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Conserved domains on  [gi|2559057711|ref|XP_058616241|]
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ceruloplasmin [Onychostoma macrolepis]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
CuRO_1_ceruloplasmin cd04222
The first cupredoxin domain of Ceruloplasmin; Ceruloplasmin is a multicopper oxidase essential ...
 23-205 1.90e-116

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: 356.73  E-value: 1.90e-116
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2559057711   23 REYFFAIKEIQWDYAPSGKNLIQNKTIKEDEEARVFLERGEQRIGRVYKKAVYQQYTDATYRQEIDKPKWLGYLGPLISA 102
Cdd:cd04222      1 REYYIGIRETQWDYAPSGKNLITNQTFDDDEHASVFLKRGPDRIGRVYKKAVYLQYTDDTYRTEIEKPVWLGFLGPILKA 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2559057711  103 EEDDVVIVHLKNTARRAYSIHAHGLSYNKTNEGALYPDSSEKVEKADDSVAPGKSFTYVWTLPASHTPGKDETNCLTRIY 182
Cdd:cd04222     81 EVGDVIVVHLKNFASRPYSLHPHGVFYNKENEGALYPDNTSGFEKADDAVPPGGSYTYTWTVPEEQAPTKADANCLTRIY 160

                          170       180
                   ....*....|....*....|...
gi 2559057711  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 1.56e-108

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: 335.21  E-value: 1.56e-108
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2559057711  745 KKYYIAAVEMDWDYSPTRTWEEQLHHSLKDSPGNKFLKKEGKFIGSKYKKVLYREYTDETFTKPKERSADMEHLGIMGPM 824
Cdd:cd04225      1 RTYYIAAEEVEWDYSPQRTWEQELHNTHEESPGNAFLNKGDKFIGSKYKKVVYREYTDDTFSVPKERTAEEEHLGILGPL 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2559057711  825 IHGKVGEKVKIVFKNMAKRPYSIHAHGVKTDSPQVALTRPGETKTYTWYLPKNSGPTEQQEECSVGAYYSTVDVIKDMYS 904
Cdd:cd04225     81 IHAEVGEKVKIVFKNMASRPYSIHAHGVKTDSSWVAPTEPGETQTYTWKIPERSGPGVEDSNCISWAYYSTVDQIKDLYS 160

                          170
                   ....*....|.
gi 2559057711  905 GLIGPLVICKK 915
Cdd:cd04225    161 GLIGPLVICRR 171
Cupredoxin super family cl19115
Cupredoxin superfamily; Cupredoxins contain type I copper centers and are involved in ...
 371-585 7.76e-101

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: 315.95  E-value: 7.76e-101
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2559057711  371 GEVRQYYIAAEEIIWDYGPTGINQYSGMKLVD-DSVSDTFFENRNDRIGGKYKKVQYVEYADDTFTKRKERTPEEQHLGI 449
Cdd:cd04224      1 GKVRHYFIAAEEIMWDYAPSGKNLFTGQNLTApGSDSEVFFQRNETRIGGTYWKVRYVEYTDATFTTRKHRSKEEEHLGI 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2559057711  450 LGPIIRAEEEDTIKVTFRNKASRPYSIQPHGVQYSIEMDGTLYHNvleesytakklrelkkearvVEPLPAALVRPDTTY 529
Cdd:cd04224     81 LGPVIRAEVGDTIKVTFRNKASRPFSIQPHGVFYEKNYEGAMYRD--------------------GDPSPGSHVSPGETF 140

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 2559057711  530 QYEWVVPKDGGPTEKDPDCITYMYYSAVDPIRDTNSGLVGPLLICKPKTL-KSGKQK 585
Cdd:cd04224    141 TYEWTVPEGVGPTNQDPPCLTYLYFSAVDPVRDTNSGLVGPLLVCKKGSLnANGRQK 197
CuRO_2_ceruloplasmin cd11021
The second cupredoxin domain of Ceruloplasmin; Ceruloplasmin is a multicopper oxidase ...
 217-357 8.18e-93

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: 292.07  E-value: 8.18e-93
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2559057711  217 DYLYTLMFTVSDENLSWYLEENIKTYCTAPAKVNKDDEGFQESNKMHSINGYVYGNLPDLSMCMGNKIHWHLFGMGNEVD 296
Cdd:cd11021      1 DREFVLMFSVVDENLSWYLDENIKTYCSEPAKVDKDDEDFQESNKMHSINGYTFGNLPGLSMCAGDRVKWHLFGMGNEVD 80

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2559057711  297 LHSAFFHGQILTDKRHHVDTVSLFPATFVHVEMVADNPGQWLLSCQVNDHMEAGMQAIFEI 357
Cdd:cd11021     81 IHSAFFHGQTLTDRGHRTDTINLFPATFVTAEMVAQNPGKWLLSCQVNDHLKAGMQAFYEV 141
CuRO_4_ceruloplasmin cd11022
The fourth cupredoxin domain of Ceruloplasmin; Ceruloplasmin is a multicopper oxidase ...
 588-731 6.97e-92

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: 289.77  E-value: 6.97e-92
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2559057711  588 DKEFHLLATVFDENLSWYLDDNINRFAKQPKSVKKEDEDFQESNKMHSLNGYMYGNLIGLSMCKGDKVSWHLSGLGSEVD 667
Cdd:cd11022      1 DKEFFLLFTVFDENESWYLDENIQQFTLDPRSVDKEDEDFQESNKMHSINGYMYGNQPGLDMCKGDTVSWHLFGLGTETD 80

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2559057711  668 IHGLYFEGNRFLYKDTRRDTINVFPHISHTVIMEPDSMGQFEVGCKTTDHYHGGMRANYTVEKC 731
Cdd:cd11022     81 VHGIYFSGNTFLLQGTRRDTANLFPHTSVTAIMQPDNEGTFEVNCQTTDHYSAGMRQIYTVSQC 144
Cupredoxin super family cl19115
Cupredoxin superfamily; Cupredoxins contain type I copper centers and are involved in ...
 928-1071 9.47e-91

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 cd11012:

Pssm-ID: 473140 [Multi-domain]  Cd Length: 145  Bit Score: 286.76  E-value: 9.47e-91
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2559057711  928 EEFALLFMVFDENESWYLDDNIKAHVKTPPTTLKEDEEFIESNKMHGINGLVYGNLKGLNMKVGDKVYWYLMGMGNEVDI 1007
Cdd:cd11012      2 LEFALLFLVFDENESWYLDENIKTYSDHPEKVNKEDEEFIESNKMHAINGKVFGNLQGLTMHVGDEVYWYLMGMGNEIDI 81

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2559057711 1008 HTAHFHGHSFDYKIGGTHRADVFDLFPGTFQTITMRPLYSGTWLLHCHVTDHIQAGMETTYTVL 1071
Cdd:cd11012     82 HTAHFHGHSFDYKHRGVYRSDVFDLFPGTFQTVEMIPRTPGTWLLHCHVTDHIHAGMETTYTVL 145
 
Name Accession Description Interval E-value
CuRO_1_ceruloplasmin cd04222
The first cupredoxin domain of Ceruloplasmin; Ceruloplasmin is a multicopper oxidase essential ...
 23-205 1.90e-116

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: 356.73  E-value: 1.90e-116
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2559057711   23 REYFFAIKEIQWDYAPSGKNLIQNKTIKEDEEARVFLERGEQRIGRVYKKAVYQQYTDATYRQEIDKPKWLGYLGPLISA 102
Cdd:cd04222      1 REYYIGIRETQWDYAPSGKNLITNQTFDDDEHASVFLKRGPDRIGRVYKKAVYLQYTDDTYRTEIEKPVWLGFLGPILKA 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2559057711  103 EEDDVVIVHLKNTARRAYSIHAHGLSYNKTNEGALYPDSSEKVEKADDSVAPGKSFTYVWTLPASHTPGKDETNCLTRIY 182
Cdd:cd04222     81 EVGDVIVVHLKNFASRPYSLHPHGVFYNKENEGALYPDNTSGFEKADDAVPPGGSYTYTWTVPEEQAPTKADANCLTRIY 160

                          170       180
                   ....*....|....*....|...
gi 2559057711  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 1.56e-108

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: 335.21  E-value: 1.56e-108
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2559057711  745 KKYYIAAVEMDWDYSPTRTWEEQLHHSLKDSPGNKFLKKEGKFIGSKYKKVLYREYTDETFTKPKERSADMEHLGIMGPM 824
Cdd:cd04225      1 RTYYIAAEEVEWDYSPQRTWEQELHNTHEESPGNAFLNKGDKFIGSKYKKVVYREYTDDTFSVPKERTAEEEHLGILGPL 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2559057711  825 IHGKVGEKVKIVFKNMAKRPYSIHAHGVKTDSPQVALTRPGETKTYTWYLPKNSGPTEQQEECSVGAYYSTVDVIKDMYS 904
Cdd:cd04225     81 IHAEVGEKVKIVFKNMASRPYSIHAHGVKTDSSWVAPTEPGETQTYTWKIPERSGPGVEDSNCISWAYYSTVDQIKDLYS 160

                          170
                   ....*....|.
gi 2559057711  905 GLIGPLVICKK 915
Cdd:cd04225    161 GLIGPLVICRR 171
CuRO_3_ceruloplasmin cd04224
The third cupredoxin domain of Ceruloplasmin; Ceruloplasmin is a multicopper oxidase essential ...
 371-585 7.76e-101

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: 315.95  E-value: 7.76e-101
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2559057711  371 GEVRQYYIAAEEIIWDYGPTGINQYSGMKLVD-DSVSDTFFENRNDRIGGKYKKVQYVEYADDTFTKRKERTPEEQHLGI 449
Cdd:cd04224      1 GKVRHYFIAAEEIMWDYAPSGKNLFTGQNLTApGSDSEVFFQRNETRIGGTYWKVRYVEYTDATFTTRKHRSKEEEHLGI 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2559057711  450 LGPIIRAEEEDTIKVTFRNKASRPYSIQPHGVQYSIEMDGTLYHNvleesytakklrelkkearvVEPLPAALVRPDTTY 529
Cdd:cd04224     81 LGPVIRAEVGDTIKVTFRNKASRPFSIQPHGVFYEKNYEGAMYRD--------------------GDPSPGSHVSPGETF 140

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 2559057711  530 QYEWVVPKDGGPTEKDPDCITYMYYSAVDPIRDTNSGLVGPLLICKPKTL-KSGKQK 585
Cdd:cd04224    141 TYEWTVPEGVGPTNQDPPCLTYLYFSAVDPVRDTNSGLVGPLLVCKKGSLnANGRQK 197
CuRO_2_ceruloplasmin cd11021
The second cupredoxin domain of Ceruloplasmin; Ceruloplasmin is a multicopper oxidase ...
 217-357 8.18e-93

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: 292.07  E-value: 8.18e-93
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2559057711  217 DYLYTLMFTVSDENLSWYLEENIKTYCTAPAKVNKDDEGFQESNKMHSINGYVYGNLPDLSMCMGNKIHWHLFGMGNEVD 296
Cdd:cd11021      1 DREFVLMFSVVDENLSWYLDENIKTYCSEPAKVDKDDEDFQESNKMHSINGYTFGNLPGLSMCAGDRVKWHLFGMGNEVD 80

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2559057711  297 LHSAFFHGQILTDKRHHVDTVSLFPATFVHVEMVADNPGQWLLSCQVNDHMEAGMQAIFEI 357
Cdd:cd11021     81 IHSAFFHGQTLTDRGHRTDTINLFPATFVTAEMVAQNPGKWLLSCQVNDHLKAGMQAFYEV 141
CuRO_4_ceruloplasmin cd11022
The fourth cupredoxin domain of Ceruloplasmin; Ceruloplasmin is a multicopper oxidase ...
 588-731 6.97e-92

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: 289.77  E-value: 6.97e-92
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2559057711  588 DKEFHLLATVFDENLSWYLDDNINRFAKQPKSVKKEDEDFQESNKMHSLNGYMYGNLIGLSMCKGDKVSWHLSGLGSEVD 667
Cdd:cd11022      1 DKEFFLLFTVFDENESWYLDENIQQFTLDPRSVDKEDEDFQESNKMHSINGYMYGNQPGLDMCKGDTVSWHLFGLGTETD 80

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2559057711  668 IHGLYFEGNRFLYKDTRRDTINVFPHISHTVIMEPDSMGQFEVGCKTTDHYHGGMRANYTVEKC 731
Cdd:cd11022     81 VHGIYFSGNTFLLQGTRRDTANLFPHTSVTAIMQPDNEGTFEVNCQTTDHYSAGMRQIYTVSQC 144
CuRO_6_ceruloplasmin cd11012
The sixth cupredoxin domain of Ceruloplasmin; Ceruloplasmin is a multicopper oxidase essential ...
 928-1071 9.47e-91

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: 286.76  E-value: 9.47e-91
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2559057711  928 EEFALLFMVFDENESWYLDDNIKAHVKTPPTTLKEDEEFIESNKMHGINGLVYGNLKGLNMKVGDKVYWYLMGMGNEVDI 1007
Cdd:cd11012      2 LEFALLFLVFDENESWYLDENIKTYSDHPEKVNKEDEEFIESNKMHAINGKVFGNLQGLTMHVGDEVYWYLMGMGNEIDI 81

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2559057711 1008 HTAHFHGHSFDYKIGGTHRADVFDLFPGTFQTITMRPLYSGTWLLHCHVTDHIQAGMETTYTVL 1071
Cdd:cd11012     82 HTAHFHGHSFDYKHRGVYRSDVFDLFPGTFQTVEMIPRTPGTWLLHCHVTDHIHAGMETTYTVL 145
Cu-oxidase_2 pfam07731
Multicopper oxidase; This entry contains many divergent copper oxidase-like domains that are ...
 970-1074 7.19e-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: 81.33  E-value: 7.19e-18
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2559057711  970 NKMHGINGLVYG-NLKGLNMKVGDKVYWYLMGMGNevDIHTAHFHGHSFD----------YKIGGTH------RADVFDL 1032
Cdd:pfam07731   19 RNDWAINGLLFPpNTNVITLPYGTVVEWVLQNTTT--GVHPFHLHGHSFQvlgrgggpwpEEDPKTYnlvdpvRRDTVQV 96

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|..
gi 2559057711 1033 FPGTFQTITMRPLYSGTWLLHCHVTDHIQAGMETTYTVLEKD 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 7.82e-10

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: 57.64  E-value: 7.82e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2559057711   95 YLGPLISAEEDDVVIVHLKNTARRAYSIHAHGLSYNKTNEGALYPDSSEkvekadDSVAPGKSFTYVWtlPASHTPGkde 174
Cdd:pfam07732   24 FPGPTIRVREGDTVVVNVTNNLDEPTSIHWHGLQQRGTPWMDGVPGVTQ------CPIPPGQSFTYRF--QVKQQAG--- 92

                           90       100
                   ....*....|....*....|....*...
gi 2559057711  175 tnclTRIYHSHVNAPKdiASGLIGPLII 202
Cdd:pfam07732   93 ----TYWYHSHTSGQQ--AAGLAGAIII 114
SufI COG2132
Multicopper oxidase with three cupredoxin domains (includes cell division protein FtsP and ...
 95-202 1.19e-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: 58.79  E-value: 1.19e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2559057711   95 YLGPLISAEEDDVVIVHLKNTARRAYSIHAHGLSYNKTNEGAlypdssekvekADDSVAPGKSFTYVWTLPasHTPGkde 174
Cdd:COG2132     42 YPGPTIRVREGDRVRVRVTNRLPEPTTVHWHGLRVPNAMDGV-----------PGDPIAPGETFTYEFPVP--QPAG--- 105

                           90       100       110
                   ....*....|....*....|....*....|
gi 2559057711  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 2.57e-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: 2.57e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2559057711  449 ILGPIIRAEEEDTIKVTFRNKASRPYSIQPHGVQYSIEMDGTlyhnvleesytakklrelkkearvveplPAALVRPDTT 528
Cdd:COG2132     42 YPGPTIRVREGDRVRVRVTNRLPEPTTVHWHGLRVPNAMDGV----------------------------PGDPIAPGET 93

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*..
gi 2559057711  529 YQYEWVVPKDGGptekdpdciTYMYYSAVDPIRDTN--SGLVGPLLI 573
Cdd:COG2132     94 FTYEFPVPQPAG---------TYWYHPHTHGSTAEQvyRGLAGALIV 131
Cu-oxidase_2 pfam07731
Multicopper oxidase; This entry contains many divergent copper oxidase-like domains that are ...
 256-358 4.27e-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: 50.13  E-value: 4.27e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2559057711  256 FQESNKMHSINGYVYG-NLPDLSMCMGNKIHWHLFGMGNEVD---LHSAFF------HGQILTDKRHHV--------DTV 317
Cdd:pfam07731   15 GNFRRNDWAINGLLFPpNTNVITLPYGTVVEWVLQNTTTGVHpfhLHGHSFqvlgrgGGPWPEEDPKTYnlvdpvrrDTV 94

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|.
gi 2559057711  318 SLFPATFVHVEMVADNPGQWLLSCQVNDHMEAGMQAIFEIK 358
Cdd:pfam07731   95 QVPPGGWVAIRFRADNPGVWLFHCHILWHLDQGMMGQFVVR 135
SufI COG2132
Multicopper oxidase with three cupredoxin domains (includes cell division protein FtsP and ...
 972-1072 8.32e-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: 52.63  E-value: 8.32e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2559057711  972 MHGINGLVYGNLK-GLNMKVGDKVYWYLMGMGNevDIHTAHFHGHSF------DYKIGGTHRADVFDLFPGtfQTITMR- 1043
Cdd:COG2132    317 VWTINGKAFDPDRpDLTVKLGERERWTLVNDTM--MPHPFHLHGHQFqvlsrnGKPPPEGGWKDTVLVPPG--ETVRILf 392

