NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|1776487195|ref|XP_031410897|]
View 

ceruloplasmin isoform X2 [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 ...
 381-579 2.43e-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: 2.43e-124
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776487195  381 TKIRQYFIAAEEIIWNYGPSAFNHFTGQELIA-DSESSVFFERSETRIGGSYKKAIYKEYTDGTFTAHKKRLPEEEHLGL 459
Cdd:cd04224      1 GKVRHYFIAAEEIMWDYAPSGKNLFTGQNLTApGSDSEVFFQRNETRIGGTYWKVRYVEYTDATFTTRKHRSKEEEHLGI 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776487195  460 LGPVIKAEVGESIRVTFRNNASRPFSIQPHGVSYLKSNEGALYRtasRDTESPASYVSPGASFTYEWNVPEDVGPTDQDP 539
Cdd:cd04224     81 LGPVIRAEVGDTIKVTFRNKASRPFSIQPHGVFYEKNYEGAMYR---DGDPSPGSHVSPGETFTYEWTVPEGVGPTNQDP 157

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|
gi 1776487195  540 DCLTWFYYSAVDSVRDTNSGLVGPLLVCRKGALLPSAKQR 579
Cdd:cd04224    158 PCLTYLYFSAVDPVRDTNSGLVGPLLVCKKGSLNANGRQK 197
CuRO_1_ceruloplasmin cd04222
The first cupredoxin domain of Ceruloplasmin; Ceruloplasmin is a multicopper oxidase essential ...
 33-215 2.30e-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: 2.30e-122
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776487195   33 REYYIGIVETAWDYAPGSTDIISGQRFAEEEQAEVFLKRGPQRIGSIYKKAVYTQYTNILYDVIVEKPSWLGFLGPIIKG 112
Cdd:cd04222      1 REYYIGIRETQWDYAPSGKNLITNQTFDDDEHASVFLKRGPDRIGRVYKKAVYLQYTDDTYRTEIEKPVWLGFLGPILKA 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776487195  113 EVGDSIVVHLKNFASRNYTLHPHGVKYTKENEGAFYPDNTKGFEKRDDAVKPGGQYTYTWDVTEDQGPAKGDADCITRVY 192
Cdd:cd04222     81 EVGDVIVVHLKNFASRPYSLHPHGVFYNKENEGALYPDNTSGFEKADDAVPPGGSYTYTWTVPEEQAPTKADANCLTRIY 160

                          170       180
                   ....*....|....*....|...
gi 1776487195  193 HSHIDAPRDVASGLVGPLIICRK 215
Cdd:cd04222    161 HSHIDAPKDIASGLIGPLIICKK 183
CuRO_5_ceruloplasmin cd04225
The fifth cupredoxin domain of Ceruloplasmin; Ceruloplasmin is a multicopper oxidase essential ...
 739-909 3.70e-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: 3.70e-108
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776487195  739 KTHYIAAVEVEWDYSPNRTWEFERHQFHKESPGNSFLNKEDAFIGSKYKKVVYREYTDQTFSTPKSRAEEEQHLQIQGPL 818
Cdd:cd04225      1 RTYYIAAEEVEWDYSPQRTWEQELHNTHEESPGNAFLNKGDKFIGSKYKKVVYREYTDDTFSVPKERTAEEEHLGILGPL 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776487195  819 IMSSVGDKINIVFKNLASRPYSIHAHGVKTDSSVVAITNPGETKMYVWKISARSSSERDDSHCTAWAYHSTVDIIKDTYS 898
Cdd:cd04225     81 IHAEVGEKVKIVFKNMASRPYSIHAHGVKTDSSWVAPTEPGETQTYTWKIPERSGPGVEDSNCISWAYYSTVDQIKDLYS 160

                          170
                   ....*....|.
gi 1776487195  899 GLIGTLVVCPR 909
Cdd:cd04225    161 GLIGPLVICRR 171
CuRO_6_ceruloplasmin cd11012
The sixth cupredoxin domain of Ceruloplasmin; Ceruloplasmin is a multicopper oxidase essential ...
 920-1064 7.10e-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: 7.10e-96
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776487195  920 KVHFALLFMVFDENESWYLDENIETYSANPHLVDKENEEFLESNKMHAINGKVFGNLHGLTMHVGDEVSWYLMAMGNEID 999
Cdd:cd11012      1 KLEFALLFLVFDENESWYLDENIKTYSDHPEKVNKEDEEFIESNKMHAINGKVFGNLQGLTMHVGDEVYWYLMGMGNEID 80

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1776487195 1000 IHTAHFHGHSFDYKQTGIYRADVFDLFPGTFQTVEMIPQNPGTWLLHCHVTDHIHAGMEATYTVL 1064
Cdd:cd11012     81 IHTAHFHGHSFDYKHRGVYRSDVFDLFPGTFQTVEMIPRTPGTWLLHCHVTDHIHAGMETTYTVL 145
CuRO_2_ceruloplasmin cd11021
The second cupredoxin domain of Ceruloplasmin; Ceruloplasmin is a multicopper oxidase ...
 227-367 9.65e-96

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: 300.16  E-value: 9.65e-96
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776487195  227 DAEFILMFSVMDENLSWYLEDNIRMYCSEPSKVDKDDEDFQESNKMHSINGYMYGYLPNLTMCVEDKVKWHLFGMGNEAD 306
Cdd:cd11021      1 DREFVLMFSVVDENLSWYLDENIKTYCSEPAKVDKDDEDFQESNKMHSINGYTFGNLPGLSMCAGDRVKWHLFGMGNEVD 80

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1776487195  307 IHSAYFHGQTLIERHHRVDTINLFPATFIDALMIPRNPGEWLLSCQVNDHIEGGMQALFKV 367
Cdd:cd11021     81 IHSAFFHGQTLTDRGHRTDTINLFPATFVTAEMVAQNPGKWLLSCQVNDHLKAGMQAFYEV 141
CuRO_4_ceruloplasmin cd11022
The fourth cupredoxin domain of Ceruloplasmin; Ceruloplasmin is a multicopper oxidase ...
 582-725 1.48e-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: 1.48e-95
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776487195  582 TREFFLLATVFDENLSWYLDDNILMFTLNPNEIDKDNEDFQESNKMHSINGYMYGNQPGLEMCKGDVISWHLMGLGSEVD 661
Cdd:cd11022      1 DKEFFLLFTVFDENESWYLDENIQQFTLDPRSVDKEDEDFQESNKMHSINGYMYGNQPGLDMCKGDTVSWHLFGLGTETD 80

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1776487195  662 VHGIYFSQNTFITKGTRKDTANLFPHTFVTAIMKPDSEGIFEVSCLTTDHHRGGMKQKYKVKPC 725
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 ...
 381-579 2.43e-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: 2.43e-124
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776487195  381 TKIRQYFIAAEEIIWNYGPSAFNHFTGQELIA-DSESSVFFERSETRIGGSYKKAIYKEYTDGTFTAHKKRLPEEEHLGL 459
Cdd:cd04224      1 GKVRHYFIAAEEIMWDYAPSGKNLFTGQNLTApGSDSEVFFQRNETRIGGTYWKVRYVEYTDATFTTRKHRSKEEEHLGI 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776487195  460 LGPVIKAEVGESIRVTFRNNASRPFSIQPHGVSYLKSNEGALYRtasRDTESPASYVSPGASFTYEWNVPEDVGPTDQDP 539
Cdd:cd04224     81 LGPVIRAEVGDTIKVTFRNKASRPFSIQPHGVFYEKNYEGAMYR---DGDPSPGSHVSPGETFTYEWTVPEGVGPTNQDP 157

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|
gi 1776487195  540 DCLTWFYYSAVDSVRDTNSGLVGPLLVCRKGALLPSAKQR 579
Cdd:cd04224    158 PCLTYLYFSAVDPVRDTNSGLVGPLLVCKKGSLNANGRQK 197
CuRO_1_ceruloplasmin cd04222
The first cupredoxin domain of Ceruloplasmin; Ceruloplasmin is a multicopper oxidase essential ...
 33-215 2.30e-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: 2.30e-122
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776487195   33 REYYIGIVETAWDYAPGSTDIISGQRFAEEEQAEVFLKRGPQRIGSIYKKAVYTQYTNILYDVIVEKPSWLGFLGPIIKG 112
Cdd:cd04222      1 REYYIGIRETQWDYAPSGKNLITNQTFDDDEHASVFLKRGPDRIGRVYKKAVYLQYTDDTYRTEIEKPVWLGFLGPILKA 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776487195  113 EVGDSIVVHLKNFASRNYTLHPHGVKYTKENEGAFYPDNTKGFEKRDDAVKPGGQYTYTWDVTEDQGPAKGDADCITRVY 192
Cdd:cd04222     81 EVGDVIVVHLKNFASRPYSLHPHGVFYNKENEGALYPDNTSGFEKADDAVPPGGSYTYTWTVPEEQAPTKADANCLTRIY 160

                          170       180
                   ....*....|....*....|...
gi 1776487195  193 HSHIDAPRDVASGLVGPLIICRK 215
Cdd:cd04222    161 HSHIDAPKDIASGLIGPLIICKK 183
CuRO_5_ceruloplasmin cd04225
The fifth cupredoxin domain of Ceruloplasmin; Ceruloplasmin is a multicopper oxidase essential ...
 739-909 3.70e-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: 3.70e-108
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776487195  739 KTHYIAAVEVEWDYSPNRTWEFERHQFHKESPGNSFLNKEDAFIGSKYKKVVYREYTDQTFSTPKSRAEEEQHLQIQGPL 818
Cdd:cd04225      1 RTYYIAAEEVEWDYSPQRTWEQELHNTHEESPGNAFLNKGDKFIGSKYKKVVYREYTDDTFSVPKERTAEEEHLGILGPL 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776487195  819 IMSSVGDKINIVFKNLASRPYSIHAHGVKTDSSVVAITNPGETKMYVWKISARSSSERDDSHCTAWAYHSTVDIIKDTYS 898
Cdd:cd04225     81 IHAEVGEKVKIVFKNMASRPYSIHAHGVKTDSSWVAPTEPGETQTYTWKIPERSGPGVEDSNCISWAYYSTVDQIKDLYS 160

                          170
                   ....*....|.
gi 1776487195  899 GLIGTLVVCPR 909
Cdd:cd04225    161 GLIGPLVICRR 171
CuRO_6_ceruloplasmin cd11012
The sixth cupredoxin domain of Ceruloplasmin; Ceruloplasmin is a multicopper oxidase essential ...
 920-1064 7.10e-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: 7.10e-96
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776487195  920 KVHFALLFMVFDENESWYLDENIETYSANPHLVDKENEEFLESNKMHAINGKVFGNLHGLTMHVGDEVSWYLMAMGNEID 999
Cdd:cd11012      1 KLEFALLFLVFDENESWYLDENIKTYSDHPEKVNKEDEEFIESNKMHAINGKVFGNLQGLTMHVGDEVYWYLMGMGNEID 80

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1776487195 1000 IHTAHFHGHSFDYKQTGIYRADVFDLFPGTFQTVEMIPQNPGTWLLHCHVTDHIHAGMEATYTVL 1064
Cdd:cd11012     81 IHTAHFHGHSFDYKHRGVYRSDVFDLFPGTFQTVEMIPRTPGTWLLHCHVTDHIHAGMETTYTVL 145
CuRO_2_ceruloplasmin cd11021
The second cupredoxin domain of Ceruloplasmin; Ceruloplasmin is a multicopper oxidase ...
 227-367 9.65e-96

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: 300.16  E-value: 9.65e-96
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776487195  227 DAEFILMFSVMDENLSWYLEDNIRMYCSEPSKVDKDDEDFQESNKMHSINGYMYGYLPNLTMCVEDKVKWHLFGMGNEAD 306
Cdd:cd11021      1 DREFVLMFSVVDENLSWYLDENIKTYCSEPAKVDKDDEDFQESNKMHSINGYTFGNLPGLSMCAGDRVKWHLFGMGNEVD 80

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1776487195  307 IHSAYFHGQTLIERHHRVDTINLFPATFIDALMIPRNPGEWLLSCQVNDHIEGGMQALFKV 367
Cdd:cd11021     81 IHSAFFHGQTLTDRGHRTDTINLFPATFVTAEMVAQNPGKWLLSCQVNDHLKAGMQAFYEV 141
CuRO_4_ceruloplasmin cd11022
The fourth cupredoxin domain of Ceruloplasmin; Ceruloplasmin is a multicopper oxidase ...
 582-725 1.48e-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: 1.48e-95
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776487195  582 TREFFLLATVFDENLSWYLDDNILMFTLNPNEIDKDNEDFQESNKMHSINGYMYGNQPGLEMCKGDVISWHLMGLGSEVD 661
Cdd:cd11022      1 DKEFFLLFTVFDENESWYLDENIQQFTLDPRSVDKEDEDFQESNKMHSINGYMYGNQPGLDMCKGDTVSWHLFGLGTETD 80

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1776487195  662 VHGIYFSQNTFITKGTRKDTANLFPHTFVTAIMKPDSEGIFEVSCLTTDHHRGGMKQKYKVKPC 725
Cdd:cd11022     81 VHGIYFSGNTFLLQGTRRDTANLFPHTSVTAIMQPDNEGTFEVNCQTTDHYSAGMRQIYTVSQC 144
Cu-oxidase_2 pfam07731
Multicopper oxidase; This entry contains many divergent copper oxidase-like domains that are ...
 963-1067 5.81e-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: 84.41  E-value: 5.81e-19
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776487195  963 NKMHAINGKVFG-NLHGLTMHVGDEVSWYLMamGNEIDIHTAHFHGHSFDYKQTGI----------------YRADVFDL 1025
Cdd:pfam07731   19 RNDWAINGLLFPpNTNVITLPYGTVVEWVLQ--NTTTGVHPFHLHGHSFQVLGRGGgpwpeedpktynlvdpVRRDTVQV 96

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|..
gi 1776487195 1026 FPGTFQTVEMIPQNPGTWLLHCHVTDHIHAGMEATYTVLPKE 1067
Cdd:pfam07731   97 PPGGWVAIRFRADNPGVWLFHCHILWHLDQGMMGQFVVRPGD 138
Cu-oxidase_3 pfam07732
Multicopper oxidase; This entry contains many divergent copper oxidase-like domains that are ...
 87-212 1.77e-12

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


Pssm-ID: 462247 [Multi-domain]  Cd Length: 119  Bit Score: 64.96  E-value: 1.77e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776487195   87 QYTNILYDVIVEKPSWL---GFLGPIIKGEVGDSIVVHLKNFASRNYTLHPHGVKYTKENEGAFYPDNTKgfekrdDAVK 163
Cdd:pfam07732    3 TYGTVSPLGGTRQAVIGvngQFPGPTIRVREGDTVVVNVTNNLDEPTSIHWHGLQQRGTPWMDGVPGVTQ------CPIP 76

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*....
gi 1776487195  164 PGGQYTYTWDVTEDQGpakgdadciTRVYHSHIDAPRdvASGLVGPLII 212
Cdd:pfam07732   77 PGQSFTYRFQVKQQAG---------TYWYHSHTSGQQ--AAGLAGAIII 114
SufI COG2132
Multicopper oxidase with three cupredoxin domains (includes cell division protein FtsP and ...
 965-1065 2.42e-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: 2.42e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776487195  965 MHAINGKVFGNLH-GLTMHVGDEVSWYLMAMGNeiDIHTAHFHGHSF------DYKQTGIYRADVFDLFPGtfQTVEMI- 1036
Cdd:COG2132    317 VWTINGKAFDPDRpDLTVKLGERERWTLVNDTM--MPHPFHLHGHQFqvlsrnGKPPPEGGWKDTVLVPPG--ETVRILf 392

                           90       100       110
                   ....*....|....*....|....*....|.
gi 1776487195 1037 --PQNPGTWLLHCHVTDHIHAGMEATYTVLP 1065
Cdd:COG2132    393 rfDNYPGDWMFHCHILEHEDAGMMGQFEVVP 423
Cu-oxidase pfam00394
Multicopper oxidase; Many of the proteins in this family contain multiple similar copies of ...
 234-370 6.96e-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: 6.96e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776487195  234 FSVMDENLSWYlEDNIRMYCSEPSKVDKDDEDFQESNKMHSINGYMYGYLPNLTMCVEDKVKWHLFgMGNEADIHSAYFH 313
Cdd:pfam00394    1 EDYVITLSDWY-HKDAKDLEKELLASGKAPTDFPPVPDAVLINGKDGASLATLTVTPGKTYRLRII-NVALDDSLNFSIE 78

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1776487195  314 GQ--TLIE---RHH---RVDTINLFPATFIDALMIP-RNPGEWLLSCQVN-DHIEGGMQALFKVEGC 370
Cdd:pfam00394   79 GHkmTVVEvdgVYVnpfTVDSLDIFPGQRYSVLVTAnQDPGNYWIVASPNiPAFDNGTAAAILRYSG 145
SufI COG2132
Multicopper oxidase with three cupredoxin domains (includes cell division protein FtsP and ...
 105-235 1.26e-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: 1.26e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776487195  105 FLGPIIKGEVGDSIVVHLKNFASRNYTLHPHGVKYTKENEGafYPdntkgfekrDDAVKPGGQYTYTWDVteDQGPAkgd 184
Cdd:COG2132     42 YPGPTIRVREGDRVRVRVTNRLPEPTTVHWHGLRVPNAMDG--VP---------GDPIAPGETFTYEFPV--PQPAG--- 105

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 1776487195  185 adciTRVYHSHIDA--PRDVASGLVGPLIIcrkgamNKDNDKY--VDAEFILMFS 235
Cdd:COG2132    106 ----TYWYHPHTHGstAEQVYRGLAGALIV------EDPEEDLprYDRDIPLVLQ 150
PLN02191 PLN02191
L-ascorbate oxidase
 105-235 3.07e-07

L-ascorbate oxidase


Pssm-ID: 177843 [Multi-domain]  Cd Length: 574  Bit Score: 54.63  E-value: 3.07e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776487195  105 FLGPIIKGEVGDSIVVHLKN-FASRNYTLHPHGVKytkeNEGAFYPDNTKGFEKRddAVKPGGQYTYTWDVtEDQGpakg 183
Cdd:PLN02191    51 FPGPTIDAVAGDTIVVHLTNkLTTEGLVIHWHGIR----QKGSPWADGAAGVTQC--AINPGETFTYKFTV-EKPG---- 119

