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Conserved domains on  [gi|1159645229|gb|OPJ75537|]
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ceruloplasmin [Patagioenas fasciata monilis]

Protein Classification

multicopper oxidase( domain architecture ID 10362973)

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

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
CuRO_3_ceruloplasmin cd04224
The third cupredoxin domain of Ceruloplasmin; Ceruloplasmin is a multicopper oxidase essential ...
 371-568 7.57e-123

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: 374.12  E-value: 7.57e-123
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1159645229  371 RLRRYFIAAEEIIWNYGPSAMNGFTGQELIA-DSESRVFFEQSEMRIGGSYRKAVYKEYTDSSFTERKKRLAEEAHLGLL 449
Cdd:cd04224      2 KVRHYFIAAEEIMWDYAPSGKNLFTGQNLTApGSDSEVFFQRNETRIGGTYWKVRYVEYTDATFTTRKHRSKEEEHLGIL 81

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1159645229  450 GPVIKAEVGESIRVTFRNNASRPFSIQPHGLSYRKSDEGASYgasSRGTESPASHVSPGATFTYEWNVPEDVGPTDQDPD 529
Cdd:cd04224     82 GPVIRAEVGDTIKVTFRNKASRPFSIQPHGVFYEKNYEGAMY---RDGDPSPGSHVSPGETFTYEWTVPEGVGPTNQDPP 158

                          170       180       190
                   ....*....|....*....|....*....|....*....
gi 1159645229  530 CLTWLYYSAVDAVRDTSSGLVGPLLVCRKGALLPSGKQK 568
Cdd:cd04224    159 CLTYLYFSAVDPVRDTNSGLVGPLLVCKKGSLNANGRQK 197
Cupredoxin super family cl19115
Cupredoxin superfamily; Cupredoxins contain type I copper centers and are involved in ...
 22-204 3.83e-106

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: 329.38  E-value: 3.83e-106
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1159645229   22 REYWVGIAEREWNYAPGAASAPSAQLFAEHEQARAFLQRGPRRIGSTYKKAVYTQYTSQLYDVAVDKPSWLGFLGPIIKG 101
Cdd:cd04222      1 REYYIGIRETQWDYAPSGKNLITNQTFDDDEHASVFLKRGPDRIGRVYKKAVYLQYTDDTYRTEIEKPVWLGFLGPILKA 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1159645229  102 EVGDSIVIHLKNFASRNYTLHPHGVTYTKENEGALYPDGTGGLQKRDDAVEPGGQFTYTWDVSEDQGPAAGDADCVTRAY 181
Cdd:cd04222     81 EVGDVIVVHLKNFASRPYSLHPHGVFYNKENEGALYPDNTSGFEKADDAVPPGGSYTYTWTVPEEQAPTKADANCLTRIY 160

                          170       180
                   ....*....|....*....|...
gi 1159645229  182 HSHIDAPRDVASGLVGPLIICRK 204
Cdd:cd04222    161 HSHIDAPKDIASGLIGPLIICKK 183
CuRO_5_ceruloplasmin cd04225
The fifth cupredoxin domain of Ceruloplasmin; Ceruloplasmin is a multicopper oxidase essential ...
 728-898 2.01e-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: 324.42  E-value: 2.01e-104
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1159645229  728 KTYYIAAVEVEWDYSPNRTWEFERHQYLEDSPGNQFLNKEDKFIGSKYRKAVYREYTDGTFSTPKHRAEEQQHLEIQGPL 807
Cdd:cd04225      1 RTYYIAAEEVEWDYSPQRTWEQELHNTHEESPGNAFLNKGDKFIGSKYKKVVYREYTDDTFSVPKERTAEEEHLGILGPL 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1159645229  808 LMSNIGDKIVIVFKNLASRPYSIHAHGVKTDSSAVAVTNPGETKTYVWKIPGRSSSERGDPPCIAWAYHSAVDMVKDTYS 887
Cdd:cd04225     81 IHAEVGEKVKIVFKNMASRPYSIHAHGVKTDSSWVAPTEPGETQTYTWKIPERSGPGVEDSNCISWAYYSTVDQIKDLYS 160

                          170
                   ....*....|.
gi 1159645229  888 GLIGTLVVCHR 898
Cdd:cd04225    161 GLIGPLVICRR 171
CuRO_6_ceruloplasmin cd11012
The sixth cupredoxin domain of Ceruloplasmin; Ceruloplasmin is a multicopper oxidase essential ...
 909-1053 1.11e-97

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: 305.25  E-value: 1.11e-97
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1159645229  909 KVQFALLFMVFDENESWYLDENIKTYSPNPHLVDKEDEEFLESNKMHAINGKVFGNLGGLTMHVGDRVSWYLMGMGNEID 988
Cdd:cd11012      1 KLEFALLFLVFDENESWYLDENIKTYSDHPEKVNKEDEEFIESNKMHAINGKVFGNLQGLTMHVGDEVYWYLMGMGNEID 80

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1159645229  989 IHTAHFHGHSFDYKQTGVYRADVFDLFPGTFQTVEMIPRNPGTWLLHCHVTDHIHAGMETTYTVL 1053
Cdd:cd11012     81 IHTAHFHGHSFDYKHRGVYRSDVFDLFPGTFQTVEMIPRTPGTWLLHCHVTDHIHAGMETTYTVL 145
CuRO_2_ceruloplasmin cd11021
The second cupredoxin domain of Ceruloplasmin; Ceruloplasmin is a multicopper oxidase ...
 216-356 4.31e-95

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


:

Pssm-ID: 259907 [Multi-domain]  Cd Length: 141  Bit Score: 298.23  E-value: 4.31e-95
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1159645229  216 DAEFILMFSVMDENLSWYLEDNIRTYCSEPSEVDKDDEDFQESNKMHSINGYMYGYLPNLTMCVEDKVKWHLFGMGNEAD 295
Cdd:cd11021      1 DREFVLMFSVVDENLSWYLDENIKTYCSEPAKVDKDDEDFQESNKMHSINGYTFGNLPGLSMCAGDRVKWHLFGMGNEVD 80

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1159645229  296 IHSAYFHGQTLIERHHRVDTISLFPATFVDAVMVPRTPGEWLLSCQVNDHIQGGMQALFKV 356
Cdd:cd11021     81 IHSAFFHGQTLTDRGHRTDTINLFPATFVTAEMVAQNPGKWLLSCQVNDHLKAGMQAFYEV 141
CuRO_4_ceruloplasmin cd11022
The fourth cupredoxin domain of Ceruloplasmin; Ceruloplasmin is a multicopper oxidase ...
 573-714 3.51e-94

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: 295.93  E-value: 3.51e-94
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1159645229  573 EFFLLATVFDENLSWYLDDNILMFTLNPNKIDKDDEDFQESNKMHSINGYMYGNQPGLRMCKGSVVSWHLMGLGSEVDVH 652
Cdd:cd11022      3 EFFLLFTVFDENESWYLDENIQQFTLDPRSVDKEDEDFQESNKMHSINGYMYGNQPGLDMCKGDTVSWHLFGLGTETDVH 82

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1159645229  653 GIYFSENTFTARGTRRDTANLFPHTFLTAIMKPDSEGVFEVSCLTTDHYTGGMKQNYRVEQC 714
Cdd:cd11022     83 GIYFSGNTFLLQGTRRDTANLFPHTSVTAIMQPDNEGTFEVNCQTTDHYSAGMRQIYTVSQC 144
 
Name Accession Description Interval E-value
CuRO_3_ceruloplasmin cd04224
The third cupredoxin domain of Ceruloplasmin; Ceruloplasmin is a multicopper oxidase essential ...
 371-568 7.57e-123

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: 374.12  E-value: 7.57e-123
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1159645229  371 RLRRYFIAAEEIIWNYGPSAMNGFTGQELIA-DSESRVFFEQSEMRIGGSYRKAVYKEYTDSSFTERKKRLAEEAHLGLL 449
Cdd:cd04224      2 KVRHYFIAAEEIMWDYAPSGKNLFTGQNLTApGSDSEVFFQRNETRIGGTYWKVRYVEYTDATFTTRKHRSKEEEHLGIL 81

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1159645229  450 GPVIKAEVGESIRVTFRNNASRPFSIQPHGLSYRKSDEGASYgasSRGTESPASHVSPGATFTYEWNVPEDVGPTDQDPD 529
Cdd:cd04224     82 GPVIRAEVGDTIKVTFRNKASRPFSIQPHGVFYEKNYEGAMY---RDGDPSPGSHVSPGETFTYEWTVPEGVGPTNQDPP 158

                          170       180       190
                   ....*....|....*....|....*....|....*....
gi 1159645229  530 CLTWLYYSAVDAVRDTSSGLVGPLLVCRKGALLPSGKQK 568
Cdd:cd04224    159 CLTYLYFSAVDPVRDTNSGLVGPLLVCKKGSLNANGRQK 197
CuRO_1_ceruloplasmin cd04222
The first cupredoxin domain of Ceruloplasmin; Ceruloplasmin is a multicopper oxidase essential ...
 22-204 3.83e-106

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: 329.38  E-value: 3.83e-106
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1159645229   22 REYWVGIAEREWNYAPGAASAPSAQLFAEHEQARAFLQRGPRRIGSTYKKAVYTQYTSQLYDVAVDKPSWLGFLGPIIKG 101
Cdd:cd04222      1 REYYIGIRETQWDYAPSGKNLITNQTFDDDEHASVFLKRGPDRIGRVYKKAVYLQYTDDTYRTEIEKPVWLGFLGPILKA 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1159645229  102 EVGDSIVIHLKNFASRNYTLHPHGVTYTKENEGALYPDGTGGLQKRDDAVEPGGQFTYTWDVSEDQGPAAGDADCVTRAY 181
Cdd:cd04222     81 EVGDVIVVHLKNFASRPYSLHPHGVFYNKENEGALYPDNTSGFEKADDAVPPGGSYTYTWTVPEEQAPTKADANCLTRIY 160

                          170       180
                   ....*....|....*....|...
gi 1159645229  182 HSHIDAPRDVASGLVGPLIICRK 204
Cdd:cd04222    161 HSHIDAPKDIASGLIGPLIICKK 183
CuRO_5_ceruloplasmin cd04225
The fifth cupredoxin domain of Ceruloplasmin; Ceruloplasmin is a multicopper oxidase essential ...
 728-898 2.01e-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: 324.42  E-value: 2.01e-104
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1159645229  728 KTYYIAAVEVEWDYSPNRTWEFERHQYLEDSPGNQFLNKEDKFIGSKYRKAVYREYTDGTFSTPKHRAEEQQHLEIQGPL 807
Cdd:cd04225      1 RTYYIAAEEVEWDYSPQRTWEQELHNTHEESPGNAFLNKGDKFIGSKYKKVVYREYTDDTFSVPKERTAEEEHLGILGPL 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1159645229  808 LMSNIGDKIVIVFKNLASRPYSIHAHGVKTDSSAVAVTNPGETKTYVWKIPGRSSSERGDPPCIAWAYHSAVDMVKDTYS 887
Cdd:cd04225     81 IHAEVGEKVKIVFKNMASRPYSIHAHGVKTDSSWVAPTEPGETQTYTWKIPERSGPGVEDSNCISWAYYSTVDQIKDLYS 160

                          170
                   ....*....|.
gi 1159645229  888 GLIGTLVVCHR 898
Cdd:cd04225    161 GLIGPLVICRR 171
CuRO_6_ceruloplasmin cd11012
The sixth cupredoxin domain of Ceruloplasmin; Ceruloplasmin is a multicopper oxidase essential ...
 909-1053 1.11e-97

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: 305.25  E-value: 1.11e-97
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1159645229  909 KVQFALLFMVFDENESWYLDENIKTYSPNPHLVDKEDEEFLESNKMHAINGKVFGNLGGLTMHVGDRVSWYLMGMGNEID 988
Cdd:cd11012      1 KLEFALLFLVFDENESWYLDENIKTYSDHPEKVNKEDEEFIESNKMHAINGKVFGNLQGLTMHVGDEVYWYLMGMGNEID 80

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1159645229  989 IHTAHFHGHSFDYKQTGVYRADVFDLFPGTFQTVEMIPRNPGTWLLHCHVTDHIHAGMETTYTVL 1053
Cdd:cd11012     81 IHTAHFHGHSFDYKHRGVYRSDVFDLFPGTFQTVEMIPRTPGTWLLHCHVTDHIHAGMETTYTVL 145
CuRO_2_ceruloplasmin cd11021
The second cupredoxin domain of Ceruloplasmin; Ceruloplasmin is a multicopper oxidase ...
 216-356 4.31e-95

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


Pssm-ID: 259907 [Multi-domain]  Cd Length: 141  Bit Score: 298.23  E-value: 4.31e-95
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1159645229  216 DAEFILMFSVMDENLSWYLEDNIRTYCSEPSEVDKDDEDFQESNKMHSINGYMYGYLPNLTMCVEDKVKWHLFGMGNEAD 295
Cdd:cd11021      1 DREFVLMFSVVDENLSWYLDENIKTYCSEPAKVDKDDEDFQESNKMHSINGYTFGNLPGLSMCAGDRVKWHLFGMGNEVD 80

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1159645229  296 IHSAYFHGQTLIERHHRVDTISLFPATFVDAVMVPRTPGEWLLSCQVNDHIQGGMQALFKV 356
Cdd:cd11021     81 IHSAFFHGQTLTDRGHRTDTINLFPATFVTAEMVAQNPGKWLLSCQVNDHLKAGMQAFYEV 141
CuRO_4_ceruloplasmin cd11022
The fourth cupredoxin domain of Ceruloplasmin; Ceruloplasmin is a multicopper oxidase ...
 573-714 3.51e-94

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: 295.93  E-value: 3.51e-94
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1159645229  573 EFFLLATVFDENLSWYLDDNILMFTLNPNKIDKDDEDFQESNKMHSINGYMYGNQPGLRMCKGSVVSWHLMGLGSEVDVH 652
Cdd:cd11022      3 EFFLLFTVFDENESWYLDENIQQFTLDPRSVDKEDEDFQESNKMHSINGYMYGNQPGLDMCKGDTVSWHLFGLGTETDVH 82

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1159645229  653 GIYFSENTFTARGTRRDTANLFPHTFLTAIMKPDSEGVFEVSCLTTDHYTGGMKQNYRVEQC 714
Cdd:cd11022     83 GIYFSGNTFLLQGTRRDTANLFPHTSVTAIMQPDNEGTFEVNCQTTDHYSAGMRQIYTVSQC 144
Cu-oxidase_2 pfam07731
Multicopper oxidase; This entry contains many divergent copper oxidase-like domains that are ...
 952-1056 7.61e-19

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: 84.02  E-value: 7.61e-19
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1159645229  952 NKMHAINGKVFGNLG-GLTMHVGDRVSWYLMGMGNeiDIHTAHFHGHSFDYKQTGV----------------YRADVFDL 1014
Cdd:pfam07731   19 RNDWAINGLLFPPNTnVITLPYGTVVEWVLQNTTT--GVHPFHLHGHSFQVLGRGGgpwpeedpktynlvdpVRRDTVQV 96

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|..
gi 1159645229 1015 FPGTFQTVEMIPRNPGTWLLHCHVTDHIHAGMETTYTVLPRE 1056
Cdd:pfam07731   97 PPGGWVAIRFRADNPGVWLFHCHILWHLDQGMMGQFVVRPGD 138
Cu-oxidase_3 pfam07732
Multicopper oxidase; This entry contains many divergent copper oxidase-like domains that are ...
 94-201 8.77e-12

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: 63.03  E-value: 8.77e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1159645229   94 FLGPIIKGEVGDSIVIHLKNFASRNYTLHPHGVtytkENEGALYPDGTGGLQKrdDAVEPGGQFTYTWDVSEDQGpaagd 173
Cdd:pfam07732   24 FPGPTIRVREGDTVVVNVTNNLDEPTSIHWHGL----QQRGTPWMDGVPGVTQ--CPIPPGQSFTYRFQVKQQAG----- 92

                           90       100
                   ....*....|....*....|....*...
gi 1159645229  174 adcvTRAYHSHIDAPRdvASGLVGPLII 201
Cdd:pfam07732   93 ----TYWYHSHTSGQQ--AAGLAGAIII 114
PLN02191 PLN02191
L-ascorbate oxidase
 94-224 2.70e-09

L-ascorbate oxidase


Pssm-ID: 177843 [Multi-domain]  Cd Length: 574  Bit Score: 61.18  E-value: 2.70e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1159645229   94 FLGPIIKGEVGDSIVIHLKN-FASRNYTLHPHGVtytkENEGALYPDGTGGLQKRddAVEPGGQFTYTWDVSEdqgpaAG 172
Cdd:PLN02191    51 FPGPTIDAVAGDTIVVHLTNkLTTEGLVIHWHGI----RQKGSPWADGAAGVTQC--AINPGETFTYKFTVEK-----PG 119

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|...
gi 1159645229  173 dadcvTRAYHSHIDAPRdvASGLVGPLIIcrkGTMNTDSDK-RFDAEFILMFS 224
Cdd:PLN02191   120 -----THFYHGHYGMQR--SAGLYGSLIV---DVAKGPKERlRYDGEFNLLLS 162
SufI COG2132
Multicopper oxidase with three cupredoxin domains (includes cell division protein FtsP and ...
 954-1054 3.30e-09

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: 60.33  E-value: 3.30e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1159645229  954 MHAINGKVFGNLG-GLTMHVGDRVSWYLMGMGNeiDIHTAHFHGHSF--------DYKQTGvyRADVFDLFPGtfQTVEM 1024
Cdd:COG2132    317 VWTINGKAFDPDRpDLTVKLGERERWTLVNDTM--MPHPFHLHGHQFqvlsrngkPPPEGG--WKDTVLVPPG--ETVRI 390

                           90       100       110
                   ....*....|....*....|....*....|...
gi 1159645229 1025 I---PRNPGTWLLHCHVTDHIHAGMETTYTVLP 1054
Cdd:COG2132    391 LfrfDNYPGDWMFHCHILEHEDAGMMGQFEVVP 423
SufI COG2132
Multicopper oxidase with three cupredoxin domains (includes cell division protein FtsP and ...
 94-224 1.46e-08

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


Pssm-ID: 441735 [Multi-domain]  Cd Length: 423  Bit Score: 58.41  E-value: 1.46e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1159645229   94 FLGPIIKGEVGDSIVIHLKNFASRNYTLHPHGVTYTKENegalypDGTGGlqkrdDAVEPGGQFTYTWDVseDQGPAagd 173
Cdd:COG2132     42 YPGPTIRVREGDRVRVRVTNRLPEPTTVHWHGLRVPNAM------DGVPG-----DPIAPGETFTYEFPV--PQPAG--- 105

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 1159645229  174 adcvTRAYHSHIDA--PRDVASGLVGPLIIcrkgtmNTDSDK--RFDAEFILMFS 224
Cdd:COG2132    106 ----TYWYHPHTHGstAEQVYRGLAGALIV------EDPEEDlpRYDRDIPLVLQ 150
ascorbase TIGR03388
L-ascorbate oxidase, plant type; Members of this protein family are the copper-containing ...
 94-233 2.61e-08

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: 57.84  E-value: 2.61e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1159645229   94 FLGPIIKGEVGDSIVIHLKN-FASRNYTLHPHGVtytkENEGALYPDGTGGLQKRddAVEPGGQFTYTWDVSEdqgpaAG 172
Cdd:TIGR03388   29 FPGPTIRAQAGDTIVVELTNkLHTEGVVIHWHGI----RQIGTPWADGTAGVTQC--AINPGETFIYNFVVDR-----PG 97

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1159645229  173 dadcvTRAYHSHIDAPRdvASGLVGPLIIcrkgtMNTDSDK---RFDAEFILMFSvmdenlSWY 233
Cdd:TIGR03388   98 -----TYFYHGHYGMQR--SAGLYGSLIV-----DVPDGEKepfHYDGEFNLLLS------DWW 143
Cu-oxidase_3 pfam07732
Multicopper oxidase; This entry contains many divergent copper oxidase-like domains that are ...
 448-555 8.47e-08

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: 51.86  E-value: 8.47e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1159645229  448 LLGPVIKAEVGESIRVTFRNNASRPFSIQPHGLSYRKS--DEGASYgassrGTESPashVSPGATFTYEWNVPEDVGptd 525
Cdd:pfam07732   24 FPGPTIRVREGDTVVVNVTNNLDEPTSIHWHGLQQRGTpwMDGVPG-----VTQCP---IPPGQSFTYRFQVKQQAG--- 92

                           90       100       110
                   ....*....|....*....|....*....|
gi 1159645229  526 qdpdclTWLYYSAVDAVRdtSSGLVGPLLV 555
Cdd:pfam07732   93 ------TYWYHSHTSGQQ--AAGLAGAIII 114
Cu-oxidase pfam00394
Multicopper oxidase; Many of the proteins in this family contain multiple similar copies of ...
 223-360 1.05e-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: 49.24  E-value: 1.05e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1159645229  223 FSVMDENLSWYlEDNIRTYCSEPSEVDKDDEDFQESNKMHSINGYMYGYLPNLTMCVEDKVKWHLFgMGNEADIHSAYFH 302
Cdd:pfam00394    1 EDYVITLSDWY-HKDAKDLEKELLASGKAPTDFPPVPDAVLINGKDGASLATLTVTPGKTYRLRII-NVALDDSLNFSIE 78

