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Conserved domains on  [gi|1758362338|ref|NP_001361606|]
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ceruloplasmin isoform d precursor [Mus musculus]

Protein Classification

multicopper oxidase; multicopper oxidase domain-containing protein( domain architecture ID 10362974)

multicopper oxidase (MCO) that couples the oxidation of a substrate with a four-electron reduction of molecular oxygen to water, and which may contain three cupredoxin domains that include one mononuclear and one trinuclear copper center| multicopper oxidase domain-containing protein that may contain type I Cu center(s) and be involved in inter-molecular electron transfer; contains a cupredoxin domain similar to the first cupredoxin domain of bacterial laccases similar to a hyperthermophilic multicopper oxidase (MCO) from thermus thermophilus HB27; may be a partial protein

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
CuRO_3_ceruloplasmin cd04224
The third cupredoxin domain of Ceruloplasmin; Ceruloplasmin is a multicopper oxidase essential ...
 369-566 5.17e-115

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: 352.93  E-value: 5.17e-115
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1758362338  369 HVRHYYIAAEEVIWNYAPSGTDIFTGENLTALESDSRVFFEQGATRIGGSYKKMAYREYTDGSFTNRKQRGPDEEHLGIL 448
Cdd:cd04224      2 KVRHYFIAAEEIMWDYAPSGKNLFTGQNLTAPGSDSEVFFQRNETRIGGTYWKVRYVEYTDATFTTRKHRSKEEEHLGIL 81

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1758362338  449 GPVIWAEVGDTIKVTFHNKGQHPLSIQPMGVSFTAENEGTYYGPPgrSSQQASHVAPKETFTYEWTVPKEMGPTYADPVC 528
Cdd:cd04224     82 GPVIRAEVGDTIKVTFRNKASRPFSIQPHGVFYEKNYEGAMYRDG--DPSPGSHVSPGETFTYEWTVPEGVGPTNQDPPC 159

                          170       180       190
                   ....*....|....*....|....*....|....*...
gi 1758362338  529 LSKMYYSGVDPTKDIFTGLIGPMKICKKGSLLADGRQK 566
Cdd:cd04224    160 LTYLYFSAVDPVRDTNSGLVGPLLVCKKGSLNANGRQK 197
CuRO_5_ceruloplasmin cd04225
The fifth cupredoxin domain of Ceruloplasmin; Ceruloplasmin is a multicopper oxidase essential ...
 726-896 1.85e-104

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: 324.04  E-value: 1.85e-104
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1758362338  726 RTYYVAAVEVEWDYSPSRAWEKELHHLQEQNVSNVFLDKEEFFIGSKYKKVVYRQFTDSSFREQVKRRAEDEHLGILGPP 805
Cdd:cd04225      1 RTYYIAAEEVEWDYSPQRTWEQELHNTHEESPGNAFLNKGDKFIGSKYKKVVYREYTDDTFSVPKERTAEEEHLGILGPL 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1758362338  806 IHANVGDKVKVVFKNMATRPYSIHAHGVKTESSTVVPTLPGEVRTYTWQIPERSGAGREDSACIPWAYYSTVDRVKDLYS 885
Cdd:cd04225     81 IHAEVGEKVKIVFKNMASRPYSIHAHGVKTDSSWVAPTEPGETQTYTWKIPERSGPGVEDSNCISWAYYSTVDQIKDLYS 160

                          170
                   ....*....|.
gi 1758362338  886 GLIGPLIVCRK 896
Cdd:cd04225    161 GLIGPLVICRR 171
Cupredoxin super family cl19115
Cupredoxin superfamily; Cupredoxins contain type I copper centers and are involved in ...
 22-201 8.87e-99

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


The actual alignment was detected with superfamily member cd04222:

Pssm-ID: 473140 [Multi-domain]  Cd Length: 183  Bit Score: 309.35  E-value: 8.87e-99
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1758362338   22 KHYFIGITEAVWDYASGTEE--KKLISVDTEQSNFYLQNGPDRIGRKYKKALYFEYTDGTFSKTIDKPAWLGFLGPVIKA 99
Cdd:cd04222      1 REYYIGIRETQWDYAPSGKNliTNQTFDDDEHASVFLKRGPDRIGRVYKKAVYLQYTDDTYRTEIEKPVWLGFLGPILKA 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1758362338  100 EVEDKVYVHLKNLASRIYTFHAHGVTYTKEYEGAVYPDNTTDFQRADDKVLPGQQYVYVLHANEP-SPGEGDSNCVTRIY 178
Cdd:cd04222     81 EVGDVIVVHLKNFASRPYSLHPHGVFYNKENEGALYPDNTSGFEKADDAVPPGGSYTYTWTVPEEqAPTKADANCLTRIY 160

                          170       180
                   ....*....|....*....|...
gi 1758362338  179 HSHVDAPKDIASGLIGPLILCKK 201
Cdd:cd04222    161 HSHIDAPKDIASGLIGPLIICKK 183
Cupredoxin super family cl19115
Cupredoxin superfamily; Cupredoxins contain type I copper centers and are involved in ...
 907-1051 6.05e-92

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: 289.46  E-value: 6.05e-92
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1758362338  907 KMEFFLLFLVFDENESWYLDDNIKTYSEHPEKVNKDNEEFLESNKMHAINGKMFGNLQGLTMHVKDEVNWYVMGMGNEID 986
Cdd:cd11012      1 KLEFALLFLVFDENESWYLDENIKTYSDHPEKVNKEDEEFIESNKMHAINGKVFGNLQGLTMHVGDEVYWYLMGMGNEID 80

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1758362338  987 LHTVHFHGHSFQYKHRGVYSSDVFDLFPGTYQTLEMFPQTPGTWLLHCHVTDHVHAGMATTYTVL 1051
Cdd:cd11012     81 IHTAHFHGHSFDYKHRGVYRSDVFDLFPGTFQTVEMIPRTPGTWLLHCHVTDHIHAGMETTYTVL 145
CuRO_2_ceruloplasmin cd11021
The second cupredoxin domain of Ceruloplasmin; Ceruloplasmin is a multicopper oxidase ...
 213-353 2.83e-91

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: 287.44  E-value: 2.83e-91
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1758362338  213 DQEFVLMFSVVDENLSWYLEDNIKTFCSEPEKVDKDNEDFQESNRMYSINGYTFGSLPGLSMCAADRVKWYLFGMGNEVD 292
Cdd:cd11021      1 DREFVLMFSVVDENLSWYLDENIKTYCSEPAKVDKDDEDFQESNKMHSINGYTFGNLPGLSMCAGDRVKWHLFGMGNEVD 80

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1758362338  293 VHSAFFHGQALTSRNYQTDIINLFPATLIDAYMVAQNPGVWMLSCQNLNHLKAGLQAFFQV 353
Cdd:cd11021     81 IHSAFFHGQTLTDRGHRTDTINLFPATFVTAEMVAQNPGKWLLSCQVNDHLKAGMQAFYEV 141
CuRO_4_ceruloplasmin cd11022
The fourth cupredoxin domain of Ceruloplasmin; Ceruloplasmin is a multicopper oxidase ...
 569-712 1.52e-88

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: 280.52  E-value: 1.52e-88
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1758362338  569 DKEFYLFPTVFDENESLLLDDNIRMFTTAPDQVDKEDEDFQESNKMHSMNGFMYGNQPGLNMCLGESIVWYLFSAGNEAD 648
Cdd:cd11022      1 DKEFFLLFTVFDENESWYLDENIQQFTLDPRSVDKEDEDFQESNKMHSINGYMYGNQPGLDMCKGDTVSWHLFGLGTETD 80

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1758362338  649 VHGIYFSGNTYLSKGERRDTANLFPHKSLTLLMNPDTKGTFDVECLTTDHYTGGMKQKYTVNQC 712
Cdd:cd11022     81 VHGIYFSGNTFLLQGTRRDTANLFPHTSVTAIMQPDNEGTFEVNCQTTDHYSAGMRQIYTVSQC 144
 
Name Accession Description Interval E-value
CuRO_3_ceruloplasmin cd04224
The third cupredoxin domain of Ceruloplasmin; Ceruloplasmin is a multicopper oxidase essential ...
 369-566 5.17e-115

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: 352.93  E-value: 5.17e-115
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1758362338  369 HVRHYYIAAEEVIWNYAPSGTDIFTGENLTALESDSRVFFEQGATRIGGSYKKMAYREYTDGSFTNRKQRGPDEEHLGIL 448
Cdd:cd04224      2 KVRHYFIAAEEIMWDYAPSGKNLFTGQNLTAPGSDSEVFFQRNETRIGGTYWKVRYVEYTDATFTTRKHRSKEEEHLGIL 81

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1758362338  449 GPVIWAEVGDTIKVTFHNKGQHPLSIQPMGVSFTAENEGTYYGPPgrSSQQASHVAPKETFTYEWTVPKEMGPTYADPVC 528
Cdd:cd04224     82 GPVIRAEVGDTIKVTFRNKASRPFSIQPHGVFYEKNYEGAMYRDG--DPSPGSHVSPGETFTYEWTVPEGVGPTNQDPPC 159

                          170       180       190
                   ....*....|....*....|....*....|....*...
gi 1758362338  529 LSKMYYSGVDPTKDIFTGLIGPMKICKKGSLLADGRQK 566
Cdd:cd04224    160 LTYLYFSAVDPVRDTNSGLVGPLLVCKKGSLNANGRQK 197
CuRO_5_ceruloplasmin cd04225
The fifth cupredoxin domain of Ceruloplasmin; Ceruloplasmin is a multicopper oxidase essential ...
 726-896 1.85e-104

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: 324.04  E-value: 1.85e-104
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1758362338  726 RTYYVAAVEVEWDYSPSRAWEKELHHLQEQNVSNVFLDKEEFFIGSKYKKVVYRQFTDSSFREQVKRRAEDEHLGILGPP 805
Cdd:cd04225      1 RTYYIAAEEVEWDYSPQRTWEQELHNTHEESPGNAFLNKGDKFIGSKYKKVVYREYTDDTFSVPKERTAEEEHLGILGPL 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1758362338  806 IHANVGDKVKVVFKNMATRPYSIHAHGVKTESSTVVPTLPGEVRTYTWQIPERSGAGREDSACIPWAYYSTVDRVKDLYS 885
Cdd:cd04225     81 IHAEVGEKVKIVFKNMASRPYSIHAHGVKTDSSWVAPTEPGETQTYTWKIPERSGPGVEDSNCISWAYYSTVDQIKDLYS 160

                          170
                   ....*....|.
gi 1758362338  886 GLIGPLIVCRK 896
Cdd:cd04225    161 GLIGPLVICRR 171
CuRO_1_ceruloplasmin cd04222
The first cupredoxin domain of Ceruloplasmin; Ceruloplasmin is a multicopper oxidase essential ...
 22-201 8.87e-99

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: 309.35  E-value: 8.87e-99
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1758362338   22 KHYFIGITEAVWDYASGTEE--KKLISVDTEQSNFYLQNGPDRIGRKYKKALYFEYTDGTFSKTIDKPAWLGFLGPVIKA 99
Cdd:cd04222      1 REYYIGIRETQWDYAPSGKNliTNQTFDDDEHASVFLKRGPDRIGRVYKKAVYLQYTDDTYRTEIEKPVWLGFLGPILKA 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1758362338  100 EVEDKVYVHLKNLASRIYTFHAHGVTYTKEYEGAVYPDNTTDFQRADDKVLPGQQYVYVLHANEP-SPGEGDSNCVTRIY 178
Cdd:cd04222     81 EVGDVIVVHLKNFASRPYSLHPHGVFYNKENEGALYPDNTSGFEKADDAVPPGGSYTYTWTVPEEqAPTKADANCLTRIY 160

                          170       180
                   ....*....|....*....|...
gi 1758362338  179 HSHVDAPKDIASGLIGPLILCKK 201
Cdd:cd04222    161 HSHIDAPKDIASGLIGPLIICKK 183
CuRO_6_ceruloplasmin cd11012
The sixth cupredoxin domain of Ceruloplasmin; Ceruloplasmin is a multicopper oxidase essential ...
 907-1051 6.05e-92

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: 289.46  E-value: 6.05e-92
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1758362338  907 KMEFFLLFLVFDENESWYLDDNIKTYSEHPEKVNKDNEEFLESNKMHAINGKMFGNLQGLTMHVKDEVNWYVMGMGNEID 986
Cdd:cd11012      1 KLEFALLFLVFDENESWYLDENIKTYSDHPEKVNKEDEEFIESNKMHAINGKVFGNLQGLTMHVGDEVYWYLMGMGNEID 80

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1758362338  987 LHTVHFHGHSFQYKHRGVYSSDVFDLFPGTYQTLEMFPQTPGTWLLHCHVTDHVHAGMATTYTVL 1051
Cdd:cd11012     81 IHTAHFHGHSFDYKHRGVYRSDVFDLFPGTFQTVEMIPRTPGTWLLHCHVTDHIHAGMETTYTVL 145
CuRO_2_ceruloplasmin cd11021
The second cupredoxin domain of Ceruloplasmin; Ceruloplasmin is a multicopper oxidase ...
 213-353 2.83e-91

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: 287.44  E-value: 2.83e-91
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1758362338  213 DQEFVLMFSVVDENLSWYLEDNIKTFCSEPEKVDKDNEDFQESNRMYSINGYTFGSLPGLSMCAADRVKWYLFGMGNEVD 292
Cdd:cd11021      1 DREFVLMFSVVDENLSWYLDENIKTYCSEPAKVDKDDEDFQESNKMHSINGYTFGNLPGLSMCAGDRVKWHLFGMGNEVD 80

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1758362338  293 VHSAFFHGQALTSRNYQTDIINLFPATLIDAYMVAQNPGVWMLSCQNLNHLKAGLQAFFQV 353
Cdd:cd11021     81 IHSAFFHGQTLTDRGHRTDTINLFPATFVTAEMVAQNPGKWLLSCQVNDHLKAGMQAFYEV 141
CuRO_4_ceruloplasmin cd11022
The fourth cupredoxin domain of Ceruloplasmin; Ceruloplasmin is a multicopper oxidase ...
 569-712 1.52e-88

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: 280.52  E-value: 1.52e-88
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1758362338  569 DKEFYLFPTVFDENESLLLDDNIRMFTTAPDQVDKEDEDFQESNKMHSMNGFMYGNQPGLNMCLGESIVWYLFSAGNEAD 648
Cdd:cd11022      1 DKEFFLLFTVFDENESWYLDENIQQFTLDPRSVDKEDEDFQESNKMHSINGYMYGNQPGLDMCKGDTVSWHLFGLGTETD 80

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1758362338  649 VHGIYFSGNTYLSKGERRDTANLFPHKSLTLLMNPDTKGTFDVECLTTDHYTGGMKQKYTVNQC 712
Cdd:cd11022     81 VHGIYFSGNTFLLQGTRRDTANLFPHTSVTAIMQPDNEGTFEVNCQTTDHYSAGMRQIYTVSQC 144
Cu-oxidase_2 pfam07731
Multicopper oxidase; This entry contains many divergent copper oxidase-like domains that are ...
 950-1052 2.35e-17

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: 79.79  E-value: 2.35e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1758362338  950 NKMHAINGKMFG-NLQGLTMHVKDEVNWYVMGMGNeiDLHTVHFHGHSFQYKHRGVYSS----------------DVFDL 1012
Cdd:pfam07731   19 RNDWAINGLLFPpNTNVITLPYGTVVEWVLQNTTT--GVHPFHLHGHSFQVLGRGGGPWpeedpktynlvdpvrrDTVQV 96

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|
gi 1758362338 1013 FPGTYQTLEMFPQTPGTWLLHCHVTDHVHAGMATTYTVLP 1052
Cdd:pfam07731   97 PPGGWVAIRFRADNPGVWLFHCHILWHLDQGMMGQFVVRP 136
Cu-oxidase pfam00394
Multicopper oxidase; Many of the proteins in this family contain multiple similar copies of ...
 220-357 1.69e-15

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: 74.66  E-value: 1.69e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1758362338  220 FSVVDENLSWYlEDNIKTFCSEPEKVDKDNEDFQESNRMYSINGYTFGSLPGLSMCAADRVKWYLFgMGNEVDVHSAFFH 299
Cdd:pfam00394    1 EDYVITLSDWY-HKDAKDLEKELLASGKAPTDFPPVPDAVLINGKDGASLATLTVTPGKTYRLRII-NVALDDSLNFSIE 78

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1758362338  300 GQALT--------SRNYQTDIINLFPATLIDAYMVA-QNPGVWMLSCQNLN-HLKAGLQAFFQVRDCN 357
Cdd:pfam00394   79 GHKMTvvevdgvyVNPFTVDSLDIFPGQRYSVLVTAnQDPGNYWIVASPNIpAFDNGTAAAILRYSGA 146
SufI COG2132
Multicopper oxidase with three cupredoxin domains (includes cell division protein FtsP and ...
 952-1052 4.04e-11

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: 66.50  E-value: 4.04e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1758362338  952 MHAINGKMFGnlqgltMHVKDEV----NWYVMGMGNEID-LHTVHFHGHSFQYKHR---GVYSS---DVFDLFPGTYQTL 1020
Cdd:COG2132    317 VWTINGKAFD------PDRPDLTvklgERERWTLVNDTMmPHPFHLHGHQFQVLSRngkPPPEGgwkDTVLVPPGETVRI 390

                           90       100       110
                   ....*....|....*....|....*....|...
gi 1758362338 1021 EM-FPQTPGTWLLHCHVTDHVHAGMATTYTVLP 1052
Cdd:COG2132    391 LFrFDNYPGDWMFHCHILEHEDAGMMGQFEVVP 423
Cu-oxidase_3 pfam07732
Multicopper oxidase; This entry contains many divergent copper oxidase-like domains that are ...
 801-860 7.09e-06

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: 46.08  E-value: 7.09e-06
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1758362338  801 ILGPPIHANVGDKVKVVFKNMATRPYSIHAHGV---KTESSTVV------PTLPGEVRTYTWQIPERSG 860
Cdd:pfam07732   24 FPGPTIRVREGDTVVVNVTNNLDEPTSIHWHGLqqrGTPWMDGVpgvtqcPIPPGQSFTYRFQVKQQAG 92
SufI COG2132
Multicopper oxidase with three cupredoxin domains (includes cell division protein FtsP and ...
 92-221 1.51e-04

Multicopper oxidase with three cupredoxin domains (includes cell division protein FtsP and spore coat protein CotA) [Cell cycle control, cell division, chromosome partitioning, Inorganic ion transport and metabolism, Cell wall/membrane/envelope biogenesis;


Pssm-ID: 441735 [Multi-domain]  Cd Length: 423  Bit Score: 45.31  E-value: 1.51e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1758362338   92 FLGPVIKAEVEDKVYVHLKN-LASRIyTFHAHGVTYTKEYEGAVYPdnttdfqraddKVLPGQQYVYVLHANEPsPGegd 170
Cdd:COG2132     42 YPGPTIRVREGDRVRVRVTNrLPEPT-TVHWHGLRVPNAMDGVPGD-----------PIAPGETFTYEFPVPQP-AG--- 105

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 1758362338  171 sncvTRIYHSHVDA--PKDIASGLIGPLILckkgslyKEKEKNI---DQEFVLMFS 221
Cdd:COG2132    106 ----TYWYHPHTHGstAEQVYRGLAGALIV-------EDPEEDLpryDRDIPLVLQ 150
PLN02191 PLN02191
L-ascorbate oxidase
 986-1048 1.71e-04