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|..
gi 1776487195  184 dadciTRVYHSHIDAPRdvASGLVGPLIIcrKGAMNKDNDKYVDAEFILMFS 235
Cdd:PLN02191   120 -----THFYHGHYGMQR--SAGLYGSLIV--DVAKGPKERLRYDGEFNLLLS 162
ascorbase TIGR03388
L-ascorbate oxidase, plant type; Members of this protein family are the copper-containing ...
 105-235 5.99e-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: 5.99e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776487195  105 FLGPIIKGEVGDSIVVHLKN-FASRNYTLHPHGVKytkeNEGAFYPDNTKGFEKRddAVKPGGQYTYTWdVTEDQGpakg 183
Cdd:TIGR03388   29 FPGPTIRAQAGDTIVVELTNkLHTEGVVIHWHGIR----QIGTPWADGTAGVTQC--AINPGETFIYNF-VVDRPG---- 97

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|..
gi 1776487195  184 dadciTRVYHSHIDAPRdvASGLVGPLIIcRKGAMNKDNDKYvDAEFILMFS 235
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 ...
 459-566 1.96e-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: 48.01  E-value: 1.96e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776487195  459 LLGPVIKAEVGESIRVTFRNNASRPFSIQPHGVSYLKSNE--GALYrtasrDTESPasyVSPGASFTYEWNVPEDVGptd 536
Cdd:pfam07732   24 FPGPTIRVREGDTVVVNVTNNLDEPTSIHWHGLQQRGTPWmdGVPG-----VTQCP---IPPGQSFTYRFQVKQQAG--- 92

                           90       100       110
                   ....*....|....*....|....*....|
gi 1776487195  537 qdpdclTWFYYSAVDSVRdtNSGLVGPLLV 566
Cdd:pfam07732   93 ------TYWYHSHTSGQQ--AAGLAGAIII 114
PLN02191 PLN02191
L-ascorbate oxidase
 999-1057 5.42e-06

L-ascorbate oxidase


Pssm-ID: 177843 [Multi-domain]  Cd Length: 574  Bit Score: 50.40  E-value: 5.42e-06
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1776487195  999 DIHTAHFHGHSF--------------DYKQTGIYRADVFD---LFPGTFQTVEMIPQNPGTWLLHCHVTDHIHAGM 1057
Cdd:PLN02191   465 EIHPWHLHGHDFwvlgygdgkfkpgiDEKTYNLKNPPLRNtaiLYPYGWTAIRFVTDNPGVWFFHCHIEPHLHMGM 540
SufI COG2132
Multicopper oxidase with three cupredoxin domains (includes cell division protein FtsP and ...
 459-588 3.23e-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: 3.23e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776487195  459 LLGPVIKAEVGESIRVTFRNNASRPFSIQPHGVsylksnegalyRTASRDTESPASYVSPGASFTYEWNVPEDVGptdqd 538
Cdd:COG2132     42 YPGPTIRVREGDRVRVRVTNRLPEPTTVHWHGL-----------RVPNAMDGVPGDPIAPGETFTYEFPVPQPAG----- 105

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|..
gi 1776487195  539 pdclTWFYYSAVD--SVRDTNSGLVGPLLVCRKGALLPsakqrSVTREFFLL 588
Cdd:COG2132    106 ----TYWYHPHTHgsTAEQVYRGLAGALIVEDPEEDLP-----RYDRDIPLV 148
SufI COG2132
Multicopper oxidase with three cupredoxin domains (includes cell division protein FtsP and ...
 816-906 2.94e-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: 2.94e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776487195  816 GPLIMSSVGDKINIVFKNLASRPYSIHAHGVKTDSS----VVAITNPGETKMYVWKIsarssserDDSHCTAWaYHSTVD 891
Cdd:COG2132     44 GPTIRVREGDRVRVRVTNRLPEPTTVHWHGLRVPNAmdgvPGDPIAPGETFTYEFPV--------PQPAGTYW-YHPHTH 114

                           90
                   ....*....|....*..
gi 1776487195  892 II--KDTYSGLIGTLVV 906
Cdd:COG2132    115 GStaEQVYRGLAGALIV 131
Cu-oxidase_3 pfam07732
Multicopper oxidase; This entry contains many divergent copper oxidase-like domains that are ...
 813-888 3.29e-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: 38.77  E-value: 3.29e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776487195  813 QIQGPLIMSSVGDKINIVFKNLASRPYSIHAHGVKTDSS-----VVAITN----PGETKMYVWKIsarssserDDSHCTA 883
Cdd:pfam07732   23 QFPGPTIRVREGDTVVVNVTNNLDEPTSIHWHGLQQRGTpwmdgVPGVTQcpipPGQSFTYRFQV--------KQQAGTY 94


                   ....*
gi 1776487195  884 WaYHS 888
Cdd:pfam07732   95 W-YHS 98
ascorbOXfungal TIGR03390
L-ascorbate oxidase, fungal type; This model describes a family of fungal ascorbate oxidases, ...
 1018-1068 3.40e-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: 3.40e-03
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|.
gi 1776487195 1018 YRADVFDLFPGTFQTVEMIPQNPGTWLLHCHVTDHIHAGMEATYTVLPKED 1068
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 ...
 381-579 2.43e-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: 2.43e-124
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776487195  381 TKIRQYFIAAEEIIWNYGPSAFNHFTGQELIA-DSESSVFFERSETRIGGSYKKAIYKEYTDGTFTAHKKRLPEEEHLGL 459
Cdd:cd04224      1 GKVRHYFIAAEEIMWDYAPSGKNLFTGQNLTApGSDSEVFFQRNETRIGGTYWKVRYVEYTDATFTTRKHRSKEEEHLGI 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776487195  460 LGPVIKAEVGESIRVTFRNNASRPFSIQPHGVSYLKSNEGALYRtasRDTESPASYVSPGASFTYEWNVPEDVGPTDQDP 539
Cdd:cd04224     81 LGPVIRAEVGDTIKVTFRNKASRPFSIQPHGVFYEKNYEGAMYR---DGDPSPGSHVSPGETFTYEWTVPEGVGPTNQDP 157

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|
gi 1776487195  540 DCLTWFYYSAVDSVRDTNSGLVGPLLVCRKGALLPSAKQR 579
Cdd:cd04224    158 PCLTYLYFSAVDPVRDTNSGLVGPLLVCKKGSLNANGRQK 197
CuRO_1_ceruloplasmin cd04222
The first cupredoxin domain of Ceruloplasmin; Ceruloplasmin is a multicopper oxidase essential ...
 33-215 2.30e-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: 2.30e-122
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776487195   33 REYYIGIVETAWDYAPGSTDIISGQRFAEEEQAEVFLKRGPQRIGSIYKKAVYTQYTNILYDVIVEKPSWLGFLGPIIKG 112
Cdd:cd04222      1 REYYIGIRETQWDYAPSGKNLITNQTFDDDEHASVFLKRGPDRIGRVYKKAVYLQYTDDTYRTEIEKPVWLGFLGPILKA 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776487195  113 EVGDSIVVHLKNFASRNYTLHPHGVKYTKENEGAFYPDNTKGFEKRDDAVKPGGQYTYTWDVTEDQGPAKGDADCITRVY 192
Cdd:cd04222     81 EVGDVIVVHLKNFASRPYSLHPHGVFYNKENEGALYPDNTSGFEKADDAVPPGGSYTYTWTVPEEQAPTKADANCLTRIY 160

                          170       180
                   ....*....|....*....|...
gi 1776487195  193 HSHIDAPRDVASGLVGPLIICRK 215
Cdd:cd04222    161 HSHIDAPKDIASGLIGPLIICKK 183
CuRO_5_ceruloplasmin cd04225
The fifth cupredoxin domain of Ceruloplasmin; Ceruloplasmin is a multicopper oxidase essential ...
 739-909 3.70e-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: 3.70e-108
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776487195  739 KTHYIAAVEVEWDYSPNRTWEFERHQFHKESPGNSFLNKEDAFIGSKYKKVVYREYTDQTFSTPKSRAEEEQHLQIQGPL 818
Cdd:cd04225      1 RTYYIAAEEVEWDYSPQRTWEQELHNTHEESPGNAFLNKGDKFIGSKYKKVVYREYTDDTFSVPKERTAEEEHLGILGPL 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776487195  819 IMSSVGDKINIVFKNLASRPYSIHAHGVKTDSSVVAITNPGETKMYVWKISARSSSERDDSHCTAWAYHSTVDIIKDTYS 898
Cdd:cd04225     81 IHAEVGEKVKIVFKNMASRPYSIHAHGVKTDSSWVAPTEPGETQTYTWKIPERSGPGVEDSNCISWAYYSTVDQIKDLYS 160

                          170
                   ....*....|.
gi 1776487195  899 GLIGTLVVCPR 909
Cdd:cd04225    161 GLIGPLVICRR 171
CuRO_6_ceruloplasmin cd11012
The sixth cupredoxin domain of Ceruloplasmin; Ceruloplasmin is a multicopper oxidase essential ...
 920-1064 7.10e-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: 7.10e-96
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776487195  920 KVHFALLFMVFDENESWYLDENIETYSANPHLVDKENEEFLESNKMHAINGKVFGNLHGLTMHVGDEVSWYLMAMGNEID 999
Cdd:cd11012      1 KLEFALLFLVFDENESWYLDENIKTYSDHPEKVNKEDEEFIESNKMHAINGKVFGNLQGLTMHVGDEVYWYLMGMGNEID 80

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1776487195 1000 IHTAHFHGHSFDYKQTGIYRADVFDLFPGTFQTVEMIPQNPGTWLLHCHVTDHIHAGMEATYTVL 1064
Cdd:cd11012     81 IHTAHFHGHSFDYKHRGVYRSDVFDLFPGTFQTVEMIPRTPGTWLLHCHVTDHIHAGMETTYTVL 145
CuRO_2_ceruloplasmin cd11021
The second cupredoxin domain of Ceruloplasmin; Ceruloplasmin is a multicopper oxidase ...
 227-367 9.65e-96

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: 300.16  E-value: 9.65e-96
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776487195  227 DAEFILMFSVMDENLSWYLEDNIRMYCSEPSKVDKDDEDFQESNKMHSINGYMYGYLPNLTMCVEDKVKWHLFGMGNEAD 306
Cdd:cd11021      1 DREFVLMFSVVDENLSWYLDENIKTYCSEPAKVDKDDEDFQESNKMHSINGYTFGNLPGLSMCAGDRVKWHLFGMGNEVD 80

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1776487195  307 IHSAYFHGQTLIERHHRVDTINLFPATFIDALMIPRNPGEWLLSCQVNDHIEGGMQALFKV 367
Cdd:cd11021     81 IHSAFFHGQTLTDRGHRTDTINLFPATFVTAEMVAQNPGKWLLSCQVNDHLKAGMQAFYEV 141
CuRO_4_ceruloplasmin cd11022
The fourth cupredoxin domain of Ceruloplasmin; Ceruloplasmin is a multicopper oxidase ...
 582-725 1.48e-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: 1.48e-95
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776487195  582 TREFFLLATVFDENLSWYLDDNILMFTLNPNEIDKDNEDFQESNKMHSINGYMYGNQPGLEMCKGDVISWHLMGLGSEVD 661
Cdd:cd11022      1 DKEFFLLFTVFDENESWYLDENIQQFTLDPRSVDKEDEDFQESNKMHSINGYMYGNQPGLDMCKGDTVSWHLFGLGTETD 80

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1776487195  662 VHGIYFSQNTFITKGTRKDTANLFPHTFVTAIMKPDSEGIFEVSCLTTDHHRGGMKQKYKVKPC 725
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 ...
 33-215 2.63e-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: 256.95  E-value: 2.63e-79
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776487195   33 REYYIGIVETAWDYAPGSTDIIsgqrfaEEEQAEVFLKRGPQRIGSIYKKAVYTQYTNILYDVIVEKPSWLGFLGPIIKG 112
Cdd:cd04199      1 RHYYIAAEEIDWDYAPSGLAEK------DLSYRNQYLDNGPFRIGRSYKKVVYREYTDESFTTPGPQPEHLGILGPTIRA 74

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776487195  113 EVGDSIVVHLKNFASRNYTLHPHGVKYTKENEGAFYPDNTKGFEKRDDAVKPGGQYTYTWDVTEDQGPAKGDADCITRVY 192
Cdd:cd04199     75 EVGDTIKVHFKNKASRPYSIHPHGVSYEKDSEGASYSDQTGPDEKKDDAVAPGETYTYVWIVTEESGPTKGDPACLTWAY 154

                          170       180
                   ....*....|....*....|...
gi 1776487195  193 HSHIDAPRDVASGLVGPLIICRK 215
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 ...
 384-569 4.54e-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: 4.54e-78
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776487195  384 RQYFIAAEEIIWNYGPSafnhftGQELIADSESSVFFERSETRIGGSYKKAIYKEYTDGTFTahkKRLPEEEHLGLLGPV 463
Cdd:cd04199      1 RHYYIAAEEIDWDYAPS------GLAEKDLSYRNQYLDNGPFRIGRSYKKVVYREYTDESFT---TPGPQPEHLGILGPT 71

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776487195  464 IKAEVGESIRVTFRNNASRPFSIQPHGVSYLKSNEGALYRTASRDTESPASYVSPGASFTYEWNVPEDVGPTDQDPDCLT 543
Cdd:cd04199     72 IRAEVGDTIKVHFKNKASRPYSIHPHGVSYEKDSEGASYSDQTGPDEKKDDAVAPGETYTYVWIVTEESGPTKGDPACLT 151

                          170       180
                   ....*....|....*....|....*.
gi 1776487195  544 WFYYSAVDSVRDTNSGLVGPLLVCRK 569
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 ...
 227-367 1.25e-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: 231.53  E-value: 1.25e-70
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776487195  227 DAEFILMFSVMDENLSWYLEDNIRMYCSEPSKVDKDDEDFQESNKMHSINGYMYGYLPNLTMCVEDKVKWHLFGMGNEAD 306
Cdd:cd04200      1 DKEFVLLFAVFDENKSWYLEDNIKRFCDNPEKVDKDDEEFQESNKMHAINGYVFGNLPGLTMCAGDRVRWHLLGMGNEVD 80

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1776487195  307 IHSAYFHGQTLIERHHRVDTINLFPATFIDALMIPRNPGEWLLSCQVNDHIEGGMQALFKV 367
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 ...
 923-1063 3.17e-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: 3.17e-68
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776487195  923 FALLFMVFDENESWYLDENIETYSANPHLVDKENEEFLESNKMHAINGKVFGNLHGLTMHVGDEVSWYLMAMGNEIDIHT 1002
Cdd:cd04200      4 FVLLFAVFDENKSWYLEDNIKRFCDNPEKVDKDDEEFQESNKMHAINGYVFGNLPGLTMCAGDRVRWHLLGMGNEVDVHS 83

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1776487195 1003 AHFHGHSFDYKQtgiYRADVFDLFPGTFQTVEMIPQNPGTWLLHCHVTDHIHAGMEATYTV 1063
Cdd:cd04200     84 IHFHGQTFLYKG---YRIDTLTLFPATFETVEMVPSNPGTWLLHCHNSDHRHAGMQAYFLV 141
CuRO_1_ceruloplasmin cd04222
The first cupredoxin domain of Ceruloplasmin; Ceruloplasmin is a multicopper oxidase essential ...
 384-569 2.05e-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: 2.05e-67
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776487195  384 RQYFIAAEEIIWNYGPSAFNHFTGQELIADSESSVFFERSETRIGGSYKKAIYKEYTDGTFTahkKRLPEEEHLGLLGPV 463
Cdd:cd04222      1 REYYIGIRETQWDYAPSGKNLITNQTFDDDEHASVFLKRGPDRIGRVYKKAVYLQYTDDTYR---TEIEKPVWLGFLGPI 77

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776487195  464 IKAEVGESIRVTFRNNASRPFSIQPHGVSYLKSNEGALYRTASRDTESPASYVSPGASFTYEWNVPEDVGPTDQDPDCLT 543
Cdd:cd04222     78 LKAEVGDVIVVHLKNFASRPYSLHPHGVFYNKENEGALYPDNTSGFEKADDAVPPGGSYTYTWTVPEEQAPTKADANCLT 157

                          170       180
                   ....*....|....*....|....*.
gi 1776487195  544 WFYYSAVDSVRDTNSGLVGPLLVCRK 569
Cdd:cd04222    158 RIYHSHIDAPKDIASGLIGPLIICKK 183
CuRO_4_ceruloplasmin cd11022
The fourth cupredoxin domain of Ceruloplasmin; Ceruloplasmin is a multicopper oxidase ...
 227-370 2.68e-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: 2.68e-63
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776487195  227 DAEFILMFSVMDENLSWYLEDNIRMYCSEPSKVDKDDEDFQESNKMHSINGYMYGYLPNLTMCVEDKVKWHLFGMGNEAD 306
Cdd:cd11022      1 DKEFFLLFTVFDENESWYLDENIQQFTLDPRSVDKEDEDFQESNKMHSINGYMYGNQPGLDMCKGDTVSWHLFGLGTETD 80

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1776487195  307 IHSAYFHGQTLIERHHRVDTINLFPATFIDALMIPRNPGEWLLSCQVNDHIEGGMQALFKVEGC 370
Cdd:cd11022     81 VHGIYFSGNTFLLQGTRRDTANLFPHTSVTAIMQPDNEGTFEVNCQTTDHYSAGMRQIYTVSQC 144
CuRO_2_ceruloplasmin cd11021
The second cupredoxin domain of Ceruloplasmin; Ceruloplasmin is a multicopper oxidase ...
 923-1063 3.36e-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: 3.36e-61
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776487195  923 FALLFMVFDENESWYLDENIETYSANPHLVDKENEEFLESNKMHAINGKVFGNLHGLTMHVGDEVSWYLMAMGNEIDIHT 1002
Cdd:cd11021      4 FVLMFSVVDENLSWYLDENIKTYCSEPAKVDKDDEDFQESNKMHSINGYTFGNLPGLSMCAGDRVKWHLFGMGNEVDIHS 83