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1159645229  303 GQ--TLIE---RHH---RVDTISLFPATFVDAVMVP-RTPGEWLLSCQVN-DHIQGGMQALFKVKECG 360
Cdd:pfam00394   79 GHkmTVVEvdgVYVnpfTVDSLDIFPGQRYSVLVTAnQDPGNYWIVASPNiPAFDNGTAAAILRYSGA 146
PLN02191 PLN02191
L-ascorbate oxidase
 988-1050 9.91e-06

L-ascorbate oxidase


Pssm-ID: 177843 [Multi-domain]  Cd Length: 574  Bit Score: 49.63  E-value: 9.91e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1159645229  988 DIHTAHFHGHSF--------------DYKQTGVYRADVFD---LFPGTFQTVEMIPRNPGTWLLHCHVTDHIHAGMETTY 1050
Cdd:PLN02191   465 EIHPWHLHGHDFwvlgygdgkfkpgiDEKTYNLKNPPLRNtaiLYPYGWTAIRFVTDNPGVWFFHCHIEPHLHMGMGVVF 544
ascorbOXfungal TIGR03390
L-ascorbate oxidase, fungal type; This model describes a family of fungal ascorbate oxidases, ...
 987-1057 4.27e-04

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


Pssm-ID: 132431 [Multi-domain]  Cd Length: 538  Bit Score: 44.06  E-value: 4.27e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1159645229  987 IDIHTAHFHG-HSFDYKQ-TGVYRA---------------DVFDLFPGTFQTVEMIP----------RNPGTWLLHCHVT 1039
Cdd:TIGR03390  439 VDTHPFHAHGrHFYDIGGgDGEYNAtaneaklenytpvlrDTTMLYRYAVKVVPGAPagwrawrirvTNPGVWMMHCHIL 518

                           90
                   ....*....|....*...
gi 1159645229 1040 DHIHAGMETTYTVLPRED 1057
Cdd:TIGR03390  519 QHMVMGMQTVWVFGDAED 536
Cu-oxidase_3 pfam07732
Multicopper oxidase; This entry contains many divergent copper oxidase-like domains that are ...
 805-895 1.03e-03

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: 39.92  E-value: 1.03e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1159645229  805 GPLLMSNIGDKIVIVFKNLASRPYSIHAHGVKTDSS-----AVAVTN----PGETKTYVWKIPGRSSSergdppciAWaY 875
Cdd:pfam07732   26 GPTIRVREGDTVVVNVTNNLDEPTSIHWHGLQQRGTpwmdgVPGVTQcpipPGQSFTYRFQVKQQAGT--------YW-Y 96

                           90       100
                   ....*....|....*....|
gi 1159645229  876 HSAVDMVKdtYSGLIGTLVV 895
Cdd:pfam07732   97 HSHTSGQQ--AAGLAGAIII 114
PLN02168 PLN02168
copper ion binding / pectinesterase
 450-522 1.99e-03

copper ion binding / pectinesterase


Pssm-ID: 215113 [Multi-domain]  Cd Length: 545  Bit Score: 42.27  E-value: 1.99e-03
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1159645229  450 GPVIKAEVGESIRVTFRNNASRPFSIQPHGLSYRKSdegaSYGASSRGTESPashVSPGATFTYEWNVPEDVG 522
Cdd:PLN02168    56 GPLLNATANDVINVNIFNNLTEPFLMTWNGLQLRKN----SWQDGVRGTNCP---ILPGTNWTYRFQVKDQIG 121
 
Name Accession Description Interval E-value
CuRO_3_ceruloplasmin cd04224
The third cupredoxin domain of Ceruloplasmin; Ceruloplasmin is a multicopper oxidase essential ...
 371-568 7.57e-123

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: 374.12  E-value: 7.57e-123
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1159645229  371 RLRRYFIAAEEIIWNYGPSAMNGFTGQELIA-DSESRVFFEQSEMRIGGSYRKAVYKEYTDSSFTERKKRLAEEAHLGLL 449
Cdd:cd04224      2 KVRHYFIAAEEIMWDYAPSGKNLFTGQNLTApGSDSEVFFQRNETRIGGTYWKVRYVEYTDATFTTRKHRSKEEEHLGIL 81

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1159645229  450 GPVIKAEVGESIRVTFRNNASRPFSIQPHGLSYRKSDEGASYgasSRGTESPASHVSPGATFTYEWNVPEDVGPTDQDPD 529
Cdd:cd04224     82 GPVIRAEVGDTIKVTFRNKASRPFSIQPHGVFYEKNYEGAMY---RDGDPSPGSHVSPGETFTYEWTVPEGVGPTNQDPP 158

                          170       180       190
                   ....*....|....*....|....*....|....*....
gi 1159645229  530 CLTWLYYSAVDAVRDTSSGLVGPLLVCRKGALLPSGKQK 568
Cdd:cd04224    159 CLTYLYFSAVDPVRDTNSGLVGPLLVCKKGSLNANGRQK 197
CuRO_1_ceruloplasmin cd04222
The first cupredoxin domain of Ceruloplasmin; Ceruloplasmin is a multicopper oxidase essential ...
 22-204 3.83e-106

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: 329.38  E-value: 3.83e-106
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1159645229   22 REYWVGIAEREWNYAPGAASAPSAQLFAEHEQARAFLQRGPRRIGSTYKKAVYTQYTSQLYDVAVDKPSWLGFLGPIIKG 101
Cdd:cd04222      1 REYYIGIRETQWDYAPSGKNLITNQTFDDDEHASVFLKRGPDRIGRVYKKAVYLQYTDDTYRTEIEKPVWLGFLGPILKA 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1159645229  102 EVGDSIVIHLKNFASRNYTLHPHGVTYTKENEGALYPDGTGGLQKRDDAVEPGGQFTYTWDVSEDQGPAAGDADCVTRAY 181
Cdd:cd04222     81 EVGDVIVVHLKNFASRPYSLHPHGVFYNKENEGALYPDNTSGFEKADDAVPPGGSYTYTWTVPEEQAPTKADANCLTRIY 160

                          170       180
                   ....*....|....*....|...
gi 1159645229  182 HSHIDAPRDVASGLVGPLIICRK 204
Cdd:cd04222    161 HSHIDAPKDIASGLIGPLIICKK 183
CuRO_5_ceruloplasmin cd04225
The fifth cupredoxin domain of Ceruloplasmin; Ceruloplasmin is a multicopper oxidase essential ...
 728-898 2.01e-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: 324.42  E-value: 2.01e-104
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1159645229  728 KTYYIAAVEVEWDYSPNRTWEFERHQYLEDSPGNQFLNKEDKFIGSKYRKAVYREYTDGTFSTPKHRAEEQQHLEIQGPL 807
Cdd:cd04225      1 RTYYIAAEEVEWDYSPQRTWEQELHNTHEESPGNAFLNKGDKFIGSKYKKVVYREYTDDTFSVPKERTAEEEHLGILGPL 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1159645229  808 LMSNIGDKIVIVFKNLASRPYSIHAHGVKTDSSAVAVTNPGETKTYVWKIPGRSSSERGDPPCIAWAYHSAVDMVKDTYS 887
Cdd:cd04225     81 IHAEVGEKVKIVFKNMASRPYSIHAHGVKTDSSWVAPTEPGETQTYTWKIPERSGPGVEDSNCISWAYYSTVDQIKDLYS 160

                          170
                   ....*....|.
gi 1159645229  888 GLIGTLVVCHR 898
Cdd:cd04225    161 GLIGPLVICRR 171
CuRO_6_ceruloplasmin cd11012
The sixth cupredoxin domain of Ceruloplasmin; Ceruloplasmin is a multicopper oxidase essential ...
 909-1053 1.11e-97

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: 305.25  E-value: 1.11e-97
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1159645229  909 KVQFALLFMVFDENESWYLDENIKTYSPNPHLVDKEDEEFLESNKMHAINGKVFGNLGGLTMHVGDRVSWYLMGMGNEID 988
Cdd:cd11012      1 KLEFALLFLVFDENESWYLDENIKTYSDHPEKVNKEDEEFIESNKMHAINGKVFGNLQGLTMHVGDEVYWYLMGMGNEID 80

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1159645229  989 IHTAHFHGHSFDYKQTGVYRADVFDLFPGTFQTVEMIPRNPGTWLLHCHVTDHIHAGMETTYTVL 1053
Cdd:cd11012     81 IHTAHFHGHSFDYKHRGVYRSDVFDLFPGTFQTVEMIPRTPGTWLLHCHVTDHIHAGMETTYTVL 145
CuRO_2_ceruloplasmin cd11021
The second cupredoxin domain of Ceruloplasmin; Ceruloplasmin is a multicopper oxidase ...
 216-356 4.31e-95

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


Pssm-ID: 259907 [Multi-domain]  Cd Length: 141  Bit Score: 298.23  E-value: 4.31e-95
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1159645229  216 DAEFILMFSVMDENLSWYLEDNIRTYCSEPSEVDKDDEDFQESNKMHSINGYMYGYLPNLTMCVEDKVKWHLFGMGNEAD 295
Cdd:cd11021      1 DREFVLMFSVVDENLSWYLDENIKTYCSEPAKVDKDDEDFQESNKMHSINGYTFGNLPGLSMCAGDRVKWHLFGMGNEVD 80

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1159645229  296 IHSAYFHGQTLIERHHRVDTISLFPATFVDAVMVPRTPGEWLLSCQVNDHIQGGMQALFKV 356
Cdd:cd11021     81 IHSAFFHGQTLTDRGHRTDTINLFPATFVTAEMVAQNPGKWLLSCQVNDHLKAGMQAFYEV 141
CuRO_4_ceruloplasmin cd11022
The fourth cupredoxin domain of Ceruloplasmin; Ceruloplasmin is a multicopper oxidase ...
 573-714 3.51e-94

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: 295.93  E-value: 3.51e-94
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1159645229  573 EFFLLATVFDENLSWYLDDNILMFTLNPNKIDKDDEDFQESNKMHSINGYMYGNQPGLRMCKGSVVSWHLMGLGSEVDVH 652
Cdd:cd11022      3 EFFLLFTVFDENESWYLDENIQQFTLDPRSVDKEDEDFQESNKMHSINGYMYGNQPGLDMCKGDTVSWHLFGLGTETDVH 82

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1159645229  653 GIYFSENTFTARGTRRDTANLFPHTFLTAIMKPDSEGVFEVSCLTTDHYTGGMKQNYRVEQC 714
Cdd:cd11022     83 GIYFSGNTFLLQGTRRDTANLFPHTSVTAIMQPDNEGTFEVNCQTTDHYSAGMRQIYTVSQC 144
CuRO_1_ceruloplasmin_like cd04199
Cupredoxin domains 1, 3, and 5 of ceruloplasmin and similar proteins; This family includes the ...
 373-558 3.88e-76

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


Pssm-ID: 259862 [Multi-domain]  Cd Length: 177  Bit Score: 248.09  E-value: 3.88e-76
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1159645229  373 RRYFIAAEEIIWNYGPSamngftGQELIADSESRVFFEQSEMRIGGSYRKAVYKEYTDSSFTERKkrlAEEAHLGLLGPV 452
Cdd:cd04199      1 RHYYIAAEEIDWDYAPS------GLAEKDLSYRNQYLDNGPFRIGRSYKKVVYREYTDESFTTPG---PQPEHLGILGPT 71

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1159645229  453 IKAEVGESIRVTFRNNASRPFSIQPHGLSYRKSDEGASYGASSRGTESPASHVSPGATFTYEWNVPEDVGPTDQDPDCLT 532
Cdd:cd04199     72 IRAEVGDTIKVHFKNKASRPYSIHPHGVSYEKDSEGASYSDQTGPDEKKDDAVAPGETYTYVWIVTEESGPTKGDPACLT 151

                          170       180
                   ....*....|....*....|....*.
gi 1159645229  533 WLYYSAVDAVRDTSSGLVGPLLVCRK 558
Cdd:cd04199    152 WAYYSHVDLEKDINSGLIGPLLICKK 177
CuRO_1_ceruloplasmin_like cd04199
Cupredoxin domains 1, 3, and 5 of ceruloplasmin and similar proteins; This family includes the ...
 22-204 1.67e-73

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: 240.77  E-value: 1.67e-73
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1159645229   22 REYWVGIAEREWNYAPGAASAPsaqlfaEHEQARAFLQRGPRRIGSTYKKAVYTQYTSQLYDVAVDKPSWLGFLGPIIKG 101
Cdd:cd04199      1 RHYYIAAEEIDWDYAPSGLAEK------DLSYRNQYLDNGPFRIGRSYKKVVYREYTDESFTTPGPQPEHLGILGPTIRA 74

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1159645229  102 EVGDSIVIHLKNFASRNYTLHPHGVTYTKENEGALYPDGTGGLQKRDDAVEPGGQFTYTWDVSEDQGPAAGDADCVTRAY 181
Cdd:cd04199     75 EVGDTIKVHFKNKASRPYSIHPHGVSYEKDSEGASYSDQTGPDEKKDDAVAPGETYTYVWIVTEESGPTKGDPACLTWAY 154

                          170       180
                   ....*....|....*....|...
gi 1159645229  182 HSHIDAPRDVASGLVGPLIICRK 204
Cdd:cd04199    155 YSHVDLEKDINSGLIGPLLICKK 177
CuRO_2_ceruloplasmin_like cd04200
Cupredoxin domains 2, 4, and 6 of ceruloplasmin and similar proteins; This family includes the ...
 911-1052 1.83e-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: 233.84  E-value: 1.83e-71
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1159645229  911 QFALLFMVFDENESWYLDENIKTYSPNPHLVDKEDEEFLESNKMHAINGKVFGNLGGLTMHVGDRVSWYLMGMGNEIDIH 990
Cdd:cd04200      3 EFVLLFAVFDENKSWYLEDNIKRFCDNPEKVDKDDEEFQESNKMHAINGYVFGNLPGLTMCAGDRVRWHLLGMGNEVDVH 82

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1159645229  991 TAHFHGHSFDYKQtgvYRADVFDLFPGTFQTVEMIPRNPGTWLLHCHVTDHIHAGMETTYTV 1052
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 ...
 216-356 5.07e-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: 232.30  E-value: 5.07e-71
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1159645229  216 DAEFILMFSVMDENLSWYLEDNIRTYCSEPSEVDKDDEDFQESNKMHSINGYMYGYLPNLTMCVEDKVKWHLFGMGNEAD 295
Cdd:cd04200      1 DKEFVLLFAVFDENKSWYLEDNIKRFCDNPEKVDKDDEEFQESNKMHAINGYVFGNLPGLTMCAGDRVRWHLLGMGNEVD 80

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1159645229  296 IHSAYFHGQTLIERHHRVDTISLFPATFVDAVMVPRTPGEWLLSCQVNDHIQGGMQALFKV 356
Cdd:cd04200     81 VHSIHFHGQTFLYKGYRIDTLTLFPATFETVEMVPSNPGTWLLHCHNSDHRHAGMQAYFLV 141
CuRO_1_ceruloplasmin cd04222
The first cupredoxin domain of Ceruloplasmin; Ceruloplasmin is a multicopper oxidase essential ...
 373-558 3.21e-66

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: 220.75  E-value: 3.21e-66
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1159645229  373 RRYFIAAEEIIWNYGPSAMNGFTGQELIADSESRVFFEQSEMRIGGSYRKAVYKEYTDSSFTerkKRLAEEAHLGLLGPV 452
Cdd:cd04222      1 REYYIGIRETQWDYAPSGKNLITNQTFDDDEHASVFLKRGPDRIGRVYKKAVYLQYTDDTYR---TEIEKPVWLGFLGPI 77

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1159645229  453 IKAEVGESIRVTFRNNASRPFSIQPHGLSYRKSDEGASYGASSRGTESPASHVSPGATFTYEWNVPEDVGPTDQDPDCLT 532
Cdd:cd04222     78 LKAEVGDVIVVHLKNFASRPYSLHPHGVFYNKENEGALYPDNTSGFEKADDAVPPGGSYTYTWTVPEEQAPTKADANCLT 157

                          170       180
                   ....*....|....*....|....*.
gi 1159645229  533 WLYYSAVDAVRDTSSGLVGPLLVCRK 558
Cdd:cd04222    158 RIYHSHIDAPKDIASGLIGPLIICKK 183
CuRO_1_ceruloplasmin_like cd04199
Cupredoxin domains 1, 3, and 5 of ceruloplasmin and similar proteins; This family includes the ...
 728-898 8.89e-65

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: 216.50  E-value: 8.89e-65
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1159645229  728 KTYYIAAVEVEWDYSPNRTWEFERHQYledspgNQFLNKEDKFIGSKYRKAVYREYTDGTFSTPKhraEEQQHLEIQGPL 807
Cdd:cd04199      1 RHYYIAAEEIDWDYAPSGLAEKDLSYR------NQYLDNGPFRIGRSYKKVVYREYTDESFTTPG---PQPEHLGILGPT 71

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1159645229  808 LMSNIGDKIVIVFKNLASRPYSIHAHGVKTDSSAVAVTN---------------PGETKTYVWKIPGRSSSERGDPPCIA 872
Cdd:cd04199     72 IRAEVGDTIKVHFKNKASRPYSIHPHGVSYEKDSEGASYsdqtgpdekkddavaPGETYTYVWIVTEESGPTKGDPACLT 151

                          170       180
                   ....*....|....*....|....*.
gi 1159645229  873 WAYHSAVDMVKDTYSGLIGTLVVCHR 898
Cdd:cd04199    152 WAYYSHVDLEKDINSGLIGPLLICKK 177
CuRO_2_ceruloplasmin cd11021
The second cupredoxin domain of Ceruloplasmin; Ceruloplasmin is a multicopper oxidase ...
 911-1052 3.25e-63

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: 210.79  E-value: 3.25e-63
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1159645229  911 QFALLFMVFDENESWYLDENIKTYSPNPHLVDKEDEEFLESNKMHAINGKVFGNLGGLTMHVGDRVSWYLMGMGNEIDIH 990
Cdd:cd11021      3 EFVLMFSVVDENLSWYLDENIKTYCSEPAKVDKDDEDFQESNKMHSINGYTFGNLPGLSMCAGDRVKWHLFGMGNEVDIH 82

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1159645229  991 TAHFHGHSFDYKQtgvYRADVFDLFPGTFQTVEMIPRNPGTWLLHCHVTDHIHAGMETTYTV 1052
Cdd:cd11021     83 SAFFHGQTLTDRG---HRTDTINLFPATFVTAEMVAQNPGKWLLSCQVNDHLKAGMQAFYEV 141
CuRO_4_ceruloplasmin cd11022
The fourth cupredoxin domain of Ceruloplasmin; Ceruloplasmin is a multicopper oxidase ...
 216-359 5.83e-63

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: 210.03  E-value: 5.83e-63
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1159645229  216 DAEFILMFSVMDENLSWYLEDNIRTYCSEPSEVDKDDEDFQESNKMHSINGYMYGYLPNLTMCVEDKVKWHLFGMGNEAD 295
Cdd:cd11022      1 DKEFFLLFTVFDENESWYLDENIQQFTLDPRSVDKEDEDFQESNKMHSINGYMYGNQPGLDMCKGDTVSWHLFGLGTETD 80

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1159645229  296 IHSAYFHGQTLIERHHRVDTISLFPATFVDAVMVPRTPGEWLLSCQVNDHIQGGMQALFKVKEC 359
Cdd:cd11022     81 VHGIYFSGNTFLLQGTRRDTANLFPHTSVTAIMQPDNEGTFEVNCQTTDHYSAGMRQIYTVSQC 144
CuRO_3_FV_like cd14450
The third cupredoxin domain of coagulation factor V and similar proteins; Factor V is an ...
 375-557 1.62e-60

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: 204.73  E-value: 1.62e-60
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1159645229  375 YFIAAEEIIWNYGPS---AMNG-FTGQELIADSEsrvffeqsemRIGGSYRKAVYKEYTDSSFTER--KKRLAEEahlGL 448
Cdd:cd14450      5 YFIAAEEVIWDYAPSipeNMDKrYRSQYLDNFSN----------NIGKKYKKAVFTQYEDGSFTKRleNPRPKEE---GI 71

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1159645229  449 LGPVIKAEVGESIRVTFRNNASRPFSIQPHGLSYRKSDEGASYGASSRGTESPASHVSPGATFTYEWNVPEDVGPTDQDP 528
Cdd:cd14450     72 LGPVIRAQVRDTIKIVFKNKASRPYSIYPHGVTVSKAAEGASYPPDPRGNETQNKAVQPGETYTYKWNILETDEPTARDP 151

                          170       180
                   ....*....|....*....|....*....
gi 1159645229  529 DCLTWLYYSAVDAVRDTSSGLVGPLLVCR 557
Cdd:cd14450    152 RCLTRMYHSAVDITRDIASGLIGPLLICK 180
CuRO_2_ceruloplasmin_like cd04200
Cupredoxin domains 2, 4, and 6 of ceruloplasmin and similar proteins; This family includes the ...
 573-711 2.59e-60

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: 202.64  E-value: 2.59e-60
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1159645229  573 EFFLLATVFDENLSWYLDDNILMFTLNPNKIDKDDEDFQESNKMHSINGYMYGNQPGLRMCKGSVVSWHLMGLGSEVDVH 652
Cdd:cd04200      3 EFVLLFAVFDENKSWYLEDNIKRFCDNPEKVDKDDEEFQESNKMHAINGYVFGNLPGLTMCAGDRVRWHLLGMGNEVDVH 82