L-ascorbate oxidase


Pssm-ID: 177843 [Multi-domain]  Cd Length: 574  Bit Score: 45.39  E-value: 1.71e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1758362338  986 DLHTVHFHGHSF------QYKHRGVYSSDVFDL-----------FPGTYQTLEMFPQTPGTWLLHCHVTDHVHAGMATTY 1048
Cdd:PLN02191   465 EIHPWHLHGHDFwvlgygDGKFKPGIDEKTYNLknpplrntailYPYGWTAIRFVTDNPGVWFFHCHIEPHLHMGMGVVF 544
Cu-oxidase_3 pfam07732
Multicopper oxidase; This entry contains many divergent copper oxidase-like domains that are ...
 447-523 3.56e-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: 3.56e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1758362338  447 ILGPVIWAEVGDTIKVTFHNKGQHPLSI------QPmgvsftaeNEGTYYGPPGrSSQQAshVAPKETFTYEWTVPKEMG 520
Cdd:pfam07732   24 FPGPTIRVREGDTVVVNVTNNLDEPTSIhwhglqQR--------GTPWMDGVPG-VTQCP--IPPGQSFTYRFQVKQQAG 92


                   ...
gi 1758362338  521 pTY 523
Cdd:pfam07732   93 -TY 94
ascorbase TIGR03388
L-ascorbate oxidase, plant type; Members of this protein family are the copper-containing ...
 982-1044 2.83e-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: 41.66  E-value: 2.83e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1758362338  982 GNEIDLHTVHFHGHSF------QYKHRGVYSSDVFDL-----------FPGTYQTLEMFPQTPGTWLLHCHVTDHVHAGM 1044
Cdd:TIGR03388  438 GNNSETHPWHLHGHDFwvlgygEGKFRPGVDEKSYNLknpplrntvviFPYGWTALRFVADNPGVWAFHCHIEPHLHMGM 517
 
Name Accession Description Interval E-value
CuRO_3_ceruloplasmin cd04224
The third cupredoxin domain of Ceruloplasmin; Ceruloplasmin is a multicopper oxidase essential ...
 369-566 5.17e-115

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: 352.93  E-value: 5.17e-115
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1758362338  369 HVRHYYIAAEEVIWNYAPSGTDIFTGENLTALESDSRVFFEQGATRIGGSYKKMAYREYTDGSFTNRKQRGPDEEHLGIL 448
Cdd:cd04224      2 KVRHYFIAAEEIMWDYAPSGKNLFTGQNLTAPGSDSEVFFQRNETRIGGTYWKVRYVEYTDATFTTRKHRSKEEEHLGIL 81

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1758362338  449 GPVIWAEVGDTIKVTFHNKGQHPLSIQPMGVSFTAENEGTYYGPPgrSSQQASHVAPKETFTYEWTVPKEMGPTYADPVC 528
Cdd:cd04224     82 GPVIRAEVGDTIKVTFRNKASRPFSIQPHGVFYEKNYEGAMYRDG--DPSPGSHVSPGETFTYEWTVPEGVGPTNQDPPC 159

                          170       180       190
                   ....*....|....*....|....*....|....*...
gi 1758362338  529 LSKMYYSGVDPTKDIFTGLIGPMKICKKGSLLADGRQK 566
Cdd:cd04224    160 LTYLYFSAVDPVRDTNSGLVGPLLVCKKGSLNANGRQK 197
CuRO_5_ceruloplasmin cd04225
The fifth cupredoxin domain of Ceruloplasmin; Ceruloplasmin is a multicopper oxidase essential ...
 726-896 1.85e-104

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: 324.04  E-value: 1.85e-104
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1758362338  726 RTYYVAAVEVEWDYSPSRAWEKELHHLQEQNVSNVFLDKEEFFIGSKYKKVVYRQFTDSSFREQVKRRAEDEHLGILGPP 805
Cdd:cd04225      1 RTYYIAAEEVEWDYSPQRTWEQELHNTHEESPGNAFLNKGDKFIGSKYKKVVYREYTDDTFSVPKERTAEEEHLGILGPL 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1758362338  806 IHANVGDKVKVVFKNMATRPYSIHAHGVKTESSTVVPTLPGEVRTYTWQIPERSGAGREDSACIPWAYYSTVDRVKDLYS 885
Cdd:cd04225     81 IHAEVGEKVKIVFKNMASRPYSIHAHGVKTDSSWVAPTEPGETQTYTWKIPERSGPGVEDSNCISWAYYSTVDQIKDLYS 160

                          170
                   ....*....|.
gi 1758362338  886 GLIGPLIVCRK 896
Cdd:cd04225    161 GLIGPLVICRR 171
CuRO_1_ceruloplasmin cd04222
The first cupredoxin domain of Ceruloplasmin; Ceruloplasmin is a multicopper oxidase essential ...
 22-201 8.87e-99

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: 309.35  E-value: 8.87e-99
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1758362338   22 KHYFIGITEAVWDYASGTEE--KKLISVDTEQSNFYLQNGPDRIGRKYKKALYFEYTDGTFSKTIDKPAWLGFLGPVIKA 99
Cdd:cd04222      1 REYYIGIRETQWDYAPSGKNliTNQTFDDDEHASVFLKRGPDRIGRVYKKAVYLQYTDDTYRTEIEKPVWLGFLGPILKA 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1758362338  100 EVEDKVYVHLKNLASRIYTFHAHGVTYTKEYEGAVYPDNTTDFQRADDKVLPGQQYVYVLHANEP-SPGEGDSNCVTRIY 178
Cdd:cd04222     81 EVGDVIVVHLKNFASRPYSLHPHGVFYNKENEGALYPDNTSGFEKADDAVPPGGSYTYTWTVPEEqAPTKADANCLTRIY 160

                          170       180
                   ....*....|....*....|...
gi 1758362338  179 HSHVDAPKDIASGLIGPLILCKK 201
Cdd:cd04222    161 HSHIDAPKDIASGLIGPLIICKK 183
CuRO_6_ceruloplasmin cd11012
The sixth cupredoxin domain of Ceruloplasmin; Ceruloplasmin is a multicopper oxidase essential ...
 907-1051 6.05e-92

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: 289.46  E-value: 6.05e-92
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1758362338  907 KMEFFLLFLVFDENESWYLDDNIKTYSEHPEKVNKDNEEFLESNKMHAINGKMFGNLQGLTMHVKDEVNWYVMGMGNEID 986
Cdd:cd11012      1 KLEFALLFLVFDENESWYLDENIKTYSDHPEKVNKEDEEFIESNKMHAINGKVFGNLQGLTMHVGDEVYWYLMGMGNEID 80

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1758362338  987 LHTVHFHGHSFQYKHRGVYSSDVFDLFPGTYQTLEMFPQTPGTWLLHCHVTDHVHAGMATTYTVL 1051
Cdd:cd11012     81 IHTAHFHGHSFDYKHRGVYRSDVFDLFPGTFQTVEMIPRTPGTWLLHCHVTDHIHAGMETTYTVL 145
CuRO_2_ceruloplasmin cd11021
The second cupredoxin domain of Ceruloplasmin; Ceruloplasmin is a multicopper oxidase ...
 213-353 2.83e-91

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: 287.44  E-value: 2.83e-91
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1758362338  213 DQEFVLMFSVVDENLSWYLEDNIKTFCSEPEKVDKDNEDFQESNRMYSINGYTFGSLPGLSMCAADRVKWYLFGMGNEVD 292
Cdd:cd11021      1 DREFVLMFSVVDENLSWYLDENIKTYCSEPAKVDKDDEDFQESNKMHSINGYTFGNLPGLSMCAGDRVKWHLFGMGNEVD 80

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1758362338  293 VHSAFFHGQALTSRNYQTDIINLFPATLIDAYMVAQNPGVWMLSCQNLNHLKAGLQAFFQV 353
Cdd:cd11021     81 IHSAFFHGQTLTDRGHRTDTINLFPATFVTAEMVAQNPGKWLLSCQVNDHLKAGMQAFYEV 141
CuRO_4_ceruloplasmin cd11022
The fourth cupredoxin domain of Ceruloplasmin; Ceruloplasmin is a multicopper oxidase ...
 569-712 1.52e-88

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: 280.52  E-value: 1.52e-88
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1758362338  569 DKEFYLFPTVFDENESLLLDDNIRMFTTAPDQVDKEDEDFQESNKMHSMNGFMYGNQPGLNMCLGESIVWYLFSAGNEAD 648
Cdd:cd11022      1 DKEFFLLFTVFDENESWYLDENIQQFTLDPRSVDKEDEDFQESNKMHSINGYMYGNQPGLDMCKGDTVSWHLFGLGTETD 80

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1758362338  649 VHGIYFSGNTYLSKGERRDTANLFPHKSLTLLMNPDTKGTFDVECLTTDHYTGGMKQKYTVNQC 712
Cdd:cd11022     81 VHGIYFSGNTFLLQGTRRDTANLFPHTSVTAIMQPDNEGTFEVNCQTTDHYSAGMRQIYTVSQC 144
CuRO_1_ceruloplasmin_like cd04199
Cupredoxin domains 1, 3, and 5 of ceruloplasmin and similar proteins; This family includes the ...
 371-556 2.68e-80

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: 259.26  E-value: 2.68e-80
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1758362338  371 RHYYIAAEEVIWNYAPSGTDIFTGENLTalesdsrVFFEQGATRIGGSYKKMAYREYTDGSFTnrkQRGPDEEHLGILGP 450
Cdd:cd04199      1 RHYYIAAEEIDWDYAPSGLAEKDLSYRN-------QYLDNGPFRIGRSYKKVVYREYTDESFT---TPGPQPEHLGILGP 70

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1758362338  451 VIWAEVGDTIKVTFHNKGQHPLSIQPMGVSFTAENEGTYYGPPGRSSQ-QASHVAPKETFTYEWTVPKEMGPTYADPVCL 529
Cdd:cd04199     71 TIRAEVGDTIKVHFKNKASRPYSIHPHGVSYEKDSEGASYSDQTGPDEkKDDAVAPGETYTYVWIVTEESGPTKGDPACL 150

                          170       180
                   ....*....|....*....|....*..
gi 1758362338  530 SKMYYSGVDPTKDIFTGLIGPMKICKK 556
Cdd:cd04199    151 TWAYYSHVDLEKDINSGLIGPLLICKK 177
CuRO_1_ceruloplasmin_like cd04199
Cupredoxin domains 1, 3, and 5 of ceruloplasmin and similar proteins; This family includes the ...
 22-201 3.94e-80

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: 258.87  E-value: 3.94e-80
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1758362338   22 KHYFIGITEAVWDYASGTEEKKLISVDteqsNFYLQNGPDRIGRKYKKALYFEYTDGTFSKTIDKPAWLGFLGPVIKAEV 101
Cdd:cd04199      1 RHYYIAAEEIDWDYAPSGLAEKDLSYR----NQYLDNGPFRIGRSYKKVVYREYTDESFTTPGPQPEHLGILGPTIRAEV 76

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1758362338  102 EDKVYVHLKNLASRIYTFHAHGVTYTKEYEGAVYPDNTTDFQRADDKVLPGQQYVYVLHANEPS-PGEGDSNCVTRIYHS 180
Cdd:cd04199     77 GDTIKVHFKNKASRPYSIHPHGVSYEKDSEGASYSDQTGPDEKKDDAVAPGETYTYVWIVTEESgPTKGDPACLTWAYYS 156

                          170       180
                   ....*....|....*....|.
gi 1758362338  181 HVDAPKDIASGLIGPLILCKK 201
Cdd:cd04199    157 HVDLEKDINSGLIGPLLICKK 177
CuRO_1_ceruloplasmin_like cd04199
Cupredoxin domains 1, 3, and 5 of ceruloplasmin and similar proteins; This family includes the ...
 726-896 3.94e-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: 245.01  E-value: 3.94e-75
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1758362338  726 RTYYVAAVEVEWDYSPSRAWEKELHHLqeqnvsNVFLDKEEFFIGSKYKKVVYRQFTDSSFReqvKRRAEDEHLGILGPP 805
Cdd:cd04199      1 RHYYIAAEEIDWDYAPSGLAEKDLSYR------NQYLDNGPFRIGRSYKKVVYREYTDESFT---TPGPQPEHLGILGPT 71

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1758362338  806 IHANVGDKVKVVFKNMATRPYSIHAHGVKTESS---------------TVVPTLPGEVRTYTWQIPERSGAGREDSACIP 870
Cdd:cd04199     72 IRAEVGDTIKVHFKNKASRPYSIHPHGVSYEKDsegasysdqtgpdekKDDAVAPGETYTYVWIVTEESGPTKGDPACLT 151

                          170       180
                   ....*....|....*....|....*.
gi 1758362338  871 WAYYSTVDRVKDLYSGLIGPLIVCRK 896
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 ...
 213-353 7.50e-71

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: 231.92  E-value: 7.50e-71
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1758362338  213 DQEFVLMFSVVDENLSWYLEDNIKTFCSEPEKVDKDNEDFQESNRMYSINGYTFGSLPGLSMCAADRVKWYLFGMGNEVD 292
Cdd:cd04200      1 DKEFVLLFAVFDENKSWYLEDNIKRFCDNPEKVDKDDEEFQESNKMHAINGYVFGNLPGLTMCAGDRVRWHLLGMGNEVD 80

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1758362338  293 VHSAFFHGQALTSRNYQTDIINLFPATLIDAYMVAQNPGVWMLSCQNLNHLKAGLQAFFQV 353
Cdd:cd04200     81 VHSIHFHGQTFLYKGYRIDTLTLFPATFETVEMVPSNPGTWLLHCHNSDHRHAGMQAYFLV 141
CuRO_2_ceruloplasmin_like cd04200
Cupredoxin domains 2, 4, and 6 of ceruloplasmin and similar proteins; This family includes the ...
 909-1050 1.79e-70

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: 230.76  E-value: 1.79e-70
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1758362338  909 EFFLLFLVFDENESWYLDDNIKTYSEHPEKVNKDNEEFLESNKMHAINGKMFGNLQGLTMHVKDEVNWYVMGMGNEIDLH 988
Cdd:cd04200      3 EFVLLFAVFDENKSWYLEDNIKRFCDNPEKVDKDDEEFQESNKMHAINGYVFGNLPGLTMCAGDRVRWHLLGMGNEVDVH 82

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1758362338  989 TVHFHGHSFQYKHrgvYSSDVFDLFPGTYQTLEMFPQTPGTWLLHCHVTDHVHAGMATTYTV 1050
Cdd:cd04200     83 SIHFHGQTFLYKG---YRIDTLTLFPATFETVEMVPSNPGTWLLHCHNSDHRHAGMQAYFLV 141
CuRO_2_ceruloplasmin_like cd04200
Cupredoxin domains 2, 4, and 6 of ceruloplasmin and similar proteins; This family includes the ...
 569-709 6.39e-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: 206.88  E-value: 6.39e-62
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1758362338  569 DKEFYLFPTVFDENESLLLDDNIRMFTTAPDQVDKEDEDFQESNKMHSMNGFMYGNQPGLNMCLGESIVWYLFSAGNEAD 648
Cdd:cd04200      1 DKEFVLLFAVFDENKSWYLEDNIKRFCDNPEKVDKDDEEFQESNKMHAINGYVFGNLPGLTMCAGDRVRWHLLGMGNEVD 80

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1758362338  649 VHGIYFSGNTYLSKGERRDTANLFPHKSLTLLMNPDTKGTFDVECLTTDHYTGGMKQKYTV 709
Cdd:cd04200     81 VHSIHFHGQTFLYKGYRIDTLTLFPATFETVEMVPSNPGTWLLHCHNSDHRHAGMQAYFLV 141
CuRO_3_ceruloplasmin cd04224
The third cupredoxin domain of Ceruloplasmin; Ceruloplasmin is a multicopper oxidase essential ...
 725-896 4.66e-59

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: 201.16  E-value: 4.66e-59
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1758362338  725 ERTYYVAAVEVEWDYSPSrawekELHHLQEQNV------SNVFLDKEEFFIGSKYKKVVYRQFTDSSFREQVKRRAEDEH 798
Cdd:cd04224      3 VRHYFIAAEEIMWDYAPS-----GKNLFTGQNLtapgsdSEVFFQRNETRIGGTYWKVRYVEYTDATFTTRKHRSKEEEH 77

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1758362338  799 LGILGPPIHANVGDKVKVVFKNMATRPYSIHAHGVKTES------------STVVPTLPGEVRTYTWQIPERSGAGREDS 866
Cdd:cd04224     78 LGILGPVIRAEVGDTIKVTFRNKASRPFSIQPHGVFYEKnyegamyrdgdpSPGSHVSPGETFTYEWTVPEGVGPTNQDP 157

                          170       180       190
                   ....*....|....*....|....*....|
gi 1758362338  867 ACIPWAYYSTVDRVKDLYSGLIGPLIVCRK 896
Cdd:cd04224    158 PCLTYLYFSAVDPVRDTNSGLVGPLLVCKK 187
CuRO_2_ceruloplasmin cd11021
The second cupredoxin domain of Ceruloplasmin; Ceruloplasmin is a multicopper oxidase ...
 909-1050 4.58e-57

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: 193.07  E-value: 4.58e-57
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1758362338  909 EFFLLFLVFDENESWYLDDNIKTYSEHPEKVNKDNEEFLESNKMHAINGKMFGNLQGLTMHVKDEVNWYVMGMGNEIDLH 988
Cdd:cd11021      3 EFVLMFSVVDENLSWYLDENIKTYCSEPAKVDKDDEDFQESNKMHSINGYTFGNLPGLSMCAGDRVKWHLFGMGNEVDIH 82

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1758362338  989 TVHFHGHSFQYKHrgvYSSDVFDLFPGTYQTLEMFPQTPGTWLLHCHVTDHVHAGMATTYTV 1050
Cdd:cd11021     83 SAFFHGQTLTDRG---HRTDTINLFPATFVTAEMVAQNPGKWLLSCQVNDHLKAGMQAFYEV 141
CuRO_1_ceruloplasmin cd04222
The first cupredoxin domain of Ceruloplasmin; Ceruloplasmin is a multicopper oxidase essential ...
 371-556 2.56e-55

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


Pssm-ID: 259884 [Multi-domain]  Cd Length: 183  Bit Score: 189.94  E-value: 2.56e-55
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1758362338  371 RHYYIAAEEVIWNYAPSGTDIFTGENLTALEsDSRVFFEQGATRIGGSYKKMAYREYTDGSFTnrkQRGPDEEHLGILGP 450
Cdd:cd04222      1 REYYIGIRETQWDYAPSGKNLITNQTFDDDE-HASVFLKRGPDRIGRVYKKAVYLQYTDDTYR---TEIEKPVWLGFLGP 76

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1758362338  451 VIWAEVGDTIKVTFHNKGQHPLSIQPMGVSFTAENEGTYYgPPGRSSQQASH--VAPKETFTYEWTVPKEMGPTYADPVC 528
Cdd:cd04222     77 ILKAEVGDVIVVHLKNFASRPYSLHPHGVFYNKENEGALY-PDNTSGFEKADdaVPPGGSYTYTWTVPEEQAPTKADANC 155