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1776487195 1003 AHFHGHSFDYKQtgiYRADVFDLFPGTFQTVEMIPQNPGTWLLHCHVTDHIHAGMEATYTV 1063
Cdd:cd11021     84 AFFHGQTLTDRG---HRTDTINLFPATFVTAEMVAQNPGKWLLSCQVNDHLKAGMQAFYEV 141
CuRO_2_ceruloplasmin cd11021
The second cupredoxin domain of Ceruloplasmin; Ceruloplasmin is a multicopper oxidase ...
 583-722 1.60e-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: 1.60e-60
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776487195  583 REFFLLATVFDENLSWYLDDNILMFTLNPNEIDKDNEDFQESNKMHSINGYMYGNQPGLEMCKGDVISWHLMGLGSEVDV 662
Cdd:cd11021      2 REFVLMFSVVDENLSWYLDENIKTYCSEPAKVDKDDEDFQESNKMHSINGYTFGNLPGLSMCAGDRVKWHLFGMGNEVDI 81

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776487195  663 HGIYFSQNTFITKGTRKDTANLFPHTFVTAIMKPDSEGIFEVSCLTTDHHRGGMKQKYKV 722
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 ...
 583-722 3.31e-60

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


Pssm-ID: 259863 [Multi-domain]  Cd Length: 141  Bit Score: 202.25  E-value: 3.31e-60
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776487195  583 REFFLLATVFDENLSWYLDDNILMFTLNPNEIDKDNEDFQESNKMHSINGYMYGNQPGLEMCKGDVISWHLMGLGSEVDV 662
Cdd:cd04200      2 KEFVLLFAVFDENKSWYLEDNIKRFCDNPEKVDKDDEEFQESNKMHAINGYVFGNLPGLTMCAGDRVRWHLLGMGNEVDV 81

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776487195  663 HGIYFSQNTFITKGTRKDTANLFPHTFVTAIMKPDSEGIFEVSCLTTDHHRGGMKQKYKV 722
Cdd:cd04200     82 HSIHFHGQTFLYKGYRIDTLTLFPATFETVEMVPSNPGTWLLHCHNSDHRHAGMQAYFLV 141
CuRO_5_ceruloplasmin cd04225
The fifth cupredoxin domain of Ceruloplasmin; Ceruloplasmin is a multicopper oxidase essential ...
 384-569 1.84e-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: 1.84e-59
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776487195  384 RQYFIAAEEIIWNYGPSAFNHFTGQELIADSESSVFFERSETRIGGSYKKAIYKEYTDGTFTAHKKRLPEEEHLGLLGPV 463
Cdd:cd04225      1 RTYYIAAEEVEWDYSPQRTWEQELHNTHEESPGNAFLNKGDKFIGSKYKKVVYREYTDDTFSVPKERTAEEEHLGILGPL 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776487195  464 IKAEVGESIRVTFRNNASRPFSIQPHGVSylksnegalyrtasrdTESPA-SYVSPGASFTYEWNVPEDVGPTDQDPDCL 542
Cdd:cd04225     81 IHAEVGEKVKIVFKNMASRPYSIHAHGVK----------------TDSSWvAPTEPGETQTYTWKIPERSGPGVEDSNCI 144

                          170       180
                   ....*....|....*....|....*..
gi 1776487195  543 TWFYYSAVDSVRDTNSGLVGPLLVCRK 569
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 ...
 739-907 1.65e-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: 1.65e-58
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776487195  739 KTHYIAAVEVEWDYSPNRTWEFERHQFhkespgNSFLNKEDAFIGSKYKKVVYREYTDQTFSTPKsraEEEQHLQIQGPL 818
Cdd:cd04199      1 RHYYIAAEEIDWDYAPSGLAEKDLSYR------NQYLDNGPFRIGRSYKKVVYREYTDESFTTPG---PQPEHLGILGPT 71

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776487195  819 IMSSVGDKINIVFKNLASRPYSIHAHGVKTDSS---------------VVAITNPGETKMYVWKISARSSSERDDSHCTA 883
Cdd:cd04199     72 IRAEVGDTIKVHFKNKASRPYSIHPHGVSYEKDsegasysdqtgpdekKDDAVAPGETYTYVWIVTEESGPTKGDPACLT 151

                          170       180
                   ....*....|....*....|....
gi 1776487195  884 WAYHSTVDIIKDTYSGLIGTLVVC 907
Cdd:cd04199    152 WAYYSHVDLEKDINSGLIGPLLIC 175
CuRO_3_ceruloplasmin cd04224
The third cupredoxin domain of Ceruloplasmin; Ceruloplasmin is a multicopper oxidase essential ...
 33-221 2.89e-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: 2.89e-58
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776487195   33 REYYIGIVETAWDYAPGSTDIISGQRF-AEEEQAEVFLKRGPQRIGSIYKKAVYTQYTNILYDV---IVEKPSWLGFLGP 108
Cdd:cd04224      4 RHYFIAAEEIMWDYAPSGKNLFTGQNLtAPGSDSEVFFQRNETRIGGTYWKVRYVEYTDATFTTrkhRSKEEEHLGILGP 83

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776487195  109 IIKGEVGDSIVVHLKNFASRNYTLHPHGVKYTKENEGAFYPDntkGFEKRDDAVKPGGQYTYTWDVTEDQGPAKGDADCI 188
Cdd:cd04224     84 VIRAEVGDTIKVTFRNKASRPFSIQPHGVFYEKNYEGAMYRD---GDPSPGSHVSPGETFTYEWTVPEGVGPTNQDPPCL 160

                          170       180       190
                   ....*....|....*....|....*....|...
gi 1776487195  189 TRVYHSHIDAPRDVASGLVGPLIICRKGAMNKD 221
Cdd:cd04224    161 TYLYFSAVDPVRDTNSGLVGPLLVCKKGSLNAN 193
CuRO_1_Ceruloplasmin_like_1 cd04229
cupredoxin domain of ceruloplasmin homologs; Uncharacterized subfamily of ceruloplasmin ...
 384-570 3.85e-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: 3.85e-58
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776487195  384 RQYFIAAEEIIWNYGPSAFNH-FTGQELiadSESSVFFERSETRIGGSYKKAIYKEYTDGTFTahkKRLPEEEHLGLLGP 462
Cdd:cd04229      1 RTYYIAAEEVDWDYAPSGKNKcCLGDDL---EVSTLDSQPGPYTIGSTYTKARYREYTDNSFS---TPKPTPAYLGILGP 74

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776487195  463 VIKAEVGESIRVTFRNNASR-PFSIQPHGVSYLKSNEGALYRTASRdtespasyVSPGASFTYEWNVPEDVGPTDQDPDC 541
Cdd:cd04229     75 VIRAEVGDTIKVVFKNNLDEfPVNMHPHGGLYSKDNEGTTDGAGDV--------VAPGETYTYRWIVPEDAGPGPGDPSS 146

                          170       180
                   ....*....|....*....|....*....
gi 1776487195  542 LTWFYYSAVDSVRDTNSGLVGPLLVCRKG 570
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 ...
 382-568 1.33e-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: 196.64  E-value: 1.33e-57
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776487195  382 KIRQYFIAAEEIIWNYGP----SAFNHFTGQELIADSEssvffersetRIGGSYKKAIYKEYTDGTFTAHKKRlPEEEHL 457
Cdd:cd14450      1 KNWEYFIAAEEVIWDYAPsipeNMDKRYRSQYLDNFSN----------NIGKKYKKAVFTQYEDGSFTKRLEN-PRPKEE 69

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776487195  458 GLLGPVIKAEVGESIRVTFRNNASRPFSIQPHGVSYLKSNEGALYRTASRDTESPASYVSPGASFTYEWNVPEDVGPTDQ 537
Cdd:cd14450     70 GILGPVIRAQVRDTIKIVFKNKASRPYSIYPHGVTVSKAAEGASYPPDPRGNETQNKAVQPGETYTYKWNILETDEPTAR 149

                          170       180       190
                   ....*....|....*....|....*....|.
gi 1776487195  538 DPDCLTWFYYSAVDSVRDTNSGLVGPLLVCR 568
Cdd:cd14450    150 DPRCLTRMYHSAVDITRDIASGLIGPLLICK 180
CuRO_1_FVIII_like cd14452
The first cupredoxin domain of coagulation factor VIII and similar proteins; Factor VIII ...
 33-216 2.02e-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: 2.02e-56
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776487195   33 REYYIGIVETAWDYApgstdiisgqrFAEEEQAEVFLKRGPQRIGSIYKKAVYTQYTNILYDVIVEKPSWLGFLGPIIKG 112
Cdd:cd14452      1 RRYYIAAVEIGWDYI-----------HSDLGDPASEQRKKPKDIPQKYIKAVFVEYLDATFTVPKPRPAWMGLLGPTIVA 69

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776487195  113 EVGDSIVVHLKNFASRNYTLHPHGVKYTKENEGAFYPDNTKGFEKRDDAVKPGGQYTYTWDVTEDQGPAKGDADCITRVY 192
Cdd:cd14452     70 EVGDTVVITFKNLASQPYSLHAVGVSYWKASEGAGYDDSTSQHEKEDDAVYPGGYHTYVWDISPKDGPTGSDPECLTYSY 149

                          170       180
                   ....*....|....*....|....
gi 1776487195  193 HSHIDAPRDVASGLVGPLIICRKG 216
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 ...
 384-570 5.56e-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: 5.56e-56
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776487195  384 RQYFIAAEEIIWNYGPSAfnhftgqeliadsESSVFFERSETRigGSYKKAIYKEYTDGTFTAHKKRLPEEEHLGLLGPV 463
Cdd:cd14451      2 RRYYIAAEEEEWDYAGYG-------------KSRLDKTQNERD--TVFKKVVFRRYLDSTFSTPDIQGEYEEHLGILGPV 66

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776487195  464 IKAEVGESIRVTFRNNASRPFSIQPHGVSYLKSNEGALYrtasrDTESPASY-----VSPGASFTYEWNVPEDVGPTDQD 538
Cdd:cd14451     67 IRAEVDDVIQVFFKNLASRPYSLHAHGLSYEKSSEGLSY-----DDESPDWFkkddaVQPNGTYTYVWYANPRSGPENNG 141

                          170       180       190
                   ....*....|....*....|....*....|..
gi 1776487195  539 PDCLTWFYYSAVDSVRDTNSGLVGPLLVCRKG 570
Cdd:cd14451    142 SDCRTWAYYSAVNPEKDIHSGLIGPLLICRKG 173
CuRO_4_ceruloplasmin cd11022
The fourth cupredoxin domain of Ceruloplasmin; Ceruloplasmin is a multicopper oxidase ...
 923-1063 3.68e-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: 3.68e-55
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776487195  923 FALLFMVFDENESWYLDENIETYSANPHLVDKENEEFLESNKMHAINGKVFGNLHGLTMHVGDEVSWYLMAMGNEIDIHT 1002
Cdd:cd11022      4 FFLLFTVFDENESWYLDENIQQFTLDPRSVDKEDEDFQESNKMHSINGYMYGNQPGLDMCKGDTVSWHLFGLGTETDVHG 83

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1776487195 1003 AHFHGHSFDYKQTgiyRADVFDLFPGTFQTVEMIPQNPGTWLLHCHVTDHIHAGMEATYTV 1063
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 ...
 34-214 1.94e-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: 1.94e-53
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776487195   34 EYYIGIVETAWDYAPGSTDIISGQRFAEeeqaevFLKRGPQRIGSIYKKAVYTQYTNILYDVIVE--KPSWLGFLGPIIK 111
Cdd:cd14450      4 EYFIAAEEVIWDYAPSIPENMDKRYRSQ------YLDNFSNNIGKKYKKAVFTQYEDGSFTKRLEnpRPKEEGILGPVIR 77

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776487195  112 GEVGDSIVVHLKNFASRNYTLHPHGVKYTKENEGAFYPDNTKGFEKRDDAVKPGGQYTYTWDVTEDQGPAKGDADCITRV 191
Cdd:cd14450     78 AQVRDTIKIVFKNKASRPYSIYPHGVTVSKAAEGASYPPDPRGNETQNKAVQPGETYTYKWNILETDEPTARDPRCLTRM 157

                          170       180
                   ....*....|....*....|...
gi 1776487195  192 YHSHIDAPRDVASGLVGPLIICR 214
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 ...
 33-216 2.51e-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: 2.51e-53
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776487195   33 REYYIGIVETAWDYAPGSTDIISgqrfaeeeqaevflkrgpQRIGSIYKKAVYTQYTNilyDVIVEKPSWL--GFLGPII 110
Cdd:cd04226      1 REYYIAAQNIDWDYTPQSEELRL------------------KRSEQSFKKIVYREYEE---GFKKEKPADLssGLLGPTL 59

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776487195  111 KGEVGDSIVVHLKNFASRNYTLHPHGVKYTKENEGAFYPDNTKGFEKRDDAVKPGGQYTYTWDVTEDQGPAKGDADCITR 190
Cdd:cd04226     60 RAEVGDTLIVHFKNMADKPLSIHPQGIAYGKKSEGSLYSDNTSPVEKLDDAVQPGQEYTYVWDITEEVGPTEADPPCLTY 139

                          170       180
                   ....*....|....*....|....*.
gi 1776487195  191 VYHSHIDAPRDVASGLVGPLIICRKG 216
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 ...
 384-570 2.76e-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: 2.76e-53
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776487195  384 RQYFIAAEEIIWNYGPsafnhftGQEliadsessvffERSETRIGGSYKKAIYKEYTDGtftaHKKRLPEEEHLGLLGPV 463
Cdd:cd04226      1 REYYIAAQNIDWDYTP-------QSE-----------ELRLKRSEQSFKKIVYREYEEG----FKKEKPADLSSGLLGPT 58

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776487195  464 IKAEVGESIRVTFRNNASRPFSIQPHGVSYLKSNEGALYRTASRDTESPASYVSPGASFTYEWNVPEDVGPTDQDPDCLT 543
Cdd:cd04226     59 LRAEVGDTLIVHFKNMADKPLSIHPQGIAYGKKSEGSLYSDNTSPVEKLDDAVQPGQEYTYVWDITEEVGPTEADPPCLT 138

                          170       180
                   ....*....|....*....|....*..
gi 1776487195  544 WFYYSAVDSVRDTNSGLVGPLLVCRKG 570
Cdd:cd04226    139 YIYYSHVNMVRDFNSGLIGALLICKKG 165
CuRO_1_Ceruloplasmin_like_1 cd04229
cupredoxin domain of ceruloplasmin homologs; Uncharacterized subfamily of ceruloplasmin ...
 33-216 4.35e-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: 180.30  E-value: 4.35e-52
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776487195   33 REYYIGIVETAWDYAP-GSTDIISGQRfaeEEQAEVFLKRGPQRIGSIYKKAVYTQYTNILYDVIVEKPSWLGFLGPIIK 111
Cdd:cd04229      1 RTYYIAAEEVDWDYAPsGKNKCCLGDD---LEVSTLDSQPGPYTIGSTYTKARYREYTDNSFSTPKPTPAYLGILGPVIR 77

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776487195  112 GEVGDSIVVHLKN-FASRNYTLHPHGVKYTKENEGafypdntkGFEKRDDAVKPGGQYTYTWDVTEDQGPAKGDADCITR 190
Cdd:cd04229     78 AEVGDTIKVVFKNnLDEFPVNMHPHGGLYSKDNEG--------TTDGAGDVVAPGETYTYRWIVPEDAGPGPGDPSSRLW 149

                          170       180
                   ....*....|....*....|....*.
gi 1776487195  191 VYHSHIDAPRDVASGLVGPLIICRKG 216
Cdd:cd04229    150 LYHSHVDVFAHTNAGLVGPIIVTSKG 175
CuRO_6_ceruloplasmin cd11012
The sixth cupredoxin domain of Ceruloplasmin; Ceruloplasmin is a multicopper oxidase essential ...
 229-367 7.97e-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: 7.97e-52
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776487195  229 EFILMFSVMDENLSWYLEDNIRMYCSEPSKVDKDDEDFQESNKMHSINGYMYGYLPNLTMCVEDKVKWHLFGMGNEADIH 308
Cdd:cd11012      3 EFALLFLVFDENESWYLDENIKTYSDHPEKVNKEDEEFIESNKMHAINGKVFGNLQGLTMHVGDEVYWYLMGMGNEIDIH 82

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1776487195  309 SAYFHGQTLIERH---HRVDTINLFPATFIDALMIPRNPGEWLLSCQVNDHIEGGMQALFKV 367
Cdd:cd11012     83 TAHFHGHSFDYKHrgvYRSDVFDLFPGTFQTVEMIPRTPGTWLLHCHVTDHIHAGMETTYTV 144
CuRO_3_ceruloplasmin cd04224
The third cupredoxin domain of Ceruloplasmin; Ceruloplasmin is a multicopper oxidase essential ...
 737-920 4.95e-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: 4.95e-51
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776487195  737 HEKTHYIAAVEVEWDYSPNRTWEFErHQFHKESPGNS--FLNKEDAFIGSKYKKVVYREYTDQTFSTPKSRAEEEQHLQI 814
Cdd:cd04224      2 KVRHYFIAAEEIMWDYAPSGKNLFT-GQNLTAPGSDSevFFQRNETRIGGTYWKVRYVEYTDATFTTRKHRSKEEEHLGI 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776487195  815 QGPLIMSSVGDKINIVFKNLASRPYSIHAHGV------------KTDSSVVAITNPGETKMYVWKISARSSSERDDSHCT 882
Cdd:cd04224     81 LGPVIRAEVGDTIKVTFRNKASRPFSIQPHGVfyeknyegamyrDGDPSPGSHVSPGETFTYEWTVPEGVGPTNQDPPCL 160

                          170       180       190
                   ....*....|....*....|....*....|....*...
gi 1776487195  883 AWAYHSTVDIIKDTYSGLIGTLVVCPRHYLpSSHARKK 920
Cdd:cd04224    161 TYLYFSAVDPVRDTNSGLVGPLLVCKKGSL-NANGRQK 197
CuRO_5_FVIII_like cd04228
The fifth cupredoxin domain of coagulation factor VIII and similar proteins; Factor VIII ...
 383-570 1.47e-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: 173.15  E-value: 1.47e-49
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776487195  383 IRQYFIAAEEIIWNYGPSAFNHFtgqelIADSESSvffeRSETRIGGSYKKAIYKEYTDGTFTAHKKRLPEEEHLGLLGP 462
Cdd:cd04228      1 IRHYFIAAVEVLWDYGMQRPQHF-----LRARDPN----RGRRKSVPQYKKVVFREYLDGSFTQPVYRGELDEHLGILGP 71

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776487195  463 VIKAEVGESIRVTFRNNASRPFSIQPHGVSYlkSNEGAlyrtasrdTESPASYVSPGASFTYEWNVPEDVGPTDQDPDCL 542
Cdd:cd04228     72 YIRAEVEDNIMVTFKNLASRPYSFHSSLISY--EEDQR--------AEPRGNFVQPGEVQTYSWKVLHQMAPTKQEFDCK 141

