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Conserved domains on  [gi|1564327556|gb|RXN24463|]
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ceruloplasmin [Labeo rohita]

Protein Classification

multicopper oxidase( domain architecture ID 10362984)

multicopper oxidase (MCO) that couples the oxidation of a substrate with a four-electron reduction of molecular oxygen to water, and which may contain three cupredoxin domains that include one mononuclear and one trinuclear copper center

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
Cupredoxin super family cl19115
Cupredoxin superfamily; Cupredoxins contain type I copper centers and are involved in ...
 23-205 4.39e-113

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


The actual alignment was detected with superfamily member cd04222:

Pssm-ID: 473140 [Multi-domain]  Cd Length: 183  Bit Score: 347.87  E-value: 4.39e-113
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1564327556   23 REYFFAIKEIQWDYAPSGKNLIQNKTIKEDEEARVFLERGEQRIGRVYRKAVYQQYTDSNYMQEIEKPKWLGFLGPLISA 102
Cdd:cd04222      1 REYYIGIRETQWDYAPSGKNLITNQTFDDDEHASVFLKRGPDRIGRVYKKAVYLQYTDDTYRTEIEKPVWLGFLGPILKA 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1564327556  103 EENDIVVVHLKNMAKRAYSIHAHGLSYNKSFEGALYPDSSEKAEKADDSVAPGKSFSYVWTLPASHSPGKDDTNCLTRIY 182
Cdd:cd04222     81 EVGDVIVVHLKNFASRPYSLHPHGVFYNKENEGALYPDNTSGFEKADDAVPPGGSYTYTWTVPEEQAPTKADANCLTRIY 160

                          170       180
                   ....*....|....*....|...
gi 1564327556  183 HSHVNAPKDIASGLIGPLIICKK 205
Cdd:cd04222    161 HSHIDAPKDIASGLIGPLIICKK 183
CuRO_5_ceruloplasmin cd04225
The fifth cupredoxin domain of Ceruloplasmin; Ceruloplasmin is a multicopper oxidase essential ...
 745-915 1.91e-107

The fifth 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 fifth cupredoxin domain of ceruloplasmin.


:

Pssm-ID: 259887 [Multi-domain]  Cd Length: 171  Bit Score: 332.51  E-value: 1.91e-107
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1564327556  745 KKYYIAAVEMDWDYSPTRTWEEKMNNGLKESKGNEFLKKEGKFIGSKYKKVLYREYTDETFTKPKERSADMEHLGIMGPM 824
Cdd:cd04225      1 RTYYIAAEEVEWDYSPQRTWEQELHNTHEESPGNAFLNKGDKFIGSKYKKVVYREYTDDTFSVPKERTAEEEHLGILGPL 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1564327556  825 IHGKVGEKVKIVFKNMAKRPYSIHAHGVKTESPQVALTRPGETQTYTWYLPKNSGPTEEQEECSVGAYYSAVDVIKDMYS 904
Cdd:cd04225     81 IHAEVGEKVKIVFKNMASRPYSIHAHGVKTDSSWVAPTEPGETQTYTWKIPERSGPGVEDSNCISWAYYSTVDQIKDLYS 160

                          170
                   ....*....|.
gi 1564327556  905 GLIGPLIVCKK 915
Cdd:cd04225    161 GLIGPLVICRR 171
Cupredoxin super family cl19115
Cupredoxin superfamily; Cupredoxins contain type I copper centers and are involved in ...
 371-585 3.64e-100

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


The actual alignment was detected with superfamily member cd04224:

Pssm-ID: 473140 [Multi-domain]  Cd Length: 197  Bit Score: 314.03  E-value: 3.64e-100
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1564327556  371 GAVRQYYIAAEEIIWDYGPTEINQYSGKKLVD-DSVSDTFFDNRNDRIGGKYKKVQYVEYTDDTFTKRKERTSEEQHLGI 449
Cdd:cd04224      1 GKVRHYFIAAEEIMWDYAPSGKNLFTGQNLTApGSDSEVFFQRNETRIGGTYWKVRYVEYTDATFTTRKHRSKEEEHLGI 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1564327556  450 LGPIIRAEEEDTIKVTFRNKASRPYSIQPHGVQYNIEMDGTLYHNvleesytakklreikkearvVEPLPAALVRPDTTY 529
Cdd:cd04224     81 LGPVIRAEVGDTIKVTFRNKASRPFSIQPHGVFYEKNYEGAMYRD--------------------GDPSPGSHVSPGETF 140

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 1564327556  530 KYEWVVPKDAGPTEKDPDCITYMYYSAVDPIRDTNSGLVGPLLICKPKTL-KSAKQK 585
Cdd:cd04224    141 TYEWTVPEGVGPTNQDPPCLTYLYFSAVDPVRDTNSGLVGPLLVCKKGSLnANGRQK 197
CuRO_2_ceruloplasmin cd11021
The second cupredoxin domain of Ceruloplasmin; Ceruloplasmin is a multicopper oxidase ...
 217-357 3.82e-95

The second 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 second cupredoxin domain of ceruloplasmin.


:

Pssm-ID: 259907 [Multi-domain]  Cd Length: 141  Bit Score: 298.23  E-value: 3.82e-95
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1564327556  217 DYLYTLMFTVSDENLSWYLDENIKTYCTAPAKVNKDDEDFQESNKMHSINGYVFGNLPDLSMCMGNKIHWHLFGMGNEVD 296
Cdd:cd11021      1 DREFVLMFSVVDENLSWYLDENIKTYCSEPAKVDKDDEDFQESNKMHSINGYTFGNLPGLSMCAGDRVKWHLFGMGNEVD 80

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1564327556  297 IHSAFFHGQILTEKQHHVDTISLFPATFVNVEMVADNPGQWLLSCQVNDHLEAGMQAIFEI 357
Cdd:cd11021     81 IHSAFFHGQTLTDRGHRTDTINLFPATFVTAEMVAQNPGKWLLSCQVNDHLKAGMQAFYEV 141
CuRO_6_ceruloplasmin cd11012
The sixth cupredoxin domain of Ceruloplasmin; Ceruloplasmin is a multicopper oxidase essential ...
 928-1071 4.47e-93

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: 292.93  E-value: 4.47e-93
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1564327556  928 EEFALLFMVFDENESWYLDDNIKANVKNPPKALKEDEEFIESNKMHGINGLVYGNLKGLNMKVGDKVYWYLMGMGNEVDI 1007
Cdd:cd11012      2 LEFALLFLVFDENESWYLDENIKTYSDHPEKVNKEDEEFIESNKMHAINGKVFGNLQGLTMHVGDEVYWYLMGMGNEIDI 81

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1564327556 1008 HTAHFHGHSFDYKVSGTHRADVFDLFPGTFQTVTMRPQYSGTWLLHCHVTDHIQAGMETTYTVL 1071
Cdd:cd11012     82 HTAHFHGHSFDYKHRGVYRSDVFDLFPGTFQTVEMIPRTPGTWLLHCHVTDHIHAGMETTYTVL 145
CuRO_4_ceruloplasmin cd11022
The fourth cupredoxin domain of Ceruloplasmin; Ceruloplasmin is a multicopper oxidase ...
 589-731 1.45e-91

The fourth 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 fourth cupredoxin domain of ceruloplasmin.


:

Pssm-ID: 259908 [Multi-domain]  Cd Length: 144  Bit Score: 289.00  E-value: 1.45e-91
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1564327556  589 KEFHLLATVFDENLSWYLDDNINRFAKQPKSVKKEDKDFQESNKMHSLNGYMYGNLKGLSMCKGDKVSWHLSGLGSEVDI 668
Cdd:cd11022      2 KEFFLLFTVFDENESWYLDENIQQFTLDPRSVDKEDEDFQESNKMHSINGYMYGNQPGLDMCKGDTVSWHLFGLGTETDV 81

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1564327556  669 HGLYFEGNRFLYKDTRRDTINVFPHISHTVIMEPDSMGQFEVGCKTTDHYHGGMRANYTVEKC 731
Cdd:cd11022     82 HGIYFSGNTFLLQGTRRDTANLFPHTSVTAIMQPDNEGTFEVNCQTTDHYSAGMRQIYTVSQC 144
 
Name Accession Description Interval E-value
CuRO_1_ceruloplasmin cd04222
The first cupredoxin domain of Ceruloplasmin; Ceruloplasmin is a multicopper oxidase essential ...
 23-205 4.39e-113

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


Pssm-ID: 259884 [Multi-domain]  Cd Length: 183  Bit Score: 347.87  E-value: 4.39e-113
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1564327556   23 REYFFAIKEIQWDYAPSGKNLIQNKTIKEDEEARVFLERGEQRIGRVYRKAVYQQYTDSNYMQEIEKPKWLGFLGPLISA 102
Cdd:cd04222      1 REYYIGIRETQWDYAPSGKNLITNQTFDDDEHASVFLKRGPDRIGRVYKKAVYLQYTDDTYRTEIEKPVWLGFLGPILKA 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1564327556  103 EENDIVVVHLKNMAKRAYSIHAHGLSYNKSFEGALYPDSSEKAEKADDSVAPGKSFSYVWTLPASHSPGKDDTNCLTRIY 182
Cdd:cd04222     81 EVGDVIVVHLKNFASRPYSLHPHGVFYNKENEGALYPDNTSGFEKADDAVPPGGSYTYTWTVPEEQAPTKADANCLTRIY 160

                          170       180
                   ....*....|....*....|...
gi 1564327556  183 HSHVNAPKDIASGLIGPLIICKK 205
Cdd:cd04222    161 HSHIDAPKDIASGLIGPLIICKK 183
CuRO_5_ceruloplasmin cd04225
The fifth cupredoxin domain of Ceruloplasmin; Ceruloplasmin is a multicopper oxidase essential ...
 745-915 1.91e-107

The fifth 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 fifth cupredoxin domain of ceruloplasmin.


Pssm-ID: 259887 [Multi-domain]  Cd Length: 171  Bit Score: 332.51  E-value: 1.91e-107
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1564327556  745 KKYYIAAVEMDWDYSPTRTWEEKMNNGLKESKGNEFLKKEGKFIGSKYKKVLYREYTDETFTKPKERSADMEHLGIMGPM 824
Cdd:cd04225      1 RTYYIAAEEVEWDYSPQRTWEQELHNTHEESPGNAFLNKGDKFIGSKYKKVVYREYTDDTFSVPKERTAEEEHLGILGPL 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1564327556  825 IHGKVGEKVKIVFKNMAKRPYSIHAHGVKTESPQVALTRPGETQTYTWYLPKNSGPTEEQEECSVGAYYSAVDVIKDMYS 904
Cdd:cd04225     81 IHAEVGEKVKIVFKNMASRPYSIHAHGVKTDSSWVAPTEPGETQTYTWKIPERSGPGVEDSNCISWAYYSTVDQIKDLYS 160

                          170
                   ....*....|.
gi 1564327556  905 GLIGPLIVCKK 915
Cdd:cd04225    161 GLIGPLVICRR 171
CuRO_3_ceruloplasmin cd04224
The third cupredoxin domain of Ceruloplasmin; Ceruloplasmin is a multicopper oxidase essential ...
 371-585 3.64e-100

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


Pssm-ID: 259886 [Multi-domain]  Cd Length: 197  Bit Score: 314.03  E-value: 3.64e-100
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1564327556  371 GAVRQYYIAAEEIIWDYGPTEINQYSGKKLVD-DSVSDTFFDNRNDRIGGKYKKVQYVEYTDDTFTKRKERTSEEQHLGI 449
Cdd:cd04224      1 GKVRHYFIAAEEIMWDYAPSGKNLFTGQNLTApGSDSEVFFQRNETRIGGTYWKVRYVEYTDATFTTRKHRSKEEEHLGI 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1564327556  450 LGPIIRAEEEDTIKVTFRNKASRPYSIQPHGVQYNIEMDGTLYHNvleesytakklreikkearvVEPLPAALVRPDTTY 529
Cdd:cd04224     81 LGPVIRAEVGDTIKVTFRNKASRPFSIQPHGVFYEKNYEGAMYRD--------------------GDPSPGSHVSPGETF 140

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 1564327556  530 KYEWVVPKDAGPTEKDPDCITYMYYSAVDPIRDTNSGLVGPLLICKPKTL-KSAKQK 585
Cdd:cd04224    141 TYEWTVPEGVGPTNQDPPCLTYLYFSAVDPVRDTNSGLVGPLLVCKKGSLnANGRQK 197
CuRO_2_ceruloplasmin cd11021
The second cupredoxin domain of Ceruloplasmin; Ceruloplasmin is a multicopper oxidase ...
 217-357 3.82e-95

The second 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 second cupredoxin domain of ceruloplasmin.


Pssm-ID: 259907 [Multi-domain]  Cd Length: 141  Bit Score: 298.23  E-value: 3.82e-95
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1564327556  217 DYLYTLMFTVSDENLSWYLDENIKTYCTAPAKVNKDDEDFQESNKMHSINGYVFGNLPDLSMCMGNKIHWHLFGMGNEVD 296
Cdd:cd11021      1 DREFVLMFSVVDENLSWYLDENIKTYCSEPAKVDKDDEDFQESNKMHSINGYTFGNLPGLSMCAGDRVKWHLFGMGNEVD 80

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1564327556  297 IHSAFFHGQILTEKQHHVDTISLFPATFVNVEMVADNPGQWLLSCQVNDHLEAGMQAIFEI 357
Cdd:cd11021     81 IHSAFFHGQTLTDRGHRTDTINLFPATFVTAEMVAQNPGKWLLSCQVNDHLKAGMQAFYEV 141
CuRO_6_ceruloplasmin cd11012
The sixth cupredoxin domain of Ceruloplasmin; Ceruloplasmin is a multicopper oxidase essential ...
 928-1071 4.47e-93

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: 292.93  E-value: 4.47e-93
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1564327556  928 EEFALLFMVFDENESWYLDDNIKANVKNPPKALKEDEEFIESNKMHGINGLVYGNLKGLNMKVGDKVYWYLMGMGNEVDI 1007
Cdd:cd11012      2 LEFALLFLVFDENESWYLDENIKTYSDHPEKVNKEDEEFIESNKMHAINGKVFGNLQGLTMHVGDEVYWYLMGMGNEIDI 81

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1564327556 1008 HTAHFHGHSFDYKVSGTHRADVFDLFPGTFQTVTMRPQYSGTWLLHCHVTDHIQAGMETTYTVL 1071
Cdd:cd11012     82 HTAHFHGHSFDYKHRGVYRSDVFDLFPGTFQTVEMIPRTPGTWLLHCHVTDHIHAGMETTYTVL 145
CuRO_4_ceruloplasmin cd11022
The fourth cupredoxin domain of Ceruloplasmin; Ceruloplasmin is a multicopper oxidase ...
 589-731 1.45e-91

The fourth 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 fourth cupredoxin domain of ceruloplasmin.


Pssm-ID: 259908 [Multi-domain]  Cd Length: 144  Bit Score: 289.00  E-value: 1.45e-91
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1564327556  589 KEFHLLATVFDENLSWYLDDNINRFAKQPKSVKKEDKDFQESNKMHSLNGYMYGNLKGLSMCKGDKVSWHLSGLGSEVDI 668
Cdd:cd11022      2 KEFFLLFTVFDENESWYLDENIQQFTLDPRSVDKEDEDFQESNKMHSINGYMYGNQPGLDMCKGDTVSWHLFGLGTETDV 81

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1564327556  669 HGLYFEGNRFLYKDTRRDTINVFPHISHTVIMEPDSMGQFEVGCKTTDHYHGGMRANYTVEKC 731
Cdd:cd11022     82 HGIYFSGNTFLLQGTRRDTANLFPHTSVTAIMQPDNEGTFEVNCQTTDHYSAGMRQIYTVSQC 144
Cu-oxidase_2 pfam07731
Multicopper oxidase; This entry contains many divergent copper oxidase-like domains that are ...
 970-1074 1.26e-18

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: 83.25  E-value: 1.26e-18
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1564327556  970 NKMHGINGLVYG-NLKGLNMKVGDKVYWYLMGMGNevDIHTAHFHGHSFDYKVSGTH----------------RADVFDL 1032
Cdd:pfam07731   19 RNDWAINGLLFPpNTNVITLPYGTVVEWVLQNTTT--GVHPFHLHGHSFQVLGRGGGpwpeedpktynlvdpvRRDTVQV 96

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|..
gi 1564327556 1033 FPGTFQTVTMRPQYSGTWLLHCHVTDHIQAGMETTYTVLEKD 1074
Cdd:pfam07731   97 PPGGWVAIRFRADNPGVWLFHCHILWHLDQGMMGQFVVRPGD 138
Cu-oxidase_3 pfam07732
Multicopper oxidase; This entry contains many divergent copper oxidase-like domains that are ...
 95-202 1.16e-09

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: 56.87  E-value: 1.16e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1564327556   95 FLGPLISAEENDIVVVHLKNMAKRAYSIHAHGLSYNKSFEGALYPDSSEkaekadDSVAPGKSFSYVWtlPASHSPGkdd 174
Cdd:pfam07732   24 FPGPTIRVREGDTVVVNVTNNLDEPTSIHWHGLQQRGTPWMDGVPGVTQ------CPIPPGQSFTYRF--QVKQQAG--- 92

                           90       100
                   ....*....|....*....|....*...
gi 1564327556  175 tnclTRIYHSHVNAPKdiASGLIGPLII 202
Cdd:pfam07732   93 ----TYWYHSHTSGQQ--AAGLAGAIII 114
SufI COG2132
Multicopper oxidase with three cupredoxin domains (includes cell division protein FtsP and ...
 972-1072 1.23e-08

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: 58.41  E-value: 1.23e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1564327556  972 MHGINGLVYGNLK-GLNMKVGDKVYWYLMGMGNevDIHTAHFHGHSF------DYKVSGTHRADVFDLFPGtfQTVTMR- 1043
Cdd:COG2132    317 VWTINGKAFDPDRpDLTVKLGERERWTLVNDTM--MPHPFHLHGHQFqvlsrnGKPPPEGGWKDTVLVPPG--ETVRILf 392

                           90       100       110
                   ....*....|....*....|....*....|.
gi 1564327556 1044 --PQYSGTWLLHCHVTDHIQAGMETTYTVLE 1072
Cdd:COG2132    393 rfDNYPGDWMFHCHILEHEDAGMMGQFEVVP 423
Cu-oxidase pfam00394
Multicopper oxidase; Many of the proteins in this family contain multiple similar copies of ...
 220-353 1.95e-08

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: 54.25  E-value: 1.95e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1564327556  220 YTLMFTvsdenlSWYlDENIKTYCTAPAKVNKDDEDFQESNKMHSINGYVFGNLPDLSMCMGNKIHWHLFgMGNEVDIHS 299
Cdd:pfam00394    3 YVITLS------DWY-HKDAKDLEKELLASGKAPTDFPPVPDAVLINGKDGASLATLTVTPGKTYRLRII-NVALDDSLN 74

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1564327556  300 AFFHGQILTE--------KQHHVDTISLFPATFVNVEMVADN-PGQWLLSCQVN-DHLEAGMQA 353
Cdd:pfam00394   75 FSIEGHKMTVvevdgvyvNPFTVDSLDIFPGQRYSVLVTANQdPGNYWIVASPNiPAFDNGTAA 138
SufI COG2132
Multicopper oxidase with three cupredoxin domains (includes cell division protein FtsP and ...
 95-202 6.81e-08

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: 56.10  E-value: 6.81e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1564327556   95 FLGPLISAEENDIVVVHLKNMAKRAYSIHAHGLSYNKSFEGAlypdssekaekADDSVAPGKSFSYVWTLPasHSPGkdd 174
Cdd:COG2132     42 YPGPTIRVREGDRVRVRVTNRLPEPTTVHWHGLRVPNAMDGV-----------PGDPIAPGETFTYEFPVP--QPAG--- 105

                           90       100       110
                   ....*....|....*....|....*....|
gi 1564327556  175 tnclTRIYHSHVNA--PKDIASGLIGPLII 202
Cdd:COG2132    106 ----TYWYHPHTHGstAEQVYRGLAGALIV 131
SufI COG2132
Multicopper oxidase with three cupredoxin domains (includes cell division protein FtsP and ...
 449-573 2.74e-07

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: 54.17  E-value: 2.74e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1564327556  449 ILGPIIRAEEEDTIKVTFRNKASRPYSIQPHGVQYNIEMDGTlyhnvleesytakklreikkearvveplPAALVRPDTT 528
Cdd:COG2132     42 YPGPTIRVREGDRVRVRVTNRLPEPTTVHWHGLRVPNAMDGV----------------------------PGDPIAPGET 93

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*..
gi 1564327556  529 YKYEWVVPKDAGptekdpdciTYMYYSAVDPIRDTN--SGLVGPLLI 573
Cdd:COG2132     94 FTYEFPVPQPAG---------TYWYHPHTHGSTAEQvyRGLAGALIV 131
SufI COG2132
Multicopper oxidase with three cupredoxin domains (includes cell division protein FtsP and ...
 822-912 8.65e-06

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: 49.55  E-value: 8.65e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1564327556  822 GPMIHGKVGEKVKIVFKNMAKRPYSIHAHGVKTESPQ----VALTRPGETQTYT----------WYLPKNSGPTEEQeec 887
Cdd:COG2132     44 GPTIRVREGDRVRVRVTNRLPEPTTVHWHGLRVPNAMdgvpGDPIAPGETFTYEfpvpqpagtyWYHPHTHGSTAEQ--- 120

                           90       100
                   ....*....|....*....|....*
gi 1564327556  888 svgayysavdvikdMYSGLIGPLIV 912
Cdd:COG2132    121 --------------VYRGLAGALIV 131
Cu-oxidase_3 pfam07732
Multicopper oxidase; This entry contains many divergent copper oxidase-like domains that are ...
 423-573 1.16e-05

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: 45.70  E-value: 1.16e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1564327556  423 KVQYVEYTDDTFTKRKERTSEEQhlgILGPIIRAEEEDTIKVTFRNKASRPYSIQPHGVQY--NIEMDGTLYhnvleesy 500
Cdd:pfam07732    1 TVTYGTVSPLGGTRQAVIGVNGQ---FPGPTIRVREGDTVVVNVTNNLDEPTSIHWHGLQQrgTPWMDGVPG-------- 69

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1564327556  501 takklreikkearvvepLPAALVRPDTTYKYEWVVPKDAGptekdpdciTYMYYSAVDPIRdtNSGLVGPLLI 573
Cdd:pfam07732   70 -----------------VTQCPIPPGQSFTYRFQVKQQAG---------TYWYHSHTSGQQ--AAGLAGAIII 114
ascorbase TIGR03388
L-ascorbate oxidase, plant type; Members of this protein family are the copper-containing ...
 95-202 7.66e-05

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: 46.67  E-value: 7.66e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1564327556   95 FLGPLISAEENDIVVVHLKN-MAKRAYSIHAHGLSYNksfeGALYPDSSEKAEKAddSVAPGKSFSYVWTLpasHSPGkd 173
Cdd:TIGR03388   29 FPGPTIRAQAGDTIVVELTNkLHTEGVVIHWHGIRQI----GTPWADGTAGVTQC--AINPGETFIYNFVV---DRPG-- 97

                           90       100
                   ....*....|....*....|....*....
gi 1564327556  174 dtnclTRIYHSHVNAPKdiASGLIGPLII 202
Cdd:TIGR03388   98 -----TYFYHGHYGMQR--SAGLYGSLIV 119
PLN02191 PLN02191
L-ascorbate oxidase
 95-202 1.77e-04

L-ascorbate oxidase


Pssm-ID: 177843 [Multi-domain]  Cd Length: 574  Bit Score: 45.39  E-value: 1.77e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1564327556   95 FLGPLISAEENDIVVVHLKN-MAKRAYSIHAHGLSYnksfEGALYPDSSEKAEKAddSVAPGKSFSYVWTLpasHSPGkd 173
Cdd:PLN02191    51 FPGPTIDAVAGDTIVVHLTNkLTTEGLVIHWHGIRQ----KGSPWADGAAGVTQC--AINPGETFTYKFTV---EKPG-- 119

                           90       100
                   ....*....|....*....|....*....
gi 1564327556  174 dtnclTRIYHSHVNAPKdiASGLIGPLII 202
Cdd:PLN02191   120 -----THFYHGHYGMQR--SAGLYGSLIV 141
PLN02191 PLN02191
L-ascorbate oxidase
 245-355 3.61e-04

L-ascorbate oxidase


Pssm-ID: 177843 [Multi-domain]  Cd Length: 574  Bit Score: 44.62  E-value: 3.61e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1564327556  245 APAKVNKDDED------FQESNKMHSINGYVFGNLPDLSMCMGN-------KIH-WHLFGMGNEVdihSAFFHGQI---L 307
Cdd:PLN02191   414 SPPRSYRMDYDimnpppFPNTTTGNGIYVFPFNVTVDVIIQNANvlkgvvsEIHpWHLHGHDFWV---LGYGDGKFkpgI 490

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....
gi 1564327556  308 TEKQHHV------DTISLFPATFVNVEMVADNPGQWLLSCQVNDHLEAGMQAIF 355
Cdd:PLN02191   491 DEKTYNLknpplrNTAILYPYGWTAIRFVTDNPGVWFFHCHIEPHLHMGMGVVF 544
SufI COG2132
Multicopper oxidase with three cupredoxin domains (includes cell division protein FtsP and ...
 262-359 5.63e-04

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: 43.77  E-value: 5.63e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1564327556  262 MHSINGYVFG-NLPDLSMCMGNKIHWHLFGMGNE---VDIHSAFFhgQIL------TEKQHHVDTISLFPATFVNVEMVA 331
Cdd:COG2132    317 VWTINGKAFDpDRPDLTVKLGERERWTLVNDTMMphpFHLHGHQF--QVLsrngkpPPEGGWKDTVLVPPGETVRILFRF 394

                           90       100
                   ....*....|....*....|....*....
gi 1564327556  332 DN-PGQWLLSCQVNDHLEAGMQAIFEIKK 359
Cdd:COG2132    395 DNyPGDWMFHCHILEHEDAGMMGQFEVVP 423
ascorbase TIGR03388
L-ascorbate oxidase, plant type; Members of this protein family are the copper-containing ...
 315-356 6.86e-04

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: 43.59  E-value: 6.86e-04
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|..
gi 1564327556  315 DTISLFPATFVNVEMVADNPGQWLLSCQVNDHLEAGMQAIFE 356
Cdd:TIGR03388  481 NTVVIFPYGWTALRFVADNPGVWAFHCHIEPHLHMGMGVVFA 522
 
Name Accession Description Interval E-value
CuRO_1_ceruloplasmin cd04222
The first cupredoxin domain of Ceruloplasmin; Ceruloplasmin is a multicopper oxidase essential ...
 23-205 4.39e-113

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


Pssm-ID: 259884 [Multi-domain]  Cd Length: 183  Bit Score: 347.87  E-value: 4.39e-113
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1564327556   23 REYFFAIKEIQWDYAPSGKNLIQNKTIKEDEEARVFLERGEQRIGRVYRKAVYQQYTDSNYMQEIEKPKWLGFLGPLISA 102
Cdd:cd04222      1 REYYIGIRETQWDYAPSGKNLITNQTFDDDEHASVFLKRGPDRIGRVYKKAVYLQYTDDTYRTEIEKPVWLGFLGPILKA 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1564327556  103 EENDIVVVHLKNMAKRAYSIHAHGLSYNKSFEGALYPDSSEKAEKADDSVAPGKSFSYVWTLPASHSPGKDDTNCLTRIY 182
Cdd:cd04222     81 EVGDVIVVHLKNFASRPYSLHPHGVFYNKENEGALYPDNTSGFEKADDAVPPGGSYTYTWTVPEEQAPTKADANCLTRIY 160

                          170       180
                   ....*....|....*....|...
gi 1564327556  183 HSHVNAPKDIASGLIGPLIICKK 205
Cdd:cd04222    161 HSHIDAPKDIASGLIGPLIICKK 183
CuRO_5_ceruloplasmin cd04225
The fifth cupredoxin domain of Ceruloplasmin; Ceruloplasmin is a multicopper oxidase essential ...
 745-915 1.91e-107

The fifth 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 fifth cupredoxin domain of ceruloplasmin.