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 1159645229  653 GIYFSENTFTARGTRRDTANLFPHTFLTAIMKPDSEGVFEVSCLTTDHYTGGMKQNYRV 711
Cdd:cd04200     83 SIHFHGQTFLYKGYRIDTLTLFPATFETVEMVPSNPGTWLLHCHNSDHRHAGMQAYFLV 141
CuRO_2_ceruloplasmin cd11021
The second cupredoxin domain of Ceruloplasmin; Ceruloplasmin is a multicopper oxidase ...
 573-711 7.58e-60

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: 201.16  E-value: 7.58e-60
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1159645229  573 EFFLLATVFDENLSWYLDDNILMFTLNPNKIDKDDEDFQESNKMHSINGYMYGNQPGLRMCKGSVVSWHLMGLGSEVDVH 652
Cdd:cd11021      3 EFVLMFSVVDENLSWYLDENIKTYCSEPAKVDKDDEDFQESNKMHSINGYTFGNLPGLSMCAGDRVKWHLFGMGNEVDIH 82

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 1159645229  653 GIYFSENTFTARGTRRDTANLFPHTFLTAIMKPDSEGVFEVSCLTTDHYTGGMKQNYRV 711
Cdd:cd11021     83 SAFFHGQTLTDRGHRTDTINLFPATFVTAEMVAQNPGKWLLSCQVNDHLKAGMQAFYEV 141
CuRO_5_ceruloplasmin cd04225
The fifth cupredoxin domain of Ceruloplasmin; Ceruloplasmin is a multicopper oxidase essential ...
 373-558 1.11e-58

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: 199.23  E-value: 1.11e-58
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1159645229  373 RRYFIAAEEIIWNYGPSAMNGFTGQELIADSESRVFFEQSEMRIGGSYRKAVYKEYTDSSFTERKKRLAEEAHLGLLGPV 452
Cdd:cd04225      1 RTYYIAAEEVEWDYSPQRTWEQELHNTHEESPGNAFLNKGDKFIGSKYKKVVYREYTDDTFSVPKERTAEEEHLGILGPL 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1159645229  453 IKAEVGESIRVTFRNNASRPFSIQPHGLSyrksdegasygassrgTESPA-SHVSPGATFTYEWNVPEDVGPTDQDPDCL 531
Cdd:cd04225     81 IHAEVGEKVKIVFKNMASRPYSIHAHGVK----------------TDSSWvAPTEPGETQTYTWKIPERSGPGVEDSNCI 144

                          170       180
                   ....*....|....*....|....*..
gi 1159645229  532 TWLYYSAVDAVRDTSSGLVGPLLVCRK 558
Cdd:cd04225    145 SWAYYSTVDQIKDLYSGLIGPLVICRR 171
CuRO_3_ceruloplasmin cd04224
The third cupredoxin domain of Ceruloplasmin; Ceruloplasmin is a multicopper oxidase essential ...
 726-896 1.63e-58

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


Pssm-ID: 259886 [Multi-domain]  Cd Length: 197  Bit Score: 199.62  E-value: 1.63e-58
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1159645229  726 HEKTYYIAAVEVEWDYSPNRTWEFErHQYL--EDSPGNQFLNKEDKFIGSKYRKAVYREYTDGTFSTPKHRAEEQQHLEI 803
Cdd:cd04224      2 KVRHYFIAAEEIMWDYAPSGKNLFT-GQNLtaPGSDSEVFFQRNETRIGGTYWKVRYVEYTDATFTTRKHRSKEEEHLGI 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1159645229  804 QGPLLMSNIGDKIVIVFKNLASRPYSIHAHGV------------KTDSSAVAVTNPGETKTYVWKIPGRSSSERGDPPCI 871
Cdd:cd04224     81 LGPVIRAEVGDTIKVTFRNKASRPFSIQPHGVfyeknyegamyrDGDPSPGSHVSPGETFTYEWTVPEGVGPTNQDPPCL 160

                          170       180
                   ....*....|....*....|....*
gi 1159645229  872 AWAYHSAVDMVKDTYSGLIGTLVVC 896
Cdd:cd04224    161 TYLYFSAVDPVRDTNSGLVGPLLVC 185
CuRO_1_Ceruloplasmin_like_1 cd04229
cupredoxin domain of ceruloplasmin homologs; Uncharacterized subfamily of ceruloplasmin ...
 373-559 3.12e-57

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: 194.94  E-value: 3.12e-57
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1159645229  373 RRYFIAAEEIIWNYGPS-AMNGFTGQELiadSESRVFFEQSEMRIGGSYRKAVYKEYTDSSFTERKkrlAEEAHLGLLGP 451
Cdd:cd04229      1 RTYYIAAEEVDWDYAPSgKNKCCLGDDL---EVSTLDSQPGPYTIGSTYTKARYREYTDNSFSTPK---PTPAYLGILGP 74

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1159645229  452 VIKAEVGESIRVTFRNNASR-PFSIQPHGLSYRKSDEGASYGASSRgtespashVSPGATFTYEWNVPEDVGPTDQDPDC 530
Cdd:cd04229     75 VIRAEVGDTIKVVFKNNLDEfPVNMHPHGGLYSKDNEGTTDGAGDV--------VAPGETYTYRWIVPEDAGPGPGDPSS 146

                          170       180
                   ....*....|....*....|....*....
gi 1159645229  531 LTWLYYSAVDAVRDTSSGLVGPLLVCRKG 559
Cdd:cd04229    147 RLWLYHSHVDVFAHTNAGLVGPIIVTSKG 175
CuRO_4_ceruloplasmin cd11022
The fourth cupredoxin domain of Ceruloplasmin; Ceruloplasmin is a multicopper oxidase ...
 911-1052 3.47e-57

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


Pssm-ID: 259908 [Multi-domain]  Cd Length: 144  Bit Score: 193.85  E-value: 3.47e-57
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1159645229  911 QFALLFMVFDENESWYLDENIKTYSPNPHLVDKEDEEFLESNKMHAINGKVFGNLGGLTMHVGDRVSWYLMGMGNEIDIH 990
Cdd:cd11022      3 EFFLLFTVFDENESWYLDENIQQFTLDPRSVDKEDEDFQESNKMHSINGYMYGNQPGLDMCKGDTVSWHLFGLGTETDVH 82

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1159645229  991 TAHFHGHSFDYKQTgvyRADVFDLFPGTFQTVEMIPRNPGTWLLHCHVTDHIHAGMETTYTV 1052
Cdd:cd11022     83 GIYFSGNTFLLQGT---RRDTANLFPHTSVTAIMQPDNEGTFEVNCQTTDHYSAGMRQIYTV 141
CuRO_5_FV_like cd14451
The fifth cupredoxin domain of coagulation factor V and similar proteins; Factor V is an ...
 373-559 2.45e-56

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: 192.36  E-value: 2.45e-56
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1159645229  373 RRYFIAAEEIIWNYGpsamnGFTGQELIADSESRvffeqsemriGGSYRKAVYKEYTDSSFTERKKRLAEEAHLGLLGPV 452
Cdd:cd14451      2 RRYYIAAEEEEWDYA-----GYGKSRLDKTQNER----------DTVFKKVVFRRYLDSTFSTPDIQGEYEEHLGILGPV 66

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1159645229  453 IKAEVGESIRVTFRNNASRPFSIQPHGLSYRKSDEGASYGASSRGTESPASHVSPGATFTYEWNVPEDVGPTDQDPDCLT 532
Cdd:cd14451     67 IRAEVDDVIQVFFKNLASRPYSLHAHGLSYEKSSEGLSYDDESPDWFKKDDAVQPNGTYTYVWYANPRSGPENNGSDCRT 146

                          170       180
                   ....*....|....*....|....*..
gi 1159645229  533 WLYYSAVDAVRDTSSGLVGPLLVCRKG 559
Cdd:cd14451    147 WAYYSAVNPEKDIHSGLIGPLLICRKG 173
CuRO_6_ceruloplasmin cd11012
The sixth cupredoxin domain of Ceruloplasmin; Ceruloplasmin is a multicopper oxidase essential ...
 218-356 5.80e-53

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


Pssm-ID: 259898 [Multi-domain]  Cd Length: 145  Bit Score: 181.61  E-value: 5.80e-53
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1159645229  218 EFILMFSVMDENLSWYLEDNIRTYCSEPSEVDKDDEDFQESNKMHSINGYMYGYLPNLTMCVEDKVKWHLFGMGNEADIH 297
Cdd:cd11012      3 EFALLFLVFDENESWYLDENIKTYSDHPEKVNKEDEEFIESNKMHAINGKVFGNLQGLTMHVGDEVYWYLMGMGNEIDIH 82

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1159645229  298 SAYFHGQTLIERH---HRVDTISLFPATFVDAVMVPRTPGEWLLSCQVNDHIQGGMQALFKV 356
Cdd:cd11012     83 TAHFHGHSFDYKHrgvYRSDVFDLFPGTFQTVEMIPRTPGTWLLHCHVTDHIHAGMETTYTV 144
CuRO_1_FVIII_like cd14452
The first cupredoxin domain of coagulation factor VIII and similar proteins; Factor VIII ...
 22-205 1.61e-52

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: 181.71  E-value: 1.61e-52
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1159645229   22 REYWVGIAEREWNYAPGaasapsaQLFAEHEQARAFlqrgPRRIGSTYKKAVYTQYTSQLYDVAVDKPSWLGFLGPIIKG 101
Cdd:cd14452      1 RRYYIAAVEIGWDYIHS-------DLGDPASEQRKK----PKDIPQKYIKAVFVEYLDATFTVPKPRPAWMGLLGPTIVA 69

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1159645229  102 EVGDSIVIHLKNFASRNYTLHPHGVTYTKENEGALYPDGTGGLQKRDDAVEPGGQFTYTWDVSEDQGPAAGDADCVTRAY 181
Cdd:cd14452     70 EVGDTVVITFKNLASQPYSLHAVGVSYWKASEGAGYDDSTSQHEKEDDAVYPGGYHTYVWDISPKDGPTGSDPECLTYSY 149

                          170       180
                   ....*....|....*....|....
gi 1159645229  182 HSHIDAPRDVASGLVGPLIICRKG 205
Cdd:cd14452    150 SSQVDPVKDVNSGLIGALLVCRMG 173
CuRO_3_ceruloplasmin cd04224
The third cupredoxin domain of Ceruloplasmin; Ceruloplasmin is a multicopper oxidase essential ...
 22-210 3.10e-50

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: 176.12  E-value: 3.10e-50
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1159645229   22 REYWVGIAEREWNYAPGAASAPSAQ-LFAEHEQARAFLQRGPRRIGSTYKKAVYTQYTSQLYDVA---VDKPSWLGFLGP 97
Cdd:cd04224      4 RHYFIAAEEIMWDYAPSGKNLFTGQnLTAPGSDSEVFFQRNETRIGGTYWKVRYVEYTDATFTTRkhrSKEEEHLGILGP 83

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1159645229   98 IIKGEVGDSIVIHLKNFASRNYTLHPHGVTYTKENEGALYPDGTGglqKRDDAVEPGGQFTYTWDVSEDQGPAAGDADCV 177
Cdd:cd04224     84 VIRAEVGDTIKVTFRNKASRPFSIQPHGVFYEKNYEGAMYRDGDP---SPGSHVSPGETFTYEWTVPEGVGPTNQDPPCL 160

                          170       180       190
                   ....*....|....*....|....*....|...
gi 1159645229  178 TRAYHSHIDAPRDVASGLVGPLIICRKGTMNTD 210
Cdd:cd04224    161 TYLYFSAVDPVRDTNSGLVGPLLVCKKGSLNAN 193
CuRO_3_FV_like cd14450
The third cupredoxin domain of coagulation factor V and similar proteins; Factor V is an ...
 23-203 4.24e-50

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


Pssm-ID: 259992 [Multi-domain]  Cd Length: 181  Bit Score: 175.07  E-value: 4.24e-50
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1159645229   23 EYWVGIAEREWNYAPGAASAPSAQLFAEHeqarafLQRGPRRIGSTYKKAVYTQY-----TSQLYDVavdKPSWLGFLGP 97
Cdd:cd14450      4 EYFIAAEEVIWDYAPSIPENMDKRYRSQY------LDNFSNNIGKKYKKAVFTQYedgsfTKRLENP---RPKEEGILGP 74

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1159645229   98 IIKGEVGDSIVIHLKNFASRNYTLHPHGVTYTKENEGALYPDGTGGLQKRDDAVEPGGQFTYTWDVSEDQGPAAGDADCV 177
Cdd:cd14450     75 VIRAQVRDTIKIVFKNKASRPYSIYPHGVTVSKAAEGASYPPDPRGNETQNKAVQPGETYTYKWNILETDEPTARDPRCL 154

                          170       180
                   ....*....|....*....|....*.
gi 1159645229  178 TRAYHSHIDAPRDVASGLVGPLIICR 203
Cdd:cd14450    155 TRMYHSAVDITRDIASGLIGPLLICK 180
CuRO_1_FV_like cd04226
The first cupredoxin domain of coagulation factor VIII and similar proteins; Factor V is an ...
 373-559 1.61e-49

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


Pssm-ID: 259888 [Multi-domain]  Cd Length: 165  Bit Score: 172.74  E-value: 1.61e-49
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1159645229  373 RRYFIAAEEIIWNYGPsamngftGQEliadsesrvffEQSEMRIGGSYRKAVYKEYtDSSFterKKRLAEEAHLGLLGPV 452
Cdd:cd04226      1 REYYIAAQNIDWDYTP-------QSE-----------ELRLKRSEQSFKKIVYREY-EEGF---KKEKPADLSSGLLGPT 58

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1159645229  453 IKAEVGESIRVTFRNNASRPFSIQPHGLSYRKSDEGASYGASSRGTESPASHVSPGATFTYEWNVPEDVGPTDQDPDCLT 532
Cdd:cd04226     59 LRAEVGDTLIVHFKNMADKPLSIHPQGIAYGKKSEGSLYSDNTSPVEKLDDAVQPGQEYTYVWDITEEVGPTEADPPCLT 138

                          170       180
                   ....*....|....*....|....*..
gi 1159645229  533 WLYYSAVDAVRDTSSGLVGPLLVCRKG 559
Cdd:cd04226    139 YIYYSHVNMVRDFNSGLIGALLICKKG 165
CuRO_1_FVIII_like cd14452
The first cupredoxin domain of coagulation factor VIII and similar proteins; Factor VIII ...
 373-559 2.97e-49

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


Pssm-ID: 259994 [Multi-domain]  Cd Length: 173  Bit Score: 172.47  E-value: 2.97e-49
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1159645229  373 RRYFIAAEEIIWNYGPSAMNgftgqELIADSESRVFFEQSEmriggsYRKAVYKEYTDSSFTERKKRlaeEAHLGLLGPV 452
Cdd:cd14452      1 RRYYIAAVEIGWDYIHSDLG-----DPASEQRKKPKDIPQK------YIKAVFVEYLDATFTVPKPR---PAWMGLLGPT 66

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1159645229  453 IKAEVGESIRVTFRNNASRPFSIQPHGLSYRKSDEGASYGASSRGTESPASHVSPGATFTYEWNVPEDVGPTDQDPDCLT 532
Cdd:cd14452     67 IVAEVGDTVVITFKNLASQPYSLHAVGVSYWKASEGAGYDDSTSQHEKEDDAVYPGGYHTYVWDISPKDGPTGSDPECLT 146

                          170       180
                   ....*....|....*....|....*..
gi 1159645229  533 WLYYSAVDAVRDTSSGLVGPLLVCRKG 559
Cdd:cd14452    147 YSYSSQVDPVKDVNSGLIGALLVCRMG 173
CuRO_5_FVIII_like cd04228
The fifth cupredoxin domain of coagulation factor VIII and similar proteins; Factor VIII ...
 373-559 3.49e-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: 168.91  E-value: 3.49e-48
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1159645229  373 RRYFIAAEEIIWNYGpsamngftgqeliaDSESRVFFEQSEMRIGGS-----YRKAVYKEYTDSSFTERKKRLAEEAHLG 447
Cdd:cd04228      2 RHYFIAAVEVLWDYG--------------MQRPQHFLRARDPNRGRRksvpqYKKVVFREYLDGSFTQPVYRGELDEHLG 67

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1159645229  448 LLGPVIKAEVGESIRVTFRNNASRPFSIQPHGLSYRKSdegasyGASSRGTESpashVSPGATFTYEWNVPEDVGPTDQD 527
Cdd:cd04228     68 ILGPYIRAEVEDNIMVTFKNLASRPYSFHSSLISYEED------QRAEPRGNF----VQPGEVQTYSWKVLHQMAPTKQE 137

                          170       180       190
                   ....*....|....*....|....*....|..
gi 1159645229  528 PDCLTWLYYSAVDAVRDTSSGLVGPLLVCRKG 559
Cdd:cd04228    138 FDCKAWAYFSNVDLEKDLHSGLIGPLIICKTG 169
CuRO_1_Ceruloplasmin_like_1 cd04229
cupredoxin domain of ceruloplasmin homologs; Uncharacterized subfamily of ceruloplasmin ...
 22-205 6.57e-48

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: 168.36  E-value: 6.57e-48
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1159645229   22 REYWVGIAEREWNYAPGAASAPSaqLFAEHEQARAFLQRGPRRIGSTYKKAVYTQYTSQLYDVAVDKPSWLGFLGPIIKG 101
Cdd:cd04229      1 RTYYIAAEEVDWDYAPSGKNKCC--LGDDLEVSTLDSQPGPYTIGSTYTKARYREYTDNSFSTPKPTPAYLGILGPVIRA 78

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1159645229  102 EVGDSIVIHLKN-FASRNYTLHPHGVTYTKENEGalypdgtgGLQKRDDAVEPGGQFTYTWDVSEDQGPAAGDADCVTRA 180
Cdd:cd04229     79 EVGDTIKVVFKNnLDEFPVNMHPHGGLYSKDNEG--------TTDGAGDVVAPGETYTYRWIVPEDAGPGPGDPSSRLWL 150

                          170       180
                   ....*....|....*....|....*
gi 1159645229  181 YHSHIDAPRDVASGLVGPLIICRKG 205
Cdd:cd04229    151 YHSHVDVFAHTNAGLVGPIIVTSKG 175
CuRO_1_FV_like cd04226
The first cupredoxin domain of coagulation factor VIII and similar proteins; Factor V is an ...
 22-205 6.81e-48

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: 168.11  E-value: 6.81e-48
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1159645229   22 REYWVGIAEREWNYApgaasapsaqlfAEHEQARAflqrgpRRIGSTYKKAVYTQYTSqlyDVAVDKPSWL--GFLGPII 99
Cdd:cd04226      1 REYYIAAQNIDWDYT------------PQSEELRL------KRSEQSFKKIVYREYEE---GFKKEKPADLssGLLGPTL 59

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1159645229  100 KGEVGDSIVIHLKNFASRNYTLHPHGVTYTKENEGALYPDGTGGLQKRDDAVEPGGQFTYTWDVSEDQGPAAGDADCVTR 179
Cdd:cd04226     60 RAEVGDTLIVHFKNMADKPLSIHPQGIAYGKKSEGSLYSDNTSPVEKLDDAVQPGQEYTYVWDITEEVGPTEADPPCLTY 139

                          170       180
                   ....*....|....*....|....*.
gi 1159645229  180 AYHSHIDAPRDVASGLVGPLIICRKG 205
Cdd:cd04226    140 IYYSHVNMVRDFNSGLIGALLICKKG 165
CuRO_3_FVIII_like cd04227
The third cupredoxin domain of coagulation factor VIII and similar proteins; Factor VIII ...
 375-558 4.92e-47

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: 166.26  E-value: 4.92e-47
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1159645229  375 YFIAAEEIIWNYGPsamngftgqeLIADSESR----VFFEQSEMRIGGSYRKAVYKEYTDSSFTERKKRLAEEahlGLLG 450
Cdd:cd04227      5 HYIAAEELDWDYAP----------LLSSTDDRelqsRYLPTGPQRIGYKYKKVAFVEYTDKTFKRREAKQTEK---GILG 71

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1159645229  451 PVIKAEVGESIRVTFRNNASRPFSIQPHGLSYRKSDEGASYGASSRGTESPAshVSPGATFTYEWNVPEDVGPTDQDPDC 530
Cdd:cd04227     72 PLLKGEVGDQIHIMFKNTASRPYNIYPHGLTSVRPMYRSRNPAGEKDLKTMP--IGPGETFGYMWELTAEDGPTEEDPRC 149

                          170       180
                   ....*....|....*....|....*...
gi 1159645229  531 LTWLYYSAVDAVRDTSSGLVGPLLVCRK 558
Cdd:cd04227    150 LTRLYQSTVDPERDLASGLIGPLLICKK 177
CuRO_5_FV_like cd14451
The fifth cupredoxin domain of coagulation factor V and similar proteins; Factor V is an ...
 727-898 5.25e-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: 160.01  E-value: 5.25e-45
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1159645229  727 EKTYYIAAVEVEWDYSPnrtweferhqyledsPGNQFLNKEDKFIGSKYRKAVYREYTDGTFSTPKHRAEEQQHLEIQGP 806
Cdd:cd14451      1 KRRYYIAAEEEEWDYAG---------------YGKSRLDKTQNERDTVFKKVVFRRYLDSTFSTPDIQGEYEEHLGILGP 65