                          170       180
                   ....*....|....*....|....*...
gi 1776487195  543 TWFYYSAVDSVRDTNSGLVGPLLVCRKG 570
Cdd:cd04228    142 AWAYFSNVDLEKDLHSGLIGPLIICKTG 169
CuRO_1_FVIII_like cd14452
The first cupredoxin domain of coagulation factor VIII and similar proteins; Factor VIII ...
 384-570 2.89e-49

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


Pssm-ID: 259994 [Multi-domain]  Cd Length: 173  Bit Score: 172.47  E-value: 2.89e-49
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776487195  384 RQYFIAAEEIIWNYGPSAfnhftgqeliaDSESSVFFERSETRIGGSYKKAIYKEYTDGTFTAHKKRLPeeeHLGLLGPV 463
Cdd:cd14452      1 RRYYIAAVEIGWDYIHSD-----------LGDPASEQRKKPKDIPQKYIKAVFVEYLDATFTVPKPRPA---WMGLLGPT 66

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776487195  464 IKAEVGESIRVTFRNNASRPFSIQPHGVSYLKSNEGALYRTASRDTESPASYVSPGASFTYEWNVPEDVGPTDQDPDCLT 543
Cdd:cd14452     67 IVAEVGDTVVITFKNLASQPYSLHAVGVSYWKASEGAGYDDSTSQHEKEDDAVYPGGYHTYVWDISPKDGPTGSDPECLT 146

                          170       180
                   ....*....|....*....|....*..
gi 1776487195  544 WFYYSAVDSVRDTNSGLVGPLLVCRKG 570
Cdd:cd14452    147 YSYSSQVDPVKDVNSGLIGALLVCRMG 173
CuRO_3_FVIII_like cd04227
The third cupredoxin domain of coagulation factor VIII and similar proteins; Factor VIII ...
 382-569 1.76e-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: 1.76e-48
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776487195  382 KIRQYFIAAEEIIWNYGPsafnHFTGQEliaDSE-SSVFFERSETRIGGSYKKAIYKEYTDGTFtahKKRLPEEEHLGLL 460
Cdd:cd04227      1 QTWEHYIAAEELDWDYAP----LLSSTD---DRElQSRYLPTGPQRIGYKYKKVAFVEYTDKTF---KRREAKQTEKGIL 70

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776487195  461 GPVIKAEVGESIRVTFRNNASRPFSIQPHGVSYLKSnegaLYRTASRDTESPASY--VSPGASFTYEWNVPEDVGPTDQD 538
Cdd:cd04227     71 GPLLKGEVGDQIHIMFKNTASRPYNIYPHGLTSVRP----MYRSRNPAGEKDLKTmpIGPGETFGYMWELTAEDGPTEED 146

                          170       180       190
                   ....*....|....*....|....*....|.
gi 1776487195  539 PDCLTWFYYSAVDSVRDTNSGLVGPLLVCRK 569
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 ...
 32-216 4.16e-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: 4.16e-47
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776487195   32 TREYYIGIVETAWDYAP-GSTDIISGQRFAEeeqaevflkrgpqrigSIYKKAVYTQYTNILY---DVIVEKPSWLGFLG 107
Cdd:cd14451      1 KRRYYIAAEEEEWDYAGyGKSRLDKTQNERD----------------TVFKKVVFRRYLDSTFstpDIQGEYEEHLGILG 64

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776487195  108 PIIKGEVGDSIVVHLKNFASRNYTLHPHGVKYTKENEGAFYPDNTKGFEKRDDAVKPGGQYTYTWDVTEDQGPAKGDADC 187
Cdd:cd14451     65 PVIRAEVDDVIQVFFKNLASRPYSLHAHGLSYEKSSEGLSYDDESPDWFKKDDAVQPNGTYTYVWYANPRSGPENNGSDC 144

                          170       180
                   ....*....|....*....|....*....
gi 1776487195  188 ITRVYHSHIDAPRDVASGLVGPLIICRKG 216
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 ...
 738-907 2.97e-46

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


Pssm-ID: 259993 [Multi-domain]  Cd Length: 173  Bit Score: 163.86  E-value: 2.97e-46
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776487195  738 EKTHYIAAVEVEWDYSPnrtweferhqfhkesPGNSFLNKEDAFIGSKYKKVVYREYTDQTFSTPKSRAEEEQHLQIQGP 817
Cdd:cd14451      1 KRRYYIAAEEEEWDYAG---------------YGKSRLDKTQNERDTVFKKVVFRRYLDSTFSTPDIQGEYEEHLGILGP 65

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776487195  818 LIMSSVGDKINIVFKNLASRPYSIHAHGVKTDSSVVAIT---------------NPGETKMYVWKISARSSSERDDSHCT 882
Cdd:cd14451     66 VIRAEVDDVIQVFFKNLASRPYSLHAHGLSYEKSSEGLSyddespdwfkkddavQPNGTYTYVWYANPRSGPENNGSDCR 145

                          170       180
                   ....*....|....*....|....*
gi 1776487195  883 AWAYHSTVDIIKDTYSGLIGTLVVC 907
Cdd:cd14451    146 TWAYYSAVNPEKDIHSGLIGPLLIC 170
CuRO_3_FVIII_like cd04227
The third cupredoxin domain of coagulation factor VIII and similar proteins; Factor VIII ...
 31-215 3.56e-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: 3.56e-43
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776487195   31 VTREYYIGIVETAWDYAP--GSTDiisgqrfaEEEQAEVFLKRGPQRIGSIYKKAVYTQYTNILYDVIVEKPSWLGFLGP 108
Cdd:cd04227      1 QTWEHYIAAEELDWDYAPllSSTD--------DRELQSRYLPTGPQRIGYKYKKVAFVEYTDKTFKRREAKQTEKGILGP 72

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776487195  109 IIKGEVGDSIVVHLKNFASRNYTLHPHGVKYTKENEGAFYPDNTKgfEKRDDAVKPGGQYTYTWDVTEDQGPAKGDADCI 188
Cdd:cd04227     73 LLKGEVGDQIHIMFKNTASRPYNIYPHGLTSVRPMYRSRNPAGEK--DLKTMPIGPGETFGYMWELTAEDGPTEEDPRCL 150

                          170       180
                   ....*....|....*....|....*..
gi 1776487195  189 TRVYHSHIDAPRDVASGLVGPLIICRK 215
Cdd:cd04227    151 TRLYQSTVDPERDLASGLIGPLLICKK 177
CuRO_5_FVIII_like cd04228
The fifth cupredoxin domain of coagulation factor VIII and similar proteins; Factor VIII ...
 741-909 1.18e-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: 1.18e-42
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776487195  741 HYIAAVEVEWDYSPNRTWEFERHQFHKESPGNSFlnkedafigSKYKKVVYREYTDQTFSTPKSRAEEEQHLQIQGPLIM 820
Cdd:cd04228      4 YFIAAVEVLWDYGMQRPQHFLRARDPNRGRRKSV---------PQYKKVVFREYLDGSFTQPVYRGELDEHLGILGPYIR 74

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776487195  821 SSVGDKINIVFKNLASRPYSIHAHGVKTDSSVVA-----ITNPGETKMYVWKISARSSSERDDSHCTAWAYHSTVDIIKD 895
Cdd:cd04228     75 AEVEDNIMVTFKNLASRPYSFHSSLISYEEDQRAeprgnFVQPGEVQTYSWKVLHQMAPTKQEFDCKAWAYFSNVDLEKD 154

                          170
                   ....*....|....
gi 1776487195  896 TYSGLIGTLVVCPR 909
Cdd:cd04228    155 LHSGLIGPLIICKT 168
CuRO_5_ceruloplasmin cd04225
The fifth cupredoxin domain of Ceruloplasmin; Ceruloplasmin is a multicopper oxidase essential ...
 33-215 1.31e-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: 1.31e-42
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776487195   33 REYYIGIVETAWDYAPGSTDIISGQRFAEEEQAEVFLKRGPQRIGSIYKKAVYTQYTNILYDVIVEKPS---WLGFLGPI 109
Cdd:cd04225      1 RTYYIAAEEVEWDYSPQRTWEQELHNTHEESPGNAFLNKGDKFIGSKYKKVVYREYTDDTFSVPKERTAeeeHLGILGPL 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776487195  110 IKGEVGDSIVVHLKNFASRNYTLHPHGVKytkenegafypdnTKGFEKRddAVKPGGQYTYTWDVTEDQGPAKGDADCIT 189
Cdd:cd04225     81 IHAEVGEKVKIVFKNMASRPYSIHAHGVK-------------TDSSWVA--PTEPGETQTYTWKIPERSGPGVEDSNCIS 145

                          170       180
                   ....*....|....*....|....*.
gi 1776487195  190 RVYHSHIDAPRDVASGLVGPLIICRK 215
Cdd:cd04225    146 WAYYSTVDQIKDLYSGLIGPLVICRR 171
CuRO_6_FVIII_like cd11018
The sixth cupredoxin domain of coagulation factor VIII and similar proteins; Factor VIII ...
 923-1063 3.38e-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: 3.38e-41
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776487195  923 FALLFMVFDENESWYLDENIETYSANPHLVDKENEEFLESNKMHAINGKVFGNLHGLTMHVGDEVSWYLMAMGNEIDIHT 1002
Cdd:cd11018      4 FALLFTIFDETKSWYFEENMRRNCRPPCHIQTQDPWFHINNKFHAINGYVADTLPGLVMAQHQRIRWHLLNMGSDEEIHS 83

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1776487195 1003 AHFHGHSFDYKQTGIYRADVFDLFPGTFQTVEMIPQNPGTWLLHCHVTDHIHAGMEATYTV 1063
Cdd:cd11018     84 VHFHGLPFTVRAKKEYRMGVYNLYPGVFGTVEMRPSTAGIWLVECTVGEHLLAGMSALFLV 144
CuRO_6_ceruloplasmin cd11012
The sixth cupredoxin domain of Ceruloplasmin; Ceruloplasmin is a multicopper oxidase essential ...
 584-722 4.53e-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: 4.53e-41
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776487195  584 EFFLLATVFDENLSWYLDDNILMFTLNPNEIDKDNEDFQESNKMHSINGYMYGNQPGLEMCKGDVISWHLMGLGSEVDVH 663
Cdd:cd11012      3 EFALLFLVFDENESWYLDENIKTYSDHPEKVNKEDEEFIESNKMHAINGKVFGNLQGLTMHVGDEVYWYLMGMGNEIDIH 82

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1776487195  664 GIYFSQNTFITKGT---RKDTANLFPHTFVTAIMKPDSEGIFEVSCLTTDHHRGGMKQKYKV 722
Cdd:cd11012     83 TAHFHGHSFDYKHRgvyRSDVFDLFPGTFQTVEMIPRTPGTWLLHCHVTDHIHAGMETTYTV 144
CuRO_1_Ceruloplasmin_like_1 cd04229
cupredoxin domain of ceruloplasmin homologs; Uncharacterized subfamily of ceruloplasmin ...
 739-906 1.85e-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: 1.85e-39
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776487195  739 KTHYIAAVEVEWDYSP-NRTWEFERHQFHKESPGnsfLNKEDAFIGSKYKKVVYREYTDQTFSTPKSraeEEQHLQIQGP 817
Cdd:cd04229      1 RTYYIAAEEVDWDYAPsGKNKCCLGDDLEVSTLD---SQPGPYTIGSTYTKARYREYTDNSFSTPKP---TPAYLGILGP 74

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776487195  818 LIMSSVGDKINIVFKN-LASRPYSIHAHGV-------KTDSSVVAITNPGETKMYVWKISARSSSERDDSHCTAWAYHST 889
Cdd:cd04229     75 VIRAEVGDTIKVVFKNnLDEFPVNMHPHGGlyskdneGTTDGAGDVVAPGETYTYRWIVPEDAGPGPGDPSSRLWLYHSH 154

                          170
                   ....*....|....*..
gi 1776487195  890 VDIIKDTYSGLIGTLVV 906
Cdd:cd04229    155 VDVFAHTNAGLVGPIIV 171
CuRO_1_ceruloplasmin cd04222
The first cupredoxin domain of Ceruloplasmin; Ceruloplasmin is a multicopper oxidase essential ...
 739-909 2.51e-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: 2.51e-39
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776487195  739 KTHYIAAVEVEWDYSPNRTWEFERHQFHKESPGNSFLNKEDAFIGSKYKKVVYREYTDQTFSTpksRAEEEQHLQIQGPL 818
Cdd:cd04222      1 REYYIGIRETQWDYAPSGKNLITNQTFDDDEHASVFLKRGPDRIGRVYKKAVYLQYTDDTYRT---EIEKPVWLGFLGPI 77

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776487195  819 IMSSVGDKINIVFKNLASRPYSIHAHGV-------------------KTDSSVvaitNPGETKMYVWKISARSSSERDDS 879
Cdd:cd04222     78 LKAEVGDVIVVHLKNFASRPYSLHPHGVfynkenegalypdntsgfeKADDAV----PPGGSYTYTWTVPEEQAPTKADA 153

                          170       180       190
                   ....*....|....*....|....*....|
gi 1776487195  880 HCTAWAYHSTVDIIKDTYSGLIGTLVVCPR 909
Cdd:cd04222    154 NCLTRIYHSHIDAPKDIASGLIGPLIICKK 183
CuRO_3_FVIII_like cd04227
The third cupredoxin domain of coagulation factor VIII and similar proteins; Factor VIII ...
 740-907 1.11e-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: 142.38  E-value: 1.11e-38
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776487195  740 THYIAAVEVEWDYSPnrtweferhqfHKESPGNS-----FLNKEDAFIGSKYKKVVYREYTDQTFSTPKSRAEEEQhlqI 814
Cdd:cd04227      4 EHYIAAEELDWDYAP-----------LLSSTDDRelqsrYLPTGPQRIGYKYKKVAFVEYTDKTFKRREAKQTEKG---I 69

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776487195  815 QGPLIMSSVGDKINIVFKNLASRPYSIHAHGVKTDSSVVAITN-------------PGETKMYVWKISARSSSERDDSHC 881
Cdd:cd04227     70 LGPLLKGEVGDQIHIMFKNTASRPYNIYPHGLTSVRPMYRSRNpagekdlktmpigPGETFGYMWELTAEDGPTEEDPRC 149

                          170       180
                   ....*....|....*....|....*.
gi 1776487195  882 TAWAYHSTVDIIKDTYSGLIGTLVVC 907
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 ...
 740-907 6.85e-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: 6.85e-38
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776487195  740 THYIAAVEVEWDYSPNRTWEFERHQFHKespgnsFLNKEDAFIGSKYKKVVYREYTDQTFsTPKSRAEEEQHLQIQGPLI 819
Cdd:cd14450      4 EYFIAAEEVIWDYAPSIPENMDKRYRSQ------YLDNFSNNIGKKYKKAVFTQYEDGSF-TKRLENPRPKEEGILGPVI 76

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776487195  820 MSSVGDKINIVFKNLASRPYSIHAHGVKTDSSVVAIT---------------NPGETKMYVWKISARSSSERDDSHCTAW 884
Cdd:cd14450     77 RAQVRDTIKIVFKNKASRPYSIYPHGVTVSKAAEGASyppdprgnetqnkavQPGETYTYKWNILETDEPTARDPRCLTR 156

                          170       180
                   ....*....|....*....|...
gi 1776487195  885 AYHSTVDIIKDTYSGLIGTLVVC 907
Cdd:cd14450    157 MYHSAVDITRDIASGLIGPLLIC 179
CuRO_6_FVIII_like cd11018
The sixth cupredoxin domain of coagulation factor VIII and similar proteins; Factor VIII ...
 229-367 2.30e-37

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


Pssm-ID: 259904 [Multi-domain]  Cd Length: 144  Bit Score: 137.32  E-value: 2.30e-37
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776487195  229 EFILMFSVMDENLSWYLEDNIRMYCSEPSKVDKDDEDFQESNKMHSINGYMYGYLPNLTMCVEDKVKWHLFGMGNEADIH 308
Cdd:cd11018      3 EFALLFTIFDETKSWYFEENMRRNCRPPCHIQTQDPWFHINNKFHAINGYVADTLPGLVMAQHQRIRWHLLNMGSDEEIH 82

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1776487195  309 SAYFHGQTLIER---HHRVDTINLFPATFIDALMIPRNPGEWLLSCQVNDHIEGGMQALFKV 367
Cdd:cd11018     83 SVHFHGLPFTVRakkEYRMGVYNLYPGVFGTVEMRPSTAGIWLVECTVGEHLLAGMSALFLV 144
CuRO_2_ceruloplasmin_like_2 cd11023
cupredoxin domain of ceruloplasmin homologs; Uncharacterized subfamily of ceruloplasmin ...
 929-1063 2.55e-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: 2.55e-35
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776487195  929 VFDENESWYLDENIEtysanphlvdkeneeflESNKMHAINGKVFGNLHGLTMHVGDEVSWYLMAMGNEIDIHTAHFHGH 1008
Cdd:cd11023      3 EFIENSSIFLDLNVE-----------------EAGLMHSINGYVFGNLPGVTIAKGKRVRWHLVAYGNEVDFHTPHWHGQ 65

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 1776487195 1009 SFDYKQTGiyRADVFDLFPGTFQTVEMIPQNPGTWLLHCHVTDHIHAGMEATYTV 1063
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 ...
 923-1063 6.53e-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: 6.53e-34
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776487195  923 FALLFMVFDENESWYLDENIETYSANPHLVDKEneeFLESNKMHAINGKVFgNLHGLTMHVGDEVSWYLMAMGNEIDIHT 1002
Cdd:cd14455      4 FVLLFMTFDEEKSWYYEKNRKRTCRENRVKDPN---VQDNHTFHAINGIIY-NLKGLRMYTNELVRWHLINMGGPKDLHV 79

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1776487195 1003 AHFHGHSFDYKQTGIYRADVFDLFPGTFQTVEMIPQNPGTWLLHCHVTDHIHAGMEATYTV 1063
Cdd:cd14455     80 VHFHGQTFTEKGLKDHQLGVYPLLPGSFATLEMKPSKPGLWLLETEVGESQQRGMQTLFLV 140
CuRO_5_FVIII_like cd04228
The fifth cupredoxin domain of coagulation factor VIII and similar proteins; Factor VIII ...
 32-216 2.22e-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: 2.22e-33
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776487195   32 TREYYIGIVETAWDYAPGS-------TDIISGQRfaeeeqaevflKRGPQrigsiYKKAVYTQYTNILYDVIV---EKPS 101
Cdd:cd04228      1 IRHYFIAAVEVLWDYGMQRpqhflraRDPNRGRR-----------KSVPQ-----YKKVVFREYLDGSFTQPVyrgELDE 64