Pssm-ID: 259887 [Multi-domain]  Cd Length: 171  Bit Score: 332.51  E-value: 1.91e-107
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1564327556  745 KKYYIAAVEMDWDYSPTRTWEEKMNNGLKESKGNEFLKKEGKFIGSKYKKVLYREYTDETFTKPKERSADMEHLGIMGPM 824
Cdd:cd04225      1 RTYYIAAEEVEWDYSPQRTWEQELHNTHEESPGNAFLNKGDKFIGSKYKKVVYREYTDDTFSVPKERTAEEEHLGILGPL 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1564327556  825 IHGKVGEKVKIVFKNMAKRPYSIHAHGVKTESPQVALTRPGETQTYTWYLPKNSGPTEEQEECSVGAYYSAVDVIKDMYS 904
Cdd:cd04225     81 IHAEVGEKVKIVFKNMASRPYSIHAHGVKTDSSWVAPTEPGETQTYTWKIPERSGPGVEDSNCISWAYYSTVDQIKDLYS 160

                          170
                   ....*....|.
gi 1564327556  905 GLIGPLIVCKK 915
Cdd:cd04225    161 GLIGPLVICRR 171
CuRO_3_ceruloplasmin cd04224
The third cupredoxin domain of Ceruloplasmin; Ceruloplasmin is a multicopper oxidase essential ...
 371-585 3.64e-100

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


Pssm-ID: 259886 [Multi-domain]  Cd Length: 197  Bit Score: 314.03  E-value: 3.64e-100
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1564327556  371 GAVRQYYIAAEEIIWDYGPTEINQYSGKKLVD-DSVSDTFFDNRNDRIGGKYKKVQYVEYTDDTFTKRKERTSEEQHLGI 449
Cdd:cd04224      1 GKVRHYFIAAEEIMWDYAPSGKNLFTGQNLTApGSDSEVFFQRNETRIGGTYWKVRYVEYTDATFTTRKHRSKEEEHLGI 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1564327556  450 LGPIIRAEEEDTIKVTFRNKASRPYSIQPHGVQYNIEMDGTLYHNvleesytakklreikkearvVEPLPAALVRPDTTY 529
Cdd:cd04224     81 LGPVIRAEVGDTIKVTFRNKASRPFSIQPHGVFYEKNYEGAMYRD--------------------GDPSPGSHVSPGETF 140

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 1564327556  530 KYEWVVPKDAGPTEKDPDCITYMYYSAVDPIRDTNSGLVGPLLICKPKTL-KSAKQK 585
Cdd:cd04224    141 TYEWTVPEGVGPTNQDPPCLTYLYFSAVDPVRDTNSGLVGPLLVCKKGSLnANGRQK 197
CuRO_2_ceruloplasmin cd11021
The second cupredoxin domain of Ceruloplasmin; Ceruloplasmin is a multicopper oxidase ...
 217-357 3.82e-95

The second 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 second cupredoxin domain of ceruloplasmin.


Pssm-ID: 259907 [Multi-domain]  Cd Length: 141  Bit Score: 298.23  E-value: 3.82e-95
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1564327556  217 DYLYTLMFTVSDENLSWYLDENIKTYCTAPAKVNKDDEDFQESNKMHSINGYVFGNLPDLSMCMGNKIHWHLFGMGNEVD 296
Cdd:cd11021      1 DREFVLMFSVVDENLSWYLDENIKTYCSEPAKVDKDDEDFQESNKMHSINGYTFGNLPGLSMCAGDRVKWHLFGMGNEVD 80

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1564327556  297 IHSAFFHGQILTEKQHHVDTISLFPATFVNVEMVADNPGQWLLSCQVNDHLEAGMQAIFEI 357
Cdd:cd11021     81 IHSAFFHGQTLTDRGHRTDTINLFPATFVTAEMVAQNPGKWLLSCQVNDHLKAGMQAFYEV 141
CuRO_6_ceruloplasmin cd11012
The sixth cupredoxin domain of Ceruloplasmin; Ceruloplasmin is a multicopper oxidase essential ...
 928-1071 4.47e-93

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: 292.93  E-value: 4.47e-93
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1564327556  928 EEFALLFMVFDENESWYLDDNIKANVKNPPKALKEDEEFIESNKMHGINGLVYGNLKGLNMKVGDKVYWYLMGMGNEVDI 1007
Cdd:cd11012      2 LEFALLFLVFDENESWYLDENIKTYSDHPEKVNKEDEEFIESNKMHAINGKVFGNLQGLTMHVGDEVYWYLMGMGNEIDI 81

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1564327556 1008 HTAHFHGHSFDYKVSGTHRADVFDLFPGTFQTVTMRPQYSGTWLLHCHVTDHIQAGMETTYTVL 1071
Cdd:cd11012     82 HTAHFHGHSFDYKHRGVYRSDVFDLFPGTFQTVEMIPRTPGTWLLHCHVTDHIHAGMETTYTVL 145
CuRO_4_ceruloplasmin cd11022
The fourth cupredoxin domain of Ceruloplasmin; Ceruloplasmin is a multicopper oxidase ...
 589-731 1.45e-91

The fourth 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 fourth cupredoxin domain of ceruloplasmin.


Pssm-ID: 259908 [Multi-domain]  Cd Length: 144  Bit Score: 289.00  E-value: 1.45e-91
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1564327556  589 KEFHLLATVFDENLSWYLDDNINRFAKQPKSVKKEDKDFQESNKMHSLNGYMYGNLKGLSMCKGDKVSWHLSGLGSEVDI 668
Cdd:cd11022      2 KEFFLLFTVFDENESWYLDENIQQFTLDPRSVDKEDEDFQESNKMHSINGYMYGNQPGLDMCKGDTVSWHLFGLGTETDV 81

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1564327556  669 HGLYFEGNRFLYKDTRRDTINVFPHISHTVIMEPDSMGQFEVGCKTTDHYHGGMRANYTVEKC 731
Cdd:cd11022     82 HGIYFSGNTFLLQGTRRDTANLFPHTSVTAIMQPDNEGTFEVNCQTTDHYSAGMRQIYTVSQC 144
CuRO_1_ceruloplasmin_like cd04199
Cupredoxin domains 1, 3, and 5 of ceruloplasmin and similar proteins; This family includes the ...
 23-205 5.04e-76

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: 247.70  E-value: 5.04e-76
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1564327556   23 REYFFAIKEIQWDYAPSGKNliqnktIKEDEEARVFLERGEQRIGRVYRKAVYQQYTDSNYMQEIEKPKWLGFLGPLISA 102
Cdd:cd04199      1 RHYYIAAEEIDWDYAPSGLA------EKDLSYRNQYLDNGPFRIGRSYKKVVYREYTDESFTTPGPQPEHLGILGPTIRA 74

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1564327556  103 EENDIVVVHLKNMAKRAYSIHAHGLSYNKSFEGALYPDSSEKAEKADDSVAPGKSFSYVWTLPASHSPGKDDTNCLTRIY 182
Cdd:cd04199     75 EVGDTIKVHFKNKASRPYSIHPHGVSYEKDSEGASYSDQTGPDEKKDDAVAPGETYTYVWIVTEESGPTKGDPACLTWAY 154

                          170       180
                   ....*....|....*....|...
gi 1564327556  183 HSHVNAPKDIASGLIGPLIICKK 205
Cdd:cd04199    155 YSHVDLEKDINSGLIGPLLICKK 177
CuRO_1_ceruloplasmin_like cd04199
Cupredoxin domains 1, 3, and 5 of ceruloplasmin and similar proteins; This family includes the ...
 374-575 2.42e-71

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: 234.99  E-value: 2.42e-71
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1564327556  374 RQYYIAAEEIIWDYGPTEINQysgkklVDDSVSDTFFDNRNDRIGGKYKKVQYVEYTDDTFTKRKErtsEEQHLGILGPI 453
Cdd:cd04199      1 RHYYIAAEEIDWDYAPSGLAE------KDLSYRNQYLDNGPFRIGRSYKKVVYREYTDESFTTPGP---QPEHLGILGPT 71

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1564327556  454 IRAEEEDTIKVTFRNKASRPYSIQPHGVQYNIEMDGTLYhnvleESYTAKKLREIKKearvveplpaalVRPDTTYKYEW 533
Cdd:cd04199     72 IRAEVGDTIKVHFKNKASRPYSIHPHGVSYEKDSEGASY-----SDQTGPDEKKDDA------------VAPGETYTYVW 134

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|..
gi 1564327556  534 VVPKDAGPTEKDPDCITYMYYSAVDPIRDTNSGLVGPLLICK 575
Cdd:cd04199    135 IVTEESGPTKGDPACLTWAYYSHVDLEKDINSGLIGPLLICK 176
CuRO_2_ceruloplasmin_like cd04200
Cupredoxin domains 2, 4, and 6 of ceruloplasmin and similar proteins; This family includes the ...
 222-357 8.16e-67

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: 220.74  E-value: 8.16e-67
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1564327556  222 LMFTVSDENLSWYLDENIKTYCTAPAKVNKDDEDFQESNKMHSINGYVFGNLPDLSMCMGNKIHWHLFGMGNEVDIHSAF 301
Cdd:cd04200      6 LLFAVFDENKSWYLEDNIKRFCDNPEKVDKDDEEFQESNKMHAINGYVFGNLPGLTMCAGDRVRWHLLGMGNEVDVHSIH 85

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 1564327556  302 FHGQILTEKQHHVDTISLFPATFVNVEMVADNPGQWLLSCQVNDHLEAGMQAIFEI 357
Cdd:cd04200     86 FHGQTFLYKGYRIDTLTLFPATFETVEMVPSNPGTWLLHCHNSDHRHAGMQAYFLV 141
CuRO_2_ceruloplasmin_like cd04200
Cupredoxin domains 2, 4, and 6 of ceruloplasmin and similar proteins; This family includes the ...
 929-1070 6.77e-65

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: 215.35  E-value: 6.77e-65
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1564327556  929 EFALLFMVFDENESWYLDDNIKANVKNPPKALKEDEEFIESNKMHGINGLVYGNLKGLNMKVGDKVYWYLMGMGNEVDIH 1008
Cdd:cd04200      3 EFVLLFAVFDENKSWYLEDNIKRFCDNPEKVDKDDEEFQESNKMHAINGYVFGNLPGLTMCAGDRVRWHLLGMGNEVDVH 82

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1564327556 1009 TAHFHGHSFDYKvsgTHRADVFDLFPGTFQTVTMRPQYSGTWLLHCHVTDHIQAGMETTYTV 1070
Cdd:cd04200     83 SIHFHGQTFLYK---GYRIDTLTLFPATFETVEMVPSNPGTWLLHCHNSDHRHAGMQAYFLV 141
CuRO_1_ceruloplasmin_like cd04199
Cupredoxin domains 1, 3, and 5 of ceruloplasmin and similar proteins; This family includes the ...
 745-915 1.08e-63

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: 213.42  E-value: 1.08e-63
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1564327556  745 KKYYIAAVEMDWDYSPTRTWEekmnngLKESKGNEFLKKEGKFIGSKYKKVLYREYTDETFTKPKERsadMEHLGIMGPM 824
Cdd:cd04199      1 RHYYIAAEEIDWDYAPSGLAE------KDLSYRNQYLDNGPFRIGRSYKKVVYREYTDESFTTPGPQ---PEHLGILGPT 71

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1564327556  825 IHGKVGEKVKIVFKNMAKRPYSIHAHGVKTESPQ---------------VALTRPGETQTYTWYLPKNSGPTEEQEECSV 889
Cdd:cd04199     72 IRAEVGDTIKVHFKNKASRPYSIHPHGVSYEKDSegasysdqtgpdekkDDAVAPGETYTYVWIVTEESGPTKGDPACLT 151

                          170       180
                   ....*....|....*....|....*.
gi 1564327556  890 GAYYSAVDVIKDMYSGLIGPLIVCKK 915
Cdd:cd04199    152 WAYYSHVDLEKDINSGLIGPLLICKK 177
CuRO_3_ceruloplasmin cd04224
The third cupredoxin domain of Ceruloplasmin; Ceruloplasmin is a multicopper oxidase essential ...
 23-212 3.48e-63

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


Pssm-ID: 259886 [Multi-domain]  Cd Length: 197  Bit Score: 212.72  E-value: 3.48e-63
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1564327556   23 REYFFAIKEIQWDYAPSGKNLIQNKTI-KEDEEARVFLERGEQRIGRVYRKAVYQQYTDSNY---MQEIEKPKWLGFLGP 98
Cdd:cd04224      4 RHYFIAAEEIMWDYAPSGKNLFTGQNLtAPGSDSEVFFQRNETRIGGTYWKVRYVEYTDATFttrKHRSKEEEHLGILGP 83

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1564327556   99 LISAEENDIVVVHLKNMAKRAYSIHAHGLSYNKSFEGALYPDSSEKAEKaddSVAPGKSFSYVWTLPASHSPGKDDTNCL 178
Cdd:cd04224     84 VIRAEVGDTIKVTFRNKASRPFSIQPHGVFYEKNYEGAMYRDGDPSPGS---HVSPGETFTYEWTVPEGVGPTNQDPPCL 160

                          170       180       190
                   ....*....|....*....|....*....|....
gi 1564327556  179 TRIYHSHVNAPKDIASGLIGPLIICKKGFLDVHG 212
Cdd:cd04224    161 TYLYFSAVDPVRDTNSGLVGPLLVCKKGSLNANG 194
CuRO_5_ceruloplasmin cd04225
The fifth cupredoxin domain of Ceruloplasmin; Ceruloplasmin is a multicopper oxidase essential ...
 374-576 2.43e-61

The fifth 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 fifth cupredoxin domain of ceruloplasmin.


Pssm-ID: 259887 [Multi-domain]  Cd Length: 171  Bit Score: 206.55  E-value: 2.43e-61
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1564327556  374 RQYYIAAEEIIWDYGPT-----EINQYSGKklvddSVSDTFFDNRNDRIGGKYKKVQYVEYTDDTFTKRKERTSEEQHLG 448
Cdd:cd04225      1 RTYYIAAEEVEWDYSPQrtweqELHNTHEE-----SPGNAFLNKGDKFIGSKYKKVVYREYTDDTFSVPKERTAEEEHLG 75

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1564327556  449 ILGPIIRAEEEDTIKVTFRNKASRPYSIQPHGVQynieMDGTlyhnvleesytakklreikkearvveplPAALVRPDTT 528
Cdd:cd04225     76 ILGPLIHAEVGEKVKIVFKNMASRPYSIHAHGVK----TDSS----------------------------WVAPTEPGET 123

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*...
gi 1564327556  529 YKYEWVVPKDAGPTEKDPDCITYMYYSAVDPIRDTNSGLVGPLLICKP 576
Cdd:cd04225    124 QTYTWKIPERSGPGVEDSNCISWAYYSTVDQIKDLYSGLIGPLVICRR 171
CuRO_4_ceruloplasmin cd11022
The fourth cupredoxin domain of Ceruloplasmin; Ceruloplasmin is a multicopper oxidase ...
 217-360 6.24e-59

The fourth 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 fourth cupredoxin domain of ceruloplasmin.


Pssm-ID: 259908 [Multi-domain]  Cd Length: 144  Bit Score: 198.86  E-value: 6.24e-59
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1564327556  217 DYLYTLMFTVSDENLSWYLDENIKTYCTAPAKVNKDDEDFQESNKMHSINGYVFGNLPDLSMCMGNKIHWHLFGMGNEVD 296
Cdd:cd11022      1 DKEFFLLFTVFDENESWYLDENIQQFTLDPRSVDKEDEDFQESNKMHSINGYMYGNQPGLDMCKGDTVSWHLFGLGTETD 80

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1564327556  297 IHSAFFHGQILTEKQHHVDTISLFPATFVNVEMVADNPGQWLLSCQVNDHLEAGMQAIFEIKKC 360
Cdd:cd11022     81 VHGIYFSGNTFLLQGTRRDTANLFPHTSVTAIMQPDNEGTFEVNCQTTDHYSAGMRQIYTVSQC 144
CuRO_3_ceruloplasmin cd04224
The third cupredoxin domain of Ceruloplasmin; Ceruloplasmin is a multicopper oxidase essential ...
 743-915 1.18e-57

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


Pssm-ID: 259886 [Multi-domain]  Cd Length: 197  Bit Score: 197.31  E-value: 1.18e-57
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1564327556  743 HQKKYYIAAVEMDWDYSPTRT-WEEKMNNGLKESKGNEFLKKEGKFIGSKYKKVLYREYTDETFTKPKERSADMEHLGIM 821
Cdd:cd04224      2 KVRHYFIAAEEIMWDYAPSGKnLFTGQNLTAPGSDSEVFFQRNETRIGGTYWKVRYVEYTDATFTTRKHRSKEEEHLGIL 81

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1564327556  822 GPMIHGKVGEKVKIVFKNMAKRPYSIHAHGVKTES------------PQVALTRPGETQTYTWYLPKNSGPTEEQEECSV 889
Cdd:cd04224     82 GPVIRAEVGDTIKVTFRNKASRPFSIQPHGVFYEKnyegamyrdgdpSPGSHVSPGETFTYEWTVPEGVGPTNQDPPCLT 161

                          170       180
                   ....*....|....*....|....*.
gi 1564327556  890 GAYYSAVDVIKDMYSGLIGPLIVCKK 915
Cdd:cd04224    162 YLYFSAVDPVRDTNSGLVGPLLVCKK 187
CuRO_2_ceruloplasmin_like cd04200
Cupredoxin domains 2, 4, and 6 of ceruloplasmin and similar proteins; This family includes the ...
 588-728 2.80e-56

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: 191.08  E-value: 2.80e-56
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1564327556  588 KKEFHLLATVFDENLSWYLDDNINRFAKQPKSVKKEDKDFQESNKMHSLNGYMYGNLKGLSMCKGDKVSWHLSGLGSEVD 667
Cdd:cd04200      1 DKEFVLLFAVFDENKSWYLEDNIKRFCDNPEKVDKDDEEFQESNKMHAINGYVFGNLPGLTMCAGDRVRWHLLGMGNEVD 80

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1564327556  668 IHGLYFEGNRFLYKDTRRDTINVFPHISHTVIMEPDSMGQFEVGCKTTDHYHGGMRANYTV 728
Cdd:cd04200     81 VHSIHFHGQTFLYKGYRIDTLTLFPATFETVEMVPSNPGTWLLHCHNSDHRHAGMQAYFLV 141
CuRO_2_ceruloplasmin cd11021
The second cupredoxin domain of Ceruloplasmin; Ceruloplasmin is a multicopper oxidase ...
 929-1070 3.56e-56

The second 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 second cupredoxin domain of ceruloplasmin.


Pssm-ID: 259907 [Multi-domain]  Cd Length: 141  Bit Score: 190.76  E-value: 3.56e-56
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1564327556  929 EFALLFMVFDENESWYLDDNIKANVKNPPKALKEDEEFIESNKMHGINGLVYGNLKGLNMKVGDKVYWYLMGMGNEVDIH 1008
Cdd:cd11021      3 EFVLMFSVVDENLSWYLDENIKTYCSEPAKVDKDDEDFQESNKMHSINGYTFGNLPGLSMCAGDRVKWHLFGMGNEVDIH 82

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1564327556 1009 TAHFHGHSFDYKvsgTHRADVFDLFPGTFQTVTMRPQYSGTWLLHCHVTDHIQAGMETTYTV 1070
Cdd:cd11021     83 SAFFHGQTLTDR---GHRTDTINLFPATFVTAEMVAQNPGKWLLSCQVNDHLKAGMQAFYEV 141
CuRO_3_FV_like cd14450
The third cupredoxin domain of coagulation factor V and similar proteins; Factor V is an ...
 375-575 1.15e-55

The third cupredoxin domain of coagulation factor V and similar proteins; Factor V is an essential coagulation protein with both pro- and anti-coagulant functions. Aberrant expression of human factor V can lead to bleeding or thromboembolic disease, which may be life-threatening. Bovine factor Va serves as the cofactor in the prothrombinase complex that results in a 300,000-fold increase in the rate of thrombin generation. Factor V is synthesized as a single polypeptide with six cupredoxin domains and a domain structure of 1-2-3-4-B-5-6-C1-C2, where 1-6 are cupredoxin domains, B is a domain with no known structural homologs and is dispensible for coagulant activity, and C are domains distantly related to discoidin protein-fold family members. Factor V has little activity prior to proteolytic cleavage by thrombin or FXa upon secretion. The resulting Factor Va is a heterodimer consisting of a heavy chain (1-2-3-4) and a light chain (5-6-C1-C2). This model represents the cupredoxin domain 3 of unprocessed Factor V or the heavy chain of Factor Va, and similar proteins including pseutarin C non-catalytic subunit. Pseutarin C is a prothrombin activator from Pseudonaja textilis venom.


Pssm-ID: 259992 [Multi-domain]  Cd Length: 181  Bit Score: 190.86  E-value: 1.15e-55
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1564327556  375 QYYIAAEEIIWDYGPTEINQysgkklVDDSVSDTFFDNRNDRIGGKYKKVQYVEYTDDTFTKRKERTSEEQhLGILGPII 454
Cdd:cd14450      4 EYFIAAEEVIWDYAPSIPEN------MDKRYRSQYLDNFSNNIGKKYKKAVFTQYEDGSFTKRLENPRPKE-EGILGPVI 76

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1564327556  455 RAEEEDTIKVTFRNKASRPYSIQPHGVQYNIEMDGTLYHNVLEESYTAKKLreikkearvveplpaalVRPDTTYKYEWV 534
Cdd:cd14450     77 RAQVRDTIKIVFKNKASRPYSIYPHGVTVSKAAEGASYPPDPRGNETQNKA-----------------VQPGETYTYKWN 139

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|.
gi 1564327556  535 VPKDAGPTEKDPDCITYMYYSAVDPIRDTNSGLVGPLLICK 575
Cdd:cd14450    140 ILETDEPTARDPRCLTRMYHSAVDITRDIASGLIGPLLICK 180
CuRO_2_ceruloplasmin cd11021
The second cupredoxin domain of Ceruloplasmin; Ceruloplasmin is a multicopper oxidase ...
 589-728 6.37e-55

The second 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 second cupredoxin domain of ceruloplasmin.