                           90       100       110
                   ....*....|....*....|....*....|.
gi 2559057711 1044 --PLYSGTWLLHCHVTDHIQAGMETTYTVLE 1072
Cdd:COG2132    393 rfDNYPGDWMFHCHILEHEDAGMMGQFEVVP 423
SufI COG2132
Multicopper oxidase with three cupredoxin domains (includes cell division protein FtsP and ...
 262-359 6.84e-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: 49.93  E-value: 6.84e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2559057711  262 MHSINGYVYG-NLPDLSMCMGNKIHWHLFGMGNE---VDLHSAFFhgQIL------TDKRHHVDTVSLFPATFVHVEMVA 331
Cdd:COG2132    317 VWTINGKAFDpDRPDLTVKLGERERWTLVNDTMMphpFHLHGHQF--QVLsrngkpPPEGGWKDTVLVPPGETVRILFRF 394

                           90       100
                   ....*....|....*....|....*....
gi 2559057711  332 DN-PGQWLLSCQVNDHMEAGMQAIFEIKK 359
Cdd:COG2132    395 DNyPGDWMFHCHILEHEDAGMMGQFEVVP 423
SufI COG2132
Multicopper oxidase with three cupredoxin domains (includes cell division protein FtsP and ...
 822-912 3.83e-05

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: 47.24  E-value: 3.83e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2559057711  822 GPMIHGKVGEKVKIVFKNMAKRPYSIHAHGVKTDSPQ----VALTRPGETKTYT----------WYLPKNSGPTEQQeec 887
Cdd:COG2132     44 GPTIRVREGDRVRVRVTNRLPEPTTVHWHGLRVPNAMdgvpGDPIAPGETFTYEfpvpqpagtyWYHPHTHGSTAEQ--- 120

                           90       100
                   ....*....|....*....|....*
gi 2559057711  888 svgayystvdvikdMYSGLIGPLVI 912
Cdd:COG2132    121 --------------VYRGLAGALIV 131
ascorbase TIGR03388
L-ascorbate oxidase, plant type; Members of this protein family are the copper-containing ...
 97-202 4.66e-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: 47.44  E-value: 4.66e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2559057711   97 GPLISAEEDDVVIVHLKNT-ARRAYSIHAHGLSYNktneGALYPDSSEKVEKAddSVAPGKSFTYVWTLpasHTPGkdet 175
Cdd:TIGR03388   31 GPTIRAQAGDTIVVELTNKlHTEGVVIHWHGIRQI----GTPWADGTAGVTQC--AINPGETFIYNFVV---DRPG---- 97

                           90       100
                   ....*....|....*....|....*..
gi 2559057711  176 nclTRIYHSHVNAPKdiASGLIGPLII 202
Cdd:TIGR03388   98 ---TYFYHGHYGMQR--SAGLYGSLIV 119
PLN02191 PLN02191
L-ascorbate oxidase
 97-202 7.54e-05

L-ascorbate oxidase


Pssm-ID: 177843 [Multi-domain]  Cd Length: 574  Bit Score: 46.55  E-value: 7.54e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2559057711   97 GPLISAEEDDVVIVHLKNT-ARRAYSIHAHGLSynktNEGALYPDSSEKVEKAddSVAPGKSFTYVWTLpasHTPGkdet 175
Cdd:PLN02191    53 GPTIDAVAGDTIVVHLTNKlTTEGLVIHWHGIR----QKGSPWADGAAGVTQC--AINPGETFTYKFTV---EKPG---- 119

                           90       100
                   ....*....|....*....|....*..
gi 2559057711  176 nclTRIYHSHVNAPKdiASGLIGPLII 202
Cdd:PLN02191   120 ---THFYHGHYGMQR--SAGLYGSLIV 141
Cu-oxidase_3 pfam07732
Multicopper oxidase; This entry contains many divergent copper oxidase-like domains that are ...
 423-573 2.79e-04

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: 41.46  E-value: 2.79e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2559057711  423 KVQYVEYADDTFTKRKERTPEEQhlgILGPIIRAEEEDTIKVTFRNKASRPYSIQPHGVQY--SIEMDGTLYhnvleesy 500
Cdd:pfam07732    1 TVTYGTVSPLGGTRQAVIGVNGQ---FPGPTIRVREGDTVVVNVTNNLDEPTSIHWHGLQQrgTPWMDGVPG-------- 69

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2559057711  501 takklrelkkearvvepLPAALVRPDTTYQYEWVVPKDGGptekdpdciTYMYYSAVDPIRdtNSGLVGPLLI 573
Cdd:pfam07732   70 -----------------VTQCPIPPGQSFTYRFQVKQQAG---------TYWYHSHTSGQQ--AAGLAGAIII 114
PLN02191 PLN02191
L-ascorbate oxidase
 315-355 4.54e-04

L-ascorbate oxidase


Pssm-ID: 177843 [Multi-domain]  Cd Length: 574  Bit Score: 44.23  E-value: 4.54e-04
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|.
gi 2559057711  315 DTVSLFPATFVHVEMVADNPGQWLLSCQVNDHMEAGMQAIF 355
Cdd:PLN02191   504 NTAILYPYGWTAIRFVTDNPGVWFFHCHIEPHLHMGMGVVF 544
ascorbase TIGR03388
L-ascorbate oxidase, plant type; Members of this protein family are the copper-containing ...
 315-356 1.07e-03

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: 42.82  E-value: 1.07e-03
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|..
gi 2559057711  315 DTVSLFPATFVHVEMVADNPGQWLLSCQVNDHMEAGMQAIFE 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 1.90e-116

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: 356.73  E-value: 1.90e-116
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2559057711   23 REYFFAIKEIQWDYAPSGKNLIQNKTIKEDEEARVFLERGEQRIGRVYKKAVYQQYTDATYRQEIDKPKWLGYLGPLISA 102
Cdd:cd04222      1 REYYIGIRETQWDYAPSGKNLITNQTFDDDEHASVFLKRGPDRIGRVYKKAVYLQYTDDTYRTEIEKPVWLGFLGPILKA 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2559057711  103 EEDDVVIVHLKNTARRAYSIHAHGLSYNKTNEGALYPDSSEKVEKADDSVAPGKSFTYVWTLPASHTPGKDETNCLTRIY 182
Cdd:cd04222     81 EVGDVIVVHLKNFASRPYSLHPHGVFYNKENEGALYPDNTSGFEKADDAVPPGGSYTYTWTVPEEQAPTKADANCLTRIY 160

                          170       180
                   ....*....|....*....|...
gi 2559057711  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 1.56e-108

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: 335.21  E-value: 1.56e-108
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2559057711  745 KKYYIAAVEMDWDYSPTRTWEEQLHHSLKDSPGNKFLKKEGKFIGSKYKKVLYREYTDETFTKPKERSADMEHLGIMGPM 824
Cdd:cd04225      1 RTYYIAAEEVEWDYSPQRTWEQELHNTHEESPGNAFLNKGDKFIGSKYKKVVYREYTDDTFSVPKERTAEEEHLGILGPL 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2559057711  825 IHGKVGEKVKIVFKNMAKRPYSIHAHGVKTDSPQVALTRPGETKTYTWYLPKNSGPTEQQEECSVGAYYSTVDVIKDMYS 904
Cdd:cd04225     81 IHAEVGEKVKIVFKNMASRPYSIHAHGVKTDSSWVAPTEPGETQTYTWKIPERSGPGVEDSNCISWAYYSTVDQIKDLYS 160

                          170
                   ....*....|.
gi 2559057711  905 GLIGPLVICKK 915
Cdd:cd04225    161 GLIGPLVICRR 171
CuRO_3_ceruloplasmin cd04224
The third cupredoxin domain of Ceruloplasmin; Ceruloplasmin is a multicopper oxidase essential ...
 371-585 7.76e-101

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: 315.95  E-value: 7.76e-101
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2559057711  371 GEVRQYYIAAEEIIWDYGPTGINQYSGMKLVD-DSVSDTFFENRNDRIGGKYKKVQYVEYADDTFTKRKERTPEEQHLGI 449
Cdd:cd04224      1 GKVRHYFIAAEEIMWDYAPSGKNLFTGQNLTApGSDSEVFFQRNETRIGGTYWKVRYVEYTDATFTTRKHRSKEEEHLGI 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2559057711  450 LGPIIRAEEEDTIKVTFRNKASRPYSIQPHGVQYSIEMDGTLYHNvleesytakklrelkkearvVEPLPAALVRPDTTY 529
Cdd:cd04224     81 LGPVIRAEVGDTIKVTFRNKASRPFSIQPHGVFYEKNYEGAMYRD--------------------GDPSPGSHVSPGETF 140

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 2559057711  530 QYEWVVPKDGGPTEKDPDCITYMYYSAVDPIRDTNSGLVGPLLICKPKTL-KSGKQK 585
Cdd:cd04224    141 TYEWTVPEGVGPTNQDPPCLTYLYFSAVDPVRDTNSGLVGPLLVCKKGSLnANGRQK 197
CuRO_2_ceruloplasmin cd11021
The second cupredoxin domain of Ceruloplasmin; Ceruloplasmin is a multicopper oxidase ...
 217-357 8.18e-93

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: 292.07  E-value: 8.18e-93
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2559057711  217 DYLYTLMFTVSDENLSWYLEENIKTYCTAPAKVNKDDEGFQESNKMHSINGYVYGNLPDLSMCMGNKIHWHLFGMGNEVD 296
Cdd:cd11021      1 DREFVLMFSVVDENLSWYLDENIKTYCSEPAKVDKDDEDFQESNKMHSINGYTFGNLPGLSMCAGDRVKWHLFGMGNEVD 80

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2559057711  297 LHSAFFHGQILTDKRHHVDTVSLFPATFVHVEMVADNPGQWLLSCQVNDHMEAGMQAIFEI 357
Cdd:cd11021     81 IHSAFFHGQTLTDRGHRTDTINLFPATFVTAEMVAQNPGKWLLSCQVNDHLKAGMQAFYEV 141
CuRO_4_ceruloplasmin cd11022
The fourth cupredoxin domain of Ceruloplasmin; Ceruloplasmin is a multicopper oxidase ...
 588-731 6.97e-92

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: 289.77  E-value: 6.97e-92
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2559057711  588 DKEFHLLATVFDENLSWYLDDNINRFAKQPKSVKKEDEDFQESNKMHSLNGYMYGNLIGLSMCKGDKVSWHLSGLGSEVD 667
Cdd:cd11022      1 DKEFFLLFTVFDENESWYLDENIQQFTLDPRSVDKEDEDFQESNKMHSINGYMYGNQPGLDMCKGDTVSWHLFGLGTETD 80

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2559057711  668 IHGLYFEGNRFLYKDTRRDTINVFPHISHTVIMEPDSMGQFEVGCKTTDHYHGGMRANYTVEKC 731
Cdd:cd11022     81 VHGIYFSGNTFLLQGTRRDTANLFPHTSVTAIMQPDNEGTFEVNCQTTDHYSAGMRQIYTVSQC 144
CuRO_6_ceruloplasmin cd11012
The sixth cupredoxin domain of Ceruloplasmin; Ceruloplasmin is a multicopper oxidase essential ...
 928-1071 9.47e-91

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: 286.76  E-value: 9.47e-91
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2559057711  928 EEFALLFMVFDENESWYLDDNIKAHVKTPPTTLKEDEEFIESNKMHGINGLVYGNLKGLNMKVGDKVYWYLMGMGNEVDI 1007
Cdd:cd11012      2 LEFALLFLVFDENESWYLDENIKTYSDHPEKVNKEDEEFIESNKMHAINGKVFGNLQGLTMHVGDEVYWYLMGMGNEIDI 81

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2559057711 1008 HTAHFHGHSFDYKIGGTHRADVFDLFPGTFQTITMRPLYSGTWLLHCHVTDHIQAGMETTYTVL 1071
Cdd:cd11012     82 HTAHFHGHSFDYKHRGVYRSDVFDLFPGTFQTVEMIPRTPGTWLLHCHVTDHIHAGMETTYTVL 145
CuRO_1_ceruloplasmin_like cd04199
Cupredoxin domains 1, 3, and 5 of ceruloplasmin and similar proteins; This family includes the ...
 23-205 2.00e-75

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: 246.16  E-value: 2.00e-75
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2559057711   23 REYFFAIKEIQWDYAPSGKNliqnktIKEDEEARVFLERGEQRIGRVYKKAVYQQYTDATYRQEIDKPKWLGYLGPLISA 102
Cdd:cd04199      1 RHYYIAAEEIDWDYAPSGLA------EKDLSYRNQYLDNGPFRIGRSYKKVVYREYTDESFTTPGPQPEHLGILGPTIRA 74

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2559057711  103 EEDDVVIVHLKNTARRAYSIHAHGLSYNKTNEGALYPDSSEKVEKADDSVAPGKSFTYVWTLPASHTPGKDETNCLTRIY 182
Cdd:cd04199     75 EVGDTIKVHFKNKASRPYSIHPHGVSYEKDSEGASYSDQTGPDEKKDDAVAPGETYTYVWIVTEESGPTKGDPACLTWAY 154

                          170       180
                   ....*....|....*....|...
gi 2559057711  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 1.53e-69

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: 229.99  E-value: 1.53e-69
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2559057711  374 RQYYIAAEEIIWDYGPTGINQysgmklVDDSVSDTFFENRNDRIGGKYKKVQYVEYADDTFTKRKertPEEQHLGILGPI 453
Cdd:cd04199      1 RHYYIAAEEIDWDYAPSGLAE------KDLSYRNQYLDNGPFRIGRSYKKVVYREYTDESFTTPG---PQPEHLGILGPT 71

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2559057711  454 IRAEEEDTIKVTFRNKASRPYSIQPHGVQYSIEMDGTLYHNvleesytAKKLRELKKEArvveplpaalVRPDTTYQYEW 533
Cdd:cd04199     72 IRAEVGDTIKVHFKNKASRPYSIHPHGVSYEKDSEGASYSD-------QTGPDEKKDDA----------VAPGETYTYVW 134

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|..
gi 2559057711  534 VVPKDGGPTEKDPDCITYMYYSAVDPIRDTNSGLVGPLLICK 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 2.22e-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: 216.89  E-value: 2.22e-65
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2559057711  222 LMFTVSDENLSWYLEENIKTYCTAPAKVNKDDEGFQESNKMHSINGYVYGNLPDLSMCMGNKIHWHLFGMGNEVDLHSAF 301
Cdd:cd04200      6 LLFAVFDENKSWYLEDNIKRFCDNPEKVDKDDEEFQESNKMHAINGYVFGNLPGLTMCAGDRVRWHLLGMGNEVDVHSIH 85

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 2559057711  302 FHGQILTDKRHHVDTVSLFPATFVHVEMVADNPGQWLLSCQVNDHMEAGMQAIFEI 357
Cdd:cd04200     86 FHGQTFLYKGYRIDTLTLFPATFETVEMVPSNPGTWLLHCHNSDHRHAGMQAYFLV 141
CuRO_3_ceruloplasmin cd04224
The third cupredoxin domain of Ceruloplasmin; Ceruloplasmin is a multicopper oxidase essential ...
 23-212 2.42e-65

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: 218.88  E-value: 2.42e-65
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2559057711   23 REYFFAIKEIQWDYAPSGKNLIQNKTI-KEDEEARVFLERGEQRIGRVYKKAVYQQYTDATY--RQEIDKP-KWLGYLGP 98
Cdd:cd04224      4 RHYFIAAEEIMWDYAPSGKNLFTGQNLtAPGSDSEVFFQRNETRIGGTYWKVRYVEYTDATFttRKHRSKEeEHLGILGP 83

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2559057711   99 LISAEEDDVVIVHLKNTARRAYSIHAHGLSYNKTNEGALYPDSSEKvekADDSVAPGKSFTYVWTLPASHTPGKDETNCL 178
Cdd:cd04224     84 VIRAEVGDTIKVTFRNKASRPFSIQPHGVFYEKNYEGAMYRDGDPS---PGSHVSPGETFTYEWTVPEGVGPTNQDPPCL 160

                          170       180       190
                   ....*....|....*....|....*....|....
gi 2559057711  179 TRIYHSHVNAPKDIASGLIGPLIICKKGSLDVHG 212
Cdd:cd04224    161 TYLYFSAVDPVRDTNSGLVGPLLVCKKGSLNANG 194
CuRO_1_ceruloplasmin_like cd04199
Cupredoxin domains 1, 3, and 5 of ceruloplasmin and similar proteins; This family includes the ...
 745-915 9.70e-64

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: 213.81  E-value: 9.70e-64
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2559057711  745 KKYYIAAVEMDWDYSPTRTWEEQLHHSlkdspgNKFLKKEGKFIGSKYKKVLYREYTDETFTKPKERsadMEHLGIMGPM 824
Cdd:cd04199      1 RHYYIAAEEIDWDYAPSGLAEKDLSYR------NQYLDNGPFRIGRSYKKVVYREYTDESFTTPGPQ---PEHLGILGPT 71

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2559057711  825 IHGKVGEKVKIVFKNMAKRPYSIHAHGVKTDSPQ---------------VALTRPGETKTYTWYLPKNSGPTEQQEECSV 889
Cdd:cd04199     72 IRAEVGDTIKVHFKNKASRPYSIHPHGVSYEKDSegasysdqtgpdekkDDAVAPGETYTYVWIVTEESGPTKGDPACLT 151

                          170       180
                   ....*....|....*....|....*.
gi 2559057711  890 GAYYSTVDVIKDMYSGLIGPLVICKK 915
Cdd:cd04199    152 WAYYSHVDLEKDINSGLIGPLLICKK 177
CuRO_2_ceruloplasmin_like cd04200
Cupredoxin domains 2, 4, and 6 of ceruloplasmin and similar proteins; This family includes the ...
 929-1070 4.73e-62

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: 207.26  E-value: 4.73e-62
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2559057711  929 EFALLFMVFDENESWYLDDNIKAHVKTPPTTLKEDEEFIESNKMHGINGLVYGNLKGLNMKVGDKVYWYLMGMGNEVDIH 1008
Cdd:cd04200      3 EFVLLFAVFDENKSWYLEDNIKRFCDNPEKVDKDDEEFQESNKMHAINGYVFGNLPGLTMCAGDRVRWHLLGMGNEVDVH 82