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1159645229  807 LLMSNIGDKIVIVFKNLASRPYSIHAHGVKTDSSAVAVT---------------NPGETKTYVWKIPGRSSSERGDPPCI 871
Cdd:cd14451     66 VIRAEVDDVIQVFFKNLASRPYSLHAHGLSYEKSSEGLSyddespdwfkkddavQPNGTYTYVWYANPRSGPENNGSDCR 145

                          170       180
                   ....*....|....*....|....*..
gi 1159645229  872 AWAYHSAVDMVKDTYSGLIGTLVVCHR 898
Cdd:cd14451    146 TWAYYSAVNPEKDIHSGLIGPLLICRK 172
CuRO_1_ceruloplasmin cd04222
The first cupredoxin domain of Ceruloplasmin; Ceruloplasmin is a multicopper oxidase essential ...
 728-898 1.59e-44

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: 159.12  E-value: 1.59e-44
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1159645229  728 KTYYIAAVEVEWDYSPNRTWEFERHQYLEDSPGNQFLNKEDKFIGSKYRKAVYREYTDGTFSTpkhRAEEQQHLEIQGPL 807
Cdd:cd04222      1 REYYIGIRETQWDYAPSGKNLITNQTFDDDEHASVFLKRGPDRIGRVYKKAVYLQYTDDTYRT---EIEKPVWLGFLGPI 77

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1159645229  808 LMSNIGDKIVIVFKNLASRPYSIHAHGV---KTDSSAVAVTN------------PGETKTYVWKIPGRSSSERGDPPCIA 872
Cdd:cd04222     78 LKAEVGDVIVVHLKNFASRPYSLHPHGVfynKENEGALYPDNtsgfekaddavpPGGSYTYTWTVPEEQAPTKADANCLT 157

                          170       180
                   ....*....|....*....|....*.
gi 1159645229  873 WAYHSAVDMVKDTYSGLIGTLVVCHR 898
Cdd:cd04222    158 RIYHSHIDAPKDIASGLIGPLIICKK 183
CuRO_1_Ceruloplasmin_like_1 cd04229
cupredoxin domain of ceruloplasmin homologs; Uncharacterized subfamily of ceruloplasmin ...
 728-895 2.22e-44

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: 158.35  E-value: 2.22e-44
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1159645229  728 KTYYIAAVEVEWDYSPNRTWEFERHQYLEDSPGnqFLNKEDKFIGSKYRKAVYREYTDGTFSTPKhraEEQQHLEIQGPL 807
Cdd:cd04229      1 RTYYIAAEEVDWDYAPSGKNKCCLGDDLEVSTL--DSQPGPYTIGSTYTKARYREYTDNSFSTPK---PTPAYLGILGPV 75

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1159645229  808 LMSNIGDKIVIVFKN-LASRPYSIHAHGV-------KTDSSAVAVTNPGETKTYVWKIPGRSSSERGDPPCIAWAYHSAV 879
Cdd:cd04229     76 IRAEVGDTIKVVFKNnLDEFPVNMHPHGGlyskdneGTTDGAGDVVAPGETYTYRWIVPEDAGPGPGDPSSRLWLYHSHV 155

                          170
                   ....*....|....*.
gi 1159645229  880 DMVKDTYSGLIGTLVV 895
Cdd:cd04229    156 DVFAHTNAGLVGPIIV 171
CuRO_5_FV_like cd14451
The fifth cupredoxin domain of coagulation factor V and similar proteins; Factor V is an ...
 21-205 1.48e-43

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: 156.15  E-value: 1.48e-43
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1159645229   21 RREYWVGIAEREWNYapgaasapsaqlfAEHEQARAFLQRGPRRigSTYKKAVYTQY---TSQLYDVAVDKPSWLGFLGP 97
Cdd:cd14451      1 KRRYYIAAEEEEWDY-------------AGYGKSRLDKTQNERD--TVFKKVVFRRYldsTFSTPDIQGEYEEHLGILGP 65

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1159645229   98 IIKGEVGDSIVIHLKNFASRNYTLHPHGVTYTKENEGALYPDGTGGLQKRDDAVEPGGQFTYTWDVSEDQGPAAGDADCV 177
Cdd:cd14451     66 VIRAEVDDVIQVFFKNLASRPYSLHAHGLSYEKSSEGLSYDDESPDWFKKDDAVQPNGTYTYVWYANPRSGPENNGSDCR 145

                          170       180
                   ....*....|....*....|....*...
gi 1159645229  178 TRAYHSHIDAPRDVASGLVGPLIICRKG 205
Cdd:cd14451    146 TWAYYSAVNPEKDIHSGLIGPLLICRKG 173
CuRO_3_FV_like cd14450
The third cupredoxin domain of coagulation factor V and similar proteins; Factor V is an ...
 729-896 8.86e-43

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: 154.26  E-value: 8.86e-43
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1159645229  729 TYYIAAVEVEWDYSPNRTweferhQYLEDSPGNQFLNKEDKFIGSKYRKAVYREYTDGTFstpKHRAEEQQHLE--IQGP 806
Cdd:cd14450      4 EYFIAAEEVIWDYAPSIP------ENMDKRYRSQYLDNFSNNIGKKYKKAVFTQYEDGSF---TKRLENPRPKEegILGP 74

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1159645229  807 LLMSNIGDKIVIVFKNLASRPYSIHAHGVKTDSSAVAVT---------------NPGETKTYVWKIPGRSSSERGDPPCI 871
Cdd:cd14450     75 VIRAQVRDTIKIVFKNKASRPYSIYPHGVTVSKAAEGASyppdprgnetqnkavQPGETYTYKWNILETDEPTARDPRCL 154

                          170       180
                   ....*....|....*....|....*
gi 1159645229  872 AWAYHSAVDMVKDTYSGLIGTLVVC 896
Cdd:cd14450    155 TRMYHSAVDITRDIASGLIGPLLIC 179
CuRO_6_ceruloplasmin cd11012
The sixth cupredoxin domain of Ceruloplasmin; Ceruloplasmin is a multicopper oxidase essential ...
 573-711 9.78e-42

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: 149.63  E-value: 9.78e-42
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1159645229  573 EFFLLATVFDENLSWYLDDNILMFTLNPNKIDKDDEDFQESNKMHSINGYMYGNQPGLRMCKGSVVSWHLMGLGSEVDVH 652
Cdd:cd11012      3 EFALLFLVFDENESWYLDENIKTYSDHPEKVNKEDEEFIESNKMHAINGKVFGNLQGLTMHVGDEVYWYLMGMGNEIDIH 82

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1159645229  653 GIYFSENTFTARGT---RRDTANLFPHTFLTAIMKPDSEGVFEVSCLTTDHYTGGMKQNYRV 711
Cdd:cd11012     83 TAHFHGHSFDYKHRgvyRSDVFDLFPGTFQTVEMIPRTPGTWLLHCHVTDHIHAGMETTYTV 144
CuRO_6_FVIII_like cd11018
The sixth cupredoxin domain of coagulation factor VIII and similar proteins; Factor VIII ...
 911-1052 9.96e-42

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


Pssm-ID: 259904 [Multi-domain]  Cd Length: 144  Bit Score: 149.65  E-value: 9.96e-42
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1159645229  911 QFALLFMVFDENESWYLDENIKTYSPNPHLVDKEDEEFLESNKMHAINGKVFGNLGGLTMHVGDRVSWYLMGMGNEIDIH 990
Cdd:cd11018      3 EFALLFTIFDETKSWYFEENMRRNCRPPCHIQTQDPWFHINNKFHAINGYVADTLPGLVMAQHQRIRWHLLNMGSDEEIH 82

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1159645229  991 TAHFHGHSFDYKQTGVYRADVFDLFPGTFQTVEMIPRNPGTWLLHCHVTDHIHAGMETTYTV 1052
Cdd:cd11018     83 SVHFHGLPFTVRAKKEYRMGVYNLYPGVFGTVEMRPSTAGIWLVECTVGEHLLAGMSALFLV 144
CuRO_5_FVIII_like cd04228
The fifth cupredoxin domain of coagulation factor VIII and similar proteins; Factor VIII ...
 730-898 1.03e-41

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: 150.42  E-value: 1.03e-41
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1159645229  730 YYIAAVEVEWDYSPNRTWEFERHQylEDSPGNQflnkedKFIgSKYRKAVYREYTDGTFSTPKHRAEEQQHLEIQGPLLM 809
Cdd:cd04228      4 YFIAAVEVLWDYGMQRPQHFLRAR--DPNRGRR------KSV-PQYKKVVFREYLDGSFTQPVYRGELDEHLGILGPYIR 74

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1159645229  810 SNIGDKIVIVFKNLASRPYSIHAHGVKTDSSAVA-----VTNPGETKTYVWKIPGRSSSERGDPPCIAWAYHSAVDMVKD 884
Cdd:cd04228     75 AEVEDNIMVTFKNLASRPYSFHSSLISYEEDQRAeprgnFVQPGEVQTYSWKVLHQMAPTKQEFDCKAWAYFSNVDLEKD 154

                          170
                   ....*....|....
gi 1159645229  885 TYSGLIGTLVVCHR 898
Cdd:cd04228    155 LHSGLIGPLIICKT 168
CuRO_5_ceruloplasmin cd04225
The fifth cupredoxin domain of Ceruloplasmin; Ceruloplasmin is a multicopper oxidase essential ...
 22-204 3.55e-41

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: 149.15  E-value: 3.55e-41
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1159645229   22 REYWVGIAEREWNYAPGAASAPSAQLFAEHEQARAFLQRGPRRIGSTYKKAVYTQYTSQLYDVAVDKPS---WLGFLGPI 98
Cdd:cd04225      1 RTYYIAAEEVEWDYSPQRTWEQELHNTHEESPGNAFLNKGDKFIGSKYKKVVYREYTDDTFSVPKERTAeeeHLGILGPL 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1159645229   99 IKGEVGDSIVIHLKNFASRNYTLHPHGVtytKENEGALYPdgtgglqkrddaVEPGGQFTYTWDVSEDQGPAAGDADCVT 178
Cdd:cd04225     81 IHAEVGEKVKIVFKNMASRPYSIHAHGV---KTDSSWVAP------------TEPGETQTYTWKIPERSGPGVEDSNCIS 145

                          170       180
                   ....*....|....*....|....*.
gi 1159645229  179 RAYHSHIDAPRDVASGLVGPLIICRK 204
Cdd:cd04225    146 WAYYSTVDQIKDLYSGLIGPLVICRR 171
CuRO_3_FVIII_like cd04227
The third cupredoxin domain of coagulation factor VIII and similar proteins; Factor VIII ...
 23-204 7.61e-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: 145.46  E-value: 7.61e-40
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1159645229   23 EYWVGIAEREWNYAPGAASAPsaqlfaEHEQARAFLQRGPRRIGSTYKKAVYTQYTSQLYDVAVDKPSWLGFLGPIIKGE 102
Cdd:cd04227      4 EHYIAAEELDWDYAPLLSSTD------DRELQSRYLPTGPQRIGYKYKKVAFVEYTDKTFKRREAKQTEKGILGPLLKGE 77

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1159645229  103 VGDSIVIHLKNFASRNYTLHPHGVTYTKENEGALYPDGTGGLqkRDDAVEPGGQFTYTWDVSEDQGPAAGDADCVTRAYH 182
Cdd:cd04227     78 VGDQIHIMFKNTASRPYNIYPHGLTSVRPMYRSRNPAGEKDL--KTMPIGPGETFGYMWELTAEDGPTEEDPRCLTRLYQ 155

                          170       180
                   ....*....|....*....|..
gi 1159645229  183 SHIDAPRDVASGLVGPLIICRK 204
Cdd:cd04227    156 STVDPERDLASGLIGPLLICKK 177
CuRO_3_FVIII_like cd04227
The third cupredoxin domain of coagulation factor VIII and similar proteins; Factor VIII ...
 729-898 1.44e-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: 141.99  E-value: 1.44e-38
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1159645229  729 TYYIAAVEVEWDYSPNRTWEFERH---QYLEDSPGNqflnkedkfIGSKYRKAVYREYTDGTFstpKHRAEEQQHLEIQG 805
Cdd:cd04227      4 EHYIAAEELDWDYAPLLSSTDDRElqsRYLPTGPQR---------IGYKYKKVAFVEYTDKTF---KRREAKQTEKGILG 71

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1159645229  806 PLLMSNIGDKIVIVFKNLASRPYSIHAHGVKTDSSAVAVTN-------------PGETKTYVWKIPGRSSSERGDPPCIA 872
Cdd:cd04227     72 PLLKGEVGDQIHIMFKNTASRPYNIYPHGLTSVRPMYRSRNpagekdlktmpigPGETFGYMWELTAEDGPTEEDPRCLT 151

                          170       180
                   ....*....|....*....|....*.
gi 1159645229  873 WAYHSAVDMVKDTYSGLIGTLVVCHR 898
Cdd:cd04227    152 RLYQSTVDPERDLASGLIGPLLICKK 177
CuRO_6_FVIII_like cd11018
The sixth cupredoxin domain of coagulation factor VIII and similar proteins; Factor VIII ...
 218-356 1.46e-37

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: 137.70  E-value: 1.46e-37
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1159645229  218 EFILMFSVMDENLSWYLEDNIRTYCSEPSEVDKDDEDFQESNKMHSINGYMYGYLPNLTMCVEDKVKWHLFGMGNEADIH 297
Cdd:cd11018      3 EFALLFTIFDETKSWYFEENMRRNCRPPCHIQTQDPWFHINNKFHAINGYVADTLPGLVMAQHQRIRWHLLNMGSDEEIH 82

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1159645229  298 SAYFHGQTLIER---HHRVDTISLFPATFVDAVMVPRTPGEWLLSCQVNDHIQGGMQALFKV 356
Cdd:cd11018     83 SVHFHGLPFTVRakkEYRMGVYNLYPGVFGTVEMRPSTAGIWLVECTVGEHLLAGMSALFLV 144
CuRO_2_ceruloplasmin_like_2 cd11023
cupredoxin domain of ceruloplasmin homologs; Uncharacterized subfamily of ceruloplasmin ...
 918-1052 3.92e-36

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


Pssm-ID: 259909 [Multi-domain]  Cd Length: 118  Bit Score: 132.73  E-value: 3.92e-36
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1159645229  918 VFDENESWYLDENIKtyspnphlvdkedeeflESNKMHAINGKVFGNLGGLTMHVGDRVSWYLMGMGNEIDIHTAHFHGH 997
Cdd:cd11023      3 EFIENSSIFLDLNVE-----------------EAGLMHSINGYVFGNLPGVTIAKGKRVRWHLVAYGNEVDFHTPHWHGQ 65

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 1159645229  998 SFDYKQTGvyRADVFDLFPGTFQTVEMIPRNPGTWLLHCHVTDHIHAGMETTYTV 1052
Cdd:cd11023     66 TVEADKSR--RTDVAELMPASMRVADMTAADVGTWLLHCHVHDHYMAGMMTQFAV 118
CuRO_1_FVIII_like cd14452
The first cupredoxin domain of coagulation factor VIII and similar proteins; Factor VIII ...
 728-896 1.94e-35

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: 132.79  E-value: 1.94e-35
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1159645229  728 KTYYIAAVEVEWDYSpnrtweferHQYLEDSPGNQflNKEDKFIGSKYRKAVYREYTDGTFSTPKHRAEeqqHLEIQGPL 807
Cdd:cd14452      1 RRYYIAAVEIGWDYI---------HSDLGDPASEQ--RKKPKDIPQKYIKAVFVEYLDATFTVPKPRPA---WMGLLGPT 66

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1159645229  808 LMSNIGDKIVIVFKNLASRPYSIHAHGVK----------TDSSAVA-----VTNPGETKTYVWKIPGRSSSERGDPPCIA 872
Cdd:cd14452     67 IVAEVGDTVVITFKNLASQPYSLHAVGVSywkasegagyDDSTSQHekeddAVYPGGYHTYVWDISPKDGPTGSDPECLT 146

                          170       180
                   ....*....|....*....|....
gi 1159645229  873 WAYHSAVDMVKDTYSGLIGTLVVC 896
Cdd:cd14452    147 YSYSSQVDPVKDVNSGLIGALLVC 170
CuRO_6_FV_like cd14455
The sixth cupredoxin domain of coagulation factor V and similar proteins; Factor V is an ...
 911-1052 4.32e-35

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


Pssm-ID: 259997 [Multi-domain]  Cd Length: 140  Bit Score: 130.37  E-value: 4.32e-35
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1159645229  911 QFALLFMVFDENESWYLDENIKTYSPNphlVDKEDEEFLESNKMHAINGKVFgNLGGLTMHVGDRVSWYLMGMGNEIDIH 990
Cdd:cd14455      3 EFVLLFMTFDEEKSWYYEKNRKRTCRE---NRVKDPNVQDNHTFHAINGIIY-NLKGLRMYTNELVRWHLINMGGPKDLH 78

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1159645229  991 TAHFHGHSFDYKQTGVYRADVFDLFPGTFQTVEMIPRNPGTWLLHCHVTDHIHAGMETTYTV 1052
Cdd:cd14455     79 VVHFHGQTFTEKGLKDHQLGVYPLLPGSFATLEMKPSKPGLWLLETEVGESQQRGMQTLFLV 140
CuRO_6_FV_like cd14455
The sixth cupredoxin domain of coagulation factor V and similar proteins; Factor V is an ...
 218-356 4.44e-33

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: 124.59  E-value: 4.44e-33
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1159645229  218 EFILMFSVMDENLSWYLEDNIRTYCSEPSEVDKDdedFQESNKMHSINGYMYGyLPNLTMCVEDKVKWHLFGMGNEADIH 297
Cdd:cd14455      3 EFVLLFMTFDEEKSWYYEKNRKRTCRENRVKDPN---VQDNHTFHAINGIIYN-LKGLRMYTNELVRWHLINMGGPKDLH 78

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1159645229  298 SAYFHGQTLIE---RHHRVDTISLFPATFVDAVMVPRTPGEWLLSCQVNDHIQGGMQALFKV 356
Cdd:cd14455     79 VVHFHGQTFTEkglKDHQLGVYPLLPGSFATLEMKPSKPGLWLLETEVGESQQRGMQTLFLV 140
CuRO_2_FV_like cd14453
The second cupredoxin domain of coagulation factor V and similar proteins; Factor V is an ...
 216-356 8.51e-33

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


Pssm-ID: 259995 [Multi-domain]  Cd Length: 123  Bit Score: 123.43  E-value: 8.51e-33
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1159645229  216 DAEFILMFSVMDENLSWYlednirtycsepsevdkdDEDFQESNKMHSINGYMYGYLPNLTMCVEDKVKWHLFGMGNEAD 295
Cdd:cd14453      1 YKEYVLMFGVFDENKSWY------------------KQNASVDSVKYTINGYTNGTLPDVSICAYDHVSWHLLGMSSEPE 62

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1159645229  296 IHSAYFHGQTLIERHHRVDTISLFPATFVDAVMVPRTPGEWLLSCQVNDHIQGGMQALFKV 356
Cdd:cd14453     63 LFSVHFNGQVLEQNGHKVSAVGLVSGSSTTASMTVVHTGRWLISSLIMKHLQAGMYGYLNI 123
CuRO_4_FVIII_like cd11016
The fourth cupredoxin domain of coagulation factor VIII and similar proteins; Factor VIII ...
 576-714 1.10e-32

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


Pssm-ID: 259902 [Multi-domain]  Cd Length: 143  Bit Score: 123.82  E-value: 1.10e-32
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1159645229  576 LLATVFDENLSWYLDDNILMFTLNPNKIDKDDEDFQESNKMHSINGYMYGNQPgLRMCKGSVVSWHLMGLGSEVDVHGIY 655
Cdd:cd11016      6 LLFSVFDENNSWYLKENIHRFTQTPAGVNDTDPDFYASNVMHTINGIVFDRRQ-FVICLTDVAYWYVLSVGAQTDFLSVF 84

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 1159645229  656 FSENTFTARGTRRDTANLFPHTFLTAIMKPDSEGVFEVSCLTTDHYTGGMKQNYRVEQC 714
Cdd:cd11016     85 FSGNTFKHQMVYEDVLTLFPFSGETVSMSPEVPGEWELGCFNGDFRSRGMSAQYTVSTC 143
CuRO_2_FVIII_like cd11015
The second cupredoxin domain of coagulation factor VIII and similar proteins; Factor VIII ...
 218-356 1.38e-32

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: 123.09  E-value: 1.38e-32
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1159645229  218 EFILMFSVMDENLSWYLEDnirtycSEPSEVDKDDEDfQESNKMHSINGYMYGYLPNLTMCVEDKVKWHLFGMGNEADIH 297
Cdd:cd11015      3 AFVLLFAVFDEGKSWYSEV------GERKSRDKFKRA-DSRKEFHTINGYINASLPGLKICQRKPVIWHVIGMGTAPEVH 75

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 1159645229  298 SAYFHGQTLIERHHRVDTISLFPATFVDAVMVPRTPGEWLLSCQVNDHIQGGMQALFKV 356
Cdd:cd11015     76 SIFFEGHTFLVRTHRKVSLEISPMTFLTAQTKPATVGSFLIFCQIHSHQHDGMEAMVKV 134
CuRO_4_FVIII_like cd11016
The fourth cupredoxin domain of coagulation factor VIII and similar proteins; Factor VIII ...
 216-359 1.41e-32

