NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|733903985|ref|XP_003209336|]
View 

ceruloplasmin isoform X1 [Meleagris gallopavo]

Protein Classification

cupredoxin domain-containing protein; multicopper oxidase( domain architecture ID 10136056)

cupredoxin domain-containing protein may contain a type I copper center and be involved in inter-molecular electron transfer reactions; 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; similar to Pleurotus ostreatus laccase-2 that may be involved in lignin degradation and detoxification of lignin-derived products

Graphical summary

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

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 ...
 388-586 3.50e-124

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: 377.97  E-value: 3.50e-124
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 733903985  388 TKIRQYFIAAEEIIWNYGPSAFNHFTGQELIA-DSESSVFFERSETRIGGSYKKAIYKEYTDGTFTAHKKRLPEEEHLGL 466
Cdd:cd04224     1 GKVRHYFIAAEEIMWDYAPSGKNLFTGQNLTApGSDSEVFFQRNETRIGGTYWKVRYVEYTDATFTTRKHRSKEEEHLGI 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 733903985  467 LGPVIKAEVGESIRVTFRNNASRPFSIQPHGVSYLKSNEGALYRtasRDTESPASYVSPGASFTYEWNVPEDVGPTDQDP 546
Cdd:cd04224    81 LGPVIRAEVGDTIKVTFRNKASRPFSIQPHGVFYEKNYEGAMYR---DGDPSPGSHVSPGETFTYEWTVPEGVGPTNQDP 157

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|
gi 733903985  547 DCLTWFYYSAVDSVRDTNSGLVGPLLVCRKGALLPSAKQR 586
Cdd:cd04224   158 PCLTYLYFSAVDPVRDTNSGLVGPLLVCKKGSLNANGRQK 197
CuRO_1_ceruloplasmin cd04222
The first cupredoxin domain of Ceruloplasmin; Ceruloplasmin is a multicopper oxidase essential ...
 40-222 2.62e-122

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: 372.52  E-value: 2.62e-122
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 733903985   40 REYYIGIVETAWDYAPGSTDIISGQRFAEEEQAEVFLKRGPQRIGSIYKKAVYTQYTNILYDVIVEKPSWLGFLGPIIKG 119
Cdd:cd04222     1 REYYIGIRETQWDYAPSGKNLITNQTFDDDEHASVFLKRGPDRIGRVYKKAVYLQYTDDTYRTEIEKPVWLGFLGPILKA 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 733903985  120 EVGDSIVVHLKNFASRNYTLHPHGVKYTKENEGAFYPDNTKGFEKRDDAVKPGGQYTYTWDVTEDQGPAKGDADCITRVY 199
Cdd:cd04222    81 EVGDVIVVHLKNFASRPYSLHPHGVFYNKENEGALYPDNTSGFEKADDAVPPGGSYTYTWTVPEEQAPTKADANCLTRIY 160

                         170       180
                  ....*....|....*....|...
gi 733903985  200 HSHIDAPRDVASGLVGPLIICRK 222
Cdd:cd04222   161 HSHIDAPKDIASGLIGPLIICKK 183
CuRO_5_ceruloplasmin cd04225
The fifth cupredoxin domain of Ceruloplasmin; Ceruloplasmin is a multicopper oxidase essential ...
 746-916 4.32e-108

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


:

Pssm-ID: 259887 [Multi-domain]  Cd Length: 171  Bit Score: 334.44  E-value: 4.32e-108
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 733903985  746 KTHYIAAVEVEWDYSPNRTWEFERHQFHKESPGNSFLNKEDAFIGSKYKKVVYREYTDQTFSTPKSRAEEEQHLQIQGPL 825
Cdd:cd04225     1 RTYYIAAEEVEWDYSPQRTWEQELHNTHEESPGNAFLNKGDKFIGSKYKKVVYREYTDDTFSVPKERTAEEEHLGILGPL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 733903985  826 IMSSVGDKINIVFKNLASRPYSIHAHGVKTDSSVVAITNPGETKMYVWKISARSSSERDDSHCTAWAYHSTVDIIKDTYS 905
Cdd:cd04225    81 IHAEVGEKVKIVFKNMASRPYSIHAHGVKTDSSWVAPTEPGETQTYTWKIPERSGPGVEDSNCISWAYYSTVDQIKDLYS 160

                         170
                  ....*....|.
gi 733903985  906 GLIGTLVVCPR 916
Cdd:cd04225   161 GLIGPLVICRR 171
CuRO_6_ceruloplasmin cd11012
The sixth cupredoxin domain of Ceruloplasmin; Ceruloplasmin is a multicopper oxidase essential ...
 927-1071 8.02e-96

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: 300.63  E-value: 8.02e-96
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 733903985  927 KVHFALLFMVFDENESWYLDENIETYSANPHLVDKENEEFLESNKMHAINGKVFGNLHGLTMHVGDEVSWYLMAMGNEID 1006
Cdd:cd11012     1 KLEFALLFLVFDENESWYLDENIKTYSDHPEKVNKEDEEFIESNKMHAINGKVFGNLQGLTMHVGDEVYWYLMGMGNEID 80

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 733903985 1007 IHTAHFHGHSFDYKQTGIYRADVFDLFPGTFQTVEMIPQNPGTWLLHCHVTDHIHAGMEATYTVL 1071
Cdd:cd11012    81 IHTAHFHGHSFDYKHRGVYRSDVFDLFPGTFQTVEMIPRTPGTWLLHCHVTDHIHAGMETTYTVL 145
CuRO_2_ceruloplasmin cd11021
The second cupredoxin domain of Ceruloplasmin; Ceruloplasmin is a multicopper oxidase ...
 234-374 1.30e-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: 299.77  E-value: 1.30e-95
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 733903985  234 DAEFILMFSVMDENLSWYLEDNIRMYCSEPSKVDKDDEDFQESNKMHSINGYMYGYLPNLTMCVEDKVKWHLFGMGNEAD 313
Cdd:cd11021     1 DREFVLMFSVVDENLSWYLDENIKTYCSEPAKVDKDDEDFQESNKMHSINGYTFGNLPGLSMCAGDRVKWHLFGMGNEVD 80

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 733903985  314 IHSAYFHGQTLIERHHRVDTINLFPATFIDALMIPRNPGEWLLSCQVNDHIEGGMQALFKV 374
Cdd:cd11021    81 IHSAFFHGQTLTDRGHRTDTINLFPATFVTAEMVAQNPGKWLLSCQVNDHLKAGMQAFYEV 141
CuRO_4_ceruloplasmin cd11022
The fourth cupredoxin domain of Ceruloplasmin; Ceruloplasmin is a multicopper oxidase ...
 589-732 1.67e-95

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: 299.78  E-value: 1.67e-95
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 733903985  589 TREFFLLATVFDENLSWYLDDNILMFTLNPNEIDKDNEDFQESNKMHSINGYMYGNQPGLEMCKGDVISWHLMGLGSEVD 668
Cdd:cd11022     1 DKEFFLLFTVFDENESWYLDENIQQFTLDPRSVDKEDEDFQESNKMHSINGYMYGNQPGLDMCKGDTVSWHLFGLGTETD 80

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 733903985  669 VHGIYFSQNTFITKGTRKDTANLFPHTFVTAIMKPDSEGIFEVSCLTTDHHRGGMKQKYKVKPC 732
Cdd:cd11022    81 VHGIYFSGNTFLLQGTRRDTANLFPHTSVTAIMQPDNEGTFEVNCQTTDHYSAGMRQIYTVSQC 144
 
Name Accession Description Interval E-value
CuRO_3_ceruloplasmin cd04224
The third cupredoxin domain of Ceruloplasmin; Ceruloplasmin is a multicopper oxidase essential ...
 388-586 3.50e-124

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: 377.97  E-value: 3.50e-124
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 733903985  388 TKIRQYFIAAEEIIWNYGPSAFNHFTGQELIA-DSESSVFFERSETRIGGSYKKAIYKEYTDGTFTAHKKRLPEEEHLGL 466
Cdd:cd04224     1 GKVRHYFIAAEEIMWDYAPSGKNLFTGQNLTApGSDSEVFFQRNETRIGGTYWKVRYVEYTDATFTTRKHRSKEEEHLGI 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 733903985  467 LGPVIKAEVGESIRVTFRNNASRPFSIQPHGVSYLKSNEGALYRtasRDTESPASYVSPGASFTYEWNVPEDVGPTDQDP 546
Cdd:cd04224    81 LGPVIRAEVGDTIKVTFRNKASRPFSIQPHGVFYEKNYEGAMYR---DGDPSPGSHVSPGETFTYEWTVPEGVGPTNQDP 157

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|
gi 733903985  547 DCLTWFYYSAVDSVRDTNSGLVGPLLVCRKGALLPSAKQR 586
Cdd:cd04224   158 PCLTYLYFSAVDPVRDTNSGLVGPLLVCKKGSLNANGRQK 197
CuRO_1_ceruloplasmin cd04222
The first cupredoxin domain of Ceruloplasmin; Ceruloplasmin is a multicopper oxidase essential ...
 40-222 2.62e-122

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: 372.52  E-value: 2.62e-122
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 733903985   40 REYYIGIVETAWDYAPGSTDIISGQRFAEEEQAEVFLKRGPQRIGSIYKKAVYTQYTNILYDVIVEKPSWLGFLGPIIKG 119
Cdd:cd04222     1 REYYIGIRETQWDYAPSGKNLITNQTFDDDEHASVFLKRGPDRIGRVYKKAVYLQYTDDTYRTEIEKPVWLGFLGPILKA 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 733903985  120 EVGDSIVVHLKNFASRNYTLHPHGVKYTKENEGAFYPDNTKGFEKRDDAVKPGGQYTYTWDVTEDQGPAKGDADCITRVY 199
Cdd:cd04222    81 EVGDVIVVHLKNFASRPYSLHPHGVFYNKENEGALYPDNTSGFEKADDAVPPGGSYTYTWTVPEEQAPTKADANCLTRIY 160

                         170       180
                  ....*....|....*....|...
gi 733903985  200 HSHIDAPRDVASGLVGPLIICRK 222
Cdd:cd04222   161 HSHIDAPKDIASGLIGPLIICKK 183
CuRO_5_ceruloplasmin cd04225
The fifth cupredoxin domain of Ceruloplasmin; Ceruloplasmin is a multicopper oxidase essential ...
 746-916 4.32e-108

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


Pssm-ID: 259887 [Multi-domain]  Cd Length: 171  Bit Score: 334.44  E-value: 4.32e-108
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 733903985  746 KTHYIAAVEVEWDYSPNRTWEFERHQFHKESPGNSFLNKEDAFIGSKYKKVVYREYTDQTFSTPKSRAEEEQHLQIQGPL 825
Cdd:cd04225     1 RTYYIAAEEVEWDYSPQRTWEQELHNTHEESPGNAFLNKGDKFIGSKYKKVVYREYTDDTFSVPKERTAEEEHLGILGPL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 733903985  826 IMSSVGDKINIVFKNLASRPYSIHAHGVKTDSSVVAITNPGETKMYVWKISARSSSERDDSHCTAWAYHSTVDIIKDTYS 905
Cdd:cd04225    81 IHAEVGEKVKIVFKNMASRPYSIHAHGVKTDSSWVAPTEPGETQTYTWKIPERSGPGVEDSNCISWAYYSTVDQIKDLYS 160

                         170
                  ....*....|.
gi 733903985  906 GLIGTLVVCPR 916
Cdd:cd04225   161 GLIGPLVICRR 171
CuRO_6_ceruloplasmin cd11012
The sixth cupredoxin domain of Ceruloplasmin; Ceruloplasmin is a multicopper oxidase essential ...
 927-1071 8.02e-96

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: 300.63  E-value: 8.02e-96
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 733903985  927 KVHFALLFMVFDENESWYLDENIETYSANPHLVDKENEEFLESNKMHAINGKVFGNLHGLTMHVGDEVSWYLMAMGNEID 1006
Cdd:cd11012     1 KLEFALLFLVFDENESWYLDENIKTYSDHPEKVNKEDEEFIESNKMHAINGKVFGNLQGLTMHVGDEVYWYLMGMGNEID 80

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 733903985 1007 IHTAHFHGHSFDYKQTGIYRADVFDLFPGTFQTVEMIPQNPGTWLLHCHVTDHIHAGMEATYTVL 1071
Cdd:cd11012    81 IHTAHFHGHSFDYKHRGVYRSDVFDLFPGTFQTVEMIPRTPGTWLLHCHVTDHIHAGMETTYTVL 145
CuRO_2_ceruloplasmin cd11021
The second cupredoxin domain of Ceruloplasmin; Ceruloplasmin is a multicopper oxidase ...
 234-374 1.30e-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: 299.77  E-value: 1.30e-95
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 733903985  234 DAEFILMFSVMDENLSWYLEDNIRMYCSEPSKVDKDDEDFQESNKMHSINGYMYGYLPNLTMCVEDKVKWHLFGMGNEAD 313
Cdd:cd11021     1 DREFVLMFSVVDENLSWYLDENIKTYCSEPAKVDKDDEDFQESNKMHSINGYTFGNLPGLSMCAGDRVKWHLFGMGNEVD 80

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 733903985  314 IHSAYFHGQTLIERHHRVDTINLFPATFIDALMIPRNPGEWLLSCQVNDHIEGGMQALFKV 374
Cdd:cd11021    81 IHSAFFHGQTLTDRGHRTDTINLFPATFVTAEMVAQNPGKWLLSCQVNDHLKAGMQAFYEV 141
CuRO_4_ceruloplasmin cd11022
The fourth cupredoxin domain of Ceruloplasmin; Ceruloplasmin is a multicopper oxidase ...
 589-732 1.67e-95

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: 299.78  E-value: 1.67e-95
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 733903985  589 TREFFLLATVFDENLSWYLDDNILMFTLNPNEIDKDNEDFQESNKMHSINGYMYGNQPGLEMCKGDVISWHLMGLGSEVD 668
Cdd:cd11022     1 DKEFFLLFTVFDENESWYLDENIQQFTLDPRSVDKEDEDFQESNKMHSINGYMYGNQPGLDMCKGDTVSWHLFGLGTETD 80

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 733903985  669 VHGIYFSQNTFITKGTRKDTANLFPHTFVTAIMKPDSEGIFEVSCLTTDHHRGGMKQKYKVKPC 732
Cdd:cd11022    81 VHGIYFSGNTFLLQGTRRDTANLFPHTSVTAIMQPDNEGTFEVNCQTTDHYSAGMRQIYTVSQC 144
Cu-oxidase_2 pfam07731
Multicopper oxidase; This entry contains many divergent copper oxidase-like domains that are ...
 970-1074 6.64e-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: 6.64e-19
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 733903985   970 NKMHAINGKVFG-NLHGLTMHVGDEVSWYLMamGNEIDIHTAHFHGHSFDYKQTGI----------------YRADVFDL 1032
Cdd:pfam07731   19 RNDWAINGLLFPpNTNVITLPYGTVVEWVLQ--NTTTGVHPFHLHGHSFQVLGRGGgpwpeedpktynlvdpVRRDTVQV 96

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|..
gi 733903985  1033 FPGTFQTVEMIPQNPGTWLLHCHVTDHIHAGMEATYTVLPKE 1074
Cdd:pfam07731   97 PPGGWVAIRFRADNPGVWLFHCHILWHLDQGMMGQFVVRPGD 138
Cu-oxidase_3 pfam07732
Multicopper oxidase; This entry contains many divergent copper oxidase-like domains that are ...
 94-219 1.78e-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: 64.96  E-value: 1.78e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 733903985    94 QYTNILYDVIVEKPSWL---GFLGPIIKGEVGDSIVVHLKNFASRNYTLHPHGVKYTKENEGAFYPDNTKgfekrdDAVK 170
Cdd:pfam07732    3 TYGTVSPLGGTRQAVIGvngQFPGPTIRVREGDTVVVNVTNNLDEPTSIHWHGLQQRGTPWMDGVPGVTQ------CPIP 76

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*....
gi 733903985   171 PGGQYTYTWDVTEDQGpakgdadciTRVYHSHIDAPRdvASGLVGPLII 219
Cdd:pfam07732   77 PGQSFTYRFQVKQQAG---------TYWYHSHTSGQQ--AAGLAGAIII 114
SufI COG2132
Multicopper oxidase with three cupredoxin domains (includes cell division protein FtsP and ...
 972-1072 2.44e-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: 57.64  E-value: 2.44e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 733903985  972 MHAINGKVFGNLH-GLTMHVGDEVSWYLMAMGNeiDIHTAHFHGHSF------DYKQTGIYRADVFDLFPGtfQTVEMI- 1043
Cdd:COG2132   317 VWTINGKAFDPDRpDLTVKLGERERWTLVNDTM--MPHPFHLHGHQFqvlsrnGKPPPEGGWKDTVLVPPG--ETVRILf 392

                          90       100       110
                  ....*....|....*....|....*....|.
gi 733903985 1044 --PQNPGTWLLHCHVTDHIHAGMEATYTVLP 1072
Cdd:COG2132   393 rfDNYPGDWMFHCHILEHEDAGMMGQFEVVP 423
Cu-oxidase pfam00394
Multicopper oxidase; Many of the proteins in this family contain multiple similar copies of ...
 241-377 7.86e-08

Multicopper oxidase; Many of the proteins in this family contain multiple similar copies of this plastocyanin-like domain.


Pssm-ID: 395317 [Multi-domain]  Cd Length: 146  Bit Score: 52.70  E-value: 7.86e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 733903985   241 FSVMDENLSWYlEDNIRMYCSEPSKVDKDDEDFQESNKMHSINGYMYGYLPNLTMCVEDKVKWHLFgMGNEADIHSAYFH 320
Cdd:pfam00394    1 EDYVITLSDWY-HKDAKDLEKELLASGKAPTDFPPVPDAVLINGKDGASLATLTVTPGKTYRLRII-NVALDDSLNFSIE 78

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 733903985   321 GQ--TLIE---RHH---RVDTINLFPATFIDALMIP-RNPGEWLLSCQVN-DHIEGGMQALFKVEGC 377
Cdd:pfam00394   79 GHkmTVVEvdgVYVnpfTVDSLDIFPGQRYSVLVTAnQDPGNYWIVASPNiPAFDNGTAAAILRYSG 145
SufI COG2132
Multicopper oxidase with three cupredoxin domains (includes cell division protein FtsP and ...
 112-242 1.27e-07

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


Pssm-ID: 441735 [Multi-domain]  Cd Length: 423  Bit Score: 55.33  E-value: 1.27e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 733903985  112 FLGPIIKGEVGDSIVVHLKNFASRNYTLHPHGVKYTKENEGafYPdntkgfekrDDAVKPGGQYTYTWDVteDQGPAkgd 191
Cdd:COG2132    42 YPGPTIRVREGDRVRVRVTNRLPEPTTVHWHGLRVPNAMDG--VP---------GDPIAPGETFTYEFPV--PQPAG--- 105

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 733903985  192 adciTRVYHSHIDA--PRDVASGLVGPLIIcrkgamNKDNDKY--VDAEFILMFS 242
Cdd:COG2132   106 ----TYWYHPHTHGstAEQVYRGLAGALIV------EDPEEDLprYDRDIPLVLQ 150
PLN02191 PLN02191
L-ascorbate oxidase
 112-242 3.09e-07

L-ascorbate oxidase


Pssm-ID: 177843 [Multi-domain]  Cd Length: 574  Bit Score: 54.63  E-value: 3.09e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 733903985  112 FLGPIIKGEVGDSIVVHLKN-FASRNYTLHPHGVKytkeNEGAFYPDNTKGFEKRddAVKPGGQYTYTWDVtEDQGpakg 190
Cdd:PLN02191   51 FPGPTIDAVAGDTIVVHLTNkLTTEGLVIHWHGIR----QKGSPWADGAAGVTQC--AINPGETFTYKFTV-EKPG---- 119

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|..
gi 733903985  191 dadciTRVYHSHIDAPRdvASGLVGPLIIcrKGAMNKDNDKYVDAEFILMFS 242
Cdd:PLN02191  120 -----THFYHGHYGMQR--SAGLYGSLIV--DVAKGPKERLRYDGEFNLLLS 162
ascorbase TIGR03388
L-ascorbate oxidase, plant type; Members of this protein family are the copper-containing ...
 112-242 6.19e-07

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: 53.60  E-value: 6.19e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 733903985   112 FLGPIIKGEVGDSIVVHLKN-FASRNYTLHPHGVKytkeNEGAFYPDNTKGFEKRddAVKPGGQYTYTWdVTEDQGpakg 190
Cdd:TIGR03388   29 FPGPTIRAQAGDTIVVELTNkLHTEGVVIHWHGIR----QIGTPWADGTAGVTQC--AINPGETFIYNF-VVDRPG---- 97

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|..
gi 733903985   191 dadciTRVYHSHIDAPRdvASGLVGPLIIcRKGAMNKDNDKYvDAEFILMFS 242
Cdd:TIGR03388   98 -----TYFYHGHYGMQR--SAGLYGSLIV-DVPDGEKEPFHY-DGEFNLLLS 140
Cu-oxidase_3 pfam07732
Multicopper oxidase; This entry contains many divergent copper oxidase-like domains that are ...
 466-573 1.99e-06

Multicopper oxidase; This entry contains many divergent copper oxidase-like domains that are not recognized by the pfam00394 model.