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776487195  102 WLGFLGPIIKGEVGDSIVVHLKNFASRNYTLHPHGVKYtkenegafypDNTKGFEKRDDAVKPGGQYTYTWDVTEDQGPA 181
Cdd:cd04228     65 HLGILGPYIRAEVEDNIMVTFKNLASRPYSFHSSLISY----------EEDQRAEPRGNFVQPGEVQTYSWKVLHQMAPT 134

                          170       180       190
                   ....*....|....*....|....*....|....*
gi 1776487195  182 KGDADCITRVYHSHIDAPRDVASGLVGPLIICRKG 216
Cdd:cd04228    135 KQEFDCKAWAYFSNVDLEKDLHSGLIGPLIICKTG 169
CuRO_2_ceruloplasmin_like_2 cd11023
cupredoxin domain of ceruloplasmin homologs; Uncharacterized subfamily of ceruloplasmin ...
 262-367 5.50e-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: 123.49  E-value: 5.50e-33
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776487195  262 DDEDFQESNKMHSINGYMYGYLPNLTMCVEDKVKWHLFGMGNEADIHSAYFHGQTL-IERHHRVDTINLFPATFIDALMI 340
Cdd:cd11023     12 LDLNVEEAGLMHSINGYVFGNLPGVTIAKGKRVRWHLVAYGNEVDFHTPHWHGQTVeADKSRRTDVAELMPASMRVADMT 91

                           90       100
                   ....*....|....*....|....*..
gi 1776487195  341 PRNPGEWLLSCQVNDHIEGGMQALFKV 367
Cdd:cd11023     92 AADVGTWLLHCHVHDHYMAGMMTQFAV 118
CuRO_1_FVIII_like cd14452
The first cupredoxin domain of coagulation factor VIII and similar proteins; Factor VIII ...
 739-907 7.49e-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: 7.49e-33
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776487195  739 KTHYIAAVEVEWDYSPNRTWEFERHQfhKESPGNsflnkedafIGSKYKKVVYREYTDQTFSTPKSRAEeeqHLQIQGPL 818
Cdd:cd14452      1 RRYYIAAVEIGWDYIHSDLGDPASEQ--RKKPKD---------IPQKYIKAVFVEYLDATFTVPKPRPA---WMGLLGPT 66

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776487195  819 IMSSVGDKINIVFKNLASRPYSIHAHGV-------------------KTDSSVvaitNPGETKMYVWKISARSSSERDDS 879
Cdd:cd14452     67 IVAEVGDTVVITFKNLASQPYSLHAVGVsywkasegagyddstsqheKEDDAV----YPGGYHTYVWDISPKDGPTGSDP 142

                          170       180
                   ....*....|....*....|....*...
gi 1776487195  880 HCTAWAYHSTVDIIKDTYSGLIGTLVVC 907
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 ...
 227-367 4.43e-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: 4.43e-32
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776487195  227 DAEFILMFSVMDENLSWYlednirmycsepskvdkdDEDFQESNKMHSINGYMYGYLPNLTMCVEDKVKWHLFGMGNEAD 306
Cdd:cd14453      1 YKEYVLMFGVFDENKSWY------------------KQNASVDSVKYTINGYTNGTLPDVSICAYDHVSWHLLGMSSEPE 62

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1776487195  307 IHSAYFHGQTLIERHHRVDTINLFPATFIDALMIPRNPGEWLLSCQVNDHIEGGMQALFKV 367
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 ...
 229-367 5.21e-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: 5.21e-32
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776487195  229 EFILMFSVMDENLSWYLEDNIRMYCSEpskVDKDDEDFQESNKMHSINGYMYGyLPNLTMCVEDKVKWHLFGMGNEADIH 308
Cdd:cd14455      3 EFVLLFMTFDEEKSWYYEKNRKRTCRE---NRVKDPNVQDNHTFHAINGIIYN-LKGLRMYTNELVRWHLINMGGPKDLH 78

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1776487195  309 SAYFHGQTLIE---RHHRVDTINLFPATFIDALMIPRNPGEWLLSCQVNDHIEGGMQALFKV 367
Cdd:cd14455     79 VVHFHGQTFTEkglKDHQLGVYPLLPGSFATLEMKPSKPGLWLLETEVGESQQRGMQTLFLV 140
CuRO_4_FVIII_like cd11016
The fourth cupredoxin domain of coagulation factor VIII and similar proteins; Factor VIII ...
 227-370 5.53e-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: 121.90  E-value: 5.53e-32
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776487195  227 DAEFILMFSVMDENLSWYLEDNIRMYCSEPSKVDKDDEDFQESNKMHSINGYMYGYLpNLTMCVEDKVKWHLFGMGNEAD 306
Cdd:cd11016      1 DKDWSLLFSVFDENNSWYLKENIHRFTQTPAGVNDTDPDFYASNVMHTINGIVFDRR-QFVICLTDVAYWYVLSVGAQTD 79

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1776487195  307 IHSAYFHGQTLIERHHRVDTINLFPATFIDALMIPRNPGEWLLSCQVNDHIEGGMQALFKVEGC 370
Cdd:cd11016     80 FLSVFFSGNTFKHQMVYEDVLTLFPFSGETVSMSPEVPGEWELGCFNGDFRSRGMSAQYTVSTC 143
CuRO_4_FVIII_like cd11016
The fourth cupredoxin domain of coagulation factor VIII and similar proteins; Factor VIII ...
 587-725 1.08e-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: 1.08e-31
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776487195  587 LLATVFDENLSWYLDDNILMFTLNPNEIDKDNEDFQESNKMHSINGYMYGNQPgLEMCKGDVISWHLMGLGSEVDVHGIY 666
Cdd:cd11016      6 LLFSVFDENNSWYLKENIHRFTQTPAGVNDTDPDFYASNVMHTINGIVFDRRQ-FVICLTDVAYWYVLSVGAQTDFLSVF 84

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 1776487195  667 FSQNTFITKGTRKDTANLFPHTFVTAIMKPDSEGIFEVSCLTTDHHRGGMKQKYKVKPC 725
Cdd:cd11016     85 FSGNTFKHQMVYEDVLTLFPFSGETVSMSPEVPGEWELGCFNGDFRSRGMSAQYTVSTC 143
CuRO_2_FVIII_like cd11015
The second cupredoxin domain of coagulation factor VIII and similar proteins; Factor VIII ...
 229-367 3.17e-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: 3.17e-31
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776487195  229 EFILMFSVMDENLSWYLEDnirmycSEPSKVDKDDEDfQESNKMHSINGYMYGYLPNLTMCVEDKVKWHLFGMGNEADIH 308
Cdd:cd11015      3 AFVLLFAVFDEGKSWYSEV------GERKSRDKFKRA-DSRKEFHTINGYINASLPGLKICQRKPVIWHVIGMGTAPEVH 75

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 1776487195  309 SAYFHGQTLIERHHRVDTINLFPATFIDALMIPRNPGEWLLSCQVNDHIEGGMQALFKV 367
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 ...
 227-366 2.61e-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: 2.61e-30
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776487195  227 DAEFILMFSVMDENLSWYLEDNIRMYCSEPSKVDKDDEDFQESNKMHSINGYMYGYLPNLTMCVEDKVKWHLFGMGNEAD 306
Cdd:cd14454      1 DLEQHAVFAVFDENKSWYLEENINKYCSNPNNVKKDDPKFYKSNIMPTINGYAYESSAPLGFCHSEVVQWHISSVGTQDE 80

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776487195  307 IHSAYFHGQTLIERHHRVDTINLFPATFIDALMIPRNPGEWLLSCQVNDHIEGGMQALFK 366
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 ...
 590-725 1.01e-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: 1.01e-29
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776487195  590 TVFDENLSWYLDDNILMFTLNPNEIDKDNEDFQESNKMHSINGYMYGNQPGLEMCKGDVISWHLMGLGSEVDVHGIYFSQ 669
Cdd:cd14454      9 AVFDENKSWYLEENINKYCSNPNNVKKDDPKFYKSNIMPTINGYAYESSAPLGFCHSEVVQWHISSVGTQDEIITVHLSG 88

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 1776487195  670 NTFITKGTRKDTANLFPHTFVTAIMKPDSEGIFEVSCLTTDHHRGGMKQKYKVKPC 725
Cdd:cd14454     89 HTFRYKGKHEDTLNLFPMSGESITVTMDNLGTWLLGSFGSSKKSKGLRVRFTDVIC 144
CuRO_4_FVIII_like cd11016
The fourth cupredoxin domain of coagulation factor VIII and similar proteins; Factor VIII ...
 925-1064 3.98e-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: 3.98e-29
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776487195  925 LLFMVFDENESWYLDENIETYSANPHLVDKENEEFLESNKMHAINGKVFGNLHgLTMHVGDEVSWYLMAMGNEIDIHTAH 1004
Cdd:cd11016      6 LLFSVFDENNSWYLKENIHRFTQTPAGVNDTDPDFYASNVMHTINGIVFDRRQ-FVICLTDVAYWYVLSVGAQTDFLSVF 84

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776487195 1005 FHGHSFdyKQTGIYRaDVFDLFPGTFQTVEMIPQNPGTWLLHCHVTDHIHAGMEATYTVL 1064
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 ...
 583-722 4.99e-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: 4.99e-28
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776487195  583 REFFLLATVFDENLSWYLDDNILMFTLNPNEIDKDNEDFQESNKMHSINGYMYGNQPGLEMCKGDVISWHLMGLGSEVDV 662
Cdd:cd11018      2 QEFALLFTIFDETKSWYFEENMRRNCRPPCHIQTQDPWFHINNKFHAINGYVADTLPGLVMAQHQRIRWHLLNMGSDEEI 81

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1776487195  663 HGIYFSQNTFITKGT---RKDTANLFPHTFVTAIMKPDSEGIFEVSCLTTDHHRGGMKQKYKV 722
Cdd:cd11018     82 HSVHFHGLPFTVRAKkeyRMGVYNLYPGVFGTVEMRPSTAGIWLVECTVGEHLLAGMSALFLV 144
CuRO_4_FV_like cd14454
The fourth cupredoxin domain of coagulation factor V and similar proteins; Factor V is an ...
 926-1045 1.65e-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: 1.65e-27
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776487195  926 LFMVFDENESWYLDENIETYSANPHLVDKENEEFLESNKMHAINGKVFGNLHGLTMHVGDEVSWYLMAMGNEIDIHTAHF 1005
Cdd:cd14454      7 VFAVFDENKSWYLEENINKYCSNPNNVKKDDPKFYKSNIMPTINGYAYESSAPLGFCHSEVVQWHISSVGTQDEIITVHL 86

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|
gi 1776487195 1006 HGHSFDYKQTgiyRADVFDLFPGTFQTVEMIPQNPGTWLL 1045
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 ...
 741-907 2.65e-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: 2.65e-27
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776487195  741 HYIAAVEVEWDYSPnrtwefERHQFHKESPGNSFlnkedafigskyKKVVYREYtDQTFSTPKSRAEEEQHLqiqGPLIM 820
Cdd:cd04226      3 YYIAAQNIDWDYTP------QSEELRLKRSEQSF------------KKIVYREY-EEGFKKEKPADLSSGLL---GPTLR 60

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776487195  821 SSVGDKINIVFKNLASRPYSIHAHGV-------------------KTDSSVVaitnPGETKMYVWKISARSSSERDDSHC 881
Cdd:cd04226     61 AEVGDTLIVHFKNMADKPLSIHPQGIaygkksegslysdntspveKLDDAVQ----PGQEYTYVWDITEEVGPTEADPPC 136

                          170       180
                   ....*....|....*....|....*.
gi 1776487195  882 TAWAYHSTVDIIKDTYSGLIGTLVVC 907
Cdd:cd04226    137 LTYIYYSHVNMVRDFNSGLIGALLIC 162
CuRO_2_FVIII_like cd11015
The second cupredoxin domain of coagulation factor VIII and similar proteins; Factor VIII ...
 583-722 3.72e-24

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


Pssm-ID: 259901 [Multi-domain]  Cd Length: 134  Bit Score: 99.21  E-value: 3.72e-24
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776487195  583 REFFLLATVFDENLSWYLDdnilmfTLNPNEIDKDNEDfQESNKMHSINGYMYGNQPGLEMCKGDVISWHLMGLGSEVDV 662
Cdd:cd11015      2 QAFVLLFAVFDEGKSWYSE------VGERKSRDKFKRA-DSRKEFHTINGYINASLPGLKICQRKPVIWHVIGMGTAPEV 74

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776487195  663 HGIYFSQNTFITKGTRKDTANLFPHTFVTAIMKPDSEGIFEVSCLTTDHHRGGMKQKYKV 722
Cdd:cd11015     75 HSIFFEGHTFLVRTHRKVSLEISPMTFLTAQTKPATVGSFLIFCQIHSHQHDGMEAMVKV 134
CuRO_2_ceruloplasmin_like_2 cd11023
cupredoxin domain of ceruloplasmin homologs; Uncharacterized subfamily of ceruloplasmin ...
 617-722 1.02e-22

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: 94.21  E-value: 1.02e-22
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776487195  617 DNEDFQESNKMHSINGYMYGNQPGLEMCKGDVISWHLMGLGSEVDVHGIYFSQNTFITKGTRK-DTANLFPHTFVTAIMK 695
Cdd:cd11023     12 LDLNVEEAGLMHSINGYVFGNLPGVTIAKGKRVRWHLVAYGNEVDFHTPHWHGQTVEADKSRRtDVAELMPASMRVADMT 91

                           90       100
                   ....*....|....*....|....*..
gi 1776487195  696 PDSEGIFEVSCLTTDHHRGGMKQKYKV 722
Cdd:cd11023     92 AADVGTWLLHCHVHDHYMAGMMTQFAV 118
CuRO_2_FVIII_like cd11015
The second cupredoxin domain of coagulation factor VIII and similar proteins; Factor VIII ...
 923-1063 6.23e-21

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


Pssm-ID: 259901 [Multi-domain]  Cd Length: 134  Bit Score: 89.96  E-value: 6.23e-21
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776487195  923 FALLFMVFDENESWYLDenietySANPHLVDKENEEFlESNKMHAINGKVFGNLHGLTMHVGDEVSWYLMAMGNEIDIHT 1002
Cdd:cd11015      4 FVLLFAVFDEGKSWYSE------VGERKSRDKFKRAD-SRKEFHTINGYINASLPGLKICQRKPVIWHVIGMGTAPEVHS 76

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1776487195 1003 AHFHGHSFDYKQtgiYRADVFDLFPGTFQTVEMIPQNPGTWLLHCHVTDHIHAGMEATYTV 1063
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 ...
 583-722 1.41e-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: 1.41e-19
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776487195  583 REFFLLATVFDENLSWYLDDNILMFTLNPNEIDKDnedFQESNKMHSINGYMYgNQPGLEMCKGDVISWHLMGLGSEVDV 662
Cdd:cd14455      2 REFVLLFMTFDEEKSWYYEKNRKRTCRENRVKDPN---VQDNHTFHAINGIIY-NLKGLRMYTNELVRWHLINMGGPKDL 77

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1776487195  663 HGIYFSQNTFITKGTRKDTAN---LFPHTFVTAIMKPDSEGIFEVSCLTTDHHRGGMKQKYKV 722
Cdd:cd14455     78 HVVHFHGQTFTEKGLKDHQLGvypLLPGSFATLEMKPSKPGLWLLETEVGESQQRGMQTLFLV 140
Cu-oxidase_2 pfam07731
Multicopper oxidase; This entry contains many divergent copper oxidase-like domains that are ...
 963-1067 5.81e-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: 84.41  E-value: 5.81e-19
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776487195  963 NKMHAINGKVFG-NLHGLTMHVGDEVSWYLMamGNEIDIHTAHFHGHSFDYKQTGI----------------YRADVFDL 1025
Cdd:pfam07731   19 RNDWAINGLLFPpNTNVITLPYGTVVEWVLQ--NTTTGVHPFHLHGHSFQVLGRGGgpwpeedpktynlvdpVRRDTVQV 96

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|..
gi 1776487195 1026 FPGTFQTVEMIPQNPGTWLLHCHVTDHIHAGMEATYTVLPKE 1067
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 ...
 923-1059 3.81e-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: 3.81e-18
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776487195  923 FALLFMVFDENESWYldenietysanphlvdkeNEEFLESNKMHAINGKVFGNLHGLTMHVGDEVSWYLMAMGNEIDIHT 1002
Cdd:cd14453      4 YVLMFGVFDENKSWY------------------KQNASVDSVKYTINGYTNGTLPDVSICAYDHVSWHLLGMSSEPELFS 65

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 1776487195 1003 AHFHGHSFDYKQtgiYRADVFDLFPGTFQTVEMIPQNPGTWLLHCHVTDHIHAGMEA 1059
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 ...
 583-716 7.44e-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: 7.44e-18
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776487195  583 REFFLLATVFDENLSWYlddnilmftlnpneidkdNEDFQESNKMHSINGYMYGNQPGLEMCKGDVISWHLMGLGSEVDV 662
Cdd:cd14453      2 KEYVLMFGVFDENKSWY------------------KQNASVDSVKYTINGYTNGTLPDVSICAYDHVSWHLLGMSSEPEL 63

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....
gi 1776487195  663 HGIYFSQNTFITKGTRKDTANLFPHTFVTAIMKPDSEGIFEVSCLTTDHHRGGM 716
Cdd:cd14453     64 FSVHFNGQVLEQNGHKVSAVGLVSGSSTTASMTVVHTGRWLISSLIMKHLQAGM 117
CuRO_1_LCC_like cd04206
Cupredoxin domain 1 of laccase-like multicopper oxidases; including laccase, CueO, spore coat ...
 104-213 2.99e-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: 2.99e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776487195  104 GFLGPIIKGEVGDSIVVHLKN-FASRNYTLHPHGVKYTKENEGAFYPDNTKgfekrdDAVKPGGQYTYTWDVTEDQGpak 182
Cdd:cd04206     27 QFPGPTIRVKEGDTVEVTVTNnLPNEPTSIHWHGLRQPGTNDGDGVAGLTQ------CPIPPGESFTYRFTVDDQAG--- 97