                          170       180
                   ....*....|....*....|....*...
gi 1758362338  529 LSKMYYSGVDPTKDIFTGLIGPMKICKK 556
Cdd:cd04222    156 LTRIYHSHIDAPKDIASGLIGPLIICKK 183
CuRO_2_ceruloplasmin cd11021
The second cupredoxin domain of Ceruloplasmin; Ceruloplasmin is a multicopper oxidase ...
 569-709 9.94e-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: 183.83  E-value: 9.94e-54
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1758362338  569 DKEFYLFPTVFDENESLLLDDNIRMFTTAPDQVDKEDEDFQESNKMHSMNGFMYGNQPGLNMCLGESIVWYLFSAGNEAD 648
Cdd:cd11021      1 DREFVLMFSVVDENLSWYLDENIKTYCSEPAKVDKDDEDFQESNKMHSINGYTFGNLPGLSMCAGDRVKWHLFGMGNEVD 80

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1758362338  649 VHGIYFSGNTYLSKGERRDTANLFPHKSLTLLMNPDTKGTFDVECLTTDHYTGGMKQKYTV 709
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 ...
 373-555 2.46e-53

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


Pssm-ID: 259992 [Multi-domain]  Cd Length: 181  Bit Score: 184.31  E-value: 2.46e-53
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1758362338  373 YYIAAEEVIWNYAPSGTDiftgenltALESDSRV-FFEQGATRIGGSYKKMAYREYTDGSFTNRKQrGPDEEHLGILGPV 451
Cdd:cd14450      5 YFIAAEEVIWDYAPSIPE--------NMDKRYRSqYLDNFSNNIGKKYKKAVFTQYEDGSFTKRLE-NPRPKEEGILGPV 75

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1758362338  452 IWAEVGDTIKVTFHNKGQHPLSIQPMGVSFTAENEGTYYGP-PGRSSQQASHVAPKETFTYEWTVPKEMGPTYADPVCLS 530
Cdd:cd14450     76 IRAQVRDTIKIVFKNKASRPYSIYPHGVTVSKAAEGASYPPdPRGNETQNKAVQPGETYTYKWNILETDEPTARDPRCLT 155

                          170       180
                   ....*....|....*....|....*
gi 1758362338  531 KMYYSGVDPTKDIFTGLIGPMKICK 555
Cdd:cd14450    156 RMYHSAVDITRDIASGLIGPLLICK 180
CuRO_3_FV_like cd14450
The third cupredoxin domain of coagulation factor V and similar proteins; Factor V is an ...
 24-200 2.51e-53

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


Pssm-ID: 259992 [Multi-domain]  Cd Length: 181  Bit Score: 184.31  E-value: 2.51e-53
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1758362338   24 YFIGITEAVWDYASGTEEkkliSVDTEQSNFYLQNGPDRIGRKYKKALYFEYTDGTFSKTID--KPAWLGFLGPVIKAEV 101
Cdd:cd14450      5 YFIAAEEVIWDYAPSIPE----NMDKRYRSQYLDNFSNNIGKKYKKAVFTQYEDGSFTKRLEnpRPKEEGILGPVIRAQV 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1758362338  102 EDKVYVHLKNLASRIYTFHAHGVTYTKEYEGAVYPDNTTDFQRADDKVLPGQQYVY---VLHANEPSpgEGDSNCVTRIY 178
Cdd:cd14450     81 RDTIKIVFKNKASRPYSIYPHGVTVSKAAEGASYPPDPRGNETQNKAVQPGETYTYkwnILETDEPT--ARDPRCLTRMY 158

                          170       180
                   ....*....|....*....|..
gi 1758362338  179 HSHVDAPKDIASGLIGPLILCK 200
Cdd:cd14450    159 HSAVDITRDIASGLIGPLLICK 180
CuRO_4_ceruloplasmin cd11022
The fourth cupredoxin domain of Ceruloplasmin; Ceruloplasmin is a multicopper oxidase ...
 909-1050 2.71e-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: 182.68  E-value: 2.71e-53
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1758362338  909 EFFLLFLVFDENESWYLDDNIKTYSEHPEKVNKDNEEFLESNKMHAINGKMFGNLQGLTMHVKDEVNWYVMGMGNEIDLH 988
Cdd:cd11022      3 EFFLLFTVFDENESWYLDENIQQFTLDPRSVDKEDEDFQESNKMHSINGYMYGNQPGLDMCKGDTVSWHLFGLGTETDVH 82

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1758362338  989 TVHFHGHSFQYK--HRgvyssDVFDLFPGTYQTLEMFPQTPGTWLLHCHVTDHVHAGMATTYTV 1050
Cdd:cd11022     83 GIYFSGNTFLLQgtRR-----DTANLFPHTSVTAIMQPDNEGTFEVNCQTTDHYSAGMRQIYTV 141
CuRO_4_ceruloplasmin cd11022
The fourth cupredoxin domain of Ceruloplasmin; Ceruloplasmin is a multicopper oxidase ...
 213-356 2.31e-52

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: 179.99  E-value: 2.31e-52
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1758362338  213 DQEFVLMFSVVDENLSWYLEDNIKTFCSEPEKVDKDNEDFQESNRMYSINGYTFGSLPGLSMCAADRVKWYLFGMGNEVD 292
Cdd:cd11022      1 DKEFFLLFTVFDENESWYLDENIQQFTLDPRSVDKEDEDFQESNKMHSINGYMYGNQPGLDMCKGDTVSWHLFGLGTETD 80

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1758362338  293 VHSAFFHGQALTSRNYQTDIINLFPATLIDAYMVAQNPGVWMLSCQNLNHLKAGLQAFFQVRDC 356
Cdd:cd11022     81 VHGIYFSGNTFLLQGTRRDTANLFPHTSVTAIMQPDNEGTFEVNCQTTDHYSAGMRQIYTVSQC 144
CuRO_1_Ceruloplasmin_like_1 cd04229
cupredoxin domain of ceruloplasmin homologs; Uncharacterized subfamily of ceruloplasmin ...
 371-557 7.65e-52

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: 179.92  E-value: 7.65e-52
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1758362338  371 RHYYIAAEEVIWNYAPSGtdiFTGENLTALESDSRVFFEQGATRIGGSYKKMAYREYTDGSFTNRKqrgPDEEHLGILGP 450
Cdd:cd04229      1 RTYYIAAEEVDWDYAPSG---KNKCCLGDDLEVSTLDSQPGPYTIGSTYTKARYREYTDNSFSTPK---PTPAYLGILGP 74

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1758362338  451 VIWAEVGDTIKVTFHNK-GQHPLSIQPMGVSFTAENEGTYYGPPGRssqqashVAPKETFTYEWTVPKEMGPTYADPVCL 529
Cdd:cd04229     75 VIRAEVGDTIKVVFKNNlDEFPVNMHPHGGLYSKDNEGTTDGAGDV-------VAPGETYTYRWIVPEDAGPGPGDPSSR 147

                          170       180
                   ....*....|....*....|....*...
gi 1758362338  530 SKMYYSGVDPTKDIFTGLIGPMKICKKG 557
Cdd:cd04229    148 LWLYHSHVDVFAHTNAGLVGPIIVTSKG 175
CuRO_1_Ceruloplasmin_like_1 cd04229
cupredoxin domain of ceruloplasmin homologs; Uncharacterized subfamily of ceruloplasmin ...
 726-896 2.92e-51

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: 177.99  E-value: 2.92e-51
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1758362338  726 RTYYVAAVEVEWDYSPSRAweKELHHLQEQNVSNVFLDKEEFFIGSKYKKVVYRQFTDSSFREQVkrrAEDEHLGILGPP 805
Cdd:cd04229      1 RTYYIAAEEVDWDYAPSGK--NKCCLGDDLEVSTLDSQPGPYTIGSTYTKARYREYTDNSFSTPK---PTPAYLGILGPV 75

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1758362338  806 IHANVGDKVKVVFKN-MATRPYSIHAHGV-------KTESSTVVPTLPGEVRTYTWQIPERSGAGREDSACIPWAYYSTV 877
Cdd:cd04229     76 IRAEVGDTIKVVFKNnLDEFPVNMHPHGGlyskdneGTTDGAGDVVAPGETYTYRWIVPEDAGPGPGDPSSRLWLYHSHV 155

                          170
                   ....*....|....*....
gi 1758362338  878 DRVKDLYSGLIGPLIVCRK 896
Cdd:cd04229    156 DVFAHTNAGLVGPIIVTSK 174
CuRO_5_ceruloplasmin cd04225
The fifth cupredoxin domain of Ceruloplasmin; Ceruloplasmin is a multicopper oxidase essential ...
 371-556 3.14e-51

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: 177.66  E-value: 3.14e-51
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1758362338  371 RHYYIAAEEVIWNYAPSGTDIFTGENLTAlESDSRVFFEQGATRIGGSYKKMAYREYTDGSFTNRKQRGPDEEHLGILGP 450
Cdd:cd04225      1 RTYYIAAEEVEWDYSPQRTWEQELHNTHE-ESPGNAFLNKGDKFIGSKYKKVVYREYTDDTFSVPKERTAEEEHLGILGP 79

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1758362338  451 VIWAEVGDTIKVTFHNKGQHPLSIQPMGVSftaenegtyygppgRSSQQASHVAPKETFTYEWTVPKEMGPTYADPVCLS 530
Cdd:cd04225     80 LIHAEVGEKVKIVFKNMASRPYSIHAHGVK--------------TDSSWVAPTEPGETQTYTWKIPERSGPGVEDSNCIS 145

                          170       180
                   ....*....|....*....|....*.
gi 1758362338  531 KMYYSGVDPTKDIFTGLIGPMKICKK 556
Cdd:cd04225    146 WAYYSTVDQIKDLYSGLIGPLVICRR 171
CuRO_3_ceruloplasmin cd04224
The third cupredoxin domain of Ceruloplasmin; Ceruloplasmin is a multicopper oxidase essential ...
 20-204 4.26e-49

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: 172.66  E-value: 4.26e-49
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1758362338   20 RDKHYFIGITEAVWDYA----SGTEEKKLISVDTEQSNFYLQNGpDRIGRKYKKALYFEYTDGTFskTIDKP-----AWL 90
Cdd:cd04224      2 KVRHYFIAAEEIMWDYApsgkNLFTGQNLTAPGSDSEVFFQRNE-TRIGGTYWKVRYVEYTDATF--TTRKHrskeeEHL 78

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1758362338   91 GFLGPVIKAEVEDKVYVHLKNLASRIYTFHAHGVTYTKEYEGAVYPDnttDFQRADDKVLPGQQYVYVLHANE-PSPGEG 169
Cdd:cd04224     79 GILGPVIRAEVGDTIKVTFRNKASRPFSIQPHGVFYEKNYEGAMYRD---GDPSPGSHVSPGETFTYEWTVPEgVGPTNQ 155

                          170       180       190
                   ....*....|....*....|....*....|....*
gi 1758362338  170 DSNCVTRIYHSHVDAPKDIASGLIGPLILCKKGSL 204
Cdd:cd04224    156 DPPCLTYLYFSAVDPVRDTNSGLVGPLLVCKKGSL 190
CuRO_1_ceruloplasmin cd04222
The first cupredoxin domain of Ceruloplasmin; Ceruloplasmin is a multicopper oxidase essential ...
 726-896 5.41e-49

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: 171.83  E-value: 5.41e-49
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1758362338  726 RTYYVAAVEVEWDYSPSRAWEKELHHLQEQNVSNVFLDKEEFFIGSKYKKVVYRQFTDSSFREQVKRRAedeHLGILGPP 805
Cdd:cd04222      1 REYYIGIRETQWDYAPSGKNLITNQTFDDDEHASVFLKRGPDRIGRVYKKAVYLQYTDDTYRTEIEKPV---WLGFLGPI 77

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1758362338  806 IHANVGDKVKVVFKNMATRPYSIHAHGV---KTESSTVVP------------TLPGEVRTYTWQIPERSGAGREDSACIP 870
Cdd:cd04222     78 LKAEVGDVIVVHLKNFASRPYSLHPHGVfynKENEGALYPdntsgfekaddaVPPGGSYTYTWTVPEEQAPTKADANCLT 157

                          170       180
                   ....*....|....*....|....*.
gi 1758362338  871 WAYYSTVDRVKDLYSGLIGPLIVCRK 896
Cdd:cd04222    158 RIYHSHIDAPKDIASGLIGPLIICKK 183
CuRO_5_FVIII_like cd04228
The fifth cupredoxin domain of coagulation factor VIII and similar proteins; Factor VIII ...
 726-896 8.74e-48

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: 167.76  E-value: 8.74e-48
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1758362338  726 RTYYVAAVEVEWDYSPSRAWekelHHLQEQNVSNvflDKEEFFigSKYKKVVYRQFTDSSFREQVKRRAEDEHLGILGPP 805
Cdd:cd04228      2 RHYFIAAVEVLWDYGMQRPQ----HFLRARDPNR---GRRKSV--PQYKKVVFREYLDGSFTQPVYRGELDEHLGILGPY 72

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1758362338  806 IHANVGDKVKVVFKNMATRPYSIHAHGVKTESSTVV-----PTLPGEVRTYTWQIPERSGAGREDSACIPWAYYSTVDRV 880
Cdd:cd04228     73 IRAEVEDNIMVTFKNLASRPYSFHSSLISYEEDQRAeprgnFVQPGEVQTYSWKVLHQMAPTKQEFDCKAWAYFSNVDLE 152

                          170
                   ....*....|....*.
gi 1758362338  881 KDLYSGLIGPLIVCRK 896
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 ...
 725-896 2.52e-47

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: 166.94  E-value: 2.52e-47
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1758362338  725 ERTYYVAAVEVEWDYSPSRawekelhhlQEQnvsnvfLDKEEFFIGSKYKKVVYRQFTDSSFREQVKRRAEDEHLGILGP 804
Cdd:cd14451      1 KRRYYIAAEEEEWDYAGYG---------KSR------LDKTQNERDTVFKKVVFRRYLDSTFSTPDIQGEYEEHLGILGP 65

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1758362338  805 PIHANVGDKVKVVFKNMATRPYSIHAHGVKTESST-----------------VVPtlPGEVRTYTWQIPERSGAGREDSA 867
Cdd:cd14451     66 VIRAEVDDVIQVFFKNLASRPYSLHAHGLSYEKSSeglsyddespdwfkkddAVQ--PNGTYTYVWYANPRSGPENNGSD 143

                          170       180
                   ....*....|....*....|....*....
gi 1758362338  868 CIPWAYYSTVDRVKDLYSGLIGPLIVCRK 896
Cdd:cd14451    144 CRTWAYYSAVNPEKDIHSGLIGPLLICRK 172
CuRO_5_FV_like cd14451
The fifth cupredoxin domain of coagulation factor V and similar proteins; Factor V is an ...
 371-557 2.43e-46

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


Pssm-ID: 259993 [Multi-domain]  Cd Length: 173  Bit Score: 163.86  E-value: 2.43e-46
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1758362338  371 RHYYIAAEEVIWNYAPSGtdiftgenltalesDSRVFFEQGATRigGSYKKMAYREYTDGSFTNRKQRGPDEEHLGILGP 450
Cdd:cd14451      2 RRYYIAAEEEEWDYAGYG--------------KSRLDKTQNERD--TVFKKVVFRRYLDSTFSTPDIQGEYEEHLGILGP 65

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1758362338  451 VIWAEVGDTIKVTFHNKGQHPLSIQPMGVSFTAENEGTYYgpPGRSS---QQASHVAPKETFTYEWTVPKEMGPTYADPV 527
Cdd:cd14451     66 VIRAEVDDVIQVFFKNLASRPYSLHAHGLSYEKSSEGLSY--DDESPdwfKKDDAVQPNGTYTYVWYANPRSGPENNGSD 143

                          170       180       190
                   ....*....|....*....|....*....|
gi 1758362338  528 CLSKMYYSGVDPTKDIFTGLIGPMKICKKG 557
Cdd:cd14451    144 CRTWAYYSAVNPEKDIHSGLIGPLLICRKG 173
CuRO_1_FVIII_like cd14452
The first cupredoxin domain of coagulation factor VIII and similar proteins; Factor VIII ...
 22-202 1.06e-45

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: 162.07  E-value: 1.06e-45
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1758362338   22 KHYFIGITEAVWDYAsgteEKKLISVDTEQSNFylqngPDRIGRKYKKALYFEYTDGTFSKTIDKPAWLGFLGPVIKAEV 101
Cdd:cd14452      1 RRYYIAAVEIGWDYI----HSDLGDPASEQRKK-----PKDIPQKYIKAVFVEYLDATFTVPKPRPAWMGLLGPTIVAEV 71

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1758362338  102 EDKVYVHLKNLASRIYTFHAHGVTYTKEYEGAVYPDNTTDFQRADDKVLPGQQYVYVLHANEPS-PGEGDSNCVTRIYHS 180
Cdd:cd14452     72 GDTVVITFKNLASQPYSLHAVGVSYWKASEGAGYDDSTSQHEKEDDAVYPGGYHTYVWDISPKDgPTGSDPECLTYSYSS 151

                          170       180
                   ....*....|....*....|..
gi 1758362338  181 HVDAPKDIASGLIGPLILCKKG 202
Cdd:cd14452    152 QVDPVKDVNSGLIGALLVCRMG 173
CuRO_6_ceruloplasmin cd11012
The sixth cupredoxin domain of Ceruloplasmin; Ceruloplasmin is a multicopper oxidase essential ...
 215-353 1.26e-45

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


Pssm-ID: 259898 [Multi-domain]  Cd Length: 145  Bit Score: 160.80  E-value: 1.26e-45
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1758362338  215 EFVLMFSVVDENLSWYLEDNIKTFCSEPEKVDKDNEDFQESNRMYSINGYTFGSLPGLSMCAADRVKWYLFGMGNEVDVH 294
Cdd:cd11012      3 EFALLFLVFDENESWYLDENIKTYSDHPEKVNKEDEEFIESNKMHAINGKVFGNLQGLTMHVGDEVYWYLMGMGNEIDIH 82

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1758362338  295 SAFFHGQALT---SRNYQTDIINLFPATLIDAYMVAQNPGVWMLSCQNLNHLKAGLQAFFQV 353
Cdd:cd11012     83 TAHFHGHSFDykhRGVYRSDVFDLFPGTFQTVEMIPRTPGTWLLHCHVTDHIHAGMETTYTV 144
CuRO_5_FV_like cd14451
The fifth cupredoxin domain of coagulation factor V and similar proteins; Factor V is an ...
 22-202 4.28e-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: 160.39  E-value: 4.28e-45
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1758362338   22 KHYFIGITEAVWDYAsGTEEKKLISVDTEQSNfylqngpdrigrKYKKALYFEYTDGTFSKTIDKPAW---LGFLGPVIK 98
Cdd:cd14451      2 RRYYIAAEEEEWDYA-GYGKSRLDKTQNERDT------------VFKKVVFRRYLDSTFSTPDIQGEYeehLGILGPVIR 68

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1758362338   99 AEVEDKVYVHLKNLASRIYTFHAHGVTYTKEYEGAVYPDNTTDFQRADDKVLPGQQYVYVLHANEPS-PGEGDSNCVTRI 177
Cdd:cd14451     69 AEVDDVIQVFFKNLASRPYSLHAHGLSYEKSSEGLSYDDESPDWFKKDDAVQPNGTYTYVWYANPRSgPENNGSDCRTWA 148

                          170       180
                   ....*....|....*....|....*
gi 1758362338  178 YHSHVDAPKDIASGLIGPLILCKKG 202
Cdd:cd14451    149 YYSAVNPEKDIHSGLIGPLLICRKG 173
CuRO_3_FVIII_like cd04227
The third cupredoxin domain of coagulation factor VIII and similar proteins; Factor VIII ...
 373-556 1.21e-44