Pssm-ID: 462247 [Multi-domain]  Cd Length: 119  Bit Score: 47.63  E-value: 1.99e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 733903985   466 LLGPVIKAEVGESIRVTFRNNASRPFSIQPHGVSYLKSNE--GALYrtasrDTESPasyVSPGASFTYEWNVPEDVGptd 543
Cdd:pfam07732   24 FPGPTIRVREGDTVVVNVTNNLDEPTSIHWHGLQQRGTPWmdGVPG-----VTQCP---IPPGQSFTYRFQVKQQAG--- 92

                           90       100       110
                   ....*....|....*....|....*....|
gi 733903985   544 qdpdclTWFYYSAVDSVRdtNSGLVGPLLV 573
Cdd:pfam07732   93 ------TYWYHSHTSGQQ--AAGLAGAIII 114
PLN02191 PLN02191
L-ascorbate oxidase
 1006-1064 5.46e-06

L-ascorbate oxidase


Pssm-ID: 177843 [Multi-domain]  Cd Length: 574  Bit Score: 50.40  E-value: 5.46e-06
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 733903985 1006 DIHTAHFHGHSF--------------DYKQTGIYRADVFD---LFPGTFQTVEMIPQNPGTWLLHCHVTDHIHAGM 1064
Cdd:PLN02191  465 EIHPWHLHGHDFwvlgygdgkfkpgiDEKTYNLKNPPLRNtaiLYPYGWTAIRFVTDNPGVWFFHCHIEPHLHMGM 540
SufI COG2132
Multicopper oxidase with three cupredoxin domains (includes cell division protein FtsP and ...
 466-595 3.29e-05

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


Pssm-ID: 441735 [Multi-domain]  Cd Length: 423  Bit Score: 47.62  E-value: 3.29e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 733903985  466 LLGPVIKAEVGESIRVTFRNNASRPFSIQPHGVsylksnegalyRTASRDTESPASYVSPGASFTYEWNVPEDVGptdqd 545
Cdd:COG2132    42 YPGPTIRVREGDRVRVRVTNRLPEPTTVHWHGL-----------RVPNAMDGVPGDPIAPGETFTYEFPVPQPAG----- 105

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|..
gi 733903985  546 pdclTWFYYSAVD--SVRDTNSGLVGPLLVCRKGALLPsakqrSVTREFFLL 595
Cdd:COG2132   106 ----TYWYHPHTHgsTAEQVYRGLAGALIVEDPEEDLP-----RYDRDIPLV 148
SufI COG2132
Multicopper oxidase with three cupredoxin domains (includes cell division protein FtsP and ...
 823-913 3.01e-03

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: 41.46  E-value: 3.01e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 733903985  823 GPLIMSSVGDKINIVFKNLASRPYSIHAHGVKTDSS----VVAITNPGETKMYVWKIsarssserDDSHCTAWaYHSTVD 898
Cdd:COG2132    44 GPTIRVREGDRVRVRVTNRLPEPTTVHWHGLRVPNAmdgvPGDPIAPGETFTYEFPV--------PQPAGTYW-YHPHTH 114

                          90
                  ....*....|....*..
gi 733903985  899 II--KDTYSGLIGTLVV 913
Cdd:COG2132   115 GStaEQVYRGLAGALIV 131
Cu-oxidase_3 pfam07732
Multicopper oxidase; This entry contains many divergent copper oxidase-like domains that are ...
 820-895 3.37e-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: 38.38  E-value: 3.37e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 733903985   820 QIQGPLIMSSVGDKINIVFKNLASRPYSIHAHGVKTDSS-----VVAITN----PGETKMYVWKIsarssserDDSHCTA 890
Cdd:pfam07732   23 QFPGPTIRVREGDTVVVNVTNNLDEPTSIHWHGLQQRGTpwmdgVPGVTQcpipPGQSFTYRFQV--------KQQAGTY 94


                   ....*
gi 733903985   891 WaYHS 895
Cdd:pfam07732   95 W-YHS 98
ascorbOXfungal TIGR03390
L-ascorbate oxidase, fungal type; This model describes a family of fungal ascorbate oxidases, ...
 1025-1075 3.45e-03

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: 41.37  E-value: 3.45e-03
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|.
gi 733903985  1025 YRADVFDLFPGTFQTVEMIPQNPGTWLLHCHVTDHIHAGMEATYTVLPKED 1075
Cdd:TIGR03390  486 YAVKVVPGAPAGWRAWRIRVTNPGVWMMHCHILQHMVMGMQTVWVFGDAED 536
 
Name Accession Description Interval E-value
CuRO_3_ceruloplasmin cd04224
The third cupredoxin domain of Ceruloplasmin; Ceruloplasmin is a multicopper oxidase essential ...
 388-586 3.50e-124

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: 377.97  E-value: 3.50e-124
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 733903985  388 TKIRQYFIAAEEIIWNYGPSAFNHFTGQELIA-DSESSVFFERSETRIGGSYKKAIYKEYTDGTFTAHKKRLPEEEHLGL 466
Cdd:cd04224     1 GKVRHYFIAAEEIMWDYAPSGKNLFTGQNLTApGSDSEVFFQRNETRIGGTYWKVRYVEYTDATFTTRKHRSKEEEHLGI 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 733903985  467 LGPVIKAEVGESIRVTFRNNASRPFSIQPHGVSYLKSNEGALYRtasRDTESPASYVSPGASFTYEWNVPEDVGPTDQDP 546
Cdd:cd04224    81 LGPVIRAEVGDTIKVTFRNKASRPFSIQPHGVFYEKNYEGAMYR---DGDPSPGSHVSPGETFTYEWTVPEGVGPTNQDP 157

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|
gi 733903985  547 DCLTWFYYSAVDSVRDTNSGLVGPLLVCRKGALLPSAKQR 586
Cdd:cd04224   158 PCLTYLYFSAVDPVRDTNSGLVGPLLVCKKGSLNANGRQK 197
CuRO_1_ceruloplasmin cd04222
The first cupredoxin domain of Ceruloplasmin; Ceruloplasmin is a multicopper oxidase essential ...
 40-222 2.62e-122

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: 372.52  E-value: 2.62e-122
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 733903985   40 REYYIGIVETAWDYAPGSTDIISGQRFAEEEQAEVFLKRGPQRIGSIYKKAVYTQYTNILYDVIVEKPSWLGFLGPIIKG 119
Cdd:cd04222     1 REYYIGIRETQWDYAPSGKNLITNQTFDDDEHASVFLKRGPDRIGRVYKKAVYLQYTDDTYRTEIEKPVWLGFLGPILKA 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 733903985  120 EVGDSIVVHLKNFASRNYTLHPHGVKYTKENEGAFYPDNTKGFEKRDDAVKPGGQYTYTWDVTEDQGPAKGDADCITRVY 199
Cdd:cd04222    81 EVGDVIVVHLKNFASRPYSLHPHGVFYNKENEGALYPDNTSGFEKADDAVPPGGSYTYTWTVPEEQAPTKADANCLTRIY 160

                         170       180
                  ....*....|....*....|...
gi 733903985  200 HSHIDAPRDVASGLVGPLIICRK 222
Cdd:cd04222   161 HSHIDAPKDIASGLIGPLIICKK 183
CuRO_5_ceruloplasmin cd04225
The fifth cupredoxin domain of Ceruloplasmin; Ceruloplasmin is a multicopper oxidase essential ...
 746-916 4.32e-108

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


Pssm-ID: 259887 [Multi-domain]  Cd Length: 171  Bit Score: 334.44  E-value: 4.32e-108
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 733903985  746 KTHYIAAVEVEWDYSPNRTWEFERHQFHKESPGNSFLNKEDAFIGSKYKKVVYREYTDQTFSTPKSRAEEEQHLQIQGPL 825
Cdd:cd04225     1 RTYYIAAEEVEWDYSPQRTWEQELHNTHEESPGNAFLNKGDKFIGSKYKKVVYREYTDDTFSVPKERTAEEEHLGILGPL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 733903985  826 IMSSVGDKINIVFKNLASRPYSIHAHGVKTDSSVVAITNPGETKMYVWKISARSSSERDDSHCTAWAYHSTVDIIKDTYS 905
Cdd:cd04225    81 IHAEVGEKVKIVFKNMASRPYSIHAHGVKTDSSWVAPTEPGETQTYTWKIPERSGPGVEDSNCISWAYYSTVDQIKDLYS 160

                         170
                  ....*....|.
gi 733903985  906 GLIGTLVVCPR 916
Cdd:cd04225   161 GLIGPLVICRR 171
CuRO_6_ceruloplasmin cd11012
The sixth cupredoxin domain of Ceruloplasmin; Ceruloplasmin is a multicopper oxidase essential ...
 927-1071 8.02e-96

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: 300.63  E-value: 8.02e-96
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 733903985  927 KVHFALLFMVFDENESWYLDENIETYSANPHLVDKENEEFLESNKMHAINGKVFGNLHGLTMHVGDEVSWYLMAMGNEID 1006
Cdd:cd11012     1 KLEFALLFLVFDENESWYLDENIKTYSDHPEKVNKEDEEFIESNKMHAINGKVFGNLQGLTMHVGDEVYWYLMGMGNEID 80

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 733903985 1007 IHTAHFHGHSFDYKQTGIYRADVFDLFPGTFQTVEMIPQNPGTWLLHCHVTDHIHAGMEATYTVL 1071
Cdd:cd11012    81 IHTAHFHGHSFDYKHRGVYRSDVFDLFPGTFQTVEMIPRTPGTWLLHCHVTDHIHAGMETTYTVL 145
CuRO_2_ceruloplasmin cd11021
The second cupredoxin domain of Ceruloplasmin; Ceruloplasmin is a multicopper oxidase ...
 234-374 1.30e-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: 299.77  E-value: 1.30e-95
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 733903985  234 DAEFILMFSVMDENLSWYLEDNIRMYCSEPSKVDKDDEDFQESNKMHSINGYMYGYLPNLTMCVEDKVKWHLFGMGNEAD 313
Cdd:cd11021     1 DREFVLMFSVVDENLSWYLDENIKTYCSEPAKVDKDDEDFQESNKMHSINGYTFGNLPGLSMCAGDRVKWHLFGMGNEVD 80

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 733903985  314 IHSAYFHGQTLIERHHRVDTINLFPATFIDALMIPRNPGEWLLSCQVNDHIEGGMQALFKV 374
Cdd:cd11021    81 IHSAFFHGQTLTDRGHRTDTINLFPATFVTAEMVAQNPGKWLLSCQVNDHLKAGMQAFYEV 141
CuRO_4_ceruloplasmin cd11022
The fourth cupredoxin domain of Ceruloplasmin; Ceruloplasmin is a multicopper oxidase ...
 589-732 1.67e-95

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: 299.78  E-value: 1.67e-95
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 733903985  589 TREFFLLATVFDENLSWYLDDNILMFTLNPNEIDKDNEDFQESNKMHSINGYMYGNQPGLEMCKGDVISWHLMGLGSEVD 668
Cdd:cd11022     1 DKEFFLLFTVFDENESWYLDENIQQFTLDPRSVDKEDEDFQESNKMHSINGYMYGNQPGLDMCKGDTVSWHLFGLGTETD 80

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 733903985  669 VHGIYFSQNTFITKGTRKDTANLFPHTFVTAIMKPDSEGIFEVSCLTTDHHRGGMKQKYKVKPC 732
Cdd:cd11022    81 VHGIYFSGNTFLLQGTRRDTANLFPHTSVTAIMQPDNEGTFEVNCQTTDHYSAGMRQIYTVSQC 144
CuRO_1_ceruloplasmin_like cd04199
Cupredoxin domains 1, 3, and 5 of ceruloplasmin and similar proteins; This family includes the ...
 40-222 3.15e-79

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: 256.56  E-value: 3.15e-79
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 733903985   40 REYYIGIVETAWDYAPGSTDIIsgqrfaEEEQAEVFLKRGPQRIGSIYKKAVYTQYTNILYDVIVEKPSWLGFLGPIIKG 119
Cdd:cd04199     1 RHYYIAAEEIDWDYAPSGLAEK------DLSYRNQYLDNGPFRIGRSYKKVVYREYTDESFTTPGPQPEHLGILGPTIRA 74

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 733903985  120 EVGDSIVVHLKNFASRNYTLHPHGVKYTKENEGAFYPDNTKGFEKRDDAVKPGGQYTYTWDVTEDQGPAKGDADCITRVY 199
Cdd:cd04199    75 EVGDTIKVHFKNKASRPYSIHPHGVSYEKDSEGASYSDQTGPDEKKDDAVAPGETYTYVWIVTEESGPTKGDPACLTWAY 154

                         170       180
                  ....*....|....*....|...
gi 733903985  200 HSHIDAPRDVASGLVGPLIICRK 222
Cdd:cd04199   155 YSHVDLEKDINSGLIGPLLICKK 177
CuRO_1_ceruloplasmin_like cd04199
Cupredoxin domains 1, 3, and 5 of ceruloplasmin and similar proteins; This family includes the ...
 391-576 5.58e-78

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: 253.48  E-value: 5.58e-78
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 733903985  391 RQYFIAAEEIIWNYGPSafnhftGQELIADSESSVFFERSETRIGGSYKKAIYKEYTDGTFTahkKRLPEEEHLGLLGPV 470
Cdd:cd04199     1 RHYYIAAEEIDWDYAPS------GLAEKDLSYRNQYLDNGPFRIGRSYKKVVYREYTDESFT---TPGPQPEHLGILGPT 71

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 733903985  471 IKAEVGESIRVTFRNNASRPFSIQPHGVSYLKSNEGALYRTASRDTESPASYVSPGASFTYEWNVPEDVGPTDQDPDCLT 550
Cdd:cd04199    72 IRAEVGDTIKVHFKNKASRPYSIHPHGVSYEKDSEGASYSDQTGPDEKKDDAVAPGETYTYVWIVTEESGPTKGDPACLT 151

                         170       180
                  ....*....|....*....|....*.
gi 733903985  551 WFYYSAVDSVRDTNSGLVGPLLVCRK 576
Cdd:cd04199   152 WAYYSHVDLEKDINSGLIGPLLICKK 177
CuRO_2_ceruloplasmin_like cd04200
Cupredoxin domains 2, 4, and 6 of ceruloplasmin and similar proteins; This family includes the ...
 234-374 1.52e-70

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


Pssm-ID: 259863 [Multi-domain]  Cd Length: 141  Bit Score: 231.14  E-value: 1.52e-70
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 733903985  234 DAEFILMFSVMDENLSWYLEDNIRMYCSEPSKVDKDDEDFQESNKMHSINGYMYGYLPNLTMCVEDKVKWHLFGMGNEAD 313
Cdd:cd04200     1 DKEFVLLFAVFDENKSWYLEDNIKRFCDNPEKVDKDDEEFQESNKMHAINGYVFGNLPGLTMCAGDRVRWHLLGMGNEVD 80

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 733903985  314 IHSAYFHGQTLIERHHRVDTINLFPATFIDALMIPRNPGEWLLSCQVNDHIEGGMQALFKV 374
Cdd:cd04200    81 VHSIHFHGQTFLYKGYRIDTLTLFPATFETVEMVPSNPGTWLLHCHNSDHRHAGMQAYFLV 141
CuRO_2_ceruloplasmin_like cd04200
Cupredoxin domains 2, 4, and 6 of ceruloplasmin and similar proteins; This family includes the ...
 930-1070 3.88e-68

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: 224.60  E-value: 3.88e-68
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 733903985  930 FALLFMVFDENESWYLDENIETYSANPHLVDKENEEFLESNKMHAINGKVFGNLHGLTMHVGDEVSWYLMAMGNEIDIHT 1009
Cdd:cd04200     4 FVLLFAVFDENKSWYLEDNIKRFCDNPEKVDKDDEEFQESNKMHAINGYVFGNLPGLTMCAGDRVRWHLLGMGNEVDVHS 83

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 733903985 1010 AHFHGHSFDYKQtgiYRADVFDLFPGTFQTVEMIPQNPGTWLLHCHVTDHIHAGMEATYTV 1070
Cdd:cd04200    84 IHFHGQTFLYKG---YRIDTLTLFPATFETVEMVPSNPGTWLLHCHNSDHRHAGMQAYFLV 141
CuRO_1_ceruloplasmin cd04222
The first cupredoxin domain of Ceruloplasmin; Ceruloplasmin is a multicopper oxidase essential ...
 391-576 2.12e-67

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: 224.22  E-value: 2.12e-67
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 733903985  391 RQYFIAAEEIIWNYGPSAFNHFTGQELIADSESSVFFERSETRIGGSYKKAIYKEYTDGTFTahkKRLPEEEHLGLLGPV 470
Cdd:cd04222     1 REYYIGIRETQWDYAPSGKNLITNQTFDDDEHASVFLKRGPDRIGRVYKKAVYLQYTDDTYR---TEIEKPVWLGFLGPI 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 733903985  471 IKAEVGESIRVTFRNNASRPFSIQPHGVSYLKSNEGALYRTASRDTESPASYVSPGASFTYEWNVPEDVGPTDQDPDCLT 550
Cdd:cd04222    78 LKAEVGDVIVVHLKNFASRPYSLHPHGVFYNKENEGALYPDNTSGFEKADDAVPPGGSYTYTWTVPEEQAPTKADANCLT 157

                         170       180
                  ....*....|....*....|....*.
gi 733903985  551 WFYYSAVDSVRDTNSGLVGPLLVCRK 576
Cdd:cd04222   158 RIYHSHIDAPKDIASGLIGPLIICKK 183
CuRO_4_ceruloplasmin cd11022
The fourth cupredoxin domain of Ceruloplasmin; Ceruloplasmin is a multicopper oxidase ...
 234-377 2.85e-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: 211.19  E-value: 2.85e-63
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 733903985  234 DAEFILMFSVMDENLSWYLEDNIRMYCSEPSKVDKDDEDFQESNKMHSINGYMYGYLPNLTMCVEDKVKWHLFGMGNEAD 313
Cdd:cd11022     1 DKEFFLLFTVFDENESWYLDENIQQFTLDPRSVDKEDEDFQESNKMHSINGYMYGNQPGLDMCKGDTVSWHLFGLGTETD 80

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 733903985  314 IHSAYFHGQTLIERHHRVDTINLFPATFIDALMIPRNPGEWLLSCQVNDHIEGGMQALFKVEGC 377
Cdd:cd11022    81 VHGIYFSGNTFLLQGTRRDTANLFPHTSVTAIMQPDNEGTFEVNCQTTDHYSAGMRQIYTVSQC 144
CuRO_2_ceruloplasmin cd11021
The second cupredoxin domain of Ceruloplasmin; Ceruloplasmin is a multicopper oxidase ...
 930-1070 3.97e-61

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: 205.01  E-value: 3.97e-61
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 733903985  930 FALLFMVFDENESWYLDENIETYSANPHLVDKENEEFLESNKMHAINGKVFGNLHGLTMHVGDEVSWYLMAMGNEIDIHT 1009
Cdd:cd11021     4 FVLMFSVVDENLSWYLDENIKTYCSEPAKVDKDDEDFQESNKMHSINGYTFGNLPGLSMCAGDRVKWHLFGMGNEVDIHS 83

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 733903985 1010 AHFHGHSFDYKQtgiYRADVFDLFPGTFQTVEMIPQNPGTWLLHCHVTDHIHAGMEATYTV 1070
Cdd:cd11021    84 AFFHGQTLTDRG---HRTDTINLFPATFVTAEMVAQNPGKWLLSCQVNDHLKAGMQAFYEV 141
CuRO_2_ceruloplasmin cd11021
The second cupredoxin domain of Ceruloplasmin; Ceruloplasmin is a multicopper oxidase ...
 590-729 1.88e-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: 203.09  E-value: 1.88e-60
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 733903985  590 REFFLLATVFDENLSWYLDDNILMFTLNPNEIDKDNEDFQESNKMHSINGYMYGNQPGLEMCKGDVISWHLMGLGSEVDV 669
Cdd:cd11021     2 REFVLMFSVVDENLSWYLDENIKTYCSEPAKVDKDDEDFQESNKMHSINGYTFGNLPGLSMCAGDRVKWHLFGMGNEVDI 81

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 733903985  670 HGIYFSQNTFITKGTRKDTANLFPHTFVTAIMKPDSEGIFEVSCLTTDHHRGGMKQKYKV 729
Cdd:cd11021    82 HSAFFHGQTLTDRGHRTDTINLFPATFVTAEMVAQNPGKWLLSCQVNDHLKAGMQAFYEV 141
CuRO_2_ceruloplasmin_like cd04200
Cupredoxin domains 2, 4, and 6 of ceruloplasmin and similar proteins; This family includes the ...
 590-729 3.94e-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: 201.87  E-value: 3.94e-60
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 733903985  590 REFFLLATVFDENLSWYLDDNILMFTLNPNEIDKDNEDFQESNKMHSINGYMYGNQPGLEMCKGDVISWHLMGLGSEVDV 669
Cdd:cd04200     2 KEFVLLFAVFDENKSWYLEDNIKRFCDNPEKVDKDDEEFQESNKMHAINGYVFGNLPGLTMCAGDRVRWHLLGMGNEVDV 81