                           90       100       110
                   ....*....|....*....|....*....|.
gi 1776487195  183 gdadciTRVYHSHIDAprDVASGLVGPLIIC 213
Cdd:cd04206     98 ------TFWYHSHVGG--QRADGLYGPLIVE 120
CuRO_1_LCC_like cd04206
Cupredoxin domain 1 of laccase-like multicopper oxidases; including laccase, CueO, spore coat ...
 446-567 5.18e-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: 5.18e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776487195  446 AHKKRLPEEEHLGLLGPVIKAEVGESIRVTFRNN-ASRPFSIQPHGVSYLKSNEGAlyrTASRDTESPasyVSPGASFTY 524
Cdd:cd04206     15 DGVLRQVITVNGQFPGPTIRVKEGDTVEVTVTNNlPNEPTSIHWHGLRQPGTNDGD---GVAGLTQCP---IPPGESFTY 88

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|...
gi 1776487195  525 EWNVPEDVGptdqdpdclTWFYYSAVDSVRDTnsGLVGPLLVC 567
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 ...
 967-1062 6.67e-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: 6.67e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776487195  967 AINGKVF----GNLHGLTMHVGDEVSWYLMAMGNEIDIHTAHFHGHSF------------DYKQTGIYRADVFDLFPGTF 1030
Cdd:cd04207     21 VINGMPFkegdANTDIFSVEAGDVVEIVLINAGNHDMQHPFHLHGHSFwvlgsgggpfdaPLNLTNPPWRDTVLVPPGGW 100

                           90       100       110
                   ....*....|....*....|....*....|..
gi 1776487195 1031 QTVEMIPQNPGTWLLHCHVTDHIHAGMEATYT 1062
Cdd:cd04207    101 VVIRFKADNPGVWMLHCHILEHEDAGMMTVFE 132
Cu-oxidase_3 pfam07732
Multicopper oxidase; This entry contains many divergent copper oxidase-like domains that are ...
 87-212 1.77e-12

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


Pssm-ID: 462247 [Multi-domain]  Cd Length: 119  Bit Score: 64.96  E-value: 1.77e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776487195   87 QYTNILYDVIVEKPSWL---GFLGPIIKGEVGDSIVVHLKNFASRNYTLHPHGVKYTKENEGAFYPDNTKgfekrdDAVK 163
Cdd:pfam07732    3 TYGTVSPLGGTRQAVIGvngQFPGPTIRVREGDTVVVNVTNNLDEPTSIHWHGLQQRGTPWMDGVPGVTQ------CPIP 76

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*....
gi 1776487195  164 PGGQYTYTWDVTEDQGpakgdadciTRVYHSHIDAPRdvASGLVGPLII 212
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 ...
 461-569 1.34e-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: 63.05  E-value: 1.34e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776487195  461 GPVIKAEVGESIRVTFRNNASRPFSIQPHGVSYLKSNEGALyrtasrdteSPASYVSPGASFTYEWNVPEDVGPTDQDPD 540
Cdd:cd14449     29 GPVIEVREGDTLKILFRNTLDVPASLHPHGVDYTTASDGTG---------MNASIVAPGDTRIYTWRTHGGYRRADGSWA 99

                           90       100       110
                   ....*....|....*....|....*....|....*.
gi 1776487195  541 CLT---WFYYSAV----DSVRDTNSGLVGPLLVCRK 569
Cdd:cd14449    100 EGTagyWHYHDHVfgteHGTEGLSRGLYGALIVRRV 135
CuRO_D2_2dMcoN_like cd04202
The second cupredoxin domain of bacterial two domain multicopper oxidase McoN and similar ...
 965-1057 5.66e-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: 5.66e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776487195  965 MHAINGKVFGNLHGLTMHVGDEVSWYLMAMGNeiDIHTAHFHGHSFDY--------KQTGIYRADVFDLFPGTFQTVEMI 1036
Cdd:cd04202     29 YFTINGKSFPATPPLVVKEGDRVRIRLINLSM--DHHPMHLHGHFFLVtatdggpiPGSAPWPKDTLNVAPGERYDIEFV 106

                           90       100
                   ....*....|....*....|.
gi 1776487195 1037 PQNPGTWLLHCHVTDHIHAGM 1057
Cdd:cd04202    107 ADNPGDWMFHCHKLHHAMNGM 127
CuRO_3_CumA_like cd13906
The third cupredoxin domain of CumA like multicopper oxidase; This multicopper oxidase (MCO) ...
 967-1063 1.71e-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: 1.71e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776487195  967 AINGKVFGNLHG-------LTMHVGDevsWYLMAMGNEID-IHTAHFHGHSFDY----KQTGIYR--ADVFDLFPGtfQT 1032
Cdd:cd13906     30 AINGTSWTGGDHshlppplATLKRGR---SYVLRLVNETAfLHPMHLHGHFFRVlsrnGRPVPEPfwRDTVLLGPK--ET 104

                           90       100       110
                   ....*....|....*....|....*....|...
gi 1776487195 1033 VE--MIPQNPGTWLLHCHVTDHIHAGMEATYTV 1063
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 ...
 107-215 3.16e-10

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


Pssm-ID: 259991 [Multi-domain]  Cd Length: 135  Bit Score: 59.20  E-value: 3.16e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776487195  107 GPIIKGEVGDSIVVHLKNFASRNYTLHPHGVKYTKENEGAFYPDNtkgfekrddAVKPGGQYTYTWDVTEDQGPAKGDAD 186
Cdd:cd14449     29 GPVIEVREGDTLKILFRNTLDVPASLHPHGVDYTTASDGTGMNAS---------IVAPGDTRIYTWRTHGGYRRADGSWA 99

                           90       100       110
                   ....*....|....*....|....*....|....*.
gi 1776487195  187 CITR---VYHSHI----DAPRDVASGLVGPLIICRK 215
Cdd:cd14449    100 EGTAgywHYHDHVfgteHGTEGLSRGLYGALIVRRV 135
CuRO_1_Diphenol_Ox cd13857
The first cupredoxin domain of fungal laccase, diphenol oxidase; Diphenol oxidase belongs to ...
 105-212 1.91e-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: 1.91e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776487195  105 FLGPIIKGEVGDSIVVHLKNFASRNYTLHPHGVKytkeNEGAFYPDNTKGFEKRddAVKPGGQYTYTWDVTEDQGpakgd 184
Cdd:cd13857     28 FPGPLIEANQGDRIVVHVTNELDEPTSIHWHGLF----QNGTNWMDGTAGITQC--PIPPGGSFTYNFTVDGQYG----- 96

                           90       100
                   ....*....|....*....|....*...
gi 1776487195  185 adciTRVYHSHIDAprDVASGLVGPLII 212
Cdd:cd13857     97 ----TYWYHSHYST--QYADGLVGPLIV 118
CuRO_1_CumA_like cd13861
The first cupredoxin domain of CumA like multicopper oxidase; This multicopper oxidase (MCO) ...
 458-566 2.93e-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: 2.93e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776487195  458 GLLGPVIKAEVGESIRVTFRNNASRPFSIQPHGVsylksnegalyRTASR-D-----TESPasyVSPGASFTYEWNVPeD 531
Cdd:cd13861     28 QVPGPELRVRQGDTLRVRLTNRLPEPTTIHWHGL-----------RLPNAmDgvpglTQPP---VPPGESFTYEFTPP-D 92

                           90       100       110
                   ....*....|....*....|....*....|....*
gi 1776487195  532 VGptdqdpdclTWFYYSAVDSVRDTNSGLVGPLLV 566
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 ...
 461-566 4.05e-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: 4.05e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776487195  461 GPVIKAEVGESIRVTFRNNASRPFSIQPHGVsylksnegalYRTASRDTESPAsyVSPGASFTYEWnVPEDVGptdqdpd 540
Cdd:cd11024     32 GPTLRATEGDLVRIHFINTGDHPHTIHFHGI----------HDAAMDGTGLGP--IMPGESFTYEF-VAEPAG------- 91

                           90       100
                   ....*....|....*....|....*..
gi 1776487195  541 clTWFYYSAVDSVRD-TNSGLVGPLLV 566
Cdd:cd11024     92 --THLYHCHVQPLKEhIAMGLYGAFIV 116
CuRO_3_CopA cd13896
The third cupredoxin domain of CopA copper resistance protein family; CopA is a multicopper ...
 968-1057 1.25e-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: 53.80  E-value: 1.25e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776487195  968 INGKVFGNLHGLTMHVGDEVswyLMAMGNEIDI-HTAHFHGHSFDYKQ-TGIYRA--DVFDLFPGTFQTVEMIPQNPGTW 1043
Cdd:cd13896     19 INGKAYPDADPLRVREGERV---RIVFVNDTMMaHPMHLHGHFFQVENgNGEYGPrkDTVLVPPGETVSVDFDADNPGRW 95

                           90
                   ....*....|....
gi 1776487195 1044 LLHCHVTDHIHAGM 1057
Cdd:cd13896     96 AFHCHNLYHMEAGM 109
CuRO_1_CumA_like cd13861
The first cupredoxin domain of CumA like multicopper oxidase; This multicopper oxidase (MCO) ...
 104-212 1.55e-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: 1.55e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776487195  104 GFLGPIIKGEVGDSIVVHLKNFASRNYTLHPHGVKYTKENEGAfyPDNTKgfekrdDAVKPGGQYTYTWdVTEDQGpakg 183
Cdd:cd13861     28 QVPGPELRVRQGDTLRVRLTNRLPEPTTIHWHGLRLPNAMDGV--PGLTQ------PPVPPGESFTYEF-TPPDAG---- 94

                           90       100
                   ....*....|....*....|....*....
gi 1776487195  184 dadciTRVYHSHIDAPRDVASGLVGPLII 212
Cdd:cd13861     95 -----TYWYHPHVGSQEQLDRGLYGPLIV 118
CuRO_3_CumA_like cd13906
The third cupredoxin domain of CumA like multicopper oxidase; This multicopper oxidase (MCO) ...
 295-367 1.64e-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: 1.64e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776487195  295 KWHLFGMGNEAD-IHSAYFHG----------QTLIERHHRvDTINLFPATFIDALMIPRNPGEWLLSCQVNDHIEGGMQA 363
Cdd:cd13906     55 RSYVLRLVNETAfLHPMHLHGhffrvlsrngRPVPEPFWR-DTVLLGPKETVDIAFVADNPGDWMFHCHILEHQETGMMG 133


                   ....
gi 1776487195  364 LFKV 367
Cdd:cd13906    134 VIRV 137
CuRO_1_LCC_like cd04206
Cupredoxin domain 1 of laccase-like multicopper oxidases; including laccase, CueO, spore coat ...
 813-907 2.01e-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: 2.01e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776487195  813 QIQGPLIMSSVGDKINIVFKN-LASRPYSIHAHGVKTDSS-----VVAIT----NPGETKMYVWKIsarssserDDSHCT 882
Cdd:cd04206     27 QFPGPTIRVKEGDTVEVTVTNnLPNEPTSIHWHGLRQPGTndgdgVAGLTqcpiPPGESFTYRFTV--------DDQAGT 98

                           90       100
                   ....*....|....*....|....*
gi 1776487195  883 AWaYHSTVDIikDTYSGLIGTLVVC 907
Cdd:cd04206     99 FW-YHSHVGG--QRADGLYGPLIVE 120
SufI COG2132
Multicopper oxidase with three cupredoxin domains (includes cell division protein FtsP and ...
 965-1065 2.42e-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: 2.42e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776487195  965 MHAINGKVFGNLH-GLTMHVGDEVSWYLMAMGNeiDIHTAHFHGHSF------DYKQTGIYRADVFDLFPGtfQTVEMI- 1036
Cdd:COG2132    317 VWTINGKAFDPDRpDLTVKLGERERWTLVNDTM--MPHPFHLHGHQFqvlsrnGKPPPEGGWKDTVLVPPG--ETVRILf 392

                           90       100       110
                   ....*....|....*....|....*....|.
gi 1776487195 1037 --PQNPGTWLLHCHVTDHIHAGMEATYTVLP 1065
Cdd:COG2132    393 rfDNYPGDWMFHCHILEHEDAGMMGQFEVVP 423
CuRO_3_LCC_like cd04207
Cupredoxin domain 3 of laccase-like multicopper oxidases; including laccase, CueO, spore coat ...
 274-365 4.47e-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: 4.47e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776487195  274 SING----YMYGYLPNLTMCVEDKVKWHLFGMGNEADIHSAYFHGQtlierHHRV--------------------DTINL 329
Cdd:cd04207     21 VINGmpfkEGDANTDIFSVEAGDVVEIVLINAGNHDMQHPFHLHGH-----SFWVlgsgggpfdaplnltnppwrDTVLV 95

                           90       100       110
                   ....*....|....*....|....*....|....*.
gi 1776487195  330 FPATFIDALMIPRNPGEWLLSCQVNDHIEGGMQALF 365
Cdd:cd04207     96 PPGGWVVIRFKADNPGVWMLHCHILEHEDAGMMTVF 131
CuRO_D1_2dMcoN_like cd13859
The first cupredoxin domain of bacterial two domain multicopper oxidase McoN and similar ...
 107-212 5.16e-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: 5.16e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776487195  107 GPIIKGEVGDSIVVHLKNFASRNYTLHPHGVKYTkeneGAFYPDNTKGFEKRddAVKPGGQYTYTWDVtEDQGpakgdad 186
Cdd:cd13859     31 GPLIHVKEGDDLVVHVTNNTTLPHTIHWHGVLQM----GSWKMDGVPGVTQP--AIEPGESFTYKFKA-ERPG------- 96

                           90       100
                   ....*....|....*....|....*..
gi 1776487195  187 ciTRVYHSHIDAPRDVA-SGLVGPLII 212
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 ...
 107-212 5.44e-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: 5.44e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776487195  107 GPIIKGEVGDSIVVHLKNFASRNYTLHPHGVKYTKENEGAFYPdntkgfekrddaVKPGGQYTYTWDVTedqgPAKgdad 186
Cdd:cd11024     32 GPTLRATEGDLVRIHFINTGDHPHTIHFHGIHDAAMDGTGLGP------------IMPGESFTYEFVAE----PAG---- 91

                           90       100
                   ....*....|....*....|....*...
gi 1776487195  187 ciTRVYHSHIdAP--RDVASGLVGPLII 212
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 ...
 981-1057 6.70e-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: 6.70e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776487195  981 MHVGDEVSWYLMAMGNEIDI-HTAHFHGHSFdY--KQ-TGIY-------------RADVFDLFPGTFQTVEMIPQNPGTW 1043
Cdd:cd13901     60 IELPKANKWVYIVIQNNSPLpHPIHLHGHDF-YilAQgTGTFdddgtilnlnnppRRDVAMLPAGGYLVIAFKTDNPGAW 138

                           90
                   ....*....|....
gi 1776487195 1044 LLHCHVTDHIHAGM 1057
Cdd:cd13901    139 LMHCHIAWHASGGL 152
Cu-oxidase pfam00394
Multicopper oxidase; Many of the proteins in this family contain multiple similar copies of ...
 234-370 6.96e-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: 6.96e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776487195  234 FSVMDENLSWYlEDNIRMYCSEPSKVDKDDEDFQESNKMHSINGYMYGYLPNLTMCVEDKVKWHLFgMGNEADIHSAYFH 313
Cdd:pfam00394    1 EDYVITLSDWY-HKDAKDLEKELLASGKAPTDFPPVPDAVLINGKDGASLATLTVTPGKTYRLRII-NVALDDSLNFSIE 78

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1776487195  314 GQ--TLIE---RHH---RVDTINLFPATFIDALMIP-RNPGEWLLSCQVN-DHIEGGMQALFKVEGC 370
Cdd:pfam00394   79 GHkmTVVEvdgVYVnpfTVDSLDIFPGQRYSVLVTAnQDPGNYWIVASPNiPAFDNGTAAAILRYSG 145
CuRO_1_Abr2_like cd13850
The first cupredoxin domain of a group of fungal Laccases similar to Abr2 from Aspergillus ...
 98-212 8.18e-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: 8.18e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776487195   98 EKPSWLG---FLGPIIKGEVGDSIVVHLKNFASRNYTLHPHGVkytkENEGAFYPDNTKGFEKRddAVKPGGQYTYTWDV 174
Cdd:cd13850     16 EREVILIngqFPGPPIILDEGDEVEILVTNNLPVNTTIHFHGI----LQRGTPWSDGVPGVTQW--PIQPGGSFTYRWKA 89

                           90       100       110
                   ....*....|....*....|....*....|....*....
gi 1776487195  175 TEDQGpakgdadciTRVYHSHIdapRDVAS-GLVGPLII 212
Cdd:cd13850     90 EDQYG---------LYWYHSHY---RGYYMdGLYGPIYI 116
CuRO_3_MCO_like_3 cd13909
The third cupredoxin domain of uncharacterized multicopper oxidase; Multicopper Oxidases (MCOs) ...
 1001-1057 8.88e-08

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


Pssm-ID: 259976 [Multi-domain]  Cd Length: 137  Bit Score: 52.14  E-value: 8.88e-08
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1776487195 1001 HTAHFHGHSF-----DYkQTGIYRaDVFDLFPGTFQTVEMIPQNPGTWLLHCHVTDHIHAGM 1057
Cdd:cd13909     71 HGMHLHGHHFrailpNG-ALGPWR-DTLLMDRGETREIAFVADNPGDWLLHCHMLEHAAAGM 130
CuRO_3_McoC_like cd13902
The third cupredoxin domain of a multicopper oxidase McoC and similar proteins; This family ...
 965-1063 9.66e-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: 9.66e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776487195  965 MHAINGKVFG-NLHGLTMHVGDEVSWYLMamgNEIDI-HTAHFHGHSF------DYKQTGIYRA--DVFDLFPGTFQTVE 1034
Cdd:cd13902     20 MFLINGKTFDmNRIDFVAKVGEVEVWEVT---NTSHMdHPFHLHGTQFqvleidGNPQKPEYRAwkDTVNLPPGEAVRIA 96