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2559057711 1009 TAHFHGHSFDYKiggTHRADVFDLFPGTFQTITMRPLYSGTWLLHCHVTDHIQAGMETTYTV 1070
Cdd:cd04200     83 SIHFHGQTFLYK---GYRIDTLTLFPATFETVEMVPSNPGTWLLHCHNSDHRHAGMQAYFLV 141
CuRO_5_ceruloplasmin cd04225
The fifth cupredoxin domain of Ceruloplasmin; Ceruloplasmin is a multicopper oxidase essential ...
 374-576 5.52e-59

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: 200.00  E-value: 5.52e-59
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2559057711  374 RQYYIAAEEIIWDYGPTGINQYSGMKLVDDSVSDTFFENRNDRIGGKYKKVQYVEYADDTFTKRKERTPEEQHLGILGPI 453
Cdd:cd04225      1 RTYYIAAEEVEWDYSPQRTWEQELHNTHEESPGNAFLNKGDKFIGSKYKKVVYREYTDDTFSVPKERTAEEEHLGILGPL 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2559057711  454 IRAEEEDTIKVTFRNKASRPYSIQPHGVQysieMDGTlyhnvleesytakklrelkkearvveplPAALVRPDTTYQYEW 533
Cdd:cd04225     81 IHAEVGEKVKIVFKNMASRPYSIHAHGVK----TDSS----------------------------WVAPTEPGETQTYTW 128

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|...
gi 2559057711  534 VVPKDGGPTEKDPDCITYMYYSAVDPIRDTNSGLVGPLLICKP 576
Cdd:cd04225    129 KIPERSGPGVEDSNCISWAYYSTVDQIKDLYSGLIGPLVICRR 171
CuRO_3_ceruloplasmin cd04224
The third cupredoxin domain of Ceruloplasmin; Ceruloplasmin is a multicopper oxidase essential ...
 743-915 3.39e-58

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: 198.85  E-value: 3.39e-58
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2559057711  743 HQKKYYIAAVEMDWDYSPTRT-WEEQLHHSLKDSPGNKFLKKEGKFIGSKYKKVLYREYTDETFTKPKERSADMEHLGIM 821
Cdd:cd04224      2 KVRHYFIAAEEIMWDYAPSGKnLFTGQNLTAPGSDSEVFFQRNETRIGGTYWKVRYVEYTDATFTTRKHRSKEEEHLGIL 81

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2559057711  822 GPMIHGKVGEKVKIVFKNMAKRPYSIHAHGV------------KTDSPQVALTRPGETKTYTWYLPKNSGPTEQQEECSV 889
Cdd:cd04224     82 GPVIRAEVGDTIKVTFRNKASRPFSIQPHGVfyeknyegamyrDGDPSPGSHVSPGETFTYEWTVPEGVGPTNQDPPCLT 161

                          170       180
                   ....*....|....*....|....*.
gi 2559057711  890 GAYYSTVDVIKDMYSGLIGPLVICKK 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 3.00e-57

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: 193.78  E-value: 3.00e-57
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2559057711  588 DKEFHLLATVFDENLSWYLDDNINRFAKQPKSVKKEDEDFQESNKMHSLNGYMYGNLIGLSMCKGDKVSWHLSGLGSEVD 667
Cdd:cd04200      1 DKEFVLLFAVFDENKSWYLEDNIKRFCDNPEKVDKDDEEFQESNKMHAINGYVFGNLPGLTMCAGDRVRWHLLGMGNEVD 80

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2559057711  668 IHGLYFEGNRFLYKDTRRDTINVFPHISHTVIMEPDSMGQFEVGCKTTDHYHGGMRANYTV 728
Cdd:cd04200     81 VHSIHFHGQTFLYKGYRIDTLTLFPATFETVEMVPSNPGTWLLHCHNSDHRHAGMQAYFLV 141
CuRO_4_ceruloplasmin cd11022
The fourth cupredoxin domain of Ceruloplasmin; Ceruloplasmin is a multicopper oxidase ...
 217-360 4.05e-57

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: 193.47  E-value: 4.05e-57
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2559057711  217 DYLYTLMFTVSDENLSWYLEENIKTYCTAPAKVNKDDEGFQESNKMHSINGYVYGNLPDLSMCMGNKIHWHLFGMGNEVD 296
Cdd:cd11022      1 DKEFFLLFTVFDENESWYLDENIQQFTLDPRSVDKEDEDFQESNKMHSINGYMYGNQPGLDMCKGDTVSWHLFGLGTETD 80

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2559057711  297 LHSAFFHGQILTDKRHHVDTVSLFPATFVHVEMVADNPGQWLLSCQVNDHMEAGMQAIFEIKKC 360
Cdd:cd11022     81 VHGIYFSGNTFLLQGTRRDTANLFPHTSVTAIMQPDNEGTFEVNCQTTDHYSAGMRQIYTVSQC 144
CuRO_2_ceruloplasmin cd11021
The second cupredoxin domain of Ceruloplasmin; Ceruloplasmin is a multicopper oxidase ...
 588-728 2.87e-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: 191.14  E-value: 2.87e-56
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2559057711  588 DKEFHLLATVFDENLSWYLDDNINRFAKQPKSVKKEDEDFQESNKMHSLNGYMYGNLIGLSMCKGDKVSWHLSGLGSEVD 667
Cdd:cd11021      1 DREFVLMFSVVDENLSWYLDENIKTYCSEPAKVDKDDEDFQESNKMHSINGYTFGNLPGLSMCAGDRVKWHLFGMGNEVD 80

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2559057711  668 IHGLYFEGNRFLYKDTRRDTINVFPHISHTVIMEPDSMGQFEVGCKTTDHYHGGMRANYTV 728
Cdd:cd11021     81 IHSAFFHGQTLTDRGHRTDTINLFPATFVTAEMVAQNPGKWLLSCQVNDHLKAGMQAFYEV 141
CuRO_3_FV_like cd14450
The third cupredoxin domain of coagulation factor V and similar proteins; Factor V is an ...
 375-575 1.04e-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: 191.24  E-value: 1.04e-55
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2559057711  375 QYYIAAEEIIWDYGPTGINQysgmklVDDSVSDTFFENRNDRIGGKYKKVQYVEYADDTFTKRKErTPEEQHLGILGPII 454
Cdd:cd14450      4 EYFIAAEEVIWDYAPSIPEN------MDKRYRSQYLDNFSNNIGKKYKKAVFTQYEDGSFTKRLE-NPRPKEEGILGPVI 76

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2559057711  455 RAEEEDTIKVTFRNKASRPYSIQPHGVQYSIEMDGTLYHNVLEESYTAKKLrelkkearvveplpaalVRPDTTYQYEWV 534
Cdd:cd14450     77 RAQVRDTIKIVFKNKASRPYSIYPHGVTVSKAAEGASYPPDPRGNETQNKA-----------------VQPGETYTYKWN 139

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|.
gi 2559057711  535 VPKDGGPTEKDPDCITYMYYSAVDPIRDTNSGLVGPLLICK 575
Cdd:cd14450    140 ILETDEPTARDPRCLTRMYHSAVDITRDIASGLIGPLLICK 180
CuRO_2_ceruloplasmin cd11021
The second cupredoxin domain of Ceruloplasmin; Ceruloplasmin is a multicopper oxidase ...
 929-1070 5.02e-54

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: 184.60  E-value: 5.02e-54
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2559057711  929 EFALLFMVFDENESWYLDDNIKAHVKTPPTTLKEDEEFIESNKMHGINGLVYGNLKGLNMKVGDKVYWYLMGMGNEVDIH 1008
Cdd:cd11021      3 EFVLMFSVVDENLSWYLDENIKTYCSEPAKVDKDDEDFQESNKMHSINGYTFGNLPGLSMCAGDRVKWHLFGMGNEVDIH 82

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2559057711 1009 TAHFHGHSFDYKiggTHRADVFDLFPGTFQTITMRPLYSGTWLLHCHVTDHIQAGMETTYTV 1070
Cdd:cd11021     83 SAFFHGQTLTDR---GHRTDTINLFPATFVTAEMVAQNPGKWLLSCQVNDHLKAGMQAFYEV 141
CuRO_1_ceruloplasmin cd04222
The first cupredoxin domain of Ceruloplasmin; Ceruloplasmin is a multicopper oxidase essential ...
 374-575 5.80e-54

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: 186.09  E-value: 5.80e-54
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2559057711  374 RQYYIAAEEIIWDYGPTGINQYSGMKLVDDSVSDTFFENRNDRIGGKYKKVQYVEYADDTFTKRKERTPeeqHLGILGPI 453
Cdd:cd04222      1 REYYIGIRETQWDYAPSGKNLITNQTFDDDEHASVFLKRGPDRIGRVYKKAVYLQYTDDTYRTEIEKPV---WLGFLGPI 77

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2559057711  454 IRAEEEDTIKVTFRNKASRPYSIQPHGVQYSIEMDGTLYHNvleesytAKKLRELKKEArvveplpaalVRPDTTYQYEW 533
Cdd:cd04222     78 LKAEVGDVIVVHLKNFASRPYSLHPHGVFYNKENEGALYPD-------NTSGFEKADDA----------VPPGGSYTYTW 140

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|..
gi 2559057711  534 VVPKDGGPTEKDPDCITYMYYSAVDPIRDTNSGLVGPLLICK 575
Cdd:cd04222    141 TVPEEQAPTKADANCLTRIYHSHIDAPKDIASGLIGPLIICK 182
CuRO_4_ceruloplasmin cd11022
The fourth cupredoxin domain of Ceruloplasmin; Ceruloplasmin is a multicopper oxidase ...
 929-1070 2.08e-53

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: 183.07  E-value: 2.08e-53
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2559057711  929 EFALLFMVFDENESWYLDDNIKAHVKTPPTTLKEDEEFIESNKMHGINGLVYGNLKGLNMKVGDKVYWYLMGMGNEVDIH 1008
Cdd:cd11022      3 EFFLLFTVFDENESWYLDENIQQFTLDPRSVDKEDEDFQESNKMHSINGYMYGNQPGLDMCKGDTVSWHLFGLGTETDVH 82

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2559057711 1009 TAHFHGHSFDYKigGTHRaDVFDLFPGTFQTITMRPLYSGTWLLHCHVTDHIQAGMETTYTV 1070
Cdd:cd11022     83 GIYFSGNTFLLQ--GTRR-DTANLFPHTSVTAIMQPDNEGTFEVNCQTTDHYSAGMRQIYTV 141
CuRO_5_FV_like cd14451
The fifth cupredoxin domain of coagulation factor V and similar proteins; Factor V is an ...
 22-206 3.57e-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: 183.50  E-value: 3.57e-53
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2559057711   22 TREYFFAIKEIQWDYAPSGKNLIQNKTIKEDEearvflergeqrigrVYKKAVYQQYTDATY-----RQEIDKPkwLGYL 96
Cdd:cd14451      1 KRRYYIAAEEEEWDYAGYGKSRLDKTQNERDT---------------VFKKVVFRRYLDSTFstpdiQGEYEEH--LGIL 63

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2559057711   97 GPLISAEEDDVVIVHLKNTARRAYSIHAHGLSYNKTNEGALYPDSSEKVEKADDSVAPGKSFTYVWTLPASHTPGKDETN 176
Cdd:cd14451     64 GPVIRAEVDDVIQVFFKNLASRPYSLHAHGLSYEKSSEGLSYDDESPDWFKKDDAVQPNGTYTYVWYANPRSGPENNGSD 143

                          170       180       190
                   ....*....|....*....|....*....|
gi 2559057711  177 CLTRIYHSHVNAPKDIASGLIGPLIICKKG 206
Cdd:cd14451    144 CRTWAYYSAVNPEKDIHSGLIGPLLICRKG 173
CuRO_5_FV_like cd14451
The fifth cupredoxin domain of coagulation factor V and similar proteins; Factor V is an ...
 374-575 2.69e-51

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: 178.11  E-value: 2.69e-51
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2559057711  374 RQYYIAAEEIIWDYGPTGINQysgmkLVDDSVSDTffenrndrigGKYKKVQYVEYADDTFTKRKERTPEEQHLGILGPI 453
Cdd:cd14451      2 RRYYIAAEEEEWDYAGYGKSR-----LDKTQNERD----------TVFKKVVFRRYLDSTFSTPDIQGEYEEHLGILGPV 66

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2559057711  454 IRAEEEDTIKVTFRNKASRPYSIQPHGVQYSIEMDGTLYHNvlEESYTAKklrelKKEArvveplpaalVRPDTTYQYEW 533
Cdd:cd14451     67 IRAEVDDVIQVFFKNLASRPYSLHAHGLSYEKSSEGLSYDD--ESPDWFK-----KDDA----------VQPNGTYTYVW 129

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|..
gi 2559057711  534 VVPKDGGPTEKDPDCITYMYYSAVDPIRDTNSGLVGPLLICK 575
Cdd:cd14451    130 YANPRSGPENNGSDCRTWAYYSAVNPEKDIHSGLIGPLLICR 171
CuRO_3_FV_like cd14450
The third cupredoxin domain of coagulation factor V and similar proteins; Factor V is an ...
 24-204 1.90e-50

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: 176.22  E-value: 1.90e-50
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2559057711   24 EYFFAIKEIQWDYAPsgknliqnkTIKEDEEARV---FLERGEQRIGRVYKKAVYQQYTDATY--RQEIDKPKWLGYLGP 98
Cdd:cd14450      4 EYFIAAEEVIWDYAP---------SIPENMDKRYrsqYLDNFSNNIGKKYKKAVFTQYEDGSFtkRLENPRPKEEGILGP 74

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2559057711   99 LISAEEDDVVIVHLKNTARRAYSIHAHGLSYNKTNEGALYPDSSEKVEKADDSVAPGKSFTYVWTLPASHTPGKDETNCL 178
Cdd:cd14450     75 VIRAQVRDTIKIVFKNKASRPYSIYPHGVTVSKAAEGASYPPDPRGNETQNKAVQPGETYTYKWNILETDEPTARDPRCL 154

                          170       180
                   ....*....|....*....|....*.
gi 2559057711  179 TRIYHSHVNAPKDIASGLIGPLIICK 204
Cdd:cd14450    155 TRMYHSAVDITRDIASGLIGPLLICK 180
CuRO_6_ceruloplasmin cd11012
The sixth cupredoxin domain of Ceruloplasmin; Ceruloplasmin is a multicopper oxidase essential ...
 220-357 2.07e-50

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: 174.67  E-value: 2.07e-50
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2559057711  220 YTLMFTVSDENLSWYLEENIKTYCTAPAKVNKDDEGFQESNKMHSINGYVYGNLPDLSMCMGNKIHWHLFGMGNEVDLHS 299
Cdd:cd11012      4 FALLFLVFDENESWYLDENIKTYSDHPEKVNKEDEEFIESNKMHAINGKVFGNLQGLTMHVGDEVYWYLMGMGNEIDIHT 83

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2559057711  300 AFFHGQILTDKR---HHVDTVSLFPATFVHVEMVADNPGQWLLSCQVNDHMEAGMQAIFEI 357
Cdd:cd11012     84 AHFHGHSFDYKHrgvYRSDVFDLFPGTFQTVEMIPRTPGTWLLHCHVTDHIHAGMETTYTV 144
CuRO_1_FV_like cd04226
The first cupredoxin domain of coagulation factor VIII and similar proteins; Factor V is an ...
 23-206 2.89e-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: 171.97  E-value: 2.89e-49
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2559057711   23 REYFFAIKEIQWDYAPsgknliqnktikEDEEARVflergeQRIGRVYKKAVYQQYtDATYRQEIDKPKWLGYLGPLISA 102
Cdd:cd04226      1 REYYIAAQNIDWDYTP------------QSEELRL------KRSEQSFKKIVYREY-EEGFKKEKPADLSSGLLGPTLRA 61

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2559057711  103 EEDDVVIVHLKNTARRAYSIHAHGLSYNKTNEGALYPDSSEKVEKADDSVAPGKSFTYVWTLPASHTPGKDETNCLTRIY 182
Cdd:cd04226     62 EVGDTLIVHFKNMADKPLSIHPQGIAYGKKSEGSLYSDNTSPVEKLDDAVQPGQEYTYVWDITEEVGPTEADPPCLTYIY 141

                          170       180
                   ....*....|....*....|....
gi 2559057711  183 HSHVNAPKDIASGLIGPLIICKKG 206
Cdd:cd04226    142 YSHVNMVRDFNSGLIGALLICKKG 165
CuRO_1_Ceruloplasmin_like_1 cd04229
cupredoxin domain of ceruloplasmin homologs; Uncharacterized subfamily of ceruloplasmin ...
 374-573 3.77e-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: 172.22  E-value: 3.77e-49
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2559057711  374 RQYYIAAEEIIWDYGPTGINQysgMKLVDDSVSDTFFENRND-RIGGKYKKVQYVEYADDTFTKRKertPEEQHLGILGP 452
Cdd:cd04229      1 RTYYIAAEEVDWDYAPSGKNK---CCLGDDLEVSTLDSQPGPyTIGSTYTKARYREYTDNSFSTPK---PTPAYLGILGP 74

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2559057711  453 IIRAEEEDTIKVTFRNKASR-PYSIQPHGVQYSIEMDGTLYHNvleesytakklrelkkearvveplpAALVRPDTTYQY 531
Cdd:cd04229     75 VIRAEVGDTIKVVFKNNLDEfPVNMHPHGGLYSKDNEGTTDGA-------------------------GDVVAPGETYTY 129

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|..
gi 2559057711  532 EWVVPKDGGPTEKDPDCITYMYYSAVDPIRDTNSGLVGPLLI 573
Cdd:cd04229    130 RWIVPEDAGPGPGDPSSRLWLYHSHVDVFAHTNAGLVGPIIV 171
CuRO_3_FVIII_like cd04227
The third cupredoxin domain of coagulation factor VIII and similar proteins; Factor VIII ...
 376-575 6.05e-49

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: 171.65  E-value: 6.05e-49
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2559057711  376 YYIAAEEIIWDYGPtginqysgMKLV--DDSVSDTFFENRNDRIGGKYKKVQYVEYADDTFTKRKERTPEEqhlGILGPI 453
Cdd:cd04227      5 HYIAAEELDWDYAP--------LLSStdDRELQSRYLPTGPQRIGYKYKKVAFVEYTDKTFKRREAKQTEK---GILGPL 73