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


Pssm-ID: 259902 [Multi-domain]  Cd Length: 143  Bit Score: 123.44  E-value: 1.41e-32
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1159645229  216 DAEFILMFSVMDENLSWYLEDNIRTYCSEPSEVDKDDEDFQESNKMHSINGYMYGYLpNLTMCVEDKVKWHLFGMGNEAD 295
Cdd:cd11016      1 DKDWSLLFSVFDENNSWYLKENIHRFTQTPAGVNDTDPDFYASNVMHTINGIVFDRR-QFVICLTDVAYWYVLSVGAQTD 79

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1159645229  296 IHSAYFHGQTLieRHHRV--DTISLFPATFVDAVMVPRTPGEWLLSCQVNDHIQGGMQALFKVKEC 359
Cdd:cd11016     80 FLSVFFSGNTF--KHQMVyeDVLTLFPFSGETVSMSPEVPGEWELGCFNGDFRSRGMSAQYTVSTC 143
CuRO_2_ceruloplasmin_like_2 cd11023
cupredoxin domain of ceruloplasmin homologs; Uncharacterized subfamily of ceruloplasmin ...
 251-356 2.86e-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: 2.86e-32
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1159645229  251 DDEDFQESNKMHSINGYMYGYLPNLTMCVEDKVKWHLFGMGNEADIHSAYFHGQTL-IERHHRVDTISLFPATFVDAVMV 329
Cdd:cd11023     12 LDLNVEEAGLMHSINGYVFGNLPGVTIAKGKRVRWHLVAYGNEVDFHTPHWHGQTVeADKSRRTDVAELMPASMRVADMT 91

                           90       100
                   ....*....|....*....|....*..
gi 1159645229  330 PRTPGEWLLSCQVNDHIQGGMQALFKV 356
Cdd:cd11023     92 AADVGTWLLHCHVHDHYMAGMMTQFAV 118
CuRO_1_FV_like cd04226
The first cupredoxin domain of coagulation factor VIII and similar proteins; Factor V is an ...
 730-896 2.23e-31

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: 120.73  E-value: 2.23e-31
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1159645229  730 YYIAAVEVEWDYSPnrtweferhqyledspgnQFLNKEDKFIGSKYRKAVYREYTDGtFSTPKHRAEEQQHLeiqGPLLM 809
Cdd:cd04226      3 YYIAAQNIDWDYTP------------------QSEELRLKRSEQSFKKIVYREYEEG-FKKEKPADLSSGLL---GPTLR 60

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1159645229  810 SNIGDKIVIVFKNLASRPYSIHAHGVK----------TDSSAVA-----VTNPGETKTYVWKIPGRSSSERGDPPCIAWA 874
Cdd:cd04226     61 AEVGDTLIVHFKNMADKPLSIHPQGIAygkksegslySDNTSPVeklddAVQPGQEYTYVWDITEEVGPTEADPPCLTYI 140

                          170       180
                   ....*....|....*....|..
gi 1159645229  875 YHSAVDMVKDTYSGLIGTLVVC 896
Cdd:cd04226    141 YYSHVNMVRDFNSGLIGALLIC 162
CuRO_4_FV_like cd14454
The fourth cupredoxin domain of coagulation factor V and similar proteins; Factor V is an ...
 216-359 4.26e-31

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: 119.21  E-value: 4.26e-31
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1159645229  216 DAEFILMFSVMDENLSWYLEDNIRTYCSEPSEVDKDDEDFQESNKMHSINGYMYGYLPNLTMCVEDKVKWHLFGMGNEAD 295
Cdd:cd14454      1 DLEQHAVFAVFDENKSWYLEENINKYCSNPNNVKKDDPKFYKSNIMPTINGYAYESSAPLGFCHSEVVQWHISSVGTQDE 80

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1159645229  296 IHSAYFHGQTLIERHHRVDTISLFPATFVDAVMVPRTPGEWLLSCQVNDHIQGGMQALFKVKEC 359
Cdd:cd14454     81 IITVHLSGHTFRYKGKHEDTLNLFPMSGESITVTMDNLGTWLLGSFGSSKKSKGLRVRFTDVIC 144
CuRO_5_FVIII_like cd04228
The fifth cupredoxin domain of coagulation factor VIII and similar proteins; Factor VIII ...
 22-205 1.16e-30

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: 118.84  E-value: 1.16e-30
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1159645229   22 REYWVGIAEREWNYAPGAASapsaQLFAEHEQARAflQRGPRRigsTYKKAVYTQYTSQLYDVAVDK---PSWLGFLGPI 98
Cdd:cd04228      2 RHYFIAAVEVLWDYGMQRPQ----HFLRARDPNRG--RRKSVP---QYKKVVFREYLDGSFTQPVYRgelDEHLGILGPY 72

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1159645229   99 IKGEVGDSIVIHLKNFASRNYTLHPHGVTYtkENEGALYPDGtgglqkrdDAVEPGGQFTYTWDVSEDQGPAAGDADCVT 178
Cdd:cd04228     73 IRAEVEDNIMVTFKNLASRPYSFHSSLISY--EEDQRAEPRG--------NFVQPGEVQTYSWKVLHQMAPTKQEFDCKA 142

                          170       180
                   ....*....|....*....|....*..
gi 1159645229  179 RAYHSHIDAPRDVASGLVGPLIICRKG 205
Cdd:cd04228    143 WAYFSNVDLEKDLHSGLIGPLIICKTG 169
CuRO_4_FVIII_like cd11016
The fourth cupredoxin domain of coagulation factor VIII and similar proteins; Factor VIII ...
 914-1053 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 1159645229  914 LLFMVFDENESWYLDENIKTYSPNPHLVDKEDEEFLESNKMHAINGKVFGNLgGLTMHVGDRVSWYLMGMGNEIDIHTAH 993
Cdd:cd11016      6 LLFSVFDENNSWYLKENIHRFTQTPAGVNDTDPDFYASNVMHTINGIVFDRR-QFVICLTDVAYWYVLSVGAQTDFLSVF 84

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1159645229  994 FHGHSFdyKQTGVYRaDVFDLFPGTFQTVEMIPRNPGTWLLHCHVTDHIHAGMETTYTVL 1053
Cdd:cd11016     85 FSGNTF--KHQMVYE-DVLTLFPFSGETVSMSPEVPGEWELGCFNGDFRSRGMSAQYTVS 141
CuRO_4_FV_like cd14454
The fourth cupredoxin domain of coagulation factor V and similar proteins; Factor V is an ...
 579-714 9.73e-30

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: 115.35  E-value: 9.73e-30
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1159645229  579 TVFDENLSWYLDDNILMFTLNPNKIDKDDEDFQESNKMHSINGYMYGNQPGLRMCKGSVVSWHLMGLGSEVDVHGIYFSE 658
Cdd:cd14454      9 AVFDENKSWYLEENINKYCSNPNNVKKDDPKFYKSNIMPTINGYAYESSAPLGFCHSEVVQWHISSVGTQDEIITVHLSG 88

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 1159645229  659 NTFTARGTRRDTANLFPHTFLTAIMKPDSEGVFEVSCLTTDHYTGGMKQNYRVEQC 714
Cdd:cd14454     89 HTFRYKGKHEDTLNLFPMSGESITVTMDNLGTWLLGSFGSSKKSKGLRVRFTDVIC 144
CuRO_4_FV_like cd14454
The fourth cupredoxin domain of coagulation factor V and similar proteins; Factor V is an ...
 915-1034 1.21e-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: 112.27  E-value: 1.21e-28
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1159645229  915 LFMVFDENESWYLDENIKTYSPNPHLVDKEDEEFLESNKMHAINGKVFGNLGGLTMHVGDRVSWYLMGMGNEIDIHTAHF 994
Cdd:cd14454      7 VFAVFDENKSWYLEENINKYCSNPNNVKKDDPKFYKSNIMPTINGYAYESSAPLGFCHSEVVQWHISSVGTQDEIITVHL 86

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|
gi 1159645229  995 HGHSFDYKQTgvyRADVFDLFPGTFQTVEMIPRNPGTWLL 1034
Cdd:cd14454     87 SGHTFRYKGK---HEDTLNLFPMSGESITVTMDNLGTWLL 123
CuRO_6_FVIII_like cd11018
The sixth cupredoxin domain of coagulation factor VIII and similar proteins; Factor VIII ...
 573-711 2.15e-28

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: 111.51  E-value: 2.15e-28
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1159645229  573 EFFLLATVFDENLSWYLDDNILMFTLNPNKIDKDDEDFQESNKMHSINGYMYGNQPGLRMCKGSVVSWHLMGLGSEVDVH 652
Cdd:cd11018      3 EFALLFTIFDETKSWYFEENMRRNCRPPCHIQTQDPWFHINNKFHAINGYVADTLPGLVMAQHQRIRWHLLNMGSDEEIH 82

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1159645229  653 GIYFSENTFTARGT---RRDTANLFPHTFLTAIMKPDSEGVFEVSCLTTDHYTGGMKQNYRV 711
Cdd:cd11018     83 SVHFHGLPFTVRAKkeyRMGVYNLYPGVFGTVEMRPSTAGIWLVECTVGEHLLAGMSALFLV 144
CuRO_2_ceruloplasmin_like_2 cd11023
cupredoxin domain of ceruloplasmin homologs; Uncharacterized subfamily of ceruloplasmin ...
 606-711 1.79e-24

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: 99.22  E-value: 1.79e-24
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1159645229  606 DDEDFQESNKMHSINGYMYGNQPGLRMCKGSVVSWHLMGLGSEVDVHGIYFSENTFTARGTRR-DTANLFPHTFLTAIMK 684
Cdd:cd11023     12 LDLNVEEAGLMHSINGYVFGNLPGVTIAKGKRVRWHLVAYGNEVDFHTPHWHGQTVEADKSRRtDVAELMPASMRVADMT 91

                           90       100
                   ....*....|....*....|....*..
gi 1159645229  685 PDSEGVFEVSCLTTDHYTGGMKQNYRV 711
Cdd:cd11023     92 AADVGTWLLHCHVHDHYMAGMMTQFAV 118
CuRO_2_FVIII_like cd11015
The second cupredoxin domain of coagulation factor VIII and similar proteins; Factor VIII ...
 571-711 4.21e-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: 98.82  E-value: 4.21e-24
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1159645229  571 NTEFFLLATVFDENLSWYLDdnilmfTLNPNKIDKDDEDfQESNKMHSINGYMYGNQPGLRMCKGSVVSWHLMGLGSEVD 650
Cdd:cd11015      1 NQAFVLLFAVFDEGKSWYSE------VGERKSRDKFKRA-DSRKEFHTINGYINASLPGLKICQRKPVIWHVIGMGTAPE 73

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1159645229  651 VHGIYFSENTFTARGTRRDTANLFPHTFLTAIMKPDSEGVFEVSCLTTDHYTGGMKQNYRV 711
Cdd:cd11015     74 VHSIFFEGHTFLVRTHRKVSLEISPMTFLTAQTKPATVGSFLIFCQIHSHQHDGMEAMVKV 134
CuRO_2_FVIII_like cd11015
The second cupredoxin domain of coagulation factor VIII and similar proteins; Factor VIII ...
 911-1052 5.76e-21

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: 89.96  E-value: 5.76e-21
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1159645229  911 QFALLFMVFDENESWYLDENiktyspNPHLVDKEDEEFlESNKMHAINGKVFGNLGGLTMHVGDRVSWYLMGMGNEIDIH 990
Cdd:cd11015      3 AFVLLFAVFDEGKSWYSEVG------ERKSRDKFKRAD-SRKEFHTINGYINASLPGLKICQRKPVIWHVIGMGTAPEVH 75

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1159645229  991 TAHFHGHSFDYKQtgvYRADVFDLFPGTFQTVEMIPRNPGTWLLHCHVTDHIHAGMETTYTV 1052
Cdd:cd11015     76 SIFFEGHTFLVRT---HRKVSLEISPMTFLTAQTKPATVGSFLIFCQIHSHQHDGMEAMVKV 134
CuRO_2_FV_like cd14453
The second cupredoxin domain of coagulation factor V and similar proteins; Factor V is an ...
 911-1046 1.05e-19

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


Pssm-ID: 259995 [Multi-domain]  Cd Length: 123  Bit Score: 86.07  E-value: 1.05e-19
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1159645229  911 QFALLFMVFDENESWYldeniKTYSPNPHLvdkedeeflesnkMHAINGKVFGNLGGLTMHVGDRVSWYLMGMGNEIDIH 990
Cdd:cd14453      3 EYVLMFGVFDENKSWY-----KQNASVDSV-------------KYTINGYTNGTLPDVSICAYDHVSWHLLGMSSEPELF 64

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 1159645229  991 TAHFHGHSFDYKQtgvYRADVFDLFPGTFQTVEMIPRNPGTWLLHCHVTDHIHAGM 1046
Cdd:cd14453     65 SVHFNGQVLEQNG---HKVSAVGLVSGSSTTASMTVVHTGRWLISSLIMKHLQAGM 117
CuRO_6_FV_like cd14455
The sixth cupredoxin domain of coagulation factor V and similar proteins; Factor V is an ...
 573-689 3.86e-19

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


Pssm-ID: 259997 [Multi-domain]  Cd Length: 140  Bit Score: 84.92  E-value: 3.86e-19
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1159645229  573 EFFLLATVFDENLSWYLDDNIlmfTLNPNKIDKDDEDFQESNKMHSINGYMYgNQPGLRMCKGSVVSWHLMGLGSEVDVH 652
Cdd:cd14455      3 EFVLLFMTFDEEKSWYYEKNR---KRTCRENRVKDPNVQDNHTFHAINGIIY-NLKGLRMYTNELVRWHLINMGGPKDLH 78

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|
gi 1159645229  653 GIYFSENTFTARGT---RRDTANLFPHTFLTAIMKPDSEG 689
Cdd:cd14455     79 VVHFHGQTFTEKGLkdhQLGVYPLLPGSFATLEMKPSKPG 118
Cu-oxidase_2 pfam07731
Multicopper oxidase; This entry contains many divergent copper oxidase-like domains that are ...
 952-1056 7.61e-19

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: 84.02  E-value: 7.61e-19
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1159645229  952 NKMHAINGKVFGNLG-GLTMHVGDRVSWYLMGMGNeiDIHTAHFHGHSFDYKQTGV----------------YRADVFDL 1014
Cdd:pfam07731   19 RNDWAINGLLFPPNTnVITLPYGTVVEWVLQNTTT--GVHPFHLHGHSFQVLGRGGgpwpeedpktynlvdpVRRDTVQV 96

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|..
gi 1159645229 1015 FPGTFQTVEMIPRNPGTWLLHCHVTDHIHAGMETTYTVLPRE 1056
Cdd:pfam07731   97 PPGGWVAIRFRADNPGVWLFHCHILWHLDQGMMGQFVVRPGD 138
CuRO_1_LCC_like cd04206
Cupredoxin domain 1 of laccase-like multicopper oxidases; including laccase, CueO, spore coat ...
 93-202 1.60e-17

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: 79.64  E-value: 1.60e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1159645229   93 GFLGPIIKGEVGDSIVIHLKN-FASRNYTLHPHGVTYTKENEGalypDGTGGLQKrdDAVEPGGQFTYTWDVSEDQGpaa 171
Cdd:cd04206     27 QFPGPTIRVKEGDTVEVTVTNnLPNEPTSIHWHGLRQPGTNDG----DGVAGLTQ--CPIPPGESFTYRFTVDDQAG--- 97

                           90       100       110
                   ....*....|....*....|....*....|.
gi 1159645229  172 gdadcvTRAYHSHIDAprDVASGLVGPLIIC 202
Cdd:cd04206     98 ------TFWYHSHVGG--QRADGLYGPLIVE 120
CuRO_2_FV_like cd14453
The second cupredoxin domain of coagulation factor V and similar proteins; Factor V is an ...
 571-705 8.49e-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: 77.59  E-value: 8.49e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1159645229  571 NTEFFLLATVFDENLSWYlddnilmfTLNPnkidkddedfQESNKMHSINGYMYGNQPGLRMCKGSVVSWHLMGLGSEVD 650
Cdd:cd14453      1 YKEYVLMFGVFDENKSWY--------KQNA----------SVDSVKYTINGYTNGTLPDVSICAYDHVSWHLLGMSSEPE 62

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 1159645229  651 VHGIYFSENTFTARGTRRDTANLFPHTFLTAIMKPDSEGVFEVSCLTTDHYTGGM 705
Cdd:cd14453     63 LFSVHFNGQVLEQNGHKVSAVGLVSGSSTTASMTVVHTGRWLISSLIMKHLQAGM 117
CuRO_1_LCC_like cd04206
Cupredoxin domain 1 of laccase-like multicopper oxidases; including laccase, CueO, spore coat ...
 436-556 1.11e-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: 71.55  E-value: 1.11e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1159645229  436 RKKRLAEEAHLGLLGPVIKAEVGESIRVTFRNN-ASRPFSIQPHGLSYRKSDEGasYGASSrGTESPashVSPGATFTYE 514
Cdd:cd04206     16 GVLRQVITVNGQFPGPTIRVKEGDTVEVTVTNNlPNEPTSIHWHGLRQPGTNDG--DGVAG-LTQCP---IPPGESFTYR 89

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|..
gi 1159645229  515 WNVPEDVGptdqdpdclTWLYYSAVDAVRDTssGLVGPLLVC 556
Cdd:cd04206     90 FTVDDQAG---------TFWYHSHVGGQRAD--GLYGPLIVE 120
CuRO_3_LCC_like cd04207
Cupredoxin domain 3 of laccase-like multicopper oxidases; including laccase, CueO, spore coat ...
 956-1051 2.04e-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: 70.95  E-value: 2.04e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1159645229  956 AINGKVF----GNLGGLTMHVGDRVSWYLMGMGNEIDIHTAHFHGHSF------------DYKQTGVYRADVFDLFPGTF 1019
Cdd:cd04207     21 VINGMPFkegdANTDIFSVEAGDVVEIVLINAGNHDMQHPFHLHGHSFwvlgsgggpfdaPLNLTNPPWRDTVLVPPGGW 100

                           90       100       110
                   ....*....|....*....|....*....|..
gi 1159645229 1020 QTVEMIPRNPGTWLLHCHVTDHIHAGMETTYT 1051
Cdd:cd04207    101 VVIRFKADNPGVWMLHCHILEHEDAGMMTVFE 132
CuRO_D2_2dMcoN_like cd04202
The second cupredoxin domain of bacterial two domain multicopper oxidase McoN and similar ...
 954-1046 3.64e-13

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: 67.66  E-value: 3.64e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1159645229  954 MHAINGKVFGNLGGLTMHVGDRVSWYLMGMGNeiDIHTAHFHGHSFDYKQT-GV-------YRADVFDLFPGTFQTVEMI 1025
Cdd:cd04202     29 YFTINGKSFPATPPLVVKEGDRVRIRLINLSM--DHHPMHLHGHFFLVTATdGGpipgsapWPKDTLNVAPGERYDIEFV 106

                           90       100
                   ....*....|....*....|.
gi 1159645229 1026 PRNPGTWLLHCHVTDHIHAGM 1046
Cdd:cd04202    107 ADNPGDWMFHCHKLHHAMNGM 127
Cu-oxidase_3 pfam07732
Multicopper oxidase; This entry contains many divergent copper oxidase-like domains that are ...
 94-201 8.77e-12

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: 63.03  E-value: 8.77e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1159645229   94 FLGPIIKGEVGDSIVIHLKNFASRNYTLHPHGVtytkENEGALYPDGTGGLQKrdDAVEPGGQFTYTWDVSEDQGpaagd 173
Cdd:pfam07732   24 FPGPTIRVREGDTVVVNVTNNLDEPTSIHWHGL----QQRGTPWMDGVPGVTQ--CPIPPGQSFTYRFQVKQQAG----- 92

                           90       100
                   ....*....|....*....|....*...
gi 1159645229  174 adcvTRAYHSHIDAPRdvASGLVGPLII 201
Cdd:pfam07732   93 ----TYWYHSHTSGQQ--AAGLAGAIII 114
CuRO_1_CumA_like cd13861
The first cupredoxin domain of CumA like multicopper oxidase; This multicopper oxidase (MCO) ...
 93-201 1.12e-11

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


Pssm-ID: 259930 [Multi-domain]  Cd Length: 119  Bit Score: 62.64  E-value: 1.12e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1159645229   93 GFLGPIIKGEVGDSIVIHLKNFASRNYTLHPHGVTYtkENEgalyPDGTGGLQKrdDAVEPGGQFTYTWDVsedqgPAAG 172
Cdd:cd13861     28 QVPGPELRVRQGDTLRVRLTNRLPEPTTIHWHGLRL--PNA----MDGVPGLTQ--PPVPPGESFTYEFTP-----PDAG 94

                           90       100
                   ....*....|....*....|....*....
gi 1159645229  173 dadcvTRAYHSHIDAPRDVASGLVGPLII 201
Cdd:cd13861     95 -----TYWYHPHVGSQEQLDRGLYGPLIV 118
CuRO_1_2DMCO_NIR_like_2 cd14449
The cupredoxin domain 1 of a two-domain laccase related to nitrite reductase; The two-domain ...
 96-204 6.85e-11

