NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|2024429024|ref|XP_040561922|]
View 

ceruloplasmin isoform X2 [Gallus gallus]

Protein Classification

CuRO_1_ceruloplasmin and CuRO_3_ceruloplasmin domain-containing protein( domain architecture ID 10136056)

protein containing domains CuRO_1_ceruloplasmin, CuRO_3_ceruloplasmin, CuRO_5_ceruloplasmin, and CuRO_6_ceruloplasmin

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 ...
 370-568 2.41e-129

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: 392.61  E-value: 2.41e-129
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024429024  370 TKIRQYFIAAEEIIWNYGPSALNHFTGQELIA-DSESYVFFERSETRIGGSYKKAIYKEYTDGTFTAHKKRLPEEEHLGL 448
Cdd:cd04224      1 GKVRHYFIAAEEIMWDYAPSGKNLFTGQNLTApGSDSEVFFQRNETRIGGTYWKVRYVEYTDATFTTRKHRSKEEEHLGI 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024429024  449 LGPVIKAEVGESIRVTFRNNASRPFSIQPHGVSYHKSNEGALYRtasRDTESPASHVSPGTTFTYEWTVPEDVGPTDQDP 528
Cdd:cd04224     81 LGPVIRAEVGDTIKVTFRNKASRPFSIQPHGVFYEKNYEGAMYR---DGDPSPGSHVSPGETFTYEWTVPEGVGPTNQDP 157

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|
gi 2024429024  529 DCLTWLYYSAVNSVRDTSSGLVGPLMVCRKGALLPSAKQK 568
Cdd:cd04224    158 PCLTYLYFSAVDPVRDTNSGLVGPLLVCKKGSLNANGRQK 197
CuRO_1_ceruloplasmin cd04222
The first cupredoxin domain of Ceruloplasmin; Ceruloplasmin is a multicopper oxidase essential ...
 22-204 5.33e-124

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: 377.92  E-value: 5.33e-124
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024429024   22 REYYIGITETAWDYAPGSTDLISGQRFAEEEQAEVFLKRGPQRIGSTYKKAVYTQYTSTLYDVIVEKPSWLGFLGPIIKG 101
Cdd:cd04222      1 REYYIGIRETQWDYAPSGKNLITNQTFDDDEHASVFLKRGPDRIGRVYKKAVYLQYTDDTYRTEIEKPVWLGFLGPILKA 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024429024  102 EVGDSIVIHLKNFASRNYTLHPHGVKYTKENEGAFYPDNTKGFEKRDDAVKPGGQYTYTWDVTEDQGPAKGDADCITRVY 181
Cdd:cd04222     81 EVGDVIVVHLKNFASRPYSLHPHGVFYNKENEGALYPDNTSGFEKADDAVPPGGSYTYTWTVPEEQAPTKADANCLTRIY 160

                          170       180
                   ....*....|....*....|...
gi 2024429024  182 HSHIDAPRDVASGLVGPLIICKK 204
Cdd:cd04222    161 HSHIDAPKDIASGLIGPLIICKK 183
CuRO_5_ceruloplasmin cd04225
The fifth cupredoxin domain of Ceruloplasmin; Ceruloplasmin is a multicopper oxidase essential ...
 728-898 8.70e-112

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: 344.84  E-value: 8.70e-112
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024429024  728 KTHYIAAVEVEWDYSPNRTWEFERHQYHKESPGNPFLNKDDKFIGSKYKKVVYREYTDQTFSIPKSRAEEEQHLQIQGPL 807
Cdd:cd04225      1 RTYYIAAEEVEWDYSPQRTWEQELHNTHEESPGNAFLNKGDKFIGSKYKKVVYREYTDDTFSVPKERTAEEEHLGILGPL 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024429024  808 IMSSIGDKINIVFKNLASRPYSIHAHGVKTDSSAVAITNPGETKMYVWKISARSGSERGDLHCTAWAYHSMVDIIKDTYS 887
Cdd:cd04225     81 IHAEVGEKVKIVFKNMASRPYSIHAHGVKTDSSWVAPTEPGETQTYTWKIPERSGPGVEDSNCISWAYYSTVDQIKDLYS 160