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2559057711  454 IRAEEEDTIKVTFRNKASRPYSIQPHGVQySIEmdgtlyhnvleeSYTAKKLRELKKEARVVEplpaalVRPDTTYQYEW 533
Cdd:cd04227     74 LKGEVGDQIHIMFKNTASRPYNIYPHGLT-SVR------------PMYRSRNPAGEKDLKTMP------IGPGETFGYMW 134

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|..
gi 2559057711  534 VVPKDGGPTEKDPDCITYMYYSAVDPIRDTNSGLVGPLLICK 575
Cdd:cd04227    135 ELTAEDGPTEEDPRCLTRLYQSTVDPERDLASGLIGPLLICK 176
CuRO_1_FVIII_like cd14452
The first cupredoxin domain of coagulation factor VIII and similar proteins; Factor VIII ...
 23-206 2.92e-48

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: 169.39  E-value: 2.92e-48
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2559057711   23 REYFFAIKEIQWDYAPSgknliqnktikEDEEARVFLERGEQRIGRVYKKAVYQQYTDATYRQEIDKPKWLGYLGPLISA 102
Cdd:cd14452      1 RRYYIAAVEIGWDYIHS-----------DLGDPASEQRKKPKDIPQKYIKAVFVEYLDATFTVPKPRPAWMGLLGPTIVA 69

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2559057711  103 EEDDVVIVHLKNTARRAYSIHAHGLSYNKTNEGALYPDSSEKVEKADDSVAPGKSFTYVWTLPASHTPGKDETNCLTRIY 182
Cdd:cd14452     70 EVGDTVVITFKNLASQPYSLHAVGVSYWKASEGAGYDDSTSQHEKEDDAVYPGGYHTYVWDISPKDGPTGSDPECLTYSY 149

                          170       180
                   ....*....|....*....|....
gi 2559057711  183 HSHVNAPKDIASGLIGPLIICKKG 206
Cdd:cd14452    150 SSQVDPVKDVNSGLIGALLVCRMG 173
CuRO_3_FV_like cd14450
The third cupredoxin domain of coagulation factor V and similar proteins; Factor V is an ...
 747-914 1.12e-47

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: 168.13  E-value: 1.12e-47
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2559057711  747 YYIAAVEMDWDYSPTrtweeqLHHSLKDSPGNKFLKKEGKFIGSKYKKVLYREYTDETFTKPKErSADMEHLGIMGPMIH 826
Cdd:cd14450      5 YFIAAEEVIWDYAPS------IPENMDKRYRSQYLDNFSNNIGKKYKKAVFTQYEDGSFTKRLE-NPRPKEEGILGPVIR 77

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2559057711  827 GKVGEKVKIVFKNMAKRPYSIHAHGVK-------TDSP--------QVALTRPGETKTYTWYLPKNSGPTEQQEECSVGA 891
Cdd:cd14450     78 AQVRDTIKIVFKNKASRPYSIYPHGVTvskaaegASYPpdprgnetQNKAVQPGETYTYKWNILETDEPTARDPRCLTRM 157

                          170       180
                   ....*....|....*....|...
gi 2559057711  892 YYSTVDVIKDMYSGLIGPLVICK 914
Cdd:cd14450    158 YHSAVDITRDIASGLIGPLLICK 180
CuRO_1_Ceruloplasmin_like_1 cd04229
cupredoxin domain of ceruloplasmin homologs; Uncharacterized subfamily of ceruloplasmin ...
 23-206 8.31e-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: 165.28  E-value: 8.31e-47
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2559057711   23 REYFFAIKEIQWDYAPSGKNLIQNKTIKEDEEarVFLERGEQRIGRVYKKAVYQQYTDATYRQEIDKPKWLGYLGPLISA 102
Cdd:cd04229      1 RTYYIAAEEVDWDYAPSGKNKCCLGDDLEVST--LDSQPGPYTIGSTYTKARYREYTDNSFSTPKPTPAYLGILGPVIRA 78

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2559057711  103 EEDDVVIVHLKN-TARRAYSIHAHGLSYNKTNEGALypdssekvEKADDSVAPGKSFTYVWTLPASHTPGKDETNCLTRI 181
Cdd:cd04229     79 EVGDTIKVVFKNnLDEFPVNMHPHGGLYSKDNEGTT--------DGAGDVVAPGETYTYRWIVPEDAGPGPGDPSSRLWL 150

                          170       180
                   ....*....|....*....|....*
gi 2559057711  182 YHSHVNAPKDIASGLIGPLIICKKG 206
Cdd:cd04229    151 YHSHVDVFAHTNAGLVGPIIVTSKG 175
CuRO_5_FVIII_like cd04228
The fifth cupredoxin domain of coagulation factor VIII and similar proteins; Factor VIII ...
 745-915 1.41e-46

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: 164.67  E-value: 1.41e-46
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2559057711  745 KKYYIAAVEMDWDYSPTRTweeqlHHSLKDSPGNKFLKKEGKfigsKYKKVLYREYTDETFTKPKERSADMEHLGIMGPM 824
Cdd:cd04228      2 RHYFIAAVEVLWDYGMQRP-----QHFLRARDPNRGRRKSVP----QYKKVVFREYLDGSFTQPVYRGELDEHLGILGPY 72

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2559057711  825 IHGKVGEKVKIVFKNMAKRPYSIHAHGVKTDSPQVALTR-----PGETKTYTWYLPKNSGPTEQQEECSVGAYYSTVDVI 899
Cdd:cd04228     73 IRAEVEDNIMVTFKNLASRPYSFHSSLISYEEDQRAEPRgnfvqPGEVQTYSWKVLHQMAPTKQEFDCKAWAYFSNVDLE 152

                          170
                   ....*....|....*.
gi 2559057711  900 KDMYSGLIGPLVICKK 915
Cdd:cd04228    153 KDLHSGLIGPLIICKT 168
CuRO_5_FV_like cd14451
The fifth cupredoxin domain of coagulation factor V and similar proteins; Factor V is an ...
 744-915 1.16e-45

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: 161.93  E-value: 1.16e-45
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2559057711  744 QKKYYIAAVEMDWDYSPtrtweeqlhhslkdsPGNKFLKKEGKFIGSKYKKVLYREYTDETFTKPKERSADMEHLGIMGP 823
Cdd:cd14451      1 KRRYYIAAEEEEWDYAG---------------YGKSRLDKTQNERDTVFKKVVFRRYLDSTFSTPDIQGEYEEHLGILGP 65

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2559057711  824 MIHGKVGEKVKIVFKNMAKRPYSIHAHGVK-----------TDSP----QVALTRPGETKTYTWYLPKNSGPTEQQEECS 888
Cdd:cd14451     66 VIRAEVDDVIQVFFKNLASRPYSLHAHGLSyeksseglsydDESPdwfkKDDAVQPNGTYTYVWYANPRSGPENNGSDCR 145

                          170       180
                   ....*....|....*....|....*..
gi 2559057711  889 VGAYYSTVDVIKDMYSGLIGPLVICKK 915
Cdd:cd14451    146 TWAYYSAVNPEKDIHSGLIGPLLICRK 172
CuRO_3_FVIII_like cd04227
The third cupredoxin domain of coagulation factor VIII and similar proteins; Factor VIII ...
 747-915 1.30e-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: 162.02  E-value: 1.30e-45
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2559057711  747 YYIAAVEMDWDYSPtrtweeQLHHSLKDSPGNKFLKKEGKFIGSKYKKVLYREYTDETFTKpkeRSADMEHLGIMGPMIH 826
Cdd:cd04227      5 HYIAAEELDWDYAP------LLSSTDDRELQSRYLPTGPQRIGYKYKKVAFVEYTDKTFKR---REAKQTEKGILGPLLK 75

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2559057711  827 GKVGEKVKIVFKNMAKRPYSIHAHGVKTDSPQVALTR-------------PGETKTYTWYLPKNSGPTEQQEECSVGAYY 893
Cdd:cd04227     76 GEVGDQIHIMFKNTASRPYNIYPHGLTSVRPMYRSRNpagekdlktmpigPGETFGYMWELTAEDGPTEEDPRCLTRLYQ 155

                          170       180
                   ....*....|....*....|..
gi 2559057711  894 STVDVIKDMYSGLIGPLVICKK 915
Cdd:cd04227    156 STVDPERDLASGLIGPLLICKK 177
CuRO_6_ceruloplasmin cd11012
The sixth cupredoxin domain of Ceruloplasmin; Ceruloplasmin is a multicopper oxidase essential ...
 589-728 1.47e-44

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: 157.72  E-value: 1.47e-44
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2559057711  589 KEFHLLATVFDENLSWYLDDNINRFAKQPKSVKKEDEDFQESNKMHSLNGYMYGNLIGLSMCKGDKVSWHLSGLGSEVDI 668
Cdd:cd11012      2 LEFALLFLVFDENESWYLDENIKTYSDHPEKVNKEDEEFIESNKMHAINGKVFGNLQGLTMHVGDEVYWYLMGMGNEIDI 81

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2559057711  669 HGLYFEGNRFLYKDT---RRDTINVFPHISHTVIMEPDSMGQFEVGCKTTDHYHGGMRANYTV 728
Cdd:cd11012     82 HTAHFHGHSFDYKHRgvyRSDVFDLFPGTFQTVEMIPRTPGTWLLHCHVTDHIHAGMETTYTV 144
CuRO_1_FV_like cd04226
The first cupredoxin domain of coagulation factor VIII and similar proteins; Factor V is an ...
 374-575 3.60e-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: 154.63  E-value: 3.60e-43
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2559057711  374 RQYYIAAEEIIWDYGPtginQYSgmklvddsvsdtffENRNDRIGGKYKKVQYVEYADDtFTKRKertPEEQHLGILGPI 453
Cdd:cd04226      1 REYYIAAQNIDWDYTP----QSE--------------ELRLKRSEQSFKKIVYREYEEG-FKKEK---PADLSSGLLGPT 58

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2559057711  454 IRAEEEDTIKVTFRNKASRPYSIQPHGVQYSIEMDGTLYHNvleesytakklrelkkEARVVEPLPAAlVRPDTTYQYEW 533
Cdd:cd04226     59 LRAEVGDTLIVHFKNMADKPLSIHPQGIAYGKKSEGSLYSD----------------NTSPVEKLDDA-VQPGQEYTYVW 121

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|..
gi 2559057711  534 VVPKDGGPTEKDPDCITYMYYSAVDPIRDTNSGLVGPLLICK 575
Cdd:cd04226    122 DITEEVGPTEADPPCLTYIYYSHVNMVRDFNSGLIGALLICK 163
CuRO_1_ceruloplasmin cd04222
The first cupredoxin domain of Ceruloplasmin; Ceruloplasmin is a multicopper oxidase essential ...
 745-915 1.36e-42

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: 153.73  E-value: 1.36e-42
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2559057711  745 KKYYIAAVEMDWDYSPTRTWEEQLHHSLKDSPGNKFLKKEGKFIGSKYKKVLYREYTDETFTKPKERSAdmeHLGIMGPM 824
Cdd:cd04222      1 REYYIGIRETQWDYAPSGKNLITNQTFDDDEHASVFLKRGPDRIGRVYKKAVYLQYTDDTYRTEIEKPV---WLGFLGPI 77

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2559057711  825 IHGKVGEKVKIVFKNMAKRPYSIHAHGVK-------------TDSPQVA--LTRPGETKTYTWYLPKNSGPTEQQEECSV 889
Cdd:cd04222     78 LKAEVGDVIVVHLKNFASRPYSLHPHGVFynkenegalypdnTSGFEKAddAVPPGGSYTYTWTVPEEQAPTKADANCLT 157

                          170       180
                   ....*....|....*....|....*.
gi 2559057711  890 GAYYSTVDVIKDMYSGLIGPLVICKK 915
Cdd:cd04222    158 RIYHSHIDAPKDIASGLIGPLIICKK 183
CuRO_5_ceruloplasmin cd04225
The fifth cupredoxin domain of Ceruloplasmin; Ceruloplasmin is a multicopper oxidase essential ...
 23-205 6.27e-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: 151.08  E-value: 6.27e-42
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2559057711   23 REYFFAIKEIQWDYAPSGKNLIQNKTIKEDEEARVFLERGEQRIGRVYKKAVYQQYTDATYRqeIDKP-----KWLGYLG 97
Cdd:cd04225      1 RTYYIAAEEVEWDYSPQRTWEQELHNTHEESPGNAFLNKGDKFIGSKYKKVVYREYTDDTFS--VPKErtaeeEHLGILG 78

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2559057711   98 PLISAEEDDVVIVHLKNTARRAYSIHAHGLsynKTNEGALYPdssekvekaddsVAPGKSFTYVWTLPASHTPGKDETNC 177
Cdd:cd04225     79 PLIHAEVGEKVKIVFKNMASRPYSIHAHGV---KTDSSWVAP------------TEPGETQTYTWKIPERSGPGVEDSNC 143

                          170       180
                   ....*....|....*....|....*...
gi 2559057711  178 LTRIYHSHVNAPKDIASGLIGPLIICKK 205
Cdd:cd04225    144 ISWAYYSTVDQIKDLYSGLIGPLVICRR 171
CuRO_5_FVIII_like cd04228
The fifth cupredoxin domain of coagulation factor VIII and similar proteins; Factor VIII ...
 373-576 6.31e-42

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: 151.19  E-value: 6.31e-42
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2559057711  373 VRQYYIAAEEIIWDYGptginqysgmklvdDSVSDTFFENRNDRIGGK-----YKKVQYVEYADDTFTKRKERTPEEQHL 447
Cdd:cd04228      1 IRHYFIAAVEVLWDYG--------------MQRPQHFLRARDPNRGRRksvpqYKKVVFREYLDGSFTQPVYRGELDEHL 66

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2559057711  448 GILGPIIRAEEEDTIKVTFRNKASRPYSIQPHGVQYsiemdgtlyhnvlEESYTAKKLRElkkearvveplpaaLVRPDT 527
Cdd:cd04228     67 GILGPYIRAEVEDNIMVTFKNLASRPYSFHSSLISY-------------EEDQRAEPRGN--------------FVQPGE 119

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*....
gi 2559057711  528 TYQYEWVVPKDGGPTEKDPDCITYMYYSAVDPIRDTNSGLVGPLLICKP 576
Cdd:cd04228    120 VQTYSWKVLHQMAPTKQEFDCKAWAYFSNVDLEKDLHSGLIGPLIICKT 168
CuRO_3_FVIII_like cd04227
The third cupredoxin domain of coagulation factor VIII and similar proteins; Factor VIII ...
 22-205 6.59e-42

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: 151.62  E-value: 6.59e-42
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2559057711   22 TREYFFAIKEIQWDYAPsgknliqNKTIKEDEE-ARVFLERGEQRIGRVYKKAVYQQYTDATYRQEIDKPKWLGYLGPLI 100
Cdd:cd04227      2 TWEHYIAAEELDWDYAP-------LLSSTDDRElQSRYLPTGPQRIGYKYKKVAFVEYTDKTFKRREAKQTEKGILGPLL 74

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2559057711  101 SAEEDDVVIVHLKNTARRAYSIHAHGLSYNKTNEgALYPDSSEKVEKaDDSVAPGKSFTYVWTLPASHTPGKDETNCLTR 180
Cdd:cd04227     75 KGEVGDQIHIMFKNTASRPYNIYPHGLTSVRPMY-RSRNPAGEKDLK-TMPIGPGETFGYMWELTAEDGPTEEDPRCLTR 152

                          170       180
                   ....*....|....*....|....*
gi 2559057711  181 IYHSHVNAPKDIASGLIGPLIICKK 205
Cdd:cd04227    153 LYQSTVDPERDLASGLIGPLLICKK 177
CuRO_1_FVIII_like cd14452
The first cupredoxin domain of coagulation factor VIII and similar proteins; Factor VIII ...
 374-576 3.86e-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: 148.97  E-value: 3.86e-41
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2559057711  374 RQYYIAAEEIIWDYgptginqysgmKLVDDSVSDTFFENRNDRIGGKYKKVQYVEYADDTFTKRKERTPeeqHLGILGPI 453
Cdd:cd14452      1 RRYYIAAVEIGWDY-----------IHSDLGDPASEQRKKPKDIPQKYIKAVFVEYLDATFTVPKPRPA---WMGLLGPT 66

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2559057711  454 IRAEEEDTIKVTFRNKASRPYSIQPHGVQYSIEMDGTLYhnvleESYTAKKLRELKKearvveplpaalVRPDTTYQYEW 533
Cdd:cd14452     67 IVAEVGDTVVITFKNLASQPYSLHAVGVSYWKASEGAGY-----DDSTSQHEKEDDA------------VYPGGYHTYVW 129

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|...
gi 2559057711  534 VVPKDGGPTEKDPDCITYMYYSAVDPIRDTNSGLVGPLLICKP 576
Cdd:cd14452    130 DISPKDGPTGSDPECLTYSYSSQVDPVKDVNSGLIGALLVCRM 172
CuRO_1_Ceruloplasmin_like_1 cd04229
cupredoxin domain of ceruloplasmin homologs; Uncharacterized subfamily of ceruloplasmin ...
 747-915 3.23e-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: 146.41  E-value: 3.23e-40
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2559057711  747 YYIAAVEMDWDYSPTRTWEEQLHHSLKDSPGnkFLKKEGKFIGSKYKKVLYREYTDETFTKPKersADMEHLGIMGPMIH 826
Cdd:cd04229      3 YYIAAEEVDWDYAPSGKNKCCLGDDLEVSTL--DSQPGPYTIGSTYTKARYREYTDNSFSTPK---PTPAYLGILGPVIR 77

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2559057711  827 GKVGEKVKIVFKNMAKR-PYSIHAHGV-------KTDSPQVALTRPGETKTYTWYLPKNSGPTEQQEECSVGAYYSTVDV 898
Cdd:cd04229     78 AEVGDTIKVVFKNNLDEfPVNMHPHGGlyskdneGTTDGAGDVVAPGETYTYRWIVPEDAGPGPGDPSSRLWLYHSHVDV 157