The cupredoxin domain 1 of a two-domain laccase related to nitrite reductase; The two-domain laccase (small laccase) in this family differs significantly from all laccases. It resembles the two domain nitrite reductase in both sequence and structure. It consists of two cupredoxin domains and forms trimers, and hence resembles the quaternary structure of nitrite reductases more than that of large laccases. There are three trinuclear copper clusters in the enzyme localized between domains 1 and 2 of each pair of neighbor chains. 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: 61.13  E-value: 6.85e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1159645229   96 GPIIKGEVGDSIVIHLKNFASRNYTLHPHGVTYTKENEGALYPdgtgglqkrDDAVEPGGQFTYTWDVSEDQGPAAGDAD 175
Cdd:cd14449     29 GPVIEVREGDTLKILFRNTLDVPASLHPHGVDYTTASDGTGMN---------ASIVAPGDTRIYTWRTHGGYRRADGSWA 99

                           90       100       110
                   ....*....|....*....|....*....|....*.
gi 1159645229  176 CVTRA---YHSHI----DAPRDVASGLVGPLIICRK 204
Cdd:cd14449    100 EGTAGywhYHDHVfgteHGTEGLSRGLYGALIVRRV 135
CuRO_1_2DMCO_NIR_like_2 cd14449
The cupredoxin domain 1 of a two-domain laccase related to nitrite reductase; The two-domain ...
 450-558 1.17e-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: 1.17e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1159645229  450 GPVIKAEVGESIRVTFRNNASRPFSIQPHGLSYRksdegasygASSRGTESPASHVSPGATFTYEWNVPEDVGPTDQDPD 529
Cdd:cd14449     29 GPVIEVREGDTLKILFRNTLDVPASLHPHGVDYT---------TASDGTGMNASIVAPGDTRIYTWRTHGGYRRADGSWA 99

                           90       100       110
                   ....*....|....*....|....*....|....*.
gi 1159645229  530 CLT---WLYYSAV----DAVRDTSSGLVGPLLVCRK 558
Cdd:cd14449    100 EGTagyWHYHDHVfgteHGTEGLSRGLYGALIVRRV 135
CuRO_3_CumA_like cd13906
The third cupredoxin domain of CumA like multicopper oxidase; This multicopper oxidase (MCO) ...
 956-1052 1.68e-10

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


Pssm-ID: 259973 [Multi-domain]  Cd Length: 138  Bit Score: 60.09  E-value: 1.68e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1159645229  956 AINGKVFGNLGG-------LTMHVGDrvsWYLMGMGNEID-IHTAHFHGHSF-----DYKQTGV-YRADVFDLFPGtfQT 1021
Cdd:cd13906     30 AINGTSWTGGDHshlppplATLKRGR---SYVLRLVNETAfLHPMHLHGHFFrvlsrNGRPVPEpFWRDTVLLGPK--ET 104

                           90       100       110
                   ....*....|....*....|....*....|...
gi 1159645229 1022 VE--MIPRNPGTWLLHCHVTDHIHAGMETTYTV 1052
Cdd:cd13906    105 VDiaFVADNPGDWMFHCHILEHQETGMMGVIRV 137
CuRO_1_Diphenol_Ox cd13857
The first cupredoxin domain of fungal laccase, diphenol oxidase; Diphenol oxidase belongs to ...
 94-201 1.74e-10

The first cupredoxin domain of fungal laccase, diphenol oxidase; Diphenol oxidase belongs to the laccase family. It catalyzes the initial steps in melanin biosynthesis from diphenols. Melanin is one of the virulence factors of infectious fungi. In the pathogenesis of C. neoformans, melanin pigments have been shown to protect the fungal cells from oxidative and microbicidal activities of host defense systems. Laccase is a blue multicopper oxidase (MCO) which catalyzes the oxidation of a variety aromatic - notably phenolic and inorganic substances coupled to the reduction of molecular oxygen to water. It has been implicated in a wide spectrum of biological activities and, in particular, plays a key role in morphogenesis, development and lignin metabolism. Although MCOs have diverse functions, majority of them have three cupredoxin domain repeats that include one mononuclear and one trinuclear copper center. The copper ions are bound in several sites: Type 1, Type 2, and/or Type 3. The ensemble of types 2 and 3 copper is called a trinuclear cluster. MCOs oxidize their substrate by accepting electrons at a mononuclear copper center and transferring them to the active site trinuclear copper center. The cupredoxin domain 1 of 3-domain MCOs contains part the trinuclear copper binding site, which is located at the interface of domains 1 and 3.


Pssm-ID: 259926 [Multi-domain]  Cd Length: 119  Bit Score: 59.58  E-value: 1.74e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1159645229   94 FLGPIIKGEVGDSIVIHLKNFASRNYTLHPHGVTytkeNEGALYPDGTGGLQKRddAVEPGGQFTYTWDVSEDQGpaagd 173
Cdd:cd13857     28 FPGPLIEANQGDRIVVHVTNELDEPTSIHWHGLF----QNGTNWMDGTAGITQC--PIPPGGSFTYNFTVDGQYG----- 96

                           90       100
                   ....*....|....*....|....*...
gi 1159645229  174 adcvTRAYHSHIDAprDVASGLVGPLII 201
Cdd:cd13857     97 ----TYWYHSHYST--QYADGLVGPLIV 118
CuRO_1_2DMCO_NIR_like cd11024
The cupredoxin domain 1 of a two-domain laccase related to nitrite reductase; The two-domain ...
 96-201 2.75e-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. 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: 58.82  E-value: 2.75e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1159645229   96 GPIIKGEVGDSIVIHLKNFASRNYTLHPHGVTYTKEnegalypDGTGGLQkrddaVEPGGQFTYTWDvsedqgpaAGDAD 175
Cdd:cd11024     32 GPTLRATEGDLVRIHFINTGDHPHTIHFHGIHDAAM-------DGTGLGP-----IMPGESFTYEFV--------AEPAG 91

                           90       100
                   ....*....|....*....|....*...
gi 1159645229  176 cvTRAYHSHIdAP--RDVASGLVGPLII 201
Cdd:cd11024     92 --THLYHCHV-QPlkEHIAMGLYGAFIV 116
CuRO_3_CopA cd13896
The third cupredoxin domain of CopA copper resistance protein family; CopA is a multicopper ...
 957-1052 7.31e-10

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: 57.65  E-value: 7.31e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1159645229  957 INGKVFGNLGGLTMHVGDRVswylmgmgnEIDI-------HTAHFHGHSFDYKQ-TGVYRA--DVFDLFPGTFQTVEMIP 1026
Cdd:cd13896     19 INGKAYPDADPLRVREGERV---------RIVFvndtmmaHPMHLHGHFFQVENgNGEYGPrkDTVLVPPGETVSVDFDA 89

                           90       100
                   ....*....|....*....|....*.
gi 1159645229 1027 RNPGTWLLHCHVTDHIHAGMETTYTV 1052
Cdd:cd13896     90 DNPGRWAFHCHNLYHMEAGMMRVVEY 115
CuRO_1_Abr2_like cd13850
The first cupredoxin domain of a group of fungal Laccases similar to Abr2 from Aspergillus ...
 94-201 9.15e-10

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: 57.31  E-value: 9.15e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1159645229   94 FLGPIIKGEVGDSIVIHLKNFASRNYTLHPHGVtytkENEGALYPDGTGGLQKRddAVEPGGQFTYTWDVSEDQGpaagd 173
Cdd:cd13850     26 FPGPPIILDEGDEVEILVTNNLPVNTTIHFHGI----LQRGTPWSDGVPGVTQW--PIQPGGSFTYRWKAEDQYG----- 94

                           90       100
                   ....*....|....*....|....*....
gi 1159645229  174 adcvTRAYHSHIdapRDVAS-GLVGPLII 201
Cdd:cd13850     95 ----LYWYHSHY---RGYYMdGLYGPIYI 116
CuRO_D1_2dMcoN_like cd13859
The first cupredoxin domain of bacterial two domain multicopper oxidase McoN and similar ...
 96-201 1.02e-09

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


Pssm-ID: 259928 [Multi-domain]  Cd Length: 122  Bit Score: 57.49  E-value: 1.02e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1159645229   96 GPIIKGEVGDSIVIHLKNFASRNYTLHPHGVTYTkeneGALYPDGTGGLQKRddAVEPGGQFTYTWDVsEDQGpaagdad 175
Cdd:cd13859     31 GPLIHVKEGDDLVVHVTNNTTLPHTIHWHGVLQM----GSWKMDGVPGVTQP--AIEPGESFTYKFKA-ERPG------- 96

                           90       100
                   ....*....|....*....|....*..
gi 1159645229  176 cvTRAYHSHIDAPRDVA-SGLVGPLII 201
Cdd:cd13859     97 --TLWYHCHVNVNEHVGmRGMWGPLIV 121
PLN02191 PLN02191
L-ascorbate oxidase
 94-224 2.70e-09

L-ascorbate oxidase


Pssm-ID: 177843 [Multi-domain]  Cd Length: 574  Bit Score: 61.18  E-value: 2.70e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1159645229   94 FLGPIIKGEVGDSIVIHLKN-FASRNYTLHPHGVtytkENEGALYPDGTGGLQKRddAVEPGGQFTYTWDVSEdqgpaAG 172
Cdd:PLN02191    51 FPGPTIDAVAGDTIVVHLTNkLTTEGLVIHWHGI----RQKGSPWADGAAGVTQC--AINPGETFTYKFTVEK-----PG 119

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|...
gi 1159645229  173 dadcvTRAYHSHIDAPRdvASGLVGPLIIcrkGTMNTDSDK-RFDAEFILMFS 224
Cdd:PLN02191   120 -----THFYHGHYGMQR--SAGLYGSLIV---DVAKGPKERlRYDGEFNLLLS 162
SufI COG2132
Multicopper oxidase with three cupredoxin domains (includes cell division protein FtsP and ...
 954-1054 3.30e-09

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: 60.33  E-value: 3.30e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1159645229  954 MHAINGKVFGNLG-GLTMHVGDRVSWYLMGMGNeiDIHTAHFHGHSF--------DYKQTGvyRADVFDLFPGtfQTVEM 1024
Cdd:COG2132    317 VWTINGKAFDPDRpDLTVKLGERERWTLVNDTM--MPHPFHLHGHQFqvlsrngkPPPEGG--WKDTVLVPPG--ETVRI 390

                           90       100       110
                   ....*....|....*....|....*....|...
gi 1159645229 1025 I---PRNPGTWLLHCHVTDHIHAGMETTYTVLP 1054
Cdd:COG2132    391 LfrfDNYPGDWMFHCHILEHEDAGMMGQFEVVP 423
CuRO_1_LCC_like cd04206
Cupredoxin domain 1 of laccase-like multicopper oxidases; including laccase, CueO, spore coat ...
 805-896 4.60e-09

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


Pssm-ID: 259869 [Multi-domain]  Cd Length: 120  Bit Score: 55.37  E-value: 4.60e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1159645229  805 GPLLMSNIGDKIVIVFKN-LASRPYSIHAHGVK----TDSSAVAVTN-----PGETKTYVWKIPgrsssergDPPCIAWa 874
Cdd:cd04206     30 GPTIRVKEGDTVEVTVTNnLPNEPTSIHWHGLRqpgtNDGDGVAGLTqcpipPGESFTYRFTVD--------DQAGTFW- 100

                           90       100
                   ....*....|....*....|..
gi 1159645229  875 YHSAVDMvkDTYSGLIGTLVVC 896
Cdd:cd04206    101 YHSHVGG--QRADGLYGPLIVE 120
CuRO_1_AAO cd13845
The first cupredoxin domain of plant Ascorbate oxidase; Ascorbate oxidase catalyzes the ...
 93-201 1.27e-08

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: 53.99  E-value: 1.27e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1159645229   93 GFLGPIIKGEVGDSIVIHLKN-FASRNYTLHPHGVtytkENEGALYPDGTGGLQKRddAVEPGGQFTYTWDVseDQgpaA 171
Cdd:cd13845     27 QFPGPTIRATAGDTIVVELENkLPTEGVAIHWHGI----RQRGTPWADGTASVSQC--PINPGETFTYQFVV--DR---P 95

                           90       100       110
                   ....*....|....*....|....*....|
gi 1159645229  172 GdadcvTRAYHSHIDAPRdvASGLVGPLII 201
Cdd:cd13845     96 G-----TYFYHGHYGMQR--SAGLYGSLIV 118
SufI COG2132
Multicopper oxidase with three cupredoxin domains (includes cell division protein FtsP and ...
 94-224 1.46e-08

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


Pssm-ID: 441735 [Multi-domain]  Cd Length: 423  Bit Score: 58.41  E-value: 1.46e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1159645229   94 FLGPIIKGEVGDSIVIHLKNFASRNYTLHPHGVTYTKENegalypDGTGGlqkrdDAVEPGGQFTYTWDVseDQGPAagd 173
Cdd:COG2132     42 YPGPTIRVREGDRVRVRVTNRLPEPTTVHWHGLRVPNAM------DGVPG-----DPIAPGETFTYEFPV--PQPAG--- 105

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 1159645229  174 adcvTRAYHSHIDA--PRDVASGLVGPLIIcrkgtmNTDSDK--RFDAEFILMFS 224
Cdd:COG2132    106 ----TYWYHPHTHGstAEQVYRGLAGALIV------EDPEEDlpRYDRDIPLVLQ 150
CuRO_1_CumA_like cd13861
The first cupredoxin domain of CumA like multicopper oxidase; This multicopper oxidase (MCO) ...
 447-555 2.03e-08

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: 53.39  E-value: 2.03e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1159645229  447 GLLGPVIKAEVGESIRVTFRNNASRPFSIQPHGLSYRKSDEGASYgassrGTESPashVSPGATFTYEWNVPeDVGptdq 526
Cdd:cd13861     28 QVPGPELRVRQGDTLRVRLTNRLPEPTTIHWHGLRLPNAMDGVPG-----LTQPP---VPPGESFTYEFTPP-DAG---- 94

                           90       100
                   ....*....|....*....|....*....
gi 1159645229  527 dpdclTWLYYSAVDAVRDTSSGLVGPLLV 555
Cdd:cd13861     95 -----TYWYHPHVGSQEQLDRGLYGPLIV 118
ascorbase TIGR03388
L-ascorbate oxidase, plant type; Members of this protein family are the copper-containing ...
 94-233 2.61e-08

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: 57.84  E-value: 2.61e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1159645229   94 FLGPIIKGEVGDSIVIHLKN-FASRNYTLHPHGVtytkENEGALYPDGTGGLQKRddAVEPGGQFTYTWDVSEdqgpaAG 172
Cdd:TIGR03388   29 FPGPTIRAQAGDTIVVELTNkLHTEGVVIHWHGI----RQIGTPWADGTAGVTQC--AINPGETFIYNFVVDR-----PG 97

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1159645229  173 dadcvTRAYHSHIDAPRdvASGLVGPLIIcrkgtMNTDSDK---RFDAEFILMFSvmdenlSWY 233
Cdd:TIGR03388   98 -----TYFYHGHYGMQR--SAGLYGSLIV-----DVPDGEKepfHYDGEFNLLLS------DWW 143
CuRO_1_2DMCO_NIR_like_2 cd14449
The cupredoxin domain 1 of a two-domain laccase related to nitrite reductase; The two-domain ...
 803-895 2.73e-08

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


Pssm-ID: 259991 [Multi-domain]  Cd Length: 135  Bit Score: 53.81  E-value: 2.73e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1159645229  803 IQGPLLMSNIGDKIVIVFKNLASRPYSIHAHGVKTDSSAVAVTN------PGETKTYVWK--IPGRSSSERGDPPCIA-W 873
Cdd:cd14449     27 VPGPVIEVREGDTLKILFRNTLDVPASLHPHGVDYTTASDGTGMnasivaPGDTRIYTWRthGGYRRADGSWAEGTAGyW 106

                           90       100
                   ....*....|....*....|....*.
gi 1159645229  874 AYHSAV----DMVKDTYSGLIGTLVV 895
Cdd:cd14449    107 HYHDHVfgteHGTEGLSRGLYGALIV 132
CuRO_3_CumA_like cd13906
The third cupredoxin domain of CumA like multicopper oxidase; This multicopper oxidase (MCO) ...
 284-357 2.79e-08

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


Pssm-ID: 259973 [Multi-domain]  Cd Length: 138  Bit Score: 53.54  E-value: 2.79e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1159645229  284 KWHLFGMGNEAD-IHSAYFHG----------QTLIERHHRvDTISLFPATFVDAVMVPRTPGEWLLSCQVNDHIQGGMQA 352
Cdd:cd13906     55 RSYVLRLVNETAfLHPMHLHGhffrvlsrngRPVPEPFWR-DTVLLGPKETVDIAFVADNPGDWMFHCHILEHQETGMMG 133


                   ....*
gi 1159645229  353 LFKVK 357
Cdd:cd13906    134 VIRVA 138
CuRO_1_2dMco_1 cd13860
The first cupredoxin domain of bacteria two domain multicopper oxidase; This subfamily ...
 96-201 5.72e-08

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


Pssm-ID: 259929 [Multi-domain]  Cd Length: 119  Bit Score: 52.20  E-value: 5.72e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1159645229   96 GPIIKGEVGDSIVIHLKNFASRNYTLHPHGVTYTKENegalypDGTGGLQKrdDAVEPGGQFTYTWDVSEdqgpaAGdad 175
Cdd:cd13860     31 GPTIEVTEGDRVRILVTNELPEPTTVHWHGLPVPNGM------DGVPGITQ--PPIQPGETFTYEFTAKQ-----AG--- 94

                           90       100
                   ....*....|....*....|....*.
gi 1159645229  176 cvTRAYHSHIDAPRDVASGLVGPLII 201
Cdd:cd13860     95 --TYMYHSHVDEAKQEDMGLYGAFIV 118
CuRO_1_Tv-LCC_like cd13856
The first cupredoxin domain of fungal laccases similar to Tv-LCC from Trametes versicolor; ...
 94-201 7.11e-08

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


Pssm-ID: 259925 [Multi-domain]  Cd Length: 125  Bit Score: 51.95  E-value: 7.11e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1159645229   94 FLGPIIKGEVGDSIVIHLKNFAS-----RNYTLHPHGVTYTKENegalYPDGTGGLQKRddAVEPGGQFTYTWDVSEDQG 168
Cdd:cd13856     28 FPGPLITANKGDTFRITVVNQLTdptmrRSTSIHWHGIFQHGTN----YADGPAFVTQC--PIAPNHSFTYDFTAGDQAG 101

                           90       100       110
                   ....*....|....*....|....*....|...
gi 1159645229  169 paagdadcvTRAYHSHIDAprDVASGLVGPLII 201
Cdd:cd13856    102 ---------TFWYHSHLST--QYCDGLRGPLVI 123
CuRO_3_MCO_like_3 cd13909
The third cupredoxin domain of uncharacterized multicopper oxidase; Multicopper Oxidases (MCOs) ...
 990-1053 8.46e-08

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: 52.14  E-value: 8.46e-08
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1159645229  990 HTAHFHGHSF-----DYkQTGVYRaDVFDLFPGTFQTVEMIPRNPGTWLLHCHVTDHIHAGMETTYTVL 1053
Cdd:cd13909     71 HGMHLHGHHFrailpNG-ALGPWR-DTLLMDRGETREIAFVADNPGDWLLHCHMLEHAAAGMMSWFRVT 137
Cu-oxidase_3 pfam07732
Multicopper oxidase; This entry contains many divergent copper oxidase-like domains that are ...
 448-555 8.47e-08

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: 51.86  E-value: 8.47e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1159645229  448 LLGPVIKAEVGESIRVTFRNNASRPFSIQPHGLSYRKS--DEGASYgassrGTESPashVSPGATFTYEWNVPEDVGptd 525
Cdd:pfam07732   24 FPGPTIRVREGDTVVVNVTNNLDEPTSIHWHGLQQRGTpwMDGVPG-----VTQCP---IPPGQSFTYRFQVKQQAG--- 92

                           90       100       110
                   ....*....|....*....|....*....|
gi 1159645229  526 qdpdclTWLYYSAVDAVRdtSSGLVGPLLV 555
Cdd:pfam07732   93 ------TYWYHSHTSGQQ--AAGLAGAIII 114
CuRO_1_2DMCO_NIR_like cd11024
The cupredoxin domain 1 of a two-domain laccase related to nitrite reductase; The two-domain ...
 450-555 1.41e-07

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


Pssm-ID: 259910 [Multi-domain]  Cd Length: 119  Bit Score: 51.12  E-value: 1.41e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1159645229  450 GPVIKAEVGESIRVTFRNNASRPFSIQPHGLSYRKSDEGAsygassrgtespASHVSPGATFTYEWnVPEDVGptdqdpd 529
Cdd:cd11024     32 GPTLRATEGDLVRIHFINTGDHPHTIHFHGIHDAAMDGTG------------LGPIMPGESFTYEF-VAEPAG------- 91

                           90       100
                   ....*....|....*....|....*..
gi 1159645229  530 clTWLYYSAVDAVRD-TSSGLVGPLLV 555
Cdd:cd11024     92 --THLYHCHVQPLKEhIAMGLYGAFIV 116
CuRO_1_Diphenol_Ox cd13857
The first cupredoxin domain of fungal laccase, diphenol oxidase; Diphenol oxidase belongs to ...
 450-555 1.42e-07