                           90       100
                   ....*....|....*....|....*....
gi 1776487195 1035 MIPQNPGTWLLHCHVTDHIHAGMEATYTV 1063
Cdd:cd13902     97 TRQDDPGMWMYHCHILEHEDAGMMGMLHV 125
SufI COG2132
Multicopper oxidase with three cupredoxin domains (includes cell division protein FtsP and ...
 105-235 1.26e-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: 1.26e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776487195  105 FLGPIIKGEVGDSIVVHLKNFASRNYTLHPHGVKYTKENEGafYPdntkgfekrDDAVKPGGQYTYTWDVteDQGPAkgd 184
Cdd:COG2132     42 YPGPTIRVREGDRVRVRVTNRLPEPTTVHWHGLRVPNAMDG--VP---------GDPIAPGETFTYEFPV--PQPAG--- 105

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 1776487195  185 adciTRVYHSHIDA--PRDVASGLVGPLIIcrkgamNKDNDKY--VDAEFILMFS 235
Cdd:COG2132    106 ----TYWYHPHTHGstAEQVYRGLAGALIV------EDPEEDLprYDRDIPLVLQ 150
CuRO_3_Fet3p cd13899
The third Cupredoxin domain of multicopper oxidase Fet3p; Fet3p catalyzes the ferroxidase ...
 1001-1065 1.83e-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: 1.83e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776487195 1001 HTAHFHGHSFD--YKQTGIY----------------RADVFDLFPGTFQTVEMIPQNPGTWLLHCHVTDHIHAGMEATYT 1062
Cdd:cd13899     78 HPFHLHGHKFQvvQRSPDVAsddpnppinefpenpmRRDTVMVPPGGSVVIRFRADNPGVWFFHCHIEWHLEAGLAATFI 157


                   ...
gi 1776487195 1063 VLP 1065
Cdd:cd13899    158 EAP 160
CuRO_1_2DMCO_NIR_like_2 cd14449
The cupredoxin domain 1 of a two-domain laccase related to nitrite reductase; The two-domain ...
 814-890 1.94e-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: 51.11  E-value: 1.94e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776487195  814 IQGPLIMSSVGDKINIVFKNLASRPYSIHAHGVKTD-SSVVAITN-----PGETKMYVWKiSARSSSERDDSHCTA---- 883
Cdd:cd14449     27 VPGPVIEVREGDTLKILFRNTLDVPASLHPHGVDYTtASDGTGMNasivaPGDTRIYTWR-THGGYRRADGSWAEGtagy 105


                   ....*..
gi 1776487195  884 WAYHSTV 890
Cdd:cd14449    106 WHYHDHV 112
CuRO_3_MCO_like_2 cd13908
The third cupredoxin domain of uncharacterized multicopper oxidase; Multicopper Oxidases (MCOs) ...
 939-1059 2.02e-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: 2.02e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776487195  939 DENIE-TYSANPHLVDKENeeflesnkMHAINGKVFGNLHG-LTMHVGDEvswYLMAMGNEI-DIHTAHFHGHSF----- 1010
Cdd:cd13908      1 DETIDmTFEKRNAGDGGFN--------LWTINGKSYPDEDPpLVVQQGRR---YRLVFRNASdDAHPMHLHRHTFevtri 69

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*....
gi 1776487195 1011 DYKQTGIYRADVFDLFPGTFQTVEMIPQNPGTWLLHCHVTDHIHAGMEA 1059
Cdd:cd13908     70 DGKPTSGLRKDVVMLGGYQRVEVDFVADNPGLTLFHCHQQLHMDYGFMA 118
CuRO_1_AAO cd13845
The first cupredoxin domain of plant Ascorbate oxidase; Ascorbate oxidase catalyzes the ...
 104-212 2.03e-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: 2.03e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776487195  104 GFLGPIIKGEVGDSIVVHLKN-FASRNYTLHPHGVKytkeNEGAFYPDNTKGFEKRddAVKPGGQYTYTWDVteDQgPAk 182
Cdd:cd13845     27 QFPGPTIRATAGDTIVVELENkLPTEGVAIHWHGIR----QRGTPWADGTASVSQC--PINPGETFTYQFVV--DR-PG- 96

                           90       100       110
                   ....*....|....*....|....*....|
gi 1776487195  183 gdadciTRVYHSHIDAPRdvASGLVGPLII 212
Cdd:cd13845     97 ------TYFYHGHYGMQR--SAGLYGSLIV 118
CuRO_1_MaLCC_like cd13854
The first cupredoxin domain of the fungal laccases similar to Ma-LCC from Melanocarpus ...
 107-212 2.08e-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: 2.08e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776487195  107 GPIIKGEVGDSIVVHLKNFASRNYT-LHPHGV--KYTKENEGAfyPDNTKGfekrddAVKPGGQYTYTWDVTEdQGpakg 183
Cdd:cd13854     33 GPLIEANWGDTIEVTVINKLQDNGTsIHWHGIrqLNTNWQDGV--PGVTEC------PIAPGDTRTYRFRATQ-YG---- 99

                           90       100
                   ....*....|....*....|....*....
gi 1776487195  184 dadciTRVYHSHIDAprDVASGLVGPLII 212
Cdd:cd13854    100 -----TSWYHSHYSA--QYGDGVVGPIVI 121
PLN02191 PLN02191
L-ascorbate oxidase
 105-235 3.07e-07

L-ascorbate oxidase


Pssm-ID: 177843 [Multi-domain]  Cd Length: 574  Bit Score: 54.63  E-value: 3.07e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776487195  105 FLGPIIKGEVGDSIVVHLKN-FASRNYTLHPHGVKytkeNEGAFYPDNTKGFEKRddAVKPGGQYTYTWDVtEDQGpakg 183
Cdd:PLN02191    51 FPGPTIDAVAGDTIVVHLTNkLTTEGLVIHWHGIR----QKGSPWADGAAGVTQC--AINPGETFTYKFTV-EKPG---- 119

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|..
gi 1776487195  184 dadciTRVYHSHIDAPRdvASGLVGPLIIcrKGAMNKDNDKYVDAEFILMFS 235
Cdd:PLN02191   120 -----THFYHGHYGMQR--SAGLYGSLIV--DVAKGPKERLRYDGEFNLLLS 162
ascorbase TIGR03388
L-ascorbate oxidase, plant type; Members of this protein family are the copper-containing ...
 105-235 5.99e-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: 5.99e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776487195  105 FLGPIIKGEVGDSIVVHLKN-FASRNYTLHPHGVKytkeNEGAFYPDNTKGFEKRddAVKPGGQYTYTWdVTEDQGpakg 183
Cdd:TIGR03388   29 FPGPTIRAQAGDTIVVELTNkLHTEGVVIHWHGIR----QIGTPWADGTAGVTQC--AINPGETFIYNF-VVDRPG---- 97

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|..
gi 1776487195  184 dadciTRVYHSHIDAPRdvASGLVGPLIIcRKGAMNKDNDKYvDAEFILMFS 235
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 ...
 107-212 6.52e-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: 6.52e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776487195  107 GPIIKGEVGDSIVVHLKNFASRNYTLHPHGVKYTKENEGAfyPDNTKgfekrdDAVKPGGQYTYTWDVTEdQGpakgdad 186
Cdd:cd13860     31 GPTIEVTEGDRVRILVTNELPEPTTVHWHGLPVPNGMDGV--PGITQ------PPIQPGETFTYEFTAKQ-AG------- 94

                           90       100
                   ....*....|....*....|....*.
gi 1776487195  187 ciTRVYHSHIDAPRDVASGLVGPLII 212
Cdd:cd13860     95 --TYMYHSHVDEAKQEDMGLYGAFIV 118
CuRO_D2_2dMcoN_like cd04202
The second cupredoxin domain of bacterial two domain multicopper oxidase McoN and similar ...
 227-368 9.25e-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: 9.25e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776487195  227 DAEFILMFSvmdenlSWYLEDNirmycSEPSKVDKDDEDFqesnkmHSINGYMYGYLPNLTMCVEDKVKWHLFGMGNeaD 306
Cdd:cd04202      1 DRDYTLVLQ------EWFVDPG-----TTPMPPEGMDFNY------FTINGKSFPATPPLVVKEGDRVRIRLINLSM--D 61

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1776487195  307 IHSAYFHGQT---------LIERHHRV--DTINLFPATFIDALMIPRNPGEWLLSCQVNDHIE----GGMQALFKVE 368
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; ...
 995-1057 1.48e-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: 1.48e-06
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1776487195  995 GNEIDIHTAHFHGHSFDYKQ---TGIY------RADVFDL-FPGTFQTVEMIPQNPGTWLLHCHVTDHIHAGM 1057
Cdd:cd13903     67 GAIGGPHPFHLHGHAFSVVRsagSNTYnyvnpvRRDVVSVgTPGDGVTIRFVTDNPGPWFLHCHIDWHLEAGL 139
Cu-oxidase_3 pfam07732
Multicopper oxidase; This entry contains many divergent copper oxidase-like domains that are ...
 459-566 1.96e-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: 48.01  E-value: 1.96e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776487195  459 LLGPVIKAEVGESIRVTFRNNASRPFSIQPHGVSYLKSNE--GALYrtasrDTESPasyVSPGASFTYEWNVPEDVGptd 536
Cdd:pfam07732   24 FPGPTIRVREGDTVVVNVTNNLDEPTSIHWHGLQQRGTPWmdGVPG-----VTQCP---IPPGQSFTYRFQVKQQAG--- 92

                           90       100       110
                   ....*....|....*....|....*....|
gi 1776487195  537 qdpdclTWFYYSAVDSVRdtNSGLVGPLLV 566
Cdd:pfam07732   93 ------TYWYHSHTSGQQ--AAGLAGAIII 114
CuRO_3_AAO cd13893
The third cupredoxin domain of plant Ascorbate oxidase; Ascorbate oxidase catalyzes the ...
 996-1057 1.99e-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: 1.99e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776487195  996 NEIDIHTAHFHGHSF---DYKqTGIYRA---------------DVFDLFPGTFQTVEMIPQNPGTWLLHCHVTDHIHAGM 1057
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 ...
 1001-1066 3.00e-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: 3.00e-06
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1776487195 1001 HTAHFHGhSFDYKQTGIYRADVFdlfPGTFQTVEMIPQNPGTWLLHCHV---TDHIHAGMEATYTVLPK 1066
Cdd:cd11024     55 HTIHFHG-IHDAAMDGTGLGPIM---PGESFTYEFVAEPAGTHLYHCHVqplKEHIAMGLYGAFIVDPK 119
PLN02191 PLN02191
L-ascorbate oxidase
 999-1057 5.42e-06

L-ascorbate oxidase


Pssm-ID: 177843 [Multi-domain]  Cd Length: 574  Bit Score: 50.40  E-value: 5.42e-06
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1776487195  999 DIHTAHFHGHSF--------------DYKQTGIYRADVFD---LFPGTFQTVEMIPQNPGTWLLHCHVTDHIHAGM 1057
Cdd:PLN02191   465 EIHPWHLHGHDFwvlgygdgkfkpgiDEKTYNLKNPPLRNtaiLYPYGWTAIRFVTDNPGVWFFHCHIEPHLHMGM 540
CuRO_1_Diphenol_Ox cd13857
The first cupredoxin domain of fungal laccase, diphenol oxidase; Diphenol oxidase belongs to ...
 461-566 6.20e-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: 6.20e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776487195  461 GPVIKAEVGESIRVTFRNNASRPFSIQPHGvsyLKSNEGALYRTASRDTESPasyVSPGASFTYEWNVPEDVGptdqdpd 540
Cdd:cd13857     30 GPLIEANQGDRIVVHVTNELDEPTSIHWHG---LFQNGTNWMDGTAGITQCP---IPPGGSFTYNFTVDGQYG------- 96

                           90       100
                   ....*....|....*....|....*..
gi 1776487195  541 clTWFYYSAVDSvrdTNS-GLVGPLLV 566
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; ...
 105-212 6.76e-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: 6.76e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776487195  105 FLGPIIKGEVGDSIVVHLKNFAS-----RNYTLHPHGVKYTKENegafYPDNTKGFEKRddAVKPGGQYTYTWDVTEDQG 179
Cdd:cd13856     28 FPGPLITANKGDTFRITVVNQLTdptmrRSTSIHWHGIFQHGTN----YADGPAFVTQC--PIAPNHSFTYDFTAGDQAG 101

                           90       100       110
                   ....*....|....*....|....*....|...
gi 1776487195  180 pakgdadciTRVYHSHIDAprDVASGLVGPLII 212
Cdd:cd13856    102 ---------TFWYHSHLST--QYCDGLRGPLVI 123
CuRO_1_CuNIR_like cd04201
Cupredoxin domain 1 of Copper-containing nitrite reductase and two-domain laccase; ...
 969-1066 1.01e-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: 1.01e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776487195  969 NGKVFGNLhgLTMHVGDEVSWYLMAMGNEIDIHTAHFHGHSfdyKQTGIYRADVFDlfPGTFQTVEMIPQNPGTWLLHCH 1048
Cdd:cd04201     27 DGDIPGPM--LRVREGDTVELHFSNNPSSTMPHNIDFHAAT---GAGGGAGATFIA--PGETSTFSFKATQPGLYVYHCA 99

                           90       100
                   ....*....|....*....|.
gi 1776487195 1049 VTD---HIHAGMEATYTVLPK 1066
Cdd:cd04201    100 VAPvpmHIANGMYGLILVEPK 120
CuRO_1_LCC_plant cd13849
The first cupredoxin domain of plant laccases; Laccase is a blue multicopper oxidase (MCO) ...
 105-212 1.08e-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: 1.08e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776487195  105 FLGPIIKGEVGDSIVVHLKNFASRNYTLHPHGVKYTKENegafYPDNTKGFEKRddAVKPGGQYTYTWDVTEDQGpakgd 184
Cdd:cd13849     26 FPGPTIRVHEGDTVVVNVTNRSPYNITIHWHGIRQLRSG----WADGPAYITQC--PIQPGQSYTYRFTVTGQEG----- 94

                           90       100
                   ....*....|....*....|....*...
gi 1776487195  185 adciTRVYHSHIDAPRdvaSGLVGPLII 212
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, ...
 105-212 1.73e-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: 1.73e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776487195  105 FLGPIIKGEVGDSIVVHLKNFASRNYTLHPHGVKYTKENEGAfyPDNTkgfekrddaVKPGGQYTYTWDVteDQGPAkgd 184
Cdd:cd04232     29 YLGPTIRVKKGDTVRINVTNNLDEETTVHWHGLHVPGEMDGG--PHQP---------IAPGQTWSPTFTI--DQPAA--- 92

                           90       100       110
                   ....*....|....*....|....*....|
gi 1776487195  185 adciTRVYHSHIDA--PRDVASGLVGPLII 212
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; ...
 461-566 1.79e-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: 45.41  E-value: 1.79e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776487195  461 GPVIKAEVGESIRVTFRNNAS-----RPFSIQPHGVSYLKSN--EGALYRTasrdtESPasyVSPGASFTYEWNVPEDVG 533
Cdd:cd13856     30 GPLITANKGDTFRITVVNQLTdptmrRSTSIHWHGIFQHGTNyaDGPAFVT-----QCP---IAPNHSFTYDFTAGDQAG 101

                           90       100       110
                   ....*....|....*....|....*....|...
gi 1776487195  534 ptdqdpdclTWFYYSAVDSvrDTNSGLVGPLLV 566
Cdd:cd13856    102 ---------TFWYHSHLST--QYCDGLRGPLVI 123
CuRO_1_2dMco_1 cd13860
The first cupredoxin domain of bacteria two domain multicopper oxidase; This subfamily ...
 461-566 2.46e-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: 2.46e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776487195  461 GPVIKAEVGESIRVTFRNNASRPFSIQPHGVSYLKSNEGalyrtASRDTESPasyVSPGASFTYEWNVpEDVGptdqdpd 540
Cdd:cd13860     31 GPTIEVTEGDRVRILVTNELPEPTTVHWHGLPVPNGMDG-----VPGITQPP---IQPGETFTYEFTA-KQAG------- 94

                           90       100
                   ....*....|....*....|....*.
gi 1776487195  541 clTWFYYSAVDSVRDTNSGLVGPLLV 566
Cdd:cd13860     95 --TYMYHSHVDEAKQEDMGLYGAFIV 118
SufI COG2132
Multicopper oxidase with three cupredoxin domains (includes cell division protein FtsP and ...
 459-588 3.23e-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: 3.23e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776487195  459 LLGPVIKAEVGESIRVTFRNNASRPFSIQPHGVsylksnegalyRTASRDTESPASYVSPGASFTYEWNVPEDVGptdqd 538
Cdd:COG2132     42 YPGPTIRVREGDRVRVRVTNRLPEPTTVHWHGL-----------RVPNAMDGVPGDPIAPGETFTYEFPVPQPAG----- 105

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|..
gi 1776487195  539 pdclTWFYYSAVD--SVRDTNSGLVGPLLVCRKGALLPsakqrSVTREFFLL 588
Cdd:COG2132    106 ----TYWYHPHTHgsTAEQVYRGLAGALIVEDPEEDLP-----RYDRDIPLV 148
CuRO_1_Fet3p cd13851
The first Cupredoxin domain of multicopper oxidase Fet3P; Fet3p catalyzes the ferroxidase ...
 108-212 3.97e-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: 3.97e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776487195  108 PIIKGEVGDSIVVHLKN-FASRNYTLHPHGV--KYTKENEGAFY----PdntkgfekrddaVKPGGQYTYTWDVTEDQGp 180
Cdd:cd13851     32 PPIEVNKGDTVVIHATNsLGDQPTSLHFHGLfqNGTNYMDGPVGvtqcP------------IPPGQSFTYEFTVDTQVG- 98

                           90       100       110
                   ....*....|....*....|....*....|..
gi 1776487195  181 akgdadciTRVYHSHIDAprDVASGLVGPLII 212
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 ...
 813-906 4.68e-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: 4.68e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776487195  813 QIQGPLIMSSVGDKINIVFKNLASRPYSIHAHGV----KTDSSVVAITNPGETKMYVWKISArssserdDSHCTAWAY-H 887
Cdd:cd13855     29 SVPGPLIEVFEGDTVEITFRNRLPEPTTVHWHGLpvppDQDGNPHDPVAPGNDRVYRFTLPQ-------DSAGTYWYHpH 101

                           90
                   ....*....|....*....
gi 1776487195  888 STVDIIKDTYSGLIGTLVV 906
Cdd:cd13855    102 PHGHTAEQVYRGLAGAFVV 120
CuRO_1_2dMco_1 cd13860
The first cupredoxin domain of bacteria two domain multicopper oxidase; This subfamily ...
 813-906 5.04e-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: 5.04e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776487195  813 QIQGPLIMSSVGDKINIVFKNLASRPYSIHAHGVKTDSS---VVAITN----PGETKMYVWKISArssserddsHCTAWa 885
Cdd:cd13860     28 SVPGPTIEVTEGDRVRILVTNELPEPTTVHWHGLPVPNGmdgVPGITQppiqPGETFTYEFTAKQ---------AGTYM- 97