                          170
                   ....*....|....*..
gi 2559057711  899 IKDMYSGLIGPLVICKK 915
Cdd:cd04229    158 FAHTNAGLVGPIIVTSK 174
CuRO_6_FVIII_like cd11018
The sixth cupredoxin domain of coagulation factor VIII and similar proteins; Factor VIII ...
 927-1070 1.66e-39

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: 143.48  E-value: 1.66e-39
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2559057711  927 IEEFALLFMVFDENESWYLDDNIKAHVKTPPTTLKEDEEFIESNKMHGINGLVYGNLKGLNMKVGDKVYWYLMGMGNEVD 1006
Cdd:cd11018      1 VQEFALLFTIFDETKSWYFEENMRRNCRPPCHIQTQDPWFHINNKFHAINGYVADTLPGLVMAQHQRIRWHLLNMGSDEE 80

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2559057711 1007 IHTAHFHGHSFDYKIGGTHRADVFDLFPGTFQTITMRPLYSGTWLLHCHVTDHIQAGMETTYTV 1070
Cdd:cd11018     81 IHSVHFHGLPFTVRAKKEYRMGVYNLYPGVFGTVEMRPSTAGIWLVECTVGEHLLAGMSALFLV 144
CuRO_1_FVIII_like cd14452
The first cupredoxin domain of coagulation factor VIII and similar proteins; Factor VIII ...
 745-916 7.45e-39

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: 142.42  E-value: 7.45e-39
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2559057711  745 KKYYIAAVEMDWDYsptrtweeqLHHSLKDSPGNKflKKEGKFIGSKYKKVLYREYTDETFTKPKERSADMehlGIMGPM 824
Cdd:cd14452      1 RRYYIAAVEIGWDY---------IHSDLGDPASEQ--RKKPKDIPQKYIKAVFVEYLDATFTVPKPRPAWM---GLLGPT 66

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2559057711  825 IHGKVGEKVKIVFKNMAKRPYSIHAHGV-------------KTDSPQVALTR--PGETKTYTWYLPKNSGPTEQQEECSV 889
Cdd:cd14452     67 IVAEVGDTVVITFKNLASQPYSLHAVGVsywkasegagyddSTSQHEKEDDAvyPGGYHTYVWDISPKDGPTGSDPECLT 146

                          170       180
                   ....*....|....*....|....*..
gi 2559057711  890 GAYYSTVDVIKDMYSGLIGPLVICKKS 916
Cdd:cd14452    147 YSYSSQVDPVKDVNSGLIGALLVCRMG 173
CuRO_6_FVIII_like cd11018
The sixth cupredoxin domain of coagulation factor VIII and similar proteins; Factor VIII ...
 220-355 1.53e-36

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: 135.01  E-value: 1.53e-36
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2559057711  220 YTLMFTVSDENLSWYLEENIKTYCTAPAKVNKDDEGFQESNKMHSINGYVYGNLPDLSMCMGNKIHWHLFGMGNEVDLHS 299
Cdd:cd11018      4 FALLFTIFDETKSWYFEENMRRNCRPPCHIQTQDPWFHINNKFHAINGYVADTLPGLVMAQHQRIRWHLLNMGSDEEIHS 83

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 2559057711  300 AFFHGQILT---DKRHHVDTVSLFPATFVHVEMVADNPGQWLLSCQVNDHMEAGMQAIF 355
Cdd:cd11018     84 VHFHGLPFTvraKKEYRMGVYNLYPGVFGTVEMRPSTAGIWLVECTVGEHLLAGMSALF 142
CuRO_2_ceruloplasmin_like_2 cd11023
cupredoxin domain of ceruloplasmin homologs; Uncharacterized subfamily of ceruloplasmin ...
 252-357 3.83e-36

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: 132.73  E-value: 3.83e-36
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2559057711  252 DDEGFQESNKMHSINGYVYGNLPDLSMCMGNKIHWHLFGMGNEVDLHSAFFHGQ-ILTDKRHHVDTVSLFPATFVHVEMV 330
Cdd:cd11023     12 LDLNVEEAGLMHSINGYVFGNLPGVTIAKGKRVRWHLVAYGNEVDFHTPHWHGQtVEADKSRRTDVAELMPASMRVADMT 91

                           90       100
                   ....*....|....*....|....*..
gi 2559057711  331 ADNPGQWLLSCQVNDHMEAGMQAIFEI 357
Cdd:cd11023     92 AADVGTWLLHCHVHDHYMAGMMTQFAV 118
CuRO_1_FV_like cd04226
The first cupredoxin domain of coagulation factor VIII and similar proteins; Factor V is an ...
 745-915 1.64e-35

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: 132.68  E-value: 1.64e-35
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2559057711  745 KKYYIAAVEMDWDYSPtrtweEQLHHSLKDSpgnkflkkegkfiGSKYKKVLYREYtDETFTKPKERSadmEHLGIMGPM 824
Cdd:cd04226      1 REYYIAAQNIDWDYTP-----QSEELRLKRS-------------EQSFKKIVYREY-EEGFKKEKPAD---LSSGLLGPT 58

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2559057711  825 IHGKVGEKVKIVFKNMAKRPYSIHAHGVK----------TD--SPQVAL---TRPGETKTYTWYLPKNSGPTEQQEECSV 889
Cdd:cd04226     59 LRAEVGDTLIVHFKNMADKPLSIHPQGIAygkksegslySDntSPVEKLddaVQPGQEYTYVWDITEEVGPTEADPPCLT 138

                          170       180
                   ....*....|....*....|....*.
gi 2559057711  890 GAYYSTVDVIKDMYSGLIGPLVICKK 915
Cdd:cd04226    139 YIYYSHVNMVRDFNSGLIGALLICKK 164
CuRO_6_FV_like cd14455
The sixth cupredoxin domain of coagulation factor V and similar proteins; Factor V is an ...
 927-1070 3.05e-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: 3.05e-35
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2559057711  927 IEEFALLFMVFDENESWYLDDNIKahvKTPPTTLKEDEEFIESNKMHGINGLVYgNLKGLNMKVGDKVYWYLMGMGNEVD 1006
Cdd:cd14455      1 RREFVLLFMTFDEEKSWYYEKNRK---RTCRENRVKDPNVQDNHTFHAINGIIY-NLKGLRMYTNELVRWHLINMGGPKD 76

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2559057711 1007 IHTAHFHGHSFDYKIGGTHRADVFDLFPGTFQTITMRPLYSGTWLLHCHVTDHIQAGMETTYTV 1070
Cdd:cd14455     77 LHVVHFHGQTFTEKGLKDHQLGVYPLLPGSFATLEMKPSKPGLWLLETEVGESQQRGMQTLFLV 140
CuRO_4_FVIII_like cd11016
The fourth cupredoxin domain of coagulation factor VIII and similar proteins; Factor VIII ...
 588-731 3.78e-35

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: 130.76  E-value: 3.78e-35
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2559057711  588 DKEFHLLATVFDENLSWYLDDNINRFAKQPKSVKKEDEDFQESNKMHSLNGYMYGNLiGLSMCKGDKVSWHLSGLGSEVD 667
Cdd:cd11016      1 DKDWSLLFSVFDENNSWYLKENIHRFTQTPAGVNDTDPDFYASNVMHTINGIVFDRR-QFVICLTDVAYWYVLSVGAQTD 79

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2559057711  668 IHGLYFEGNRFLYKDTRRDTINVFPHISHTVIMEPDSMGQFEVGCKTTDHYHGGMRANYTVEKC 731
Cdd:cd11016     80 FLSVFFSGNTFKHQMVYEDVLTLFPFSGETVSMSPEVPGEWELGCFNGDFRSRGMSAQYTVSTC 143
CuRO_2_ceruloplasmin_like_2 cd11023
cupredoxin domain of ceruloplasmin homologs; Uncharacterized subfamily of ceruloplasmin ...
 963-1070 2.01e-34

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: 127.73  E-value: 2.01e-34
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2559057711  963 DEEFIESNKMHGINGLVYGNLKGLNMKVGDKVYWYLMGMGNEVDIHTAHFHGHSFDykIGGTHRADVFDLFPGTFQTITM 1042
Cdd:cd11023     13 DLNVEEAGLMHSINGYVFGNLPGVTIAKGKRVRWHLVAYGNEVDFHTPHWHGQTVE--ADKSRRTDVAELMPASMRVADM 90

                           90       100
                   ....*....|....*....|....*...
gi 2559057711 1043 RPLYSGTWLLHCHVTDHIQAGMETTYTV 1070
Cdd:cd11023     91 TAADVGTWLLHCHVHDHYMAGMMTQFAV 118
CuRO_4_FV_like cd14454
The fourth cupredoxin domain of coagulation factor V and similar proteins; Factor V is an ...
 223-360 6.99e-33

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: 124.21  E-value: 6.99e-33
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2559057711  223 MFTVSDENLSWYLEENIKTYCTAPAKVNKDDEGFQESNKMHSINGYVYGNLPDLSMCMGNKIHWHLFGMGNEVDLHSAFF 302
Cdd:cd14454      7 VFAVFDENKSWYLEENINKYCSNPNNVKKDDPKFYKSNIMPTINGYAYESSAPLGFCHSEVVQWHISSVGTQDEIITVHL 86

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 2559057711  303 HGQILTDKRHHVDTVSLFPATFVHVEMVADNPGQWLLSCQVNDHMEAGMQAIFEIKKC 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 ...
 588-731 9.26e-33

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: 123.83  E-value: 9.26e-33
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2559057711  588 DKEFHLLATVFDENLSWYLDDNINRFAKQPKSVKKEDEDFQESNKMHSLNGYMYGNLIGLSMCKGDKVSWHLSGLGSEVD 667
Cdd:cd14454      1 DLEQHAVFAVFDENKSWYLEENINKYCSNPNNVKKDDPKFYKSNIMPTINGYAYESSAPLGFCHSEVVQWHISSVGTQDE 80

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2559057711  668 IHGLYFEGNRFLYKDTRRDTINVFPHISHTVIMEPDSMGQFEVGCKTTDHYHGGMRANYTVEKC 731
Cdd:cd14454     81 IITVHLSGHTFRYKGKHEDTLNLFPMSGESITVTMDNLGTWLLGSFGSSKKSKGLRVRFTDVIC 144
CuRO_5_FVIII_like cd04228
The fifth cupredoxin domain of coagulation factor VIII and similar proteins; Factor VIII ...
 22-206 1.00e-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: 121.92  E-value: 1.00e-31
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2559057711   22 TREYFFAIKEIQWDYAPSGKNliqnKTIKEDEearvfLERGEQRIGRVYKKAVYQQYTDATYRQEIDKPKW---LGYLGP 98
Cdd:cd04228      1 IRHYFIAAVEVLWDYGMQRPQ----HFLRARD-----PNRGRRKSVPQYKKVVFREYLDGSFTQPVYRGELdehLGILGP 71

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2559057711   99 LISAEEDDVVIVHLKNTARRAYSIHAHGLSYNKTnegalypdssEKVEKADDSVAPGKSFTYVWTLPASHTPGKDETNCL 178
Cdd:cd04228     72 YIRAEVEDNIMVTFKNLASRPYSFHSSLISYEED----------QRAEPRGNFVQPGEVQTYSWKVLHQMAPTKQEFDCK 141

                          170       180
                   ....*....|....*....|....*...
gi 2559057711  179 TRIYHSHVNAPKDIASGLIGPLIICKKG 206
Cdd:cd04228    142 AWAYFSNVDLEKDLHSGLIGPLIICKTG 169
CuRO_2_FV_like cd14453
The second cupredoxin domain of coagulation factor V and similar proteins; Factor V is an ...
 220-357 1.15e-31

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: 119.96  E-value: 1.15e-31
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2559057711  220 YTLMFTVSDENLSWYleeniktyctapakvnkdDEGFQESNKMHSINGYVYGNLPDLSMCMGNKIHWHLFGMGNEVDLHS 299
Cdd:cd14453      4 YVLMFGVFDENKSWY------------------KQNASVDSVKYTINGYTNGTLPDVSICAYDHVSWHLLGMSSEPELFS 65

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 2559057711  300 AFFHGQILTDKRHHVDTVSLFPATFVHVEMVADNPGQWLLSCQVNDHMEAGMQAIFEI 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 2.57e-31

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: 119.97  E-value: 2.57e-31
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2559057711  217 DYLYTLMFTVSDENLSWYLEENIKTYCTAPAKVNKDDEGFQESNKMHSINGYVYGNLpDLSMCMGNKIHWHLFGMGNEVD 296
Cdd:cd11016      1 DKDWSLLFSVFDENNSWYLKENIHRFTQTPAGVNDTDPDFYASNVMHTINGIVFDRR-QFVICLTDVAYWYVLSVGAQTD 79

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2559057711  297 LHSAFFHGQILTDKRHHVDTVSLFPATFVHVEMVADNPGQWLLSCQVNDHMEAGMQAIFEIKKC 360
Cdd:cd11016     80 FLSVFFSGNTFKHQMVYEDVLTLFPFSGETVSMSPEVPGEWELGCFNGDFRSRGMSAQYTVSTC 143
CuRO_6_FV_like cd14455
The sixth cupredoxin domain of coagulation factor V and similar proteins; Factor V is an ...
 220-357 2.71e-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: 116.89  E-value: 2.71e-30
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2559057711  220 YTLMFTVSDENLSWYLEENIKTYCTapaKVNKDDEGFQESNKMHSINGYVYgNLPDLSMCMGNKIHWHLFGMGNEVDLHS 299
Cdd:cd14455      4 FVLLFMTFDEEKSWYYEKNRKRTCR---ENRVKDPNVQDNHTFHAINGIIY-NLKGLRMYTNELVRWHLINMGGPKDLHV 79

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2559057711  300 AFFHGQILTD---KRHHVDTVSLFPATFVHVEMVADNPGQWLLSCQVNDHMEAGMQAIFEI 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 5.72e-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: 116.13  E-value: 5.72e-30
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2559057711  589 KEFHLLATVFDENLSWYLDDNINRFAKQPKSVKKEDEDFQESNKMHSLNGYMYGNLIGLSMCKGDKVSWHLSGLGSEVDI 668
Cdd:cd11018      2 QEFALLFTIFDETKSWYFEENMRRNCRPPCHIQTQDPWFHINNKFHAINGYVADTLPGLVMAQHQRIRWHLLNMGSDEEI 81

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2559057711  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 6.98e-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: 107.26  E-value: 6.98e-27
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2559057711  926 EIEEFALlFMVFDENESWYLDDNIKAHVKTPPTTLKEDEEFIESNKMHGINGLVYGNLKGLNMKVGDKVYWYLMGMGNEV 1005
Cdd:cd14454      1 DLEQHAV-FAVFDENKSWYLEENINKYCSNPNNVKKDDPKFYKSNIMPTINGYAYESSAPLGFCHSEVVQWHISSVGTQD 79

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*..
gi 2559057711 1006 DIHTAHFHGHSFDYKigGTHRaDVFDLFPGTFQTITMRPLYSGTWLL 1052
Cdd:cd14454     80 EIITVHLSGHTFRYK--GKHE-DTLNLFPMSGESITVTMDNLGTWLL 123
CuRO_2_FVIII_like cd11015
The second cupredoxin domain of coagulation factor VIII and similar proteins; Factor VIII ...
 220-357 3.09e-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: 104.99  E-value: 3.09e-26
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2559057711  220 YTLMFTVSDENLSWYLE--ENIKTYCTAPAKVNKddegfqesnKMHSINGYVYGNLPDLSMCMGNKIHWHLFGMGNEVDL 297
Cdd:cd11015      4 FVLLFAVFDEGKSWYSEvgERKSRDKFKRADSRK---------EFHTINGYINASLPGLKICQRKPVIWHVIGMGTAPEV 74

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 2559057711  298 HSAFFHGQILTDKRHHVDTVSLFPATFVHVEMVADNPGQWLLSCQVNDHMEAGMQAIFEI 357
Cdd:cd11015     75 HSIFFEGHTFLVRTHRKVSLEISPMTFLTAQTKPATVGSFLIFCQIHSHQHDGMEAMVKV 134
CuRO_4_FVIII_like cd11016
The fourth cupredoxin domain of coagulation factor VIII and similar proteins; Factor VIII ...
 932-1072 1.80e-25

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: 103.02  E-value: 1.80e-25
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2559057711  932 LLFMVFDENESWYLDDNIKAHVKTPPTTLKEDEEFIESNKMHGINGLVYGNLKgLNMKVGDKVYWYLMGMGNEVDIHTAH 1011
Cdd:cd11016      6 LLFSVFDENNSWYLKENIHRFTQTPAGVNDTDPDFYASNVMHTINGIVFDRRQ-FVICLTDVAYWYVLSVGAQTDFLSVF 84

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2559057711 1012 FHGHSFDYKigGTHRaDVFDLFPGTFQTITMRPLYSGTWLLHCHVTDHIQAGMETTYTVLE 1072
Cdd:cd11016     85 FSGNTFKHQ--MVYE-DVLTLFPFSGETVSMSPEVPGEWELGCFNGDFRSRGMSAQYTVST 142
CuRO_2_FVIII_like cd11015
The second cupredoxin domain of coagulation factor VIII and similar proteins; Factor VIII ...
 928-1070 5.08e-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: 95.74  E-value: 5.08e-23
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2559057711  928 EEFALLFMVFDENESWYLD-DNIKAHVKTPPTTLKEdeefiesnKMHGINGLVYGNLKGLNMKVGDKVYWYLMGMGNEVD 1006
Cdd:cd11015      2 QAFVLLFAVFDEGKSWYSEvGERKSRDKFKRADSRK--------EFHTINGYINASLPGLKICQRKPVIWHVIGMGTAPE 73