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: 51.10  E-value: 1.42e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1159645229  450 GPVIKAEVGESIRVTFRNNASRPFSIQPHGLSYRksdeGASYGASSRG-TESPashVSPGATFTYEWNVPEDVGptdqdp 528
Cdd:cd13857     30 GPLIEANQGDRIVVHVTNELDEPTSIHWHGLFQN----GTNWMDGTAGiTQCP---IPPGGSFTYNFTVDGQYG------ 96

                           90       100
                   ....*....|....*....|....*..
gi 1159645229  529 dclTWLYYSAVDAvrDTSSGLVGPLLV 555
Cdd:cd13857     97 ---TYWYHSHYST--QYADGLVGPLIV 118
CuRO_3_MaLCC_like cd13901
The third cupredoxin domain of the fungal laccases similar to Ma-LCC from Melanocarpus ...
 970-1046 1.74e-07

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: 51.84  E-value: 1.74e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1159645229  970 MHVGDRVSWYLMGMGNEIDI-HTAHFHGHSFdY--KQ-TGVY-------------RADVFDLFPGTFQTVEMIPRNPGTW 1032
Cdd:cd13901     60 IELPKANKWVYIVIQNNSPLpHPIHLHGHDF-YilAQgTGTFdddgtilnlnnppRRDVAMLPAGGYLVIAFKTDNPGAW 138

                           90
                   ....*....|....
gi 1159645229 1033 LLHCHVTDHIHAGM 1046
Cdd:cd13901    139 LMHCHIAWHASGGL 152
CuRO_1_Fet3p cd13851
The first Cupredoxin domain of multicopper oxidase Fet3P; Fet3p catalyzes the ferroxidase ...
 97-201 2.26e-07

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: 50.73  E-value: 2.26e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1159645229   97 PIIKGEVGDSIVIHLKN-FASRNYTLHPHGVTYTkeneGALYPDGTGGLQKRDdaVEPGGQFTYTWDVSEDQGpaagdad 175
Cdd:cd13851     32 PPIEVNKGDTVVIHATNsLGDQPTSLHFHGLFQN----GTNYMDGPVGVTQCP--IPPGQSFTYEFTVDTQVG------- 98

                           90       100
                   ....*....|....*....|....*.
gi 1159645229  176 cvTRAYHSHIDAprDVASGLVGPLII 201
Cdd:cd13851     99 --TYWYHSHDGG--QYPDGLRGPFII 120
CuRO_3_Fet3p cd13899
The third Cupredoxin domain of multicopper oxidase Fet3p; Fet3p catalyzes the ferroxidase ...
 990-1054 4.66e-07

The third Cupredoxin domain of multicopper oxidase Fet3p; Fet3p catalyzes the ferroxidase reaction, which couples the oxidation of Fe(II) to Fe(III) with the four-electron reduction of molecular oxygen to water. Fet3p is a type I membrane protein with the amino-terminal oxidase domain in the extracellular space and the carboxyl terminus in the cytoplasm. The periplasmic produced Fe(III) is transferred to the permease Ftr1p for import into the cytosol. The four copper ions are inserted post-translationally and are essential for catalytic activity, thus linking copper and iron homeostasis. Like other related multicopper oxidases (MCOs), Fet3p is composed of three cupredoxin domains that include one mononuclear and one trinuclear copper center. The copper ions are bound in several sites: Type 1, Type 2, and/or Type 3. The ensemble of types 2 and 3 copper is called a trinuclear cluster. MCOs oxidize their substrate by accepting electrons at a mononuclear copper center and transferring them to the active site trinuclear copper center. The cupredoxin domain 3 of 3-domain MCOs contains the Type 1 (T1) copper binding site and part the trinuclear copper binding site, which is located at the interface of domains 1 and 3.


Pssm-ID: 259966 [Multi-domain]  Cd Length: 160  Bit Score: 50.72  E-value: 4.66e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1159645229  990 HTAHFHGHSFD--YKQTGVY----------------RADVFDLFPGTFQTVEMIPRNPGTWLLHCHVTDHIHAGMETTYT 1051
Cdd:cd13899     78 HPFHLHGHKFQvvQRSPDVAsddpnppinefpenpmRRDTVMVPPGGSVVIRFRADNPGVWFFHCHIEWHLEAGLAATFI 157


                   ...
gi 1159645229 1052 VLP 1054
Cdd:cd13899    158 EAP 160
CuRO_1_MaLCC_like cd13854
The first cupredoxin domain of the fungal laccases similar to Ma-LCC from Melanocarpus ...
 96-201 5.06e-07

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: 49.55  E-value: 5.06e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1159645229   96 GPIIKGEVGDSIVIHLKNFASRNYT-LHPHGVTYTKENegalYPDGTGGLQKRddAVEPGGQFTYTWDVSEdQGpaagda 174
Cdd:cd13854     33 GPLIEANWGDTIEVTVINKLQDNGTsIHWHGIRQLNTN----WQDGVPGVTEC--PIAPGDTRTYRFRATQ-YG------ 99

                           90       100
                   ....*....|....*....|....*..
gi 1159645229  175 dcvTRAYHSHIDAprDVASGLVGPLII 201
Cdd:cd13854    100 ---TSWYHSHYSA--QYGDGVVGPIVI 121
CuRO_3_Tv-LCC_like cd13903
The third cupredoxin domain of the fungal laccases similar to Tv-LCC from Trametes Versicolor; ...
 984-1046 5.11e-07

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: 50.36  E-value: 5.11e-07
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1159645229  984 GNEIDIHTAHFHGHSFDYKQ---TGVY------RADVFDL-FPGTFQTVEMIPRNPGTWLLHCHVTDHIHAGM 1046
Cdd:cd13903     67 GAIGGPHPFHLHGHAFSVVRsagSNTYnyvnpvRRDVVSVgTPGDGVTIRFVTDNPGPWFLHCHIDWHLEAGL 139
Cu-oxidase pfam00394
Multicopper oxidase; Many of the proteins in this family contain multiple similar copies of ...
 223-360 1.05e-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: 49.24  E-value: 1.05e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1159645229  223 FSVMDENLSWYlEDNIRTYCSEPSEVDKDDEDFQESNKMHSINGYMYGYLPNLTMCVEDKVKWHLFgMGNEADIHSAYFH 302
Cdd:pfam00394    1 EDYVITLSDWY-HKDAKDLEKELLASGKAPTDFPPVPDAVLINGKDGASLATLTVTPGKTYRLRII-NVALDDSLNFSIE 78

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1159645229  303 GQ--TLIE---RHH---RVDTISLFPATFVDAVMVP-RTPGEWLLSCQVN-DHIQGGMQALFKVKECG 360
Cdd:pfam00394   79 GHkmTVVEvdgVYVnpfTVDSLDIFPGQRYSVLVTAnQDPGNYWIVASPNiPAFDNGTAAAILRYSGA 146
CuRO_3_MCO_like_2 cd13908
The third cupredoxin domain of uncharacterized multicopper oxidase; Multicopper Oxidases (MCOs) ...
 957-1045 1.41e-06

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


Pssm-ID: 259975 [Multi-domain]  Cd Length: 122  Bit Score: 48.22  E-value: 1.41e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1159645229  957 INGKVFGNLGG-LTMHVGDRvswYLMGMGNEI-DIHTAHFHGHSF-----DYKQTGVYRADVFDLFPGTFQTVEMIPRNP 1029
Cdd:cd13908     23 INGKSYPDEDPpLVVQQGRR---YRLVFRNASdDAHPMHLHRHTFevtriDGKPTSGLRKDVVMLGGYQRVEVDFVADNP 99

                           90
                   ....*....|....*.
gi 1159645229 1030 GTWLLHCHVTDHIHAG 1045
Cdd:cd13908    100 GLTLFHCHQQLHMDYG 115
CuRO_3_McoC_like cd13902
The third cupredoxin domain of a multicopper oxidase McoC and similar proteins; This family ...
 954-1046 2.26e-06

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: 47.78  E-value: 2.26e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1159645229  954 MHAINGKVFG-NLGGLTMHVGDRVSWYLMgmgNEIDI-HTAHFHGHSF------DYKQTGVYRA--DVFDLFPGTFQTVE 1023
Cdd:cd13902     20 MFLINGKTFDmNRIDFVAKVGEVEVWEVT---NTSHMdHPFHLHGTQFqvleidGNPQKPEYRAwkDTVNLPPGEAVRIA 96

                           90       100
                   ....*....|....*....|...
gi 1159645229 1024 MIPRNPGTWLLHCHVTDHIHAGM 1046
Cdd:cd13902     97 TRQDDPGMWMYHCHILEHEDAGM 119
CuRO_1_Diphenol_Ox cd13857
The first cupredoxin domain of fungal laccase, diphenol oxidase; Diphenol oxidase belongs to ...
 805-895 2.45e-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: 47.64  E-value: 2.45e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1159645229  805 GPLLMSNIGDKIVIVFKNLASRPYSIHAHGVKTDSS-----AVAVTN----PGETKTYVWKIPGRSSSergdppciAWaY 875
Cdd:cd13857     30 GPLIEANQGDRIVVHVTNELDEPTSIHWHGLFQNGTnwmdgTAGITQcpipPGGSFTYNFTVDGQYGT--------YW-Y 100

                           90       100
                   ....*....|....*....|.
gi 1159645229  876 HSAVDMvkdTYS-GLIGTLVV 895
Cdd:cd13857    101 HSHYST---QYAdGLVGPLIV 118
CuRO_3_LCC_like cd04207
Cupredoxin domain 3 of laccase-like multicopper oxidases; including laccase, CueO, spore coat ...
 263-354 3.74e-06

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: 47.45  E-value: 3.74e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1159645229  263 SING----YMYGYLPNLTMCVEDKVKWHLFGMGNEADIHSAYFHGQtlierHHRV--------------------DTISL 318
Cdd:cd04207     21 VINGmpfkEGDANTDIFSVEAGDVVEIVLINAGNHDMQHPFHLHGH-----SFWVlgsgggpfdaplnltnppwrDTVLV 95

                           90       100       110
                   ....*....|....*....|....*....|....*.
gi 1159645229  319 FPATFVDAVMVPRTPGEWLLSCQVNDHIQGGMQALF 354
Cdd:cd04207     96 PPGGWVVIRFKADNPGVWMLHCHILEHEDAGMMTVF 131
CuRO_3_AAO cd13893
The third cupredoxin domain of plant Ascorbate oxidase; Ascorbate oxidase catalyzes the ...
 985-1046 3.92e-06

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: 47.80  E-value: 3.92e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1159645229  985 NEIDIHTAHFHGHSF---DYKqTGVYRA---------------DVFDLFPGTFQTVEMIPRNPGTWLLHCHVTDHIHAGM 1046
Cdd:cd13893     62 NASEQHPWHLHGHDFwvlGYG-LGGFDPaadpsslnlvnppmrNTVTIFPYGWTALRFKADNPGVWAFHCHIEWHFHMGM 140
CuRO_1_2dMco_1 cd13860
The first cupredoxin domain of bacteria two domain multicopper oxidase; This subfamily ...
 450-555 5.49e-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: 46.42  E-value: 5.49e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1159645229  450 GPVIKAEVGESIRVTFRNNASRPFSIQPHGLSYRKSDEGASygassrgtESPASHVSPGATFTYEWNVpEDVGptdqdpd 529
Cdd:cd13860     31 GPTIEVTEGDRVRILVTNELPEPTTVHWHGLPVPNGMDGVP--------GITQPPIQPGETFTYEFTA-KQAG------- 94

                           90       100
                   ....*....|....*....|....*.
gi 1159645229  530 clTWLYYSAVDAVRDTSSGLVGPLLV 555
Cdd:cd13860     95 --TYMYHSHVDEAKQEDMGLYGAFIV 118
CuRO_1_Tv-LCC_like cd13856
The first cupredoxin domain of fungal laccases similar to Tv-LCC from Trametes versicolor; ...
 450-555 6.13e-06

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


Pssm-ID: 259925 [Multi-domain]  Cd Length: 125  Bit Score: 46.56  E-value: 6.13e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1159645229  450 GPVIKAEVGESIRVTFRNNAS-----RPFSIQPHGLSYRKS--DEGASYgassrGTESPashVSPGATFTYEWNVPEDVG 522
Cdd:cd13856     30 GPLITANKGDTFRITVVNQLTdptmrRSTSIHWHGIFQHGTnyADGPAF-----VTQCP---IAPNHSFTYDFTAGDQAG 101

                           90       100       110
                   ....*....|....*....|....*....|...
gi 1159645229  523 ptdqdpdclTWLYYSAVDAvrDTSSGLVGPLLV 555
Cdd:cd13856    102 ---------TFWYHSHLST--QYCDGLRGPLVI 123
CuRO_1_2DMCO_NIR_like cd11024
The cupredoxin domain 1 of a two-domain laccase related to nitrite reductase; The two-domain ...
 803-895 6.97e-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: 46.11  E-value: 6.97e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1159645229  803 IQGPLLMSNIGDKIVIVFKNLASRPYSIHAHGV---KTDSSAVAVTNPGETKTYVWKipgrssserGDPPCIaWAYHSAV 879
Cdd:cd11024     30 VPGPTLRATEGDLVRIHFINTGDHPHTIHFHGIhdaAMDGTGLGPIMPGESFTYEFV---------AEPAGT-HLYHCHV 99

                           90
                   ....*....|....*..
gi 1159645229  880 DMVKD-TYSGLIGTLVV 895
Cdd:cd11024    100 QPLKEhIAMGLYGAFIV 116
CuRO_1_CueO_FtsP cd04232
The first Cupredoxin domain of the multicopper oxidase CueO, the cell division protein FtsP, ...
 94-201 6.98e-06

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


Pssm-ID: 259894 [Multi-domain]  Cd Length: 120  Bit Score: 46.41  E-value: 6.98e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1159645229   94 FLGPIIKGEVGDSIVIHLKNFASRNYTLHPHGVTYTKENEGalypdgtGGLQkrddAVEPGGQFTYTWDVseDQgPAAgd 173
Cdd:cd04232     29 YLGPTIRVKKGDTVRINVTNNLDEETTVHWHGLHVPGEMDG-------GPHQ----PIAPGQTWSPTFTI--DQ-PAA-- 92

                           90       100       110
                   ....*....|....*....|....*....|
gi 1159645229  174 adcvTRAYHSHIDA--PRDVASGLVGPLII 201
Cdd:cd04232     93 ----TLWYHPHTHGktAEQVYRGLAGLFII 118
CuRO_1_CumA_like cd13861
The first cupredoxin domain of CumA like multicopper oxidase; This multicopper oxidase (MCO) ...
 805-895 7.95e-06

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


Pssm-ID: 259930 [Multi-domain]  Cd Length: 119  Bit Score: 46.07  E-value: 7.95e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1159645229  805 GPLLMSNIGDKIVIVFKNLASRPYSIHAHGVKTDS----------SAVAvtnPGETKTYVWKIPgrsssergdPPCIAWa 874
Cdd:cd13861     31 GPELRVRQGDTLRVRLTNRLPEPTTIHWHGLRLPNamdgvpgltqPPVP---PGESFTYEFTPP---------DAGTYW- 97

                           90       100
                   ....*....|....*....|.
gi 1159645229  875 YHSAVDMVKDTYSGLIGTLVV 895
Cdd:cd13861     98 YHPHVGSQEQLDRGLYGPLIV 118
CuRO_1_2DMCO_NIR_like cd11024
The cupredoxin domain 1 of a two-domain laccase related to nitrite reductase; The two-domain ...
 973-1055 9.31e-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: 45.72  E-value: 9.31e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1159645229  973 GDRVSWYLMGMGNeiDIHTAHFHGHSFDYKQTGVYRadvfDLFPGTFQTVEMIPRNPGTWLLHCHV---TDHIHAGMETT 1049
Cdd:cd11024     40 GDLVRIHFINTGD--HPHTIHFHGIHDAAMDGTGLG----PIMPGESFTYEFVAEPAGTHLYHCHVqplKEHIAMGLYGA 113


                   ....*.
gi 1159645229 1050 YTVLPR 1055
Cdd:cd11024    114 FIVDPK 119
CuRO_1_LCC_plant cd13849
The first cupredoxin domain of plant laccases; Laccase is a blue multicopper oxidase (MCO) ...
 94-201 9.52e-06

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: 45.71  E-value: 9.52e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1159645229   94 FLGPIIKGEVGDSIVIHLKNFASRNYTLHPHGVtYTKENEGAlypDGTGGLQKRddAVEPGGQFTYTWDVSEDQGpaagd 173
Cdd:cd13849     26 FPGPTIRVHEGDTVVVNVTNRSPYNITIHWHGI-RQLRSGWA---DGPAYITQC--PIQPGQSYTYRFTVTGQEG----- 94

                           90       100
                   ....*....|....*....|....*...
gi 1159645229  174 adcvTRAYHSHIDAPRdvaSGLVGPLII 201
Cdd:cd13849     95 ----TLWWHAHISWLR---ATVYGAFII 115
PLN02191 PLN02191
L-ascorbate oxidase
 988-1050 9.91e-06

L-ascorbate oxidase


Pssm-ID: 177843 [Multi-domain]  Cd Length: 574  Bit Score: 49.63  E-value: 9.91e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1159645229  988 DIHTAHFHGHSF--------------DYKQTGVYRADVFD---LFPGTFQTVEMIPRNPGTWLLHCHVTDHIHAGMETTY 1050
Cdd:PLN02191   465 EIHPWHLHGHDFwvlgygdgkfkpgiDEKTYNLKNPPLRNtaiLYPYGWTAIRFVTDNPGVWFFHCHIEPHLHMGMGVVF 544
CuRO_1_McoC_like cd13855
The first cupredoxin domain of a multicopper oxidase McoC and similar proteins; This family ...
 96-201 1.37e-05

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


Pssm-ID: 259924 [Multi-domain]  Cd Length: 121  Bit Score: 45.54  E-value: 1.37e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1159645229   96 GPIIKGEVGDSIVIHLKNFASRNYTLHPHGVTYTKENEGALYpdgtgglqkrdDAVEPGGQFTYTWDVSEDqgpAAGdad 175
Cdd:cd13855     32 GPLIEVFEGDTVEITFRNRLPEPTTVHWHGLPVPPDQDGNPH-----------DPVAPGNDRVYRFTLPQD---SAG--- 94

                           90       100
                   ....*....|....*....|....*...
gi 1159645229  176 cvTRAY--HSHIDAPRDVASGLVGPLII 201
Cdd:cd13855     95 --TYWYhpHPHGHTAEQVYRGLAGAFVV 120
CuRO_1_CuNIR_like cd04201
Cupredoxin domain 1 of Copper-containing nitrite reductase and two-domain laccase; ...
 958-1055 1.46e-05

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: 45.56  E-value: 1.46e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1159645229  958 NGKVFGNLggLTMHVGDRVSWYLMGMGNEIDIHTAHFHGHSfdyKQTGVYRADVFDlfPGTFQTVEMIPRNPGTWLLHCH 1037
Cdd:cd04201     27 DGDIPGPM--LRVREGDTVELHFSNNPSSTMPHNIDFHAAT---GAGGGAGATFIA--PGETSTFSFKATQPGLYVYHCA 99

                           90       100
                   ....*....|....*....|.
gi 1159645229 1038 VTD---HIHAGMETTYTVLPR 1055
Cdd:cd04201    100 VAPvpmHIANGMYGLILVEPK 120
CuRO_3_tcLLC2_insect_like cd13905
The third cupredoxin domain of the insect laccases similar to laccase 2 in Tribolium castaneum; ...
 990-1063 2.12e-05

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: 46.13  E-value: 2.12e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1159645229  990 HTAHFHGHSF--------DY-KQTGVYRA--------DVFDLFPGTFQ------TVeMIPR-----------NPGTWLLH 1035
Cdd:cd13905     70 HPFHLHGHSFyvlgmgfpGYnSTTGEILSqnwnnkllDRGGLPGRNLVnpplkdTV-VVPNggyvvirfradNPGYWLLH 148

                           90       100
                   ....*....|....*....|....*...
gi 1159645229 1036 CHVTDHIHAGMETTYTVlpREDKQPLLP 1063
Cdd:cd13905    149 CHIEFHLLEGMALVLKV--GEPSDPPPP 174
CuRO_1_Tth-MCO_like cd13853
The first cupredoxin domain of the bacterial laccases similar to Tth-MCO from Thermus ...
 94-201 3.00e-05

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


Pssm-ID: 259922 [Multi-domain]  Cd Length: 139  Bit Score: 44.94  E-value: 3.00e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1159645229   94 FLGPIIKGEVGDSIVIHLKN----------------FASRNYT-LHPHGVTYTkenegalyPDGTGglqkrDD---AVEP 153
Cdd:cd13853     29 IPGPTLRVRPGDTLRITLKNdlppegaaneapapntPHCPNTTnLHFHGLHVS--------PTGNS-----DNvflTIAP 95