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: 159.32  E-value: 1.21e-44
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1758362338  373 YYIAAEEVIWNYAPsgtdiftgenLTALESDSRV---FFEQGATRIGGSYKKMAYREYTDGSFTNRKQRGPDEehlGILG 449
Cdd:cd04227      5 HYIAAEELDWDYAP----------LLSSTDDRELqsrYLPTGPQRIGYKYKKVAFVEYTDKTFKRREAKQTEK---GILG 71

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1758362338  450 PVIWAEVGDTIKVTFHNKGQHPLSIQPMGVSftaeNEGTYYG---PPGRSSQQASHVAPKETFTYEWTVPKEMGPTYADP 526
Cdd:cd04227     72 PLLKGEVGDQIHIMFKNTASRPYNIYPHGLT----SVRPMYRsrnPAGEKDLKTMPIGPGETFGYMWELTAEDGPTEEDP 147

                          170       180       190
                   ....*....|....*....|....*....|
gi 1758362338  527 VCLSKMYYSGVDPTKDIFTGLIGPMKICKK 556
Cdd:cd04227    148 RCLTRLYQSTVDPERDLASGLIGPLLICKK 177
CuRO_1_FV_like cd04226
The first cupredoxin domain of coagulation factor VIII and similar proteins; Factor V is an ...
 371-557 3.56e-44

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: 157.33  E-value: 3.56e-44
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1758362338  371 RHYYIAAEEVIWNYAPSGTdiftgenltalesdsrvffEQGATRIGGSYKKMAYREYTDGSftnrKQRGPDEEHLGILGP 450
Cdd:cd04226      1 REYYIAAQNIDWDYTPQSE-------------------ELRLKRSEQSFKKIVYREYEEGF----KKEKPADLSSGLLGP 57

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1758362338  451 VIWAEVGDTIKVTFHNKGQHPLSIQPMGVSFTAENEGTYYgppgrsSQQASH-------VAPKETFTYEWTVPKEMGPTY 523
Cdd:cd04226     58 TLRAEVGDTLIVHFKNMADKPLSIHPQGIAYGKKSEGSLY------SDNTSPveklddaVQPGQEYTYVWDITEEVGPTE 131

                          170       180       190
                   ....*....|....*....|....*....|....
gi 1758362338  524 ADPVCLSKMYYSGVDPTKDIFTGLIGPMKICKKG 557
Cdd:cd04226    132 ADPPCLTYIYYSHVNMVRDFNSGLIGALLICKKG 165
CuRO_3_FV_like cd14450
The third cupredoxin domain of coagulation factor V and similar proteins; Factor V is an ...
 727-895 8.51e-44

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: 156.96  E-value: 8.51e-44
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1758362338  727 TYYVAAVEVEWDYSPSRAWEkelhhlQEQNVSNVFLDKEEFFIGSKYKKVVYRQFTDSSFREQVKRRAEDEhLGILGPPI 806
Cdd:cd14450      4 EYFIAAEEVIWDYAPSIPEN------MDKRYRSQYLDNFSNNIGKKYKKAVFTQYEDGSFTKRLENPRPKE-EGILGPVI 76

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1758362338  807 HANVGDKVKVVFKNMATRPYSIHAHGV---KTESSTVVPT------------LPGEVRTYTWQIPERSGAGREDSACIPW 871
Cdd:cd14450     77 RAQVRDTIKIVFKNKASRPYSIYPHGVtvsKAAEGASYPPdprgnetqnkavQPGETYTYKWNILETDEPTARDPRCLTR 156

                          170       180
                   ....*....|....*....|....
gi 1758362338  872 AYYSTVDRVKDLYSGLIGPLIVCR 895
Cdd:cd14450    157 MYHSAVDITRDIASGLIGPLLICK 180
CuRO_1_Ceruloplasmin_like_1 cd04229
cupredoxin domain of ceruloplasmin homologs; Uncharacterized subfamily of ceruloplasmin ...
 22-202 1.56e-43

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: 156.04  E-value: 1.56e-43
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1758362338   22 KHYFIGITEAVWDYASGTEEKKLISVDTEQSNFYLQNGPDRIGRKYKKALYFEYTDGTFSKTIDKPAWLGFLGPVIKAEV 101
Cdd:cd04229      1 RTYYIAAEEVDWDYAPSGKNKCCLGDDLEVSTLDSQPGPYTIGSTYTKARYREYTDNSFSTPKPTPAYLGILGPVIRAEV 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1758362338  102 EDKVYVHLKN-LASRIYTFHAHGVTYTKEYEGAVypdnttdfQRADDKVLPGQQYVYVLHANEPS-PGEGDSNCVTRIYH 179
Cdd:cd04229     81 GDTIKVVFKNnLDEFPVNMHPHGGLYSKDNEGTT--------DGAGDVVAPGETYTYRWIVPEDAgPGPGDPSSRLWLYH 152

                          170       180
                   ....*....|....*....|...
gi 1758362338  180 SHVDAPKDIASGLIGPLILCKKG 202
Cdd:cd04229    153 SHVDVFAHTNAGLVGPIIVTSKG 175
CuRO_5_FVIII_like cd04228
The fifth cupredoxin domain of coagulation factor VIII and similar proteins; Factor VIII ...
 370-557 4.08e-43

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


Pssm-ID: 259890 [Multi-domain]  Cd Length: 169  Bit Score: 154.66  E-value: 4.08e-43
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1758362338  370 VRHYYIAAEEVIWNYAPSGTDIFTgeNLTALESDSRVFFEQgatriggsYKKMAYREYTDGSFTNRKQRGPDEEHLGILG 449
Cdd:cd04228      1 IRHYFIAAVEVLWDYGMQRPQHFL--RARDPNRGRRKSVPQ--------YKKVVFREYLDGSFTQPVYRGELDEHLGILG 70

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1758362338  450 PVIWAEVGDTIKVTFHNKGQHPLSIQpmgvsftaeNEGTYYGPPGRSSQQASHVAPKETFTYEWTVPKEMGPTYADPVCL 529
Cdd:cd04228     71 PYIRAEVEDNIMVTFKNLASRPYSFH---------SSLISYEEDQRAEPRGNFVQPGEVQTYSWKVLHQMAPTKQEFDCK 141

                          170       180
                   ....*....|....*....|....*...
gi 1758362338  530 SKMYYSGVDPTKDIFTGLIGPMKICKKG 557
Cdd:cd04228    142 AWAYFSNVDLEKDLHSGLIGPLIICKTG 169
CuRO_1_FV_like cd04226
The first cupredoxin domain of coagulation factor VIII and similar proteins; Factor V is an ...
 22-202 2.83e-42

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: 151.94  E-value: 2.83e-42
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1758362338   22 KHYFIGITEAVWDYASGTEEKKLisvdteqsnfylqngpDRIGRKYKKALYFEYTDGtFSKTIDKPAWLGFLGPVIKAEV 101
Cdd:cd04226      1 REYYIAAQNIDWDYTPQSEELRL----------------KRSEQSFKKIVYREYEEG-FKKEKPADLSSGLLGPTLRAEV 63

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1758362338  102 EDKVYVHLKNLASRIYTFHAHGVTYTKEYEGAVYPDNTTDFQRADDKVLPGQQYVYVLHANEPS-PGEGDSNCVTRIYHS 180
Cdd:cd04226     64 GDTLIVHFKNMADKPLSIHPQGIAYGKKSEGSLYSDNTSPVEKLDDAVQPGQEYTYVWDITEEVgPTEADPPCLTYIYYS 143

                          170       180
                   ....*....|....*....|..
gi 1758362338  181 HVDAPKDIASGLIGPLILCKKG 202
Cdd:cd04226    144 HVNMVRDFNSGLIGALLICKKG 165
CuRO_5_ceruloplasmin cd04225
The fifth cupredoxin domain of Ceruloplasmin; Ceruloplasmin is a multicopper oxidase essential ...
 22-201 1.06e-40

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: 147.61  E-value: 1.06e-40
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1758362338   22 KHYFIGITEAVWDYASGTEEKKLISVDTEQS--NFYLQNGPDRIGRKYKKALYFEYTDGTFSKTIDKPA---WLGFLGPV 96
Cdd:cd04225      1 RTYYIAAEEVEWDYSPQRTWEQELHNTHEESpgNAFLNKGDKFIGSKYKKVVYREYTDDTFSVPKERTAeeeHLGILGPL 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1758362338   97 IKAEVEDKVYVHLKNLASRIYTFHAHGVtytKEYEGAVYPdnttdfqraddkVLPGQQYVYVLHANEPS-PGEGDSNCVT 175
Cdd:cd04225     81 IHAEVGEKVKIVFKNMASRPYSIHAHGV---KTDSSWVAP------------TEPGETQTYTWKIPERSgPGVEDSNCIS 145

                          170       180
                   ....*....|....*....|....*.
gi 1758362338  176 RIYHSHVDAPKDIASGLIGPLILCKK 201
Cdd:cd04225    146 WAYYSTVDQIKDLYSGLIGPLVICRR 171
CuRO_3_FVIII_like cd04227
The third cupredoxin domain of coagulation factor VIII and similar proteins; Factor VIII ...
 24-201 1.95e-40

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: 147.38  E-value: 1.95e-40
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1758362338   24 YFIGITEAVWDYASgteeKKLISVDTEQSNFYLQNGPDRIGRKYKKALYFEYTDGTFSKTIDKPAWLGFLGPVIKAEVED 103
Cdd:cd04227      5 HYIAAEELDWDYAP----LLSSTDDRELQSRYLPTGPQRIGYKYKKVAFVEYTDKTFKRREAKQTEKGILGPLLKGEVGD 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1758362338  104 KVYVHLKNLASRIYTFHAHGVTYTKEYEGAVYPDNTTDFQraDDKVLPGQ--QYVYVLHANEpSPGEGDSNCVTRIYHSH 181
Cdd:cd04227     81 QIHIMFKNTASRPYNIYPHGLTSVRPMYRSRNPAGEKDLK--TMPIGPGEtfGYMWELTAED-GPTEEDPRCLTRLYQST 157

                          170       180
                   ....*....|....*....|
gi 1758362338  182 VDAPKDIASGLIGPLILCKK 201
Cdd:cd04227    158 VDPERDLASGLIGPLLICKK 177
CuRO_6_FVIII_like cd11018
The sixth cupredoxin domain of coagulation factor VIII and similar proteins; Factor VIII ...
 909-1050 1.39e-38

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


Pssm-ID: 259904 [Multi-domain]  Cd Length: 144  Bit Score: 140.79  E-value: 1.39e-38
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1758362338  909 EFFLLFLVFDENESWYLDDNIKTYSEHPEKVNKDNEEFLESNKMHAINGKMFGNLQGLTMHVKDEVNWYVMGMGNEIDLH 988
Cdd:cd11018      3 EFALLFTIFDETKSWYFEENMRRNCRPPCHIQTQDPWFHINNKFHAINGYVADTLPGLVMAQHQRIRWHLLNMGSDEEIH 82

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1758362338  989 TVHFHGHSFQYKHRGVYSSDVFDLFPGTYQTLEMFPQTPGTWLLHCHVTDHVHAGMATTYTV 1050
Cdd:cd11018     83 SVHFHGLPFTVRAKKEYRMGVYNLYPGVFGTVEMRPSTAGIWLVECTVGEHLLAGMSALFLV 144
CuRO_3_FVIII_like cd04227
The third cupredoxin domain of coagulation factor VIII and similar proteins; Factor VIII ...
 727-896 1.89e-38

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: 141.61  E-value: 1.89e-38
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1758362338  727 TYYVAAVEVEWDYSPsrawekELHHLQEQNVSNVFLDKEEFFIGSKYKKVVYRQFTDSSFReqvKRRAEDEHLGILGPPI 806
Cdd:cd04227      4 EHYIAAEELDWDYAP------LLSSTDDRELQSRYLPTGPQRIGYKYKKVAFVEYTDKTFK---RREAKQTEKGILGPLL 74

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1758362338  807 HANVGDKVKVVFKNMATRPYSIHAHGVKT-------------ESSTVVPTLPGEVRTYTWQIPERSGAGREDSACIPWAY 873
Cdd:cd04227     75 KGEVGDQIHIMFKNTASRPYNIYPHGLTSvrpmyrsrnpageKDLKTMPIGPGETFGYMWELTAEDGPTEEDPRCLTRLY 154

                          170       180
                   ....*....|....*....|...
gi 1758362338  874 YSTVDRVKDLYSGLIGPLIVCRK 896
Cdd:cd04227    155 QSTVDPERDLASGLIGPLLICKK 177
CuRO_1_FVIII_like cd14452
The first cupredoxin domain of coagulation factor VIII and similar proteins; Factor VIII ...
 371-557 9.22e-38

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


Pssm-ID: 259994 [Multi-domain]  Cd Length: 173  Bit Score: 139.34  E-value: 9.22e-38
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1758362338  371 RHYYIAAEEVIWNYAPSgtdiftgeNLTALESDSRVFfeqgATRIGGSYKKMAYREYTDGSFTNRKQRGPdeeHLGILGP 450
Cdd:cd14452      1 RRYYIAAVEIGWDYIHS--------DLGDPASEQRKK----PKDIPQKYIKAVFVEYLDATFTVPKPRPA---WMGLLGP 65

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1758362338  451 VIWAEVGDTIKVTFHNKGQHPLSIQPMGVSFTAENEGTYY-GPPGRSSQQASHVAPKETFTYEWTVPKEMGPTYADPVCL 529
Cdd:cd14452     66 TIVAEVGDTVVITFKNLASQPYSLHAVGVSYWKASEGAGYdDSTSQHEKEDDAVYPGGYHTYVWDISPKDGPTGSDPECL 145

                          170       180
                   ....*....|....*....|....*...
gi 1758362338  530 SKMYYSGVDPTKDIFTGLIGPMKICKKG 557
Cdd:cd14452    146 TYSYSSQVDPVKDVNSGLIGALLVCRMG 173
CuRO_6_ceruloplasmin cd11012
The sixth cupredoxin domain of Ceruloplasmin; Ceruloplasmin is a multicopper oxidase essential ...
 570-709 1.61e-37

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: 137.69  E-value: 1.61e-37
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1758362338  570 KEFYLFPTVFDENESLLLDDNIRMFTTAPDQVDKEDEDFQESNKMHSMNGFMYGNQPGLNMCLGESIVWYLFSAGNEADV 649
Cdd:cd11012      2 LEFALLFLVFDENESWYLDENIKTYSDHPEKVNKEDEEFIESNKMHAINGKVFGNLQGLTMHVGDEVYWYLMGMGNEIDI 81

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1758362338  650 HGIYFSGNTYLSKGE---RRDTANLFPHKSLTLLMNPDTKGTFDVECLTTDHYTGGMKQKYTV 709
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 ...
 726-896 2.34e-36

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: 134.99  E-value: 2.34e-36
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1758362338  726 RTYYVAAVEVEWDYSPsrawekELHHLQeqnvsnvfLDKEEFfigsKYKKVVYRQFtDSSFReqvKRRAEDEHLGILGPP 805
Cdd:cd04226      1 REYYIAAQNIDWDYTP------QSEELR--------LKRSEQ----SFKKIVYREY-EEGFK---KEKPADLSSGLLGPT 58

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1758362338  806 IHANVGDKVKVVFKNMATRPYSIHAHGV----KTESST-------------VVPtlPGEVRTYTWQIPERSGAGREDSAC 868
Cdd:cd04226     59 LRAEVGDTLIVHFKNMADKPLSIHPQGIaygkKSEGSLysdntspveklddAVQ--PGQEYTYVWDITEEVGPTEADPPC 136

                          170       180
                   ....*....|....*....|....*...
gi 1758362338  869 IPWAYYSTVDRVKDLYSGLIGPLIVCRK 896
Cdd:cd04226    137 LTYIYYSHVNMVRDFNSGLIGALLICKK 164
CuRO_1_FVIII_like cd14452
The first cupredoxin domain of coagulation factor VIII and similar proteins; Factor VIII ...
 726-897 5.95e-36

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: 134.34  E-value: 5.95e-36
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1758362338  726 RTYYVAAVEVEWDYSPSrawekelhhlqEQNVSNVFLDKEEFFIGSKYKKVVYRQFTDSSFREQVKRRAedeHLGILGPP 805
Cdd:cd14452      1 RRYYIAAVEIGWDYIHS-----------DLGDPASEQRKKPKDIPQKYIKAVFVEYLDATFTVPKPRPA---WMGLLGPT 66

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1758362338  806 IHANVGDKVKVVFKNMATRPYSIHAHGVKT---------ESSTVVP------TLPGEVRTYTWQIPERSGAGREDSACIP 870
Cdd:cd14452     67 IVAEVGDTVVITFKNLASQPYSLHAVGVSYwkasegagyDDSTSQHekeddaVYPGGYHTYVWDISPKDGPTGSDPECLT 146

                          170       180
                   ....*....|....*....|....*..
gi 1758362338  871 WAYYSTVDRVKDLYSGLIGPLIVCRKS 897
Cdd:cd14452    147 YSYSSQVDPVKDVNSGLIGALLVCRMG 173
CuRO_6_FV_like cd14455
The sixth cupredoxin domain of coagulation factor V and similar proteins; Factor V is an ...
 909-1050 4.47e-34

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: 127.67  E-value: 4.47e-34
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1758362338  909 EFFLLFLVFDENESWYLDDNiKTYSEhpEKVNKDNEEFLESNKMHAINGKMFgNLQGLTMHVKDEVNWYVMGMGNEIDLH 988
Cdd:cd14455      3 EFVLLFMTFDEEKSWYYEKN-RKRTC--RENRVKDPNVQDNHTFHAINGIIY-NLKGLRMYTNELVRWHLINMGGPKDLH 78

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1758362338  989 TVHFHGHSFQYKHRGVYSSDVFDLFPGTYQTLEMFPQTPGTWLLHCHVTDHVHAGMATTYTV 1050
Cdd:cd14455     79 VVHFHGQTFTEKGLKDHQLGVYPLLPGSFATLEMKPSKPGLWLLETEVGESQQRGMQTLFLV 140
CuRO_6_FVIII_like cd11018
The sixth cupredoxin domain of coagulation factor VIII and similar proteins; Factor VIII ...
 214-353 4.25e-33

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: 124.99  E-value: 4.25e-33
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1758362338  214 QEFVLMFSVVDENLSWYLEDNIKTFCSEPEKVDKDNEDFQESNRMYSINGYTFGSLPGLSMCAADRVKWYLFGMGNEVDV 293
Cdd:cd11018      2 QEFALLFTIFDETKSWYFEENMRRNCRPPCHIQTQDPWFHINNKFHAINGYVADTLPGLVMAQHQRIRWHLLNMGSDEEI 81

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1758362338  294 HSAFFHGQALT---SRNYQTDIINLFPATLIDAYMVAQNPGVWMLSCQNLNHLKAGLQAFFQV 353
Cdd:cd11018     82 HSVHFHGLPFTvraKKEYRMGVYNLYPGVFGTVEMRPSTAGIWLVECTVGEHLLAGMSALFLV 144
CuRO_2_ceruloplasmin_like_2 cd11023
cupredoxin domain of ceruloplasmin homologs; Uncharacterized subfamily of ceruloplasmin ...
 940-1050 3.22e-32

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: 121.56  E-value: 3.22e-32
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1758362338  940 NKDNEEflESNKMHAINGKMFGNLQGLTMHVKDEVNWYVMGMGNEIDLHTVHFHGHSFQYKHRGvySSDVFDLFPGTYQT 1019
Cdd:cd11023     12 LDLNVE--EAGLMHSINGYVFGNLPGVTIAKGKRVRWHLVAYGNEVDFHTPHWHGQTVEADKSR--RTDVAELMPASMRV 87