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2559057711 1007 IHTAHFHGHSFDYKiggTHRADVFDLFPGTFQTITMRPLYSGTWLLHCHVTDHIQAGMETTYTV 1070
Cdd:cd11015     74 VHSIFFEGHTFLVR---THRKVSLEISPMTFLTAQTKPATVGSFLIFCQIHSHQHDGMEAMVKV 134
CuRO_2_ceruloplasmin_like_2 cd11023
cupredoxin domain of ceruloplasmin homologs; Uncharacterized subfamily of ceruloplasmin ...
 624-728 6.37e-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: 94.98  E-value: 6.37e-23
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2559057711  624 DEDFQESNKMHSLNGYMYGNLIGLSMCKGDKVSWHLSGLGSEVDIHGLYFEGNRFLYKDTRR-DTINVFPHISHTVIMEP 702
Cdd:cd11023     13 DLNVEEAGLMHSINGYVFGNLPGVTIAKGKRVRWHLVAYGNEVDFHTPHWHGQTVEADKSRRtDVAELMPASMRVADMTA 92

                           90       100
                   ....*....|....*....|....*.
gi 2559057711  703 DSMGQFEVGCKTTDHYHGGMRANYTV 728
Cdd:cd11023     93 ADVGTWLLHCHVHDHYMAGMMTQFAV 118
CuRO_2_FVIII_like cd11015
The second cupredoxin domain of coagulation factor VIII and similar proteins; Factor VIII ...
 589-728 1.59e-22

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: 94.20  E-value: 1.59e-22
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2559057711  589 KEFHLLATVFDENLSWYLDDNINRFAKQPKSVKKEDEdfqesnkMHSLNGYMYGNLIGLSMCKGDKVSWHLSGLGSEVDI 668
Cdd:cd11015      2 QAFVLLFAVFDEGKSWYSEVGERKSRDKFKRADSRKE-------FHTINGYINASLPGLKICQRKPVIWHVIGMGTAPEV 74

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 2559057711  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 1.49e-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: 85.29  E-value: 1.49e-19
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2559057711  928 EEFALLFMVFDENESWYLDDNIKAHVktppttlkedeefiesnkMHGINGLVYGNLKGLNMKVGDKVYWYLMGMGNEVDI 1007
Cdd:cd14453      2 KEYVLMFGVFDENKSWYKQNASVDSV------------------KYTINGYTNGTLPDVSICAYDHVSWHLLGMSSEPEL 63

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 2559057711 1008 HTAHFHGHSFDYKiggTHRADVFDLFPGTFQTITMRPLYSGTWLLHCHVTDHIQAGM 1064
Cdd:cd14453     64 FSVHFNGQVLEQN---GHKVSAVGLVSGSSTTASMTVVHTGRWLISSLIMKHLQAGM 117
CuRO_6_FV_like cd14455
The sixth cupredoxin domain of coagulation factor V and similar proteins; Factor V is an ...
 589-728 6.97e-18

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: 81.45  E-value: 6.97e-18
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2559057711  589 KEFHLLATVFDENLSWYLDDNINRFAKQpksVKKEDEDFQESNKMHSLNGYMYgNLIGLSMCKGDKVSWHLSGLGSEVDI 668
Cdd:cd14455      2 REFVLLFMTFDEEKSWYYEKNRKRTCRE---NRVKDPNVQDNHTFHAINGIIY-NLKGLRMYTNELVRWHLINMGGPKDL 77

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2559057711  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 7.19e-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: 81.33  E-value: 7.19e-18
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2559057711  970 NKMHGINGLVYG-NLKGLNMKVGDKVYWYLMGMGNevDIHTAHFHGHSFD----------YKIGGTH------RADVFDL 1032
Cdd:pfam07731   19 RNDWAINGLLFPpNTNVITLPYGTVVEWVLQNTTT--GVHPFHLHGHSFQvlgrgggpwpEEDPKTYnlvdpvRRDTVQV 96

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|..
gi 2559057711 1033 FPGTFQTITMRPLYSGTWLLHCHVTDHIQAGMETTYTVLEKD 1074
Cdd:pfam07731   97 PPGGWVAIRFRADNPGVWLFHCHILWHLDQGMMGQFVVRPGD 138
CuRO_1_LCC_like cd04206
Cupredoxin domain 1 of laccase-like multicopper oxidases; including laccase, CueO, spore coat ...
 96-203 5.26e-15

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: 72.32  E-value: 5.26e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2559057711   96 LGPLISAEEDDVVIVHLKNT-ARRAYSIHAHGLSYNKTNEGALYPDSSEkvekadDSVAPGKSFTYVWTLPasHTPGkde 174
Cdd:cd04206     29 PGPTIRVKEGDTVEVTVTNNlPNEPTSIHWHGLRQPGTNDGDGVAGLTQ------CPIPPGESFTYRFTVD--DQAG--- 97

                           90       100
                   ....*....|....*....|....*....
gi 2559057711  175 tnclTRIYHSHVNApkDIASGLIGPLIIC 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 ...
 588-724 5.88e-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: 72.20  E-value: 5.88e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2559057711  588 DKEFHLLATVFDENLSWYlddninrfakqpksvkkeDEDFQESNKMHSLNGYMYGNLIGLSMCKGDKVSWHLSGLGSEVD 667
Cdd:cd14453      1 YKEYVLMFGVFDENKSWY------------------KQNASVDSVKYTINGYTNGTLPDVSICAYDHVSWHLLGMSSEPE 62

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 2559057711  668 IHGLYFEGNRFLYKDTRRDTINVFPHISHTVIMEPDSMGQFEVGCKTTDHYHGGMRA 724
Cdd:cd14453     63 LFSVHFNGQVLEQNGHKVSAVGLVSGSSTTASMTVVHTGRWLISSLIMKHLQAGMYG 119
CuRO_1_Diphenol_Ox cd13857
The first cupredoxin domain of fungal laccase, diphenol oxidase; Diphenol oxidase belongs to ...
 95-202 3.35e-12

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: 64.20  E-value: 3.35e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2559057711   95 YLGPLISAEEDDVVIVHLKNTARRAYSIHAHGLSYNKTNegalYPDSSEKVEKAddSVAPGKSFTYVWTLpashtpgKDE 174
Cdd:cd13857     28 FPGPLIEANQGDRIVVHVTNELDEPTSIHWHGLFQNGTN----WMDGTAGITQC--PIPPGGSFTYNFTV-------DGQ 94

                           90       100
                   ....*....|....*....|....*...
gi 2559057711  175 TNclTRIYHSHVNAPKdiASGLIGPLII 202
Cdd:cd13857     95 YG--TYWYHSHYSTQY--ADGLVGPLIV 118
CuRO_3_LCC_like cd04207
Cupredoxin domain 3 of laccase-like multicopper oxidases; including laccase, CueO, spore coat ...
 264-356 4.89e-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: 61.32  E-value: 4.89e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2559057711  264 SINGYVY----GNLPDLSMCMGNKIHWHLFGMGNEVDLHSAFFHG---QIL---TDKRHHV---------DTVSLFPATF 324
Cdd:cd04207     21 VINGMPFkegdANTDIFSVEAGDVVEIVLINAGNHDMQHPFHLHGhsfWVLgsgGGPFDAPlnltnppwrDTVLVPPGGW 100

                           90       100       110
                   ....*....|....*....|....*....|..
gi 2559057711  325 VHVEMVADNPGQWLLSCQVNDHMEAGMQAIFE 356
Cdd:cd04207    101 VVIRFKADNPGVWMLHCHILEHEDAGMMTVFE 132
CuRO_1_CumA_like cd13861
The first cupredoxin domain of CumA like multicopper oxidase; This multicopper oxidase (MCO) ...
 448-573 9.69e-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: 59.94  E-value: 9.69e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2559057711  448 GILGPIIRAEEEDTIKVTFRNKASRPYSIQPHGVQYSIEMDGtlyhnvleesytakklrelkkearvVEPLPAALVRPDT 527
Cdd:cd13861     28 QVPGPELRVRQGDTLRVRLTNRLPEPTTIHWHGLRLPNAMDG-------------------------VPGLTQPPVPPGE 82

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*.
gi 2559057711  528 TYQYEWVVPkDGGptekdpdciTYMYYSAVDPIRDTNSGLVGPLLI 573
Cdd:cd13861     83 SFTYEFTPP-DAG---------TYWYHPHVGSQEQLDRGLYGPLIV 118
CuRO_3_CumA_like cd13906
The third cupredoxin domain of CumA like multicopper oxidase; This multicopper oxidase (MCO) ...
 286-358 1.45e-10

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


Pssm-ID: 259973 [Multi-domain]  Cd Length: 138  Bit Score: 60.09  E-value: 1.45e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2559057711  286 WHLFGMGNEVD-LHSAFFHGQILT---------DKRHHVDTVSLFPATFVHVEMVADNPGQWLLSCQVNDHMEAGMQAIF 355
Cdd:cd13906     56 SYVLRLVNETAfLHPMHLHGHFFRvlsrngrpvPEPFWRDTVLLGPKETVDIAFVADNPGDWMFHCHILEHQETGMMGVI 135


                   ...
gi 2559057711  356 EIK 358
Cdd:cd13906    136 RVA 138
CuRO_D2_2dMcoN_like cd04202
The second cupredoxin domain of bacterial two domain multicopper oxidase McoN and similar ...
 975-1064 5.51e-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: 58.42  E-value: 5.51e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2559057711  975 INGLVYGNLKGLNMKVGDKVYWYLMGMGNevDIHTAHFHGHSFDY--KIGGT------HRADVFDLFPGTFQTITMRPLY 1046
Cdd:cd04202     32 INGKSFPATPPLVVKEGDRVRIRLINLSM--DHHPMHLHGHFFLVtaTDGGPipgsapWPKDTLNVAPGERYDIEFVADN 109

                           90
                   ....*....|....*...
gi 2559057711 1047 SGTWLLHCHVTDHIQAGM 1064
Cdd:cd04202    110 PGDWMFHCHKLHHAMNGM 127
Cu-oxidase_3 pfam07732
Multicopper oxidase; This entry contains many divergent copper oxidase-like domains that are ...
 95-202 7.82e-10

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: 57.64  E-value: 7.82e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2559057711   95 YLGPLISAEEDDVVIVHLKNTARRAYSIHAHGLSYNKTNEGALYPDSSEkvekadDSVAPGKSFTYVWtlPASHTPGkde 174
Cdd:pfam07732   24 FPGPTIRVREGDTVVVNVTNNLDEPTSIHWHGLQQRGTPWMDGVPGVTQ------CPIPPGQSFTYRF--QVKQQAG--- 92

                           90       100
                   ....*....|....*....|....*...
gi 2559057711  175 tnclTRIYHSHVNAPKdiASGLIGPLII 202
Cdd:pfam07732   93 ----TYWYHSHTSGQQ--AAGLAGAIII 114
CuRO_1_CumA_like cd13861
The first cupredoxin domain of CumA like multicopper oxidase; This multicopper oxidase (MCO) ...
 97-202 9.29e-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: 57.24  E-value: 9.29e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2559057711   97 GPLISAEEDDVVIVHLKNTARRAYSIHAHGLSYNKTNEGAlyPDSSEkvekadDSVAPGKSFTYVWTLPashTPGkdetn 176
Cdd:cd13861     31 GPELRVRQGDTLRVRLTNRLPEPTTIHWHGLRLPNAMDGV--PGLTQ------PPVPPGESFTYEFTPP---DAG----- 94

                           90       100
                   ....*....|....*....|....*.
gi 2559057711  177 clTRIYHSHVNAPKDIASGLIGPLII 202
Cdd:cd13861     95 --TYWYHPHVGSQEQLDRGLYGPLIV 118
CuRO_3_LCC_like cd04207
Cupredoxin domain 3 of laccase-like multicopper oxidases; including laccase, CueO, spore coat ...
 975-1069 9.89e-10

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: 57.86  E-value: 9.89e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2559057711  975 INGLVY----GNLKGLNMKVGDKVYWYLMGMGNEVDIHTAHFHGHSF---DYKIGGTHRA---------DVFDLFPGTFQ 1038
Cdd:cd04207     22 INGMPFkegdANTDIFSVEAGDVVEIVLINAGNHDMQHPFHLHGHSFwvlGSGGGPFDAPlnltnppwrDTVLVPPGGWV 101

                           90       100       110
                   ....*....|....*....|....*....|.
gi 2559057711 1039 TITMRPLYSGTWLLHCHVTDHIQAGMETTYT 1069
Cdd:cd04207    102 VIRFKADNPGVWMLHCHILEHEDAGMMTVFE 132
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 2.49e-09

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: 56.51  E-value: 2.49e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2559057711   97 GPLISAEEDDVVIVHLKNTARRAYSIHAHGLSYNKTNEGALYPDSsekvekaddSVAPGKSFTYVWTlpaSHTPGKDETN 176
Cdd:cd14449     29 GPVIEVREGDTLKILFRNTLDVPASLHPHGVDYTTASDGTGMNAS---------IVAPGDTRIYTWR---THGGYRRADG 96

                           90       100       110
                   ....*....|....*....|....*....|....*.
gi 2559057711  177 CL------TRIYHSHV----NAPKDIASGLIGPLII 202
Cdd:cd14449     97 SWaegtagYWHYHDHVfgteHGTEGLSRGLYGALIV 132
CuRO_D1_2dMcoN_like cd13859
The first cupredoxin domain of bacterial two domain multicopper oxidase McoN and similar ...
 97-202 3.95e-09

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: 55.56  E-value: 3.95e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2559057711   97 GPLISAEEDDVVIVHLKNTARRAYSIHAHGLSYNKT--NEGAlyPDSSEKvekaddSVAPGKSFTYVWTlpaSHTPGkde 174
Cdd:cd13859     31 GPLIHVKEGDDLVVHVTNNTTLPHTIHWHGVLQMGSwkMDGV--PGVTQP------AIEPGESFTYKFK---AERPG--- 96

                           90       100
                   ....*....|....*....|....*....
gi 2559057711  175 tnclTRIYHSHVNAPKDIA-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 9.42e-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: 54.60  E-value: 9.42e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2559057711  427 VEYADDTFtKRKERTPEEQHLGILGPIIRAEEEDTIKVTFRNK-ASRPYSIQPHGVQYSIEMDGTlyhnvleesytakkl 505
Cdd:cd04206      7 ITETTVNP-DGVLRQVITVNGQFPGPTIRVKEGDTVEVTVTNNlPNEPTSIHWHGLRQPGTNDGD--------------- 70

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2559057711  506 relkkearVVEPLPAALVRPDTTYQYEWVVPKDGGptekdpdciTYMYYSAVDPIRDTnsGLVGPLLIC 574
Cdd:cd04206     71 --------GVAGLTQCPIPPGESFTYRFTVDDQAG---------TFWYHSHVGGQRAD--GLYGPLIVE 120
CuRO_1_2dMco_1 cd13860
The first cupredoxin domain of bacteria two domain multicopper oxidase; This subfamily ...
 97-202 1.01e-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: 54.51  E-value: 1.01e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2559057711   97 GPLISAEEDDVVIVHLKNTARRAYSIHAHGLSYNKTNEGAlyPDSSEkvekadDSVAPGKSFTYVWTLpasHTPGkdetn 176
Cdd:cd13860     31 GPTIEVTEGDRVRILVTNELPEPTTVHWHGLPVPNGMDGV--PGITQ------PPIQPGETFTYEFTA---KQAG----- 94

                           90       100
                   ....*....|....*....|....*.
gi 2559057711  177 clTRIYHSHVNAPKDIASGLIGPLII 202
Cdd:cd13860     95 --TYMYHSHVDEAKQEDMGLYGAFIV 118
SufI COG2132
Multicopper oxidase with three cupredoxin domains (includes cell division protein FtsP and ...
 95-202 1.19e-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: 58.79  E-value: 1.19e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2559057711   95 YLGPLISAEEDDVVIVHLKNTARRAYSIHAHGLSYNKTNEGAlypdssekvekADDSVAPGKSFTYVWTLPasHTPGkde 174
Cdd:COG2132     42 YPGPTIRVREGDRVRVRVTNRLPEPTTVHWHGLRVPNAMDGV-----------PGDPIAPGETFTYEFPVP--QPAG--- 105

                           90       100       110
                   ....*....|....*....|....*....|
gi 2559057711  175 tnclTRIYHSHVNA--PKDIASGLIGPLII 202
Cdd:COG2132    106 ----TYWYHPHTHGstAEQVYRGLAGALIV 131
CuRO_3_Fet3p cd13899
The third Cupredoxin domain of multicopper oxidase Fet3p; Fet3p catalyzes the ferroxidase ...
 315-355 2.03e-08

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: 54.57  E-value: 2.03e-08
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|.
gi 2559057711  315 DTVSLFPATFVHVEMVADNPGQWLLSCQVNDHMEAGMQAIF 355
Cdd:cd13899    116 DTVMVPPGGSVVIRFRADNPGVWFFHCHIEWHLEAGLAATF 156
CuRO_1_Tv-LCC_like cd13856
The first cupredoxin domain of fungal laccases similar to Tv-LCC from Trametes versicolor; ...
 95-202 3.21e-08

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: 53.11  E-value: 3.21e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2559057711   95 YLGPLISAEEDDVVIVHLKN-----TARRAYSIHAHGLSYNKTNegalYPDSSEKVEKAddSVAPGKSFTYVWTLPasht 169
Cdd:cd13856     28 FPGPLITANKGDTFRITVVNqltdpTMRRSTSIHWHGIFQHGTN----YADGPAFVTQC--PIAPNHSFTYDFTAG---- 97

                           90       100       110
                   ....*....|....*....|....*....|...
gi 2559057711  170 pgkDETNclTRIYHSHVNApkDIASGLIGPLII 202
Cdd:cd13856     98 ---DQAG--TFWYHSHLST--QYCDGLRGPLVI 123
CuRO_3_CumA_like cd13906
The third cupredoxin domain of CumA like multicopper oxidase; This multicopper oxidase (MCO) ...
 986-1070 1.41e-07

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: 51.62  E-value: 1.41e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2559057711  986 LNMKVGDkvyWYLMGMGNEVD-IHTAHFHGHSFDY------KIGGTHRADVFDLFPGTFQTITMRPLYSGTWLLHCHVTD 1058
Cdd:cd13906     49 ATLKRGR---SYVLRLVNETAfLHPMHLHGHFFRVlsrngrPVPEPFWRDTVLLGPKETVDIAFVADNPGDWMFHCHILE 125