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 733903985  670 HGIYFSQNTFITKGTRKDTANLFPHTFVTAIMKPDSEGIFEVSCLTTDHHRGGMKQKYKV 729
Cdd:cd04200    82 HSIHFHGQTFLYKGYRIDTLTLFPATFETVEMVPSNPGTWLLHCHNSDHRHAGMQAYFLV 141
CuRO_5_ceruloplasmin cd04225
The fifth cupredoxin domain of Ceruloplasmin; Ceruloplasmin is a multicopper oxidase essential ...
 391-576 1.89e-59

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


Pssm-ID: 259887 [Multi-domain]  Cd Length: 171  Bit Score: 201.16  E-value: 1.89e-59
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 733903985  391 RQYFIAAEEIIWNYGPSAFNHFTGQELIADSESSVFFERSETRIGGSYKKAIYKEYTDGTFTAHKKRLPEEEHLGLLGPV 470
Cdd:cd04225     1 RTYYIAAEEVEWDYSPQRTWEQELHNTHEESPGNAFLNKGDKFIGSKYKKVVYREYTDDTFSVPKERTAEEEHLGILGPL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 733903985  471 IKAEVGESIRVTFRNNASRPFSIQPHGVSylksnegalyrtasrdTESPA-SYVSPGASFTYEWNVPEDVGPTDQDPDCL 549
Cdd:cd04225    81 IHAEVGEKVKIVFKNMASRPYSIHAHGVK----------------TDSSWvAPTEPGETQTYTWKIPERSGPGVEDSNCI 144

                         170       180
                  ....*....|....*....|....*..
gi 733903985  550 TWFYYSAVDSVRDTNSGLVGPLLVCRK 576
Cdd:cd04225   145 SWAYYSTVDQIKDLYSGLIGPLVICRR 171
CuRO_1_ceruloplasmin_like cd04199
Cupredoxin domains 1, 3, and 5 of ceruloplasmin and similar proteins; This family includes the ...
 746-914 1.85e-58

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: 198.78  E-value: 1.85e-58
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 733903985  746 KTHYIAAVEVEWDYSPNRTWEFERHQFhkespgNSFLNKEDAFIGSKYKKVVYREYTDQTFSTPKsraEEEQHLQIQGPL 825
Cdd:cd04199     1 RHYYIAAEEIDWDYAPSGLAEKDLSYR------NQYLDNGPFRIGRSYKKVVYREYTDESFTTPG---PQPEHLGILGPT 71

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 733903985  826 IMSSVGDKINIVFKNLASRPYSIHAHGVKTDSS---------------VVAITNPGETKMYVWKISARSSSERDDSHCTA 890
Cdd:cd04199    72 IRAEVGDTIKVHFKNKASRPYSIHPHGVSYEKDsegasysdqtgpdekKDDAVAPGETYTYVWIVTEESGPTKGDPACLT 151

                         170       180
                  ....*....|....*....|....
gi 733903985  891 WAYHSTVDIIKDTYSGLIGTLVVC 914
Cdd:cd04199   152 WAYYSHVDLEKDINSGLIGPLLIC 175
CuRO_3_ceruloplasmin cd04224
The third cupredoxin domain of Ceruloplasmin; Ceruloplasmin is a multicopper oxidase essential ...
 40-228 3.28e-58

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


Pssm-ID: 259886 [Multi-domain]  Cd Length: 197  Bit Score: 198.85  E-value: 3.28e-58
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 733903985   40 REYYIGIVETAWDYAPGSTDIISGQRF-AEEEQAEVFLKRGPQRIGSIYKKAVYTQYTNILYDV---IVEKPSWLGFLGP 115
Cdd:cd04224     4 RHYFIAAEEIMWDYAPSGKNLFTGQNLtAPGSDSEVFFQRNETRIGGTYWKVRYVEYTDATFTTrkhRSKEEEHLGILGP 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 733903985  116 IIKGEVGDSIVVHLKNFASRNYTLHPHGVKYTKENEGAFYPDntkGFEKRDDAVKPGGQYTYTWDVTEDQGPAKGDADCI 195
Cdd:cd04224    84 VIRAEVGDTIKVTFRNKASRPFSIQPHGVFYEKNYEGAMYRD---GDPSPGSHVSPGETFTYEWTVPEGVGPTNQDPPCL 160

                         170       180       190
                  ....*....|....*....|....*....|...
gi 733903985  196 TRVYHSHIDAPRDVASGLVGPLIICRKGAMNKD 228
Cdd:cd04224   161 TYLYFSAVDPVRDTNSGLVGPLLVCKKGSLNAN 193
CuRO_1_Ceruloplasmin_like_1 cd04229
cupredoxin domain of ceruloplasmin homologs; Uncharacterized subfamily of ceruloplasmin ...
 391-577 3.87e-58

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: 197.64  E-value: 3.87e-58
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 733903985  391 RQYFIAAEEIIWNYGPSAFNH-FTGQELiadSESSVFFERSETRIGGSYKKAIYKEYTDGTFTahkKRLPEEEHLGLLGP 469
Cdd:cd04229     1 RTYYIAAEEVDWDYAPSGKNKcCLGDDL---EVSTLDSQPGPYTIGSTYTKARYREYTDNSFS---TPKPTPAYLGILGP 74

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 733903985  470 VIKAEVGESIRVTFRNNASR-PFSIQPHGVSYLKSNEGALYRTASRdtespasyVSPGASFTYEWNVPEDVGPTDQDPDC 548
Cdd:cd04229    75 VIRAEVGDTIKVVFKNNLDEfPVNMHPHGGLYSKDNEGTTDGAGDV--------VAPGETYTYRWIVPEDAGPGPGDPSS 146

                         170       180
                  ....*....|....*....|....*....
gi 733903985  549 LTWFYYSAVDSVRDTNSGLVGPLLVCRKG 577
Cdd:cd04229   147 RLWLYHSHVDVFAHTNAGLVGPIIVTSKG 175
CuRO_3_FV_like cd14450
The third cupredoxin domain of coagulation factor V and similar proteins; Factor V is an ...
 389-575 1.40e-57

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: 196.25  E-value: 1.40e-57
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 733903985  389 KIRQYFIAAEEIIWNYGP----SAFNHFTGQELIADSEssvffersetRIGGSYKKAIYKEYTDGTFTAHKKRlPEEEHL 464
Cdd:cd14450     1 KNWEYFIAAEEVIWDYAPsipeNMDKRYRSQYLDNFSN----------NIGKKYKKAVFTQYEDGSFTKRLEN-PRPKEE 69

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 733903985  465 GLLGPVIKAEVGESIRVTFRNNASRPFSIQPHGVSYLKSNEGALYRTASRDTESPASYVSPGASFTYEWNVPEDVGPTDQ 544
Cdd:cd14450    70 GILGPVIRAQVRDTIKIVFKNKASRPYSIYPHGVTVSKAAEGASYPPDPRGNETQNKAVQPGETYTYKWNILETDEPTAR 149

                         170       180       190
                  ....*....|....*....|....*....|.
gi 733903985  545 DPDCLTWFYYSAVDSVRDTNSGLVGPLLVCR 575
Cdd:cd14450   150 DPRCLTRMYHSAVDITRDIASGLIGPLLICK 180
CuRO_1_FVIII_like cd14452
The first cupredoxin domain of coagulation factor VIII and similar proteins; Factor VIII ...
 40-223 2.11e-56

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: 192.89  E-value: 2.11e-56
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 733903985   40 REYYIGIVETAWDYApgstdiisgqrFAEEEQAEVFLKRGPQRIGSIYKKAVYTQYTNILYDVIVEKPSWLGFLGPIIKG 119
Cdd:cd14452     1 RRYYIAAVEIGWDYI-----------HSDLGDPASEQRKKPKDIPQKYIKAVFVEYLDATFTVPKPRPAWMGLLGPTIVA 69

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 733903985  120 EVGDSIVVHLKNFASRNYTLHPHGVKYTKENEGAFYPDNTKGFEKRDDAVKPGGQYTYTWDVTEDQGPAKGDADCITRVY 199
Cdd:cd14452    70 EVGDTVVITFKNLASQPYSLHAVGVSYWKASEGAGYDDSTSQHEKEDDAVYPGGYHTYVWDISPKDGPTGSDPECLTYSY 149

                         170       180
                  ....*....|....*....|....
gi 733903985  200 HSHIDAPRDVASGLVGPLIICRKG 223
Cdd:cd14452   150 SSQVDPVKDVNSGLIGALLVCRMG 173
CuRO_5_FV_like cd14451
The fifth cupredoxin domain of coagulation factor V and similar proteins; Factor V is an ...
 391-577 6.16e-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: 191.59  E-value: 6.16e-56
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 733903985  391 RQYFIAAEEIIWNYGPSAfnhftgqeliadsESSVFFERSETRigGSYKKAIYKEYTDGTFTAHKKRLPEEEHLGLLGPV 470
Cdd:cd14451     2 RRYYIAAEEEEWDYAGYG-------------KSRLDKTQNERD--TVFKKVVFRRYLDSTFSTPDIQGEYEEHLGILGPV 66

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 733903985  471 IKAEVGESIRVTFRNNASRPFSIQPHGVSYLKSNEGALYrtasrDTESPASY-----VSPGASFTYEWNVPEDVGPTDQD 545
Cdd:cd14451    67 IRAEVDDVIQVFFKNLASRPYSLHAHGLSYEKSSEGLSY-----DDESPDWFkkddaVQPNGTYTYVWYANPRSGPENNG 141

                         170       180       190
                  ....*....|....*....|....*....|..
gi 733903985  546 PDCLTWFYYSAVDSVRDTNSGLVGPLLVCRKG 577
Cdd:cd14451   142 SDCRTWAYYSAVNPEKDIHSGLIGPLLICRKG 173
CuRO_4_ceruloplasmin cd11022
The fourth cupredoxin domain of Ceruloplasmin; Ceruloplasmin is a multicopper oxidase ...
 930-1070 3.80e-55

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: 188.07  E-value: 3.80e-55
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 733903985  930 FALLFMVFDENESWYLDENIETYSANPHLVDKENEEFLESNKMHAINGKVFGNLHGLTMHVGDEVSWYLMAMGNEIDIHT 1009
Cdd:cd11022     4 FFLLFTVFDENESWYLDENIQQFTLDPRSVDKEDEDFQESNKMHSINGYMYGNQPGLDMCKGDTVSWHLFGLGTETDVHG 83

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 733903985 1010 AHFHGHSFDYKQTgiyRADVFDLFPGTFQTVEMIPQNPGTWLLHCHVTDHIHAGMEATYTV 1070
Cdd:cd11022    84 IYFSGNTFLLQGT---RRDTANLFPHTSVTAIMQPDNEGTFEVNCQTTDHYSAGMRQIYTV 141
CuRO_3_FV_like cd14450
The third cupredoxin domain of coagulation factor V and similar proteins; Factor V is an ...
 41-221 2.00e-53

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


Pssm-ID: 259992 [Multi-domain]  Cd Length: 181  Bit Score: 184.70  E-value: 2.00e-53
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 733903985   41 EYYIGIVETAWDYAPGSTDIISGQRFAEeeqaevFLKRGPQRIGSIYKKAVYTQYTNILYDVIVE--KPSWLGFLGPIIK 118
Cdd:cd14450     4 EYFIAAEEVIWDYAPSIPENMDKRYRSQ------YLDNFSNNIGKKYKKAVFTQYEDGSFTKRLEnpRPKEEGILGPVIR 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 733903985  119 GEVGDSIVVHLKNFASRNYTLHPHGVKYTKENEGAFYPDNTKGFEKRDDAVKPGGQYTYTWDVTEDQGPAKGDADCITRV 198
Cdd:cd14450    78 AQVRDTIKIVFKNKASRPYSIYPHGVTVSKAAEGASYPPDPRGNETQNKAVQPGETYTYKWNILETDEPTARDPRCLTRM 157

                         170       180
                  ....*....|....*....|...
gi 733903985  199 YHSHIDAPRDVASGLVGPLIICR 221
Cdd:cd14450   158 YHSAVDITRDIASGLIGPLLICK 180
CuRO_1_FV_like cd04226
The first cupredoxin domain of coagulation factor VIII and similar proteins; Factor V is an ...
 40-223 2.56e-53

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: 183.52  E-value: 2.56e-53
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 733903985   40 REYYIGIVETAWDYAPGSTDIISgqrfaeeeqaevflkrgpQRIGSIYKKAVYTQYTNilyDVIVEKPSWL--GFLGPII 117
Cdd:cd04226     1 REYYIAAQNIDWDYTPQSEELRL------------------KRSEQSFKKIVYREYEE---GFKKEKPADLssGLLGPTL 59

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 733903985  118 KGEVGDSIVVHLKNFASRNYTLHPHGVKYTKENEGAFYPDNTKGFEKRDDAVKPGGQYTYTWDVTEDQGPAKGDADCITR 197
Cdd:cd04226    60 RAEVGDTLIVHFKNMADKPLSIHPQGIAYGKKSEGSLYSDNTSPVEKLDDAVQPGQEYTYVWDITEEVGPTEADPPCLTY 139

                         170       180
                  ....*....|....*....|....*.
gi 733903985  198 VYHSHIDAPRDVASGLVGPLIICRKG 223
Cdd:cd04226   140 IYYSHVNMVRDFNSGLIGALLICKKG 165
CuRO_1_FV_like cd04226
The first cupredoxin domain of coagulation factor VIII and similar proteins; Factor V is an ...
 391-577 2.85e-53

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: 183.52  E-value: 2.85e-53
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 733903985  391 RQYFIAAEEIIWNYGPsafnhftGQEliadsessvffERSETRIGGSYKKAIYKEYTDGtftaHKKRLPEEEHLGLLGPV 470
Cdd:cd04226     1 REYYIAAQNIDWDYTP-------QSE-----------ELRLKRSEQSFKKIVYREYEEG----FKKEKPADLSSGLLGPT 58

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 733903985  471 IKAEVGESIRVTFRNNASRPFSIQPHGVSYLKSNEGALYRTASRDTESPASYVSPGASFTYEWNVPEDVGPTDQDPDCLT 550
Cdd:cd04226    59 LRAEVGDTLIVHFKNMADKPLSIHPQGIAYGKKSEGSLYSDNTSPVEKLDDAVQPGQEYTYVWDITEEVGPTEADPPCLT 138

                         170       180
                  ....*....|....*....|....*..
gi 733903985  551 WFYYSAVDSVRDTNSGLVGPLLVCRKG 577
Cdd:cd04226   139 YIYYSHVNMVRDFNSGLIGALLICKKG 165
CuRO_1_Ceruloplasmin_like_1 cd04229
cupredoxin domain of ceruloplasmin homologs; Uncharacterized subfamily of ceruloplasmin ...
 40-223 4.31e-52

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


Pssm-ID: 259891 [Multi-domain]  Cd Length: 175  Bit Score: 180.69  E-value: 4.31e-52
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 733903985   40 REYYIGIVETAWDYAP-GSTDIISGQRfaeEEQAEVFLKRGPQRIGSIYKKAVYTQYTNILYDVIVEKPSWLGFLGPIIK 118
Cdd:cd04229     1 RTYYIAAEEVDWDYAPsGKNKCCLGDD---LEVSTLDSQPGPYTIGSTYTKARYREYTDNSFSTPKPTPAYLGILGPVIR 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 733903985  119 GEVGDSIVVHLKN-FASRNYTLHPHGVKYTKENEGafypdntkGFEKRDDAVKPGGQYTYTWDVTEDQGPAKGDADCITR 197
Cdd:cd04229    78 AEVGDTIKVVFKNnLDEFPVNMHPHGGLYSKDNEG--------TTDGAGDVVAPGETYTYRWIVPEDAGPGPGDPSSRLW 149

                         170       180
                  ....*....|....*....|....*.
gi 733903985  198 VYHSHIDAPRDVASGLVGPLIICRKG 223
Cdd:cd04229   150 LYHSHVDVFAHTNAGLVGPIIVTSKG 175
CuRO_6_ceruloplasmin cd11012
The sixth cupredoxin domain of Ceruloplasmin; Ceruloplasmin is a multicopper oxidase essential ...
 236-374 8.12e-52

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: 178.52  E-value: 8.12e-52
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 733903985  236 EFILMFSVMDENLSWYLEDNIRMYCSEPSKVDKDDEDFQESNKMHSINGYMYGYLPNLTMCVEDKVKWHLFGMGNEADIH 315
Cdd:cd11012     3 EFALLFLVFDENESWYLDENIKTYSDHPEKVNKEDEEFIESNKMHAINGKVFGNLQGLTMHVGDEVYWYLMGMGNEIDIH 82

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 733903985  316 SAYFHGQTLIERH---HRVDTINLFPATFIDALMIPRNPGEWLLSCQVNDHIEGGMQALFKV 374
Cdd:cd11012    83 TAHFHGHSFDYKHrgvYRSDVFDLFPGTFQTVEMIPRTPGTWLLHCHVTDHIHAGMETTYTV 144
CuRO_3_ceruloplasmin cd04224
The third cupredoxin domain of Ceruloplasmin; Ceruloplasmin is a multicopper oxidase essential ...
 744-927 5.40e-51

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: 178.44  E-value: 5.40e-51
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 733903985  744 HEKTHYIAAVEVEWDYSPNRTWEFErHQFHKESPGNS--FLNKEDAFIGSKYKKVVYREYTDQTFSTPKSRAEEEQHLQI 821
Cdd:cd04224     2 KVRHYFIAAEEIMWDYAPSGKNLFT-GQNLTAPGSDSevFFQRNETRIGGTYWKVRYVEYTDATFTTRKHRSKEEEHLGI 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 733903985  822 QGPLIMSSVGDKINIVFKNLASRPYSIHAHGV------------KTDSSVVAITNPGETKMYVWKISARSSSERDDSHCT 889
Cdd:cd04224    81 LGPVIRAEVGDTIKVTFRNKASRPFSIQPHGVfyeknyegamyrDGDPSPGSHVSPGETFTYEWTVPEGVGPTNQDPPCL 160

                         170       180       190
                  ....*....|....*....|....*....|....*...
gi 733903985  890 AWAYHSTVDIIKDTYSGLIGTLVVCPRHYLpSSHARKK 927
Cdd:cd04224   161 TYLYFSAVDPVRDTNSGLVGPLLVCKKGSL-NANGRQK 197
CuRO_5_FVIII_like cd04228
The fifth cupredoxin domain of coagulation factor VIII and similar proteins; Factor VIII ...
 390-577 1.70e-49

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: 172.76  E-value: 1.70e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 733903985  390 IRQYFIAAEEIIWNYGPSAFNHFtgqelIADSESSvffeRSETRIGGSYKKAIYKEYTDGTFTAHKKRLPEEEHLGLLGP 469
Cdd:cd04228     1 IRHYFIAAVEVLWDYGMQRPQHF-----LRARDPN----RGRRKSVPQYKKVVFREYLDGSFTQPVYRGELDEHLGILGP 71

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 733903985  470 VIKAEVGESIRVTFRNNASRPFSIQPHGVSYlkSNEGAlyrtasrdTESPASYVSPGASFTYEWNVPEDVGPTDQDPDCL 549
Cdd:cd04228    72 YIRAEVEDNIMVTFKNLASRPYSFHSSLISY--EEDQR--------AEPRGNFVQPGEVQTYSWKVLHQMAPTKQEFDCK 141

                         170       180
                  ....*....|....*....|....*...
gi 733903985  550 TWFYYSAVDSVRDTNSGLVGPLLVCRKG 577
Cdd:cd04228   142 AWAYFSNVDLEKDLHSGLIGPLIICKTG 169
CuRO_1_FVIII_like cd14452
The first cupredoxin domain of coagulation factor VIII and similar proteins; Factor VIII ...
 391-577 3.06e-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: 3.06e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 733903985  391 RQYFIAAEEIIWNYGPSAfnhftgqeliaDSESSVFFERSETRIGGSYKKAIYKEYTDGTFTAHKKRLPeeeHLGLLGPV 470
Cdd:cd14452     1 RRYYIAAVEIGWDYIHSD-----------LGDPASEQRKKPKDIPQKYIKAVFVEYLDATFTVPKPRPA---WMGLLGPT 66

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 733903985  471 IKAEVGESIRVTFRNNASRPFSIQPHGVSYLKSNEGALYRTASRDTESPASYVSPGASFTYEWNVPEDVGPTDQDPDCLT 550
Cdd:cd14452    67 IVAEVGDTVVITFKNLASQPYSLHAVGVSYWKASEGAGYDDSTSQHEKEDDAVYPGGYHTYVWDISPKDGPTGSDPECLT 146

                         170       180
                  ....*....|....*....|....*..
gi 733903985  551 WFYYSAVDSVRDTNSGLVGPLLVCRKG 577
Cdd:cd14452   147 YSYSSQVDPVKDVNSGLIGALLVCRMG 173
CuRO_3_FVIII_like cd04227
The third cupredoxin domain of coagulation factor VIII and similar proteins; Factor VIII ...
 389-576 1.96e-48