                           90       100       110
                   ....*....|....*....|....*....|.
gi 1758362338 1020 LEMFPQTPGTWLLHCHVTDHVHAGMATTYTV 1050
Cdd:cd11023     88 ADMTAADVGTWLLHCHVHDHYMAGMMTQFAV 118
CuRO_5_FVIII_like cd04228
The fifth cupredoxin domain of coagulation factor VIII and similar proteins; Factor VIII ...
 22-202 2.39e-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: 120.76  E-value: 2.39e-31
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1758362338   22 KHYFIGITEAVWDYASGTEEKKLISVDTEQSnfylQNGPdriGRKYKKALYFEYTDGTFSKTIDK---PAWLGFLGPVIK 98
Cdd:cd04228      2 RHYFIAAVEVLWDYGMQRPQHFLRARDPNRG----RRKS---VPQYKKVVFREYLDGSFTQPVYRgelDEHLGILGPYIR 74

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1758362338   99 AEVEDKVYVHLKNLASRIYTFHAHGVTYtkeyegavypDNTTDFQRADDKVLPGQQYVY---VLHANEPSPGEGDsnCVT 175
Cdd:cd04228     75 AEVEDNIMVTFKNLASRPYSFHSSLISY----------EEDQRAEPRGNFVQPGEVQTYswkVLHQMAPTKQEFD--CKA 142

                          170       180
                   ....*....|....*....|....*..
gi 1758362338  176 RIYHSHVDAPKDIASGLIGPLILCKKG 202
Cdd:cd04228    143 WAYFSNVDLEKDLHSGLIGPLIICKTG 169
CuRO_4_FVIII_like cd11016
The fourth cupredoxin domain of coagulation factor VIII and similar proteins; Factor VIII ...
 912-1051 1.82e-30

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: 117.28  E-value: 1.82e-30
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1758362338  912 LLFLVFDENESWYLDDNIKTYSEHPEKVNKDNEEFLESNKMHAINGKMFGNLQgLTMHVKDEVNWYVMGMGNEIDLHTVH 991
Cdd:cd11016      6 LLFSVFDENNSWYLKENIHRFTQTPAGVNDTDPDFYASNVMHTINGIVFDRRQ-FVICLTDVAYWYVLSVGAQTDFLSVF 84

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1758362338  992 FHGHSFqyKHRGVYsSDVFDLFPGTYQTLEMFPQTPGTWLLHCHVTDHVHAGMATTYTVL 1051
Cdd:cd11016     85 FSGNTF--KHQMVY-EDVLTLFPFSGETVSMSPEVPGEWELGCFNGDFRSRGMSAQYTVS 141
CuRO_2_FV_like cd14453
The second cupredoxin domain of coagulation factor V and similar proteins; Factor V is an ...
 213-353 2.00e-30

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: 116.50  E-value: 2.00e-30
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1758362338  213 DQEFVLMFSVVDENLSWYledniktfcsepekvdkdNEDFQESNRMYSINGYTFGSLPGLSMCAADRVKWYLFGMGNEVD 292
Cdd:cd14453      1 YKEYVLMFGVFDENKSWY------------------KQNASVDSVKYTINGYTNGTLPDVSICAYDHVSWHLLGMSSEPE 62

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1758362338  293 VHSAFFHGQALTSRNYQTDIINLFPATLIDAYMVAQNPGVWMLSCQNLNHLKAGLQAFFQV 353
Cdd:cd14453     63 LFSVHFNGQVLEQNGHKVSAVGLVSGSSTTASMTVVHTGRWLISSLIMKHLQAGMYGYLNI 123
CuRO_4_FVIII_like cd11016
The fourth cupredoxin domain of coagulation factor VIII and similar proteins; Factor VIII ...
 569-712 2.30e-30

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: 116.89  E-value: 2.30e-30
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1758362338  569 DKEFYLFPTVFDENESLLLDDNIRMFTTAPDQVDKEDEDFQESNKMHSMNGFMYGNQPgLNMCLGESIVWYLFSAGNEAD 648
Cdd:cd11016      1 DKDWSLLFSVFDENNSWYLKENIHRFTQTPAGVNDTDPDFYASNVMHTINGIVFDRRQ-FVICLTDVAYWYVLSVGAQTD 79

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1758362338  649 VHGIYFSGNTYLSKGERRDTANLFPHKSLTLLMNPDTKGTFDVECLTTDHYTGGMKQKYTVNQC 712
Cdd:cd11016     80 FLSVFFSGNTFKHQMVYEDVLTLFPFSGETVSMSPEVPGEWELGCFNGDFRSRGMSAQYTVSTC 143
CuRO_4_FVIII_like cd11016
The fourth cupredoxin domain of coagulation factor VIII and similar proteins; Factor VIII ...
 213-356 4.58e-30

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: 116.12  E-value: 4.58e-30
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1758362338  213 DQEFVLMFSVVDENLSWYLEDNIKTFCSEPEKVDKDNEDFQESNRMYSINGYTFGSLPgLSMCAADRVKWYLFGMGNEVD 292
Cdd:cd11016      1 DKDWSLLFSVFDENNSWYLKENIHRFTQTPAGVNDTDPDFYASNVMHTINGIVFDRRQ-FVICLTDVAYWYVLSVGAQTD 79

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1758362338  293 VHSAFFHGQALTSRNYQTDIINLFPATLIDAYMVAQNPGVWMLSCQNLNHLKAGLQAFFQVRDC 356
Cdd:cd11016     80 FLSVFFSGNTFKHQMVYEDVLTLFPFSGETVSMSPEVPGEWELGCFNGDFRSRGMSAQYTVSTC 143
CuRO_4_FV_like cd14454
The fourth cupredoxin domain of coagulation factor V and similar proteins; Factor V is an ...
 213-356 7.74e-29

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: 112.66  E-value: 7.74e-29
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1758362338  213 DQEFVLMFSVVDENLSWYLEDNIKTFCSEPEKVDKDNEDFQESNRMYSINGYTFGSLPGLSMCAADRVKWYLFGMGNEVD 292
Cdd:cd14454      1 DLEQHAVFAVFDENKSWYLEENINKYCSNPNNVKKDDPKFYKSNIMPTINGYAYESSAPLGFCHSEVVQWHISSVGTQDE 80

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1758362338  293 VHSAFFHGQALTSRNYQTDIINLFPATLIDAYMVAQNPGVWMLSCQNLNHLKAGLQAFFQVRDC 356
Cdd:cd14454     81 IITVHLSGHTFRYKGKHEDTLNLFPMSGESITVTMDNLGTWLLGSFGSSKKSKGLRVRFTDVIC 144
CuRO_4_FV_like cd14454
The fourth cupredoxin domain of coagulation factor V and similar proteins; Factor V is an ...
 913-1032 5.58e-28

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: 110.35  E-value: 5.58e-28
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1758362338  913 LFLVFDENESWYLDDNIKTYSEHPEKVNKDNEEFLESNKMHAINGKMFGNLQGLTMHVKDEVNWYVMGMGNEIDLHTVHF 992
Cdd:cd14454      7 VFAVFDENKSWYLEENINKYCSNPNNVKKDDPKFYKSNIMPTINGYAYESSAPLGFCHSEVVQWHISSVGTQDEIITVHL 86

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|
gi 1758362338  993 HGHSFQYKHRgvySSDVFDLFPGTYQTLEMFPQTPGTWLL 1032
Cdd:cd14454     87 SGHTFRYKGK---HEDTLNLFPMSGESITVTMDNLGTWLL 123
CuRO_2_ceruloplasmin_like_2 cd11023
cupredoxin domain of ceruloplasmin homologs; Uncharacterized subfamily of ceruloplasmin ...
 248-353 2.74e-27

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: 107.31  E-value: 2.74e-27
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1758362338  248 DNEDFQESNRMYSINGYTFGSLPGLSMCAADRVKWYLFGMGNEVDVHSAFFHGQALTS-RNYQTDIINLFPATLIDAYMV 326
Cdd:cd11023     12 LDLNVEEAGLMHSINGYVFGNLPGVTIAKGKRVRWHLVAYGNEVDFHTPHWHGQTVEAdKSRRTDVAELMPASMRVADMT 91

                           90       100
                   ....*....|....*....|....*..
gi 1758362338  327 AQNPGVWMLSCQNLNHLKAGLQAFFQV 353
Cdd:cd11023     92 AADVGTWLLHCHVHDHYMAGMMTQFAV 118
CuRO_4_FV_like cd14454
The fourth cupredoxin domain of coagulation factor V and similar proteins; Factor V is an ...
 569-712 2.01e-26

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: 105.72  E-value: 2.01e-26
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1758362338  569 DKEFYLFPTVFDENESLLLDDNIRMFTTAPDQVDKEDEDFQESNKMHSMNGFMYGNQPGLNMCLGESIVWYLFSAGNEAD 648
Cdd:cd14454      1 DLEQHAVFAVFDENKSWYLEENINKYCSNPNNVKKDDPKFYKSNIMPTINGYAYESSAPLGFCHSEVVQWHISSVGTQDE 80

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1758362338  649 VHGIYFSGNTYLSKGERRDTANLFPHKSLTLLMNPDTKGTFDVECLTTDHYTGGMKQKYTVNQC 712
Cdd:cd14454     81 IITVHLSGHTFRYKGKHEDTLNLFPMSGESITVTMDNLGTWLLGSFGSSKKSKGLRVRFTDVIC 144
CuRO_6_FVIII_like cd11018
The sixth cupredoxin domain of coagulation factor VIII and similar proteins; Factor VIII ...
 570-709 5.33e-25

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: 101.88  E-value: 5.33e-25
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1758362338  570 KEFYLFPTVFDENESLLLDDNIRMFTTAPDQVDKEDEDFQESNKMHSMNGFMYGNQPGLNMCLGESIVWYLFSAGNEADV 649
Cdd:cd11018      2 QEFALLFTIFDETKSWYFEENMRRNCRPPCHIQTQDPWFHINNKFHAINGYVADTLPGLVMAQHQRIRWHLLNMGSDEEI 81

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1758362338  650 HGIYFSGNTYL---SKGERRDTANLFPHKSLTLLMNPDTKGTFDVECLTTDHYTGGMKQKYTV 709
Cdd:cd11018     82 HSVHFHGLPFTvraKKEYRMGVYNLYPGVFGTVEMRPSTAGIWLVECTVGEHLLAGMSALFLV 144
CuRO_2_FVIII_like cd11015
The second cupredoxin domain of coagulation factor VIII and similar proteins; Factor VIII ...
 214-353 3.15e-24

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: 99.21  E-value: 3.15e-24
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1758362338  214 QEFVLMFSVVDENLSWYLEDniktfcSEPEKVDKDNEDfQESNRMYSINGYTFGSLPGLSMCAADRVKWYLFGMGNEVDV 293
Cdd:cd11015      2 QAFVLLFAVFDEGKSWYSEV------GERKSRDKFKRA-DSRKEFHTINGYINASLPGLKICQRKPVIWHVIGMGTAPEV 74

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1758362338  294 HSAFFHGQALTSRNYQTDIINLFPATLIDAYMVAQNPGVWMLSCQNLNHLKAGLQAFFQV 353
Cdd:cd11015     75 HSIFFEGHTFLVRTHRKVSLEISPMTFLTAQTKPATVGSFLIFCQIHSHQHDGMEAMVKV 134
CuRO_2_FVIII_like cd11015
The second cupredoxin domain of coagulation factor VIII and similar proteins; Factor VIII ...
 909-1050 3.07e-23

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


Pssm-ID: 259901 [Multi-domain]  Cd Length: 134  Bit Score: 96.51  E-value: 3.07e-23
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1758362338  909 EFFLLFLVFDENESWYlddniktySEHPEKVNKDNEEFLES-NKMHAINGKMFGNLQGLTMHVKDEVNWYVMGMGNEIDL 987
Cdd:cd11015      3 AFVLLFAVFDEGKSWY--------SEVGERKSRDKFKRADSrKEFHTINGYINASLPGLKICQRKPVIWHVIGMGTAPEV 74

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1758362338  988 HTVHFHGHSFQYK-HRGVyssdVFDLFPGTYQTLEMFPQTPGTWLLHCHVTDHVHAGMATTYTV 1050
Cdd:cd11015     75 HSIFFEGHTFLVRtHRKV----SLEISPMTFLTAQTKPATVGSFLIFCQIHSHQHDGMEAMVKV 134
CuRO_6_FV_like cd14455
The sixth cupredoxin domain of coagulation factor V and similar proteins; Factor V is an ...
 214-353 5.07e-23

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: 96.09  E-value: 5.07e-23
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1758362338  214 QEFVLMFSVVDENLSWYLEDNIKTFCsepEKVDKDNEDFQESNRMYSINGYTFgSLPGLSMCAADRVKWYLFGMGNEVDV 293
Cdd:cd14455      2 REFVLLFMTFDEEKSWYYEKNRKRTC---RENRVKDPNVQDNHTFHAINGIIY-NLKGLRMYTNELVRWHLINMGGPKDL 77

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1758362338  294 HSAFFHGQALTS---RNYQTDIINLFPATLIDAYMVAQNPGVWMLSCQNLNHLKAGLQAFFQV 353
Cdd:cd14455     78 HVVHFHGQTFTEkglKDHQLGVYPLLPGSFATLEMKPSKPGLWLLETEVGESQQRGMQTLFLV 140
CuRO_2_ceruloplasmin_like_2 cd11023
cupredoxin domain of ceruloplasmin homologs; Uncharacterized subfamily of ceruloplasmin ...
 605-709 1.00e-20

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: 88.44  E-value: 1.00e-20
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1758362338  605 DEDFQESNKMHSMNGFMYGNQPGLNMCLGESIVWYLFSAGNEADVHGIYFSGNTYLSKGERR-DTANLFPHKSLTLLMNP 683
Cdd:cd11023     13 DLNVEEAGLMHSINGYVFGNLPGVTIAKGKRVRWHLVAYGNEVDFHTPHWHGQTVEADKSRRtDVAELMPASMRVADMTA 92

                           90       100
                   ....*....|....*....|....*.
gi 1758362338  684 DTKGTFDVECLTTDHYTGGMKQKYTV 709
Cdd:cd11023     93 ADVGTWLLHCHVHDHYMAGMMTQFAV 118
CuRO_2_FV_like cd14453
The second cupredoxin domain of coagulation factor V and similar proteins; Factor V is an ...
 909-1044 1.15e-17

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: 79.90  E-value: 1.15e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1758362338  909 EFFLLFLVFDENESWYlddniktysehpekvnkdNEEFLESNKMHAINGKMFGNLQGLTMHVKDEVNWYVMGMGNEIDLH 988
Cdd:cd14453      3 EYVLMFGVFDENKSWY------------------KQNASVDSVKYTINGYTNGTLPDVSICAYDHVSWHLLGMSSEPELF 64

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 1758362338  989 TVHFHGHSFQYKHrgvYSSDVFDLFPGTYQTLEMFPQTPGTWLLHCHVTDHVHAGM 1044
Cdd:cd14453     65 SVHFNGQVLEQNG---HKVSAVGLVSGSSTTASMTVVHTGRWLISSLIMKHLQAGM 117
Cu-oxidase_2 pfam07731
Multicopper oxidase; This entry contains many divergent copper oxidase-like domains that are ...
 950-1052 2.35e-17

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: 79.79  E-value: 2.35e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1758362338  950 NKMHAINGKMFG-NLQGLTMHVKDEVNWYVMGMGNeiDLHTVHFHGHSFQYKHRGVYSS----------------DVFDL 1012
Cdd:pfam07731   19 RNDWAINGLLFPpNTNVITLPYGTVVEWVLQNTTT--GVHPFHLHGHSFQVLGRGGGPWpeedpktynlvdpvrrDTVQV 96

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|
gi 1758362338 1013 FPGTYQTLEMFPQTPGTWLLHCHVTDHVHAGMATTYTVLP 1052
Cdd:pfam07731   97 PPGGWVAIRFRADNPGVWLFHCHILWHLDQGMMGQFVVRP 136
CuRO_3_LCC_like cd04207
Cupredoxin domain 3 of laccase-like multicopper oxidases; including laccase, CueO, spore coat ...
 255-352 3.19e-17

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: 79.04  E-value: 3.19e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1758362338  255 SNRMYSINGYTF----GSLPGLSMCAADRVKWYLFGMGNEVDVHSAFFHGQA--LTSRN-------------YQTDIINL 315
Cdd:cd04207     16 GTTRWVINGMPFkegdANTDIFSVEAGDVVEIVLINAGNHDMQHPFHLHGHSfwVLGSGggpfdaplnltnpPWRDTVLV 95

                           90       100       110
                   ....*....|....*....|....*....|....*..
gi 1758362338  316 FPATLIDAYMVAQNPGVWMLSCQNLNHLKAGLQAFFQ 352
Cdd:cd04207     96 PPGGWVVIRFKADNPGVWMLHCHILEHEDAGMMTVFE 132
Cu-oxidase pfam00394
Multicopper oxidase; Many of the proteins in this family contain multiple similar copies of ...
 220-357 1.69e-15

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: 74.66  E-value: 1.69e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1758362338  220 FSVVDENLSWYlEDNIKTFCSEPEKVDKDNEDFQESNRMYSINGYTFGSLPGLSMCAADRVKWYLFgMGNEVDVHSAFFH 299
Cdd:pfam00394    1 EDYVITLSDWY-HKDAKDLEKELLASGKAPTDFPPVPDAVLINGKDGASLATLTVTPGKTYRLRII-NVALDDSLNFSIE 78

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1758362338  300 GQALT--------SRNYQTDIINLFPATLIDAYMVA-QNPGVWMLSCQNLN-HLKAGLQAFFQVRDCN 357
Cdd:pfam00394   79 GHKMTvvevdgvyVNPFTVDSLDIFPGQRYSVLVTAnQDPGNYWIVASPNIpAFDNGTAAAILRYSGA 146
CuRO_3_LCC_like cd04207
Cupredoxin domain 3 of laccase-like multicopper oxidases; including laccase, CueO, spore coat ...
 954-1049 2.78e-14

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: 70.57  E-value: 2.78e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1758362338  954 AINGKMF----GNLQGLTMHVKDEVNWYVMGMGNEIDLHTVHFHGHSFQYKHRGVYSS------------DVFDLFPGTY 1017
Cdd:cd04207     21 VINGMPFkegdANTDIFSVEAGDVVEIVLINAGNHDMQHPFHLHGHSFWVLGSGGGPFdaplnltnppwrDTVLVPPGGW 100

                           90       100       110
                   ....*....|....*....|....*....|..
gi 1758362338 1018 QTLEMFPQTPGTWLLHCHVTDHVHAGMATTYT 1049
Cdd:cd04207    101 VVIRFKADNPGVWMLHCHILEHEDAGMMTVFE 132
CuRO_2_FVIII_like cd11015
The second cupredoxin domain of coagulation factor VIII and similar proteins; Factor VIII ...
 570-709 4.67e-14

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: 69.93  E-value: 4.67e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1758362338  570 KEFYLFPTVFDENESLLLDdnirmfTTAPDQVDKEDEDfQESNKMHSMNGFMYGNQPGLNMCLGESIVWYLFSAGNEADV 649
Cdd:cd11015      2 QAFVLLFAVFDEGKSWYSE------VGERKSRDKFKRA-DSRKEFHTINGYINASLPGLKICQRKPVIWHVIGMGTAPEV 74