Pssm-ID: 259907 [Multi-domain]  Cd Length: 141  Bit Score: 187.29  E-value: 6.37e-55
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1564327556  589 KEFHLLATVFDENLSWYLDDNINRFAKQPKSVKKEDKDFQESNKMHSLNGYMYGNLKGLSMCKGDKVSWHLSGLGSEVDI 668
Cdd:cd11021      2 REFVLMFSVVDENLSWYLDENIKTYCSEPAKVDKDDEDFQESNKMHSINGYTFGNLPGLSMCAGDRVKWHLFGMGNEVDI 81

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1564327556  669 HGLYFEGNRFLYKDTRRDTINVFPHISHTVIMEPDSMGQFEVGCKTTDHYHGGMRANYTV 728
Cdd:cd11021     82 HSAFFHGQTLTDRGHRTDTINLFPATFVTAEMVAQNPGKWLLSCQVNDHLKAGMQAFYEV 141
CuRO_1_ceruloplasmin cd04222
The first cupredoxin domain of Ceruloplasmin; Ceruloplasmin is a multicopper oxidase essential ...
 374-575 6.44e-55

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


Pssm-ID: 259884 [Multi-domain]  Cd Length: 183  Bit Score: 188.78  E-value: 6.44e-55
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1564327556  374 RQYYIAAEEIIWDYGPTEINQYSGKKLVDDSVSDTFFDNRNDRIGGKYKKVQYVEYTDDTFTKRKERTseeQHLGILGPI 453
Cdd:cd04222      1 REYYIGIRETQWDYAPSGKNLITNQTFDDDEHASVFLKRGPDRIGRVYKKAVYLQYTDDTYRTEIEKP---VWLGFLGPI 77

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1564327556  454 IRAEEEDTIKVTFRNKASRPYSIQPHGVQYNIEMDGTLYHNvleesytAKKLREIKKEArvveplpaalVRPDTTYKYEW 533
Cdd:cd04222     78 LKAEVGDVIVVHLKNFASRPYSLHPHGVFYNKENEGALYPD-------NTSGFEKADDA----------VPPGGSYTYTW 140

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|..
gi 1564327556  534 VVPKDAGPTEKDPDCITYMYYSAVDPIRDTNSGLVGPLLICK 575
Cdd:cd04222    141 TVPEEQAPTKADANCLTRIYHSHIDAPKDIASGLIGPLIICK 182
CuRO_4_ceruloplasmin cd11022
The fourth cupredoxin domain of Ceruloplasmin; Ceruloplasmin is a multicopper oxidase ...
 929-1070 3.68e-54

The fourth 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 fourth cupredoxin domain of ceruloplasmin.


Pssm-ID: 259908 [Multi-domain]  Cd Length: 144  Bit Score: 184.99  E-value: 3.68e-54
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1564327556  929 EFALLFMVFDENESWYLDDNIKANVKNPPKALKEDEEFIESNKMHGINGLVYGNLKGLNMKVGDKVYWYLMGMGNEVDIH 1008
Cdd:cd11022      3 EFFLLFTVFDENESWYLDENIQQFTLDPRSVDKEDEDFQESNKMHSINGYMYGNQPGLDMCKGDTVSWHLFGLGTETDVH 82

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1564327556 1009 TAHFHGHSFDYKvsGTHRaDVFDLFPGTFQTVTMRPQYSGTWLLHCHVTDHIQAGMETTYTV 1070
Cdd:cd11022     83 GIYFSGNTFLLQ--GTRR-DTANLFPHTSVTAIMQPDNEGTFEVNCQTTDHYSAGMRQIYTV 141
CuRO_6_ceruloplasmin cd11012
The sixth cupredoxin domain of Ceruloplasmin; Ceruloplasmin is a multicopper oxidase essential ...
 220-357 7.55e-53

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: 181.61  E-value: 7.55e-53
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1564327556  220 YTLMFTVSDENLSWYLDENIKTYCTAPAKVNKDDEDFQESNKMHSINGYVFGNLPDLSMCMGNKIHWHLFGMGNEVDIHS 299
Cdd:cd11012      4 FALLFLVFDENESWYLDENIKTYSDHPEKVNKEDEEFIESNKMHAINGKVFGNLQGLTMHVGDEVYWYLMGMGNEIDIHT 83

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1564327556  300 AFFHGQILTEKQ---HHVDTISLFPATFVNVEMVADNPGQWLLSCQVNDHLEAGMQAIFEI 357
Cdd:cd11012     84 AHFHGHSFDYKHrgvYRSDVFDLFPGTFQTVEMIPRTPGTWLLHCHVTDHIHAGMETTYTV 144
CuRO_3_FV_like cd14450
The third cupredoxin domain of coagulation factor V and similar proteins; Factor V is an ...
 24-204 7.82e-53

The third cupredoxin domain of coagulation factor V and similar proteins; Factor V is an essential coagulation protein with both pro- and anti-coagulant functions. Aberrant expression of human factor V can lead to bleeding or thromboembolic disease, which may be life-threatening. Bovine factor Va serves as the cofactor in the prothrombinase complex that results in a 300,000-fold increase in the rate of thrombin generation. Factor V is synthesized as a single polypeptide with six cupredoxin domains and a domain structure of 1-2-3-4-B-5-6-C1-C2, where 1-6 are cupredoxin domains, B is a domain with no known structural homologs and is dispensible for coagulant activity, and C are domains distantly related to discoidin protein-fold family members. Factor V has little activity prior to proteolytic cleavage by thrombin or FXa upon secretion. The resulting Factor Va is a heterodimer consisting of a heavy chain (1-2-3-4) and a light chain (5-6-C1-C2). This model represents the cupredoxin domain 3 of unprocessed Factor V or the heavy chain of Factor Va, and similar proteins including pseutarin C non-catalytic subunit. Pseutarin C is a prothrombin activator from Pseudonaja textilis venom.


Pssm-ID: 259992 [Multi-domain]  Cd Length: 181  Bit Score: 182.77  E-value: 7.82e-53
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1564327556   24 EYFFAIKEIQWDYAPsgknliqnkTIKEDEEARV---FLERGEQRIGRVYRKAVYQQYTDSNYMQEIE--KPKWLGFLGP 98
Cdd:cd14450      4 EYFIAAEEVIWDYAP---------SIPENMDKRYrsqYLDNFSNNIGKKYKKAVFTQYEDGSFTKRLEnpRPKEEGILGP 74

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1564327556   99 LISAEENDIVVVHLKNMAKRAYSIHAHGLSYNKSFEGALYPDSSEKAEKADDSVAPGKSFSYVWTLPASHSPGKDDTNCL 178
Cdd:cd14450     75 VIRAQVRDTIKIVFKNKASRPYSIYPHGVTVSKAAEGASYPPDPRGNETQNKAVQPGETYTYKWNILETDEPTARDPRCL 154

                          170       180
                   ....*....|....*....|....*.
gi 1564327556  179 TRIYHSHVNAPKDIASGLIGPLIICK 204
Cdd:cd14450    155 TRMYHSAVDITRDIASGLIGPLLICK 180
CuRO_5_FV_like cd14451
The fifth cupredoxin domain of coagulation factor V and similar proteins; Factor V is an ...
 22-206 8.23e-53

The fifth cupredoxin domain of coagulation factor V and similar proteins; Factor V is an essential coagulation protein with both pro- and anti-coagulant functions. Aberrant expression of human factor V can lead to bleeding or thromboembolic disease, which may be life-threatening. Bovine factor Va serves as the cofactor in the prothrombinase complex that results in a 300,000-fold increase in the rate of thrombin generation. Factor V is synthesized as a single polypeptide with six cupredoxin domains and a domain structure of 1-2-3-4-B-5-6-C1-C2, where 1-6 are cupredoxin domains, B is a domain with no known structural homologs and is dispensible for coagulant activity, and C are domains distantly related to discoidin protein-fold family members. Factor V has little activity prior to proteolytic cleavage by thrombin or FXa upon secretion. The resulting Factor Va is a heterodimer consisting of a heavy chain (1-2-3-4) and a light chain (5-6-C1-C2). This model represents the cupredoxin domain 5 of unprocessed Factor V or the first cupredoxin domain of the light chain of coagulation factor Va, and similar proteins including pseutarin C non-catalytic subunit. Pseutarin C is a prothrombin activator from Pseudonaja textilis venom.


Pssm-ID: 259993 [Multi-domain]  Cd Length: 173  Bit Score: 182.35  E-value: 8.23e-53
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1564327556   22 TREYFFAIKEIQWDYAPSGKNLIQNKTIKEDEearvflergeqrigrVYRKAVYQQYTDSNYMQ---EIEKPKWLGFLGP 98
Cdd:cd14451      1 KRRYYIAAEEEEWDYAGYGKSRLDKTQNERDT---------------VFKKVVFRRYLDSTFSTpdiQGEYEEHLGILGP 65

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1564327556   99 LISAEENDIVVVHLKNMAKRAYSIHAHGLSYNKSFEGALYPDSSEKAEKADDSVAPGKSFSYVWTLPASHSPGKDDTNCL 178
Cdd:cd14451     66 VIRAEVDDVIQVFFKNLASRPYSLHAHGLSYEKSSEGLSYDDESPDWFKKDDAVQPNGTYTYVWYANPRSGPENNGSDCR 145

                          170       180
                   ....*....|....*....|....*...
gi 1564327556  179 TRIYHSHVNAPKDIASGLIGPLIICKKG 206
Cdd:cd14451    146 TWAYYSAVNPEKDIHSGLIGPLLICRKG 173
CuRO_5_FV_like cd14451
The fifth cupredoxin domain of coagulation factor V and similar proteins; Factor V is an ...
 374-575 1.56e-52

The fifth cupredoxin domain of coagulation factor V and similar proteins; Factor V is an essential coagulation protein with both pro- and anti-coagulant functions. Aberrant expression of human factor V can lead to bleeding or thromboembolic disease, which may be life-threatening. Bovine factor Va serves as the cofactor in the prothrombinase complex that results in a 300,000-fold increase in the rate of thrombin generation. Factor V is synthesized as a single polypeptide with six cupredoxin domains and a domain structure of 1-2-3-4-B-5-6-C1-C2, where 1-6 are cupredoxin domains, B is a domain with no known structural homologs and is dispensible for coagulant activity, and C are domains distantly related to discoidin protein-fold family members. Factor V has little activity prior to proteolytic cleavage by thrombin or FXa upon secretion. The resulting Factor Va is a heterodimer consisting of a heavy chain (1-2-3-4) and a light chain (5-6-C1-C2). This model represents the cupredoxin domain 5 of unprocessed Factor V or the first cupredoxin domain of the light chain of coagulation factor Va, and similar proteins including pseutarin C non-catalytic subunit. Pseutarin C is a prothrombin activator from Pseudonaja textilis venom.


Pssm-ID: 259993 [Multi-domain]  Cd Length: 173  Bit Score: 181.58  E-value: 1.56e-52
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1564327556  374 RQYYIAAEEIIWDYGPteinqYSGKKLVDDSVSDTffdnrndrigGKYKKVQYVEYTDDTFTKRKERTSEEQHLGILGPI 453
Cdd:cd14451      2 RRYYIAAEEEEWDYAG-----YGKSRLDKTQNERD----------TVFKKVVFRRYLDSTFSTPDIQGEYEEHLGILGPV 66

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1564327556  454 IRAEEEDTIKVTFRNKASRPYSIQPHGVQYNIEMDGTLYHNvlEESYTAKKLREIKkearvveplpaalvrPDTTYKYEW 533
Cdd:cd14451     67 IRAEVDDVIQVFFKNLASRPYSLHAHGLSYEKSSEGLSYDD--ESPDWFKKDDAVQ---------------PNGTYTYVW 129

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|..
gi 1564327556  534 VVPKDAGPTEKDPDCITYMYYSAVDPIRDTNSGLVGPLLICK 575
Cdd:cd14451    130 YANPRSGPENNGSDCRTWAYYSAVNPEKDIHSGLIGPLLICR 171
CuRO_3_FVIII_like cd04227
The third cupredoxin domain of coagulation factor VIII and similar proteins; Factor VIII ...
 376-575 9.60e-50

The third cupredoxin domain of coagulation factor VIII and similar proteins; Factor VIII functions in the factor X-activating complex of the intrinsic coagulation pathway. It facilitates blood clotting by acting as a cofactor for factor IXa. In the presence of Ca2+ and phospholipids, Factor VIII and IXa form a complex that converts factor X to the activated form Xa. A variety of mutations in the Factor VIII gene can cause hemophilia A, which typically requires replacement therapy with purified protein. Factor VIII is synthesized as a single polypeptide with six cupredoxin domains and a domain structure of 1-2-3-4-B-5-6-C1-C2, where 1-6 are cupredoxin domains, B is a domain with no known structural homologs and is dispensible for coagulant activity, and C are domains distantly related to discoidin protein-fold family members. Factor VIII is initially processed through proteolysis to generate a heterodimer consisting of a heavy chain (1-2-3-4) and a light chain (5-6-C1-C2), which circulates in a tight complex with von Willebrand factor (VWF). Further processing of the heavy chain produces activated factor VIIIa, a heterotrimer composed of polypeptides (1-2), (3-4), and the light chain. This model represents the cupredoxin domain 3 of unprocessed Factor VIII or the heavy chain of circulating Factor VIII, and similar proteins.


Pssm-ID: 259889 [Multi-domain]  Cd Length: 177  Bit Score: 173.96  E-value: 9.60e-50
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1564327556  376 YYIAAEEIIWDYGPTEINQysgkklVDDSVSDTFFDNRNDRIGGKYKKVQYVEYTDDTFTKRKERTSEEqhlGILGPIIR 455
Cdd:cd04227      5 HYIAAEELDWDYAPLLSST------DDRELQSRYLPTGPQRIGYKYKKVAFVEYTDKTFKRREAKQTEK---GILGPLLK 75

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1564327556  456 AEEEDTIKVTFRNKASRPYSIQPHGVQyniemdgtlyhNVleESYTAKKLREIKKEARVVEplpaalVRPDTTYKYEWVV 535
Cdd:cd04227     76 GEVGDQIHIMFKNTASRPYNIYPHGLT-----------SV--RPMYRSRNPAGEKDLKTMP------IGPGETFGYMWEL 136

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|
gi 1564327556  536 PKDAGPTEKDPDCITYMYYSAVDPIRDTNSGLVGPLLICK 575
Cdd:cd04227    137 TAEDGPTEEDPRCLTRLYQSTVDPERDLASGLIGPLLICK 176
CuRO_1_FVIII_like cd14452
The first cupredoxin domain of coagulation factor VIII and similar proteins; Factor VIII ...
 23-206 1.46e-49

The first cupredoxin domain of coagulation factor VIII and similar proteins; Factor VIII functions in the factor X-activating complex of the intrinsic coagulation pathway. It facilitates blood clotting by acting as a cofactor for factor IXa. In the presence of Ca2+ and phospholipids, Factor VIII and IXa form a complex that converts factor X to the activated form Xa. A variety of mutations in the Factor VIII gene can cause hemophilia A, which typically requires replacement therapy with purified protein. Factor VIII is synthesized as a single polypeptide with six cupredoxin domains and a domain structure of 1-2-3-4-B-5-6-C1-C2, where 1-6 are cupredoxin domains, B is a domain with no known structural homologs and is dispensible for coagulant activity, and C are domains distantly related to discoidin protein-fold family members. Factor VIII is initially processed through proteolysis to generate a heterodimer consisting of a heavy chain (1-2-3-4) and a light chain (5-6-C1-C2), which circulates in a tight complex with von Willebrand factor (VWF). Further processing of the heavy chain produces activated factor VIIIa, a heterotrimer composed of polypeptides (1-2), (3-4), and the light chain. This model represents the cupredoxin domain 1 of unprocessed Factor VIII or the heavy chain of circulating Factor VIII, and similar proteins.


Pssm-ID: 259994 [Multi-domain]  Cd Length: 173  Bit Score: 173.24  E-value: 1.46e-49
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1564327556   23 REYFFAIKEIQWDYAPSgknliqnktikEDEEARVFLERGEQRIGRVYRKAVYQQYTDSNYMQEIEKPKWLGFLGPLISA 102
Cdd:cd14452      1 RRYYIAAVEIGWDYIHS-----------DLGDPASEQRKKPKDIPQKYIKAVFVEYLDATFTVPKPRPAWMGLLGPTIVA 69

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1564327556  103 EENDIVVVHLKNMAKRAYSIHAHGLSYNKSFEGALYPDSSEKAEKADDSVAPGKSFSYVWTLPASHSPGKDDTNCLTRIY 182
Cdd:cd14452     70 EVGDTVVITFKNLASQPYSLHAVGVSYWKASEGAGYDDSTSQHEKEDDAVYPGGYHTYVWDISPKDGPTGSDPECLTYSY 149

                          170       180
                   ....*....|....*....|....
gi 1564327556  183 HSHVNAPKDIASGLIGPLIICKKG 206
Cdd:cd14452    150 SSQVDPVKDVNSGLIGALLVCRMG 173
CuRO_1_Ceruloplasmin_like_1 cd04229
cupredoxin domain of ceruloplasmin homologs; Uncharacterized subfamily of ceruloplasmin ...
 374-573 1.86e-49

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: 172.99  E-value: 1.86e-49
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1564327556  374 RQYYIAAEEIIWDYGPTEINQ-----YSGKKLVDDSVSDTffdnrndRIGGKYKKVQYVEYTDDTFTKRKertSEEQHLG 448
Cdd:cd04229      1 RTYYIAAEEVDWDYAPSGKNKcclgdDLEVSTLDSQPGPY-------TIGSTYTKARYREYTDNSFSTPK---PTPAYLG 70

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1564327556  449 ILGPIIRAEEEDTIKVTFRNKASR-PYSIQPHGVQYNIEMDGTLYHNvleesytakklreikkearvveplpAALVRPDT 527
Cdd:cd04229     71 ILGPVIRAEVGDTIKVVFKNNLDEfPVNMHPHGGLYSKDNEGTTDGA-------------------------GDVVAPGE 125

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*.
gi 1564327556  528 TYKYEWVVPKDAGPTEKDPDCITYMYYSAVDPIRDTNSGLVGPLLI 573
Cdd:cd04229    126 TYTYRWIVPEDAGPGPGDPSSRLWLYHSHVDVFAHTNAGLVGPIIV 171
CuRO_1_FV_like cd04226
The first cupredoxin domain of coagulation factor VIII and similar proteins; Factor V is an ...
 23-206 5.59e-49

The first cupredoxin domain of coagulation factor VIII and similar proteins; Factor V is an essential coagulation protein with both pro- and anti-coagulant functions. Aberrant expression of human factor V can lead to bleeding or thromboembolic disease, which may be life-threatening. Bovine factor Va serves as the cofactor in the prothrombinase complex that results in a 300,000-fold increase in the rate of thrombin generation. Factor V is synthesized as a single polypeptide with six cupredoxin domains and a domain structure of 1-2-3-4-B-5-6-C1-C2, where 1-6 are cupredoxin domains, B is a domain with no known structural homologs and is dispensible for coagulant activity, and C are domains distantly related to discoidin protein-fold family members. Factor V has little activity prior to proteolytic cleavage by thrombin or FXa upon secretion. The resulting Factor Va is a heterodimer consisting of a heavy chain (1-2-3-4) and a light chain (5-6-C1-C2). This model represents the cupredoxin domain 1 of unprocessed Factor V or the heavy chain of Factor Va, and similar proteins including pseutarin C non-catalytic subunit. Pseutarin C is a prothrombin activator from Pseudonaja textilis venom.


Pssm-ID: 259888 [Multi-domain]  Cd Length: 165  Bit Score: 171.20  E-value: 5.59e-49
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1564327556   23 REYFFAIKEIQWDYAPsgknliqnktikEDEEARVflergeQRIGRVYRKAVYQQYtDSNYMQEIEKPKWLGFLGPLISA 102
Cdd:cd04226      1 REYYIAAQNIDWDYTP------------QSEELRL------KRSEQSFKKIVYREY-EEGFKKEKPADLSSGLLGPTLRA 61

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1564327556  103 EENDIVVVHLKNMAKRAYSIHAHGLSYNKSFEGALYPDSSEKAEKADDSVAPGKSFSYVWTLPASHSPGKDDTNCLTRIY 182
Cdd:cd04226     62 EVGDTLIVHFKNMADKPLSIHPQGIAYGKKSEGSLYSDNTSPVEKLDDAVQPGQEYTYVWDITEEVGPTEADPPCLTYIY 141

                          170       180
                   ....*....|....*....|....
gi 1564327556  183 HSHVNAPKDIASGLIGPLIICKKG 206
Cdd:cd04226    142 YSHVNMVRDFNSGLIGALLICKKG 165
CuRO_3_FV_like cd14450
The third cupredoxin domain of coagulation factor V and similar proteins; Factor V is an ...
 747-914 9.27e-48

The third cupredoxin domain of coagulation factor V and similar proteins; Factor V is an essential coagulation protein with both pro- and anti-coagulant functions. Aberrant expression of human factor V can lead to bleeding or thromboembolic disease, which may be life-threatening. Bovine factor Va serves as the cofactor in the prothrombinase complex that results in a 300,000-fold increase in the rate of thrombin generation. Factor V is synthesized as a single polypeptide with six cupredoxin domains and a domain structure of 1-2-3-4-B-5-6-C1-C2, where 1-6 are cupredoxin domains, B is a domain with no known structural homologs and is dispensible for coagulant activity, and C are domains distantly related to discoidin protein-fold family members. Factor V has little activity prior to proteolytic cleavage by thrombin or FXa upon secretion. The resulting Factor Va is a heterodimer consisting of a heavy chain (1-2-3-4) and a light chain (5-6-C1-C2). This model represents the cupredoxin domain 3 of unprocessed Factor V or the heavy chain of Factor Va, and similar proteins including pseutarin C non-catalytic subunit. Pseutarin C is a prothrombin activator from Pseudonaja textilis venom.


Pssm-ID: 259992 [Multi-domain]  Cd Length: 181  Bit Score: 168.52  E-value: 9.27e-48
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1564327556  747 YYIAAVEMDWDYSPTRTweEKMNNGLKeskgNEFLKKEGKFIGSKYKKVLYREYTDETFTKPKErSADMEHLGIMGPMIH 826
Cdd:cd14450      5 YFIAAEEVIWDYAPSIP--ENMDKRYR----SQYLDNFSNNIGKKYKKAVFTQYEDGSFTKRLE-NPRPKEEGILGPVIR 77

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1564327556  827 GKVGEKVKIVFKNMAKRPYSIHAHGV---------------KTESPQVALTRPGETQTYTWYLPKNSGPTEEQEECSVGA 891
Cdd:cd14450     78 AQVRDTIKIVFKNKASRPYSIYPHGVtvskaaegasyppdpRGNETQNKAVQPGETYTYKWNILETDEPTARDPRCLTRM 157

                          170       180
                   ....*....|....*....|...
gi 1564327556  892 YYSAVDVIKDMYSGLIGPLIVCK 914
Cdd:cd14450    158 YHSAVDITRDIASGLIGPLLICK 180
CuRO_1_Ceruloplasmin_like_1 cd04229
cupredoxin domain of ceruloplasmin homologs; Uncharacterized subfamily of ceruloplasmin ...
 23-206 2.12e-47

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: 167.21  E-value: 2.12e-47
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1564327556   23 REYFFAIKEIQWDYAPSGKNLIQNKTIKEDEEarVFLERGEQRIGRVYRKAVYQQYTDSNYMQEIEKPKWLGFLGPLISA 102
Cdd:cd04229      1 RTYYIAAEEVDWDYAPSGKNKCCLGDDLEVST--LDSQPGPYTIGSTYTKARYREYTDNSFSTPKPTPAYLGILGPVIRA 78

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1564327556  103 EENDIVVVHLKNMAKR-AYSIHAHGLSYNKSFEGAlypdssekAEKADDSVAPGKSFSYVWTLPASHSPGKDDTNCLTRI 181
Cdd:cd04229     79 EVGDTIKVVFKNNLDEfPVNMHPHGGLYSKDNEGT--------TDGAGDVVAPGETYTYRWIVPEDAGPGPGDPSSRLWL 150

                          170       180
                   ....*....|....*....|....*
gi 1564327556  182 YHSHVNAPKDIASGLIGPLIICKKG 206
Cdd:cd04229    151 YHSHVDVFAHTNAGLVGPIIVTSKG 175
CuRO_5_FV_like cd14451
The fifth cupredoxin domain of coagulation factor V and similar proteins; Factor V is an ...
 744-915 1.25e-46

The fifth cupredoxin domain of coagulation factor V and similar proteins; Factor V is an essential coagulation protein with both pro- and anti-coagulant functions. Aberrant expression of human factor V can lead to bleeding or thromboembolic disease, which may be life-threatening. Bovine factor Va serves as the cofactor in the prothrombinase complex that results in a 300,000-fold increase in the rate of thrombin generation. Factor V is synthesized as a single polypeptide with six cupredoxin domains and a domain structure of 1-2-3-4-B-5-6-C1-C2, where 1-6 are cupredoxin domains, B is a domain with no known structural homologs and is dispensible for coagulant activity, and C are domains distantly related to discoidin protein-fold family members. Factor V has little activity prior to proteolytic cleavage by thrombin or FXa upon secretion. The resulting Factor Va is a heterodimer consisting of a heavy chain (1-2-3-4) and a light chain (5-6-C1-C2). This model represents the cupredoxin domain 5 of unprocessed Factor V or the first cupredoxin domain of the light chain of coagulation factor Va, and similar proteins including pseutarin C non-catalytic subunit. Pseutarin C is a prothrombin activator from Pseudonaja textilis venom.