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|.
gi 1159645229  154 GGQFTYTWDVSEDQGPaaGdadcvTRAYHSHID---APrDVASGLVGPLII 201
Cdd:cd13853     96 GESFTYEYDIPADHPP--G-----TYWYHPHLHgstAL-QVAGGMAGALVV 138
CuRO_D1_2dMcoN_like cd13859
The first cupredoxin domain of bacterial two domain multicopper oxidase McoN and similar ...
 802-895 3.43e-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: 44.39  E-value: 3.43e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1159645229  802 EIQGPLLMSNIGDKIVIVFKNLASRPYSIHAHGV-KTDS----SAVAVTN----PGETKTYVWKipgrssserGDPPCIA 872
Cdd:cd13859     28 QVPGPLIHVKEGDDLVVHVTNNTTLPHTIHWHGVlQMGSwkmdGVPGVTQpaiePGESFTYKFK---------AERPGTL 98

                           90       100
                   ....*....|....*....|....
gi 1159645229  873 WaYHSAVDMVK-DTYSGLIGTLVV 895
Cdd:cd13859     99 W-YHCHVNVNEhVGMRGMWGPLIV 121
CuRO_3_LCC_plant cd13897
The third cupredoxin domain of the plant laccases; Laccase is a blue multicopper oxidase (MCO) ...
 988-1052 5.78e-05

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: 44.17  E-value: 5.78e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1159645229  988 DIHTAHFHGHSFdY---KQTGVYRA--DV--FDLF-PGTFQTVeMIPR-----------NPGTWLLHCHVTDHIHAGMET 1048
Cdd:cd13897     55 ENHPMHLHGFDF-YvvgRGFGNFDPstDPatFNLVdPPLRNTV-GVPRggwaairfvadNPGVWFMHCHFERHTSWGMAT 132


                   ....
gi 1159645229 1049 TYTV 1052
Cdd:cd13897    133 VFIV 136
CuRO_1_CuNIR cd11020
Cupredoxin domain 1 of Copper-containing nitrite reductase; Copper-containing nitrite ...
 805-895 1.26e-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: 1.26e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1159645229  805 GPLLMSNIGDKIVIVFKNLASR--PYSIHAHGVKTDSSAVAVT-NPGETKTYVWK--IPGrsssergdppciAWAYHSAV 879
Cdd:cd11020     32 GPVIRVREGDTVELTLTNPGTNtmPHSIDFHAATGPGGGEFTTiAPGETKTFSFKalYPG------------VFMYHCAT 99

                           90
                   ....*....|....*..
gi 1159645229  880 D-MVKDTYSGLIGTLVV 895
Cdd:cd11020    100 ApVLMHIANGMYGAIIV 116
CuRO_D2_2dMcoN_like cd04202
The second cupredoxin domain of bacterial two domain multicopper oxidase McoN and similar ...
 216-357 1.53e-04

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: 43.01  E-value: 1.53e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1159645229  216 DAEFILMFSvmdenlSWYLEDNirtycSEPSEVDKDDEDFqesnkmHSINGYMYGYLPNLTMCVEDKVKWHLFGMGNeaD 295
Cdd:cd04202      1 DRDYTLVLQ------EWFVDPG-----TTPMPPEGMDFNY------FTINGKSFPATPPLVVKEGDRVRIRLINLSM--D 61

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1159645229  296 IHSAYFHGQT---------LIERHHRV--DTISLFPATFVDAVMVPRTPGEWLLSCQVNDHI----QGGMQALFKVK 357
Cdd:cd04202     62 HHPMHLHGHFflvtatdggPIPGSAPWpkDTLNVAPGERYDIEFVADNPGDWMFHCHKLHHAmngmGGGMMTLIGYE 138
Cu-oxidase pfam00394
Multicopper oxidase; Many of the proteins in this family contain multiple similar copies of ...
 918-1050 2.17e-04

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: 42.69  E-value: 2.17e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1159645229  918 VFDENESWYlDENIKTYSPNPHLVDKEDEEF-LESNKmHAINGKVFGNLGGLTMHVGDRVSWYLMgMGNEIDIHTAHFHG 996
Cdd:pfam00394    3 YVITLSDWY-HKDAKDLEKELLASGKAPTDFpPVPDA-VLINGKDGASLATLTVTPGKTYRLRII-NVALDDSLNFSIEG 79

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1159645229  997 HSF-----DYKQTGVYRADVFDLFPGTFQTVeMI--PRNPGTWLLHCHVT-DHIHAGMETTY 1050
Cdd:pfam00394   80 HKMtvvevDGVYVNPFTVDSLDIFPGQRYSV-LVtaNQDPGNYWIVASPNiPAFDNGTAAAI 140
CuRO_1_McoC_like cd13855
The first cupredoxin domain of a multicopper oxidase McoC and similar proteins; This family ...
 447-520 2.41e-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: 42.08  E-value: 2.41e-04
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1159645229  447 GLLGPVIKAEVGESIRVTFRNNASRPFSIQPHGLSYRKSDEGasygassrgteSPASHVSPGATFTYEWNVPED 520
Cdd:cd13855     29 SVPGPLIEVFEGDTVEITFRNRLPEPTTVHWHGLPVPPDQDG-----------NPHDPVAPGNDRVYRFTLPQD 91
CuRO_3_Abr2_like cd13898
The third cupredoxin domain of a group of fungal Laccases similar to Abr2 from Aspergillus ...
 1007-1046 3.61e-04

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: 42.24  E-value: 3.61e-04
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....
gi 1159645229 1007 YRaDVFDLFPGTFQTVEMIPR----NPGTWLLHCHVTDHIHAGM 1046
Cdd:cd13898    115 LR-DTFTTPPSTEGPSWLVIRyhvvNPGAWLLHCHIQSHLAGGM 157
ascorbOXfungal TIGR03390
L-ascorbate oxidase, fungal type; This model describes a family of fungal ascorbate oxidases, ...
 987-1057 4.27e-04

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


Pssm-ID: 132431 [Multi-domain]  Cd Length: 538  Bit Score: 44.06  E-value: 4.27e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1159645229  987 IDIHTAHFHG-HSFDYKQ-TGVYRA---------------DVFDLFPGTFQTVEMIP----------RNPGTWLLHCHVT 1039
Cdd:TIGR03390  439 VDTHPFHAHGrHFYDIGGgDGEYNAtaneaklenytpvlrDTTMLYRYAVKVVPGAPagwrawrirvTNPGVWMMHCHIL 518

                           90
                   ....*....|....*...
gi 1159645229 1040 DHIHAGMETTYTVLPRED 1057
Cdd:TIGR03390  519 QHMVMGMQTVWVFGDAED 536
CuRO_D1_2dMcoN_like cd13859
The first cupredoxin domain of bacterial two domain multicopper oxidase McoN and similar ...
 450-522 6.58e-04

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


Pssm-ID: 259928 [Multi-domain]  Cd Length: 122  Bit Score: 40.54  E-value: 6.58e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1159645229  450 GPVIKAEVGESIRVTFRNNASRPFSIQPHGLSYRKS--DEGASygassrGTESPAshVSPGATFTYEW------------ 515
Cdd:cd13859     31 GPLIHVKEGDDLVVHVTNNTTLPHTIHWHGVLQMGSwkMDGVP------GVTQPA--IEPGESFTYKFkaerpgtlwyhc 102


                   ....*....
gi 1159645229  516 --NVPEDVG 522
Cdd:cd13859    103 hvNVNEHVG 111
CuRO_1_CuNIR_like cd04201
Cupredoxin domain 1 of Copper-containing nitrite reductase and two-domain laccase; ...
 803-895 7.32e-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: 40.55  E-value: 7.32e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1159645229  803 IQGPLLMSNIGDKIVIVFKNLASR--PYSIHAHGV--KTDSSAVAVTNPGETKTYVWK--IPGrsssergdppciAWAYH 876
Cdd:cd04201     30 IPGPMLRVREGDTVELHFSNNPSStmPHNIDFHAAtgAGGGAGATFIAPGETSTFSFKatQPG------------LYVYH 97

                           90       100
                   ....*....|....*....|
gi 1159645229  877 SAVDMVK-DTYSGLIGTLVV 895
Cdd:cd04201     98 CAVAPVPmHIANGMYGLILV 117
CuRO_1_McoC_like cd13855
The first cupredoxin domain of a multicopper oxidase McoC and similar proteins; This family ...
 805-895 8.07e-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: 40.54  E-value: 8.07e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1159645229  805 GPLLMSNIGDKIVIVFKNLASRPYSIHAHGV----KTDSSAVAVTNPGETKTYVWKIPGRSSSergdppciAWAYHSAVD 880
Cdd:cd13855     32 GPLIEVFEGDTVEITFRNRLPEPTTVHWHGLpvppDQDGNPHDPVAPGNDRVYRFTLPQDSAG--------TYWYHPHPH 103

                           90
                   ....*....|....*..
gi 1159645229  881 M--VKDTYSGLIGTLVV 895
Cdd:cd13855    104 GhtAEQVYRGLAGAFVV 120
CuRO_1_2dMco_1 cd13860
The first cupredoxin domain of bacteria two domain multicopper oxidase; This subfamily ...
 805-895 8.54e-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: 40.26  E-value: 8.54e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1159645229  805 GPLLMSNIGDKIVIVFKNLASRPYSIHAHGVKTDSSAVAVTN-------PGETKTYVWKIpgrsssergDPPCIAWaYHS 877
Cdd:cd13860     31 GPTIEVTEGDRVRILVTNELPEPTTVHWHGLPVPNGMDGVPGitqppiqPGETFTYEFTA---------KQAGTYM-YHS 100

                           90
                   ....*....|....*...
gi 1159645229  878 AVDMVKDTYSGLIGTLVV 895
Cdd:cd13860    101 HVDEAKQEDMGLYGAFIV 118
CuRO_3_MCO_like_4 cd13910
The third cupredoxin domain of uncharacterized multicopper oxidase; Multicopper Oxidases (MCOs) ...
 990-1046 8.70e-04

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


Pssm-ID: 259977 [Multi-domain]  Cd Length: 166  Bit Score: 41.13  E-value: 8.70e-04
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1159645229  990 HTAHFHGHSF-------DYKQTGVYRADVFDLFPGTFQ----TVEmIPR-----------NPGTWLLHCHVTDHIHAGM 1046
Cdd:cd13910     83 HPFHLHGHKFwvlgsgdGRYGGGGYTAPDGTSLNTTNPlrrdTVS-VPGfgwavlrfvadNPGLWAFHCHILWHMAAGM 160
Cu-oxidase_3 pfam07732
Multicopper oxidase; This entry contains many divergent copper oxidase-like domains that are ...
 805-895 1.03e-03

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: 39.92  E-value: 1.03e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1159645229  805 GPLLMSNIGDKIVIVFKNLASRPYSIHAHGVKTDSS-----AVAVTN----PGETKTYVWKIPGRSSSergdppciAWaY 875
Cdd:pfam07732   26 GPTIRVREGDTVVVNVTNNLDEPTSIHWHGLQQRGTpwmdgVPGVTQcpipPGQSFTYRFQVKQQAGT--------YW-Y 96

                           90       100
                   ....*....|....*....|
gi 1159645229  876 HSAVDMVKdtYSGLIGTLVV 895
Cdd:pfam07732   97 HSHTSGQQ--AAGLAGAIII 114
CuRO_1_AAO cd13845
The first cupredoxin domain of plant Ascorbate oxidase; Ascorbate oxidase catalyzes the ...
 450-555 1.44e-03

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: 39.74  E-value: 1.44e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1159645229  450 GPVIKAEVGESIRVTFRNN-ASRPFSIQPHGLSYRksdeGASYgasSRGTESPAS-HVSPGATFTYEWNVpedvgptDQD 527
Cdd:cd13845     30 GPTIRATAGDTIVVELENKlPTEGVAIHWHGIRQR----GTPW---ADGTASVSQcPINPGETFTYQFVV-------DRP 95

                           90       100
                   ....*....|....*....|....*...
gi 1159645229  528 PdclTWLYYSAVDAVRdtSSGLVGPLLV 555
Cdd:cd13845     96 G---TYFYHGHYGMQR--SAGLYGSLIV 118
CuRO_1_MaLCC_like cd13854
The first cupredoxin domain of the fungal laccases similar to Ma-LCC from Melanocarpus ...
 805-895 1.46e-03

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: 39.53  E-value: 1.46e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1159645229  805 GPLLMSNIGDKIVI-VFKNLASRPYSIHAHGVK-----TDSSAVAVTN----PGETKTYVWKIPGRSSSergdppciaWa 874
Cdd:cd13854     33 GPLIEANWGDTIEVtVINKLQDNGTSIHWHGIRqlntnWQDGVPGVTEcpiaPGDTRTYRFRATQYGTS---------W- 102

                           90       100
                   ....*....|....*....|....*.
gi 1159645229  875 YHSAvdmvkdtYS-----GLIGTLVV 895
Cdd:cd13854    103 YHSH-------YSaqygdGVVGPIVI 121
CuRO_3_AAO_like_2 cd13895
The third cupredoxin domain of Ascorbate oxidase homologs; This family includes fungal ...
 988-1049 1.68e-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: 1.68e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1159645229  988 DIHTAHFHG-HSFDYKQ-TGVYRADVFD-----------------LFPGTFQTVEMIP-------------RNPGTWLLH 1035
Cdd:cd13895     91 DAHPWHAHGaHYYDLGSgLGTYSATALAneeklrgynpirrdttmLYRYGGKGYYPPPgtgsgwrawrlrvDDPGVWMLH 170

                           90
                   ....*....|....
gi 1159645229 1036 CHVTDHIHAGMETT 1049
Cdd:cd13895    171 CHILQHMIMGMQTV 184
PLN02168 PLN02168
copper ion binding / pectinesterase
 450-522 1.99e-03

copper ion binding / pectinesterase


Pssm-ID: 215113 [Multi-domain]  Cd Length: 545  Bit Score: 42.27  E-value: 1.99e-03
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1159645229  450 GPVIKAEVGESIRVTFRNNASRPFSIQPHGLSYRKSdegaSYGASSRGTESPashVSPGATFTYEWNVPEDVG 522
Cdd:PLN02168    56 GPLLNATANDVINVNIFNNLTEPFLMTWNGLQLRKN----SWQDGVRGTNCP---ILPGTNWTYRFQVKDQIG 121
CuRO_1_Fet3p cd13851
The first Cupredoxin domain of multicopper oxidase Fet3P; Fet3p catalyzes the ferroxidase ...
 451-555 2.47e-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: 38.79  E-value: 2.47e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1159645229  451 PVIKAEVGESIRVTFRNN-ASRPFSIQPHGLSYRksdeGASY--GASSRgTESPashVSPGATFTYEWNVPEDVGptdqd 527
Cdd:cd13851     32 PPIEVNKGDTVVIHATNSlGDQPTSLHFHGLFQN----GTNYmdGPVGV-TQCP---IPPGQSFTYEFTVDTQVG----- 98

                           90       100
                   ....*....|....*....|....*...
gi 1159645229  528 pdclTWLYYSAVDAvrDTSSGLVGPLLV 555
Cdd:cd13851     99 ----TYWYHSHDGG--QYPDGLRGPFII 120
CuRO_1_CuNIR_like cd04201
Cupredoxin domain 1 of Copper-containing nitrite reductase and two-domain laccase; ...
 96-201 2.96e-03

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


Pssm-ID: 259864 [Multi-domain]  Cd Length: 120  Bit Score: 38.63  E-value: 2.96e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1159645229   96 GPIIKGEVGDSIVIHLKNFASrnyTLHPHGVTYtkenEGALYPDGTGGLQkrddAVEPGGQFTYTWDVSEdqgpaAGdad 175
Cdd:cd04201     32 GPMLRVREGDTVELHFSNNPS---STMPHNIDF----HAATGAGGGAGAT----FIAPGETSTFSFKATQ-----PG--- 92

                           90       100
                   ....*....|....*....|....*..
gi 1159645229  176 cvTRAYHSHIDA-PRDVASGLVGPLII 201
Cdd:cd04201     93 --LYVYHCAVAPvPMHIANGMYGLILV 117
Cupredoxin cd00920
Cupredoxin superfamily; Cupredoxins contain type I copper centers and are involved in ...
 968-1049 3.21e-03

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


Pssm-ID: 259860 [Multi-domain]  Cd Length: 110  Bit Score: 38.37  E-value: 3.21e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1159645229  968 LTMHVGDRVSWYL---MGMGNEIDIHTAHFHGHSFDYKQTGVYRADVFdLFPGTFQTVEMIPRNPGTWLLHCHVTDHIHA 1044
Cdd:cd00920     25 LVVPVGDTVRVQFvnkLGENHSVTIAGFGVPVVAMAGGANPGLVNTLV-IGPGESAEVTFTTDQAGVYWFYCTIPGHNHA 103


                   ....*
gi 1159645229 1045 GMETT 1049
Cdd:cd00920    104 GMVGT 108
CuRO_1_Abr2_like cd13850
The first cupredoxin domain of a group of fungal Laccases similar to Abr2 from Aspergillus ...
 450-517 3.59e-03

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: 38.43  E-value: 3.59e-03
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1159645229  450 GPVIKAEVGESIRVTFRNNASRPFSIQPHGLSYRKSDEgasygasSRG----TESPashVSPGATFTYEWNV 517
Cdd:cd13850     28 GPPIILDEGDEVEILVTNNLPVNTTIHFHGILQRGTPW-------SDGvpgvTQWP---IQPGGSFTYRWKA 89
PLN02604 PLN02604
oxidoreductase
 985-1050 3.91e-03

oxidoreductase


Pssm-ID: 215324 [Multi-domain]  Cd Length: 566  Bit Score: 41.00  E-value: 3.91e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1159645229  985 NEIDIHTAHFHGHsfDYKQTGvYRADVFDLF--PGTFQTVEMIPRN------------------PGTWLLHCHVTDHIHA 1044
Cdd:PLN02604   462 NNSETHPWHLHGH--DFWVLG-YGEGKFNMSsdPKKYNLVDPIMKNtvpvhpygwtalrfradnPGVWAFHCHIESHFFM 538


                   ....*.
gi 1159645229 1045 GMETTY 1050
Cdd:PLN02604   539 GMGVVF 544
CuRO_3_Tth-MCO_like cd13900
The third cupredoxin domain of the bacterial laccases similar to Tth-MCO from Thermus ...
 957-1046 4.69e-03

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


Pssm-ID: 259967 [Multi-domain]  Cd Length: 123  Bit Score: 38.38  E-value: 4.69e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1159645229  957 INGKVFG-NLGGLTMHVGDRVSWYLMGMGNEIdiHTAHFHGHSF-------DYKQTGVYRaDVFDLFPGTFQTVEMIPRN 1028
Cdd:cd13900     22 INGKPFDpDRPDRTVRLGTVEEWTLINTSGED--HPFHIHVNPFqvvsingKPGLPPVWR-DTVNVPAGGSVTIRTRFRD 98

                           90
                   ....*....|....*....
gi 1159645229 1029 P-GTWLLHCHVTDHIHAGM 1046
Cdd:cd13900     99 FtGEFVLHCHILDHEDQGM 117
CuRO_1_McoP_like cd13852
The first cupredoxin domain of multicopper oxidase McoP and similar proteins; This family ...
 449-517 5.79e-03

The first cupredoxin domain of multicopper oxidase McoP and similar proteins; This family includes archaeal and bacterial multicopper oxidases (MCOs), represented by the extremely thermostable McoP from the hyperthermophilic archaeon Pyrobaculum aerophilum. McoP is an efficient metallo-oxidase that catalyzes the oxidation of cuprous and ferrous ions. It is noteworthy that McoP has three-fold higher catalytic efficiency when using nitrous oxide as the electron acceptor than when using dioxygen, the typical oxidizing substrate of MCOs. McoP may function as a novel archaeal nitrous oxide reductase that is probably involved in the denitrification pathway in archaea. Although MCOs have diverse functions, majority of them have three cupredoxin domain repeats that include one mononuclear and one trinuclear copper center. The copper ions are bound in several sites: Type 1, Type 2, and/or Type 3. The ensemble of types 2 and 3 copper is called a trinuclear cluster. MCOs oxidize their substrate by accepting electrons at a mononuclear copper center and transferring them to the active site trinuclear copper center. The cupredoxin domain 1 of 3-domain MCOs contains part the trinuclear copper binding site, which is located at the interface of domains 1 and 3.


Pssm-ID: 259921 [Multi-domain]  Cd Length: 114  Bit Score: 37.65  E-value: 5.79e-03
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1159645229  449 LGPVIKAEVGESIRVTFRNNASRPFSIQPHGLSYRKSDEGasygassrgteSPASHVSPGATFTYEWNV 517
Cdd:cd13852     23 LGPILRLRKGQKVRITFKNNLPEPTIIHWHGLHVPAAMDG-----------HPRYAIDPGETYVYEFEV 80
Cu-oxidase_2 pfam07731
Multicopper oxidase; This entry contains many divergent copper oxidase-like domains that are ...
 254-358 9.75e-03

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: 37.80  E-value: 9.75e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1159645229  254 DFQESNKMHSINGYMYGYLPN-LTMCVEDKVKWHLFGMGNeaDIHSAYFHGQT--LIERHH-----------------RV 313
Cdd:pfam07731   14 SGNFRRNDWAINGLLFPPNTNvITLPYGTVVEWVLQNTTT--GVHPFHLHGHSfqVLGRGGgpwpeedpktynlvdpvRR 91

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*
gi 1159645229  314 DTISLFPATFVDAVMVPRTPGEWLLSCQVNDHIQGGMQALFKVKE 358
Cdd:pfam07731   92 DTVQVPPGGWVAIRFRADNPGVWLFHCHILWHLDQGMMGQFVVRP 136
 
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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