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: 170.11  E-value: 1.96e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 733903985  389 KIRQYFIAAEEIIWNYGPsafnHFTGQEliaDSE-SSVFFERSETRIGGSYKKAIYKEYTDGTFtahKKRLPEEEHLGLL 467
Cdd:cd04227     1 QTWEHYIAAEELDWDYAP----LLSSTD---DRElQSRYLPTGPQRIGYKYKKVAFVEYTDKTF---KRREAKQTEKGIL 70

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 733903985  468 GPVIKAEVGESIRVTFRNNASRPFSIQPHGVSYLKSnegaLYRTASRDTESPASY--VSPGASFTYEWNVPEDVGPTDQD 545
Cdd:cd04227    71 GPLLKGEVGDQIHIMFKNTASRPYNIYPHGLTSVRP----MYRSRNPAGEKDLKTmpIGPGETFGYMWELTAEDGPTEED 146

                         170       180       190
                  ....*....|....*....|....*....|.
gi 733903985  546 PDCLTWFYYSAVDSVRDTNSGLVGPLLVCRK 576
Cdd:cd04227   147 PRCLTRLYQSTVDPERDLASGLIGPLLICKK 177
CuRO_5_FV_like cd14451
The fifth cupredoxin domain of coagulation factor V and similar proteins; Factor V is an ...
 39-223 4.44e-47

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


Pssm-ID: 259993 [Multi-domain]  Cd Length: 173  Bit Score: 166.17  E-value: 4.44e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 733903985   39 TREYYIGIVETAWDYAP-GSTDIISGQRFAEeeqaevflkrgpqrigSIYKKAVYTQYTNILY---DVIVEKPSWLGFLG 114
Cdd:cd14451     1 KRRYYIAAEEEEWDYAGyGKSRLDKTQNERD----------------TVFKKVVFRRYLDSTFstpDIQGEYEEHLGILG 64

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 733903985  115 PIIKGEVGDSIVVHLKNFASRNYTLHPHGVKYTKENEGAFYPDNTKGFEKRDDAVKPGGQYTYTWDVTEDQGPAKGDADC 194
Cdd:cd14451    65 PVIRAEVDDVIQVFFKNLASRPYSLHAHGLSYEKSSEGLSYDDESPDWFKKDDAVQPNGTYTYVWYANPRSGPENNGSDC 144

                         170       180
                  ....*....|....*....|....*....
gi 733903985  195 ITRVYHSHIDAPRDVASGLVGPLIICRKG 223
Cdd:cd14451   145 RTWAYYSAVNPEKDIHSGLIGPLLICRKG 173
CuRO_5_FV_like cd14451
The fifth cupredoxin domain of coagulation factor V and similar proteins; Factor V is an ...
 745-914 3.14e-46

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


Pssm-ID: 259993 [Multi-domain]  Cd Length: 173  Bit Score: 163.86  E-value: 3.14e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 733903985  745 EKTHYIAAVEVEWDYSPnrtweferhqfhkesPGNSFLNKEDAFIGSKYKKVVYREYTDQTFSTPKSRAEEEQHLQIQGP 824
Cdd:cd14451     1 KRRYYIAAEEEEWDYAG---------------YGKSRLDKTQNERDTVFKKVVFRRYLDSTFSTPDIQGEYEEHLGILGP 65

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 733903985  825 LIMSSVGDKINIVFKNLASRPYSIHAHGVKTDSSVVAIT---------------NPGETKMYVWKISARSSSERDDSHCT 889
Cdd:cd14451    66 VIRAEVDDVIQVFFKNLASRPYSLHAHGLSYEKSSEGLSyddespdwfkkddavQPNGTYTYVWYANPRSGPENNGSDCR 145

                         170       180
                  ....*....|....*....|....*
gi 733903985  890 AWAYHSTVDIIKDTYSGLIGTLVVC 914
Cdd:cd14451   146 TWAYYSAVNPEKDIHSGLIGPLLIC 170
CuRO_3_FVIII_like cd04227
The third cupredoxin domain of coagulation factor VIII and similar proteins; Factor VIII ...
 38-222 3.91e-43

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: 155.09  E-value: 3.91e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 733903985   38 VTREYYIGIVETAWDYAP--GSTDiisgqrfaEEEQAEVFLKRGPQRIGSIYKKAVYTQYTNILYDVIVEKPSWLGFLGP 115
Cdd:cd04227     1 QTWEHYIAAEELDWDYAPllSSTD--------DRELQSRYLPTGPQRIGYKYKKVAFVEYTDKTFKRREAKQTEKGILGP 72

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 733903985  116 IIKGEVGDSIVVHLKNFASRNYTLHPHGVKYTKENEGAFYPDNTKgfEKRDDAVKPGGQYTYTWDVTEDQGPAKGDADCI 195
Cdd:cd04227    73 LLKGEVGDQIHIMFKNTASRPYNIYPHGLTSVRPMYRSRNPAGEK--DLKTMPIGPGETFGYMWELTAEDGPTEEDPRCL 150

                         170       180
                  ....*....|....*....|....*..
gi 733903985  196 TRVYHSHIDAPRDVASGLVGPLIICRK 222
Cdd:cd04227   151 TRLYQSTVDPERDLASGLIGPLLICKK 177
CuRO_5_ceruloplasmin cd04225
The fifth cupredoxin domain of Ceruloplasmin; Ceruloplasmin is a multicopper oxidase essential ...
 40-222 1.33e-42

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


Pssm-ID: 259887 [Multi-domain]  Cd Length: 171  Bit Score: 153.39  E-value: 1.33e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 733903985   40 REYYIGIVETAWDYAPGSTDIISGQRFAEEEQAEVFLKRGPQRIGSIYKKAVYTQYTNILYDVIVEKPS---WLGFLGPI 116
Cdd:cd04225     1 RTYYIAAEEVEWDYSPQRTWEQELHNTHEESPGNAFLNKGDKFIGSKYKKVVYREYTDDTFSVPKERTAeeeHLGILGPL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 733903985  117 IKGEVGDSIVVHLKNFASRNYTLHPHGVKytkenegafypdnTKGFEKRddAVKPGGQYTYTWDVTEDQGPAKGDADCIT 196
Cdd:cd04225    81 IHAEVGEKVKIVFKNMASRPYSIHAHGVK-------------TDSSWVA--PTEPGETQTYTWKIPERSGPGVEDSNCIS 145

                         170       180
                  ....*....|....*....|....*.
gi 733903985  197 RVYHSHIDAPRDVASGLVGPLIICRK 222
Cdd:cd04225   146 WAYYSTVDQIKDLYSGLIGPLVICRR 171
CuRO_5_FVIII_like cd04228
The fifth cupredoxin domain of coagulation factor VIII and similar proteins; Factor VIII ...
 748-916 1.36e-42

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


Pssm-ID: 259890 [Multi-domain]  Cd Length: 169  Bit Score: 153.12  E-value: 1.36e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 733903985  748 HYIAAVEVEWDYSPNRTWEFERHQFHKESPGNSFlnkedafigSKYKKVVYREYTDQTFSTPKSRAEEEQHLQIQGPLIM 827
Cdd:cd04228     4 YFIAAVEVLWDYGMQRPQHFLRARDPNRGRRKSV---------PQYKKVVFREYLDGSFTQPVYRGELDEHLGILGPYIR 74

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 733903985  828 SSVGDKINIVFKNLASRPYSIHAHGVKTDSSVVA-----ITNPGETKMYVWKISARSSSERDDSHCTAWAYHSTVDIIKD 902
Cdd:cd04228    75 AEVEDNIMVTFKNLASRPYSFHSSLISYEEDQRAeprgnFVQPGEVQTYSWKVLHQMAPTKQEFDCKAWAYFSNVDLEKD 154

                         170
                  ....*....|....
gi 733903985  903 TYSGLIGTLVVCPR 916
Cdd:cd04228   155 LHSGLIGPLIICKT 168
CuRO_6_FVIII_like cd11018
The sixth cupredoxin domain of coagulation factor VIII and similar proteins; Factor VIII ...
 930-1070 3.61e-41

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: 148.10  E-value: 3.61e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 733903985  930 FALLFMVFDENESWYLDENIETYSANPHLVDKENEEFLESNKMHAINGKVFGNLHGLTMHVGDEVSWYLMAMGNEIDIHT 1009
Cdd:cd11018     4 FALLFTIFDETKSWYFEENMRRNCRPPCHIQTQDPWFHINNKFHAINGYVADTLPGLVMAQHQRIRWHLLNMGSDEEIHS 83

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 733903985 1010 AHFHGHSFDYKQTGIYRADVFDLFPGTFQTVEMIPQNPGTWLLHCHVTDHIHAGMEATYTV 1070
Cdd:cd11018    84 VHFHGLPFTVRAKKEYRMGVYNLYPGVFGTVEMRPSTAGIWLVECTVGEHLLAGMSALFLV 144
CuRO_6_ceruloplasmin cd11012
The sixth cupredoxin domain of Ceruloplasmin; Ceruloplasmin is a multicopper oxidase essential ...
 591-729 4.60e-41

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: 147.71  E-value: 4.60e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 733903985  591 EFFLLATVFDENLSWYLDDNILMFTLNPNEIDKDNEDFQESNKMHSINGYMYGNQPGLEMCKGDVISWHLMGLGSEVDVH 670
Cdd:cd11012     3 EFALLFLVFDENESWYLDENIKTYSDHPEKVNKEDEEFIESNKMHAINGKVFGNLQGLTMHVGDEVYWYLMGMGNEIDIH 82

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 733903985  671 GIYFSQNTFITKGT---RKDTANLFPHTFVTAIMKPDSEGIFEVSCLTTDHHRGGMKQKYKV 729
Cdd:cd11012    83 TAHFHGHSFDYKHRgvyRSDVFDLFPGTFQTVEMIPRTPGTWLLHCHVTDHIHAGMETTYTV 144
CuRO_1_Ceruloplasmin_like_1 cd04229
cupredoxin domain of ceruloplasmin homologs; Uncharacterized subfamily of ceruloplasmin ...
 746-913 1.82e-39

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: 144.48  E-value: 1.82e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 733903985  746 KTHYIAAVEVEWDYSP-NRTWEFERHQFHKESPGnsfLNKEDAFIGSKYKKVVYREYTDQTFSTPKSraeEEQHLQIQGP 824
Cdd:cd04229     1 RTYYIAAEEVDWDYAPsGKNKCCLGDDLEVSTLD---SQPGPYTIGSTYTKARYREYTDNSFSTPKP---TPAYLGILGP 74

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 733903985  825 LIMSSVGDKINIVFKN-LASRPYSIHAHGV-------KTDSSVVAITNPGETKMYVWKISARSSSERDDSHCTAWAYHST 896
Cdd:cd04229    75 VIRAEVGDTIKVVFKNnLDEFPVNMHPHGGlyskdneGTTDGAGDVVAPGETYTYRWIVPEDAGPGPGDPSSRLWLYHSH 154

                         170
                  ....*....|....*..
gi 733903985  897 VDIIKDTYSGLIGTLVV 913
Cdd:cd04229   155 VDVFAHTNAGLVGPIIV 171
CuRO_1_ceruloplasmin cd04222
The first cupredoxin domain of Ceruloplasmin; Ceruloplasmin is a multicopper oxidase essential ...
 746-916 2.53e-39

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: 144.10  E-value: 2.53e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 733903985  746 KTHYIAAVEVEWDYSPNRTWEFERHQFHKESPGNSFLNKEDAFIGSKYKKVVYREYTDQTFSTpksRAEEEQHLQIQGPL 825
Cdd:cd04222     1 REYYIGIRETQWDYAPSGKNLITNQTFDDDEHASVFLKRGPDRIGRVYKKAVYLQYTDDTYRT---EIEKPVWLGFLGPI 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 733903985  826 IMSSVGDKINIVFKNLASRPYSIHAHGV-------------------KTDSSVvaitNPGETKMYVWKISARSSSERDDS 886
Cdd:cd04222    78 LKAEVGDVIVVHLKNFASRPYSLHPHGVfynkenegalypdntsgfeKADDAV----PPGGSYTYTWTVPEEQAPTKADA 153

                         170       180       190
                  ....*....|....*....|....*....|
gi 733903985  887 HCTAWAYHSTVDIIKDTYSGLIGTLVVCPR 916
Cdd:cd04222   154 NCLTRIYHSHIDAPKDIASGLIGPLIICKK 183
CuRO_3_FVIII_like cd04227
The third cupredoxin domain of coagulation factor VIII and similar proteins; Factor VIII ...
 747-914 1.19e-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: 1.19e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 733903985  747 THYIAAVEVEWDYSPnrtweferhqfHKESPGNS-----FLNKEDAFIGSKYKKVVYREYTDQTFSTPKSRAEEEQhlqI 821
Cdd:cd04227     4 EHYIAAEELDWDYAP-----------LLSSTDDRelqsrYLPTGPQRIGYKYKKVAFVEYTDKTFKRREAKQTEKG---I 69

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 733903985  822 QGPLIMSSVGDKINIVFKNLASRPYSIHAHGVKTDSSVVAITN-------------PGETKMYVWKISARSSSERDDSHC 888
Cdd:cd04227    70 LGPLLKGEVGDQIHIMFKNTASRPYNIYPHGLTSVRPMYRSRNpagekdlktmpigPGETFGYMWELTAEDGPTEEDPRC 149

                         170       180
                  ....*....|....*....|....*.
gi 733903985  889 TAWAYHSTVDIIKDTYSGLIGTLVVC 914
Cdd:cd04227   150 LTRLYQSTVDPERDLASGLIGPLLIC 175
CuRO_3_FV_like cd14450
The third cupredoxin domain of coagulation factor V and similar proteins; Factor V is an ...
 747-914 6.97e-38

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: 140.01  E-value: 6.97e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 733903985  747 THYIAAVEVEWDYSPNRTWEFERHQFHKespgnsFLNKEDAFIGSKYKKVVYREYTDQTFsTPKSRAEEEQHLQIQGPLI 826
Cdd:cd14450     4 EYFIAAEEVIWDYAPSIPENMDKRYRSQ------YLDNFSNNIGKKYKKAVFTQYEDGSF-TKRLENPRPKEEGILGPVI 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 733903985  827 MSSVGDKINIVFKNLASRPYSIHAHGVKTDSSVVAIT---------------NPGETKMYVWKISARSSSERDDSHCTAW 891
Cdd:cd14450    77 RAQVRDTIKIVFKNKASRPYSIYPHGVTVSKAAEGASyppdprgnetqnkavQPGETYTYKWNILETDEPTARDPRCLTR 156

                         170       180
                  ....*....|....*....|...
gi 733903985  892 AYHSTVDIIKDTYSGLIGTLVVC 914
Cdd:cd14450   157 MYHSAVDITRDIASGLIGPLLIC 179
CuRO_6_FVIII_like cd11018
The sixth cupredoxin domain of coagulation factor VIII and similar proteins; Factor VIII ...
 236-374 2.46e-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: 136.93  E-value: 2.46e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 733903985  236 EFILMFSVMDENLSWYLEDNIRMYCSEPSKVDKDDEDFQESNKMHSINGYMYGYLPNLTMCVEDKVKWHLFGMGNEADIH 315
Cdd:cd11018     3 EFALLFTIFDETKSWYFEENMRRNCRPPCHIQTQDPWFHINNKFHAINGYVADTLPGLVMAQHQRIRWHLLNMGSDEEIH 82

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 733903985  316 SAYFHGQTLIER---HHRVDTINLFPATFIDALMIPRNPGEWLLSCQVNDHIEGGMQALFKV 374
Cdd:cd11018    83 SVHFHGLPFTVRakkEYRMGVYNLYPGVFGTVEMRPSTAGIWLVECTVGEHLLAGMSALFLV 144
CuRO_2_ceruloplasmin_like_2 cd11023
cupredoxin domain of ceruloplasmin homologs; Uncharacterized subfamily of ceruloplasmin ...
 936-1070 2.37e-35

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


Pssm-ID: 259909 [Multi-domain]  Cd Length: 118  Bit Score: 130.42  E-value: 2.37e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 733903985  936 VFDENESWYLDENIEtysanphlvdkeneeflESNKMHAINGKVFGNLHGLTMHVGDEVSWYLMAMGNEIDIHTAHFHGH 1015
Cdd:cd11023     3 EFIENSSIFLDLNVE-----------------EAGLMHSINGYVFGNLPGVTIAKGKRVRWHLVAYGNEVDFHTPHWHGQ 65

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 733903985 1016 SFDYKQTGiyRADVFDLFPGTFQTVEMIPQNPGTWLLHCHVTDHIHAGMEATYTV 1070
Cdd:cd11023    66 TVEADKSR--RTDVAELMPASMRVADMTAADVGTWLLHCHVHDHYMAGMMTQFAV 118
CuRO_6_FV_like cd14455
The sixth cupredoxin domain of coagulation factor V and similar proteins; Factor V is an ...
 930-1070 6.20e-34

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


Pssm-ID: 259997 [Multi-domain]  Cd Length: 140  Bit Score: 127.29  E-value: 6.20e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 733903985  930 FALLFMVFDENESWYLDENIETYSANPHLVDKEneeFLESNKMHAINGKVFgNLHGLTMHVGDEVSWYLMAMGNEIDIHT 1009
Cdd:cd14455     4 FVLLFMTFDEEKSWYYEKNRKRTCRENRVKDPN---VQDNHTFHAINGIIY-NLKGLRMYTNELVRWHLINMGGPKDLHV 79

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 733903985 1010 AHFHGHSFDYKQTGIYRADVFDLFPGTFQTVEMIPQNPGTWLLHCHVTDHIHAGMEATYTV 1070
Cdd:cd14455    80 VHFHGQTFTEKGLKDHQLGVYPLLPGSFATLEMKPSKPGLWLLETEVGESQQRGMQTLFLV 140
CuRO_5_FVIII_like cd04228
The fifth cupredoxin domain of coagulation factor VIII and similar proteins; Factor VIII ...
 39-223 2.42e-33

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: 126.54  E-value: 2.42e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 733903985   39 TREYYIGIVETAWDYAPGS-------TDIISGQRfaeeeqaevflKRGPQrigsiYKKAVYTQYTNILYDVIV---EKPS 108
Cdd:cd04228     1 IRHYFIAAVEVLWDYGMQRpqhflraRDPNRGRR-----------KSVPQ-----YKKVVFREYLDGSFTQPVyrgELDE 64

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 733903985  109 WLGFLGPIIKGEVGDSIVVHLKNFASRNYTLHPHGVKYtkenegafypDNTKGFEKRDDAVKPGGQYTYTWDVTEDQGPA 188
Cdd:cd04228    65 HLGILGPYIRAEVEDNIMVTFKNLASRPYSFHSSLISY----------EEDQRAEPRGNFVQPGEVQTYSWKVLHQMAPT 134

                         170       180       190
                  ....*....|....*....|....*....|....*
gi 733903985  189 KGDADCITRVYHSHIDAPRDVASGLVGPLIICRKG 223
Cdd:cd04228   135 KQEFDCKAWAYFSNVDLEKDLHSGLIGPLIICKTG 169
CuRO_2_ceruloplasmin_like_2 cd11023
cupredoxin domain of ceruloplasmin homologs; Uncharacterized subfamily of ceruloplasmin ...
 269-374 5.03e-33

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: 123.87  E-value: 5.03e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 733903985  269 DDEDFQESNKMHSINGYMYGYLPNLTMCVEDKVKWHLFGMGNEADIHSAYFHGQTL-IERHHRVDTINLFPATFIDALMI 347
Cdd:cd11023    12 LDLNVEEAGLMHSINGYVFGNLPGVTIAKGKRVRWHLVAYGNEVDFHTPHWHGQTVeADKSRRTDVAELMPASMRVADMT 91

                          90       100
                  ....*....|....*....|....*..
gi 733903985  348 PRNPGEWLLSCQVNDHIEGGMQALFKV 374
Cdd:cd11023    92 AADVGTWLLHCHVHDHYMAGMMTQFAV 118
CuRO_1_FVIII_like cd14452
The first cupredoxin domain of coagulation factor VIII and similar proteins; Factor VIII ...
 746-914 7.62e-33

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: 125.48  E-value: 7.62e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 733903985  746 KTHYIAAVEVEWDYSPNRTWEFERHQfhKESPGNsflnkedafIGSKYKKVVYREYTDQTFSTPKSRAEeeqHLQIQGPL 825
Cdd:cd14452     1 RRYYIAAVEIGWDYIHSDLGDPASEQ--RKKPKD---------IPQKYIKAVFVEYLDATFTVPKPRPA---WMGLLGPT 66

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 733903985  826 IMSSVGDKINIVFKNLASRPYSIHAHGV-------------------KTDSSVvaitNPGETKMYVWKISARSSSERDDS 886
Cdd:cd14452    67 IVAEVGDTVVITFKNLASQPYSLHAVGVsywkasegagyddstsqheKEDDAV----YPGGYHTYVWDISPKDGPTGSDP 142