Pssm-ID: 259993 [Multi-domain]  Cd Length: 173  Bit Score: 164.63  E-value: 1.25e-46
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1564327556  744 QKKYYIAAVEMDWDYSptrtweekmnnGLKESKgnefLKKEGKFIGSKYKKVLYREYTDETFTKPKERSADMEHLGIMGP 823
Cdd:cd14451      1 KRRYYIAAEEEEWDYA-----------GYGKSR----LDKTQNERDTVFKKVVFRRYLDSTFSTPDIQGEYEEHLGILGP 65

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1564327556  824 MIHGKVGEKVKIVFKNMAKRPYSIHAHGVKTESPQVALT---------------RPGETQTYTWYLPKNSGPTEEQEECS 888
Cdd:cd14451     66 VIRAEVDDVIQVFFKNLASRPYSLHAHGLSYEKSSEGLSyddespdwfkkddavQPNGTYTYVWYANPRSGPENNGSDCR 145

                          170       180
                   ....*....|....*....|....*..
gi 1564327556  889 VGAYYSAVDVIKDMYSGLIGPLIVCKK 915
Cdd:cd14451    146 TWAYYSAVNPEKDIHSGLIGPLLICRK 172
CuRO_6_ceruloplasmin cd11012
The sixth cupredoxin domain of Ceruloplasmin; Ceruloplasmin is a multicopper oxidase essential ...
 588-728 1.52e-45

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: 160.80  E-value: 1.52e-45
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1564327556  588 KKEFHLLATVFDENLSWYLDDNINRFAKQPKSVKKEDKDFQESNKMHSLNGYMYGNLKGLSMCKGDKVSWHLSGLGSEVD 667
Cdd:cd11012      1 KLEFALLFLVFDENESWYLDENIKTYSDHPEKVNKEDEEFIESNKMHAINGKVFGNLQGLTMHVGDEVYWYLMGMGNEID 80

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1564327556  668 IHGLYFEGNRFLYKDT---RRDTINVFPHISHTVIMEPDSMGQFEVGCKTTDHYHGGMRANYTV 728
Cdd:cd11012     81 IHTAHFHGHSFDYKHRgvyRSDVFDLFPGTFQTVEMIPRTPGTWLLHCHVTDHIHAGMETTYTV 144
CuRO_5_FVIII_like cd04228
The fifth cupredoxin domain of coagulation factor VIII and similar proteins; Factor VIII ...
 745-915 4.11e-45

The fifth cupredoxin domain of coagulation factor VIII and similar proteins; Factor VIII functions in the factor X-activating complex of the intrinsic coagulation pathway. It facilitates blood clotting by acting as a cofactor for factor IXa. In the presence of Ca2+ and phospholipids, Factor VIII and IXa form a complex that converts factor X to the activated form Xa. A variety of mutations in the Factor VIII gene can cause hemophilia A, which typically requires replacement therapy with purified protein. Factor VIII is synthesized as a single polypeptide with six cupredoxin domains and a domain structure of 1-2-3-4-B-5-6-C1-C2, where 1-6 are cupredoxin domains, B is a domain with no known structural homologs and is dispensible for coagulant activity, and C are domains distantly related to discoidin protein-fold family members. Factor VIII is initially processed through proteolysis to generate a heterodimer consisting of a heavy chain (1-2-3-4) and a light chain (5-6-C1-C2), which circulates in a tight complex with von Willebrand factor (VWF). Further processing of the heavy chain produces activated factor VIIIa, a heterotrimer composed of polypeptides (1-2), (3-4), and the light chain. This model represents the cupredoxin domain 5 of unprocessed Factor VIII or the first cupredoxin domain of the light chain of circulating Factor VIII, and similar proteins.


Pssm-ID: 259890 [Multi-domain]  Cd Length: 169  Bit Score: 160.44  E-value: 4.11e-45
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1564327556  745 KKYYIAAVEMDWDYSPTRTWEEkmnngLKESKGNEFLKKEGKfigsKYKKVLYREYTDETFTKPKERSADMEHLGIMGPM 824
Cdd:cd04228      2 RHYFIAAVEVLWDYGMQRPQHF-----LRARDPNRGRRKSVP----QYKKVVFREYLDGSFTQPVYRGELDEHLGILGPY 72

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1564327556  825 IHGKVGEKVKIVFKNMAKRPYSIHAHGVKTESPQVALTR-----PGETQTYTWYLPKNSGPTEEQEECSVGAYYSAVDVI 899
Cdd:cd04228     73 IRAEVEDNIMVTFKNLASRPYSFHSSLISYEEDQRAEPRgnfvqPGEVQTYSWKVLHQMAPTKQEFDCKAWAYFSNVDLE 152

                          170
                   ....*....|....*.
gi 1564327556  900 KDMYSGLIGPLIVCKK 915
Cdd:cd04228    153 KDLHSGLIGPLIICKT 168
CuRO_3_FVIII_like cd04227
The third cupredoxin domain of coagulation factor VIII and similar proteins; Factor VIII ...
 747-915 6.15e-45

The third cupredoxin domain of coagulation factor VIII and similar proteins; Factor VIII functions in the factor X-activating complex of the intrinsic coagulation pathway. It facilitates blood clotting by acting as a cofactor for factor IXa. In the presence of Ca2+ and phospholipids, Factor VIII and IXa form a complex that converts factor X to the activated form Xa. A variety of mutations in the Factor VIII gene can cause hemophilia A, which typically requires replacement therapy with purified protein. Factor VIII is synthesized as a single polypeptide with six cupredoxin domains and a domain structure of 1-2-3-4-B-5-6-C1-C2, where 1-6 are cupredoxin domains, B is a domain with no known structural homologs and is dispensible for coagulant activity, and C are domains distantly related to discoidin protein-fold family members. Factor VIII is initially processed through proteolysis to generate a heterodimer consisting of a heavy chain (1-2-3-4) and a light chain (5-6-C1-C2), which circulates in a tight complex with von Willebrand factor (VWF). Further processing of the heavy chain produces activated factor VIIIa, a heterotrimer composed of polypeptides (1-2), (3-4), and the light chain. This model represents the cupredoxin domain 3 of unprocessed Factor VIII or the heavy chain of circulating Factor VIII, and similar proteins.


Pssm-ID: 259889 [Multi-domain]  Cd Length: 177  Bit Score: 160.10  E-value: 6.15e-45
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1564327556  747 YYIAAVEMDWDYSPTRTweekmnNGLKESKGNEFLKKEGKFIGSKYKKVLYREYTDETFTKpkeRSADMEHLGIMGPMIH 826
Cdd:cd04227      5 HYIAAEELDWDYAPLLS------STDDRELQSRYLPTGPQRIGYKYKKVAFVEYTDKTFKR---REAKQTEKGILGPLLK 75

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1564327556  827 GKVGEKVKIVFKNMAKRPYSIHAHGVKTESPQVALTR-------------PGETQTYTWYLPKNSGPTEEQEECSVGAYY 893
Cdd:cd04227     76 GEVGDQIHIMFKNTASRPYNIYPHGLTSVRPMYRSRNpagekdlktmpigPGETFGYMWELTAEDGPTEEDPRCLTRLYQ 155

                          170       180
                   ....*....|....*....|..
gi 1564327556  894 SAVDVIKDMYSGLIGPLIVCKK 915
Cdd:cd04227    156 STVDPERDLASGLIGPLLICKK 177
CuRO_1_FV_like cd04226
The first cupredoxin domain of coagulation factor VIII and similar proteins; Factor V is an ...
 374-575 1.60e-43

The first cupredoxin domain of coagulation factor VIII and similar proteins; Factor V is an essential coagulation protein with both pro- and anti-coagulant functions. Aberrant expression of human factor V can lead to bleeding or thromboembolic disease, which may be life-threatening. Bovine factor Va serves as the cofactor in the prothrombinase complex that results in a 300,000-fold increase in the rate of thrombin generation. Factor V is synthesized as a single polypeptide with six cupredoxin domains and a domain structure of 1-2-3-4-B-5-6-C1-C2, where 1-6 are cupredoxin domains, B is a domain with no known structural homologs and is dispensible for coagulant activity, and C are domains distantly related to discoidin protein-fold family members. Factor V has little activity prior to proteolytic cleavage by thrombin or FXa upon secretion. The resulting Factor Va is a heterodimer consisting of a heavy chain (1-2-3-4) and a light chain (5-6-C1-C2). This model represents the cupredoxin domain 1 of unprocessed Factor V or the heavy chain of Factor Va, and similar proteins including pseutarin C non-catalytic subunit. Pseutarin C is a prothrombin activator from Pseudonaja textilis venom.


Pssm-ID: 259888 [Multi-domain]  Cd Length: 165  Bit Score: 155.79  E-value: 1.60e-43
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1564327556  374 RQYYIAAEEIIWDYGPteinQYSGKKLvddsvsdtffdnrnDRIGGKYKKVQYVEYTDDtFTKRKERTSEEqhlGILGPI 453
Cdd:cd04226      1 REYYIAAQNIDWDYTP----QSEELRL--------------KRSEQSFKKIVYREYEEG-FKKEKPADLSS---GLLGPT 58

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1564327556  454 IRAEEEDTIKVTFRNKASRPYSIQPHGVQYNIEMDGTLYHNvleesytakklreikkEARVVEPLPAAlVRPDTTYKYEW 533
Cdd:cd04226     59 LRAEVGDTLIVHFKNMADKPLSIHPQGIAYGKKSEGSLYSD----------------NTSPVEKLDDA-VQPGQEYTYVW 121

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|..
gi 1564327556  534 VVPKDAGPTEKDPDCITYMYYSAVDPIRDTNSGLVGPLLICK 575
Cdd:cd04226    122 DITEEVGPTEADPPCLTYIYYSHVNMVRDFNSGLIGALLICK 163
CuRO_5_FVIII_like cd04228
The fifth cupredoxin domain of coagulation factor VIII and similar proteins; Factor VIII ...
 373-576 2.80e-43

The fifth cupredoxin domain of coagulation factor VIII and similar proteins; Factor VIII functions in the factor X-activating complex of the intrinsic coagulation pathway. It facilitates blood clotting by acting as a cofactor for factor IXa. In the presence of Ca2+ and phospholipids, Factor VIII and IXa form a complex that converts factor X to the activated form Xa. A variety of mutations in the Factor VIII gene can cause hemophilia A, which typically requires replacement therapy with purified protein. Factor VIII is synthesized as a single polypeptide with six cupredoxin domains and a domain structure of 1-2-3-4-B-5-6-C1-C2, where 1-6 are cupredoxin domains, B is a domain with no known structural homologs and is dispensible for coagulant activity, and C are domains distantly related to discoidin protein-fold family members. Factor VIII is initially processed through proteolysis to generate a heterodimer consisting of a heavy chain (1-2-3-4) and a light chain (5-6-C1-C2), which circulates in a tight complex with von Willebrand factor (VWF). Further processing of the heavy chain produces activated factor VIIIa, a heterotrimer composed of polypeptides (1-2), (3-4), and the light chain. This model represents the cupredoxin domain 5 of unprocessed Factor VIII or the first cupredoxin domain of the light chain of circulating Factor VIII, and similar proteins.


Pssm-ID: 259890 [Multi-domain]  Cd Length: 169  Bit Score: 155.04  E-value: 2.80e-43
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1564327556  373 VRQYYIAAEEIIWDYGpteinqysgkklvdDSVSDTFFDNRNDRIGGK-----YKKVQYVEYTDDTFTKRKERTSEEQHL 447
Cdd:cd04228      1 IRHYFIAAVEVLWDYG--------------MQRPQHFLRARDPNRGRRksvpqYKKVVFREYLDGSFTQPVYRGELDEHL 66

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1564327556  448 GILGPIIRAEEEDTIKVTFRNKASRPYSIQPHGVQYniemdgtlyhnvlEESYTAKKLREIkkearvveplpaalVRPDT 527
Cdd:cd04228     67 GILGPYIRAEVEDNIMVTFKNLASRPYSFHSSLISY-------------EEDQRAEPRGNF--------------VQPGE 119

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*....
gi 1564327556  528 TYKYEWVVPKDAGPTEKDPDCITYMYYSAVDPIRDTNSGLVGPLLICKP 576
Cdd:cd04228    120 VQTYSWKVLHQMAPTKQEFDCKAWAYFSNVDLEKDLHSGLIGPLIICKT 168
CuRO_1_ceruloplasmin cd04222
The first cupredoxin domain of Ceruloplasmin; Ceruloplasmin is a multicopper oxidase essential ...
 745-915 7.74e-43

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


Pssm-ID: 259884 [Multi-domain]  Cd Length: 183  Bit Score: 154.50  E-value: 7.74e-43
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1564327556  745 KKYYIAAVEMDWDYSPTRTwEEKMNNGLKESK-GNEFLKKEGKFIGSKYKKVLYREYTDETFTKPKERSAdmeHLGIMGP 823
Cdd:cd04222      1 REYYIGIRETQWDYAPSGK-NLITNQTFDDDEhASVFLKRGPDRIGRVYKKAVYLQYTDDTYRTEIEKPV---WLGFLGP 76

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1564327556  824 MIHGKVGEKVKIVFKNMAKRPYSIHAHGVK-------------TESPQVA--LTRPGETQTYTWYLPKNSGPTEEQEECS 888
Cdd:cd04222     77 ILKAEVGDVIVVHLKNFASRPYSLHPHGVFynkenegalypdnTSGFEKAddAVPPGGSYTYTWTVPEEQAPTKADANCL 156

                          170       180
                   ....*....|....*....|....*..
gi 1564327556  889 VGAYYSAVDVIKDMYSGLIGPLIVCKK 915
Cdd:cd04222    157 TRIYHSHIDAPKDIASGLIGPLIICKK 183
CuRO_5_ceruloplasmin cd04225
The fifth cupredoxin domain of Ceruloplasmin; Ceruloplasmin is a multicopper oxidase essential ...
 23-205 1.98e-42

The fifth 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 fifth cupredoxin domain of ceruloplasmin.


Pssm-ID: 259887 [Multi-domain]  Cd Length: 171  Bit Score: 152.62  E-value: 1.98e-42
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1564327556   23 REYFFAIKEIQWDYAPSGKNLIQNKTIKEDEEARVFLERGEQRIGRVYRKAVYQQYTDSNYMQEIEKP---KWLGFLGPL 99
Cdd:cd04225      1 RTYYIAAEEVEWDYSPQRTWEQELHNTHEESPGNAFLNKGDKFIGSKYKKVVYREYTDDTFSVPKERTaeeEHLGILGPL 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1564327556  100 ISAEENDIVVVHLKNMAKRAYSIHAHGLSynksfegalyPDSSEKAekaddSVAPGKSFSYVWTLPASHSPGKDDTNCLT 179
Cdd:cd04225     81 IHAEVGEKVKIVFKNMASRPYSIHAHGVK----------TDSSWVA-----PTEPGETQTYTWKIPERSGPGVEDSNCIS 145

                          170       180
                   ....*....|....*....|....*.
gi 1564327556  180 RIYHSHVNAPKDIASGLIGPLIICKK 205
Cdd:cd04225    146 WAYYSTVDQIKDLYSGLIGPLVICRR 171
CuRO_6_FVIII_like cd11018
The sixth cupredoxin domain of coagulation factor VIII and similar proteins; Factor VIII ...
 927-1070 3.96e-42

The sixth cupredoxin domain of coagulation factor VIII and similar proteins; Factor VIII functions in the factor X-activating complex of the intrinsic coagulation pathway. It facilitates blood clotting by acting as a cofactor for factor IXa. In the presence of Ca2+ and phospholipids, Factor VIII and IXa form a complex that converts factor X to the activated form Xa. A variety of mutations in the Factor VIII gene can cause hemophilia A, which typically requires replacement therapy with purified protein. Factor VIII is synthesized as a single polypeptide with six cupredoxin domains and a domain structure of 1-2-3-4-B-5-6-C1-C2, where 1-6 are cupredoxin domains, B is a domain with no known structural homologs and is dispensible for coagulant activity, and C are domains distantly related to discoidin protein-fold family members. Factor VIII is initially processed through proteolysis to generate a heterodimer consisting of a heavy chain (1-2-3-4) and a light chain (5-6-C1-C2), which circulates in a tight complex with von Willebrand factor (VWF). Further processing of the heavy chain produces activated factor VIIIa, a heterotrimer composed of polypeptides (1-2), (3-4), and the light chain. This model represents the cupredoxin domain 6 of unprocessed Factor VIII or the second cupredoxin domain the light chain of circulating Factor VIII, and similar proteins.


Pssm-ID: 259904 [Multi-domain]  Cd Length: 144  Bit Score: 150.80  E-value: 3.96e-42
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1564327556  927 IEEFALLFMVFDENESWYLDDNIKANVKNPPKALKEDEEFIESNKMHGINGLVYGNLKGLNMKVGDKVYWYLMGMGNEVD 1006
Cdd:cd11018      1 VQEFALLFTIFDETKSWYFEENMRRNCRPPCHIQTQDPWFHINNKFHAINGYVADTLPGLVMAQHQRIRWHLLNMGSDEE 80

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1564327556 1007 IHTAHFHGHSFDYKVSGTHRADVFDLFPGTFQTVTMRPQYSGTWLLHCHVTDHIQAGMETTYTV 1070
Cdd:cd11018     81 IHSVHFHGLPFTVRAKKEYRMGVYNLYPGVFGTVEMRPSTAGIWLVECTVGEHLLAGMSALFLV 144
CuRO_1_FVIII_like cd14452
The first cupredoxin domain of coagulation factor VIII and similar proteins; Factor VIII ...
 374-576 1.83e-41

The first cupredoxin domain of coagulation factor VIII and similar proteins; Factor VIII functions in the factor X-activating complex of the intrinsic coagulation pathway. It facilitates blood clotting by acting as a cofactor for factor IXa. In the presence of Ca2+ and phospholipids, Factor VIII and IXa form a complex that converts factor X to the activated form Xa. A variety of mutations in the Factor VIII gene can cause hemophilia A, which typically requires replacement therapy with purified protein. Factor VIII is synthesized as a single polypeptide with six cupredoxin domains and a domain structure of 1-2-3-4-B-5-6-C1-C2, where 1-6 are cupredoxin domains, B is a domain with no known structural homologs and is dispensible for coagulant activity, and C are domains distantly related to discoidin protein-fold family members. Factor VIII is initially processed through proteolysis to generate a heterodimer consisting of a heavy chain (1-2-3-4) and a light chain (5-6-C1-C2), which circulates in a tight complex with von Willebrand factor (VWF). Further processing of the heavy chain produces activated factor VIIIa, a heterotrimer composed of polypeptides (1-2), (3-4), and the light chain. This model represents the cupredoxin domain 1 of unprocessed Factor VIII or the heavy chain of circulating Factor VIII, and similar proteins.


Pssm-ID: 259994 [Multi-domain]  Cd Length: 173  Bit Score: 150.13  E-value: 1.83e-41
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1564327556  374 RQYYIAAEEIIWDYGPTEINQYSGKKLVDDSVsdtffdnrndrIGGKYKKVQYVEYTDDTFTKRKERTSeeqHLGILGPI 453
Cdd:cd14452      1 RRYYIAAVEIGWDYIHSDLGDPASEQRKKPKD-----------IPQKYIKAVFVEYLDATFTVPKPRPA---WMGLLGPT 66

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1564327556  454 IRAEEEDTIKVTFRNKASRPYSIQPHGVQYNIEMDGTLYhnvleESYTAKKLREIKKearvveplpaalVRPDTTYKYEW 533
Cdd:cd14452     67 IVAEVGDTVVITFKNLASQPYSLHAVGVSYWKASEGAGY-----DDSTSQHEKEDDA------------VYPGGYHTYVW 129

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|...
gi 1564327556  534 VVPKDAGPTEKDPDCITYMYYSAVDPIRDTNSGLVGPLLICKP 576
Cdd:cd14452    130 DISPKDGPTGSDPECLTYSYSSQVDPVKDVNSGLIGALLVCRM 172
CuRO_3_FVIII_like cd04227
The third cupredoxin domain of coagulation factor VIII and similar proteins; Factor VIII ...
 22-205 2.04e-41

The third cupredoxin domain of coagulation factor VIII and similar proteins; Factor VIII functions in the factor X-activating complex of the intrinsic coagulation pathway. It facilitates blood clotting by acting as a cofactor for factor IXa. In the presence of Ca2+ and phospholipids, Factor VIII and IXa form a complex that converts factor X to the activated form Xa. A variety of mutations in the Factor VIII gene can cause hemophilia A, which typically requires replacement therapy with purified protein. Factor VIII is synthesized as a single polypeptide with six cupredoxin domains and a domain structure of 1-2-3-4-B-5-6-C1-C2, where 1-6 are cupredoxin domains, B is a domain with no known structural homologs and is dispensible for coagulant activity, and C are domains distantly related to discoidin protein-fold family members. Factor VIII is initially processed through proteolysis to generate a heterodimer consisting of a heavy chain (1-2-3-4) and a light chain (5-6-C1-C2), which circulates in a tight complex with von Willebrand factor (VWF). Further processing of the heavy chain produces activated factor VIIIa, a heterotrimer composed of polypeptides (1-2), (3-4), and the light chain. This model represents the cupredoxin domain 3 of unprocessed Factor VIII or the heavy chain of circulating Factor VIII, and similar proteins.


Pssm-ID: 259889 [Multi-domain]  Cd Length: 177  Bit Score: 150.08  E-value: 2.04e-41
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1564327556   22 TREYFFAIKEIQWDYAPsgknliqNKTIKEDEE-ARVFLERGEQRIGRVYRKAVYQQYTDSNYMQEIEKPKWLGFLGPLI 100
Cdd:cd04227      2 TWEHYIAAEELDWDYAP-------LLSSTDDRElQSRYLPTGPQRIGYKYKKVAFVEYTDKTFKRREAKQTEKGILGPLL 74

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1564327556  101 SAEENDIVVVHLKNMAKRAYSIHAHGLSYNKSFEgALYPDSSEKAEKaDDSVAPGKSFSYVWTLPASHSPGKDDTNCLTR 180
Cdd:cd04227     75 KGEVGDQIHIMFKNTASRPYNIYPHGLTSVRPMY-RSRNPAGEKDLK-TMPIGPGETFGYMWELTAEDGPTEEDPRCLTR 152

                          170       180
                   ....*....|....*....|....*
gi 1564327556  181 IYHSHVNAPKDIASGLIGPLIICKK 205
Cdd:cd04227    153 LYQSTVDPERDLASGLIGPLLICKK 177
CuRO_1_Ceruloplasmin_like_1 cd04229
cupredoxin domain of ceruloplasmin homologs; Uncharacterized subfamily of ceruloplasmin ...
 747-915 1.81e-40

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: 147.18  E-value: 1.81e-40
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1564327556  747 YYIAAVEMDWDYSPTrtweekmnNGLKESKGNEFLKKEGKF------IGSKYKKVLYREYTDETFTKPKersADMEHLGI 820
Cdd:cd04229      3 YYIAAEEVDWDYAPS--------GKNKCCLGDDLEVSTLDSqpgpytIGSTYTKARYREYTDNSFSTPK---PTPAYLGI 71

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1564327556  821 MGPMIHGKVGEKVKIVFKNMAKR-PYSIHAHGV-------KTESPQVALTRPGETQTYTWYLPKNSGPTEEQEECSVGAY 892
Cdd:cd04229     72 LGPVIRAEVGDTIKVVFKNNLDEfPVNMHPHGGlyskdneGTTDGAGDVVAPGETYTYRWIVPEDAGPGPGDPSSRLWLY 151

                          170       180
                   ....*....|....*....|...
gi 1564327556  893 YSAVDVIKDMYSGLIGPLIVCKK 915
Cdd:cd04229    152 HSHVDVFAHTNAGLVGPIIVTSK 174
CuRO_6_FVIII_like cd11018
The sixth cupredoxin domain of coagulation factor VIII and similar proteins; Factor VIII ...
 220-355 1.37e-38

The sixth cupredoxin domain of coagulation factor VIII and similar proteins; Factor VIII functions in the factor X-activating complex of the intrinsic coagulation pathway. It facilitates blood clotting by acting as a cofactor for factor IXa. In the presence of Ca2+ and phospholipids, Factor VIII and IXa form a complex that converts factor X to the activated form Xa. A variety of mutations in the Factor VIII gene can cause hemophilia A, which typically requires replacement therapy with purified protein. Factor VIII is synthesized as a single polypeptide with six cupredoxin domains and a domain structure of 1-2-3-4-B-5-6-C1-C2, where 1-6 are cupredoxin domains, B is a domain with no known structural homologs and is dispensible for coagulant activity, and C are domains distantly related to discoidin protein-fold family members. Factor VIII is initially processed through proteolysis to generate a heterodimer consisting of a heavy chain (1-2-3-4) and a light chain (5-6-C1-C2), which circulates in a tight complex with von Willebrand factor (VWF). Further processing of the heavy chain produces activated factor VIIIa, a heterotrimer composed of polypeptides (1-2), (3-4), and the light chain. This model represents the cupredoxin domain 6 of unprocessed Factor VIII or the second cupredoxin domain the light chain of circulating Factor VIII, and similar proteins.