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1758362338  650 HGIYFSGNTYLSKGERRDTANLFPHKSLTLLMNPDTKGTFDVECLTTDHYTGGMKQKYTV 709
Cdd:cd11015     75 HSIFFEGHTFLVRTHRKVSLEISPMTFLTAQTKPATVGSFLIFCQIHSHQHDGMEAMVKV 134
CuRO_1_LCC_like cd04206
Cupredoxin domain 1 of laccase-like multicopper oxidases; including laccase, CueO, spore coat ...
 446-554 6.51e-14

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: 69.24  E-value: 6.51e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1758362338  446 GILGPVIWAEVGDTIKVTFHNKGQH-PLSIQPMGVSFTAENEGTyygPPGRSSQQAshVAPKETFTYEWTVPKEMGpTYa 524
Cdd:cd04206     27 QFPGPTIRVKEGDTVEVTVTNNLPNePTSIHWHGLRQPGTNDGD---GVAGLTQCP--IPPGESFTYRFTVDDQAG-TF- 99

                           90       100       110
                   ....*....|....*....|....*....|
gi 1758362338  525 dpvclskMYYSGVDPtkDIFTGLIGPMKIC 554
Cdd:cd04206    100 -------WYHSHVGG--QRADGLYGPLIVE 120
CuRO_6_FV_like cd14455
The sixth cupredoxin domain of coagulation factor V and similar proteins; Factor V is an ...
 570-709 1.88e-13

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: 68.74  E-value: 1.88e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1758362338  570 KEFYLFPTVFDENESLLLDDNIrmfTTAPDQVDKEDEDFQESNKMHSMNGFMYgNQPGLNMCLGESIVWYLFSAGNEADV 649
Cdd:cd14455      2 REFVLLFMTFDEEKSWYYEKNR---KRTCRENRVKDPNVQDNHTFHAINGIIY-NLKGLRMYTNELVRWHLINMGGPKDL 77

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1758362338  650 HGIYFSGNTYLSKG---ERRDTANLFPHKSLTLLMNPDTKGTFDVECLTTDHYTGGMKQKYTV 709
Cdd:cd14455     78 HVVHFHGQTFTEKGlkdHQLGVYPLLPGSFATLEMKPSKPGLWLLETEVGESQQRGMQTLFLV 140
CuRO_1_LCC_like cd04206
Cupredoxin domain 1 of laccase-like multicopper oxidases; including laccase, CueO, spore coat ...
 790-894 7.07e-12

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: 63.46  E-value: 7.07e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1758362338  790 VKRRAEDEHLGILGPPIHANVGDKVKVVFKN-MATRPYSIHAHGVK---------TESSTVVPTLPGEVRTYTWQIPERS 859
Cdd:cd04206     17 VLRQVITVNGQFPGPTIRVKEGDTVEVTVTNnLPNEPTSIHWHGLRqpgtndgdgVAGLTQCPIPPGESFTYRFTVDDQA 96

                           90       100       110
                   ....*....|....*....|....*....|....*
gi 1758362338  860 GAgredsacipWAYYSTVDrvKDLYSGLIGPLIVC 894
Cdd:cd04206     97 GT---------FWYHSHVG--GQRADGLYGPLIVE 120
SufI COG2132
Multicopper oxidase with three cupredoxin domains (includes cell division protein FtsP and ...
 952-1052 4.04e-11

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: 66.50  E-value: 4.04e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1758362338  952 MHAINGKMFGnlqgltMHVKDEV----NWYVMGMGNEID-LHTVHFHGHSFQYKHR---GVYSS---DVFDLFPGTYQTL 1020
Cdd:COG2132    317 VWTINGKAFD------PDRPDLTvklgERERWTLVNDTMmPHPFHLHGHQFQVLSRngkPPPEGgwkDTVLVPPGETVRI 390

                           90       100       110
                   ....*....|....*....|....*....|...
gi 1758362338 1021 EM-FPQTPGTWLLHCHVTDHVHAGMATTYTVLP 1052
Cdd:COG2132    391 LFrFDNYPGDWMFHCHILEHEDAGMMGQFEVVP 423
CuRO_1_2DMCO_NIR_like_2 cd14449
The cupredoxin domain 1 of a two-domain laccase related to nitrite reductase; The two-domain ...
 803-896 1.16e-10

The cupredoxin domain 1 of a two-domain laccase related to nitrite reductase; The two-domain laccase (small laccase) in this family differs significantly from all laccases. It resembles the two domain nitrite reductase in both sequence and structure. It consists of two cupredoxin domains and forms trimers, and hence resembles the quaternary structure of nitrite reductases more than that of large laccases. There are three trinuclear copper clusters in the enzyme localized between domains 1 and 2 of each pair of neighbor chains. 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: 60.36  E-value: 1.16e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1758362338  803 GPPIHANVGDKVKVVFKNMATRPYSIHAHGVKTESSTVVPTL------PGEVRTYTWQipERSGAGREDSACIP-----W 871
Cdd:cd14449     29 GPVIEVREGDTLKILFRNTLDVPASLHPHGVDYTTASDGTGMnasivaPGDTRIYTWR--THGGYRRADGSWAEgtagyW 106

                           90       100
                   ....*....|....*....|....*....
gi 1758362338  872 AYYSTV----DRVKDLYSGLIGPLIVCRK 896
Cdd:cd14449    107 HYHDHVfgteHGTEGLSRGLYGALIVRRV 135
CuRO_2_FV_like cd14453
The second cupredoxin domain of coagulation factor V and similar proteins; Factor V is an ...
 569-703 1.75e-10

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: 59.49  E-value: 1.75e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1758362338  569 DKEFYLFPTVFDENESlllddnirmfttapdqvdKEDEDFQESNKMHSMNGFMYGNQPGLNMCLGESIVWYLFSAGNEAD 648
Cdd:cd14453      1 YKEYVLMFGVFDENKS------------------WYKQNASVDSVKYTINGYTNGTLPDVSICAYDHVSWHLLGMSSEPE 62

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 1758362338  649 VHGIYFSGNTYLSKGERRDTANLFPHKSLTLLMNPDTKGTFDVECLTTDHYTGGM 703
Cdd:cd14453     63 LFSVHFNGQVLEQNGHKVSAVGLVSGSSTTASMTVVHTGRWLISSLIMKHLQAGM 117
CuRO_1_LCC_like cd04206
Cupredoxin domain 1 of laccase-like multicopper oxidases; including laccase, CueO, spore coat ...
 91-199 2.19e-10

Cupredoxin domain 1 of laccase-like multicopper oxidases; including laccase, CueO, spore coat protein A, ascorbate oxidase and similar proteins; Laccase-like multicopper oxidases (MCOs) in this family contain three cupredoxin domains. They are able to couple oxidation of substrates with reduction of dioxygen to water. MCOs are capable of oxidizing a vast range of substrates, varying from aromatic to inorganic compounds such as metals. Although the members of this family have diverse functions, majority of them have three cupredoxin domain repeats. The copper ions are bound in several sites; Type 1, Type 2, and/or Type 3. The ensemble of types 2 and 3 copper is called a trinuclear cluster. MCOs oxidize their substrate by accepting electrons at a mononuclear copper center and transferring them to the active site trinuclear copper center. The cupredoxin domain 1 of 3-domain MCOs contains part the trinuclear copper binding site, which is located at the interface of domains 1 and 3. Also included in this family are cupredoxin domains 1, 3, and 5 of the 6-domain MCO ceruloplasmin and similar proteins.


Pssm-ID: 259869 [Multi-domain]  Cd Length: 120  Bit Score: 59.22  E-value: 2.19e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1758362338   91 GFLGPVIKAEVEDKVYVHLKN-LASRIYTFHAHGVTYTKEYEGAVYPDNTTdfqradDKVLPGQQYVYVLHANEPsPGeg 169
Cdd:cd04206     27 QFPGPTIRVKEGDTVEVTVTNnLPNEPTSIHWHGLRQPGTNDGDGVAGLTQ------CPIPPGESFTYRFTVDDQ-AG-- 97

                           90       100       110
                   ....*....|....*....|....*....|
gi 1758362338  170 dsncvTRIYHSHVDApkDIASGLIGPLILC 199
Cdd:cd04206     98 -----TFWYHSHVGG--QRADGLYGPLIVE 120
CuRO_3_CumA_like cd13906
The third cupredoxin domain of CumA like multicopper oxidase; This multicopper oxidase (MCO) ...
 976-1050 8.36e-09

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: 55.08  E-value: 8.36e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1758362338  976 WYVMGMGNEID-LHTVHFHGHSFQykhrgVYSSDVFDLFPG----TY-----QTLE--MFPQTPGTWLLHCHVTDHVHAG 1043
Cdd:cd13906     56 SYVLRLVNETAfLHPMHLHGHFFR-----VLSRNGRPVPEPfwrdTVllgpkETVDiaFVADNPGDWMFHCHILEHQETG 130


                   ....*..
gi 1758362338 1044 MATTYTV 1050
Cdd:cd13906    131 MMGVIRV 137
CuRO_D2_2dMcoN_like cd04202
The second cupredoxin domain of bacterial two domain multicopper oxidase McoN and similar ...
 952-1045 1.66e-08

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


Pssm-ID: 259865 [Multi-domain]  Cd Length: 138  Bit Score: 54.18  E-value: 1.66e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1758362338  952 MHAINGKMFGNLQGLTMHVKDEVNWYVMGMGNEIdlHTVHFHGHSFQYKHR-GV-------YSSDVFDLFPGTYQTLEMF 1023
Cdd:cd04202     29 YFTINGKSFPATPPLVVKEGDRVRIRLINLSMDH--HPMHLHGHFFLVTATdGGpipgsapWPKDTLNVAPGERYDIEFV 106

                           90       100
                   ....*....|....*....|..
gi 1758362338 1024 PQTPGTWLLHCHVTDHVHAGMA 1045
Cdd:cd04202    107 ADNPGDWMFHCHKLHHAMNGMG 128
CuRO_1_2DMCO_NIR_like cd11024
The cupredoxin domain 1 of a two-domain laccase related to nitrite reductase; The two-domain ...
 449-514 3.07e-08

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


Pssm-ID: 259910 [Multi-domain]  Cd Length: 119  Bit Score: 53.04  E-value: 3.07e-08
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1758362338  449 GPVIWAEVGDTIKVTFHNKGQHPLSIQPMGVSfTAENEGTYYGPpgrssqqashVAPKETFTYEWT 514
Cdd:cd11024     32 GPTLRATEGDLVRIHFINTGDHPHTIHFHGIH-DAAMDGTGLGP----------IMPGESFTYEFV 86
CuRO_3_CumA_like cd13906
The third cupredoxin domain of CumA like multicopper oxidase; This multicopper oxidase (MCO) ...
 263-354 6.46e-08

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


Pssm-ID: 259973 [Multi-domain]  Cd Length: 138  Bit Score: 52.77  E-value: 6.46e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1758362338  263 GYTFGSLPGLSMCAAD------------RVKWYLFGMGNEVD-VHSAFFHGQALT--SRN-------YQTDIINLFPATL 320
Cdd:cd13906     25 GGTFWAINGTSWTGGDhshlppplatlkRGRSYVLRLVNETAfLHPMHLHGHFFRvlSRNgrpvpepFWRDTVLLGPKET 104

                           90       100       110
                   ....*....|....*....|....*....|....
gi 1758362338  321 IDAYMVAQNPGVWMLSCQNLNHLKAGLQAFFQVR 354
Cdd:cd13906    105 VDIAFVADNPGDWMFHCHILEHQETGMMGVIRVA 138
CuRO_3_Fet3p cd13899
The third Cupredoxin domain of multicopper oxidase Fet3p; Fet3p catalyzes the ferroxidase ...
 974-1052 9.01e-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: 52.64  E-value: 9.01e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1758362338  974 VNWYVMGMGNEIDL---------HTVHFHGHSFQYKHRGVYSSDVFD------------------LFPGTYQTLEMFPQT 1026
Cdd:cd13899     55 TNAFVLNHGEVVELvvnnwdagkHPFHLHGHKFQVVQRSPDVASDDPnppinefpenpmrrdtvmVPPGGSVVIRFRADN 134

                           90       100
                   ....*....|....*....|....*.
gi 1758362338 1027 PGTWLLHCHVTDHVHAGMATTYTVLP 1052
Cdd:cd13899    135 PGVWFFHCHIEWHLEAGLAATFIEAP 160
CuRO_3_MaLCC_like cd13901
The third cupredoxin domain of the fungal laccases similar to Ma-LCC from Melanocarpus ...
 988-1045 9.53e-08

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: 52.61  E-value: 9.53e-08
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1758362338  988 HTVHFHGHSFQ--YKHRGVYSS-------------DVFDLFPGTYQTLEMFPQTPGTWLLHCHVTDHVHAGMA 1045
Cdd:cd13901     81 HPIHLHGHDFYilAQGTGTFDDdgtilnlnnpprrDVAMLPAGGYLVIAFKTDNPGAWLMHCHIAWHASGGLA 153
CuRO_1_McoC_like cd13855
The first cupredoxin domain of a multicopper oxidase McoC and similar proteins; This family ...
 803-893 1.25e-07

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


Pssm-ID: 259924 [Multi-domain]  Cd Length: 121  Bit Score: 51.32  E-value: 1.25e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1758362338  803 GPPIHANVGDKVKVVFKNMATRPYSIHAHGV----KTESSTVVPTLPGEVRTYTWQIPersgagrEDSACIPWAYYSTVD 878
Cdd:cd13855     32 GPLIEVFEGDTVEITFRNRLPEPTTVHWHGLpvppDQDGNPHDPVAPGNDRVYRFTLP-------QDSAGTYWYHPHPHG 104

                           90
                   ....*....|....*.
gi 1758362338  879 RV-KDLYSGLIGPLIV 893
Cdd:cd13855    105 HTaEQVYRGLAGAFVV 120
CuRO_1_CumA_like cd13861
The first cupredoxin domain of CumA like multicopper oxidase; This multicopper oxidase (MCO) ...
 800-893 1.70e-07

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: 50.70  E-value: 1.70e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1758362338  800 GILGPPIHANVGDKVKVVFKNMATRPYSIHAHGVKTESS-------TVVPTLPGEVRTYTWQIPErsgAGredsacIPWa 872
Cdd:cd13861     28 QVPGPELRVRQGDTLRVRLTNRLPEPTTIHWHGLRLPNAmdgvpglTQPPVPPGESFTYEFTPPD---AG------TYW- 97

                           90       100
                   ....*....|....*....|.
gi 1758362338  873 YYSTVDRVKDLYSGLIGPLIV 893
Cdd:cd13861     98 YHPHVGSQEQLDRGLYGPLIV 118
CuRO_D2_2dMcoN_like cd04202
The second cupredoxin domain of bacterial two domain multicopper oxidase McoN and similar ...
 213-342 2.08e-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: 51.10  E-value: 2.08e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1758362338  213 DQEFVLMFSvvdenlSWYLEDNIKtfcsepeKVDKDNEDFQesnrMYSINGYTFGSLPGLSMCAADRVKWYLFGMGNevD 292
Cdd:cd04202      1 DRDYTLVLQ------EWFVDPGTT-------PMPPEGMDFN----YFTINGKSFPATPPLVVKEGDRVRIRLINLSM--D 61

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1758362338  293 VHSAFFHG--QALTSRN---------YQTDIINLFPATLIDAYMVAQNPGVWMLSCQNLNH 342
Cdd:cd04202     62 HHPMHLHGhfFLVTATDggpipgsapWPKDTLNVAPGERYDIEFVADNPGDWMFHCHKLHH 122
CuRO_3_CopA cd13896
The third cupredoxin domain of CopA copper resistance protein family; CopA is a multicopper ...
 988-1050 2.67e-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: 50.33  E-value: 2.67e-07
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1758362338  988 HTVHFHGHSFQY-KHRGVYSS--DVFDLFPGTYQTLEMFPQTPGTWLLHCHVTDHVHAGMATTYTV 1050
Cdd:cd13896     50 HPMHLHGHFFQVeNGNGEYGPrkDTVLVPPGETVSVDFDADNPGRWAFHCHNLYHMEAGMMRVVEY 115
CuRO_3_MCO_like_3 cd13909
The third cupredoxin domain of uncharacterized multicopper oxidase; Multicopper Oxidases (MCOs) ...
 988-1051 7.75e-07

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


Pssm-ID: 259976 [Multi-domain]  Cd Length: 137  Bit Score: 49.44  E-value: 7.75e-07
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1758362338  988 HTVHFHGHSF-QYKHRGVYS--SDVFDLFPGTYQTLEMFPQTPGTWLLHCHVTDHVHAGMATTYTVL 1051
Cdd:cd13909     71 HGMHLHGHHFrAILPNGALGpwRDTLLMDRGETREIAFVADNPGDWLLHCHMLEHAAAGMMSWFRVT 137
CuRO_1_Diphenol_Ox cd13857
The first cupredoxin domain of fungal laccase, diphenol oxidase; Diphenol oxidase belongs to ...
 803-893 1.16e-06

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: 48.41  E-value: 1.16e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1758362338  803 GPPIHANVGDKVKVVFKNMATRPYSIHAHGVKTESS---------TVVPTLPGEVRTYTWQIPERSGAgredsaciPW-- 871
Cdd:cd13857     30 GPLIEANQGDRIVVHVTNELDEPTSIHWHGLFQNGTnwmdgtagiTQCPIPPGGSFTYNFTVDGQYGT--------YWyh 101

                           90       100
                   ....*....|....*....|...
gi 1758362338  872 AYYSTvdrvkdLYS-GLIGPLIV 893
Cdd:cd13857    102 SHYST------QYAdGLVGPLIV 118
CuRO_1_2dMco_1 cd13860
The first cupredoxin domain of bacteria two domain multicopper oxidase; This subfamily ...
 94-197 1.24e-06

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: 48.35  E-value: 1.24e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1758362338   94 GPVIKAEVEDKVYVHLKNLASRIYTFHAHGVTYTKEYEGAvyPDNTtdfQRAddkVLPGQQYVYVLHANEPSpgegdsnc 173
Cdd:cd13860     31 GPTIEVTEGDRVRILVTNELPEPTTVHWHGLPVPNGMDGV--PGIT---QPP---IQPGETFTYEFTAKQAG-------- 94

                           90       100
                   ....*....|....*....|....
gi 1758362338  174 vTRIYHSHVDAPKDIASGLIGPLI 197
Cdd:cd13860     95 -TYMYHSHVDEAKQEDMGLYGAFI 117
CuRO_1_CumA_like cd13861
The first cupredoxin domain of CumA like multicopper oxidase; This multicopper oxidase (MCO) ...
 87-197 1.53e-06

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


Pssm-ID: 259930 [Multi-domain]  Cd Length: 119  Bit Score: 48.00  E-value: 1.53e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1758362338   87 PAWL---GFLGPVIKAEVEDKVYVHLKNLASRIYTFHAHGVTYTKEYEGAvyPDNTtdfQRAddkVLPGQQYVYVLHAne 163
Cdd:cd13861     21 RTWGyngQVPGPELRVRQGDTLRVRLTNRLPEPTTIHWHGLRLPNAMDGV--PGLT---QPP---VPPGESFTYEFTP-- 90

