domain]  Cd Length: 135  Bit Score: 41.10  E-value: 3.11e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 558695371  50 PGTLIQVNKGDTVRIPVNNKLTNPLmrrstSIHWHGFfqARTSAQDGpSFVNQCPQPPNTTFTYEF-----------SVA 118
Cdd:cd14449   28 PGPVIEVREGDTLKILFRNTLDVPA-----SLHPHGV--DYTTASDG-TGMNASIVAPGDTRIYTWrthggyrradgSWA 99

                         90
                 ....*....|..
gi 558695371 119 NQTGTYW-YHSH 129
Cdd:cd14449  100 EGTAGYWhYHDH 111
CuRO_2_ceruloplasmin_like_2 cd11023
cupredoxin domain of ceruloplasmin homologs; Uncharacterized subfamily of ceruloplasmin ...
 462-486 5.48e-04

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


Pssm-ID: 259909 [Multi-domain]  Cd Length: 118  Bit Score: 39.90  E-value: 5.48e-04
                         10        20
                 ....*....|....*....|....*
gi 558695371 462 DNPGTWFLHCHIDWHLEAGLAIVFA 486
Cdd:cd11023   93 ADVGTWLLHCHVHDHYMAGMMTQFA 117
Cupredoxin cd00920
Cupredoxin superfamily; Cupredoxins contain type I copper centers and are involved in ...
 54-129 1.46e-03

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


Pssm-ID: 259860 [Multi-domain]  Cd Length: 110  Bit Score: 38.37  E-value: 1.46e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 558695371  54 IQVNKGDTVRIPVNNKLTnplmrRSTSIHWHGFFQA--RTSAQDGPSFVNQCPQPPNTTFTYEFsVANQTGTYWYHSH 129
Cdd:cd00920   25 LVVPVGDTVRVQFVNKLG-----ENHSVTIAGFGVPvvAMAGGANPGLVNTLVIGPGESAEVTF-TTDQAGVYWFYCT 96
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
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