Pssm-ID: 259904 [Multi-domain]  Cd Length: 144  Bit Score: 140.79  E-value: 1.37e-38
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1564327556  220 YTLMFTVSDENLSWYLDENIKTYCTAPAKVNKDDEDFQESNKMHSINGYVFGNLPDLSMCMGNKIHWHLFGMGNEVDIHS 299
Cdd:cd11018      4 FALLFTIFDETKSWYFEENMRRNCRPPCHIQTQDPWFHINNKFHAINGYVADTLPGLVMAQHQRIRWHLLNMGSDEEIHS 83

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 1564327556  300 AFFHGQILT---EKQHHVDTISLFPATFVNVEMVADNPGQWLLSCQVNDHLEAGMQAIF 355
Cdd:cd11018     84 VHFHGLPFTvraKKEYRMGVYNLYPGVFGTVEMRPSTAGIWLVECTVGEHLLAGMSALF 142
CuRO_1_FVIII_like cd14452
The first cupredoxin domain of coagulation factor VIII and similar proteins; Factor VIII ...
 745-916 3.12e-38

The first cupredoxin domain of coagulation factor VIII and similar proteins; Factor VIII functions in the factor X-activating complex of the intrinsic coagulation pathway. It facilitates blood clotting by acting as a cofactor for factor IXa. In the presence of Ca2+ and phospholipids, Factor VIII and IXa form a complex that converts factor X to the activated form Xa. A variety of mutations in the Factor VIII gene can cause hemophilia A, which typically requires replacement therapy with purified protein. Factor VIII is synthesized as a single polypeptide with six cupredoxin domains and a domain structure of 1-2-3-4-B-5-6-C1-C2, where 1-6 are cupredoxin domains, B is a domain with no known structural homologs and is dispensible for coagulant activity, and C are domains distantly related to discoidin protein-fold family members. Factor VIII is initially processed through proteolysis to generate a heterodimer consisting of a heavy chain (1-2-3-4) and a light chain (5-6-C1-C2), which circulates in a tight complex with von Willebrand factor (VWF). Further processing of the heavy chain produces activated factor VIIIa, a heterotrimer composed of polypeptides (1-2), (3-4), and the light chain. This model represents the cupredoxin domain 1 of unprocessed Factor VIII or the heavy chain of circulating Factor VIII, and similar proteins.


Pssm-ID: 259994 [Multi-domain]  Cd Length: 173  Bit Score: 140.88  E-value: 3.12e-38
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1564327556  745 KKYYIAAVEMDWDYsptrtweekMNNGLKESKGNEflKKEGKFIGSKYKKVLYREYTDETFTKPKERSADMehlGIMGPM 824
Cdd:cd14452      1 RRYYIAAVEIGWDY---------IHSDLGDPASEQ--RKKPKDIPQKYIKAVFVEYLDATFTVPKPRPAWM---GLLGPT 66

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1564327556  825 IHGKVGEKVKIVFKNMAKRPYSIHAHGV-------------KTESPQVALTR--PGETQTYTWYLPKNSGPTEEQEECSV 889
Cdd:cd14452     67 IVAEVGDTVVITFKNLASQPYSLHAVGVsywkasegagyddSTSQHEKEDDAvyPGGYHTYVWDISPKDGPTGSDPECLT 146

                          170       180
                   ....*....|....*....|....*..
gi 1564327556  890 GAYYSAVDVIKDMYSGLIGPLIVCKKS 916
Cdd:cd14452    147 YSYSSQVDPVKDVNSGLIGALLVCRMG 173
CuRO_6_FV_like cd14455
The sixth cupredoxin domain of coagulation factor V and similar proteins; Factor V is an ...
 927-1070 2.41e-35

The sixth cupredoxin domain of coagulation factor V and similar proteins; Factor V is an essential coagulation protein with both pro- and anti-coagulant functions. Aberrant expression of human factor V can lead to bleeding or thromboembolic disease, which may be life-threatening. Bovine factor Va serves as the cofactor in the prothrombinase complex that results in a 300,000-fold increase in the rate of thrombin generation. Factor V is synthesized as a single polypeptide with six cupredoxin domains and a domain structure of 1-2-3-4-B-5-6-C1-C2, where 1-6 are cupredoxin domains, B is a domain with no known structural homologs and is dispensible for coagulant activity, and C are domains distantly related to discoidin protein-fold family members. Factor V has little activity prior to proteolytic cleavage by thrombin or FXa upon secretion. The resulting Factor Va is a heterodimer consisting of a heavy chain (1-2-3-4) and a light chain (5-6-C1-C2). This model represents the cupredoxin domain 6 of unprocessed Factor V or the second cupredoxin domain of the light chain of coagulation factor Va, and similar proteins including pseutarin C non-catalytic subunit. Pseutarin C is a prothrombin activator from Pseudonaja textilis venom.


Pssm-ID: 259997 [Multi-domain]  Cd Length: 140  Bit Score: 131.14  E-value: 2.41e-35
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1564327556  927 IEEFALLFMVFDENESWYLDDNIKANVKnppKALKEDEEFIESNKMHGINGLVYgNLKGLNMKVGDKVYWYLMGMGNEVD 1006
Cdd:cd14455      1 RREFVLLFMTFDEEKSWYYEKNRKRTCR---ENRVKDPNVQDNHTFHAINGIIY-NLKGLRMYTNELVRWHLINMGGPKD 76

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1564327556 1007 IHTAHFHGHSFDYKVSGTHRADVFDLFPGTFQTVTMRPQYSGTWLLHCHVTDHIQAGMETTYTV 1070
Cdd:cd14455     77 LHVVHFHGQTFTEKGLKDHQLGVYPLLPGSFATLEMKPSKPGLWLLETEVGESQQRGMQTLFLV 140
CuRO_2_ceruloplasmin_like_2 cd11023
cupredoxin domain of ceruloplasmin homologs; Uncharacterized subfamily of ceruloplasmin ...
 252-357 2.54e-35

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: 130.42  E-value: 2.54e-35
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1564327556  252 DDEDFQESNKMHSINGYVFGNLPDLSMCMGNKIHWHLFGMGNEVDIHSAFFHGQ-ILTEKQHHVDTISLFPATFVNVEMV 330
Cdd:cd11023     12 LDLNVEEAGLMHSINGYVFGNLPGVTIAKGKRVRWHLVAYGNEVDFHTPHWHGQtVEADKSRRTDVAELMPASMRVADMT 91

                           90       100
                   ....*....|....*....|....*..
gi 1564327556  331 ADNPGQWLLSCQVNDHLEAGMQAIFEI 357
Cdd:cd11023     92 AADVGTWLLHCHVHDHYMAGMMTQFAV 118
CuRO_2_ceruloplasmin_like_2 cd11023
cupredoxin domain of ceruloplasmin homologs; Uncharacterized subfamily of ceruloplasmin ...
 963-1070 3.71e-35

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: 130.04  E-value: 3.71e-35
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1564327556  963 DEEFIESNKMHGINGLVYGNLKGLNMKVGDKVYWYLMGMGNEVDIHTAHFHGHSFDykVSGTHRADVFDLFPGTFQTVTM 1042
Cdd:cd11023     13 DLNVEEAGLMHSINGYVFGNLPGVTIAKGKRVRWHLVAYGNEVDFHTPHWHGQTVE--ADKSRRTDVAELMPASMRVADM 90

                           90       100
                   ....*....|....*....|....*...
gi 1564327556 1043 RPQYSGTWLLHCHVTDHIQAGMETTYTV 1070
Cdd:cd11023     91 TAADVGTWLLHCHVHDHYMAGMMTQFAV 118
CuRO_4_FVIII_like cd11016
The fourth cupredoxin domain of coagulation factor VIII and similar proteins; Factor VIII ...
 589-731 1.19e-34

The fourth cupredoxin domain of coagulation factor VIII and similar proteins; Factor VIII functions in the factor X-activating complex of the intrinsic coagulation pathway. It facilitates blood clotting by acting as a cofactor for factor IXa. In the presence of Ca2+ and phospholipids, Factor VIII and IXa form a complex that converts factor X to the activated form Xa. A variety of mutations in the Factor VIII gene can cause hemophilia A, which typically requires replacement therapy with purified protein. Factor VIII is synthesized as a single polypeptide with six cupredoxin domains and a domain structure of 1-2-3-4-B-5-6-C1-C2, where 1-6 are cupredoxin domains, B is a domain with no known structural homologs and is dispensible for coagulant activity, and C are domains distantly related to discoidin protein-fold family members. Factor VIII is initially processed through proteolysis to generate a heterodimer consisting of a heavy chain (1-2-3-4) and a light chain (5-6-C1-C2), which circulates in a tight complex with von Willebrand factor (VWF). Further processing of the heavy chain produces activated factor VIIIa, a heterotrimer composed of polypeptides (1-2), (3-4), and the light chain. This model represents the cupredoxin domain 4 of unprocessed Factor VIII or the heavy chain of circulating Factor VIII, and similar proteins.


Pssm-ID: 259902 [Multi-domain]  Cd Length: 143  Bit Score: 129.22  E-value: 1.19e-34
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1564327556  589 KEFHLLATVFDENLSWYLDDNINRFAKQPKSVKKEDKDFQESNKMHSLNGYMYGNLKgLSMCKGDKVSWHLSGLGSEVDI 668
Cdd:cd11016      2 KDWSLLFSVFDENNSWYLKENIHRFTQTPAGVNDTDPDFYASNVMHTINGIVFDRRQ-FVICLTDVAYWYVLSVGAQTDF 80

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1564327556  669 HGLYFEGNRFLYKDTRRDTINVFPHISHTVIMEPDSMGQFEVGCKTTDHYHGGMRANYTVEKC 731
Cdd:cd11016     81 LSVFFSGNTFKHQMVYEDVLTLFPFSGETVSMSPEVPGEWELGCFNGDFRSRGMSAQYTVSTC 143
CuRO_1_FV_like cd04226
The first cupredoxin domain of coagulation factor VIII and similar proteins; Factor V is an ...
 745-915 2.27e-34

The first cupredoxin domain of coagulation factor VIII and similar proteins; Factor V is an essential coagulation protein with both pro- and anti-coagulant functions. Aberrant expression of human factor V can lead to bleeding or thromboembolic disease, which may be life-threatening. Bovine factor Va serves as the cofactor in the prothrombinase complex that results in a 300,000-fold increase in the rate of thrombin generation. Factor V is synthesized as a single polypeptide with six cupredoxin domains and a domain structure of 1-2-3-4-B-5-6-C1-C2, where 1-6 are cupredoxin domains, B is a domain with no known structural homologs and is dispensible for coagulant activity, and C are domains distantly related to discoidin protein-fold family members. Factor V has little activity prior to proteolytic cleavage by thrombin or FXa upon secretion. The resulting Factor Va is a heterodimer consisting of a heavy chain (1-2-3-4) and a light chain (5-6-C1-C2). This model represents the cupredoxin domain 1 of unprocessed Factor V or the heavy chain of Factor Va, and similar proteins including pseutarin C non-catalytic subunit. Pseutarin C is a prothrombin activator from Pseudonaja textilis venom.


Pssm-ID: 259888 [Multi-domain]  Cd Length: 165  Bit Score: 129.21  E-value: 2.27e-34
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1564327556  745 KKYYIAAVEMDWDYSPtrtweEKMNNGLKESkgneflkkegkfiGSKYKKVLYREYtDETFTKPKERSadmEHLGIMGPM 824
Cdd:cd04226      1 REYYIAAQNIDWDYTP-----QSEELRLKRS-------------EQSFKKIVYREY-EEGFKKEKPAD---LSSGLLGPT 58

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1564327556  825 IHGKVGEKVKIVFKNMAKRPYSIHAHGV----KTESPQVA-----------LTRPGETQTYTWYLPKNSGPTEEQEECSV 889
Cdd:cd04226     59 LRAEVGDTLIVHFKNMADKPLSIHPQGIaygkKSEGSLYSdntspveklddAVQPGQEYTYVWDITEEVGPTEADPPCLT 138

                          170       180
                   ....*....|....*....|....*.
gi 1564327556  890 GAYYSAVDVIKDMYSGLIGPLIVCKK 915
Cdd:cd04226    139 YIYYSHVNMVRDFNSGLIGALLICKK 164
CuRO_2_FV_like cd14453
The second cupredoxin domain of coagulation factor V and similar proteins; Factor V is an ...
 220-357 8.83e-33

The second cupredoxin domain of coagulation factor V and similar proteins; Factor V is an essential coagulation protein with both pro- and anti-coagulant functions. Aberrant expression of human factor V can lead to bleeding or thromboembolic disease, which may be life-threatening. Bovine factor Va serves as the cofactor in the prothrombinase complex that results in a 300,000-fold increase in the rate of thrombin generation. Factor V is synthesized as a single polypeptide with six cupredoxin domains and a domain structure of 1-2-3-4-B-5-6-C1-C2, where 1-6 are cupredoxin domains, B is a domain with no known structural homologs and is dispensible for coagulant activity, and C are domains distantly related to discoidin protein-fold family members. Factor V has little activity prior to proteolytic cleavage by thrombin or FXa upon secretion. The resulting Factor Va is a heterodimer consisting of a heavy chain (1-2-3-4) and a light chain (5-6-C1-C2). This model represents the cupredoxin domain 2 of unprocessed Factor V or the heavy chain of Factor Va, and similar proteins including pseutarin C non-catalytic subunit. Pseutarin C is a prothrombin activator from Pseudonaja textilis venom.


Pssm-ID: 259995 [Multi-domain]  Cd Length: 123  Bit Score: 123.43  E-value: 8.83e-33
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1564327556  220 YTLMFTVSDENLSWYldeniktyctapakvnkdDEDFQESNKMHSINGYVFGNLPDLSMCMGNKIHWHLFGMGNEVDIHS 299
Cdd:cd14453      4 YVLMFGVFDENKSWY------------------KQNASVDSVKYTINGYTNGTLPDVSICAYDHVSWHLLGMSSEPELFS 65

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 1564327556  300 AFFHGQILTEKQHHVDTISLFPATFVNVEMVADNPGQWLLSCQVNDHLEAGMQAIFEI 357
Cdd:cd14453     66 VHFNGQVLEQNGHKVSAVGLVSGSSTTASMTVVHTGRWLISSLIMKHLQAGMYGYLNI 123
CuRO_4_FVIII_like cd11016
The fourth cupredoxin domain of coagulation factor VIII and similar proteins; Factor VIII ...
 217-360 1.05e-32

The fourth cupredoxin domain of coagulation factor VIII and similar proteins; Factor VIII functions in the factor X-activating complex of the intrinsic coagulation pathway. It facilitates blood clotting by acting as a cofactor for factor IXa. In the presence of Ca2+ and phospholipids, Factor VIII and IXa form a complex that converts factor X to the activated form Xa. A variety of mutations in the Factor VIII gene can cause hemophilia A, which typically requires replacement therapy with purified protein. Factor VIII is synthesized as a single polypeptide with six cupredoxin domains and a domain structure of 1-2-3-4-B-5-6-C1-C2, where 1-6 are cupredoxin domains, B is a domain with no known structural homologs and is dispensible for coagulant activity, and C are domains distantly related to discoidin protein-fold family members. Factor VIII is initially processed through proteolysis to generate a heterodimer consisting of a heavy chain (1-2-3-4) and a light chain (5-6-C1-C2), which circulates in a tight complex with von Willebrand factor (VWF). Further processing of the heavy chain produces activated factor VIIIa, a heterotrimer composed of polypeptides (1-2), (3-4), and the light chain. This model represents the cupredoxin domain 4 of unprocessed Factor VIII or the heavy chain of circulating Factor VIII, and similar proteins.


Pssm-ID: 259902 [Multi-domain]  Cd Length: 143  Bit Score: 123.82  E-value: 1.05e-32
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1564327556  217 DYLYTLMFTVSDENLSWYLDENIKTYCTAPAKVNKDDEDFQESNKMHSINGYVFGNLpDLSMCMGNKIHWHLFGMGNEVD 296
Cdd:cd11016      1 DKDWSLLFSVFDENNSWYLKENIHRFTQTPAGVNDTDPDFYASNVMHTINGIVFDRR-QFVICLTDVAYWYVLSVGAQTD 79

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1564327556  297 IHSAFFHGQILTEKQHHVDTISLFPATFVNVEMVADNPGQWLLSCQVNDHLEAGMQAIFEIKKC 360
Cdd:cd11016     80 FLSVFFSGNTFKHQMVYEDVLTLFPFSGETVSMSPEVPGEWELGCFNGDFRSRGMSAQYTVSTC 143
CuRO_4_FV_like cd14454
The fourth cupredoxin domain of coagulation factor V and similar proteins; Factor V is an ...
 223-360 1.97e-32

The fourth cupredoxin domain of coagulation factor V and similar proteins; Factor V is an essential coagulation protein with both pro- and anti-coagulant functions. Aberrant expression of human factor V can lead to bleeding or thromboembolic disease, which may be life-threatening. Bovine factor Va serves as the cofactor in the prothrombinase complex that results in a 300,000-fold increase in the rate of thrombin generation. Factor V is synthesized as a single polypeptide with six cupredoxin domains and a domain structure of 1-2-3-4-B-5-6-C1-C2, where 1-6 are cupredoxin domains, B is a domain with no known structural homologs and is dispensible for coagulant activity, and C are domains distantly related to discoidin protein-fold family members. Factor V has little activity prior to proteolytic cleavage by thrombin or FXa upon secretion. The resulting Factor Va is a heterodimer consisting of a heavy chain (1-2-3-4) and a light chain (5-6-C1-C2). This model represents the cupredoxin domain 4 of unprocessed Factor V or the heavy chain of Factor Va, and similar proteins including pseutarin C non-catalytic subunit. Pseutarin C is a prothrombin activator from Pseudonaja textilis venom.


Pssm-ID: 259996 [Multi-domain]  Cd Length: 144  Bit Score: 123.06  E-value: 1.97e-32
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1564327556  223 MFTVSDENLSWYLDENIKTYCTAPAKVNKDDEDFQESNKMHSINGYVFGNLPDLSMCMGNKIHWHLFGMGNEVDIHSAFF 302
Cdd:cd14454      7 VFAVFDENKSWYLEENINKYCSNPNNVKKDDPKFYKSNIMPTINGYAYESSAPLGFCHSEVVQWHISSVGTQDEIITVHL 86

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 1564327556  303 HGQILTEKQHHVDTISLFPATFVNVEMVADNPGQWLLSCQVNDHLEAGMQAIFEIKKC 360
Cdd:cd14454     87 SGHTFRYKGKHEDTLNLFPMSGESITVTMDNLGTWLLGSFGSSKKSKGLRVRFTDVIC 144
CuRO_4_FV_like cd14454
The fourth cupredoxin domain of coagulation factor V and similar proteins; Factor V is an ...
 589-731 4.36e-32

The fourth cupredoxin domain of coagulation factor V and similar proteins; Factor V is an essential coagulation protein with both pro- and anti-coagulant functions. Aberrant expression of human factor V can lead to bleeding or thromboembolic disease, which may be life-threatening. Bovine factor Va serves as the cofactor in the prothrombinase complex that results in a 300,000-fold increase in the rate of thrombin generation. Factor V is synthesized as a single polypeptide with six cupredoxin domains and a domain structure of 1-2-3-4-B-5-6-C1-C2, where 1-6 are cupredoxin domains, B is a domain with no known structural homologs and is dispensible for coagulant activity, and C are domains distantly related to discoidin protein-fold family members. Factor V has little activity prior to proteolytic cleavage by thrombin or FXa upon secretion. The resulting Factor Va is a heterodimer consisting of a heavy chain (1-2-3-4) and a light chain (5-6-C1-C2). This model represents the cupredoxin domain 4 of unprocessed Factor V or the heavy chain of Factor Va, and similar proteins including pseutarin C non-catalytic subunit. Pseutarin C is a prothrombin activator from Pseudonaja textilis venom.


Pssm-ID: 259996 [Multi-domain]  Cd Length: 144  Bit Score: 121.90  E-value: 4.36e-32
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1564327556  589 KEFHLLATVFDENLSWYLDDNINRFAKQPKSVKKEDKDFQESNKMHSLNGYMYGNLKGLSMCKGDKVSWHLSGLGSEVDI 668
Cdd:cd14454      2 LEQHAVFAVFDENKSWYLEENINKYCSNPNNVKKDDPKFYKSNIMPTINGYAYESSAPLGFCHSEVVQWHISSVGTQDEI 81

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1564327556  669 HGLYFEGNRFLYKDTRRDTINVFPHISHTVIMEPDSMGQFEVGCKTTDHYHGGMRANYTVEKC 731
Cdd:cd14454     82 ITVHLSGHTFRYKGKHEDTLNLFPMSGESITVTMDNLGTWLLGSFGSSKKSKGLRVRFTDVIC 144
CuRO_5_FVIII_like cd04228
The fifth cupredoxin domain of coagulation factor VIII and similar proteins; Factor VIII ...
 22-206 1.79e-31

The fifth cupredoxin domain of coagulation factor VIII and similar proteins; Factor VIII functions in the factor X-activating complex of the intrinsic coagulation pathway. It facilitates blood clotting by acting as a cofactor for factor IXa. In the presence of Ca2+ and phospholipids, Factor VIII and IXa form a complex that converts factor X to the activated form Xa. A variety of mutations in the Factor VIII gene can cause hemophilia A, which typically requires replacement therapy with purified protein. Factor VIII is synthesized as a single polypeptide with six cupredoxin domains and a domain structure of 1-2-3-4-B-5-6-C1-C2, where 1-6 are cupredoxin domains, B is a domain with no known structural homologs and is dispensible for coagulant activity, and C are domains distantly related to discoidin protein-fold family members. Factor VIII is initially processed through proteolysis to generate a heterodimer consisting of a heavy chain (1-2-3-4) and a light chain (5-6-C1-C2), which circulates in a tight complex with von Willebrand factor (VWF). Further processing of the heavy chain produces activated factor VIIIa, a heterotrimer composed of polypeptides (1-2), (3-4), and the light chain. This model represents the cupredoxin domain 5 of unprocessed Factor VIII or the first cupredoxin domain of the light chain of circulating Factor VIII, and similar proteins.


Pssm-ID: 259890 [Multi-domain]  Cd Length: 169  Bit Score: 121.15  E-value: 1.79e-31
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1564327556   22 TREYFFAIKEIQWDYAPSGKNliqnKTIKEDEearvfLERGEQRIGRVYRKAVYQQYTDSNYMQEI---EKPKWLGFLGP 98
Cdd:cd04228      1 IRHYFIAAVEVLWDYGMQRPQ----HFLRARD-----PNRGRRKSVPQYKKVVFREYLDGSFTQPVyrgELDEHLGILGP 71

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1564327556   99 LISAEENDIVVVHLKNMAKRAYSIHAHGLSYnksfegalypDSSEKAEKADDSVAPGKSFSYVWTLPASHSPGKDDTNCL 178
Cdd:cd04228     72 YIRAEVEDNIMVTFKNLASRPYSFHSSLISY----------EEDQRAEPRGNFVQPGEVQTYSWKVLHQMAPTKQEFDCK 141

                          170       180
                   ....*....|....*....|....*...
gi 1564327556  179 TRIYHSHVNAPKDIASGLIGPLIICKKG 206
Cdd:cd04228    142 AWAYFSNVDLEKDLHSGLIGPLIICKTG 169
CuRO_6_FV_like cd14455
The sixth cupredoxin domain of coagulation factor V and similar proteins; Factor V is an ...
 220-357 2.01e-30

The sixth cupredoxin domain of coagulation factor V and similar proteins; Factor V is an essential coagulation protein with both pro- and anti-coagulant functions. Aberrant expression of human factor V can lead to bleeding or thromboembolic disease, which may be life-threatening. Bovine factor Va serves as the cofactor in the prothrombinase complex that results in a 300,000-fold increase in the rate of thrombin generation. Factor V is synthesized as a single polypeptide with six cupredoxin domains and a domain structure of 1-2-3-4-B-5-6-C1-C2, where 1-6 are cupredoxin domains, B is a domain with no known structural homologs and is dispensible for coagulant activity, and C are domains distantly related to discoidin protein-fold family members. Factor V has little activity prior to proteolytic cleavage by thrombin or FXa upon secretion. The resulting Factor Va is a heterodimer consisting of a heavy chain (1-2-3-4) and a light chain (5-6-C1-C2). This model represents the cupredoxin domain 6 of unprocessed Factor V or the second cupredoxin domain of the light chain of coagulation factor Va, and similar proteins including pseutarin C non-catalytic subunit. Pseutarin C is a prothrombin activator from Pseudonaja textilis venom.


Pssm-ID: 259997 [Multi-domain]  Cd Length: 140  Bit Score: 117.27  E-value: 2.01e-30
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1564327556  220 YTLMFTVSDENLSWYLDENIKTYCTapaKVNKDDEDFQESNKMHSINGYVFgNLPDLSMCMGNKIHWHLFGMGNEVDIHS 299
Cdd:cd14455      4 FVLLFMTFDEEKSWYYEKNRKRTCR---ENRVKDPNVQDNHTFHAINGIIY-NLKGLRMYTNELVRWHLINMGGPKDLHV 79

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1564327556  300 AFFHGQILTE---KQHHVDTISLFPATFVNVEMVADNPGQWLLSCQVNDHLEAGMQAIFEI 357
Cdd:cd14455     80 VHFHGQTFTEkglKDHQLGVYPLLPGSFATLEMKPSKPGLWLLETEVGESQQRGMQTLFLV 140
CuRO_6_FVIII_like cd11018
The sixth cupredoxin domain of coagulation factor VIII and similar proteins; Factor VIII ...
 589-728 2.19e-30

The sixth cupredoxin domain of coagulation factor VIII and similar proteins; Factor VIII functions in the factor X-activating complex of the intrinsic coagulation pathway. It facilitates blood clotting by acting as a cofactor for factor IXa. In the presence of Ca2+ and phospholipids, Factor VIII and IXa form a complex that converts factor X to the activated form Xa. A variety of mutations in the Factor VIII gene can cause hemophilia A, which typically requires replacement therapy with purified protein. Factor VIII is synthesized as a single polypeptide with six cupredoxin domains and a domain structure of 1-2-3-4-B-5-6-C1-C2, where 1-6 are cupredoxin domains, B is a domain with no known structural homologs and is dispensible for coagulant activity, and C are domains distantly related to discoidin protein-fold family members. Factor VIII is initially processed through proteolysis to generate a heterodimer consisting of a heavy chain (1-2-3-4) and a light chain (5-6-C1-C2), which circulates in a tight complex with von Willebrand factor (VWF). Further processing of the heavy chain produces activated factor VIIIa, a heterotrimer composed of polypeptides (1-2), (3-4), and the light chain. This model represents the cupredoxin domain 6 of unprocessed Factor VIII or the second cupredoxin domain the light chain of circulating Factor VIII, and similar proteins.