                          170
                   ....*....|.
gi 2024429024  888 GLIGTLVVCPR 898
Cdd:cd04225    161 GLIGPLVICRR 171
CuRO_2_ceruloplasmin cd11021
The second cupredoxin domain of Ceruloplasmin; Ceruloplasmin is a multicopper oxidase ...
 216-356 1.63e-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: 302.85  E-value: 1.63e-96
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024429024  216 DAEFILMFSVMDENLSWYLDDNIRMYCSEPSKVDKDDEDFQESNKMHSINGYMYGYLPDLTMCVEDKVKWHLFGMGNEAD 295
Cdd:cd11021      1 DREFVLMFSVVDENLSWYLDENIKTYCSEPAKVDKDDEDFQESNKMHSINGYTFGNLPGLSMCAGDRVKWHLFGMGNEVD 80

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2024429024  296 IHSAYFHGQTLIERHHRVDTINLFPATFIDALMIPRNPGEWLLSCQVNDHIEGGMQALFKV 356
Cdd:cd11021     81 IHSAFFHGQTLTDRGHRTDTINLFPATFVTAEMVAQNPGKWLLSCQVNDHLKAGMQAFYEV 141
CuRO_6_ceruloplasmin cd11012
The sixth cupredoxin domain of Ceruloplasmin; Ceruloplasmin is a multicopper oxidase essential ...
 909-1053 5.27e-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: 301.79  E-value: 5.27e-96
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024429024  909 KVRFALLFMVFDENESWYLDENIETYSANPHLVDKENEEFLESNKMHAINGKVFGNLHGLTMHVGDEVSWYLMAMGNEID 988
Cdd:cd11012      1 KLEFALLFLVFDENESWYLDENIKTYSDHPEKVNKEDEEFIESNKMHAINGKVFGNLQGLTMHVGDEVYWYLMGMGNEID 80

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2024429024  989 IHTAHFHGHSFDYKQTEVYRADVFDLFPGTFQTVEMIPQNPGVWLLHCHVTDHIHAGMEATYTVL 1053
Cdd:cd11012     81 IHTAHFHGHSFDYKHRGVYRSDVFDLFPGTFQTVEMIPRTPGTWLLHCHVTDHIHAGMETTYTVL 145
CuRO_4_ceruloplasmin cd11022
The fourth cupredoxin domain of Ceruloplasmin; Ceruloplasmin is a multicopper oxidase ...
 571-714 7.02e-96

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: 301.32  E-value: 7.02e-96
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024429024  571 TREFFLLATVFDENLSWYLDDNILMFTAKPNEIDKDNEDFQESNKMHSINGYMYGNQPGLEMCKGDVISWHLMGLGSEVD 650
Cdd:cd11022      1 DKEFFLLFTVFDENESWYLDENIQQFTLDPRSVDKEDEDFQESNKMHSINGYMYGNQPGLDMCKGDTVSWHLFGLGTETD 80

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2024429024  651 VHGIYFSQNTFVTKGARKDTANLFPHTFVTAIMKPDSEGIFEVSCLTTDHYRGGMKQKYKVKPC 714
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 ...
 370-568 2.41e-129

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: 392.61  E-value: 2.41e-129
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024429024  370 TKIRQYFIAAEEIIWNYGPSALNHFTGQELIA-DSESYVFFERSETRIGGSYKKAIYKEYTDGTFTAHKKRLPEEEHLGL 448
Cdd:cd04224      1 GKVRHYFIAAEEIMWDYAPSGKNLFTGQNLTApGSDSEVFFQRNETRIGGTYWKVRYVEYTDATFTTRKHRSKEEEHLGI 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024429024  449 LGPVIKAEVGESIRVTFRNNASRPFSIQPHGVSYHKSNEGALYRtasRDTESPASHVSPGTTFTYEWTVPEDVGPTDQDP 528
Cdd:cd04224     81 LGPVIRAEVGDTIKVTFRNKASRPFSIQPHGVFYEKNYEGAMYR---DGDPSPGSHVSPGETFTYEWTVPEGVGPTNQDP 157

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|
gi 2024429024  529 DCLTWLYYSAVNSVRDTSSGLVGPLMVCRKGALLPSAKQK 568
Cdd:cd04224    158 PCLTYLYFSAVDPVRDTNSGLVGPLLVCKKGSLNANGRQK 197
CuRO_1_ceruloplasmin cd04222
The first cupredoxin domain of Ceruloplasmin; Ceruloplasmin is a multicopper oxidase essential ...
 22-204 5.33e-124