                         170       180
                  ....*....|....*....|....*...
gi 733903985  887 HCTAWAYHSTVDIIKDTYSGLIGTLVVC 914
Cdd:cd14452   143 ECLTYSYSSQVDPVKDVNSGLIGALLVC 170
CuRO_2_FV_like cd14453
The second cupredoxin domain of coagulation factor V and similar proteins; Factor V is an ...
 234-374 4.73e-32

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: 121.12  E-value: 4.73e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 733903985  234 DAEFILMFSVMDENLSWYlednirmycsepskvdkdDEDFQESNKMHSINGYMYGYLPNLTMCVEDKVKWHLFGMGNEAD 313
Cdd:cd14453     1 YKEYVLMFGVFDENKSWY------------------KQNASVDSVKYTINGYTNGTLPDVSICAYDHVSWHLLGMSSEPE 62

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 733903985  314 IHSAYFHGQTLIERHHRVDTINLFPATFIDALMIPRNPGEWLLSCQVNDHIEGGMQALFKV 374
Cdd:cd14453    63 LFSVHFNGQVLEQNGHKVSAVGLVSGSSTTASMTVVHTGRWLISSLIMKHLQAGMYGYLNI 123
CuRO_6_FV_like cd14455
The sixth cupredoxin domain of coagulation factor V and similar proteins; Factor V is an ...
 236-374 4.95e-32

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: 121.90  E-value: 4.95e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 733903985  236 EFILMFSVMDENLSWYLEDNIRMYCSEpskVDKDDEDFQESNKMHSINGYMYGyLPNLTMCVEDKVKWHLFGMGNEADIH 315
Cdd:cd14455     3 EFVLLFMTFDEEKSWYYEKNRKRTCRE---NRVKDPNVQDNHTFHAINGIIYN-LKGLRMYTNELVRWHLINMGGPKDLH 78

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 733903985  316 SAYFHGQTLIE---RHHRVDTINLFPATFIDALMIPRNPGEWLLSCQVNDHIEGGMQALFKV 374
Cdd:cd14455    79 VVHFHGQTFTEkglKDHQLGVYPLLPGSFATLEMKPSKPGLWLLETEVGESQQRGMQTLFLV 140
CuRO_4_FVIII_like cd11016
The fourth cupredoxin domain of coagulation factor VIII and similar proteins; Factor VIII ...
 234-377 6.96e-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: 121.51  E-value: 6.96e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 733903985  234 DAEFILMFSVMDENLSWYLEDNIRMYCSEPSKVDKDDEDFQESNKMHSINGYMYGYLpNLTMCVEDKVKWHLFGMGNEAD 313
Cdd:cd11016     1 DKDWSLLFSVFDENNSWYLKENIHRFTQTPAGVNDTDPDFYASNVMHTINGIVFDRR-QFVICLTDVAYWYVLSVGAQTD 79

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 733903985  314 IHSAYFHGQTLIERHHRVDTINLFPATFIDALMIPRNPGEWLLSCQVNDHIEGGMQALFKVEGC 377
Cdd:cd11016    80 FLSVFFSGNTFKHQMVYEDVLTLFPFSGETVSMSPEVPGEWELGCFNGDFRSRGMSAQYTVSTC 143
CuRO_4_FVIII_like cd11016
The fourth cupredoxin domain of coagulation factor VIII and similar proteins; Factor VIII ...
 594-732 1.38e-31

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


Pssm-ID: 259902 [Multi-domain]  Cd Length: 143  Bit Score: 120.74  E-value: 1.38e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 733903985  594 LLATVFDENLSWYLDDNILMFTLNPNEIDKDNEDFQESNKMHSINGYMYGNQPgLEMCKGDVISWHLMGLGSEVDVHGIY 673
Cdd:cd11016     6 LLFSVFDENNSWYLKENIHRFTQTPAGVNDTDPDFYASNVMHTINGIVFDRRQ-FVICLTDVAYWYVLSVGAQTDFLSVF 84

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 733903985  674 FSQNTFITKGTRKDTANLFPHTFVTAIMKPDSEGIFEVSCLTTDHHRGGMKQKYKVKPC 732
Cdd:cd11016    85 FSGNTFKHQMVYEDVLTLFPFSGETVSMSPEVPGEWELGCFNGDFRSRGMSAQYTVSTC 143
CuRO_2_FVIII_like cd11015
The second cupredoxin domain of coagulation factor VIII and similar proteins; Factor VIII ...
 236-374 3.42e-31

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: 119.24  E-value: 3.42e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 733903985  236 EFILMFSVMDENLSWYLEDnirmycSEPSKVDKDDEDfQESNKMHSINGYMYGYLPNLTMCVEDKVKWHLFGMGNEADIH 315
Cdd:cd11015     3 AFVLLFAVFDEGKSWYSEV------GERKSRDKFKRA-DSRKEFHTINGYINASLPGLKICQRKPVIWHVIGMGTAPEVH 75

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 733903985  316 SAYFHGQTLIERHHRVDTINLFPATFIDALMIPRNPGEWLLSCQVNDHIEGGMQALFKV 374
Cdd:cd11015    76 SIFFEGHTFLVRTHRKVSLEISPMTFLTAQTKPATVGSFLIFCQIHSHQHDGMEAMVKV 134
CuRO_4_FV_like cd14454
The fourth cupredoxin domain of coagulation factor V and similar proteins; Factor V is an ...
 234-373 3.01e-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: 116.89  E-value: 3.01e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 733903985  234 DAEFILMFSVMDENLSWYLEDNIRMYCSEPSKVDKDDEDFQESNKMHSINGYMYGYLPNLTMCVEDKVKWHLFGMGNEAD 313
Cdd:cd14454     1 DLEQHAVFAVFDENKSWYLEENINKYCSNPNNVKKDDPKFYKSNIMPTINGYAYESSAPLGFCHSEVVQWHISSVGTQDE 80

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 733903985  314 IHSAYFHGQTLIERHHRVDTINLFPATFIDALMIPRNPGEWLLSCQVNDHIEGGMQALFK 373
Cdd:cd14454    81 IITVHLSGHTFRYKGKHEDTLNLFPMSGESITVTMDNLGTWLLGSFGSSKKSKGLRVRFT 140
CuRO_4_FV_like cd14454
The fourth cupredoxin domain of coagulation factor V and similar proteins; Factor V is an ...
 597-732 1.15e-29

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


Pssm-ID: 259996 [Multi-domain]  Cd Length: 144  Bit Score: 115.35  E-value: 1.15e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 733903985  597 TVFDENLSWYLDDNILMFTLNPNEIDKDNEDFQESNKMHSINGYMYGNQPGLEMCKGDVISWHLMGLGSEVDVHGIYFSQ 676
Cdd:cd14454     9 AVFDENKSWYLEENINKYCSNPNNVKKDDPKFYKSNIMPTINGYAYESSAPLGFCHSEVVQWHISSVGTQDEIITVHLSG 88

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 733903985  677 NTFITKGTRKDTANLFPHTFVTAIMKPDSEGIFEVSCLTTDHHRGGMKQKYKVKPC 732
Cdd:cd14454    89 HTFRYKGKHEDTLNLFPMSGESITVTMDNLGTWLLGSFGSSKKSKGLRVRFTDVIC 144
CuRO_4_FVIII_like cd11016
The fourth cupredoxin domain of coagulation factor VIII and similar proteins; Factor VIII ...
 932-1071 4.91e-29

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: 113.42  E-value: 4.91e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 733903985  932 LLFMVFDENESWYLDENIETYSANPHLVDKENEEFLESNKMHAINGKVFGNLHgLTMHVGDEVSWYLMAMGNEIDIHTAH 1011
Cdd:cd11016     6 LLFSVFDENNSWYLKENIHRFTQTPAGVNDTDPDFYASNVMHTINGIVFDRRQ-FVICLTDVAYWYVLSVGAQTDFLSVF 84

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 733903985 1012 FHGHSFdyKQTGIYRaDVFDLFPGTFQTVEMIPQNPGTWLLHCHVTDHIHAGMEATYTVL 1071
Cdd:cd11016    85 FSGNTF--KHQMVYE-DVLTLFPFSGETVSMSPEVPGEWELGCFNGDFRSRGMSAQYTVS 141
CuRO_6_FVIII_like cd11018
The sixth cupredoxin domain of coagulation factor VIII and similar proteins; Factor VIII ...
 590-729 5.33e-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: 110.36  E-value: 5.33e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 733903985  590 REFFLLATVFDENLSWYLDDNILMFTLNPNEIDKDNEDFQESNKMHSINGYMYGNQPGLEMCKGDVISWHLMGLGSEVDV 669
Cdd:cd11018     2 QEFALLFTIFDETKSWYFEENMRRNCRPPCHIQTQDPWFHINNKFHAINGYVADTLPGLVMAQHQRIRWHLLNMGSDEEI 81

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 733903985  670 HGIYFSQNTFITKGT---RKDTANLFPHTFVTAIMKPDSEGIFEVSCLTTDHHRGGMKQKYKV 729
Cdd:cd11018    82 HSVHFHGLPFTVRAKkeyRMGVYNLYPGVFGTVEMRPSTAGIWLVECTVGEHLLAGMSALFLV 144
CuRO_4_FV_like cd14454
The fourth cupredoxin domain of coagulation factor V and similar proteins; Factor V is an ...
 933-1052 1.83e-27

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


Pssm-ID: 259996 [Multi-domain]  Cd Length: 144  Bit Score: 108.81  E-value: 1.83e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 733903985  933 LFMVFDENESWYLDENIETYSANPHLVDKENEEFLESNKMHAINGKVFGNLHGLTMHVGDEVSWYLMAMGNEIDIHTAHF 1012
Cdd:cd14454     7 VFAVFDENKSWYLEENINKYCSNPNNVKKDDPKFYKSNIMPTINGYAYESSAPLGFCHSEVVQWHISSVGTQDEIITVHL 86

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 733903985 1013 HGHSFDYKQTgiyRADVFDLFPGTFQTVEMIPQNPGTWLL 1052
Cdd:cd14454    87 SGHTFRYKGK---HEDTLNLFPMSGESITVTMDNLGTWLL 123
CuRO_1_FV_like cd04226
The first cupredoxin domain of coagulation factor VIII and similar proteins; Factor V is an ...
 748-914 2.67e-27

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: 109.18  E-value: 2.67e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 733903985  748 HYIAAVEVEWDYSPnrtwefERHQFHKESPGNSFlnkedafigskyKKVVYREYtDQTFSTPKSRAEEEQHLqiqGPLIM 827
Cdd:cd04226     3 YYIAAQNIDWDYTP------QSEELRLKRSEQSF------------KKIVYREY-EEGFKKEKPADLSSGLL---GPTLR 60

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 733903985  828 SSVGDKINIVFKNLASRPYSIHAHGV-------------------KTDSSVVaitnPGETKMYVWKISARSSSERDDSHC 888
Cdd:cd04226    61 AEVGDTLIVHFKNMADKPLSIHPQGIaygkksegslysdntspveKLDDAVQ----PGQEYTYVWDITEEVGPTEADPPC 136

                         170       180
                  ....*....|....*....|....*.
gi 733903985  889 TAWAYHSTVDIIKDTYSGLIGTLVVC 914
Cdd:cd04226   137 LTYIYYSHVNMVRDFNSGLIGALLIC 162
CuRO_2_FVIII_like cd11015
The second cupredoxin domain of coagulation factor VIII and similar proteins; Factor VIII ...
 590-729 4.05e-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: 4.05e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 733903985  590 REFFLLATVFDENLSWYLDdnilmfTLNPNEIDKDNEDfQESNKMHSINGYMYGNQPGLEMCKGDVISWHLMGLGSEVDV 669
Cdd:cd11015     2 QAFVLLFAVFDEGKSWYSE------VGERKSRDKFKRA-DSRKEFHTINGYINASLPGLKICQRKPVIWHVIGMGTAPEV 74

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 733903985  670 HGIYFSQNTFITKGTRKDTANLFPHTFVTAIMKPDSEGIFEVSCLTTDHHRGGMKQKYKV 729
Cdd:cd11015    75 HSIFFEGHTFLVRTHRKVSLEISPMTFLTAQTKPATVGSFLIFCQIHSHQHDGMEAMVKV 134
CuRO_2_ceruloplasmin_like_2 cd11023
cupredoxin domain of ceruloplasmin homologs; Uncharacterized subfamily of ceruloplasmin ...
 624-729 9.58e-23

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


Pssm-ID: 259909 [Multi-domain]  Cd Length: 118  Bit Score: 94.60  E-value: 9.58e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 733903985  624 DNEDFQESNKMHSINGYMYGNQPGLEMCKGDVISWHLMGLGSEVDVHGIYFSQNTFITKGTRK-DTANLFPHTFVTAIMK 702
Cdd:cd11023    12 LDLNVEEAGLMHSINGYVFGNLPGVTIAKGKRVRWHLVAYGNEVDFHTPHWHGQTVEADKSRRtDVAELMPASMRVADMT 91

                          90       100
                  ....*....|....*....|....*..
gi 733903985  703 PDSEGIFEVSCLTTDHHRGGMKQKYKV 729
Cdd:cd11023    92 AADVGTWLLHCHVHDHYMAGMMTQFAV 118
CuRO_2_FVIII_like cd11015
The second cupredoxin domain of coagulation factor VIII and similar proteins; Factor VIII ...
 930-1070 6.59e-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: 89.58  E-value: 6.59e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 733903985  930 FALLFMVFDENESWYLDenietySANPHLVDKENEEFlESNKMHAINGKVFGNLHGLTMHVGDEVSWYLMAMGNEIDIHT 1009
Cdd:cd11015     4 FVLLFAVFDEGKSWYSE------VGERKSRDKFKRAD-SRKEFHTINGYINASLPGLKICQRKPVIWHVIGMGTAPEVHS 76

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 733903985 1010 AHFHGHSFDYKQtgiYRADVFDLFPGTFQTVEMIPQNPGTWLLHCHVTDHIHAGMEATYTV 1070
Cdd:cd11015    77 IFFEGHTFLVRT---HRKVSLEISPMTFLTAQTKPATVGSFLIFCQIHSHQHDGMEAMVKV 134
CuRO_6_FV_like cd14455
The sixth cupredoxin domain of coagulation factor V and similar proteins; Factor V is an ...
 590-729 1.38e-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: 86.07  E-value: 1.38e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 733903985  590 REFFLLATVFDENLSWYLDDNILMFTLNPNEIDKDnedFQESNKMHSINGYMYgNQPGLEMCKGDVISWHLMGLGSEVDV 669
Cdd:cd14455     2 REFVLLFMTFDEEKSWYYEKNRKRTCRENRVKDPN---VQDNHTFHAINGIIY-NLKGLRMYTNELVRWHLINMGGPKDL 77

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 733903985  670 HGIYFSQNTFITKGTRKDTAN---LFPHTFVTAIMKPDSEGIFEVSCLTTDHHRGGMKQKYKV 729
Cdd:cd14455    78 HVVHFHGQTFTEKGLKDHQLGvypLLPGSFATLEMKPSKPGLWLLETEVGESQQRGMQTLFLV 140
Cu-oxidase_2 pfam07731
Multicopper oxidase; This entry contains many divergent copper oxidase-like domains that are ...
 970-1074 6.64e-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: 6.64e-19
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 733903985   970 NKMHAINGKVFG-NLHGLTMHVGDEVSWYLMamGNEIDIHTAHFHGHSFDYKQTGI----------------YRADVFDL 1032
Cdd:pfam07731   19 RNDWAINGLLFPpNTNVITLPYGTVVEWVLQ--NTTTGVHPFHLHGHSFQVLGRGGgpwpeedpktynlvdpVRRDTVQV 96

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|..
gi 733903985  1033 FPGTFQTVEMIPQNPGTWLLHCHVTDHIHAGMEATYTVLPKE 1074
Cdd:pfam07731   97 PPGGWVAIRFRADNPGVWLFHCHILWHLDQGMMGQFVVRPGD 138
CuRO_2_FV_like cd14453
The second cupredoxin domain of coagulation factor V and similar proteins; Factor V is an ...
 930-1066 3.99e-18

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: 81.44  E-value: 3.99e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 733903985  930 FALLFMVFDENESWYldenietysanphlvdkeNEEFLESNKMHAINGKVFGNLHGLTMHVGDEVSWYLMAMGNEIDIHT 1009
Cdd:cd14453     4 YVLMFGVFDENKSWY------------------KQNASVDSVKYTINGYTNGTLPDVSICAYDHVSWHLLGMSSEPELFS 65

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 733903985 1010 AHFHGHSFDYKQtgiYRADVFDLFPGTFQTVEMIPQNPGTWLLHCHVTDHIHAGMEA 1066
Cdd:cd14453    66 VHFNGQVLEQNG---HKVSAVGLVSGSSTTASMTVVHTGRWLISSLIMKHLQAGMYG 119
CuRO_2_FV_like cd14453
The second cupredoxin domain of coagulation factor V and similar proteins; Factor V is an ...
 590-723 7.71e-18

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: 80.67  E-value: 7.71e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 733903985  590 REFFLLATVFDENLSWYlddnilmftlnpneidkdNEDFQESNKMHSINGYMYGNQPGLEMCKGDVISWHLMGLGSEVDV 669
Cdd:cd14453     2 KEYVLMFGVFDENKSWY------------------KQNASVDSVKYTINGYTNGTLPDVSICAYDHVSWHLLGMSSEPEL 63

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....
gi 733903985  670 HGIYFSQNTFITKGTRKDTANLFPHTFVTAIMKPDSEGIFEVSCLTTDHHRGGM 723
Cdd:cd14453    64 FSVHFNGQVLEQNGHKVSAVGLVSGSSTTASMTVVHTGRWLISSLIMKHLQAGM 117
CuRO_1_LCC_like cd04206
Cupredoxin domain 1 of laccase-like multicopper oxidases; including laccase, CueO, spore coat ...
 111-220 3.01e-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: 78.87  E-value: 3.01e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 733903985  111 GFLGPIIKGEVGDSIVVHLKN-FASRNYTLHPHGVKYTKENEGAFYPDNTKgfekrdDAVKPGGQYTYTWDVTEDQGpak 189
Cdd:cd04206    27 QFPGPTIRVKEGDTVEVTVTNnLPNEPTSIHWHGLRQPGTNDGDGVAGLTQ------CPIPPGESFTYRFTVDDQAG--- 97

                          90       100       110
                  ....*....|....*....|....*....|.
gi 733903985  190 gdadciTRVYHSHIDAprDVASGLVGPLIIC 220
Cdd:cd04206    98 ------TFWYHSHVGG--QRADGLYGPLIVE 120
CuRO_1_LCC_like cd04206
Cupredoxin domain 1 of laccase-like multicopper oxidases; including laccase, CueO, spore coat ...
 453-574 5.31e-15

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


Pssm-ID: 259869 [Multi-domain]  Cd Length: 120  Bit Score: 72.32  E-value: 5.31e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 733903985  453 AHKKRLPEEEHLGLLGPVIKAEVGESIRVTFRNN-ASRPFSIQPHGVSYLKSNEGAlyrTASRDTESPasyVSPGASFTY 531
Cdd:cd04206    15 DGVLRQVITVNGQFPGPTIRVKEGDTVEVTVTNNlPNEPTSIHWHGLRQPGTNDGD---GVAGLTQCP---IPPGESFTY 88

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|...
gi 733903985  532 EWNVPEDVGptdqdpdclTWFYYSAVDSVRDTnsGLVGPLLVC 574
Cdd:cd04206    89 RFTVDDQAG---------TFWYHSHVGGQRAD--GLYGPLIVE 120
CuRO_3_LCC_like cd04207
Cupredoxin domain 3 of laccase-like multicopper oxidases; including laccase, CueO, spore coat ...
 974-1069 7.05e-13

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: 66.71  E-value: 7.05e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 733903985  974 AINGKVF----GNLHGLTMHVGDEVSWYLMAMGNEIDIHTAHFHGHSF------------DYKQTGIYRADVFDLFPGTF 1037
Cdd:cd04207    21 VINGMPFkegdANTDIFSVEAGDVVEIVLINAGNHDMQHPFHLHGHSFwvlgsgggpfdaPLNLTNPPWRDTVLVPPGGW 100

                          90       100       110
                  ....*....|....*....|....*....|..
gi 733903985 1038 QTVEMIPQNPGTWLLHCHVTDHIHAGMEATYT 1069
Cdd:cd04207   101 VVIRFKADNPGVWMLHCHILEHEDAGMMTVFE 132
Cu-oxidase_3 pfam07732
Multicopper oxidase; This entry contains many divergent copper oxidase-like domains that are ...
 94-219 1.78e-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: 64.96  E-value: 1.78e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 733903985    94 QYTNILYDVIVEKPSWL---GFLGPIIKGEVGDSIVVHLKNFASRNYTLHPHGVKYTKENEGAFYPDNTKgfekrdDAVK 170
Cdd:pfam07732    3 TYGTVSPLGGTRQAVIGvngQFPGPTIRVREGDTVVVNVTNNLDEPTSIHWHGLQQRGTPWMDGVPGVTQ------CPIP 76