Pssm-ID: 259904 [Multi-domain]  Cd Length: 144  Bit Score: 117.29  E-value: 2.19e-30
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1564327556  589 KEFHLLATVFDENLSWYLDDNINRFAKQPKSVKKEDKDFQESNKMHSLNGYMYGNLKGLSMCKGDKVSWHLSGLGSEVDI 668
Cdd:cd11018      2 QEFALLFTIFDETKSWYFEENMRRNCRPPCHIQTQDPWFHINNKFHAINGYVADTLPGLVMAQHQRIRWHLLNMGSDEEI 81

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1564327556  669 HGLYFEGNRFLY---KDTRRDTINVFPHISHTVIMEPDSMGQFEVGCKTTDHYHGGMRANYTV 728
Cdd:cd11018     82 HSVHFHGLPFTVrakKEYRMGVYNLYPGVFGTVEMRPSTAGIWLVECTVGEHLLAGMSALFLV 144
CuRO_4_FV_like cd14454
The fourth cupredoxin domain of coagulation factor V and similar proteins; Factor V is an ...
 926-1052 5.32e-27

The fourth cupredoxin domain of coagulation factor V and similar proteins; Factor V is an essential coagulation protein with both pro- and anti-coagulant functions. Aberrant expression of human factor V can lead to bleeding or thromboembolic disease, which may be life-threatening. Bovine factor Va serves as the cofactor in the prothrombinase complex that results in a 300,000-fold increase in the rate of thrombin generation. Factor V is synthesized as a single polypeptide with six cupredoxin domains and a domain structure of 1-2-3-4-B-5-6-C1-C2, where 1-6 are cupredoxin domains, B is a domain with no known structural homologs and is dispensible for coagulant activity, and C are domains distantly related to discoidin protein-fold family members. Factor V has little activity prior to proteolytic cleavage by thrombin or FXa upon secretion. The resulting Factor Va is a heterodimer consisting of a heavy chain (1-2-3-4) and a light chain (5-6-C1-C2). This model represents the cupredoxin domain 4 of unprocessed Factor V or the heavy chain of Factor Va, and similar proteins including pseutarin C non-catalytic subunit. Pseutarin C is a prothrombin activator from Pseudonaja textilis venom.


Pssm-ID: 259996 [Multi-domain]  Cd Length: 144  Bit Score: 107.65  E-value: 5.32e-27
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1564327556  926 EIEEFALlFMVFDENESWYLDDNIKANVKNPPKALKEDEEFIESNKMHGINGLVYGNLKGLNMKVGDKVYWYLMGMGNEV 1005
Cdd:cd14454      1 DLEQHAV-FAVFDENKSWYLEENINKYCSNPNNVKKDDPKFYKSNIMPTINGYAYESSAPLGFCHSEVVQWHISSVGTQD 79

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*..
gi 1564327556 1006 DIHTAHFHGHSFDYKvsGTHRaDVFDLFPGTFQTVTMRPQYSGTWLL 1052
Cdd:cd14454     80 EIITVHLSGHTFRYK--GKHE-DTLNLFPMSGESITVTMDNLGTWLL 123
CuRO_4_FVIII_like cd11016
The fourth cupredoxin domain of coagulation factor VIII and similar proteins; Factor VIII ...
 932-1072 1.06e-26

The fourth cupredoxin domain of coagulation factor VIII and similar proteins; Factor VIII functions in the factor X-activating complex of the intrinsic coagulation pathway. It facilitates blood clotting by acting as a cofactor for factor IXa. In the presence of Ca2+ and phospholipids, Factor VIII and IXa form a complex that converts factor X to the activated form Xa. A variety of mutations in the Factor VIII gene can cause hemophilia A, which typically requires replacement therapy with purified protein. Factor VIII is synthesized as a single polypeptide with six cupredoxin domains and a domain structure of 1-2-3-4-B-5-6-C1-C2, where 1-6 are cupredoxin domains, B is a domain with no known structural homologs and is dispensible for coagulant activity, and C are domains distantly related to discoidin protein-fold family members. Factor VIII is initially processed through proteolysis to generate a heterodimer consisting of a heavy chain (1-2-3-4) and a light chain (5-6-C1-C2), which circulates in a tight complex with von Willebrand factor (VWF). Further processing of the heavy chain produces activated factor VIIIa, a heterotrimer composed of polypeptides (1-2), (3-4), and the light chain. This model represents the cupredoxin domain 4 of unprocessed Factor VIII or the heavy chain of circulating Factor VIII, and similar proteins.


Pssm-ID: 259902 [Multi-domain]  Cd Length: 143  Bit Score: 106.49  E-value: 1.06e-26
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1564327556  932 LLFMVFDENESWYLDDNIKANVKNPPKALKEDEEFIESNKMHGINGLVYGNLKgLNMKVGDKVYWYLMGMGNEVDIHTAH 1011
Cdd:cd11016      6 LLFSVFDENNSWYLKENIHRFTQTPAGVNDTDPDFYASNVMHTINGIVFDRRQ-FVICLTDVAYWYVLSVGAQTDFLSVF 84

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1564327556 1012 FHGHSFDYKVSgthRADVFDLFPGTFQTVTMRPQYSGTWLLHCHVTDHIQAGMETTYTVLE 1072
Cdd:cd11016     85 FSGNTFKHQMV---YEDVLTLFPFSGETVSMSPEVPGEWELGCFNGDFRSRGMSAQYTVST 142
CuRO_2_FVIII_like cd11015
The second cupredoxin domain of coagulation factor VIII and similar proteins; Factor VIII ...
 220-357 3.71e-26

The second cupredoxin domain of coagulation factor VIII and similar proteins; Factor VIII functions in the factor X-activating complex of the intrinsic coagulation pathway. It facilitates blood clotting by acting as a cofactor for factor IXa. In the presence of Ca2+ and phospholipids, Factor VIII and IXa form a complex that converts factor X to the activated form Xa. A variety of mutations in the Factor VIII gene can cause hemophilia A, which typically requires replacement therapy with purified protein. Factor VIII is synthesized as a single polypeptide with six cupredoxin domains and a domain structure of 1-2-3-4-B-5-6-C1-C2, where 1-6 are cupredoxin domains, B is a domain with no known structural homologs and is dispensible for coagulant activity, and C are domains distantly related to discoidin protein-fold family members. Factor VIII is initially processed through proteolysis to generate a heterodimer consisting of a heavy chain (1-2-3-4) and a light chain (5-6-C1-C2), which circulates in a tight complex with von Willebrand factor (VWF). Further processing of the heavy chain produces activated factor VIIIa, a heterotrimer composed of polypeptides (1-2), (3-4), and the light chain. This model represents the cupredoxin domain 2 of unprocessed Factor VIII or the heavy chain of circulating Factor VIII, and similar proteins.


Pssm-ID: 259901 [Multi-domain]  Cd Length: 134  Bit Score: 104.60  E-value: 3.71e-26
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1564327556  220 YTLMFTVSDENLSWY--LDENIKTYCTAPAKVNKddedfqesnKMHSINGYVFGNLPDLSMCMGNKIHWHLFGMGNEVDI 297
Cdd:cd11015      4 FVLLFAVFDEGKSWYseVGERKSRDKFKRADSRK---------EFHTINGYINASLPGLKICQRKPVIWHVIGMGTAPEV 74

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1564327556  298 HSAFFHGQILTEKQHHVDTISLFPATFVNVEMVADNPGQWLLSCQVNDHLEAGMQAIFEI 357
Cdd:cd11015     75 HSIFFEGHTFLVRTHRKVSLEISPMTFLTAQTKPATVGSFLIFCQIHSHQHDGMEAMVKV 134
CuRO_2_FVIII_like cd11015
The second cupredoxin domain of coagulation factor VIII and similar proteins; Factor VIII ...
 928-1070 1.17e-23

The second cupredoxin domain of coagulation factor VIII and similar proteins; Factor VIII functions in the factor X-activating complex of the intrinsic coagulation pathway. It facilitates blood clotting by acting as a cofactor for factor IXa. In the presence of Ca2+ and phospholipids, Factor VIII and IXa form a complex that converts factor X to the activated form Xa. A variety of mutations in the Factor VIII gene can cause hemophilia A, which typically requires replacement therapy with purified protein. Factor VIII is synthesized as a single polypeptide with six cupredoxin domains and a domain structure of 1-2-3-4-B-5-6-C1-C2, where 1-6 are cupredoxin domains, B is a domain with no known structural homologs and is dispensible for coagulant activity, and C are domains distantly related to discoidin protein-fold family members. Factor VIII is initially processed through proteolysis to generate a heterodimer consisting of a heavy chain (1-2-3-4) and a light chain (5-6-C1-C2), which circulates in a tight complex with von Willebrand factor (VWF). Further processing of the heavy chain produces activated factor VIIIa, a heterotrimer composed of polypeptides (1-2), (3-4), and the light chain. This model represents the cupredoxin domain 2 of unprocessed Factor VIII or the heavy chain of circulating Factor VIII, and similar proteins.


Pssm-ID: 259901 [Multi-domain]  Cd Length: 134  Bit Score: 97.67  E-value: 1.17e-23
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1564327556  928 EEFALLFMVFDENESWYLDDNIKANVKNPPKALKEDEefiesnkMHGINGLVYGNLKGLNMKVGDKVYWYLMGMGNEVDI 1007
Cdd:cd11015      2 QAFVLLFAVFDEGKSWYSEVGERKSRDKFKRADSRKE-------FHTINGYINASLPGLKICQRKPVIWHVIGMGTAPEV 74

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1564327556 1008 HTAHFHGHSFDYKvsgTHRADVFDLFPGTFQTVTMRPQYSGTWLLHCHVTDHIQAGMETTYTV 1070
Cdd:cd11015     75 HSIFFEGHTFLVR---THRKVSLEISPMTFLTAQTKPATVGSFLIFCQIHSHQHDGMEAMVKV 134
CuRO_2_ceruloplasmin_like_2 cd11023
cupredoxin domain of ceruloplasmin homologs; Uncharacterized subfamily of ceruloplasmin ...
 597-728 2.37e-23

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: 96.14  E-value: 2.37e-23
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1564327556  597 VFDENLSWYLDDNInrfakqpksvkkedkdfQESNKMHSLNGYMYGNLKGLSMCKGDKVSWHLSGLGSEVDIHGLYFEGN 676
Cdd:cd11023      3 EFIENSSIFLDLNV-----------------EEAGLMHSINGYVFGNLPGVTIAKGKRVRWHLVAYGNEVDFHTPHWHGQ 65

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|...
gi 1564327556  677 RFLYKDTRR-DTINVFPHISHTVIMEPDSMGQFEVGCKTTDHYHGGMRANYTV 728
Cdd:cd11023     66 TVEADKSRRtDVAELMPASMRVADMTAADVGTWLLHCHVHDHYMAGMMTQFAV 118
CuRO_2_FVIII_like cd11015
The second cupredoxin domain of coagulation factor VIII and similar proteins; Factor VIII ...
 589-728 3.19e-23

The second cupredoxin domain of coagulation factor VIII and similar proteins; Factor VIII functions in the factor X-activating complex of the intrinsic coagulation pathway. It facilitates blood clotting by acting as a cofactor for factor IXa. In the presence of Ca2+ and phospholipids, Factor VIII and IXa form a complex that converts factor X to the activated form Xa. A variety of mutations in the Factor VIII gene can cause hemophilia A, which typically requires replacement therapy with purified protein. Factor VIII is synthesized as a single polypeptide with six cupredoxin domains and a domain structure of 1-2-3-4-B-5-6-C1-C2, where 1-6 are cupredoxin domains, B is a domain with no known structural homologs and is dispensible for coagulant activity, and C are domains distantly related to discoidin protein-fold family members. Factor VIII is initially processed through proteolysis to generate a heterodimer consisting of a heavy chain (1-2-3-4) and a light chain (5-6-C1-C2), which circulates in a tight complex with von Willebrand factor (VWF). Further processing of the heavy chain produces activated factor VIIIa, a heterotrimer composed of polypeptides (1-2), (3-4), and the light chain. This model represents the cupredoxin domain 2 of unprocessed Factor VIII or the heavy chain of circulating Factor VIII, and similar proteins.


Pssm-ID: 259901 [Multi-domain]  Cd Length: 134  Bit Score: 96.51  E-value: 3.19e-23
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1564327556  589 KEFHLLATVFDENLSWYLDdninrfAKQPKSVKKEdKDFQESNKMHSLNGYMYGNLKGLSMCKGDKVSWHLSGLGSEVDI 668
Cdd:cd11015      2 QAFVLLFAVFDEGKSWYSE------VGERKSRDKF-KRADSRKEFHTINGYINASLPGLKICQRKPVIWHVIGMGTAPEV 74

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1564327556  669 HGLYFEGNRFLYKDTRRDTINVFPHISHTVIMEPDSMGQFEVGCKTTDHYHGGMRANYTV 728
Cdd:cd11015     75 HSIFFEGHTFLVRTHRKVSLEISPMTFLTAQTKPATVGSFLIFCQIHSHQHDGMEAMVKV 134
CuRO_2_FV_like cd14453
The second cupredoxin domain of coagulation factor V and similar proteins; Factor V is an ...
 928-1064 1.22e-19

The second cupredoxin domain of coagulation factor V and similar proteins; Factor V is an essential coagulation protein with both pro- and anti-coagulant functions. Aberrant expression of human factor V can lead to bleeding or thromboembolic disease, which may be life-threatening. Bovine factor Va serves as the cofactor in the prothrombinase complex that results in a 300,000-fold increase in the rate of thrombin generation. Factor V is synthesized as a single polypeptide with six cupredoxin domains and a domain structure of 1-2-3-4-B-5-6-C1-C2, where 1-6 are cupredoxin domains, B is a domain with no known structural homologs and is dispensible for coagulant activity, and C are domains distantly related to discoidin protein-fold family members. Factor V has little activity prior to proteolytic cleavage by thrombin or FXa upon secretion. The resulting Factor Va is a heterodimer consisting of a heavy chain (1-2-3-4) and a light chain (5-6-C1-C2). This model represents the cupredoxin domain 2 of unprocessed Factor V or the heavy chain of Factor Va, and similar proteins including pseutarin C non-catalytic subunit. Pseutarin C is a prothrombin activator from Pseudonaja textilis venom.


Pssm-ID: 259995 [Multi-domain]  Cd Length: 123  Bit Score: 85.68  E-value: 1.22e-19
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1564327556  928 EEFALLFMVFDENESWYlddniKANVKnppkalkedeefiESNKMHGINGLVYGNLKGLNMKVGDKVYWYLMGMGNEVDI 1007
Cdd:cd14453      2 KEYVLMFGVFDENKSWY-----KQNAS-------------VDSVKYTINGYTNGTLPDVSICAYDHVSWHLLGMSSEPEL 63

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 1564327556 1008 HTAHFHGHSFDykvSGTHRADVFDLFPGTFQTVTMRPQYSGTWLLHCHVTDHIQAGM 1064
Cdd:cd14453     64 FSVHFNGQVLE---QNGHKVSAVGLVSGSSTTASMTVVHTGRWLISSLIMKHLQAGM 117
CuRO_6_FV_like cd14455
The sixth cupredoxin domain of coagulation factor V and similar proteins; Factor V is an ...
 589-728 5.85e-19

The sixth cupredoxin domain of coagulation factor V and similar proteins; Factor V is an essential coagulation protein with both pro- and anti-coagulant functions. Aberrant expression of human factor V can lead to bleeding or thromboembolic disease, which may be life-threatening. Bovine factor Va serves as the cofactor in the prothrombinase complex that results in a 300,000-fold increase in the rate of thrombin generation. Factor V is synthesized as a single polypeptide with six cupredoxin domains and a domain structure of 1-2-3-4-B-5-6-C1-C2, where 1-6 are cupredoxin domains, B is a domain with no known structural homologs and is dispensible for coagulant activity, and C are domains distantly related to discoidin protein-fold family members. Factor V has little activity prior to proteolytic cleavage by thrombin or FXa upon secretion. The resulting Factor Va is a heterodimer consisting of a heavy chain (1-2-3-4) and a light chain (5-6-C1-C2). This model represents the cupredoxin domain 6 of unprocessed Factor V or the second cupredoxin domain of the light chain of coagulation factor Va, and similar proteins including pseutarin C non-catalytic subunit. Pseutarin C is a prothrombin activator from Pseudonaja textilis venom.


Pssm-ID: 259997 [Multi-domain]  Cd Length: 140  Bit Score: 84.53  E-value: 5.85e-19
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1564327556  589 KEFHLLATVFDENLSWYLDDNINRFAKQpksVKKEDKDFQESNKMHSLNGYMYgNLKGLSMCKGDKVSWHLSGLGSEVDI 668
Cdd:cd14455      2 REFVLLFMTFDEEKSWYYEKNRKRTCRE---NRVKDPNVQDNHTFHAINGIIY-NLKGLRMYTNELVRWHLINMGGPKDL 77

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1564327556  669 HGLYFEGNRFLYKDTRRDTINVFPHIS---HTVIMEPDSMGQFEVGCKTTDHYHGGMRANYTV 728
Cdd:cd14455     78 HVVHFHGQTFTEKGLKDHQLGVYPLLPgsfATLEMKPSKPGLWLLETEVGESQQRGMQTLFLV 140
Cu-oxidase_2 pfam07731
Multicopper oxidase; This entry contains many divergent copper oxidase-like domains that are ...
 970-1074 1.26e-18

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: 83.25  E-value: 1.26e-18
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1564327556  970 NKMHGINGLVYG-NLKGLNMKVGDKVYWYLMGMGNevDIHTAHFHGHSFDYKVSGTH----------------RADVFDL 1032
Cdd:pfam07731   19 RNDWAINGLLFPpNTNVITLPYGTVVEWVLQNTTT--GVHPFHLHGHSFQVLGRGGGpwpeedpktynlvdpvRRDTVQV 96

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|..
gi 1564327556 1033 FPGTFQTVTMRPQYSGTWLLHCHVTDHIQAGMETTYTVLEKD 1074
Cdd:pfam07731   97 PPGGWVAIRFRADNPGVWLFHCHILWHLDQGMMGQFVVRPGD 138
CuRO_1_LCC_like cd04206
Cupredoxin domain 1 of laccase-like multicopper oxidases; including laccase, CueO, spore coat ...
 94-203 1.15e-16

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: 76.94  E-value: 1.15e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1564327556   94 GFLGPLISAEENDIVVVHLKN-MAKRAYSIHAHGLSYNKSFEGALYPDSSEKAekaddsVAPGKSFSYVWTLPasHSPGk 172
Cdd:cd04206     27 QFPGPTIRVKEGDTVEVTVTNnLPNEPTSIHWHGLRQPGTNDGDGVAGLTQCP------IPPGESFTYRFTVD--DQAG- 97

                           90       100       110
                   ....*....|....*....|....*....|.
gi 1564327556  173 ddtnclTRIYHSHVNApkDIASGLIGPLIIC 203
Cdd:cd04206     98 ------TFWYHSHVGG--QRADGLYGPLIVE 120
CuRO_2_FV_like cd14453
The second cupredoxin domain of coagulation factor V and similar proteins; Factor V is an ...
 589-724 7.79e-15

The second cupredoxin domain of coagulation factor V and similar proteins; Factor V is an essential coagulation protein with both pro- and anti-coagulant functions. Aberrant expression of human factor V can lead to bleeding or thromboembolic disease, which may be life-threatening. Bovine factor Va serves as the cofactor in the prothrombinase complex that results in a 300,000-fold increase in the rate of thrombin generation. Factor V is synthesized as a single polypeptide with six cupredoxin domains and a domain structure of 1-2-3-4-B-5-6-C1-C2, where 1-6 are cupredoxin domains, B is a domain with no known structural homologs and is dispensible for coagulant activity, and C are domains distantly related to discoidin protein-fold family members. Factor V has little activity prior to proteolytic cleavage by thrombin or FXa upon secretion. The resulting Factor Va is a heterodimer consisting of a heavy chain (1-2-3-4) and a light chain (5-6-C1-C2). This model represents the cupredoxin domain 2 of unprocessed Factor V or the heavy chain of Factor Va, and similar proteins including pseutarin C non-catalytic subunit. Pseutarin C is a prothrombin activator from Pseudonaja textilis venom.


Pssm-ID: 259995 [Multi-domain]  Cd Length: 123  Bit Score: 71.81  E-value: 7.79e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1564327556  589 KEFHLLATVFDENLSWYlddninrfakqpksvkkeDKDFQESNKMHSLNGYMYGNLKGLSMCKGDKVSWHLSGLGSEVDI 668
Cdd:cd14453      2 KEYVLMFGVFDENKSWY------------------KQNASVDSVKYTINGYTNGTLPDVSICAYDHVSWHLLGMSSEPEL 63

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 1564327556  669 HGLYFEGNRFLYKDTRRDTINVFPHISHTVIMEPDSMGQFEVGCKTTDHYHGGMRA 724
Cdd:cd14453     64 FSVHFNGQVLEQNGHKVSAVGLVSGSSTTASMTVVHTGRWLISSLIMKHLQAGMYG 119
CuRO_1_CumA_like cd13861
The first cupredoxin domain of CumA like multicopper oxidase; This multicopper oxidase (MCO) ...
 448-573 3.78e-11

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: 61.48  E-value: 3.78e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1564327556  448 GILGPIIRAEEEDTIKVTFRNKASRPYSIQPHGVQYNIEMDGtlyhnvleesytakklreikkearvVEPLPAALVRPDT 527
Cdd:cd13861     28 QVPGPELRVRQGDTLRVRLTNRLPEPTTIHWHGLRLPNAMDG-------------------------VPGLTQPPVPPGE 82

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*.
gi 1564327556  528 TYKYEWVVPkDAGptekdpdciTYMYYSAVDPIRDTNSGLVGPLLI 573
Cdd:cd13861     83 SFTYEFTPP-DAG---------TYWYHPHVGSQEQLDRGLYGPLIV 118
CuRO_3_LCC_like cd04207
Cupredoxin domain 3 of laccase-like multicopper oxidases; including laccase, CueO, spore coat ...
 975-1069 6.66e-11

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: 60.94  E-value: 6.66e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1564327556  975 INGLVY----GNLKGLNMKVGDKVYWYLMGMGNEVDIHTAHFHGHSFDYKVSGTHRA------------DVFDLFPGTFQ 1038
Cdd:cd04207     22 INGMPFkegdANTDIFSVEAGDVVEIVLINAGNHDMQHPFHLHGHSFWVLGSGGGPFdaplnltnppwrDTVLVPPGGWV 101

                           90       100       110
                   ....*....|....*....|....*....|.
gi 1564327556 1039 TVTMRPQYSGTWLLHCHVTDHIQAGMETTYT 1069
Cdd:cd04207    102 VIRFKADNPGVWMLHCHILEHEDAGMMTVFE 132
CuRO_3_LCC_like cd04207
Cupredoxin domain 3 of laccase-like multicopper oxidases; including laccase, CueO, spore coat ...
 264-356 7.13e-11

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: 60.94  E-value: 7.13e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1564327556  264 SINGYVF----GNLPDLSMCMGNKIHWHLFGMGNEVDIHSAFFHG---QILTEKQHHV------------DTISLFPATF 324
Cdd:cd04207     21 VINGMPFkegdANTDIFSVEAGDVVEIVLINAGNHDMQHPFHLHGhsfWVLGSGGGPFdaplnltnppwrDTVLVPPGGW 100

                           90       100       110
                   ....*....|....*....|....*....|..
gi 1564327556  325 VNVEMVADNPGQWLLSCQVNDHLEAGMQAIFE 356
Cdd:cd04207    101 VVIRFKADNPGVWMLHCHILEHEDAGMMTVFE 132
CuRO_D1_2dMcoN_like cd13859
The first cupredoxin domain of bacterial two domain multicopper oxidase McoN and similar ...
 97-202 7.56e-11

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: 60.57  E-value: 7.56e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1564327556   97 GPLISAEENDIVVVHLKNMAKRAYSIHAHGLSYNKSFEGALYPDSSEKAekaddsVAPGKSFSYVWTlpaSHSPGkddtn 176
Cdd:cd13859     31 GPLIHVKEGDDLVVHVTNNTTLPHTIHWHGVLQMGSWKMDGVPGVTQPA------IEPGESFTYKFK---AERPG----- 96

                           90       100
                   ....*....|....*....|....*..
gi 1564327556  177 clTRIYHSHVNAPKDIA-SGLIGPLII 202
Cdd:cd13859     97 --TLWYHCHVNVNEHVGmRGMWGPLIV 121
CuRO_1_LCC_like cd04206
Cupredoxin domain 1 of laccase-like multicopper oxidases; including laccase, CueO, spore coat ...
 427-574 1.07e-10