                           90       100
                   ....*....|....*....|.
gi 1776487195  886 YHSTVDIIKDTYSGLIGTLVV 906
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 ...
 813-867 5.32e-05

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


Pssm-ID: 259910 [Multi-domain]  Cd Length: 119  Bit Score: 43.80  E-value: 5.32e-05
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 1776487195  813 QIQGPLIMSSVGDKINIVFKNLASRPYSIHAHGV---KTDSSVVAITNPGETKMYVWK 867
Cdd:cd11024     29 TVPGPTLRATEGDLVRIHFINTGDHPHTIHFHGIhdaAMDGTGLGPIMPGESFTYEFV 86
CuRO_D1_2dMcoN_like cd13859
The first cupredoxin domain of bacterial two domain multicopper oxidase McoN and similar ...
 813-906 7.88e-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: 7.88e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776487195  813 QIQGPLIMSSVGDKINIVFKNLASRPYSIHAHGV-KTDS----SVVAITN----PGETKMYVWKIsarssserdDSHCTA 883
Cdd:cd13859     28 QVPGPLIHVKEGDDLVVHVTNNTTLPHTIHWHGVlQMGSwkmdGVPGVTQpaiePGESFTYKFKA---------ERPGTL 98

                           90       100
                   ....*....|....*....|....
gi 1776487195  884 WaYHSTVDIIK-DTYSGLIGTLVV 906
Cdd:cd13859     99 W-YHCHVNVNEhVGMRGMWGPLIV 121
CuRO_1_Diphenol_Ox cd13857
The first cupredoxin domain of fungal laccase, diphenol oxidase; Diphenol oxidase belongs to ...
 813-906 8.87e-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: 8.87e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776487195  813 QIQGPLIMSSVGDKINIVFKNLASRPYSIHAHGVKTDSS-----VVAITN----PGETKMYVWKIsarssserDDSHCTA 883
Cdd:cd13857     27 QFPGPLIEANQGDRIVVHVTNELDEPTSIHWHGLFQNGTnwmdgTAGITQcpipPGGSFTYNFTV--------DGQYGTY 98

                           90       100
                   ....*....|....*....|....
gi 1776487195  884 WaYHSTVDIikdTYS-GLIGTLVV 906
Cdd:cd13857     99 W-YHSHYST---QYAdGLVGPLIV 118
CuRO_3_LCC_plant cd13897
The third cupredoxin domain of the plant laccases; Laccase is a blue multicopper oxidase (MCO) ...
 999-1063 2.03e-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: 42.63  E-value: 2.03e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776487195  999 DIHTAHFHGHSFdY---KQTGIYRA--DV--FDLF-PGTFQTVeMIPQ-----------NPGTWLLHCHVTDHIHAGMEA 1059
Cdd:cd13897     55 ENHPMHLHGFDF-YvvgRGFGNFDPstDPatFNLVdPPLRNTV-GVPRggwaairfvadNPGVWFMHCHFERHTSWGMAT 132


                   ....
gi 1776487195 1060 TYTV 1063
Cdd:cd13897    133 VFIV 136
CuRO_1_McoC_like cd13855
The first cupredoxin domain of a multicopper oxidase McoC and similar proteins; This family ...
 458-531 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 1776487195  458 GLLGPVIKAEVGESIRVTFRNNASRPFSIQPHGVSYLKSNEGalyrtasrdteSPASYVSPGASFTYEWNVPED 531
Cdd:cd13855     29 SVPGPLIEVFEGDTVEITFRNRLPEPTTVHWHGLPVPPDQDG-----------NPHDPVAPGNDRVYRFTLPQD 91
CuRO_1_CuNIR cd11020
Cupredoxin domain 1 of Copper-containing nitrite reductase; Copper-containing nitrite ...
 813-909 2.25e-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: 2.25e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776487195  813 QIQGPLIMSSVGDKINIVFKNLASR--PYSIHAHGVKTDSSVVAIT-NPGETKMYVWKisARssserddsHCTAWAYH-S 888
Cdd:cd11020     29 QVPGPVIRVREGDTVELTLTNPGTNtmPHSIDFHAATGPGGGEFTTiAPGETKTFSFK--AL--------YPGVFMYHcA 98

                           90       100
                   ....*....|....*....|.
gi 1776487195  889 TVDIIKDTYSGLIGTLVVCPR 909
Cdd:cd11020     99 TAPVLMHIANGMYGAIIVEPK 119
CuRO_3_tcLLC2_insect_like cd13905
The third cupredoxin domain of the insect laccases similar to laccase 2 in Tribolium castaneum; ...
 984-1058 2.40e-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: 2.40e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776487195  984 GDEVSWYLMAMGNEIDI-HTAHFHGHSF--------DY-KQTGIY--------RADVFDLFPGTFQ------TVeMIP-- 1037
Cdd:cd13905     52 NSVVEIVLINEGPGPGLsHPFHLHGHSFyvlgmgfpGYnSTTGEIlsqnwnnkLLDRGGLPGRNLVnpplkdTV-VVPng 130

                           90       100       110
                   ....*....|....*....|....*....|
gi 1776487195 1038 ---------QNPGTWLLHCHVTDHIHAGME 1058
Cdd:cd13905    131 gyvvirfraDNPGYWLLHCHIEFHLLEGMA 160
Cu-oxidase_2 pfam07731
Multicopper oxidase; This entry contains many divergent copper oxidase-like domains that are ...
 265-368 2.56e-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: 42.42  E-value: 2.56e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776487195  265 DFQESNKMHSINGYMYGYLPN-LTMCVEDKVKWHLFGMGNeaDIHSAYFHGQT--LIERHH-----------------RV 324
Cdd:pfam07731   14 SGNFRRNDWAINGLLFPPNTNvITLPYGTVVEWVLQNTTT--GVHPFHLHGHSfqVLGRGGgpwpeedpktynlvdpvRR 91

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....
gi 1776487195  325 DTINLFPATFIDALMIPRNPGEWLLSCQVNDHIEGGMQALFKVE 368
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 ...
 968-1057 5.48e-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: 41.08  E-value: 5.48e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776487195  968 INGKVFG-NLHGLTMHVGDEVSWYLMAMGNEIdiHTAHFHGHSF-------DYKQTGIYRaDVFDLFPGTFQTVEMIPQN 1039
Cdd:cd13900     22 INGKPFDpDRPDRTVRLGTVEEWTLINTSGED--HPFHIHVNPFqvvsingKPGLPPVWR-DTVNVPAGGSVTIRTRFRD 98

                           90
                   ....*....|....*....
gi 1776487195 1040 P-GTWLLHCHVTDHIHAGM 1057
Cdd:cd13900     99 FtGEFVLHCHILDHEDQGM 117
CuRO_1_MaLCC_like cd13854
The first cupredoxin domain of the fungal laccases similar to Ma-LCC from Melanocarpus ...
 813-906 7.05e-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: 7.05e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776487195  813 QIQGPLIMSSVGDKINI-VFKNLASRPYSIHAHGVK-----TDSSVVAITN----PGETKMYVWKIsarssserdDSHCT 882
Cdd:cd13854     30 QYPGPLIEANWGDTIEVtVINKLQDNGTSIHWHGIRqlntnWQDGVPGVTEcpiaPGDTRTYRFRA---------TQYGT 100

                           90       100
                   ....*....|....*....|....*
gi 1776487195  883 AWaYHSTVDIikdTYS-GLIGTLVV 906
Cdd:cd13854    101 SW-YHSHYSA---QYGdGVVGPIVI 121
Cu-oxidase pfam00394
Multicopper oxidase; Many of the proteins in this family contain multiple similar copies of ...
 929-1061 7.07e-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: 7.07e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776487195  929 VFDENESWYlDENIETYSANPHLVDKENEEF-LESNKmHAINGKVFGNLHGLTMHVGDEVSWYLmAMGNEIDIHTAHFHG 1007
Cdd:pfam00394    3 YVITLSDWY-HKDAKDLEKELLASGKAPTDFpPVPDA-VLINGKDGASLATLTVTPGKTYRLRI-INVALDDSLNFSIEG 79

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1776487195 1008 HSF-----DYKQTGIYRADVFDLFPGTFQTVeMI--PQNPGTWLLHCHVT-DHIHAGMEATY 1061
Cdd:pfam00394   80 HKMtvvevDGVYVNPFTVDSLDIFPGQRYSV-LVtaNQDPGNYWIVASPNiPAFDNGTAAAI 140
CuRO_D1_2dMcoN_like cd13859
The first cupredoxin domain of bacterial two domain multicopper oxidase McoN and similar ...
 461-566 8.97e-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: 8.97e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776487195  461 GPVIKAEVGESIRVTFRNNASRPFSIQPHGVSYLKS--NEGAlyrtasRDTESPAsyVSPGASFTYEWNVpedvgptdqD 538
Cdd:cd13859     31 GPLIHVKEGDDLVVHVTNNTTLPHTIHWHGVLQMGSwkMDGV------PGVTQPA--IEPGESFTYKFKA---------E 93

                           90       100
                   ....*....|....*....|....*...
gi 1776487195  539 PDCLTWFYYSAVDSVRDTNSGLVGPLLV 566
Cdd:cd13859     94 RPGTLWYHCHVNVNEHVGMRGMWGPLIV 121
Cupredoxin cd00920
Cupredoxin superfamily; Cupredoxins contain type I copper centers and are involved in ...
 969-1060 1.70e-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: 1.70e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776487195  969 NGKVFGNLHgLTMHVGDEVSWYLMAMGNEIdiHTAHFHGHSFDY-KQTGIYRAD-VFDLFPGTFQTVEMI--PQNPGTWL 1044
Cdd:cd00920     16 GVLLFGPPV-LVVPVGDTVRVQFVNKLGEN--HSVTIAGFGVPVvAMAGGANPGlVNTLVIGPGESAEVTftTDQAGVYW 92

                           90
                   ....*....|....*.
gi 1776487195 1045 LHCHVTDHIHAGMEAT 1060
Cdd:cd00920     93 FYCTIPGHNHAGMVGT 108
CuRO_3_MCO_like_4 cd13910
The third cupredoxin domain of uncharacterized multicopper oxidase; Multicopper Oxidases (MCOs) ...
 1001-1057 2.77e-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: 2.77e-03
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1776487195 1001 HTAHFHGHSF-------DYKQTGIYRADVFDLFPGTFQ----TVEmIPQ-----------NPGTWLLHCHVTDHIHAGM 1057
Cdd:cd13910     83 HPFHLHGHKFwvlgsgdGRYGGGGYTAPDGTSLNTTNPlrrdTVS-VPGfgwavlrfvadNPGLWAFHCHILWHMAAGM 160
SufI COG2132
Multicopper oxidase with three cupredoxin domains (includes cell division protein FtsP and ...
 816-906 2.94e-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: 2.94e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776487195  816 GPLIMSSVGDKINIVFKNLASRPYSIHAHGVKTDSS----VVAITNPGETKMYVWKIsarssserDDSHCTAWaYHSTVD 891
Cdd:COG2132     44 GPTIRVREGDRVRVRVTNRLPEPTTVHWHGLRVPNAmdgvPGDPIAPGETFTYEFPV--------PQPAGTYW-YHPHTH 114

                           90
                   ....*....|....*..
gi 1776487195  892 II--KDTYSGLIGTLVV 906
Cdd:COG2132    115 GStaEQVYRGLAGALIV 131
CuRO_1_Fet3p cd13851
The first Cupredoxin domain of multicopper oxidase Fet3P; Fet3p catalyzes the ferroxidase ...
 462-566 3.03e-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: 3.03e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776487195  462 PVIKAEVGESIRVTFRNN-ASRPFSIQPHGVSYLKSNEgalYRTASRDTESPasyVSPGASFTYEWNVPEDVGptdqdpd 540
Cdd:cd13851     32 PPIEVNKGDTVVIHATNSlGDQPTSLHFHGLFQNGTNY---MDGPVGVTQCP---IPPGQSFTYEFTVDTQVG------- 98

                           90       100
                   ....*....|....*....|....*.
gi 1776487195  541 clTWFYYSAVDSvrDTNSGLVGPLLV 566
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 ...
 107-212 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 1776487195  107 GPIIKGEVGDSIVVHLKNFASRNYTLHPHGVKYTKENEGafypdntkgfeKRDDAVKPGGQYTYTWDVTEDQGPakgdad 186
Cdd:cd13855     32 GPLIEVFEGDTVEITFRNRLPEPTTVHWHGLPVPPDQDG-----------NPHDPVAPGNDRVYRFTLPQDSAG------ 94

                           90       100
                   ....*....|....*....|....*...
gi 1776487195  187 ciTRVY--HSHIDAPRDVASGLVGPLII 212
Cdd:cd13855     95 --TYWYhpHPHGHTAEQVYRGLAGAFVV 120
CuRO_1_CumA_like cd13861
The first cupredoxin domain of CumA like multicopper oxidase; This multicopper oxidase (MCO) ...
 813-906 3.13e-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: 3.13e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776487195  813 QIQGPLIMSSVGDKINIVFKNLASRPYSIHAHGVKTDSS---VVAIT----NPGETKMYVWKIsarssserDDSHcTAWa 885
Cdd:cd13861     28 QVPGPELRVRQGDTLRVRLTNRLPEPTTIHWHGLRLPNAmdgVPGLTqppvPPGESFTYEFTP--------PDAG-TYW- 97

                           90       100
                   ....*....|....*....|.
gi 1776487195  886 YHSTVDIIKDTYSGLIGTLVV 906
Cdd:cd13861     98 YHPHVGSQEQLDRGLYGPLIV 118
Cu-oxidase_3 pfam07732
Multicopper oxidase; This entry contains many divergent copper oxidase-like domains that are ...
 813-888 3.29e-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: 38.77  E-value: 3.29e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776487195  813 QIQGPLIMSSVGDKINIVFKNLASRPYSIHAHGVKTDSS-----VVAITN----PGETKMYVWKIsarssserDDSHCTA 883
Cdd:pfam07732   23 QFPGPTIRVREGDTVVVNVTNNLDEPTSIHWHGLQQRGTpwmdgVPGVTQcpipPGQSFTYRFQV--------KQQAGTY 94


                   ....*
gi 1776487195  884 WaYHS 888
Cdd:pfam07732   95 W-YHS 98
ascorbOXfungal TIGR03390
L-ascorbate oxidase, fungal type; This model describes a family of fungal ascorbate oxidases, ...
 1018-1068 3.40e-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: 3.40e-03
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|.
gi 1776487195 1018 YRADVFDLFPGTFQTVEMIPQNPGTWLLHCHVTDHIHAGMEATYTVLPKED 1068
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 ...
 1038-1057 3.81e-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: 3.81e-03
                           10        20
                   ....*....|....*....|
gi 1776487195 1038 QNPGTWLLHCHVTDHIHAGM 1057
Cdd:cd13898    138 VNPGAWLLHCHIQSHLAGGM 157
CuRO_3_AAO_like_2 cd13895
The third cupredoxin domain of Ascorbate oxidase homologs; This family includes fungal ...
 999-1060 4.82e-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: 4.82e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776487195  999 DIHTAHFHG-HSFDYKQ-TGIYRADVFD-----------------LFPGTFQTVEMIP-------------QNPGTWLLH 1046
Cdd:cd13895     91 DAHPWHAHGaHYYDLGSgLGTYSATALAneeklrgynpirrdttmLYRYGGKGYYPPPgtgsgwrawrlrvDDPGVWMLH 170

                           90
                   ....*....|....
gi 1776487195 1047 CHVTDHIHAGMEAT 1060
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 ...
 813-906 4.94e-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: 4.94e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776487195  813 QIQGPLIMSSVGDKINIVFKNLASRPYSIHAHGVKTDSS-----VVAITN----PGETKMYVWKIsarssserDDSHCTA 883
Cdd:cd13850     25 QFPGPPIILDEGDEVEILVTNNLPVNTTIHFHGILQRGTpwsdgVPGVTQwpiqPGGSFTYRWKA--------EDQYGLY 96

                           90       100
                   ....*....|....*....|....
gi 1776487195  884 WaYHSTvdiIKDTYS-GLIGTLVV 906
Cdd:cd13850     97 W-YHSH---YRGYYMdGLYGPIYI 116
CuRO_1_AAO cd13845
The first cupredoxin domain of plant Ascorbate oxidase; Ascorbate oxidase catalyzes the ...
 461-566 5.62e-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: 5.62e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776487195  461 GPVIKAEVGESIRVTFRNN-ASRPFSIQPHGVSYLKS--NEGALYRtasrdTESPasyVSPGASFTYEWNVpedvgptDQ 537
Cdd:cd13845     30 GPTIRATAGDTIVVELENKlPTEGVAIHWHGIRQRGTpwADGTASV-----SQCP---INPGETFTYQFVV-------DR 94

                           90       100
                   ....*....|....*....|....*....
gi 1776487195  538 DPdclTWFYYSAVDSVRdtNSGLVGPLLV 566
Cdd:cd13845     95 PG---TYFYHGHYGMQR--SAGLYGSLIV 118
PLN02604 PLN02604
oxidoreductase
 996-1061 6.55e-03

oxidoreductase


Pssm-ID: 215324 [Multi-domain]  Cd Length: 566  Bit Score: 40.61  E-value: 6.55e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776487195  996 NEIDIHTAHFHGHsfDYKQTGiYRADVFDLF--PGTFQTVEMIPQN------------------PGTWLLHCHVTDHIHA 1055
Cdd:PLN02604   462 NNSETHPWHLHGH--DFWVLG-YGEGKFNMSsdPKKYNLVDPIMKNtvpvhpygwtalrfradnPGVWAFHCHIESHFFM 538


                   ....*.
gi 1776487195 1056 GMEATY 1061
Cdd:PLN02604   539 GMGVVF 544
CuRO_1_LCC_plant cd13849
The first cupredoxin domain of plant laccases; Laccase is a blue multicopper oxidase (MCO) ...
 461-533 8.88e-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: 8.88e-03
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1776487195  461 GPVIKAEVGESIRVTFRNNASRPFSIQPHGVSYLKSN--EGALYRtasrdTESPasyVSPGASFTYEWNVPEDVG 533
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