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*....
gi 733903985   171 PGGQYTYTWDVTEDQGpakgdadciTRVYHSHIDAPRdvASGLVGPLII 219
Cdd:pfam07732   77 PGQSFTYRFQVKQQAG---------TYWYHSHTSGQQ--AAGLAGAIII 114
CuRO_1_2DMCO_NIR_like_2 cd14449
The cupredoxin domain 1 of a two-domain laccase related to nitrite reductase; The two-domain ...
 468-576 1.21e-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: 63.44  E-value: 1.21e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 733903985  468 GPVIKAEVGESIRVTFRNNASRPFSIQPHGVSYLKSNEGALyrtasrdteSPASYVSPGASFTYEWNVPEDVGPTDQDPD 547
Cdd:cd14449    29 GPVIEVREGDTLKILFRNTLDVPASLHPHGVDYTTASDGTG---------MNASIVAPGDTRIYTWRTHGGYRRADGSWA 99

                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 733903985  548 CLT---WFYYSAV----DSVRDTNSGLVGPLLVCRK 576
Cdd:cd14449   100 EGTagyWHYHDHVfgteHGTEGLSRGLYGALIVRRV 135
CuRO_D2_2dMcoN_like cd04202
The second cupredoxin domain of bacterial two domain multicopper oxidase McoN and similar ...
 972-1064 5.48e-11

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: 61.50  E-value: 5.48e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 733903985  972 MHAINGKVFGNLHGLTMHVGDEVSWYLMAMGNeiDIHTAHFHGHSFDY--------KQTGIYRADVFDLFPGTFQTVEMI 1043
Cdd:cd04202    29 YFTINGKSFPATPPLVVKEGDRVRIRLINLSM--DHHPMHLHGHFFLVtatdggpiPGSAPWPKDTLNVAPGERYDIEFV 106

                          90       100
                  ....*....|....*....|.
gi 733903985 1044 PQNPGTWLLHCHVTDHIHAGM 1064
Cdd:cd04202   107 ADNPGDWMFHCHKLHHAMNGM 127
CuRO_3_CumA_like cd13906
The third cupredoxin domain of CumA like multicopper oxidase; This multicopper oxidase (MCO) ...
 974-1070 1.69e-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: 1.69e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 733903985  974 AINGKVFGNLHG-------LTMHVGDevsWYLMAMGNEID-IHTAHFHGHSFDY----KQTGIYR--ADVFDLFPGtfQT 1039
Cdd:cd13906    30 AINGTSWTGGDHshlppplATLKRGR---SYVLRLVNETAfLHPMHLHGHFFRVlsrnGRPVPEPfwRDTVLLGPK--ET 104

                          90       100       110
                  ....*....|....*....|....*....|...
gi 733903985 1040 VE--MIPQNPGTWLLHCHVTDHIHAGMEATYTV 1070
Cdd:cd13906   105 VDiaFVADNPGDWMFHCHILEHQETGMMGVIRV 137
CuRO_1_2DMCO_NIR_like_2 cd14449
The cupredoxin domain 1 of a two-domain laccase related to nitrite reductase; The two-domain ...
 114-222 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. 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: 59.20  E-value: 2.75e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 733903985  114 GPIIKGEVGDSIVVHLKNFASRNYTLHPHGVKYTKENEGAFYPDNtkgfekrddAVKPGGQYTYTWDVTEDQGPAKGDAD 193
Cdd:cd14449    29 GPVIEVREGDTLKILFRNTLDVPASLHPHGVDYTTASDGTGMNAS---------IVAPGDTRIYTWRTHGGYRRADGSWA 99

                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 733903985  194 CITR---VYHSHI----DAPRDVASGLVGPLIICRK 222
Cdd:cd14449   100 EGTAgywHYHDHVfgteHGTEGLSRGLYGALIVRRV 135
CuRO_1_Diphenol_Ox cd13857
The first cupredoxin domain of fungal laccase, diphenol oxidase; Diphenol oxidase belongs to ...
 112-219 1.95e-09

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: 56.50  E-value: 1.95e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 733903985  112 FLGPIIKGEVGDSIVVHLKNFASRNYTLHPHGVKytkeNEGAFYPDNTKGFEKRddAVKPGGQYTYTWDVTEDQGpakgd 191
Cdd:cd13857    28 FPGPLIEANQGDRIVVHVTNELDEPTSIHWHGLF----QNGTNWMDGTAGITQC--PIPPGGSFTYNFTVDGQYG----- 96

                          90       100
                  ....*....|....*....|....*...
gi 733903985  192 adciTRVYHSHIDAprDVASGLVGPLII 219
Cdd:cd13857    97 ----TYWYHSHYST--QYADGLVGPLIV 118
CuRO_1_CumA_like cd13861
The first cupredoxin domain of CumA like multicopper oxidase; This multicopper oxidase (MCO) ...
 465-573 2.95e-09

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: 56.09  E-value: 2.95e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 733903985  465 GLLGPVIKAEVGESIRVTFRNNASRPFSIQPHGVsylksnegalyRTASR-D-----TESPasyVSPGASFTYEWNVPeD 538
Cdd:cd13861    28 QVPGPELRVRQGDTLRVRLTNRLPEPTTIHWHGL-----------RLPNAmDgvpglTQPP---VPPGESFTYEFTPP-D 92

                          90       100       110
                  ....*....|....*....|....*....|....*
gi 733903985  539 VGptdqdpdclTWFYYSAVDSVRDTNSGLVGPLLV 573
Cdd:cd13861    93 AG---------TYWYHPHVGSQEQLDRGLYGPLIV 118
CuRO_1_2DMCO_NIR_like cd11024
The cupredoxin domain 1 of a two-domain laccase related to nitrite reductase; The two-domain ...
 468-573 4.23e-09

The cupredoxin domain 1 of a two-domain laccase related to nitrite reductase; The two-domain laccase (small laccase) in this family differs significantly from all laccases. It resembles the two domain nitrite reductase in both sequence and structure. It consists of two cupredoxin domains and forms trimers and hence resembles the quaternary structure of nitrite reductases more than that of large laccases. There are three trinuclear copper clusters in the enzyme localized between domains 1 and 2 of each pair of neighbor chains. 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: 55.35  E-value: 4.23e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 733903985  468 GPVIKAEVGESIRVTFRNNASRPFSIQPHGVsylksnegalYRTASRDTESPAsyVSPGASFTYEWnVPEDVGptdqdpd 547
Cdd:cd11024    32 GPTLRATEGDLVRIHFINTGDHPHTIHFHGI----------HDAAMDGTGLGP--IMPGESFTYEF-VAEPAG------- 91

                          90       100
                  ....*....|....*....|....*..
gi 733903985  548 clTWFYYSAVDSVRD-TNSGLVGPLLV 573
Cdd:cd11024    92 --THLYHCHVQPLKEhIAMGLYGAFIV 116
CuRO_3_CopA cd13896
The third cupredoxin domain of CopA copper resistance protein family; CopA is a multicopper ...
 975-1064 1.19e-08

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: 54.18  E-value: 1.19e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 733903985  975 INGKVFGNLHGLTMHVGDEVswyLMAMGNEIDI-HTAHFHGHSFDYKQ-TGIYRA--DVFDLFPGTFQTVEMIPQNPGTW 1050
Cdd:cd13896    19 INGKAYPDADPLRVREGERV---RIVFVNDTMMaHPMHLHGHFFQVENgNGEYGPrkDTVLVPPGETVSVDFDADNPGRW 95

                          90
                  ....*....|....
gi 733903985 1051 LLHCHVTDHIHAGM 1064
Cdd:cd13896    96 AFHCHNLYHMEAGM 109
CuRO_1_CumA_like cd13861
The first cupredoxin domain of CumA like multicopper oxidase; This multicopper oxidase (MCO) ...
 111-219 1.56e-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: 53.78  E-value: 1.56e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 733903985  111 GFLGPIIKGEVGDSIVVHLKNFASRNYTLHPHGVKYTKENEGAfyPDNTKgfekrdDAVKPGGQYTYTWdVTEDQGpakg 190
Cdd:cd13861    28 QVPGPELRVRQGDTLRVRLTNRLPEPTTIHWHGLRLPNAMDGV--PGLTQ------PPVPPGESFTYEF-TPPDAG---- 94

                          90       100
                  ....*....|....*....|....*....
gi 733903985  191 dadciTRVYHSHIDAPRDVASGLVGPLII 219
Cdd:cd13861    95 -----TYWYHPHVGSQEQLDRGLYGPLIV 118
CuRO_3_CumA_like cd13906
The third cupredoxin domain of CumA like multicopper oxidase; This multicopper oxidase (MCO) ...
 302-374 1.62e-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: 54.31  E-value: 1.62e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 733903985  302 KWHLFGMGNEAD-IHSAYFHG----------QTLIERHHRvDTINLFPATFIDALMIPRNPGEWLLSCQVNDHIEGGMQA 370
Cdd:cd13906    55 RSYVLRLVNETAfLHPMHLHGhffrvlsrngRPVPEPFWR-DTVLLGPKETVDIAFVADNPGDWMFHCHILEHQETGMMG 133


                  ....
gi 733903985  371 LFKV 374
Cdd:cd13906   134 VIRV 137
CuRO_1_LCC_like cd04206
Cupredoxin domain 1 of laccase-like multicopper oxidases; including laccase, CueO, spore coat ...
 820-914 2.05e-08

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: 53.44  E-value: 2.05e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 733903985  820 QIQGPLIMSSVGDKINIVFKN-LASRPYSIHAHGVKTDSS-----VVAIT----NPGETKMYVWKIsarssserDDSHCT 889
Cdd:cd04206    27 QFPGPTIRVKEGDTVEVTVTNnLPNEPTSIHWHGLRQPGTndgdgVAGLTqcpiPPGESFTYRFTV--------DDQAGT 98

                          90       100
                  ....*....|....*....|....*
gi 733903985  890 AWaYHSTVDIikDTYSGLIGTLVVC 914
Cdd:cd04206    99 FW-YHSHVGG--QRADGLYGPLIVE 120
SufI COG2132
Multicopper oxidase with three cupredoxin domains (includes cell division protein FtsP and ...
 972-1072 2.44e-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: 57.64  E-value: 2.44e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 733903985  972 MHAINGKVFGNLH-GLTMHVGDEVSWYLMAMGNeiDIHTAHFHGHSF------DYKQTGIYRADVFDLFPGtfQTVEMI- 1043
Cdd:COG2132   317 VWTINGKAFDPDRpDLTVKLGERERWTLVNDTM--MPHPFHLHGHQFqvlsrnGKPPPEGGWKDTVLVPPG--ETVRILf 392

                          90       100       110
                  ....*....|....*....|....*....|.
gi 733903985 1044 --PQNPGTWLLHCHVTDHIHAGMEATYTVLP 1072
Cdd:COG2132   393 rfDNYPGDWMFHCHILEHEDAGMMGQFEVVP 423
CuRO_3_LCC_like cd04207
Cupredoxin domain 3 of laccase-like multicopper oxidases; including laccase, CueO, spore coat ...
 281-372 4.72e-08

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: 52.85  E-value: 4.72e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 733903985  281 SING----YMYGYLPNLTMCVEDKVKWHLFGMGNEADIHSAYFHGQtlierHHRV--------------------DTINL 336
Cdd:cd04207    21 VINGmpfkEGDANTDIFSVEAGDVVEIVLINAGNHDMQHPFHLHGH-----SFWVlgsgggpfdaplnltnppwrDTVLV 95

                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 733903985  337 FPATFIDALMIPRNPGEWLLSCQVNDHIEGGMQALF 372
Cdd:cd04207    96 PPGGWVVIRFKADNPGVWMLHCHILEHEDAGMMTVF 131
CuRO_D1_2dMcoN_like cd13859
The first cupredoxin domain of bacterial two domain multicopper oxidase McoN and similar ...
 114-219 5.24e-08

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: 52.48  E-value: 5.24e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 733903985  114 GPIIKGEVGDSIVVHLKNFASRNYTLHPHGVKYTkeneGAFYPDNTKGFEKRddAVKPGGQYTYTWDVtEDQGpakgdad 193
Cdd:cd13859    31 GPLIHVKEGDDLVVHVTNNTTLPHTIHWHGVLQM----GSWKMDGVPGVTQP--AIEPGESFTYKFKA-ERPG------- 96

                          90       100
                  ....*....|....*....|....*..
gi 733903985  194 ciTRVYHSHIDAPRDVA-SGLVGPLII 219
Cdd:cd13859    97 --TLWYHCHVNVNEHVGmRGMWGPLIV 121
CuRO_1_2DMCO_NIR_like cd11024
The cupredoxin domain 1 of a two-domain laccase related to nitrite reductase; The two-domain ...
 114-219 5.48e-08

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


Pssm-ID: 259910 [Multi-domain]  Cd Length: 119  Bit Score: 52.27  E-value: 5.48e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 733903985  114 GPIIKGEVGDSIVVHLKNFASRNYTLHPHGVKYTKENEGAFYPdntkgfekrddaVKPGGQYTYTWDVTedqgPAKgdad 193
Cdd:cd11024    32 GPTLRATEGDLVRIHFINTGDHPHTIHFHGIHDAAMDGTGLGP------------IMPGESFTYEFVAE----PAG---- 91

                          90       100
                  ....*....|....*....|....*...
gi 733903985  194 ciTRVYHSHIdAP--RDVASGLVGPLII 219
Cdd:cd11024    92 --THLYHCHV-QPlkEHIAMGLYGAFIV 116
CuRO_3_MaLCC_like cd13901
The third cupredoxin domain of the fungal laccases similar to Ma-LCC from Melanocarpus ...
 988-1064 7.08e-08

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


Pssm-ID: 259968 [Multi-domain]  Cd Length: 157  Bit Score: 53.00  E-value: 7.08e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 733903985  988 MHVGDEVSWYLMAMGNEIDI-HTAHFHGHSFdY--KQ-TGIY-------------RADVFDLFPGTFQTVEMIPQNPGTW 1050
Cdd:cd13901    60 IELPKANKWVYIVIQNNSPLpHPIHLHGHDF-YilAQgTGTFdddgtilnlnnppRRDVAMLPAGGYLVIAFKTDNPGAW 138

                          90
                  ....*....|....
gi 733903985 1051 LLHCHVTDHIHAGM 1064
Cdd:cd13901   139 LMHCHIAWHASGGL 152
Cu-oxidase pfam00394
Multicopper oxidase; Many of the proteins in this family contain multiple similar copies of ...
 241-377 7.86e-08

Multicopper oxidase; Many of the proteins in this family contain multiple similar copies of this plastocyanin-like domain.


Pssm-ID: 395317 [Multi-domain]  Cd Length: 146  Bit Score: 52.70  E-value: 7.86e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 733903985   241 FSVMDENLSWYlEDNIRMYCSEPSKVDKDDEDFQESNKMHSINGYMYGYLPNLTMCVEDKVKWHLFgMGNEADIHSAYFH 320
Cdd:pfam00394    1 EDYVITLSDWY-HKDAKDLEKELLASGKAPTDFPPVPDAVLINGKDGASLATLTVTPGKTYRLRII-NVALDDSLNFSIE 78

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 733903985   321 GQ--TLIE---RHH---RVDTINLFPATFIDALMIP-RNPGEWLLSCQVN-DHIEGGMQALFKVEGC 377
Cdd:pfam00394   79 GHkmTVVEvdgVYVnpfTVDSLDIFPGQRYSVLVTAnQDPGNYWIVASPNiPAFDNGTAAAILRYSG 145
CuRO_3_MCO_like_3 cd13909
The third cupredoxin domain of uncharacterized multicopper oxidase; Multicopper Oxidases (MCOs) ...
 1008-1064 8.12e-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: 52.52  E-value: 8.12e-08
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 733903985 1008 HTAHFHGHSF-----DYkQTGIYRaDVFDLFPGTFQTVEMIPQNPGTWLLHCHVTDHIHAGM 1064
Cdd:cd13909    71 HGMHLHGHHFrailpNG-ALGPWR-DTLLMDRGETREIAFVADNPGDWLLHCHMLEHAAAGM 130
CuRO_1_Abr2_like cd13850
The first cupredoxin domain of a group of fungal Laccases similar to Abr2 from Aspergillus ...
 105-219 8.90e-08

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: 51.53  E-value: 8.90e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 733903985  105 EKPSWLG---FLGPIIKGEVGDSIVVHLKNFASRNYTLHPHGVkytkENEGAFYPDNTKGFEKRddAVKPGGQYTYTWDV 181
Cdd:cd13850    16 EREVILIngqFPGPPIILDEGDEVEILVTNNLPVNTTIHFHGI----LQRGTPWSDGVPGVTQW--PIQPGGSFTYRWKA 89

                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 733903985  182 TEDQGpakgdadciTRVYHSHIdapRDVAS-GLVGPLII 219
Cdd:cd13850    90 EDQYG---------LYWYHSHY---RGYYMdGLYGPIYI 116
CuRO_3_McoC_like cd13902
The third cupredoxin domain of a multicopper oxidase McoC and similar proteins; This family ...
 972-1070 9.72e-08

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: 51.63  E-value: 9.72e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 733903985  972 MHAINGKVFG-NLHGLTMHVGDEVSWYLMamgNEIDI-HTAHFHGHSF------DYKQTGIYRA--DVFDLFPGTFQTVE 1041
Cdd:cd13902    20 MFLINGKTFDmNRIDFVAKVGEVEVWEVT---NTSHMdHPFHLHGTQFqvleidGNPQKPEYRAwkDTVNLPPGEAVRIA 96

                          90       100
                  ....*....|....*....|....*....
gi 733903985 1042 MIPQNPGTWLLHCHVTDHIHAGMEATYTV 1070
Cdd:cd13902    97 TRQDDPGMWMYHCHILEHEDAGMMGMLHV 125
SufI COG2132
Multicopper oxidase with three cupredoxin domains (includes cell division protein FtsP and ...
 112-242 1.27e-07

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


Pssm-ID: 441735 [Multi-domain]  Cd Length: 423  Bit Score: 55.33  E-value: 1.27e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 733903985  112 FLGPIIKGEVGDSIVVHLKNFASRNYTLHPHGVKYTKENEGafYPdntkgfekrDDAVKPGGQYTYTWDVteDQGPAkgd 191
Cdd:COG2132    42 YPGPTIRVREGDRVRVRVTNRLPEPTTVHWHGLRVPNAMDG--VP---------GDPIAPGETFTYEFPV--PQPAG--- 105

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 733903985  192 adciTRVYHSHIDA--PRDVASGLVGPLIIcrkgamNKDNDKY--VDAEFILMFS 242
Cdd:COG2132   106 ----TYWYHPHTHGstAEQVYRGLAGALIV------EDPEEDLprYDRDIPLVLQ 150
CuRO_1_2DMCO_NIR_like_2 cd14449
The cupredoxin domain 1 of a two-domain laccase related to nitrite reductase; The two-domain ...
 821-897 1.79e-07

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


Pssm-ID: 259991 [Multi-domain]  Cd Length: 135  Bit Score: 51.50  E-value: 1.79e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 733903985  821 IQGPLIMSSVGDKINIVFKNLASRPYSIHAHGVKTD-SSVVAITN-----PGETKMYVWKiSARSSSERDDSHCTA---- 890
Cdd:cd14449    27 VPGPVIEVREGDTLKILFRNTLDVPASLHPHGVDYTtASDGTGMNasivaPGDTRIYTWR-THGGYRRADGSWAEGtagy 105


                  ....*..
gi 733903985  891 WAYHSTV 897
Cdd:cd14449   106 WHYHDHV 112
CuRO_1_MaLCC_like cd13854
The first cupredoxin domain of the fungal laccases similar to Ma-LCC from Melanocarpus ...
 114-219 1.95e-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: 50.70  E-value: 1.95e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 733903985  114 GPIIKGEVGDSIVVHLKNFASRNYT-LHPHGV--KYTKENEGAfyPDNTKGfekrddAVKPGGQYTYTWDVTEdQGpakg 190
Cdd:cd13854    33 GPLIEANWGDTIEVTVINKLQDNGTsIHWHGIrqLNTNWQDGV--PGVTEC------PIAPGDTRTYRFRATQ-YG---- 99

                          90       100
                  ....*....|....*....|....*....
gi 733903985  191 dadciTRVYHSHIDAprDVASGLVGPLII 219
Cdd:cd13854   100 -----TSWYHSHYSA--QYGDGVVGPIVI 121
CuRO_3_Fet3p cd13899
The third Cupredoxin domain of multicopper oxidase Fet3p; Fet3p catalyzes the ferroxidase ...
 1008-1072 1.99e-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: 51.87  E-value: 1.99e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 733903985 1008 HTAHFHGHSFD--YKQTGIY----------------RADVFDLFPGTFQTVEMIPQNPGTWLLHCHVTDHIHAGMEATYT 1069
Cdd:cd13899    78 HPFHLHGHKFQvvQRSPDVAsddpnppinefpenpmRRDTVMVPPGGSVVIRFRADNPGVWFFHCHIEWHLEAGLAATFI 157


                  ...
gi 733903985 1070 VLP 1072
Cdd:cd13899   158 EAP 160
CuRO_1_AAO cd13845
The first cupredoxin domain of plant Ascorbate oxidase; Ascorbate oxidase catalyzes the ...
 111-219 2.08e-07