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: 59.99  E-value: 1.07e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1564327556  427 VEYTDDTFtKRKERTSEEQHLGILGPIIRAEEEDTIKVTFRNK-ASRPYSIQPHGVQYNIEMDGTlyhnvleesytakkl 505
Cdd:cd04206      7 ITETTVNP-DGVLRQVITVNGQFPGPTIRVKEGDTVEVTVTNNlPNEPTSIHWHGLRQPGTNDGD--------------- 70

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1564327556  506 reikkearVVEPLPAALVRPDTTYKYEWVVPKDAGptekdpdciTYMYYSAVDPIRDTnsGLVGPLLIC 574
Cdd:cd04206     71 --------GVAGLTQCPIPPGESFTYRFTVDDQAG---------TFWYHSHVGGQRAD--GLYGPLIVE 120
CuRO_D2_2dMcoN_like cd04202
The second cupredoxin domain of bacterial two domain multicopper oxidase McoN and similar ...
 975-1064 1.65e-10

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: 59.96  E-value: 1.65e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1564327556  975 INGLVYGNLKGLNMKVGDKVYWYLMGMGNevDIHTAHFHGHSFDY--------KVSGTHRADVFDLFPGTFQTVTMRPQY 1046
Cdd:cd04202     32 INGKSFPATPPLVVKEGDRVRIRLINLSM--DHHPMHLHGHFFLVtatdggpiPGSAPWPKDTLNVAPGERYDIEFVADN 109

                           90
                   ....*....|....*...
gi 1564327556 1047 SGTWLLHCHVTDHIQAGM 1064
Cdd:cd04202    110 PGDWMFHCHKLHHAMNGM 127
CuRO_1_CumA_like cd13861
The first cupredoxin domain of CumA like multicopper oxidase; This multicopper oxidase (MCO) ...
 94-202 3.04e-10

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: 58.79  E-value: 3.04e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1564327556   94 GFLGPLISAEENDIVVVHLKNMAKRAYSIHAHGLSYNKSFEGAlyPDSSEKAekaddsVAPGKSFSYVWTLPAshsPGkd 173
Cdd:cd13861     28 QVPGPELRVRQGDTLRVRLTNRLPEPTTIHWHGLRLPNAMDGV--PGLTQPP------VPPGESFTYEFTPPD---AG-- 94

                           90       100
                   ....*....|....*....|....*....
gi 1564327556  174 dtnclTRIYHSHVNAPKDIASGLIGPLII 202
Cdd:cd13861     95 -----TYWYHPHVGSQEQLDRGLYGPLIV 118
CuRO_1_Diphenol_Ox cd13857
The first cupredoxin domain of fungal laccase, diphenol oxidase; Diphenol oxidase belongs to ...
 95-202 4.72e-10

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: 58.04  E-value: 4.72e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1564327556   95 FLGPLISAEENDIVVVHLKNMAKRAYSIHAHGLSYNKS--FEGAlyPDSSEKAekaddsVAPGKSFSYVWTLpashspgk 172
Cdd:cd13857     28 FPGPLIEANQGDRIVVHVTNELDEPTSIHWHGLFQNGTnwMDGT--AGITQCP------IPPGGSFTYNFTV-------- 91

                           90       100       110
                   ....*....|....*....|....*....|
gi 1564327556  173 dDTNCLTRIYHSHVNAPKdiASGLIGPLII 202
Cdd:cd13857     92 -DGQYGTYWYHSHYSTQY--ADGLVGPLIV 118
Cu-oxidase_3 pfam07732
Multicopper oxidase; This entry contains many divergent copper oxidase-like domains that are ...
 95-202 1.16e-09

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: 56.87  E-value: 1.16e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1564327556   95 FLGPLISAEENDIVVVHLKNMAKRAYSIHAHGLSYNKSFEGALYPDSSEkaekadDSVAPGKSFSYVWtlPASHSPGkdd 174
Cdd:pfam07732   24 FPGPTIRVREGDTVVVNVTNNLDEPTSIHWHGLQQRGTPWMDGVPGVTQ------CPIPPGQSFTYRF--QVKQQAG--- 92

                           90       100
                   ....*....|....*....|....*...
gi 1564327556  175 tnclTRIYHSHVNAPKdiASGLIGPLII 202
Cdd:pfam07732   93 ----TYWYHSHTSGQQ--AAGLAGAIII 114
CuRO_1_2dMco_1 cd13860
The first cupredoxin domain of bacteria two domain multicopper oxidase; This subfamily ...
 97-202 1.52e-09

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: 56.82  E-value: 1.52e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1564327556   97 GPLISAEENDIVVVHLKNMAKRAYSIHAHGLSYNKSFEGAlyPDSSEKAekaddsVAPGKSFSYVWTLpasHSPGkddtn 176
Cdd:cd13860     31 GPTIEVTEGDRVRILVTNELPEPTTVHWHGLPVPNGMDGV--PGITQPP------IQPGETFTYEFTA---KQAG----- 94

                           90       100
                   ....*....|....*....|....*.
gi 1564327556  177 clTRIYHSHVNAPKDIASGLIGPLII 202
Cdd:cd13860     95 --TYMYHSHVDEAKQEDMGLYGAFIV 118
CuRO_1_LCC_like cd04206
Cupredoxin domain 1 of laccase-like multicopper oxidases; including laccase, CueO, spore coat ...
 819-913 4.21e-09

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: 55.37  E-value: 4.21e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1564327556  819 GIMGPMIHGKVGEKVKIVFKN-MAKRPYSIHAHGVKTE-----SPQVALT----RPGETQTYTWylpknsgPTEEQeecs 888
Cdd:cd04206     27 QFPGPTIRVKEGDTVEVTVTNnLPNEPTSIHWHGLRQPgtndgDGVAGLTqcpiPPGESFTYRF-------TVDDQ---- 95

                           90       100
                   ....*....|....*....|....*..
gi 1564327556  889 VGA--YYSAVDVikDMYSGLIGPLIVC 913
Cdd:cd04206     96 AGTfwYHSHVGG--QRADGLYGPLIVE 120
SufI COG2132
Multicopper oxidase with three cupredoxin domains (includes cell division protein FtsP and ...
 972-1072 1.23e-08

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: 58.41  E-value: 1.23e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1564327556  972 MHGINGLVYGNLK-GLNMKVGDKVYWYLMGMGNevDIHTAHFHGHSF------DYKVSGTHRADVFDLFPGtfQTVTMR- 1043
Cdd:COG2132    317 VWTINGKAFDPDRpDLTVKLGERERWTLVNDTM--MPHPFHLHGHQFqvlsrnGKPPPEGGWKDTVLVPPG--ETVRILf 392

                           90       100       110
                   ....*....|....*....|....*....|.
gi 1564327556 1044 --PQYSGTWLLHCHVTDHIQAGMETTYTVLE 1072
Cdd:COG2132    393 rfDNYPGDWMFHCHILEHEDAGMMGQFEVVP 423
CuRO_1_2DMCO_NIR_like_2 cd14449
The cupredoxin domain 1 of a two-domain laccase related to nitrite reductase; The two-domain ...
 97-202 1.57e-08

The cupredoxin domain 1 of a two-domain laccase related to nitrite reductase; The two-domain laccase (small laccase) in this family differs significantly from all laccases. It resembles the two domain nitrite reductase in both sequence and structure. It consists of two cupredoxin domains and forms trimers, and hence resembles the quaternary structure of nitrite reductases more than that of large laccases. There are three trinuclear copper clusters in the enzyme localized between domains 1 and 2 of each pair of neighbor chains. 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: 54.20  E-value: 1.57e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1564327556   97 GPLISAEENDIVVVHLKNMAKRAYSIHAHGLSYNKSFEGALYPDSsekaekaddSVAPGKSFSYVWTlpaSHSPGKDDTN 176
Cdd:cd14449     29 GPVIEVREGDTLKILFRNTLDVPASLHPHGVDYTTASDGTGMNAS---------IVAPGDTRIYTWR---THGGYRRADG 96

                           90       100       110
                   ....*....|....*....|....*....|....*.
gi 1564327556  177 CL------TRIYHSHV----NAPKDIASGLIGPLII 202
Cdd:cd14449     97 SWaegtagYWHYHDHVfgteHGTEGLSRGLYGALIV 132
Cu-oxidase pfam00394
Multicopper oxidase; Many of the proteins in this family contain multiple similar copies of ...
 220-353 1.95e-08

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: 54.25  E-value: 1.95e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1564327556  220 YTLMFTvsdenlSWYlDENIKTYCTAPAKVNKDDEDFQESNKMHSINGYVFGNLPDLSMCMGNKIHWHLFgMGNEVDIHS 299
Cdd:pfam00394    3 YVITLS------DWY-HKDAKDLEKELLASGKAPTDFPPVPDAVLINGKDGASLATLTVTPGKTYRLRII-NVALDDSLN 74

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1564327556  300 AFFHGQILTE--------KQHHVDTISLFPATFVNVEMVADN-PGQWLLSCQVN-DHLEAGMQA 353
Cdd:pfam00394   75 FSIEGHKMTVvevdgvyvNPFTVDSLDIFPGQRYSVLVTANQdPGNYWIVASPNiPAFDNGTAA 138
CuRO_3_CumA_like cd13906
The third cupredoxin domain of CumA like multicopper oxidase; This multicopper oxidase (MCO) ...
 286-358 2.81e-08

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: 53.54  E-value: 2.81e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1564327556  286 WHLFGMGNEVD------IHSAFF-----HGQILTEkQHHVDTISLFPATFVNVEMVADNPGQWLLSCQVNDHLEAGMQAI 354
Cdd:cd13906     56 SYVLRLVNETAflhpmhLHGHFFrvlsrNGRPVPE-PFWRDTVLLGPKETVDIAFVADNPGDWMFHCHILEHQETGMMGV 134


                   ....
gi 1564327556  355 FEIK 358
Cdd:cd13906    135 IRVA 138
CuRO_3_CumA_like cd13906
The third cupredoxin domain of CumA like multicopper oxidase; This multicopper oxidase (MCO) ...
 986-1070 4.02e-08

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: 53.16  E-value: 4.02e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1564327556  986 LNMKVGDkvyWYLMGMGNEVD-IHTAHFHGHSFDY------KVSGTHRADVFDLFPGTFQTVTMRPQYSGTWLLHCHVTD 1058
Cdd:cd13906     49 ATLKRGR---SYVLRLVNETAfLHPMHLHGHFFRVlsrngrPVPEPFWRDTVLLGPKETVDIAFVADNPGDWMFHCHILE 125

                           90
                   ....*....|..
gi 1564327556 1059 HIQAGMETTYTV 1070
Cdd:cd13906    126 HQETGMMGVIRV 137
CuRO_1_2DMCO_NIR_like cd11024
The cupredoxin domain 1 of a two-domain laccase related to nitrite reductase; The two-domain ...
 451-577 5.37e-08

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


Pssm-ID: 259910 [Multi-domain]  Cd Length: 119  Bit Score: 52.27  E-value: 5.37e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1564327556  451 GPIIRAEEEDTIKVTFRNKASRPYSIQPHGVQYNiEMDGTlyhnvleesytakklreikkearVVEPlpaalVRPDTTYK 530
Cdd:cd11024     32 GPTLRATEGDLVRIHFINTGDHPHTIHFHGIHDA-AMDGT-----------------------GLGP-----IMPGESFT 82

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*...
gi 1564327556  531 YEWvVPKDAGptekdpdciTYMYYSAVDPIRD-TNSGLVGpLLICKPK 577
Cdd:cd11024     83 YEF-VAEPAG---------THLYHCHVQPLKEhIAMGLYG-AFIVDPK 119
SufI COG2132
Multicopper oxidase with three cupredoxin domains (includes cell division protein FtsP and ...
 95-202 6.81e-08

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: 56.10  E-value: 6.81e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1564327556   95 FLGPLISAEENDIVVVHLKNMAKRAYSIHAHGLSYNKSFEGAlypdssekaekADDSVAPGKSFSYVWTLPasHSPGkdd 174
Cdd:COG2132     42 YPGPTIRVREGDRVRVRVTNRLPEPTTVHWHGLRVPNAMDGV-----------PGDPIAPGETFTYEFPVP--QPAG--- 105

                           90       100       110
                   ....*....|....*....|....*....|
gi 1564327556  175 tnclTRIYHSHVNA--PKDIASGLIGPLII 202
Cdd:COG2132    106 ----TYWYHPHTHGstAEQVYRGLAGALIV 131
CuRO_1_2dMco_1 cd13860
The first cupredoxin domain of bacteria two domain multicopper oxidase; This subfamily ...
 451-573 7.35e-08

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: 51.81  E-value: 7.35e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1564327556  451 GPIIRAEEEDTIKVTFRNKASRPYSIQPHGVQYNIEMDGtlyhnvleesytakklreikkearvVEPLPAALVRPDTTYK 530
Cdd:cd13860     31 GPTIEVTEGDRVRILVTNELPEPTTVHWHGLPVPNGMDG-------------------------VPGITQPPIQPGETFT 85

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|...
gi 1564327556  531 YEWVVpKDAGptekdpdciTYMYYSAVDPIRDTNSGLVGPLLI 573
Cdd:cd13860     86 YEFTA-KQAG---------TYMYHSHVDEAKQEDMGLYGAFIV 118
CuRO_1_2DMCO_NIR_like_2 cd14449
The cupredoxin domain 1 of a two-domain laccase related to nitrite reductase; The two-domain ...
 451-545 1.02e-07

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: 51.88  E-value: 1.02e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1564327556  451 GPIIRAEEEDTIKVTFRNKASRPYSIQPHGVQYNIEMDGTLyhnvleesytakklreikkearvvepLPAALVRPDTTYK 530
Cdd:cd14449     29 GPVIEVREGDTLKILFRNTLDVPASLHPHGVDYTTASDGTG--------------------------MNASIVAPGDTRI 82

                           90
                   ....*....|....*
gi 1564327556  531 YEWvvpKDAGPTEKD 545
Cdd:cd14449     83 YTW---RTHGGYRRA 94
CuRO_3_Fet3p cd13899
The third Cupredoxin domain of multicopper oxidase Fet3p; Fet3p catalyzes the ferroxidase ...
 315-355 1.04e-07

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: 52.64  E-value: 1.04e-07
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|.
gi 1564327556  315 DTISLFPATFVNVEMVADNPGQWLLSCQVNDHLEAGMQAIF 355
Cdd:cd13899    116 DTVMVPPGGSVVIRFRADNPGVWFFHCHIEWHLEAGLAATF 156
Cu-oxidase_2 pfam07731
Multicopper oxidase; This entry contains many divergent copper oxidase-like domains that are ...
 255-358 1.09e-07

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: 52.05  E-value: 1.09e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1564327556  255 DFQESNKMHSINGYVFG-NLPDLSMCMGNKIHWHLFGMGNevDIHSAFFHG---QIL-------TEKQHHV--------- 314
Cdd:pfam07731   14 SGNFRRNDWAINGLLFPpNTNVITLPYGTVVEWVLQNTTT--GVHPFHLHGhsfQVLgrgggpwPEEDPKTynlvdpvrr 91

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....
gi 1564327556  315 DTISLFPATFVNVEMVADNPGQWLLSCQVNDHLEAGMQAIFEIK 358
Cdd:pfam07731   92 DTVQVPPGGWVAIRFRADNPGVWLFHCHILWHLDQGMMGQFVVR 135
CuRO_1_McoC_like cd13855
The first cupredoxin domain of a multicopper oxidase McoC and similar proteins; This family ...
 97-202 1.45e-07

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: 51.32  E-value: 1.45e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1564327556   97 GPLISAEENDIVVVHLKNMAKRAYSIHAHGLsynksfegalyPDSSEKAEKADDSVAPGKSFSYVWTLPAShSPGkddtn 176
Cdd:cd13855     32 GPLIEVFEGDTVEITFRNRLPEPTTVHWHGL-----------PVPPDQDGNPHDPVAPGNDRVYRFTLPQD-SAG----- 94

                           90       100
                   ....*....|....*....|....*...
gi 1564327556  177 clTRIYHSHVN--APKDIASGLIGPLII 202
Cdd:cd13855     95 --TYWYHPHPHghTAEQVYRGLAGAFVV 120
CuRO_1_tcLCC2_insect_like cd13858
The first cupredoxin domain of insect laccases similar to laccase 2 in Tribolium castaneum; ...
 97-202 1.58e-07

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: 50.62  E-value: 1.58e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1564327556   97 GPLISAEENDIVVVHLKN-MAKRAYSIHAHGLSYNKSfegalyPDSsekaekadDSVA--------PGKSFSYVWTlpAS 167
Cdd:cd13858     16 GPSIEVCEGDTVVVDVKNrLPGESTTIHWHGIHQRGT------PYM--------DGVPmvtqcpilPGQTFRYKFK--AD 79

                           90       100       110
                   ....*....|....*....|....*....|....*
gi 1564327556  168 HsPGkddtnclTRIYHSHVNAPKdiASGLIGPLII 202
Cdd:cd13858     80 P-AG-------THWYHSHSGTQR--ADGLFGALIV 104
SufI COG2132
Multicopper oxidase with three cupredoxin domains (includes cell division protein FtsP and ...
 449-573 2.74e-07

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: 54.17  E-value: 2.74e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1564327556  449 ILGPIIRAEEEDTIKVTFRNKASRPYSIQPHGVQYNIEMDGTlyhnvleesytakklreikkearvveplPAALVRPDTT 528
Cdd:COG2132     42 YPGPTIRVREGDRVRVRVTNRLPEPTTVHWHGLRVPNAMDGV----------------------------PGDPIAPGET 93

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*..
gi 1564327556  529 YKYEWVVPKDAGptekdpdciTYMYYSAVDPIRDTN--SGLVGPLLI 573
Cdd:COG2132     94 FTYEFPVPQPAG---------TYWYHPHTHGSTAEQvyRGLAGALIV 131
CuRO_D2_2dMcoN_like cd04202
The second cupredoxin domain of bacterial two domain multicopper oxidase McoN and similar ...
 262-351 6.04e-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: 6.04e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1564327556  262 MHSINGYVFGNLPDLSMCMGNKIHWHLFGMGNEVD---IHSAFFH------GQILTEKQHHVDTISLFPATFVNVEMVAD 332
Cdd:cd04202     29 YFTINGKSFPATPPLVVKEGDRVRIRLINLSMDHHpmhLHGHFFLvtatdgGPIPGSAPWPKDTLNVAPGERYDIEFVAD 108

                           90
                   ....*....|....*....
gi 1564327556  333 NPGQWLLSCQVNDHLEAGM 351
Cdd:cd04202    109 NPGDWMFHCHKLHHAMNGM 127
CuRO_1_CumA_like cd13861
The first cupredoxin domain of CumA like multicopper oxidase; This multicopper oxidase (MCO) ...
 819-912 1.59e-06

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: 48.00  E-value: 1.59e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1564327556  819 GIMGPMIHGKVGEKVKIVFKNMAKRPYSIHAHGVKTES-----PQV--ALTRPGETQTYTWYLPkNSGpteeqeecsVGA 891
Cdd:cd13861     28 QVPGPELRVRQGDTLRVRLTNRLPEPTTIHWHGLRLPNamdgvPGLtqPPVPPGESFTYEFTPP-DAG---------TYW 97

                           90       100
                   ....*....|....*....|.
gi 1564327556  892 YYSAVDVIKDMYSGLIGPLIV 912
Cdd:cd13861     98 YHPHVGSQEQLDRGLYGPLIV 118
CuRO_1_Tth-MCO_like cd13853
The first cupredoxin domain of the bacterial laccases similar to Tth-MCO from Thermus ...
 95-202 2.07e-06

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: 48.40  E-value: 2.07e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1564327556   95 FLGPLISAEENDIVVVHLKNMAKRAYS-----------------IHAHGLSYNksfegalyPDSSekaekADD---SVAP 154
Cdd:cd13853     29 IPGPTLRVRPGDTLRITLKNDLPPEGAaneapapntphcpnttnLHFHGLHVS--------PTGN-----SDNvflTIAP 95

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|..
gi 1564327556  155 GKSFSYVWTLPASHSPGkddtnclTRIYHSH----VNApkDIASGLIGPLII 202
Cdd:cd13853     96 GESFTYEYDIPADHPPG-------TYWYHPHlhgsTAL--QVAGGMAGALVV 138
CuRO_3_CopA cd13896
The third cupredoxin domain of CopA copper resistance protein family; CopA is a multicopper ...
 315-356 2.84e-06

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: 47.25  E-value: 2.84e-06
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|..
gi 1564327556  315 DTISLFPATFVNVEMVADNPGQWLLSCQVNDHLEAGMQAIFE 356
Cdd:cd13896     73 DTVLVPPGETVSVDFDADNPGRWAFHCHNLYHMEAGMMRVVE 114
CuRO_1_2DMCO_NIR_like_2 cd14449
The cupredoxin domain 1 of a two-domain laccase related to nitrite reductase; The two-domain ...
 822-872 2.95e-06

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: 47.65  E-value: 2.95e-06
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 1564327556  822 GPMIHGKVGEKVKIVFKNMAKRPYSIHAHGVKTESPQV------ALTRPGETQTYTW 872
Cdd:cd14449     29 GPVIEVREGDTLKILFRNTLDVPASLHPHGVDYTTASDgtgmnaSIVAPGDTRIYTW 85
CuRO_1_MaLCC_like cd13854
The first cupredoxin domain of the fungal laccases similar to Ma-LCC from Melanocarpus ...
 97-202 3.85e-06

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: 47.24  E-value: 3.85e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1564327556   97 GPLISAEENDIVVVHLKN-MAKRAYSIHAHGLS--YNKSFEGAlyPDSSEKAekaddsVAPGKSFSYVWTLpashspgkd 173
Cdd:cd13854     33 GPLIEANWGDTIEVTVINkLQDNGTSIHWHGIRqlNTNWQDGV--PGVTECP------IAPGDTRTYRFRA--------- 95

                           90       100
                   ....*....|....*....|....*....
gi 1564327556  174 dTNCLTRIYHSHVNApkDIASGLIGPLII 202
Cdd:cd13854     96 -TQYGTSWYHSHYSA--QYGDGVVGPIVI 121
SufI COG2132
Multicopper oxidase with three cupredoxin domains (includes cell division protein FtsP and ...
 822-912 8.65e-06

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: 49.55  E-value: 8.65e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1564327556  822 GPMIHGKVGEKVKIVFKNMAKRPYSIHAHGVKTESPQ----VALTRPGETQTYT----------WYLPKNSGPTEEQeec 887
Cdd:COG2132     44 GPTIRVREGDRVRVRVTNRLPEPTTVHWHGLRVPNAMdgvpGDPIAPGETFTYEfpvpqpagtyWYHPHTHGSTAEQ--- 120

                           90       100
                   ....*....|....*....|....*
gi 1564327556  888 svgayysavdvikdMYSGLIGPLIV 912
Cdd:COG2132    121 --------------VYRGLAGALIV 131
CuRO_1_AAO cd13845
The first cupredoxin domain of plant Ascorbate oxidase; Ascorbate oxidase catalyzes the ...
 94-202 9.54e-06

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: 45.90  E-value: 9.54e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1564327556   94 GFLGPLISAEENDIVVVHLKN-MAKRAYSIHAHGLSYnksfEGALYPDSSEKAEKAddSVAPGKSFSYVWTLpasHSPGk 172
Cdd:cd13845     27 QFPGPTIRATAGDTIVVELENkLPTEGVAIHWHGIRQ----RGTPWADGTASVSQC--PINPGETFTYQFVV---DRPG- 96

                           90       100       110
                   ....*....|....*....|....*....|
gi 1564327556  173 ddtnclTRIYHSHVNAPKdiASGLIGPLII 202
Cdd:cd13845     97 ------TYFYHGHYGMQR--SAGLYGSLIV 118
CuRO_3_McoC_like cd13902
The third cupredoxin domain of a multicopper oxidase McoC and similar proteins; This family ...
 972-1064 1.06e-05

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: 45.85  E-value: 1.06e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1564327556  972 MHGINGLVYG-NLKGLNMKVGDKVYWYLmgmgnevdIHTAH----FHGHSFDYKVSGTHRA----------DVFDLFPGT 1036
Cdd:cd13902     20 MFLINGKTFDmNRIDFVAKVGEVEVWEV--------TNTSHmdhpFHLHGTQFQVLEIDGNpqkpeyrawkDTVNLPPGE 91

                           90       100
                   ....*....|....*....|....*...
gi 1564327556 1037 FQTVTMRPQYSGTWLLHCHVTDHIQAGM 1064
Cdd:cd13902     92 AVRIATRQDDPGMWMYHCHILEHEDAGM 119
Cu-oxidase_3 pfam07732
Multicopper oxidase; This entry contains many divergent copper oxidase-like domains that are ...
 423-573 1.16e-05

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: 45.70  E-value: 1.16e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1564327556  423 KVQYVEYTDDTFTKRKERTSEEQhlgILGPIIRAEEEDTIKVTFRNKASRPYSIQPHGVQY--NIEMDGTLYhnvleesy 500
Cdd:pfam07732    1 TVTYGTVSPLGGTRQAVIGVNGQ---FPGPTIRVREGDTVVVNVTNNLDEPTSIHWHGLQQrgTPWMDGVPG-------- 69