                           90
                   ....*....|..
gi 2559057711 1059 HIQAGMETTYTV 1070
Cdd:cd13906    126 HQETGMMGVIRV 137
CuRO_1_Abr2_like cd13850
The first cupredoxin domain of a group of fungal Laccases similar to Abr2 from Aspergillus ...
 97-202 2.24e-07

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: 50.37  E-value: 2.24e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2559057711   97 GPLISAEEDDVVIVHLKNTARRAYSIHAHGLSYNKTNEGALYPDSSEKVekaddsVAPGKSFTYVWTLpashtpgKDETN 176
Cdd:cd13850     28 GPPIILDEGDEVEILVTNNLPVNTTIHFHGILQRGTPWSDGVPGVTQWP------IQPGGSFTYRWKA-------EDQYG 94

                           90       100
                   ....*....|....*....|....*.
gi 2559057711  177 clTRIYHSHVNApkDIASGLIGPLII 202
Cdd:cd13850     95 --LYWYHSHYRG--YYMDGLYGPIYI 116
CuRO_1_2DMCO_NIR_like_2 cd14449
The cupredoxin domain 1 of a two-domain laccase related to nitrite reductase; The two-domain ...
 451-533 2.55e-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: 50.73  E-value: 2.55e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2559057711  451 GPIIRAEEEDTIKVTFRNKASRPYSIQPHGVQYSIEMDGTLyhnvleesytakklrelkkearvvepLPAALVRPDTTYQ 530
Cdd:cd14449     29 GPVIEVREGDTLKILFRNTLDVPASLHPHGVDYTTASDGTG--------------------------MNASIVAPGDTRI 82


                   ...
gi 2559057711  531 YEW 533
Cdd:cd14449     83 YTW 85
CuRO_1_2DMCO_NIR_like cd11024
The cupredoxin domain 1 of a two-domain laccase related to nitrite reductase; The two-domain ...
 451-490 2.56e-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. 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: 50.35  E-value: 2.56e-07
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|
gi 2559057711  451 GPIIRAEEEDTIKVTFRNKASRPYSIQPHGVQYSiEMDGT 490
Cdd:cd11024     32 GPTLRATEGDLVRIHFINTGDHPHTIHFHGIHDA-AMDGT 70
SufI COG2132
Multicopper oxidase with three cupredoxin domains (includes cell division protein FtsP and ...
 449-573 2.57e-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: 2.57e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2559057711  449 ILGPIIRAEEEDTIKVTFRNKASRPYSIQPHGVQYSIEMDGTlyhnvleesytakklrelkkearvveplPAALVRPDTT 528
Cdd:COG2132     42 YPGPTIRVREGDRVRVRVTNRLPEPTTVHWHGLRVPNAMDGV----------------------------PGDPIAPGET 93

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*..
gi 2559057711  529 YQYEWVVPKDGGptekdpdciTYMYYSAVDPIRDTN--SGLVGPLLI 573
Cdd:COG2132     94 FTYEFPVPQPAG---------TYWYHPHTHGSTAEQvyRGLAGALIV 131
CuRO_1_LCC_like cd04206
Cupredoxin domain 1 of laccase-like multicopper oxidases; including laccase, CueO, spore coat ...
 819-913 2.97e-07

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: 50.36  E-value: 2.97e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2559057711  819 GIMGPMIHGKVGEKVKIVFKN-MAKRPYSIHAHGVKT-----DSPQVALT----RPGETKTYTWylpknsgPTEQQeecs 888
Cdd:cd04206     27 QFPGPTIRVKEGDTVEVTVTNnLPNEPTSIHWHGLRQpgtndGDGVAGLTqcpiPPGESFTYRF-------TVDDQ---- 95

                           90       100
                   ....*....|....*....|....*..
gi 2559057711  889 VGA--YYSTVDVikDMYSGLIGPLVIC 913
Cdd:cd04206     96 AGTfwYHSHVGG--QRADGLYGPLIVE 120
CuRO_1_2DMCO_NIR_like cd11024
The cupredoxin domain 1 of a two-domain laccase related to nitrite reductase; The two-domain ...
 97-202 3.13e-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. 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: 49.96  E-value: 3.13e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2559057711   97 GPLISAEEDDVVIVHLKNTARRAYSIHAHGLSYNKTNEGALypdssekvekadDSVAPGKSFTYVWTlpaSHTPGkdetn 176
Cdd:cd11024     32 GPTLRATEGDLVRIHFINTGDHPHTIHFHGIHDAAMDGTGL------------GPIMPGESFTYEFV---AEPAG----- 91

                           90       100
                   ....*....|....*....|....*...
gi 2559057711  177 clTRIYHSHVnAP--KDIASGLIGPLII 202
Cdd:cd11024     92 --THLYHCHV-QPlkEHIAMGLYGAFIV 116
CuRO_D2_2dMcoN_like cd04202
The second cupredoxin domain of bacterial two domain multicopper oxidase McoN and similar ...
 262-351 3.14e-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: 50.72  E-value: 3.14e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2559057711  262 MHSINGYVYGNLPDLSMCMGNKIHWHLFGMGNEVD---LHSAFFH------GQILTDKRHHVDTVSLFPATFVHVEMVAD 332
Cdd:cd04202     29 YFTINGKSFPATPPLVVKEGDRVRIRLINLSMDHHpmhLHGHFFLvtatdgGPIPGSAPWPKDTLNVAPGERYDIEFVAD 108

                           90
                   ....*....|....*....
gi 2559057711  333 NPGQWLLSCQVNDHMEAGM 351
Cdd:cd04202    109 NPGDWMFHCHKLHHAMNGM 127
CuRO_3_CopA cd13896
The third cupredoxin domain of CopA copper resistance protein family; CopA is a multicopper ...
 315-356 3.24e-07

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: 49.95  E-value: 3.24e-07
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|..
gi 2559057711  315 DTVSLFPATFVHVEMVADNPGQWLLSCQVNDHMEAGMQAIFE 356
Cdd:cd13896     73 DTVLVPPGETVSVDFDADNPGRWAFHCHNLYHMEAGMMRVVE 114
CuRO_1_2dMco_1 cd13860
The first cupredoxin domain of bacteria two domain multicopper oxidase; This subfamily ...
 451-573 3.27e-07

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: 49.89  E-value: 3.27e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2559057711  451 GPIIRAEEEDTIKVTFRNKASRPYSIQPHGVQYSIEMDGtlyhnvleesytakklrelkkearvVEPLPAALVRPDTTYQ 530
Cdd:cd13860     31 GPTIEVTEGDRVRILVTNELPEPTTVHWHGLPVPNGMDG-------------------------VPGITQPPIQPGETFT 85

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|...
gi 2559057711  531 YEWVVPKDGgptekdpdciTYMYYSAVDPIRDTNSGLVGPLLI 573
Cdd:cd13860     86 YEFTAKQAG----------TYMYHSHVDEAKQEDMGLYGAFIV 118
Cu-oxidase_2 pfam07731
Multicopper oxidase; This entry contains many divergent copper oxidase-like domains that are ...
 256-358 4.27e-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: 50.13  E-value: 4.27e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2559057711  256 FQESNKMHSINGYVYG-NLPDLSMCMGNKIHWHLFGMGNEVD---LHSAFF------HGQILTDKRHHV--------DTV 317
Cdd:pfam07731   15 GNFRRNDWAINGLLFPpNTNVITLPYGTVVEWVLQNTTTGVHpfhLHGHSFqvlgrgGGPWPEEDPKTYnlvdpvrrDTV 94

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|.
gi 2559057711  318 SLFPATFVHVEMVADNPGQWLLSCQVNDHMEAGMQAIFEIK 358
Cdd:pfam07731   95 QVPPGGWVAIRFRADNPGVWLFHCHILWHLDQGMMGQFVVR 135
SufI COG2132
Multicopper oxidase with three cupredoxin domains (includes cell division protein FtsP and ...
 972-1072 8.32e-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: 52.63  E-value: 8.32e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2559057711  972 MHGINGLVYGNLK-GLNMKVGDKVYWYLMGMGNevDIHTAHFHGHSF------DYKIGGTHRADVFDLFPGtfQTITMR- 1043
Cdd:COG2132    317 VWTINGKAFDPDRpDLTVKLGERERWTLVNDTM--MPHPFHLHGHQFqvlsrnGKPPPEGGWKDTVLVPPG--ETVRILf 392

                           90       100       110
                   ....*....|....*....|....*....|.
gi 2559057711 1044 --PLYSGTWLLHCHVTDHIQAGMETTYTVLE 1072
Cdd:COG2132    393 rfDNYPGDWMFHCHILEHEDAGMMGQFEVVP 423
CuRO_1_Fet3p cd13851
The first Cupredoxin domain of multicopper oxidase Fet3P; Fet3p catalyzes the ferroxidase ...
 98-202 1.25e-06

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: 48.42  E-value: 1.25e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2559057711   98 PLISAEEDDVVIVHLKNT-ARRAYSIHAHGLSYNKTNegalYPDSSEKVEKADdsVAPGKSFTYVWTLPASHTpgkdetn 176
Cdd:cd13851     32 PPIEVNKGDTVVIHATNSlGDQPTSLHFHGLFQNGTN----YMDGPVGVTQCP--IPPGQSFTYEFTVDTQVG------- 98

                           90       100
                   ....*....|....*....|....*.
gi 2559057711  177 clTRIYHSHVNApkDIASGLIGPLII 202
Cdd:cd13851     99 --TYWYHSHDGG--QYPDGLRGPFII 120
CuRO_1_McoC_like cd13855
The first cupredoxin domain of a multicopper oxidase McoC and similar proteins; This family ...
 97-202 2.54e-06

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: 47.47  E-value: 2.54e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2559057711   97 GPLISAEEDDVVIVHLKNTARRAYSIHAHGLsynktnegalyPDSSEKVEKADDSVAPGKSFTYVWTLPashtpgkdETN 176
Cdd:cd13855     32 GPLIEVFEGDTVEITFRNRLPEPTTVHWHGL-----------PVPPDQDGNPHDPVAPGNDRVYRFTLP--------QDS 92

                           90       100
                   ....*....|....*....|....*...
gi 2559057711  177 CLTRIYHSHVN--APKDIASGLIGPLII 202
Cdd:cd13855     93 AGTYWYHPHPHghTAEQVYRGLAGAFVV 120
CuRO_1_MaLCC_like cd13854
The first cupredoxin domain of the fungal laccases similar to Ma-LCC from Melanocarpus ...
 95-202 2.61e-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: 47.62  E-value: 2.61e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2559057711   95 YLGPLISAEEDDVVIVHLKNTARR-AYSIHAHGLS--YNKTNEGAlyPDSSEKvekaddSVAPGKSFTYVWTLpashtpg 171
Cdd:cd13854     31 YPGPLIEANWGDTIEVTVINKLQDnGTSIHWHGIRqlNTNWQDGV--PGVTEC------PIAPGDTRTYRFRA------- 95

                           90       100       110
                   ....*....|....*....|....*....|.
gi 2559057711  172 kdeTNCLTRIYHSHVNApkDIASGLIGPLII 202
Cdd:cd13854     96 ---TQYGTSWYHSHYSA--QYGDGVVGPIVI 121
CuRO_1_Tth-MCO_like cd13853
The first cupredoxin domain of the bacterial laccases similar to Tth-MCO from Thermus ...
 95-202 2.85e-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: 48.02  E-value: 2.85e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2559057711   95 YLGPLISAEEDDVVIVHLKN---------------TARRAYS--IHAHGLSYNktnegalyPDSSekvekADD---SVAP 154
Cdd:cd13853     29 IPGPTLRVRPGDTLRITLKNdlppegaaneapapnTPHCPNTtnLHFHGLHVS--------PTGN-----SDNvflTIAP 95

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|..
gi 2559057711  155 GKSFTYVWTLPASHTPGkdetnclTRIYHSH----VNApkDIASGLIGPLII 202
Cdd:cd13853     96 GESFTYEYDIPADHPPG-------TYWYHPHlhgsTAL--QVAGGMAGALVV 138
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 3.16e-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: 3.16e-06
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 2559057711  822 GPMIHGKVGEKVKIVFKNMAKRPYSIHAHGVKTDSPQV------ALTRPGETKTYTW 872
Cdd:cd14449     29 GPVIEVREGDTLKILFRNTLDVPASLHPHGVDYTTASDgtgmnaSIVAPGDTRIYTW 85
Cu-oxidase pfam00394
Multicopper oxidase; Many of the proteins in this family contain multiple similar copies of ...
 220-353 4.09e-06

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: 47.70  E-value: 4.09e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2559057711  220 YTLMFTvsdenlSWYlEENIKTYCTAPAKVNKDDEGFQESNKMHSINGYVYGNLPDLSMCMGNKIHWHLFgMGNEVDLHS 299
Cdd:pfam00394    3 YVITLS------DWY-HKDAKDLEKELLASGKAPTDFPPVPDAVLINGKDGASLATLTVTPGKTYRLRII-NVALDDSLN 74

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2559057711  300 AFFHGQILT----DKRHH----VDTVSLFPATFVHVEMVADN-PGQWLLSCQVN-DHMEAGMQA 353
Cdd:pfam00394   75 FSIEGHKMTvvevDGVYVnpftVDSLDIFPGQRYSVLVTANQdPGNYWIVASPNiPAFDNGTAA 138
CuRO_3_MCO_like_3 cd13909
The third cupredoxin domain of uncharacterized multicopper oxidase; Multicopper Oxidases (MCOs) ...
 1008-1071 5.00e-06

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: 47.13  E-value: 5.00e-06
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2559057711 1008 HTAHFHGHSF-----DYKIGGTHraDVFDLFPGTFQTITMRPLYSGTWLLHCHVTDHIQAGMETTYTVL 1071
Cdd:cd13909     71 HGMHLHGHHFrailpNGALGPWR--DTLLMDRGETREIAFVADNPGDWLLHCHMLEHAAAGMMSWFRVT 137
CuRO_1_CumA_like cd13861
The first cupredoxin domain of CumA like multicopper oxidase; This multicopper oxidase (MCO) ...
 819-912 6.73e-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: 46.46  E-value: 6.73e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2559057711  819 GIMGPMIHGKVGEKVKIVFKNMAKRPYSIHAHGVKTDS-----PQV--ALTRPGETKTYT---------WYLPKNsGPTE 882
Cdd:cd13861     28 QVPGPELRVRQGDTLRVRLTNRLPEPTTIHWHGLRLPNamdgvPGLtqPPVPPGESFTYEftppdagtyWYHPHV-GSQE 106

                           90       100       110
                   ....*....|....*....|....*....|
gi 2559057711  883 QQEEcsvgayystvdvikdmysGLIGPLVI 912
Cdd:cd13861    107 QLDR------------------GLYGPLIV 118
SufI COG2132
Multicopper oxidase with three cupredoxin domains (includes cell division protein FtsP and ...
 262-359 6.84e-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: 49.93  E-value: 6.84e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2559057711  262 MHSINGYVYG-NLPDLSMCMGNKIHWHLFGMGNE---VDLHSAFFhgQIL------TDKRHHVDTVSLFPATFVHVEMVA 331
Cdd:COG2132    317 VWTINGKAFDpDRPDLTVKLGERERWTLVNDTMMphpFHLHGHQF--QVLsrngkpPPEGGWKDTVLVPPGETVRILFRF 394

                           90       100
                   ....*....|....*....|....*....
gi 2559057711  332 DN-PGQWLLSCQVNDHMEAGMQAIFEIKK 359
Cdd:COG2132    395 DNyPGDWMFHCHILEHEDAGMMGQFEVVP 423
CuRO_1_AAO cd13845
The first cupredoxin domain of plant Ascorbate oxidase; Ascorbate oxidase catalyzes the ...
 94-202 8.58e-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: 8.58e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2559057711   94 GYLGPLISAEEDDVVIVHLKNT-ARRAYSIHAHGLSynktNEGALYPDSSEKVEKAddSVAPGKSFTYVWTLpasHTPGk 172
Cdd:cd13845     27 QFPGPTIRATAGDTIVVELENKlPTEGVAIHWHGIR----QRGTPWADGTASVSQC--PINPGETFTYQFVV---DRPG- 96

                           90       100       110
                   ....*....|....*....|....*....|
gi 2559057711  173 detnclTRIYHSHVNAPKdiASGLIGPLII 202
Cdd:cd13845     97 ------TYFYHGHYGMQR--SAGLYGSLIV 118
CuRO_3_CopA cd13896
The third cupredoxin domain of CopA copper resistance protein family; CopA is a multicopper ...
 974-1070 9.83e-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: 45.71  E-value: 9.83e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2559057711  974 GINGLVYGNLKGLNMKVGDKVywyLMGMGNEVDI-HTAHFHGHSFDY-KIGGTHRA--DVFDLFPGTFQTITMRPLYSGT 1049
Cdd:cd13896     18 TINGKAYPDADPLRVREGERV---RIVFVNDTMMaHPMHLHGHFFQVeNGNGEYGPrkDTVLVPPGETVSVDFDADNPGR 94

                           90       100
                   ....*....|....*....|.
gi 2559057711 1050 WLLHCHVTDHIQAGMETTYTV 1070
Cdd:cd13896     95 WAFHCHNLYHMEAGMMRVVEY 115
CuRO_1_2DMCO_NIR_like cd11024
The cupredoxin domain 1 of a two-domain laccase related to nitrite reductase; The two-domain ...
 822-872 1.32e-05

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: 45.34  E-value: 1.32e-05
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....
gi 2559057711  822 GPMIHGKVGEKVKIVFKNMAKRPYSIHAHGV---KTDSPQVALTRPGETKTYTW 872
Cdd:cd11024     32 GPTLRATEGDLVRIHFINTGDHPHTIHFHGIhdaAMDGTGLGPIMPGESFTYEF 85
CuRO_1_McoC_like cd13855
The first cupredoxin domain of a multicopper oxidase McoC and similar proteins; This family ...
 822-912 1.51e-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: 45.54  E-value: 1.51e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2559057711  822 GPMIHGKVGEKVKIVFKNMAKRPYSIHAHGVKTDSPQ-------VAltrPGETKTYTWYLPKNSGpteqqeecsvGAYY- 893
Cdd:cd13855     32 GPLIEVFEGDTVEITFRNRLPEPTTVHWHGLPVPPDQdgnphdpVA---PGNDRVYRFTLPQDSA----------GTYWy 98