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: 50.52  E-value: 2.08e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 733903985  111 GFLGPIIKGEVGDSIVVHLKN-FASRNYTLHPHGVKytkeNEGAFYPDNTKGFEKRddAVKPGGQYTYTWDVteDQgPAk 189
Cdd:cd13845    27 QFPGPTIRATAGDTIVVELENkLPTEGVAIHWHGIR----QRGTPWADGTASVSQC--PINPGETFTYQFVV--DR-PG- 96

                          90       100       110
                  ....*....|....*....|....*....|
gi 733903985  190 gdadciTRVYHSHIDAPRdvASGLVGPLII 219
Cdd:cd13845    97 ------TYFYHGHYGMQR--SAGLYGSLIV 118
CuRO_3_MCO_like_2 cd13908
The third cupredoxin domain of uncharacterized multicopper oxidase; Multicopper Oxidases (MCOs) ...
 946-1066 2.09e-07

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


Pssm-ID: 259975 [Multi-domain]  Cd Length: 122  Bit Score: 50.91  E-value: 2.09e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 733903985  946 DENIE-TYSANPHLVDKENeeflesnkMHAINGKVFGNLHG-LTMHVGDEvswYLMAMGNEI-DIHTAHFHGHSF----- 1017
Cdd:cd13908     1 DETIDmTFEKRNAGDGGFN--------LWTINGKSYPDEDPpLVVQQGRR---YRLVFRNASdDAHPMHLHRHTFevtri 69

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*....
gi 733903985 1018 DYKQTGIYRADVFDLFPGTFQTVEMIPQNPGTWLLHCHVTDHIHAGMEA 1066
Cdd:cd13908    70 DGKPTSGLRKDVVMLGGYQRVEVDFVADNPGLTLFHCHQQLHMDYGFMA 118
PLN02191 PLN02191
L-ascorbate oxidase
 112-242 3.09e-07

L-ascorbate oxidase


Pssm-ID: 177843 [Multi-domain]  Cd Length: 574  Bit Score: 54.63  E-value: 3.09e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 733903985  112 FLGPIIKGEVGDSIVVHLKN-FASRNYTLHPHGVKytkeNEGAFYPDNTKGFEKRddAVKPGGQYTYTWDVtEDQGpakg 190
Cdd:PLN02191   51 FPGPTIDAVAGDTIVVHLTNkLTTEGLVIHWHGIR----QKGSPWADGAAGVTQC--AINPGETFTYKFTV-EKPG---- 119

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|..
gi 733903985  191 dadciTRVYHSHIDAPRdvASGLVGPLIIcrKGAMNKDNDKYVDAEFILMFS 242
Cdd:PLN02191  120 -----THFYHGHYGMQR--SAGLYGSLIV--DVAKGPKERLRYDGEFNLLLS 162
ascorbase TIGR03388
L-ascorbate oxidase, plant type; Members of this protein family are the copper-containing ...
 112-242 6.19e-07

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: 53.60  E-value: 6.19e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 733903985   112 FLGPIIKGEVGDSIVVHLKN-FASRNYTLHPHGVKytkeNEGAFYPDNTKGFEKRddAVKPGGQYTYTWdVTEDQGpakg 190
Cdd:TIGR03388   29 FPGPTIRAQAGDTIVVELTNkLHTEGVVIHWHGIR----QIGTPWADGTAGVTQC--AINPGETFIYNF-VVDRPG---- 97

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|..
gi 733903985   191 dadciTRVYHSHIDAPRdvASGLVGPLIIcRKGAMNKDNDKYvDAEFILMFS 242
Cdd:TIGR03388   98 -----TYFYHGHYGMQR--SAGLYGSLIV-DVPDGEKEPFHY-DGEFNLLLS 140
CuRO_1_2dMco_1 cd13860
The first cupredoxin domain of bacteria two domain multicopper oxidase; This subfamily ...
 114-219 6.57e-07

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


Pssm-ID: 259929 [Multi-domain]  Cd Length: 119  Bit Score: 49.12  E-value: 6.57e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 733903985  114 GPIIKGEVGDSIVVHLKNFASRNYTLHPHGVKYTKENEGAfyPDNTKgfekrdDAVKPGGQYTYTWDVTEdQGpakgdad 193
Cdd:cd13860    31 GPTIEVTEGDRVRILVTNELPEPTTVHWHGLPVPNGMDGV--PGITQ------PPIQPGETFTYEFTAKQ-AG------- 94

                          90       100
                  ....*....|....*....|....*.
gi 733903985  194 ciTRVYHSHIDAPRDVASGLVGPLII 219
Cdd:cd13860    95 --TYMYHSHVDEAKQEDMGLYGAFIV 118
CuRO_D2_2dMcoN_like cd04202
The second cupredoxin domain of bacterial two domain multicopper oxidase McoN and similar ...
 234-375 9.14e-07

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


Pssm-ID: 259865 [Multi-domain]  Cd Length: 138  Bit Score: 49.17  E-value: 9.14e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 733903985  234 DAEFILMFSvmdenlSWYLEDNirmycSEPSKVDKDDEDFqesnkmHSINGYMYGYLPNLTMCVEDKVKWHLFGMGNeaD 313
Cdd:cd04202     1 DRDYTLVLQ------EWFVDPG-----TTPMPPEGMDFNY------FTINGKSFPATPPLVVKEGDRVRIRLINLSM--D 61

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 733903985  314 IHSAYFHGQT---------LIERHHRV--DTINLFPATFIDALMIPRNPGEWLLSCQVNDHIE----GGMQALFKVE 375
Cdd:cd04202    62 HHPMHLHGHFflvtatdggPIPGSAPWpkDTLNVAPGERYDIEFVADNPGDWMFHCHKLHHAMngmgGGMMTLIGYE 138
CuRO_3_Tv-LCC_like cd13903
The third cupredoxin domain of the fungal laccases similar to Tv-LCC from Trametes Versicolor; ...
 1002-1064 1.68e-06

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: 48.82  E-value: 1.68e-06
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 733903985 1002 GNEIDIHTAHFHGHSFDYKQ---TGIY------RADVFDL-FPGTFQTVEMIPQNPGTWLLHCHVTDHIHAGM 1064
Cdd:cd13903    67 GAIGGPHPFHLHGHAFSVVRsagSNTYnyvnpvRRDVVSVgTPGDGVTIRFVTDNPGPWFLHCHIDWHLEAGL 139
Cu-oxidase_3 pfam07732
Multicopper oxidase; This entry contains many divergent copper oxidase-like domains that are ...
 466-573 1.99e-06

Multicopper oxidase; This entry contains many divergent copper oxidase-like domains that are not recognized by the pfam00394 model.


Pssm-ID: 462247 [Multi-domain]  Cd Length: 119  Bit Score: 47.63  E-value: 1.99e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 733903985   466 LLGPVIKAEVGESIRVTFRNNASRPFSIQPHGVSYLKSNE--GALYrtasrDTESPasyVSPGASFTYEWNVPEDVGptd 543
Cdd:pfam07732   24 FPGPTIRVREGDTVVVNVTNNLDEPTSIHWHGLQQRGTPWmdGVPG-----VTQCP---IPPGQSFTYRFQVKQQAG--- 92

                           90       100       110
                   ....*....|....*....|....*....|
gi 733903985   544 qdpdclTWFYYSAVDSVRdtNSGLVGPLLV 573
Cdd:pfam07732   93 ------TYWYHSHTSGQQ--AAGLAGAIII 114
CuRO_3_AAO cd13893
The third cupredoxin domain of plant Ascorbate oxidase; Ascorbate oxidase catalyzes the ...
 1003-1064 2.05e-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: 48.57  E-value: 2.05e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 733903985 1003 NEIDIHTAHFHGHSF---DYKqTGIYRA---------------DVFDLFPGTFQTVEMIPQNPGTWLLHCHVTDHIHAGM 1064
Cdd:cd13893    62 NASEQHPWHLHGHDFwvlGYG-LGGFDPaadpsslnlvnppmrNTVTIFPYGWTALRFKADNPGVWAFHCHIEWHFHMGM 140
CuRO_1_2DMCO_NIR_like cd11024
The cupredoxin domain 1 of a two-domain laccase related to nitrite reductase; The two-domain ...
 1008-1073 3.21e-06

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


Pssm-ID: 259910 [Multi-domain]  Cd Length: 119  Bit Score: 47.27  E-value: 3.21e-06
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 733903985 1008 HTAHFHGhSFDYKQTGIYRADVFdlfPGTFQTVEMIPQNPGTWLLHCHV---TDHIHAGMEATYTVLPK 1073
Cdd:cd11024    55 HTIHFHG-IHDAAMDGTGLGPIM---PGESFTYEFVAEPAGTHLYHCHVqplKEHIAMGLYGAFIVDPK 119
PLN02191 PLN02191
L-ascorbate oxidase
 1006-1064 5.46e-06

L-ascorbate oxidase


Pssm-ID: 177843 [Multi-domain]  Cd Length: 574  Bit Score: 50.40  E-value: 5.46e-06
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 733903985 1006 DIHTAHFHGHSF--------------DYKQTGIYRADVFD---LFPGTFQTVEMIPQNPGTWLLHCHVTDHIHAGM 1064
Cdd:PLN02191  465 EIHPWHLHGHDFwvlgygdgkfkpgiDEKTYNLKNPPLRNtaiLYPYGWTAIRFVTDNPGVWFFHCHIEPHLHMGM 540
CuRO_1_Diphenol_Ox cd13857
The first cupredoxin domain of fungal laccase, diphenol oxidase; Diphenol oxidase belongs to ...
 468-573 6.55e-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: 46.48  E-value: 6.55e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 733903985  468 GPVIKAEVGESIRVTFRNNASRPFSIQPHGvsyLKSNEGALYRTASRDTESPasyVSPGASFTYEWNVPEDVGptdqdpd 547
Cdd:cd13857    30 GPLIEANQGDRIVVHVTNELDEPTSIHWHG---LFQNGTNWMDGTAGITQCP---IPPGGSFTYNFTVDGQYG------- 96

                          90       100
                  ....*....|....*....|....*..
gi 733903985  548 clTWFYYSAVDSvrdTNS-GLVGPLLV 573
Cdd:cd13857    97 --TYWYHSHYST---QYAdGLVGPLIV 118
CuRO_1_Tv-LCC_like cd13856
The first cupredoxin domain of fungal laccases similar to Tv-LCC from Trametes versicolor; ...
 112-219 6.81e-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: 6.81e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 733903985  112 FLGPIIKGEVGDSIVVHLKNFAS-----RNYTLHPHGVKYTKENegafYPDNTKGFEKRddAVKPGGQYTYTWDVTEDQG 186
Cdd:cd13856    28 FPGPLITANKGDTFRITVVNQLTdptmrRSTSIHWHGIFQHGTN----YADGPAFVTQC--PIAPNHSFTYDFTAGDQAG 101

                          90       100       110
                  ....*....|....*....|....*....|...
gi 733903985  187 pakgdadciTRVYHSHIDAprDVASGLVGPLII 219
Cdd:cd13856   102 ---------TFWYHSHLST--QYCDGLRGPLVI 123
CuRO_1_CuNIR_like cd04201
Cupredoxin domain 1 of Copper-containing nitrite reductase and two-domain laccase; ...
 976-1073 1.02e-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: 45.94  E-value: 1.02e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 733903985  976 NGKVFGNLhgLTMHVGDEVSWYLMAMGNEIDIHTAHFHGHSfdyKQTGIYRADVFDlfPGTFQTVEMIPQNPGTWLLHCH 1055
Cdd:cd04201    27 DGDIPGPM--LRVREGDTVELHFSNNPSSTMPHNIDFHAAT---GAGGGAGATFIA--PGETSTFSFKATQPGLYVYHCA 99

                          90       100
                  ....*....|....*....|.
gi 733903985 1056 VTD---HIHAGMEATYTVLPK 1073
Cdd:cd04201   100 VAPvpmHIANGMYGLILVEPK 120
CuRO_1_LCC_plant cd13849
The first cupredoxin domain of plant laccases; Laccase is a blue multicopper oxidase (MCO) ...
 112-219 1.16e-05

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: 1.16e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 733903985  112 FLGPIIKGEVGDSIVVHLKNFASRNYTLHPHGVKYTKENegafYPDNTKGFEKRddAVKPGGQYTYTWDVTEDQGpakgd 191
Cdd:cd13849    26 FPGPTIRVHEGDTVVVNVTNRSPYNITIHWHGIRQLRSG----WADGPAYITQC--PIQPGQSYTYRFTVTGQEG----- 94

                          90       100
                  ....*....|....*....|....*...
gi 733903985  192 adciTRVYHSHIDAPRdvaSGLVGPLII 219
Cdd:cd13849    95 ----TLWWHAHISWLR---ATVYGAFII 115
CuRO_1_CueO_FtsP cd04232
The first Cupredoxin domain of the multicopper oxidase CueO, the cell division protein FtsP, ...
 112-219 1.63e-05

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: 45.26  E-value: 1.63e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 733903985  112 FLGPIIKGEVGDSIVVHLKNFASRNYTLHPHGVKYTKENEGAfyPDNTkgfekrddaVKPGGQYTYTWDVteDQGPAkgd 191
Cdd:cd04232    29 YLGPTIRVKKGDTVRINVTNNLDEETTVHWHGLHVPGEMDGG--PHQP---------IAPGQTWSPTFTI--DQPAA--- 92

                          90       100       110
                  ....*....|....*....|....*....|
gi 733903985  192 adciTRVYHSHIDA--PRDVASGLVGPLII 219
Cdd:cd04232    93 ----TLWYHPHTHGktAEQVYRGLAGLFII 118
CuRO_1_Tv-LCC_like cd13856
The first cupredoxin domain of fungal laccases similar to Tv-LCC from Trametes versicolor; ...
 468-573 1.89e-05

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: 45.02  E-value: 1.89e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 733903985  468 GPVIKAEVGESIRVTFRNNAS-----RPFSIQPHGVSYLKSN--EGALYRTasrdtESPasyVSPGASFTYEWNVPEDVG 540
Cdd:cd13856    30 GPLITANKGDTFRITVVNQLTdptmrRSTSIHWHGIFQHGTNyaDGPAFVT-----QCP---IAPNHSFTYDFTAGDQAG 101

                          90       100       110
                  ....*....|....*....|....*....|...
gi 733903985  541 ptdqdpdclTWFYYSAVDSvrDTNSGLVGPLLV 573
Cdd:cd13856   102 ---------TFWYHSHLST--QYCDGLRGPLVI 123
CuRO_1_2dMco_1 cd13860
The first cupredoxin domain of bacteria two domain multicopper oxidase; This subfamily ...
 468-573 2.48e-05

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


Pssm-ID: 259929 [Multi-domain]  Cd Length: 119  Bit Score: 44.49  E-value: 2.48e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 733903985  468 GPVIKAEVGESIRVTFRNNASRPFSIQPHGVSYLKSNEGalyrtASRDTESPasyVSPGASFTYEWNVpEDVGptdqdpd 547
Cdd:cd13860    31 GPTIEVTEGDRVRILVTNELPEPTTVHWHGLPVPNGMDG-----VPGITQPP---IQPGETFTYEFTA-KQAG------- 94

                          90       100
                  ....*....|....*....|....*.
gi 733903985  548 clTWFYYSAVDSVRDTNSGLVGPLLV 573
Cdd:cd13860    95 --TYMYHSHVDEAKQEDMGLYGAFIV 118
SufI COG2132
Multicopper oxidase with three cupredoxin domains (includes cell division protein FtsP and ...
 466-595 3.29e-05

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


Pssm-ID: 441735 [Multi-domain]  Cd Length: 423  Bit Score: 47.62  E-value: 3.29e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 733903985  466 LLGPVIKAEVGESIRVTFRNNASRPFSIQPHGVsylksnegalyRTASRDTESPASYVSPGASFTYEWNVPEDVGptdqd 545
Cdd:COG2132    42 YPGPTIRVREGDRVRVRVTNRLPEPTTVHWHGL-----------RVPNAMDGVPGDPIAPGETFTYEFPVPQPAG----- 105

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|..
gi 733903985  546 pdclTWFYYSAVD--SVRDTNSGLVGPLLVCRKGALLPsakqrSVTREFFLL 595
Cdd:COG2132   106 ----TYWYHPHTHgsTAEQVYRGLAGALIVEDPEEDLP-----RYDRDIPLV 148
CuRO_1_Fet3p cd13851
The first Cupredoxin domain of multicopper oxidase Fet3P; Fet3p catalyzes the ferroxidase ...
 115-219 4.11e-05

The first Cupredoxin domain of multicopper oxidase Fet3P; Fet3p catalyzes the ferroxidase reaction, which couples the oxidation of Fe(II) to Fe(III) and a four-electron reduction of molecular oxygen to water. Fet3p is a type I membrane protein with the amino-terminal oxidase domain in the exocellular space and the carboxyl terminus in the cytoplasm. The periplamic produced Fe(III) is transferred to the permease Ftr1p for import into the cytosol. The four copper ions are inserted post-translationally and are essential for catalytic activity, thus linking copper and iron homeostasis. Like other related multicopper oxidases (MCOs), Fet3p is composed of three cupredoxin domains that include one mononuclear and one trinuclear copper center. The copper ions are bound in several sites: Type 1, Type 2, and/or Type 3. The ensemble of types 2 and 3 copper is called a trinuclear cluster. MCOs oxidize their substrate by accepting electrons at a mononuclear copper center and transferring them to the active site trinuclear copper center. The cupredoxin domain 1 of 3-domain MCOs contains part the trinuclear copper binding site, which is located at the interface of domains 1 and 3.


Pssm-ID: 259920 [Multi-domain]  Cd Length: 121  Bit Score: 44.18  E-value: 4.11e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 733903985  115 PIIKGEVGDSIVVHLKN-FASRNYTLHPHGV--KYTKENEGAFY----PdntkgfekrddaVKPGGQYTYTWDVTEDQGp 187
Cdd:cd13851    32 PPIEVNKGDTVVIHATNsLGDQPTSLHFHGLfqNGTNYMDGPVGvtqcP------------IPPGQSFTYEFTVDTQVG- 98

                          90       100       110
                  ....*....|....*....|....*....|..
gi 733903985  188 akgdadciTRVYHSHIDAprDVASGLVGPLII 219
Cdd:cd13851    99 --------TYWYHSHDGG--QYPDGLRGPFII 120
CuRO_1_McoC_like cd13855
The first cupredoxin domain of a multicopper oxidase McoC and similar proteins; This family ...
 820-913 4.67e-05

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


Pssm-ID: 259924 [Multi-domain]  Cd Length: 121  Bit Score: 44.00  E-value: 4.67e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 733903985  820 QIQGPLIMSSVGDKINIVFKNLASRPYSIHAHGV----KTDSSVVAITNPGETKMYVWKISArssserdDSHCTAWAY-H 894
Cdd:cd13855    29 SVPGPLIEVFEGDTVEITFRNRLPEPTTVHWHGLpvppDQDGNPHDPVAPGNDRVYRFTLPQ-------DSAGTYWYHpH 101

                          90
                  ....*....|....*....
gi 733903985  895 STVDIIKDTYSGLIGTLVV 913
Cdd:cd13855   102 PHGHTAEQVYRGLAGAFVV 120
CuRO_1_2dMco_1 cd13860
The first cupredoxin domain of bacteria two domain multicopper oxidase; This subfamily ...
 820-913 5.02e-05

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


Pssm-ID: 259929 [Multi-domain]  Cd Length: 119  Bit Score: 43.72  E-value: 5.02e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 733903985  820 QIQGPLIMSSVGDKINIVFKNLASRPYSIHAHGVKTDSS---VVAITN----PGETKMYVWKISArssserddsHCTAWa 892
Cdd:cd13860    28 SVPGPTIEVTEGDRVRILVTNELPEPTTVHWHGLPVPNGmdgVPGITQppiqPGETFTYEFTAKQ---------AGTYM- 97

                          90       100
                  ....*....|....*....|.
gi 733903985  893 YHSTVDIIKDTYSGLIGTLVV 913
Cdd:cd13860    98 YHSHVDEAKQEDMGLYGAFIV 118
CuRO_1_2DMCO_NIR_like cd11024
The cupredoxin domain 1 of a two-domain laccase related to nitrite reductase; The two-domain ...
 820-874 5.57e-05

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


Pssm-ID: 259910 [Multi-domain]  Cd Length: 119  Bit Score: 43.80  E-value: 5.57e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 733903985  820 QIQGPLIMSSVGDKINIVFKNLASRPYSIHAHGV---KTDSSVVAITNPGETKMYVWK 874
Cdd:cd11024    29 TVPGPTLRATEGDLVRIHFINTGDHPHTIHFHGIhdaAMDGTGLGPIMPGESFTYEFV 86
CuRO_D1_2dMcoN_like cd13859
The first cupredoxin domain of bacterial two domain multicopper oxidase McoN and similar ...
 820-913 7.86e-05