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1564327556  501 takklreikkearvvepLPAALVRPDTTYKYEWVVPKDAGptekdpdciTYMYYSAVDPIRdtNSGLVGPLLI 573
Cdd:pfam07732   70 -----------------VTQCPIPPGQSFTYRFQVKQQAG---------TYWYHSHTSGQQ--AAGLAGAIII 114
CuRO_1_Abr2_like cd13850
The first cupredoxin domain of a group of fungal Laccases similar to Abr2 from Aspergillus ...
 88-202 1.27e-05

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: 45.37  E-value: 1.27e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1564327556   88 EKPKWLG---FLGPLISAEENDIVVVHLKNMAKRAYSIHAHGLSYNKSFEGALYPDSSEKAekaddsVAPGKSFSYVWTL 164
Cdd:cd13850     16 EREVILIngqFPGPPIILDEGDEVEILVTNNLPVNTTIHFHGILQRGTPWSDGVPGVTQWP------IQPGGSFTYRWKA 89

                           90       100       110
                   ....*....|....*....|....*....|....*...
gi 1564327556  165 PASHSpgkddtnclTRIYHSHVNApkDIASGLIGPLII 202
Cdd:cd13850     90 EDQYG---------LYWYHSHYRG--YYMDGLYGPIYI 116
CuRO_1_MCO_like_1 cd13862
The first cupredoxin domain of uncharacterized multicopper oxidase; Multicopper Oxidases (MCOs) ...
 97-202 1.41e-05

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: 45.59  E-value: 1.41e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1564327556   97 GPLISAEENDIVVVHLKNMAKRAYSIHAHGLSYNKSFEGAlypdssekAEKADDSVAPGKSFSYVWT-LPAShspgkddt 175
Cdd:cd13862     31 GPLLRMRQGVSVTVDVFNDTDIPEYVHWHGLPLPADVDGA--------MEEGTPSVPPHGHRRYRMTpRPAG-------- 94

                           90       100       110
                   ....*....|....*....|....*....|.
gi 1564327556  176 nclTRIYHSHVNAPKDIA----SGLIGPLII 202
Cdd:cd13862     95 ---FRWYHTHVMTMDDLTrgqySGLFGFVYI 122
CuRO_3_Tv-LCC_like cd13903
The third cupredoxin domain of the fungal laccases similar to Tv-LCC from Trametes Versicolor; ...
 1002-1064 1.59e-05

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: 46.12  E-value: 1.59e-05
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1564327556 1002 GNEVDIHTAHFHGHSFDYKVSGTH---------RADVFDL-FPGTFQTVTMRPQYSGTWLLHCHVTDHIQAGM 1064
Cdd:cd13903     67 GAIGGPHPFHLHGHAFSVVRSAGSntynyvnpvRRDVVSVgTPGDGVTIRFVTDNPGPWFLHCHIDWHLEAGL 139
CuRO_3_CopA cd13896
The third cupredoxin domain of CopA copper resistance protein family; CopA is a multicopper ...
 974-1070 2.16e-05

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: 44.55  E-value: 2.16e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1564327556  974 GINGLVYGNLKGLNMKVGDKVywyLMGMGNEVDI-HTAHFHGHSFDY-KVSGTHRA--DVFDLFPGtfQTVTMRPQYS-- 1047
Cdd:cd13896     18 TINGKAYPDADPLRVREGERV---RIVFVNDTMMaHPMHLHGHFFQVeNGNGEYGPrkDTVLVPPG--ETVSVDFDADnp 92

                           90       100
                   ....*....|....*....|...
gi 1564327556 1048 GTWLLHCHVTDHIQAGMETTYTV 1070
Cdd:cd13896     93 GRWAFHCHNLYHMEAGMMRVVEY 115
CuRO_1_McoC_like cd13855
The first cupredoxin domain of a multicopper oxidase McoC and similar proteins; This family ...
 822-912 2.54e-05

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: 44.77  E-value: 2.54e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1564327556  822 GPMIHGKVGEKVKIVFKNMAKRPYSIHAHGVKTESPQ-------VAltrPGETQTYTWYLPKNSGpteeqeecsvGAYY- 893
Cdd:cd13855     32 GPLIEVFEGDTVEITFRNRLPEPTTVHWHGLPVPPDQdgnphdpVA---PGNDRVYRFTLPQDSA----------GTYWy 98

                           90       100
                   ....*....|....*....|..
gi 1564327556  894 ---SAVDVIKDMYSGLIGPLIV 912
Cdd:cd13855     99 hphPHGHTAEQVYRGLAGAFVV 120
CuRO_1_Fet3p cd13851
The first Cupredoxin domain of multicopper oxidase Fet3P; Fet3p catalyzes the ferroxidase ...
 98-202 4.32e-05

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: 44.18  E-value: 4.32e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1564327556   98 PLISAEENDIVVVHLKN-MAKRAYSIHAHGLSYNksfeGALYPDSSEKAEKADdsVAPGKSFSYVWTLPASHSpgkddtn 176
Cdd:cd13851     32 PPIEVNKGDTVVIHATNsLGDQPTSLHFHGLFQN----GTNYMDGPVGVTQCP--IPPGQSFTYEFTVDTQVG------- 98

                           90       100
                   ....*....|....*....|....*.
gi 1564327556  177 clTRIYHSHVNApkDIASGLIGPLII 202
Cdd:cd13851     99 --TYWYHSHDGG--QYPDGLRGPFII 120
CuRO_3_MCO_like_3 cd13909
The third cupredoxin domain of uncharacterized multicopper oxidase; Multicopper Oxidases (MCOs) ...
 1008-1071 4.69e-05

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


Pssm-ID: 259976 [Multi-domain]  Cd Length: 137  Bit Score: 44.43  E-value: 4.69e-05
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1564327556 1008 HTAHFHGHSFdykvsgthRADVFDLFPGTFQ-TVTMRPQYS----------GTWLLHCHVTDHIQAGMETTYTVL 1071
Cdd:cd13909     71 HGMHLHGHHF--------RAILPNGALGPWRdTLLMDRGETreiafvadnpGDWLLHCHMLEHAAAGMMSWFRVT 137
CuRO_3_Fet3p cd13899
The third Cupredoxin domain of multicopper oxidase Fet3p; Fet3p catalyzes the ferroxidase ...
 1008-1072 4.75e-05

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: 44.94  E-value: 4.75e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1564327556 1008 HTAHFHGHSF--------------DYKVSGTH----RADVFDLFPGTFQTVTMRPQYSGTWLLHCHVTDHIQAGMetTYT 1069
Cdd:cd13899     78 HPFHLHGHKFqvvqrspdvasddpNPPINEFPenpmRRDTVMVPPGGSVVIRFRADNPGVWFFHCHIEWHLEAGL--AAT 155


                   ...
gi 1564327556 1070 VLE 1072
Cdd:cd13899    156 FIE 158
CuRO_1_2dMco_1 cd13860
The first cupredoxin domain of bacteria two domain multicopper oxidase; This subfamily ...
 822-912 4.83e-05

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: 43.72  E-value: 4.83e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1564327556  822 GPMIHGKVGEKVKIVFKNMAKRPYSIHAHGVK-----------TESPqvalTRPGETQTYTWYLpKNSGPTeeqeecsvg 890
Cdd:cd13860     31 GPTIEVTEGDRVRILVTNELPEPTTVHWHGLPvpngmdgvpgiTQPP----IQPGETFTYEFTA-KQAGTY--------- 96

                           90       100
                   ....*....|....*....|..
gi 1564327556  891 AYYSAVDVIKDMYSGLIGPLIV 912
Cdd:cd13860     97 MYHSHVDEAKQEDMGLYGAFIV 118
CuRO_3_Tv-LCC_like cd13903
The third cupredoxin domain of the fungal laccases similar to Tv-LCC from Trametes Versicolor; ...
 315-355 7.12e-05

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: 44.19  E-value: 7.12e-05
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|..
gi 1564327556  315 DTISL-FPATFVNVEMVADNPGQWLLSCQVNDHLEAGMQAIF 355
Cdd:cd13903    102 DVVSVgTPGDGVTIRFVTDNPGPWFLHCHIDWHLEAGLAVVF 143
ascorbase TIGR03388
L-ascorbate oxidase, plant type; Members of this protein family are the copper-containing ...
 95-202 7.66e-05

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: 46.67  E-value: 7.66e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1564327556   95 FLGPLISAEENDIVVVHLKN-MAKRAYSIHAHGLSYNksfeGALYPDSSEKAEKAddSVAPGKSFSYVWTLpasHSPGkd 173
Cdd:TIGR03388   29 FPGPTIRAQAGDTIVVELTNkLHTEGVVIHWHGIRQI----GTPWADGTAGVTQC--AINPGETFIYNFVV---DRPG-- 97

                           90       100
                   ....*....|....*....|....*....
gi 1564327556  174 dtnclTRIYHSHVNAPKdiASGLIGPLII 202
Cdd:TIGR03388   98 -----TYFYHGHYGMQR--SAGLYGSLIV 119
CuRO_1_2DMCO_NIR_like cd11024
The cupredoxin domain 1 of a two-domain laccase related to nitrite reductase; The two-domain ...
 97-202 1.07e-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. 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: 43.03  E-value: 1.07e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1564327556   97 GPLISAEENDIVVVHLKNMAKRAYSIHAHGLSYNKsfegalypdssEKAEKADDsVAPGKSFSYVWTlpaSHSPGkddtn 176
Cdd:cd11024     32 GPTLRATEGDLVRIHFINTGDHPHTIHFHGIHDAA-----------MDGTGLGP-IMPGESFTYEFV---AEPAG----- 91

                           90       100
                   ....*....|....*....|....*...
gi 1564327556  177 clTRIYHSHVnAP--KDIASGLIGPLII 202
Cdd:cd11024     92 --THLYHCHV-QPlkEHIAMGLYGAFIV 116
CuRO_3_MCO_like_3 cd13909
The third cupredoxin domain of uncharacterized multicopper oxidase; Multicopper Oxidases (MCOs) ...
 315-357 1.43e-04

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


Pssm-ID: 259976 [Multi-domain]  Cd Length: 137  Bit Score: 42.89  E-value: 1.43e-04
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|...
gi 1564327556  315 DTISLFPATFVNVEMVADNPGQWLLSCQVNDHLEAGMQAIFEI 357
Cdd:cd13909     94 DTLLMDRGETREIAFVADNPGDWLLHCHMLEHAAAGMMSWFRV 136
CuRO_3_AAO cd13893
The third cupredoxin domain of plant Ascorbate oxidase; Ascorbate oxidase catalyzes the ...
 315-356 1.62e-04

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: 43.18  E-value: 1.62e-04
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|..
gi 1564327556  315 DTISLFPATFVNVEMVADNPGQWLLSCQVNDHLEAGMQAIFE 356
Cdd:cd13893    104 NTVTIFPYGWTALRFKADNPGVWAFHCHIEWHFHMGMGVVFA 145
CuRO_3_McoC_like cd13902
The third cupredoxin domain of a multicopper oxidase McoC and similar proteins; This family ...
 255-357 1.67e-04

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: 42.39  E-value: 1.67e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1564327556  255 DFQE--SNKMHS----INGYVFG-NLPDLSMCMGNKIHWHLFG---MGNEVDIHSAFFhgQILTEKQHHV--------DT 316
Cdd:cd13902      7 VFSEgmSMGAGGmmflINGKTFDmNRIDFVAKVGEVEVWEVTNtshMDHPFHLHGTQF--QVLEIDGNPQkpeyrawkDT 84

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|.
gi 1564327556  317 ISLFPATFVNVEMVADNPGQWLLSCQVNDHLEAGMQAIFEI 357
Cdd:cd13902     85 VNLPPGEAVRIATRQDDPGMWMYHCHILEHEDAGMMGMLHV 125
PLN02191 PLN02191
L-ascorbate oxidase
 95-202 1.77e-04

L-ascorbate oxidase


Pssm-ID: 177843 [Multi-domain]  Cd Length: 574  Bit Score: 45.39  E-value: 1.77e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1564327556   95 FLGPLISAEENDIVVVHLKN-MAKRAYSIHAHGLSYnksfEGALYPDSSEKAEKAddSVAPGKSFSYVWTLpasHSPGkd 173
Cdd:PLN02191    51 FPGPTIDAVAGDTIVVHLTNkLTTEGLVIHWHGIRQ----KGSPWADGAAGVTQC--AINPGETFTYKFTV---EKPG-- 119

                           90       100
                   ....*....|....*....|....*....
gi 1564327556  174 dtnclTRIYHSHVNAPKdiASGLIGPLII 202
Cdd:PLN02191   120 -----THFYHGHYGMQR--SAGLYGSLIV 141
CuRO_D1_2dMcoN_like cd13859
The first cupredoxin domain of bacterial two domain multicopper oxidase McoN and similar ...
 820-872 2.04e-04

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: 42.08  E-value: 2.04e-04
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1564327556  820 IMGPMIHGKVGEKVKIVFKNMAKRPYSIHAHGV-KTES------PQVA--LTRPGETQTYTW 872
Cdd:cd13859     29 VPGPLIHVKEGDDLVVHVTNNTTLPHTIHWHGVlQMGSwkmdgvPGVTqpAIEPGESFTYKF 90
CuRO_3_MaLCC_like cd13901
The third cupredoxin domain of the fungal laccases similar to Ma-LCC from Melanocarpus ...
 1008-1064 2.33e-04

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: 42.60  E-value: 2.33e-04
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1564327556 1008 HTAHFHGHSF--------DYKVSGT-------HRADVFDLFPGTFQTVTMRPQYSGTWLLHCHVTDHIQAGM 1064
Cdd:cd13901     81 HPIHLHGHDFyilaqgtgTFDDDGTilnlnnpPRRDVAMLPAGGYLVIAFKTDNPGAWLMHCHIAWHASGGL 152
CuRO_1_2DMCO_NIR_like cd11024
The cupredoxin domain 1 of a two-domain laccase related to nitrite reductase; The two-domain ...
 822-872 3.30e-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. 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: 41.49  E-value: 3.30e-04
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....
gi 1564327556  822 GPMIHGKVGEKVKIVFKNMAKRPYSIHAHGVKTES---PQVALTRPGETQTYTW 872
Cdd:cd11024     32 GPTLRATEGDLVRIHFINTGDHPHTIHFHGIHDAAmdgTGLGPIMPGESFTYEF 85
PLN02191 PLN02191
L-ascorbate oxidase
 245-355 3.61e-04

L-ascorbate oxidase


Pssm-ID: 177843 [Multi-domain]  Cd Length: 574  Bit Score: 44.62  E-value: 3.61e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1564327556  245 APAKVNKDDED------FQESNKMHSINGYVFGNLPDLSMCMGN-------KIH-WHLFGMGNEVdihSAFFHGQI---L 307
Cdd:PLN02191   414 SPPRSYRMDYDimnpppFPNTTTGNGIYVFPFNVTVDVIIQNANvlkgvvsEIHpWHLHGHDFWV---LGYGDGKFkpgI 490

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....
gi 1564327556  308 TEKQHHV------DTISLFPATFVNVEMVADNPGQWLLSCQVNDHLEAGMQAIF 355
Cdd:PLN02191   491 DEKTYNLknpplrNTAILYPYGWTAIRFVTDNPGVWFFHCHIEPHLHMGMGVVF 544
CuRO_1_CuNIR cd11020
Cupredoxin domain 1 of Copper-containing nitrite reductase; Copper-containing nitrite ...
 820-872 4.64e-04

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: 41.04  E-value: 4.64e-04
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 1564327556  820 IMGPMIHGKVGEKVKIVFKNM--AKRPYSIHAHGVkTESPQVALT--RPGETQTYTW 872
Cdd:cd11020     30 VPGPVIRVREGDTVELTLTNPgtNTMPHSIDFHAA-TGPGGGEFTtiAPGETKTFSF 85
CuRO_1_Tv-LCC_like cd13856
The first cupredoxin domain of fungal laccases similar to Tv-LCC from Trametes versicolor; ...
 95-202 5.38e-04

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: 41.17  E-value: 5.38e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1564327556   95 FLGPLISAEENDIVVVHLKN------MaKRAYSIHAHGLSynksFEGALYPDSSEKAEKAddSVAPGKSFSYvwTLPASH 168
Cdd:cd13856     28 FPGPLITANKGDTFRITVVNqltdptM-RRSTSIHWHGIF----QHGTNYADGPAFVTQC--PIAPNHSFTY--DFTAGD 98

                           90       100       110
                   ....*....|....*....|....*....|....
gi 1564327556  169 SPGkddtnclTRIYHSHVNApkDIASGLIGPLII 202
Cdd:cd13856     99 QAG-------TFWYHSHLST--QYCDGLRGPLVI 123
SufI COG2132
Multicopper oxidase with three cupredoxin domains (includes cell division protein FtsP and ...
 262-359 5.63e-04

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: 43.77  E-value: 5.63e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1564327556  262 MHSINGYVFG-NLPDLSMCMGNKIHWHLFGMGNE---VDIHSAFFhgQIL------TEKQHHVDTISLFPATFVNVEMVA 331
Cdd:COG2132    317 VWTINGKAFDpDRPDLTVKLGERERWTLVNDTMMphpFHLHGHQF--QVLsrngkpPPEGGWKDTVLVPPGETVRILFRF 394

                           90       100
                   ....*....|....*....|....*....
gi 1564327556  332 DN-PGQWLLSCQVNDHLEAGMQAIFEIKK 359
Cdd:COG2132    395 DNyPGDWMFHCHILEHEDAGMMGQFEVVP 423
ascorbase TIGR03388
L-ascorbate oxidase, plant type; Members of this protein family are the copper-containing ...
 315-356 6.86e-04

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: 43.59  E-value: 6.86e-04
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|..
gi 1564327556  315 DTISLFPATFVNVEMVADNPGQWLLSCQVNDHLEAGMQAIFE 356
Cdd:TIGR03388  481 NTVVIFPYGWTALRFVADNPGVWAFHCHIEPHLHMGMGVVFA 522
CuRO_3_tcLLC2_insect_like cd13905
The third cupredoxin domain of the insect laccases similar to laccase 2 in Tribolium castaneum; ...
 315-367 7.39e-04

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: 41.51  E-value: 7.39e-04
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....
gi 1564327556  315 DTISLfPAT-FVNVEMVADNPGQWLLSCQVNDHLEAGMQAIFeiKKCFPNVHKP 367
Cdd:cd13905    123 DTVVV-PNGgYVVIRFRADNPGYWLLHCHIEFHLLEGMALVL--KVGEPSDPPP 173
CuRO_1_Diphenol_Ox cd13857
The first cupredoxin domain of fungal laccase, diphenol oxidase; Diphenol oxidase belongs to ...
 451-573 1.01e-03

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: 39.93  E-value: 1.01e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1564327556  451 GPIIRAEEEDTIKVTFRNKASRPYSIQPHGV-QYNI-EMDGTlyhnvleesytakklreikkeARVVE-PLPaalvrPDT 527
Cdd:cd13857     30 GPLIEANQGDRIVVHVTNELDEPTSIHWHGLfQNGTnWMDGT---------------------AGITQcPIP-----PGG 83

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*..
gi 1564327556  528 TYKYEWVVPKDAGptekdpdciTYMYYSAVDPirdTNS-GLVGPLLI 573
Cdd:cd13857     84 SFTYNFTVDGQYG---------TYWYHSHYST---QYAdGLVGPLIV 118
CuRO_1_McoP_like cd13852
The first cupredoxin domain of multicopper oxidase McoP and similar proteins; This family ...
 450-555 1.38e-03

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: 39.58  E-value: 1.38e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1564327556  450 LGPIIRAEEEDTIKVTFRNKASRPYSIQPHGVQYNIEMDGtlyHnvleesytakklreikkearvveplPAALVRPDTTY 529
Cdd:cd13852     23 LGPILRLRKGQKVRITFKNNLPEPTIIHWHGLHVPAAMDG---H-------------------------PRYAIDPGETY 74

                           90       100
                   ....*....|....*....|....*.
gi 1564327556  530 KYEWVVPKDAGptekdpdciTYMYYS 555
Cdd:cd13852     75 VYEFEVLNRAG---------TYWYHP 91
CuRO_3_MCO_like_4 cd13910
The third cupredoxin domain of uncharacterized multicopper oxidase; Multicopper Oxidases (MCOs) ...
 1008-1064 2.25e-03

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: 39.97  E-value: 2.25e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1564327556 1008 HTAHFHGHSF-------DYKVSGTHRADVfdlfPGTFQTVT-MR------PQYS-----------GTWLLHCHVTDHIQA 1062
Cdd:cd13910     83 HPFHLHGHKFwvlgsgdGRYGGGGYTAPD----GTSLNTTNpLRrdtvsvPGFGwavlrfvadnpGLWAFHCHILWHMAA 158


                   ..
gi 1564327556 1063 GM 1064
Cdd:cd13910    159 GM 160
PLN02604 PLN02604
oxidoreductase
 94-202 2.49e-03

oxidoreductase


Pssm-ID: 215324 [Multi-domain]  Cd Length: 566  Bit Score: 41.77  E-value: 2.49e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1564327556   94 GFLGPLISAEENDIVVVHLKN-MAKRAYSIHAHGLSYnksfEGALYPDSSEKAEKAddSVAPGKSFSYVWTLpasHSPGk 172
Cdd:PLN02604    51 RSPGPTILAQQGDTVIVELKNsLLTENVAIHWHGIRQ----IGTPWFDGTEGVTQC--PILPGETFTYEFVV---DRPG- 120

                           90       100       110
                   ....*....|....*....|....*....|
gi 1564327556  173 ddtnclTRIYHSHVNAPKdiASGLIGPLII 202
Cdd:PLN02604   121 ------TYLYHAHYGMQR--EAGLYGSIRV 142
CuRO_1_2DMCO_NIR_like cd11024
The cupredoxin domain 1 of a two-domain laccase related to nitrite reductase; The two-domain ...
 976-1064 4.83e-03

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: 38.02  E-value: 4.83e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1564327556  976 NGLVYGNLkgLNMKVGDKVYWYLMGMGNevDIHTAHFHGhsfdykvsgTHRA----DVF-DLFPGTFQTVTMRPQYSGTW 1050
Cdd:cd11024     27 NGTVPGPT--LRATEGDLVRIHFINTGD--HPHTIHFHG---------IHDAamdgTGLgPIMPGESFTYEFVAEPAGTH 93

                           90
                   ....*....|....*..
gi 1564327556 1051 LLHCHV---TDHIQAGM 1064
Cdd:cd11024     94 LYHCHVqplKEHIAMGL 110
CuRO_1_CuNIR_like cd04201
Cupredoxin domain 1 of Copper-containing nitrite reductase and two-domain laccase; ...
 97-202 5.08e-03

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: 38.24  E-value: 5.08e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1564327556   97 GPLISAEENDIVVVHLKNMAKRA--YSIHAHGLSynksfeGALypdssekAEKADDSVAPGKSFSYVW--TLPASHspgk 172
Cdd:cd04201     32 GPMLRVREGDTVELHFSNNPSSTmpHNIDFHAAT------GAG-------GGAGATFIAPGETSTFSFkaTQPGLY---- 94

                           90       100       110
                   ....*....|....*....|....*....|.
gi 1564327556  173 ddtncltrIYHSHVNA-PKDIASGLIGPLII 202
Cdd:cd04201     95 --------VYHCAVAPvPMHIANGMYGLILV 117
CuRO_3_MCO_like_4 cd13910
The third cupredoxin domain of uncharacterized multicopper oxidase; Multicopper Oxidases (MCOs) ...
 315-351 5.42e-03

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: 38.82  E-value: 5.42e-03
                           10        20        30
                   ....*....|....*....|....*....|....*..
gi 1564327556  315 DTISLFPATFVNVEMVADNPGQWLLSCQVNDHLEAGM 351
Cdd:cd13910    124 DTVSVPGFGWAVLRFVADNPGLWAFHCHILWHMAAGM 160
CuRO_3_MCO_like_2 cd13908
The third cupredoxin domain of uncharacterized multicopper oxidase; Multicopper Oxidases (MCOs) ...
 315-356 5.57e-03

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: 38.20  E-value: 5.57e-03
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|..
gi 1564327556  315 DTISLFPATFVNVEMVADNPGQWLLSCQVNDHLEAGMQAIFE 356
Cdd:cd13908     80 DVVMLGGYQRVEVDFVADNPGLTLFHCHQQLHMDYGFMALFK 121
CuRO_1_CopA cd13848
The first cupredoxin domain of CopA copper resistance protein family; CopA is a multicopper ...
 97-202 5.93e-03

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: 37.65  E-value: 5.93e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1564327556   97 GPLISAEENDIVVVHLKNMAKRAYSIHAHGLSYNKSFEGAlyPDSSEKAekaddsVAPGKSFSYVWTLPASHspgkddtn 176
Cdd:cd13848     30 GPLLRFKEGDDATIRVHNRLDEDTSIHWHGLLLPNDMDGV--PGLSFPG------IKPGETFTYRFPVRQSG-------- 93

                           90       100
                   ....*....|....*....|....*.
gi 1564327556  177 clTRIYHSHVNAPKDIasGLIGPLII 202
Cdd:cd13848     94 --TYWYHSHSGLQEQT--GLYGPIII 115
CuRO_1_LCC_plant cd13849
The first cupredoxin domain of plant laccases; Laccase is a blue multicopper oxidase (MCO) ...
 95-126 9.02e-03

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: 37.24  E-value: 9.02e-03
                           10        20        30
                   ....*....|....*....|....*....|..
gi 1564327556   95 FLGPLISAEENDIVVVHLKNMAKRAYSIHAHG 126
Cdd:cd13849     26 FPGPTIRVHEGDTVVVNVTNRSPYNITIHWHG 57
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

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