                           90       100       110
                   ....*....|....*....|....*....|....
gi 1758362338  164 PSPGegdsncvTRIYHSHVDAPKDIASGLIGPLI 197
Cdd:cd13861     91 PDAG-------TYWYHPHVGSQEQLDRGLYGPLI 117
CuRO_1_2DMCO_NIR_like_2 cd14449
The cupredoxin domain 1 of a two-domain laccase related to nitrite reductase; The two-domain ...
 449-513 1.79e-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: 48.42  E-value: 1.79e-06
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1758362338  449 GPVIWAEVGDTIKVTFHNKGQHPLSIQPMGVSFTAENEGTyygppgrsSQQASHVAPKETFTYEW 513
Cdd:cd14449     29 GPVIEVREGDTLKILFRNTLDVPASLHPHGVDYTTASDGT--------GMNASIVAPGDTRIYTW 85
Cu-oxidase pfam00394
Multicopper oxidase; Many of the proteins in this family contain multiple similar copies of ...
 914-1048 2.10e-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: 48.47  E-value: 2.10e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1758362338  914 FLVFDENESWYlDDNIKTYSEHPEKVNKDNEEF-LESNKmHAINGKMFGNLQGLTMHVKDEVNWYVMgMGNEIDLHTVHF 992
Cdd:pfam00394    1 EDYVITLSDWY-HKDAKDLEKELLASGKAPTDFpPVPDA-VLINGKDGASLATLTVTPGKTYRLRII-NVALDDSLNFSI 77

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1758362338  993 HGHSFQY-----KHRGVYSSDVFDLFPG-TYQTLEMFPQTPGTWLLHCHVT-DHVHAGMATTY 1048
Cdd:pfam00394   78 EGHKMTVvevdgVYVNPFTVDSLDIFPGqRYSVLVTANQDPGNYWIVASPNiPAFDNGTAAAI 140
CuRO_1_2DMCO_NIR_like cd11024
The cupredoxin domain 1 of a two-domain laccase related to nitrite reductase; The two-domain ...
 94-197 3.28e-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. 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: 47.27  E-value: 3.28e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1758362338   94 GPVIKAEVEDKVYVHLKNLASRIYTFHAHGVTYTKEyEGAVYPDnttdfqraddkVLPGQQYVYVLHANEPSpgegdsnc 173
Cdd:cd11024     32 GPTLRATEGDLVRIHFINTGDHPHTIHFHGIHDAAM-DGTGLGP-----------IMPGESFTYEFVAEPAG-------- 91

                           90       100
                   ....*....|....*....|....*
gi 1758362338  174 vTRIYHSHVDAPKD-IASGLIGPLI 197
Cdd:cd11024     92 -THLYHCHVQPLKEhIAMGLYGAFI 115
CuRO_1_2DMCO_NIR_like cd11024
The cupredoxin domain 1 of a two-domain laccase related to nitrite reductase; The two-domain ...
 803-853 3.90e-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. 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: 46.88  E-value: 3.90e-06
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....
gi 1758362338  803 GPPIHANVGDKVKVVFKNMATRPYSIHAHGVKTES---STVVPTLPGEVRTYTW 853
Cdd:cd11024     32 GPTLRATEGDLVRIHFINTGDHPHTIHFHGIHDAAmdgTGLGPIMPGESFTYEF 85
CuRO_1_2dMco_1 cd13860
The first cupredoxin domain of bacteria two domain multicopper oxidase; This subfamily ...
 449-550 4.03e-06

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: 46.81  E-value: 4.03e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1758362338  449 GPVIWAEVGDTIKVTFHNKGQHPLSIQPMGVSFTAEnegtYYGPPGrssQQASHVAPKETFTYEWTVpkEMGPTYadpvc 528
Cdd:cd13860     31 GPTIEVTEGDRVRILVTNELPEPTTVHWHGLPVPNG----MDGVPG---ITQPPIQPGETFTYEFTA--KQAGTY----- 96

                           90       100
                   ....*....|....*....|..
gi 1758362338  529 lskMYYSGVDPTKDIFTGLIGP 550
Cdd:cd13860     97 ---MYHSHVDEAKQEDMGLYGA 115
Cu-oxidase_3 pfam07732
Multicopper oxidase; This entry contains many divergent copper oxidase-like domains that are ...
 801-860 7.09e-06

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: 46.08  E-value: 7.09e-06
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1758362338  801 ILGPPIHANVGDKVKVVFKNMATRPYSIHAHGV---KTESSTVV------PTLPGEVRTYTWQIPERSG 860
Cdd:pfam07732   24 FPGPTIRVREGDTVVVNVTNNLDEPTSIHWHGLqqrGTPWMDGVpgvtqcPIPPGQSFTYRFQVKQQAG 92
CuRO_1_Diphenol_Ox cd13857
The first cupredoxin domain of fungal laccase, diphenol oxidase; Diphenol oxidase belongs to ...
 449-553 1.21e-05

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: 45.71  E-value: 1.21e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1758362338  449 GPVIWAEVGDTIKVTFHNKGQHPLSIQPMGVSFtaenEGTYY--GPPGRSsqqASHVAPKETFTYEWTVPKEMGPTYadp 526
Cdd:cd13857     30 GPLIEANQGDRIVVHVTNELDEPTSIHWHGLFQ----NGTNWmdGTAGIT---QCPIPPGGSFTYNFTVDGQYGTYW--- 99

                           90       100
                   ....*....|....*....|....*...
gi 1758362338  527 vclskmYYSGVDPTK-DiftGLIGPMKI 553
Cdd:cd13857    100 ------YHSHYSTQYaD---GLVGPLIV 118
CuRO_3_Tv-LCC_like cd13903
The third cupredoxin domain of the fungal laccases similar to Tv-LCC from Trametes Versicolor; ...
 982-1045 1.35e-05

The third cupredoxin domain of the fungal laccases similar to Tv-LCC from Trametes Versicolor; This subfamily of fungal laccases includes Tv-LCC from Trametes versicolor and Rs-LCC2 from plant pathogenic fungus Rhizoctonia solani. Laccase is a blue multi-copper enzyme that catalyzes the oxidation of a variety aromatic - notably phenolic and inorganic substances coupled to the reduction of molecular oxygen to water. It has been implicated in a wide spectrum of biological activities and, in particular, plays a key role in morphogenesis, development and lignin metabolism. Although MCOs have diverse functions, majority of them have three cupredoxin domain repeats that include one mononuclear and one trinuclear copper center. The copper ions are bound in several sites: Type 1, Type 2, and/or Type 3. The ensemble of types 2 and 3 copper is called a trinuclear cluster. MCOs oxidize their substrate by accepting electrons at a mononuclear copper center and transferring them to the active site trinuclear copper center. The cupredoxin domain 3 of 3-domain MCOs contains the Type 1 (T1) copper binding site and part the trinuclear copper binding site, which is located at the interface of domains 1 and 3.


Pssm-ID: 259970 [Multi-domain]  Cd Length: 147  Bit Score: 46.12  E-value: 1.35e-05
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1758362338  982 GNEIDLHTVHFHGHSFQYKhRGVYSS----------DVFDL-FPGTYQTLEMFPQTPGTWLLHCHVTDHVHAGMA 1045
Cdd:cd13903     67 GAIGGPHPFHLHGHAFSVV-RSAGSNtynyvnpvrrDVVSVgTPGDGVTIRFVTDNPGPWFLHCHIDWHLEAGLA 140
CuRO_1_2DMCO_NIR_like cd11024
The cupredoxin domain 1 of a two-domain laccase related to nitrite reductase; The two-domain ...
 988-1052 1.41e-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: 1.41e-05
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1758362338  988 HTVHFHGhsfqyKHRGVYSSDVF-DLFPGTYQTLEMFPQTPGTWLLHCHV---TDHVHAGMATTYTVLP 1052
Cdd:cd11024     55 HTIHFHG-----IHDAAMDGTGLgPIMPGESFTYEFVAEPAGTHLYHCHVqplKEHIAMGLYGAFIVDP 118
CuRO_D1_2dMcoN_like cd13859
The first cupredoxin domain of bacterial two domain multicopper oxidase McoN and similar ...
 785-893 1.70e-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: 45.16  E-value: 1.70e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1758362338  785 SFREQVKrraedehlgilGPPIHANVGDKVKVVFKNMATRPYSIHAHGVKTESS---------TVVPTLPGEVRTYTWqI 855
Cdd:cd13859     24 AFNGQVP-----------GPLIHVKEGDDLVVHVTNNTTLPHTIHWHGVLQMGSwkmdgvpgvTQPAIEPGESFTYKF-K 91

                           90       100       110
                   ....*....|....*....|....*....|....*...
gi 1758362338  856 PERSGAgredsaciPWAYYSTVDRVKDLYSGLIGPLIV 893
Cdd:cd13859     92 AERPGT--------LWYHCHVNVNEHVGMRGMWGPLIV 121
CuRO_D1_2dMcoN_like cd13859
The first cupredoxin domain of bacterial two domain multicopper oxidase McoN and similar ...
 94-197 1.83e-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: 45.16  E-value: 1.83e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1758362338   94 GPVIKAEVEDKVYVHLKNLASRIYTFHAHGVTYTKEYEGAVYPDNTtdfQRAddkVLPGQQYVYVLHANEPSpgegdsnc 173
Cdd:cd13859     31 GPLIHVKEGDDLVVHVTNNTTLPHTIHWHGVLQMGSWKMDGVPGVT---QPA---IEPGESFTYKFKAERPG-------- 96

                           90       100
                   ....*....|....*....|....*
gi 1758362338  174 vTRIYHSHVDAPKDIA-SGLIGPLI 197
Cdd:cd13859     97 -TLWYHCHVNVNEHVGmRGMWGPLI 120
CuRO_3_McoC_like cd13902
The third cupredoxin domain of a multicopper oxidase McoC and similar proteins; This family ...
 952-1044 2.04e-05

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


Pssm-ID: 259969 [Multi-domain]  Cd Length: 125  Bit Score: 45.08  E-value: 2.04e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1758362338  952 MHAINGKMFGnlqgltMHVKD------EVN-WYVMgmgNEIDL-HTVHFHGHSFQY-KHRGVYSS-------DVFDLFPG 1015
Cdd:cd13902     20 MFLINGKTFD------MNRIDfvakvgEVEvWEVT---NTSHMdHPFHLHGTQFQVlEIDGNPQKpeyrawkDTVNLPPG 90

                           90       100
                   ....*....|....*....|....*....
gi 1758362338 1016 TYQTLEMFPQTPGTWLLHCHVTDHVHAGM 1044
Cdd:cd13902     91 EAVRIATRQDDPGMWMYHCHILEHEDAGM 119
CuRO_1_CumA_like cd13861
The first cupredoxin domain of CumA like multicopper oxidase; This multicopper oxidase (MCO) ...
 446-550 3.14e-05

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: 44.15  E-value: 3.14e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1758362338  446 GILGPVIWAEVGDTIKVTFHNKGQHPLSIQPMGVSFTAENEGTyygpPGrSSQQAshVAPKETFTYEWTVPKemGPTYad 525
Cdd:cd13861     28 QVPGPELRVRQGDTLRVRLTNRLPEPTTIHWHGLRLPNAMDGV----PG-LTQPP--VPPGESFTYEFTPPD--AGTY-- 96

                           90       100
                   ....*....|....*....|....*
gi 1758362338  526 pvclskMYYSGVDPTKDIFTGLIGP 550
Cdd:cd13861     97 ------WYHPHVGSQEQLDRGLYGP 115
Cu-oxidase_2 pfam07731
Multicopper oxidase; This entry contains many divergent copper oxidase-like domains that are ...
 251-355 1.03e-04

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: 43.19  E-value: 1.03e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1758362338  251 DFQESNRMYSINGYTFG-SLPGLSMCAADRVKWYLFGMGNevDVHSAFFHG---------------QALTSRNYQT---- 310
Cdd:pfam07731   14 SGNFRRNDWAINGLLFPpNTNVITLPYGTVVEWVLQNTTT--GVHPFHLHGhsfqvlgrgggpwpeEDPKTYNLVDpvrr 91

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*
gi 1758362338  311 DIINLFPATLIDAYMVAQNPGVWMLSCQNLNHLKAGLQAFFQVRD 355
Cdd:pfam07731   92 DTVQVPPGGWVAIRFRADNPGVWLFHCHILWHLDQGMMGQFVVRP 136
CuRO_1_Fet3p cd13851
The first Cupredoxin domain of multicopper oxidase Fet3P; Fet3p catalyzes the ferroxidase ...
 450-523 1.08e-04

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: 43.02  E-value: 1.08e-04
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1758362338  450 PVIWAEVGDTIKVTFHNK-GQHPLSIQPMGVSFTAENEgtYYGPPGrSSQqaSHVAPKETFTYEWTVPKEMGpTY 523
Cdd:cd13851     32 PPIEVNKGDTVVIHATNSlGDQPTSLHFHGLFQNGTNY--MDGPVG-VTQ--CPIPPGQSFTYEFTVDTQVG-TY 100
CuRO_1_CuNIR cd11020
Cupredoxin domain 1 of Copper-containing nitrite reductase; Copper-containing nitrite ...
 449-514 1.31e-04

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


Pssm-ID: 259906 [Multi-domain]  Cd Length: 119  Bit Score: 42.58  E-value: 1.31e-04
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1758362338  449 GPVIWAEVGDTIKVTFHNKGQHPLsiqPMGVSFTAEnegtyYGPPGRSSQQashVAPKETFTYEWT 514
Cdd:cd11020     32 GPVIRVREGDTVELTLTNPGTNTM---PHSIDFHAA-----TGPGGGEFTT---IAPGETKTFSFK 86
SufI COG2132
Multicopper oxidase with three cupredoxin domains (includes cell division protein FtsP and ...
 92-221 1.51e-04

Multicopper oxidase with three cupredoxin domains (includes cell division protein FtsP and spore coat protein CotA) [Cell cycle control, cell division, chromosome partitioning, Inorganic ion transport and metabolism, Cell wall/membrane/envelope biogenesis;


Pssm-ID: 441735 [Multi-domain]  Cd Length: 423  Bit Score: 45.31  E-value: 1.51e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1758362338   92 FLGPVIKAEVEDKVYVHLKN-LASRIyTFHAHGVTYTKEYEGAVYPdnttdfqraddKVLPGQQYVYVLHANEPsPGegd 170
Cdd:COG2132     42 YPGPTIRVREGDRVRVRVTNrLPEPT-TVHWHGLRVPNAMDGVPGD-----------PIAPGETFTYEFPVPQP-AG--- 105

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 1758362338  171 sncvTRIYHSHVDA--PKDIASGLIGPLILckkgslyKEKEKNI---DQEFVLMFS 221
Cdd:COG2132    106 ----TYWYHPHTHGstAEQVYRGLAGALIV-------EDPEEDLpryDRDIPLVLQ 150
PLN02191 PLN02191
L-ascorbate oxidase
 986-1048 1.71e-04

L-ascorbate oxidase


Pssm-ID: 177843 [Multi-domain]  Cd Length: 574  Bit Score: 45.39  E-value: 1.71e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1758362338  986 DLHTVHFHGHSF------QYKHRGVYSSDVFDL-----------FPGTYQTLEMFPQTPGTWLLHCHVTDHVHAGMATTY 1048
Cdd:PLN02191   465 EIHPWHLHGHDFwvlgygDGKFKPGIDEKTYNLknpplrntailYPYGWTAIRFVTDNPGVWFFHCHIEPHLHMGMGVVF 544
CuRO_1_MaLCC_like cd13854
The first cupredoxin domain of the fungal laccases similar to Ma-LCC from Melanocarpus ...
 803-854 2.07e-04

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: 42.23  E-value: 2.07e-04
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1758362338  803 GPPIHANVGDKVKV-VFKNMATRPYSIHAHGVKTESS---------TVVPTLPGEVRTYTWQ 854
Cdd:cd13854     33 GPLIEANWGDTIEVtVINKLQDNGTSIHWHGIRQLNTnwqdgvpgvTECPIAPGDTRTYRFR 94
CuRO_3_AAO cd13893
The third cupredoxin domain of plant Ascorbate oxidase; Ascorbate oxidase catalyzes the ...
 988-1044 2.26e-04

The third cupredoxin domain of plant Ascorbate oxidase; Ascorbate oxidase catalyzes the oxidation of ascorbic acid to dehydroascorbic acid. This multicopper oxidase (MCO) is found in cucurbitaceous plants such as pumpkin, cucumber, and melon. It can detect levels of ascorbic acid and eliminate it. The biological function of ascorbate oxidase is still not clear. Ascorbate oxidase belongs to MCO family which couple oxidation of substrates with reduction of dioxygen to water. MCOs are capable of oxidizing a vast range of substrates, varying from aromatic compounds to inorganic compounds such as metals. Although the members of this family have diverse functions, majority of them have three cupredoxin domain repeats. The copper ions are bound in several sites: Type 1, Type 2, and/or Type 3. The ensemble of types 2 and 3 copper is called a trinuclear cluster. MCOs oxidize their substrate by accepting electrons at a mononuclear copper center and transferring them to the active site trinuclear copper center. The cupredoxin domain 3 of 3-domain MCOs contains the Type 1 (T1) copper binding site and part the trinuclear copper binding site, which is located at the interface of domains 1 and 3.