                           90       100
                   ....*....|....*....|..
gi 2559057711  894 ---STVDVIKDMYSGLIGPLVI 912
Cdd:cd13855     99 hphPHGHTAEQVYRGLAGAFVV 120
CuRO_1_CuNIR cd11020
Cupredoxin domain 1 of Copper-containing nitrite reductase; Copper-containing nitrite ...
 820-872 1.82e-05

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


Pssm-ID: 259906 [Multi-domain]  Cd Length: 119  Bit Score: 44.89  E-value: 1.82e-05
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 2559057711  820 IMGPMIHGKVGEKVKIVFKNM--AKRPYSIHAHGVKTD-SPQVALTRPGETKTYTW 872
Cdd:cd11020     30 VPGPVIRVREGDTVELTLTNPgtNTMPHSIDFHAATGPgGGEFTTIAPGETKTFSF 85
CuRO_3_Tv-LCC_like cd13903
The third cupredoxin domain of the fungal laccases similar to Tv-LCC from Trametes Versicolor; ...
 1002-1064 2.02e-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: 45.73  E-value: 2.02e-05
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2559057711 1002 GNEVDIHTAHFHGHSFDY-KIGGTH--------RADVFDL-FPGTFQTITMRPLYSGTWLLHCHVTDHIQAGM 1064
Cdd:cd13903     67 GAIGGPHPFHLHGHAFSVvRSAGSNtynyvnpvRRDVVSVgTPGDGVTIRFVTDNPGPWFLHCHIDWHLEAGL 139
CuRO_3_McoC_like cd13902
The third cupredoxin domain of a multicopper oxidase McoC and similar proteins; This family ...
 972-1064 3.00e-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: 44.70  E-value: 3.00e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2559057711  972 MHGINGLVYG-NLKGLNMKVGDKVYWYLMgmgNEVDI-HTAHFHGHSFDY--KIGGTHRA------DVFDLFPGTFQTIT 1041
Cdd:cd13902     20 MFLINGKTFDmNRIDFVAKVGEVEVWEVT---NTSHMdHPFHLHGTQFQVleIDGNPQKPeyrawkDTVNLPPGEAVRIA 96

                           90       100
                   ....*....|....*....|...
gi 2559057711 1042 MRPLYSGTWLLHCHVTDHIQAGM 1064
Cdd:cd13902     97 TRQDDPGMWMYHCHILEHEDAGM 119
SufI COG2132
Multicopper oxidase with three cupredoxin domains (includes cell division protein FtsP and ...
 822-912 3.83e-05

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: 47.24  E-value: 3.83e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2559057711  822 GPMIHGKVGEKVKIVFKNMAKRPYSIHAHGVKTDSPQ----VALTRPGETKTYT----------WYLPKNSGPTEQQeec 887
Cdd:COG2132     44 GPTIRVREGDRVRVRVTNRLPEPTTVHWHGLRVPNAMdgvpGDPIAPGETFTYEfpvpqpagtyWYHPHTHGSTAEQ--- 120

                           90       100
                   ....*....|....*....|....*
gi 2559057711  888 svgayystvdvikdMYSGLIGPLVI 912
Cdd:COG2132    121 --------------VYRGLAGALIV 131
CuRO_3_Tv-LCC_like cd13903
The third cupredoxin domain of the fungal laccases similar to Tv-LCC from Trametes Versicolor; ...
 315-355 4.29e-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: 44.58  E-value: 4.29e-05
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|..
gi 2559057711  315 DTVSL-FPATFVHVEMVADNPGQWLLSCQVNDHMEAGMQAIF 355
Cdd:cd13903    102 DVVSVgTPGDGVTIRFVTDNPGPWFLHCHIDWHLEAGLAVVF 143
ascorbase TIGR03388
L-ascorbate oxidase, plant type; Members of this protein family are the copper-containing ...
 97-202 4.66e-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: 47.44  E-value: 4.66e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2559057711   97 GPLISAEEDDVVIVHLKNT-ARRAYSIHAHGLSYNktneGALYPDSSEKVEKAddSVAPGKSFTYVWTLpasHTPGkdet 175
Cdd:TIGR03388   31 GPTIRAQAGDTIVVELTNKlHTEGVVIHWHGIRQI----GTPWADGTAGVTQC--AINPGETFIYNFVV---DRPG---- 97

                           90       100
                   ....*....|....*....|....*..
gi 2559057711  176 nclTRIYHSHVNAPKdiASGLIGPLII 202
Cdd:TIGR03388   98 ---TYFYHGHYGMQR--SAGLYGSLIV 119
CuRO_3_Fet3p cd13899
The third Cupredoxin domain of multicopper oxidase Fet3p; Fet3p catalyzes the ferroxidase ...
 1008-1072 6.37e-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: 44.55  E-value: 6.37e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2559057711 1008 HTAHFHGHSF--------------DYKIGGTH----RADVFDLFPGTFQTITMRPLYSGTWLLHCHVTDHIQAGMetTYT 1069
Cdd:cd13899     78 HPFHLHGHKFqvvqrspdvasddpNPPINEFPenpmRRDTVMVPPGGSVVIRFRADNPGVWFFHCHIEWHLEAGL--AAT 155


                   ...
gi 2559057711 1070 VLE 1072
Cdd:cd13899    156 FIE 158
CuRO_3_McoC_like cd13902
The third cupredoxin domain of a multicopper oxidase McoC and similar proteins; This family ...
 262-357 6.48e-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: 43.54  E-value: 6.48e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2559057711  262 MHSINGYVYG-NLPDLSMCMGNKIHWHLFG---MGNEVDLHSAFFhgQILTDKRHHV--------DTVSLFPATFVHVEM 329
Cdd:cd13902     20 MFLINGKTFDmNRIDFVAKVGEVEVWEVTNtshMDHPFHLHGTQF--QVLEIDGNPQkpeyrawkDTVNLPPGEAVRIAT 97

                           90       100
                   ....*....|....*....|....*...
gi 2559057711  330 VADNPGQWLLSCQVNDHMEAGMQAIFEI 357
Cdd:cd13902     98 RQDDPGMWMYHCHILEHEDAGMMGMLHV 125
CuRO_3_MCO_like_3 cd13909
The third cupredoxin domain of uncharacterized multicopper oxidase; Multicopper Oxidases (MCOs) ...
 315-357 6.56e-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: 44.05  E-value: 6.56e-05
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|...
gi 2559057711  315 DTVSLFPATFVHVEMVADNPGQWLLSCQVNDHMEAGMQAIFEI 357
Cdd:cd13909     94 DTLLMDRGETREIAFVADNPGDWLLHCHMLEHAAAGMMSWFRV 136
PLN02191 PLN02191
L-ascorbate oxidase
 97-202 7.54e-05

L-ascorbate oxidase


Pssm-ID: 177843 [Multi-domain]  Cd Length: 574  Bit Score: 46.55  E-value: 7.54e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2559057711   97 GPLISAEEDDVVIVHLKNT-ARRAYSIHAHGLSynktNEGALYPDSSEKVEKAddSVAPGKSFTYVWTLpasHTPGkdet 175
Cdd:PLN02191    53 GPTIDAVAGDTIVVHLTNKlTTEGLVIHWHGIR----QKGSPWADGAAGVTQC--AINPGETFTYKFTV---EKPG---- 119

                           90       100
                   ....*....|....*....|....*..
gi 2559057711  176 nclTRIYHSHVNAPKdiASGLIGPLII 202
Cdd:PLN02191   120 ---THFYHGHYGMQR--SAGLYGSLIV 141
CuRO_3_AAO cd13893
The third cupredoxin domain of plant Ascorbate oxidase; Ascorbate oxidase catalyzes the ...
 315-356 7.56e-05

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: 44.33  E-value: 7.56e-05
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|..
gi 2559057711  315 DTVSLFPATFVHVEMVADNPGQWLLSCQVNDHMEAGMQAIFE 356
Cdd:cd13893    104 NTVTIFPYGWTALRFKADNPGVWAFHCHIEWHFHMGMGVVFA 145
CuRO_D1_2dMcoN_like cd13859
The first cupredoxin domain of bacterial two domain multicopper oxidase McoN and similar ...
 820-872 7.64e-05

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: 43.24  E-value: 7.64e-05
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2559057711  820 IMGPMIHGKVGEKVKIVFKNMAKRPYSIHAHGV-KTDS------PQVA--LTRPGETKTYTW 872
Cdd:cd13859     29 VPGPLIHVKEGDDLVVHVTNNTTLPHTIHWHGVlQMGSwkmdgvPGVTqpAIEPGESFTYKF 90
CuRO_3_MCO_like_4 cd13910
The third cupredoxin domain of uncharacterized multicopper oxidase; Multicopper Oxidases (MCOs) ...
 315-351 2.75e-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: 259977 [Multi-domain]  Cd Length: 166  Bit Score: 42.67  E-value: 2.75e-04
                           10        20        30
                   ....*....|....*....|....*....|....*..
gi 2559057711  315 DTVSLFPATFVHVEMVADNPGQWLLSCQVNDHMEAGM 351
Cdd:cd13910    124 DTVSVPGFGWAVLRFVADNPGLWAFHCHILWHMAAGM 160
Cu-oxidase_3 pfam07732
Multicopper oxidase; This entry contains many divergent copper oxidase-like domains that are ...
 423-573 2.79e-04

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: 41.46  E-value: 2.79e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2559057711  423 KVQYVEYADDTFTKRKERTPEEQhlgILGPIIRAEEEDTIKVTFRNKASRPYSIQPHGVQY--SIEMDGTLYhnvleesy 500
Cdd:pfam07732    1 TVTYGTVSPLGGTRQAVIGVNGQ---FPGPTIRVREGDTVVVNVTNNLDEPTSIHWHGLQQrgTPWMDGVPG-------- 69

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2559057711  501 takklrelkkearvvepLPAALVRPDTTYQYEWVVPKDGGptekdpdciTYMYYSAVDPIRdtNSGLVGPLLI 573
Cdd:pfam07732   70 -----------------VTQCPIPPGQSFTYRFQVKQQAG---------TYWYHSHTSGQQ--AAGLAGAIII 114
CuRO_3_MaLCC_like cd13901
The third cupredoxin domain of the fungal laccases similar to Ma-LCC from Melanocarpus ...
 1008-1064 2.93e-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: 2.93e-04
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2559057711 1008 HTAHFHGHSF--------DYKIGGT-------HRADVFDLFPGTFQTITMR---PlysGTWLLHCHVTDHIQAGM 1064
Cdd:cd13901     81 HPIHLHGHDFyilaqgtgTFDDDGTilnlnnpPRRDVAMLPAGGYLVIAFKtdnP---GAWLMHCHIAWHASGGL 152
CuRO_3_MCO_like_2 cd13908
The third cupredoxin domain of uncharacterized multicopper oxidase; Multicopper Oxidases (MCOs) ...
 315-356 3.58e-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: 259975 [Multi-domain]  Cd Length: 122  Bit Score: 41.28  E-value: 3.58e-04
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|..
gi 2559057711  315 DTVSLFPATFVHVEMVADNPGQWLLSCQVNDHMEAGMQAIFE 356
Cdd:cd13908     80 DVVMLGGYQRVEVDFVADNPGLTLFHCHQQLHMDYGFMALFK 121
CuRO_1_2dMco_1 cd13860
The first cupredoxin domain of bacteria two domain multicopper oxidase; This subfamily ...
 822-912 4.30e-04

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: 41.03  E-value: 4.30e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2559057711  822 GPMIHGKVGEKVKIVFKNMAKRPYSIHAHGVK-----------TDSPqvalTRPGETKTYTWYLpKNSGPTeqqeecsvg 890
Cdd:cd13860     31 GPTIEVTEGDRVRILVTNELPEPTTVHWHGLPvpngmdgvpgiTQPP----IQPGETFTYEFTA-KQAGTY--------- 96

                           90       100
                   ....*....|....*....|..
gi 2559057711  891 AYYSTVDVIKDMYSGLIGPLVI 912
Cdd:cd13860     97 MYHSHVDEAKQEDMGLYGAFIV 118
CuRO_3_tcLLC2_insect_like cd13905
The third cupredoxin domain of the insect laccases similar to laccase 2 in Tribolium castaneum; ...
 315-367 4.45e-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: 42.28  E-value: 4.45e-04
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....
gi 2559057711  315 DTVSLfPAT-FVHVEMVADNPGQWLLSCQVNDHMEAGMQAIFeiKKCFPNVHKP 367
Cdd:cd13905    123 DTVVV-PNGgYVVIRFRADNPGYWLLHCHIEFHLLEGMALVL--KVGEPSDPPP 173
PLN02191 PLN02191
L-ascorbate oxidase
 315-355 4.54e-04

L-ascorbate oxidase


Pssm-ID: 177843 [Multi-domain]  Cd Length: 574  Bit Score: 44.23  E-value: 4.54e-04
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|.
gi 2559057711  315 DTVSLFPATFVHVEMVADNPGQWLLSCQVNDHMEAGMQAIF 355
Cdd:PLN02191   504 NTAILYPYGWTAIRFVTDNPGVWFFHCHIEPHLHMGMGVVF 544
PLN02604 PLN02604
oxidoreductase
 97-202 5.57e-04

oxidoreductase


Pssm-ID: 215324 [Multi-domain]  Cd Length: 566  Bit Score: 44.08  E-value: 5.57e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2559057711   97 GPLISAEEDDVVIVHLKNT-ARRAYSIHAHGLSynktNEGALYPDSSEKVEKAddSVAPGKSFTYVWTLpasHTPGkdet 175
Cdd:PLN02604    54 GPTILAQQGDTVIVELKNSlLTENVAIHWHGIR----QIGTPWFDGTEGVTQC--PILPGETFTYEFVV---DRPG---- 120

                           90       100
                   ....*....|....*....|....*..
gi 2559057711  176 nclTRIYHSHVNAPKdiASGLIGPLII 202
Cdd:PLN02604   121 ---TYLYHAHYGMQR--EAGLYGSIRV 142
CuRO_1_MCO_like_1 cd13862
The first cupredoxin domain of uncharacterized multicopper oxidase; Multicopper Oxidases (MCOs) ...
 97-202 9.31e-04

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: 40.19  E-value: 9.31e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2559057711   97 GPLISAEEDDVVIVHLKNTARRAYSIHAHGLSYNKTNEGALypdssekvEKADDSVAPGKSFTYVWT-LPAShtpgkdet 175
Cdd:cd13862     31 GPLLRMRQGVSVTVDVFNDTDIPEYVHWHGLPLPADVDGAM--------EEGTPSVPPHGHRRYRMTpRPAG-------- 94

                           90       100       110
                   ....*....|....*....|....*....|.
gi 2559057711  176 nclTRIYHSHVNAPKDIA----SGLIGPLII 202
Cdd:cd13862     95 ---FRWYHTHVMTMDDLTrgqySGLFGFVYI 122
ascorbase TIGR03388
L-ascorbate oxidase, plant type; Members of this protein family are the copper-containing ...
 315-356 1.07e-03

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: 42.82  E-value: 1.07e-03
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|..
gi 2559057711  315 DTVSLFPATFVHVEMVADNPGQWLLSCQVNDHMEAGMQAIFE 356
Cdd:TIGR03388  481 NTVVIFPYGWTALRFVADNPGVWAFHCHIEPHLHMGMGVVFA 522
CuRO_1_CuNIR_like cd04201
Cupredoxin domain 1 of Copper-containing nitrite reductase and two-domain laccase; ...
 97-202 2.61e-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: 39.01  E-value: 2.61e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2559057711   97 GPLISAEEDDVVIVHLKNTARRA--YSIHAHGlSYNKTNEGALypdssekvekadDSVAPGKSFTYVW--TLPASHtpgk 172
Cdd:cd04201     32 GPMLRVREGDTVELHFSNNPSSTmpHNIDFHA-ATGAGGGAGA------------TFIAPGETSTFSFkaTQPGLY---- 94

                           90       100       110
                   ....*....|....*....|....*....|.
gi 2559057711  173 detncltrIYHSHVNA-PKDIASGLIGPLII 202
Cdd:cd04201     95 --------VYHCAVAPvPMHIANGMYGLILV 117
CuRO_1_McoP_like cd13852
The first cupredoxin domain of multicopper oxidase McoP and similar proteins; This family ...
 450-500 4.81e-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: 38.04  E-value: 4.81e-03
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|..
gi 2559057711  450 LGPIIRAEEEDTIKVTFRNKASRPYSIQPHGVQYSIEMDGTLYHNVLE-ESY 500
Cdd:cd13852     23 LGPILRLRKGQKVRITFKNNLPEPTIIHWHGLHVPAAMDGHPRYAIDPgETY 74
CuRO_1_Diphenol_Ox cd13857
The first cupredoxin domain of fungal laccase, diphenol oxidase; Diphenol oxidase belongs to ...
 451-490 5.52e-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: 38.01  E-value: 5.52e-03
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|..
gi 2559057711  451 GPIIRAEEEDTIKVTFRNKASRPYSIQPHGV-QY-SIEMDGT 490
Cdd:cd13857     30 GPLIEANQGDRIVVHVTNELDEPTSIHWHGLfQNgTNWMDGT 71
CuRO_1_CuNIR_like cd04201
Cupredoxin domain 1 of Copper-containing nitrite reductase and two-domain laccase; ...
 976-1073 7.75e-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: 37.47  E-value: 7.75e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2559057711  976 NGLVYGNLkgLNMKVGDKVYWYLMGMGNEVDIHTAHFHG-HSFDYKIGGTHRAdvfdlfPGTFQTITMRPLYSGTWLLHC 1054
Cdd:cd04201     27 DGDIPGPM--LRVREGDTVELHFSNNPSSTMPHNIDFHAaTGAGGGAGATFIA------PGETSTFSFKATQPGLYVYHC 98

                           90       100
                   ....*....|....*....|..
gi 2559057711 1055 HVTD---HIQAGMETTYTVLEK 1073
Cdd:cd04201     99 AVAPvpmHIANGMYGLILVEPK 120
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

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