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


Pssm-ID: 259928 [Multi-domain]  Cd Length: 122  Bit Score: 43.24  E-value: 7.86e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 733903985  820 QIQGPLIMSSVGDKINIVFKNLASRPYSIHAHGV-KTDS----SVVAITN----PGETKMYVWKIsarssserdDSHCTA 890
Cdd:cd13859    28 QVPGPLIHVKEGDDLVVHVTNNTTLPHTIHWHGVlQMGSwkmdGVPGVTQpaiePGESFTYKFKA---------ERPGTL 98

                          90       100
                  ....*....|....*....|....
gi 733903985  891 WaYHSTVDIIK-DTYSGLIGTLVV 913
Cdd:cd13859    99 W-YHCHVNVNEhVGMRGMWGPLIV 121
CuRO_1_Diphenol_Ox cd13857
The first cupredoxin domain of fungal laccase, diphenol oxidase; Diphenol oxidase belongs to ...
 820-913 9.11e-05

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


Pssm-ID: 259926 [Multi-domain]  Cd Length: 119  Bit Score: 43.02  E-value: 9.11e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 733903985  820 QIQGPLIMSSVGDKINIVFKNLASRPYSIHAHGVKTDSS-----VVAITN----PGETKMYVWKIsarssserDDSHCTA 890
Cdd:cd13857    27 QFPGPLIEANQGDRIVVHVTNELDEPTSIHWHGLFQNGTnwmdgTAGITQcpipPGGSFTYNFTV--------DGQYGTY 98

                          90       100
                  ....*....|....*....|....
gi 733903985  891 WaYHSTVDIikdTYS-GLIGTLVV 913
Cdd:cd13857    99 W-YHSHYST---QYAdGLVGPLIV 118
CuRO_1_McoC_like cd13855
The first cupredoxin domain of a multicopper oxidase McoC and similar proteins; This family ...
 465-538 2.07e-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: 42.08  E-value: 2.07e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 733903985  465 GLLGPVIKAEVGESIRVTFRNNASRPFSIQPHGVSYLKSNEGalyrtasrdteSPASYVSPGASFTYEWNVPED 538
Cdd:cd13855    29 SVPGPLIEVFEGDTVEITFRNRLPEPTTVHWHGLPVPPDQDG-----------NPHDPVAPGNDRVYRFTLPQD 91
CuRO_1_CuNIR cd11020
Cupredoxin domain 1 of Copper-containing nitrite reductase; Copper-containing nitrite ...
 820-916 2.31e-04

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


Pssm-ID: 259906 [Multi-domain]  Cd Length: 119  Bit Score: 41.81  E-value: 2.31e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 733903985  820 QIQGPLIMSSVGDKINIVFKNLASR--PYSIHAHGVKTDSSVVAIT-NPGETKMYVWKisARssserddsHCTAWAYH-S 895
Cdd:cd11020    29 QVPGPVIRVREGDTVELTLTNPGTNtmPHSIDFHAATGPGGGEFTTiAPGETKTFSFK--AL--------YPGVFMYHcA 98

                          90       100
                  ....*....|....*....|.
gi 733903985  896 TVDIIKDTYSGLIGTLVVCPR 916
Cdd:cd11020    99 TAPVLMHIANGMYGAIIVEPK 119
CuRO_3_LCC_plant cd13897
The third cupredoxin domain of the plant laccases; Laccase is a blue multicopper oxidase (MCO) ...
 1006-1070 2.38e-04

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: 42.25  E-value: 2.38e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 733903985 1006 DIHTAHFHGHSFdY---KQTGIYRA--DV--FDLF-PGTFQTVeMIPQ-----------NPGTWLLHCHVTDHIHAGMEA 1066
Cdd:cd13897    55 ENHPMHLHGFDF-YvvgRGFGNFDPstDPatFNLVdPPLRNTV-GVPRggwaairfvadNPGVWFMHCHFERHTSWGMAT 132


                  ....
gi 733903985 1067 TYTV 1070
Cdd:cd13897   133 VFIV 136
CuRO_3_tcLLC2_insect_like cd13905
The third cupredoxin domain of the insect laccases similar to laccase 2 in Tribolium castaneum; ...
 991-1065 2.54e-04

The third cupredoxin domain of the insect laccases similar to laccase 2 in Tribolium castaneum; This multicopper oxidase (MCO) family includes the majority of insect laccases. One member of the family is laccase 2 from Tribolium castaneum. Laccase 2 is required for beetle cuticle tanning. Laccase (polyphenol oxidase EC 1.10.3.2) is a blue multi-copper enzyme that catalyzes the oxidation of a variety of organic substrates coupled to the reduction of molecular oxygen to water. It displays broad substrate specificity, catalyzing the oxidation of a wide variety of aromatic - notably phenolic and inorganic substances. Laccase has been implicated in a wide spectrum of biological activities and, in particular, plays a key role in morphogenesis, development and lignin metabolism in fungi, plants and insects. Although MCOs have diverse functions, majority of them have three cupredoxin domain repeats that include one mononuclear and one trinuclear copper center. The copper ions are bound in several sites: Type 1, Type 2, and/or Type 3. The ensemble of types 2 and 3 copper is called a trinuclear cluster. MCOs oxidize their substrate by accepting electrons at a mononuclear copper center and transferring them to the active site trinuclear copper center. The cupredoxin domain 3 of 3-domain MCOs contains the Type 1 (T1) copper binding site and part the trinuclear copper binding site, which is located at the interface of domains 1 and 3.


Pssm-ID: 259972 [Multi-domain]  Cd Length: 174  Bit Score: 43.05  E-value: 2.54e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 733903985  991 GDEVSWYLMAMGNEIDI-HTAHFHGHSF--------DY-KQTGIYRA--------DVFDLFPGTFQ------TVeMIP-- 1044
Cdd:cd13905    52 NSVVEIVLINEGPGPGLsHPFHLHGHSFyvlgmgfpGYnSTTGEILSqnwnnkllDRGGLPGRNLVnpplkdTV-VVPng 130

                          90       100       110
                  ....*....|....*....|....*....|
gi 733903985 1045 ---------QNPGTWLLHCHVTDHIHAGME 1065
Cdd:cd13905   131 gyvvirfraDNPGYWLLHCHIEFHLLEGMA 160
Cu-oxidase_2 pfam07731
Multicopper oxidase; This entry contains many divergent copper oxidase-like domains that are ...
 272-375 2.84e-04

Multicopper oxidase; This entry contains many divergent copper oxidase-like domains that are not recognized by the pfam00394 model.


Pssm-ID: 462246 [Multi-domain]  Cd Length: 138  Bit Score: 42.04  E-value: 2.84e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 733903985   272 DFQESNKMHSINGYMYGYLPN-LTMCVEDKVKWHLFGMGNeaDIHSAYFHGQT--LIERHH-----------------RV 331
Cdd:pfam07731   14 SGNFRRNDWAINGLLFPPNTNvITLPYGTVVEWVLQNTTT--GVHPFHLHGHSfqVLGRGGgpwpeedpktynlvdpvRR 91

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....
gi 733903985   332 DTINLFPATFIDALMIPRNPGEWLLSCQVNDHIEGGMQALFKVE 375
Cdd:pfam07731   92 DTVQVPPGGWVAIRFRADNPGVWLFHCHILWHLDQGMMGQFVVR 135
CuRO_3_Tth-MCO_like cd13900
The third cupredoxin domain of the bacterial laccases similar to Tth-MCO from Thermus ...
 975-1064 6.13e-04

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: 40.69  E-value: 6.13e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 733903985  975 INGKVFG-NLHGLTMHVGDEVSWYLMAMGNEIdiHTAHFHGHSF-------DYKQTGIYRaDVFDLFPGTFQTVEMIPQN 1046
Cdd:cd13900    22 INGKPFDpDRPDRTVRLGTVEEWTLINTSGED--HPFHIHVNPFqvvsingKPGLPPVWR-DTVNVPAGGSVTIRTRFRD 98

                          90
                  ....*....|....*....
gi 733903985 1047 P-GTWLLHCHVTDHIHAGM 1064
Cdd:cd13900    99 FtGEFVLHCHILDHEDQGM 117
CuRO_1_MaLCC_like cd13854
The first cupredoxin domain of the fungal laccases similar to Ma-LCC from Melanocarpus ...
 820-913 6.57e-04

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


Pssm-ID: 259923 [Multi-domain]  Cd Length: 122  Bit Score: 40.69  E-value: 6.57e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 733903985  820 QIQGPLIMSSVGDKINI-VFKNLASRPYSIHAHGVK-----TDSSVVAITN----PGETKMYVWKIsarssserdDSHCT 889
Cdd:cd13854    30 QYPGPLIEANWGDTIEVtVINKLQDNGTSIHWHGIRqlntnWQDGVPGVTEcpiaPGDTRTYRFRA---------TQYGT 100

                          90       100
                  ....*....|....*....|....*
gi 733903985  890 AWaYHSTVDIikdTYS-GLIGTLVV 913
Cdd:cd13854   101 SW-YHSHYSA---QYGdGVVGPIVI 121
Cu-oxidase pfam00394
Multicopper oxidase; Many of the proteins in this family contain multiple similar copies of ...
 936-1068 7.76e-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: 41.15  E-value: 7.76e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 733903985   936 VFDENESWYlDENIETYSANPHLVDKENEEF-LESNKmHAINGKVFGNLHGLTMHVGDEVSWYLmAMGNEIDIHTAHFHG 1014
Cdd:pfam00394    3 YVITLSDWY-HKDAKDLEKELLASGKAPTDFpPVPDA-VLINGKDGASLATLTVTPGKTYRLRI-INVALDDSLNFSIEG 79

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 733903985  1015 HSF-----DYKQTGIYRADVFDLFPGTFQTVeMI--PQNPGTWLLHCHVT-DHIHAGMEATY 1068
Cdd:pfam00394   80 HKMtvvevDGVYVNPFTVDSLDIFPGQRYSV-LVtaNQDPGNYWIVASPNiPAFDNGTAAAI 140
CuRO_D1_2dMcoN_like cd13859
The first cupredoxin domain of bacterial two domain multicopper oxidase McoN and similar ...
 468-573 8.78e-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: 40.15  E-value: 8.78e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 733903985  468 GPVIKAEVGESIRVTFRNNASRPFSIQPHGVSYLKS--NEGAlyrtasRDTESPAsyVSPGASFTYEWNVpedvgptdqD 545
Cdd:cd13859    31 GPLIHVKEGDDLVVHVTNNTTLPHTIHWHGVLQMGSwkMDGV------PGVTQPA--IEPGESFTYKFKA---------E 93

                          90       100
                  ....*....|....*....|....*...
gi 733903985  546 PDCLTWFYYSAVDSVRDTNSGLVGPLLV 573
Cdd:cd13859    94 RPGTLWYHCHVNVNEHVGMRGMWGPLIV 121
Cupredoxin cd00920
Cupredoxin superfamily; Cupredoxins contain type I copper centers and are involved in ...
 976-1067 1.79e-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: 39.14  E-value: 1.79e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 733903985  976 NGKVFGNLHgLTMHVGDEVSWYLMAMGNEIdiHTAHFHGHSFDY-KQTGIYRAD-VFDLFPGTFQTVEMI--PQNPGTWL 1051
Cdd:cd00920    16 GVLLFGPPV-LVVPVGDTVRVQFVNKLGEN--HSVTIAGFGVPVvAMAGGANPGlVNTLVIGPGESAEVTftTDQAGVYW 92

                          90
                  ....*....|....*.
gi 733903985 1052 LHCHVTDHIHAGMEAT 1067
Cdd:cd00920    93 FYCTIPGHNHAGMVGT 108
CuRO_3_MCO_like_4 cd13910
The third cupredoxin domain of uncharacterized multicopper oxidase; Multicopper Oxidases (MCOs) ...
 1008-1064 2.84e-03

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


Pssm-ID: 259977 [Multi-domain]  Cd Length: 166  Bit Score: 39.59  E-value: 2.84e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 733903985 1008 HTAHFHGHSF-------DYKQTGIYRADVFDLFPGTFQ----TVEmIPQ-----------NPGTWLLHCHVTDHIHAGM 1064
Cdd:cd13910    83 HPFHLHGHKFwvlgsgdGRYGGGGYTAPDGTSLNTTNPlrrdTVS-VPGfgwavlrfvadNPGLWAFHCHILWHMAAGM 160
SufI COG2132
Multicopper oxidase with three cupredoxin domains (includes cell division protein FtsP and ...
 823-913 3.01e-03

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: 41.46  E-value: 3.01e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 733903985  823 GPLIMSSVGDKINIVFKNLASRPYSIHAHGVKTDSS----VVAITNPGETKMYVWKIsarssserDDSHCTAWaYHSTVD 898
Cdd:COG2132    44 GPTIRVREGDRVRVRVTNRLPEPTTVHWHGLRVPNAmdgvPGDPIAPGETFTYEFPV--------PQPAGTYW-YHPHTH 114

                          90
                  ....*....|....*..
gi 733903985  899 II--KDTYSGLIGTLVV 913
Cdd:COG2132   115 GStaEQVYRGLAGALIV 131
CuRO_1_McoC_like cd13855
The first cupredoxin domain of a multicopper oxidase McoC and similar proteins; This family ...
 114-219 3.11e-03

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: 38.61  E-value: 3.11e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 733903985  114 GPIIKGEVGDSIVVHLKNFASRNYTLHPHGVKYTKENEGafypdntkgfeKRDDAVKPGGQYTYTWDVTEDQGPakgdad 193
Cdd:cd13855    32 GPLIEVFEGDTVEITFRNRLPEPTTVHWHGLPVPPDQDG-----------NPHDPVAPGNDRVYRFTLPQDSAG------ 94

                          90       100
                  ....*....|....*....|....*...
gi 733903985  194 ciTRVY--HSHIDAPRDVASGLVGPLII 219
Cdd:cd13855    95 --TYWYhpHPHGHTAEQVYRGLAGAFVV 120
CuRO_1_Fet3p cd13851
The first Cupredoxin domain of multicopper oxidase Fet3P; Fet3p catalyzes the ferroxidase ...
 469-573 3.14e-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: 3.14e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 733903985  469 PVIKAEVGESIRVTFRNN-ASRPFSIQPHGVSYLKSNEgalYRTASRDTESPasyVSPGASFTYEWNVPEDVGptdqdpd 547
Cdd:cd13851    32 PPIEVNKGDTVVIHATNSlGDQPTSLHFHGLFQNGTNY---MDGPVGVTQCP---IPPGQSFTYEFTVDTQVG------- 98

                          90       100
                  ....*....|....*....|....*.
gi 733903985  548 clTWFYYSAVDSvrDTNSGLVGPLLV 573
Cdd:cd13851    99 --TYWYHSHDGG--QYPDGLRGPFII 120
CuRO_1_CumA_like cd13861
The first cupredoxin domain of CumA like multicopper oxidase; This multicopper oxidase (MCO) ...
 820-913 3.15e-03

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: 38.75  E-value: 3.15e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 733903985  820 QIQGPLIMSSVGDKINIVFKNLASRPYSIHAHGVKTDSS---VVAIT----NPGETKMYVWKIsarssserDDSHcTAWa 892
Cdd:cd13861    28 QVPGPELRVRQGDTLRVRLTNRLPEPTTIHWHGLRLPNAmdgVPGLTqppvPPGESFTYEFTP--------PDAG-TYW- 97

                          90       100
                  ....*....|....*....|.
gi 733903985  893 YHSTVDIIKDTYSGLIGTLVV 913
Cdd:cd13861    98 YHPHVGSQEQLDRGLYGPLIV 118
Cu-oxidase_3 pfam07732
Multicopper oxidase; This entry contains many divergent copper oxidase-like domains that are ...
 820-895 3.37e-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: 38.38  E-value: 3.37e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 733903985   820 QIQGPLIMSSVGDKINIVFKNLASRPYSIHAHGVKTDSS-----VVAITN----PGETKMYVWKIsarssserDDSHCTA 890
Cdd:pfam07732   23 QFPGPTIRVREGDTVVVNVTNNLDEPTSIHWHGLQQRGTpwmdgVPGVTQcpipPGQSFTYRFQV--------KQQAGTY 94


                   ....*
gi 733903985   891 WaYHS 895
Cdd:pfam07732   95 W-YHS 98
ascorbOXfungal TIGR03390
L-ascorbate oxidase, fungal type; This model describes a family of fungal ascorbate oxidases, ...
 1025-1075 3.45e-03

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: 41.37  E-value: 3.45e-03
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|.
gi 733903985  1025 YRADVFDLFPGTFQTVEMIPQNPGTWLLHCHVTDHIHAGMEATYTVLPKED 1075
Cdd:TIGR03390  486 YAVKVVPGAPAGWRAWRIRVTNPGVWMMHCHILQHMVMGMQTVWVFGDAED 536
CuRO_3_Abr2_like cd13898
The third cupredoxin domain of a group of fungal Laccases similar to Abr2 from Aspergillus ...
 1045-1064 3.87e-03

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


Pssm-ID: 259965 [Multi-domain]  Cd Length: 164  Bit Score: 39.16  E-value: 3.87e-03
                          10        20
                  ....*....|....*....|
gi 733903985 1045 QNPGTWLLHCHVTDHIHAGM 1064
Cdd:cd13898   138 VNPGAWLLHCHIQSHLAGGM 157
CuRO_3_AAO_like_2 cd13895
The third cupredoxin domain of Ascorbate oxidase homologs; This family includes fungal ...
 1006-1067 4.86e-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: 39.22  E-value: 4.86e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 733903985 1006 DIHTAHFHG-HSFDYKQ-TGIYRADVFD-----------------LFPGTFQTVEMIP-------------QNPGTWLLH 1053
Cdd:cd13895    91 DAHPWHAHGaHYYDLGSgLGTYSATALAneeklrgynpirrdttmLYRYGGKGYYPPPgtgsgwrawrlrvDDPGVWMLH 170

                          90
                  ....*....|....
gi 733903985 1054 CHVTDHIHAGMEAT 1067
Cdd:cd13895   171 CHILQHMIMGMQTV 184
CuRO_1_Abr2_like cd13850
The first cupredoxin domain of a group of fungal Laccases similar to Abr2 from Aspergillus ...
 820-913 5.27e-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: 38.05  E-value: 5.27e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 733903985  820 QIQGPLIMSSVGDKINIVFKNLASRPYSIHAHGVKTDSS-----VVAITN----PGETKMYVWKIsarssserDDSHCTA 890
Cdd:cd13850    25 QFPGPPIILDEGDEVEILVTNNLPVNTTIHFHGILQRGTpwsdgVPGVTQwpiqPGGSFTYRWKA--------EDQYGLY 96

                          90       100
                  ....*....|....*....|....
gi 733903985  891 WaYHSTvdiIKDTYS-GLIGTLVV 913
Cdd:cd13850    97 W-YHSH---YRGYYMdGLYGPIYI 116
CuRO_1_AAO cd13845
The first cupredoxin domain of plant Ascorbate oxidase; Ascorbate oxidase catalyzes the ...
 468-573 5.93e-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: 37.81  E-value: 5.93e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 733903985  468 GPVIKAEVGESIRVTFRNN-ASRPFSIQPHGVSYLKS--NEGALYRtasrdTESPasyVSPGASFTYEWNVpedvgptDQ 544
Cdd:cd13845    30 GPTIRATAGDTIVVELENKlPTEGVAIHWHGIRQRGTpwADGTASV-----SQCP---INPGETFTYQFVV-------DR 94

                          90       100
                  ....*....|....*....|....*....
gi 733903985  545 DPdclTWFYYSAVDSVRdtNSGLVGPLLV 573
Cdd:cd13845    95 PG---TYFYHGHYGMQR--SAGLYGSLIV 118
PLN02604 PLN02604
oxidoreductase
 1003-1068 7.13e-03

oxidoreductase


Pssm-ID: 215324 [Multi-domain]  Cd Length: 566  Bit Score: 40.23  E-value: 7.13e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 733903985 1003 NEIDIHTAHFHGHsfDYKQTGiYRADVFDLF--PGTFQTVEMIPQN------------------PGTWLLHCHVTDHIHA 1062
Cdd:PLN02604  462 NNSETHPWHLHGH--DFWVLG-YGEGKFNMSsdPKKYNLVDPIMKNtvpvhpygwtalrfradnPGVWAFHCHIESHFFM 538


                  ....*.
gi 733903985 1063 GMEATY 1068
Cdd:PLN02604  539 GMGVVF 544
CuRO_1_LCC_plant cd13849
The first cupredoxin domain of plant laccases; Laccase is a blue multicopper oxidase (MCO) ...
 468-540 9.47e-03

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


Pssm-ID: 259918 [Multi-domain]  Cd Length: 117  Bit Score: 37.24  E-value: 9.47e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 733903985  468 GPVIKAEVGESIRVTFRNNASRPFSIQPHGVSYLKSN--EGALYRtasrdTESPasyVSPGASFTYEWNVPEDVG 540
Cdd:cd13849    28 GPTIRVHEGDTVVVNVTNRSPYNITIHWHGIRQLRSGwaDGPAYI-----TQCP---IQPGQSYTYRFTVTGQEG 94
 
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.
Help | Disclaimer | Write to the Help Desk
NCBI | NLM | NIH