Pssm-ID: 259960 [Multi-domain]  Cd Length: 155  Bit Score: 42.79  E-value: 2.26e-04
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1758362338  988 HTVHFHGHSFQYKHRGVYS-----------------SDVFDLFPGTYQTLEMFPQTPGTWLLHCHVTDHVHAGM 1044
Cdd:cd13893     67 HPWHLHGHDFWVLGYGLGGfdpaadpsslnlvnppmRNTVTIFPYGWTALRFKADNPGVWAFHCHIEWHFHMGM 140
CuRO_1_AAO cd13845
The first cupredoxin domain of plant Ascorbate oxidase; Ascorbate oxidase catalyzes the ...
 91-198 3.23e-04

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: 41.66  E-value: 3.23e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1758362338   91 GFLGPVIKAEVEDKVYVHLKN-LASRIYTFHAHGVtytkEYEGAVYPDNTTDFQRAddKVLPGQQYVYVLHANEPSpgeg 169
Cdd:cd13845     27 QFPGPTIRATAGDTIVVELENkLPTEGVAIHWHGI----RQRGTPWADGTASVSQC--PINPGETFTYQFVVDRPG---- 96

                           90       100
                   ....*....|....*....|....*....
gi 1758362338  170 dsncvTRIYHSHVDAPKdiASGLIGPLIL 198
Cdd:cd13845     97 -----TYFYHGHYGMQR--SAGLYGSLIV 118
Cu-oxidase_3 pfam07732
Multicopper oxidase; This entry contains many divergent copper oxidase-like domains that are ...
 447-523 3.56e-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: 3.56e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1758362338  447 ILGPVIWAEVGDTIKVTFHNKGQHPLSI------QPmgvsftaeNEGTYYGPPGrSSQQAshVAPKETFTYEWTVPKEMG 520
Cdd:pfam07732   24 FPGPTIRVREGDTVVVNVTNNLDEPTSIhwhglqQR--------GTPWMDGVPG-VTQCP--IPPGQSFTYRFQVKQQAG 92


                   ...
gi 1758362338  521 pTY 523
Cdd:pfam07732   93 -TY 94
CuRO_3_tcLLC2_insect_like cd13905
The third cupredoxin domain of the insect laccases similar to laccase 2 in Tribolium castaneum; ...
 988-1045 3.69e-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: 3.69e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1758362338  988 HTVHFHGHSFQ--YKHRGVYSSDVFDLFPGTYQTLEMFPQT-------------------------------PGTWLLHC 1034
Cdd:cd13905     70 HPFHLHGHSFYvlGMGFPGYNSTTGEILSQNWNNKLLDRGGlpgrnlvnpplkdtvvvpnggyvvirfradnPGYWLLHC 149

                           90
                   ....*....|.
gi 1758362338 1035 HVTDHVHAGMA 1045
Cdd:cd13905    150 HIEFHLLEGMA 160
CuRO_1_2DMCO_NIR_like_2 cd14449
The cupredoxin domain 1 of a two-domain laccase related to nitrite reductase; The two-domain ...
 94-198 3.74e-04

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


Pssm-ID: 259991 [Multi-domain]  Cd Length: 135  Bit Score: 41.87  E-value: 3.74e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1758362338   94 GPVIKAEVEDKVYVHLKNLASRIYTFHAHGVTYTKEYEGAVYPDNTtdfqraddkVLPGQQYVYVLHANEPSPGEGDSNC 173
Cdd:cd14449     29 GPVIEVREGDTLKILFRNTLDVPASLHPHGVDYTTASDGTGMNASI---------VAPGDTRIYTWRTHGGYRRADGSWA 99

                           90       100       110
                   ....*....|....*....|....*....|...
gi 1758362338  174 V----TRIYHSHV----DAPKDIASGLIGPLIL 198
Cdd:cd14449    100 EgtagYWHYHDHVfgteHGTEGLSRGLYGALIV 132
CuRO_1_CuNIR_like cd04201
Cupredoxin domain 1 of Copper-containing nitrite reductase and two-domain laccase; ...
 956-1052 4.31e-04

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


Pssm-ID: 259864 [Multi-domain]  Cd Length: 120  Bit Score: 41.32  E-value: 4.31e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1758362338  956 NGKMFGNLqgLTMHVKDEVNWYVMGMGNEIDLHTVHFHGHSFQYKHRGVYSSDvfdlfPGTYQTLEMFPQTPGTWLLHCH 1035
Cdd:cd04201     27 DGDIPGPM--LRVREGDTVELHFSNNPSSTMPHNIDFHAATGAGGGAGATFIA-----PGETSTFSFKATQPGLYVYHCA 99

                           90       100
                   ....*....|....*....|
gi 1758362338 1036 VTD---HVHAGMATTYTVLP 1052
Cdd:cd04201    100 VAPvpmHIANGMYGLILVEP 119
CuRO_1_2dMco_1 cd13860
The first cupredoxin domain of bacteria two domain multicopper oxidase; This subfamily ...
 803-893 4.79e-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: 4.79e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1758362338  803 GPPIHANVGDKVKVVFKNMATRPYSIHAHGVKTESS-------TVVPTLPGEVRTYTWQIpERSGAgredsacipWAYYS 875
Cdd:cd13860     31 GPTIEVTEGDRVRILVTNELPEPTTVHWHGLPVPNGmdgvpgiTQPPIQPGETFTYEFTA-KQAGT---------YMYHS 100

                           90
                   ....*....|....*...
gi 1758362338  876 TVDRVKDLYSGLIGPLIV 893
Cdd:cd13860    101 HVDEAKQEDMGLYGAFIV 118
CuRO_1_McoC_like cd13855
The first cupredoxin domain of a multicopper oxidase McoC and similar proteins; This family ...
 449-523 8.89e-04

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: 40.15  E-value: 8.89e-04
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1758362338  449 GPVIWAEVGDTIKVTFHNKGQHPLSIQPMGVSFTAENEGTYYGPpgrssqqashVAPKETFTYEWTVPKEMGPTY 523
Cdd:cd13855     32 GPLIEVFEGDTVEITFRNRLPEPTTVHWHGLPVPPDQDGNPHDP----------VAPGNDRVYRFTLPQDSAGTY 96
CuRO_1_Abr2_like cd13850
The first cupredoxin domain of a group of fungal Laccases similar to Abr2 from Aspergillus ...
 803-861 9.55e-04

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: 39.97  E-value: 9.55e-04
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1758362338  803 GPPIHANVGDKVKVVFKNMATRPYSIHAHGVK---TESSTVVPTL------PGEVRTYTWQIPERSGA 861
Cdd:cd13850     28 GPPIILDEGDEVEILVTNNLPVNTTIHFHGILqrgTPWSDGVPGVtqwpiqPGGSFTYRWKAEDQYGL 95
CuRO_1_CuNIR_like cd04201
Cupredoxin domain 1 of Copper-containing nitrite reductase and two-domain laccase; ...
 447-513 1.44e-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: 39.78  E-value: 1.44e-03
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1758362338  447 ILGPVIWAEVGDTIKVTFHNkgqHPLSIQPMGVSFTAENegtyyGPPGRSSqqASHVAPKETFTYEW 513
Cdd:cd04201     30 IPGPMLRVREGDTVELHFSN---NPSSTMPHNIDFHAAT-----GAGGGAG--ATFIAPGETSTFSF 86
CuRO_3_AAO_like_2 cd13895
The third cupredoxin domain of Ascorbate oxidase homologs; This family includes fungal ...
 986-1047 1.63e-03

The third cupredoxin domain of Ascorbate oxidase homologs; This family includes fungal proteins with similarity to ascorbate oxidase. Ascorbate oxidase catalyzes the oxidation of ascorbic acid to dehydroascorbic acid. It can detect levels of ascorbic acid and eliminate it. The biological function of ascorbate oxidase is still not clear. Ascorbate oxidase belongs to multicopper oxidase (MCO) family which couple oxidation of substrates with reduction of dioxygen to water. MCOs are capable of oxidizing a vast range of substrates, varying from aromatic compounds to inorganic compounds such as metals. Although the members of this family have diverse functions, majority of them have three cupredoxin domain repeats. The copper ions are bound in several sites: Type 1, Type 2, and/or Type 3. The ensemble of types 2 and 3 copper is called a trinuclear cluster. MCOs oxidize their substrate by accepting electrons at a mononuclear copper center and transferring them to the active site trinuclear copper center. The cupredoxin domain 3 of 3-domain MCOs contains the Type 1 (T1) copper binding site and part the trinuclear copper binding site, which is located at the interface of domains 1 and 3.


Pssm-ID: 259962 [Multi-domain]  Cd Length: 188  Bit Score: 40.76  E-value: 1.63e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1758362338  986 DLHTVHFHGHSFQY--KHRGVYSSDVFD-----------------LFPGTYQTLEMFP-------------QTPGTWLLH 1033
Cdd:cd13895     91 DAHPWHAHGAHYYDlgSGLGTYSATALAneeklrgynpirrdttmLYRYGGKGYYPPPgtgsgwrawrlrvDDPGVWMLH 170

                           90
                   ....*....|....
gi 1758362338 1034 CHVTDHVHAGMATT 1047
Cdd:cd13895    171 CHILQHMIMGMQTV 184
CuRO_1_Fet3p cd13851
The first Cupredoxin domain of multicopper oxidase Fet3P; Fet3p catalyzes the ferroxidase ...
 804-860 1.81e-03

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: 39.17  E-value: 1.81e-03
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1758362338  804 PPIHANVGDKVKV-VFKNMATRPYSIHAHGVKTESS---------TVVPTLPGEVRTYTWQIPERSG 860
Cdd:cd13851     32 PPIEVNKGDTVVIhATNSLGDQPTSLHFHGLFQNGTnymdgpvgvTQCPIPPGQSFTYEFTVDTQVG 98
CuRO_3_MCO_like_4 cd13910
The third cupredoxin domain of uncharacterized multicopper oxidase; Multicopper Oxidases (MCOs) ...
 988-1045 1.90e-03

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


Pssm-ID: 259977 [Multi-domain]  Cd Length: 166  Bit Score: 40.36  E-value: 1.90e-03
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1758362338  988 HTVHFHGHSFQYK--HRGVYSSDVFDLFPGTYQTLE--MFPQT-----------------PGTWLLHCHVTDHVHAGMA 1045
Cdd:cd13910     83 HPFHLHGHKFWVLgsGDGRYGGGGYTAPDGTSLNTTnpLRRDTvsvpgfgwavlrfvadnPGLWAFHCHILWHMAAGML 161
ascorbase TIGR03388
L-ascorbate oxidase, plant type; Members of this protein family are the copper-containing ...
 982-1044 2.83e-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: 41.66  E-value: 2.83e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1758362338  982 GNEIDLHTVHFHGHSF------QYKHRGVYSSDVFDL-----------FPGTYQTLEMFPQTPGTWLLHCHVTDHVHAGM 1044
Cdd:TIGR03388  438 GNNSETHPWHLHGHDFwvlgygEGKFRPGVDEKSYNLknpplrntvviFPYGWTALRFVADNPGVWAFHCHIEPHLHMGM 517
CuRO_1_Diphenol_Ox cd13857
The first cupredoxin domain of fungal laccase, diphenol oxidase; Diphenol oxidase belongs to ...
 92-198 2.98e-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: 38.78  E-value: 2.98e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1758362338   92 FLGPVIKAEVEDKVYVHLKNLASRIYTFHAHGVTytkeYEGAVYPDNTTDFQRAddKVLPGQQYVYVLHANEPSPgegds 171
Cdd:cd13857     28 FPGPLIEANQGDRIVVHVTNELDEPTSIHWHGLF----QNGTNWMDGTAGITQC--PIPPGGSFTYNFTVDGQYG----- 96

                           90       100
                   ....*....|....*....|....*..
gi 1758362338  172 ncvTRIYHSHVDAPKdiASGLIGPLIL 198
Cdd:cd13857     97 ---TYWYHSHYSTQY--ADGLVGPLIV 118
CuRO_3_LCC_plant cd13897
The third cupredoxin domain of the plant laccases; Laccase is a blue multicopper oxidase (MCO) ...
 988-1050 3.06e-03

The third cupredoxin domain of the plant laccases; Laccase is a blue multicopper oxidase (MCO) which catalyzes the oxidation of a variety aromatic - notably phenolic and inorganic substances coupled to the reduction of molecular oxygen to water. Laccase has been implicated in a wide spectrum of biological activities and, in particular, plays a key role in morphogenesis, development and lignin metabolism. Plants usually express multiple laccase genes, but their precise physiological/biochemical roles remain largely unclear. MCOs are capable of oxidizing a vast range of substrates, varying from aromatic compounds to inorganic compounds such as metals. Although the members of this family have diverse functions, majority of them have three cupredoxin domain repeats. The copper ions are bound in several sites: Type 1, Type 2, and/or Type 3. The ensemble of types 2 and 3 copper is called a trinuclear cluster. MCOs oxidize their substrate by accepting electrons at a mononuclear copper center and transferring them to the active site trinuclear copper center. The cupredoxin domain 3 of 3-domain MCOs contains the Type 1 (T1) copper binding site and part the trinuclear copper binding site, which is located at the interface of domains 1 and 3.


Pssm-ID: 259964 [Multi-domain]  Cd Length: 139  Bit Score: 39.16  E-value: 3.06e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1758362338  988 HTVHFHGHSFQYKHRGV--Y--SSDV--FDLF-----------PGTYQTLEMFPQTPGTWLLHCHVTDHVHAGMATTYTV 1050
Cdd:cd13897     57 HPMHLHGFDFYVVGRGFgnFdpSTDPatFNLVdpplrntvgvpRGGWAAIRFVADNPGVWFMHCHFERHTSWGMATVFIV 136
CuRO_1_LCC_plant cd13849
The first cupredoxin domain of plant laccases; Laccase is a blue multicopper oxidase (MCO) ...
 803-834 5.37e-03

The first cupredoxin domain of plant laccases; Laccase is a blue multicopper oxidase (MCO) which catalyzes the oxidation of a variety aromatic - notably phenolic and inorganic substances coupled to the reduction of molecular oxygen to water. Laccase has been implicated in a wide spectrum of biological activities and, in particular, plays a key role in morphogenesis, development and lignin metabolism. Plants usually express multiple laccase genes, but their precise physiological/biochemical roles remain largely unclear. MCOs are capable of oxidizing a vast range of substrates, varying from aromatic compounds to inorganic compounds such as metals. Although the members of this family have diverse functions, majority of them have three cupredoxin domain repeats. The copper ions are bound in several sites: Type 1, Type 2, and/or Type 3. The ensemble of types 2 and 3 copper is called a trinuclear cluster. MCOs oxidize their substrate by accepting electrons at a mononuclear copper center and transferring them to the active site trinuclear copper center. The cupredoxin domain 1 of 3-domain MCOs contains part the trinuclear copper binding site, which is located at the interface of domains 1 and 3.


Pssm-ID: 259918 [Multi-domain]  Cd Length: 117  Bit Score: 38.01  E-value: 5.37e-03
                           10        20        30
                   ....*....|....*....|....*....|..
gi 1758362338  803 GPPIHANVGDKVKVVFKNMATRPYSIHAHGVK 834
Cdd:cd13849     28 GPTIRVHEGDTVVVNVTNRSPYNITIHWHGIR 59
CuRO_3_Abr2_like cd13898
The third cupredoxin domain of a group of fungal Laccases similar to Abr2 from Aspergillus ...
 1025-1045 5.38e-03

The third cupredoxin domain of a group of fungal Laccases similar to Abr2 from Aspergillus fumigatus; Abr2 is involved in conidial pigment biosynthesis in Aspergillus fumigatus. Laccase is a blue multi-copper enzyme that catalyzes the oxidation of a variety aromatic - notably phenolic and inorganic substances coupled to the reduction of molecular oxygen to water. Laccase has been implicated in a wide spectrum of biological activities and, in particular, plays a key role in morphogenesis, development and lignin metabolism in fungi and plants. Like other related multicopper oxidases (MCOs), laccase is composed of three cupredoxin domains that include one mononuclear and one trinuclear copper center. The copper ions are bound in several sites: Type 1, Type 2, and/or Type 3. The ensemble of types 2 and 3 copper is called a trinuclear cluster. MCOs oxidize their substrate by accepting electrons at a mononuclear copper center and transferring them to the active site trinuclear copper center. The cupredoxin domain 3 of 3-domain MCOs contains the Type 1 (T1) copper binding site and part the trinuclear copper binding site, which is located at the interface of domains 1 and 3.


Pssm-ID: 259965 [Multi-domain]  Cd Length: 164  Bit Score: 38.78  E-value: 5.38e-03
                           10        20
                   ....*....|....*....|.
gi 1758362338 1025 QTPGTWLLHCHVTDHVHAGMA 1045
Cdd:cd13898    138 VNPGAWLLHCHIQSHLAGGMA 158
CuRO_1_LCC_plant cd13849
The first cupredoxin domain of plant laccases; Laccase is a blue multicopper oxidase (MCO) ...
 449-520 5.69e-03

The first cupredoxin domain of plant laccases; Laccase is a blue multicopper oxidase (MCO) which catalyzes the oxidation of a variety aromatic - notably phenolic and inorganic substances coupled to the reduction of molecular oxygen to water. Laccase has been implicated in a wide spectrum of biological activities and, in particular, plays a key role in morphogenesis, development and lignin metabolism. Plants usually express multiple laccase genes, but their precise physiological/biochemical roles remain largely unclear. MCOs are capable of oxidizing a vast range of substrates, varying from aromatic compounds to inorganic compounds such as metals. Although the members of this family have diverse functions, majority of them have three cupredoxin domain repeats. The copper ions are bound in several sites: Type 1, Type 2, and/or Type 3. The ensemble of types 2 and 3 copper is called a trinuclear cluster. MCOs oxidize their substrate by accepting electrons at a mononuclear copper center and transferring them to the active site trinuclear copper center. The cupredoxin domain 1 of 3-domain MCOs contains part the trinuclear copper binding site, which is located at the interface of domains 1 and 3.


Pssm-ID: 259918 [Multi-domain]  Cd Length: 117  Bit Score: 37.62  E-value: 5.69e-03
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1758362338  449 GPVIWAEVGDTIKVTFHNKGQHPLSIQPMGVS--FTAENEGTYYgppgrsSQQAsHVAPKETFTYEWTVPKEMG 520
Cdd:cd13849     28 GPTIRVHEGDTVVVNVTNRSPYNITIHWHGIRqlRSGWADGPAY------ITQC-PIQPGQSYTYRFTVTGQEG 94
CuRO_3_MCO_like_1 cd13907
The third cupredoxin domain of uncharacterized multicopper oxidase; Multicopper Oxidases (MCOs) ...
 979-1050 6.25e-03

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


Pssm-ID: 259974 [Multi-domain]  Cd Length: 154  Bit Score: 38.62  E-value: 6.25e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1758362338  979 MGMGNEIDL-HTVHFHGHSFQ-------YKHRGVYSS-----------DVFDLFPGTYQTLEM-FPQTPGTWLLHCHVTD 1038
Cdd:cd13907     62 MMMGGMMAMpHPIHLHGVQFQvlersvgPKDRAYWATvkdgfidegwkDTVLVMPGERVRIIKpFDDYKGLFLYHCHNLE 141

                           90
                   ....*....|..
gi 1758362338 1039 HVHAGMATTYTV 1050
Cdd:cd13907    142 HEDMGMMRNFLV 153
CuRO_1_CuNIR cd11020
Cupredoxin domain 1 of Copper-containing nitrite reductase; Copper-containing nitrite ...
 803-861 8.57e-03

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: 37.19  E-value: 8.57e-03
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1758362338  803 GPPIHANVGDKVKVVFKNMATR--PYSIHAHGVKTE-SSTVVPTLPGEVRTYTWqIPERSGA 861
Cdd:cd11020     32 GPVIRVREGDTVELTLTNPGTNtmPHSIDFHAATGPgGGEFTTIAPGETKTFSF-KALYPGV 92
CuRO_1_tcLCC2_insect_like cd13858
The first cupredoxin domain of insect laccases similar to laccase 2 in Tribolium castaneum; ...
 803-893 9.38e-03

The first cupredoxin domain of insect laccases similar to laccase 2 in Tribolium castaneum; This multicopper oxidase (MCO) family includes the majority of insect laccases. One member of the family is laccase 2 from Tribolium castaneum. Laccase 2 is required for beetle cuticle tanning. Laccase (polyphenol oxidase EC 1.10.3.2) is a blue multi-copper enzyme that catalyzes the oxidation of a variety of organic substrates coupled to the reduction of molecular oxygen to water. It displays broad substrate specificity, catalyzing the oxidation of a wide variety of aromatic - notably phenolic and inorganic substances. Laccase has been implicated in a wide spectrum of biological activities and, in particular, plays a key role in morphogenesis, development and lignin metabolism in fungi, plants and insects. Although MCOs have diverse functions, majority of them have three cupredoxin domain repeats that include one mononuclear and one trinuclear copper center. The copper ions are bound in several sites: Type 1, Type 2, and/or Type 3. The ensemble of types 2 and 3 copper is called a trinuclear cluster. MCOs oxidize their substrate by accepting electrons at a mononuclear copper center and transferring them to the active site trinuclear copper center. The cupredoxin domain 1 of 3-domain MCOs contains part the trinuclear copper binding site, which is located at the interface of domains 1 and 3.


Pssm-ID: 259927 [Multi-domain]  Cd Length: 105  Bit Score: 36.75  E-value: 9.38e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1758362338  803 GPPIHANVGDKVKVVFKN-MATRPYSIHAHGVKTESS---------TVVPTLPGEVRTYTWqIPERSGagredsacIPWa 872
Cdd:cd13858     16 GPSIEVCEGDTVVVDVKNrLPGESTTIHWHGIHQRGTpymdgvpmvTQCPILPGQTFRYKF-KADPAG--------THW- 85

                           90       100
                   ....*....|....*....|...
gi 1758362338  873 YYSTV--DRVKdlysGLIGPLIV 893
Cdd:cd13858     86 YHSHSgtQRAD----GLFGALIV 104
 
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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