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: 377.92  E-value: 5.33e-124
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024429024   22 REYYIGITETAWDYAPGSTDLISGQRFAEEEQAEVFLKRGPQRIGSTYKKAVYTQYTSTLYDVIVEKPSWLGFLGPIIKG 101
Cdd:cd04222      1 REYYIGIRETQWDYAPSGKNLITNQTFDDDEHASVFLKRGPDRIGRVYKKAVYLQYTDDTYRTEIEKPVWLGFLGPILKA 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024429024  102 EVGDSIVIHLKNFASRNYTLHPHGVKYTKENEGAFYPDNTKGFEKRDDAVKPGGQYTYTWDVTEDQGPAKGDADCITRVY 181
Cdd:cd04222     81 EVGDVIVVHLKNFASRPYSLHPHGVFYNKENEGALYPDNTSGFEKADDAVPPGGSYTYTWTVPEEQAPTKADANCLTRIY 160

                          170       180
                   ....*....|....*....|...
gi 2024429024  182 HSHIDAPRDVASGLVGPLIICKK 204
Cdd:cd04222    161 HSHIDAPKDIASGLIGPLIICKK 183
CuRO_5_ceruloplasmin cd04225
The fifth cupredoxin domain of Ceruloplasmin; Ceruloplasmin is a multicopper oxidase essential ...
 728-898 8.70e-112

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: 344.84  E-value: 8.70e-112
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024429024  728 KTHYIAAVEVEWDYSPNRTWEFERHQYHKESPGNPFLNKDDKFIGSKYKKVVYREYTDQTFSIPKSRAEEEQHLQIQGPL 807
Cdd:cd04225      1 RTYYIAAEEVEWDYSPQRTWEQELHNTHEESPGNAFLNKGDKFIGSKYKKVVYREYTDDTFSVPKERTAEEEHLGILGPL 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024429024  808 IMSSIGDKINIVFKNLASRPYSIHAHGVKTDSSAVAITNPGETKMYVWKISARSGSERGDLHCTAWAYHSMVDIIKDTYS 887
Cdd:cd04225     81 IHAEVGEKVKIVFKNMASRPYSIHAHGVKTDSSWVAPTEPGETQTYTWKIPERSGPGVEDSNCISWAYYSTVDQIKDLYS 160

                          170
                   ....*....|.
gi 2024429024  888 GLIGTLVVCPR 898
Cdd:cd04225    161 GLIGPLVICRR 171
CuRO_2_ceruloplasmin cd11021
The second cupredoxin domain of Ceruloplasmin; Ceruloplasmin is a multicopper oxidase ...
 216-356 1.63e-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: 302.85  E-value: 1.63e-96
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024429024  216 DAEFILMFSVMDENLSWYLDDNIRMYCSEPSKVDKDDEDFQESNKMHSINGYMYGYLPDLTMCVEDKVKWHLFGMGNEAD 295
Cdd:cd11021      1 DREFVLMFSVVDENLSWYLDENIKTYCSEPAKVDKDDEDFQESNKMHSINGYTFGNLPGLSMCAGDRVKWHLFGMGNEVD 80

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2024429024  296 IHSAYFHGQTLIERHHRVDTINLFPATFIDALMIPRNPGEWLLSCQVNDHIEGGMQALFKV 356
Cdd:cd11021     81 IHSAFFHGQTLTDRGHRTDTINLFPATFVTAEMVAQNPGKWLLSCQVNDHLKAGMQAFYEV 141
CuRO_6_ceruloplasmin cd11012
The sixth cupredoxin domain of Ceruloplasmin; Ceruloplasmin is a multicopper oxidase essential ...
 909-1053 5.27e-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: 301.79  E-value: 5.27e-96
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024429024  909 KVRFALLFMVFDENESWYLDENIETYSANPHLVDKENEEFLESNKMHAINGKVFGNLHGLTMHVGDEVSWYLMAMGNEID 988
Cdd:cd11012      1 KLEFALLFLVFDENESWYLDENIKTYSDHPEKVNKEDEEFIESNKMHAINGKVFGNLQGLTMHVGDEVYWYLMGMGNEID 80

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2024429024  989 IHTAHFHGHSFDYKQTEVYRADVFDLFPGTFQTVEMIPQNPGVWLLHCHVTDHIHAGMEATYTVL 1053
Cdd:cd11012     81 IHTAHFHGHSFDYKHRGVYRSDVFDLFPGTFQTVEMIPRTPGTWLLHCHVTDHIHAGMETTYTVL 145
CuRO_4_ceruloplasmin cd11022
The fourth cupredoxin domain of Ceruloplasmin; Ceruloplasmin is a multicopper oxidase ...
 571-714 7.02e-96

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: 301.32  E-value: 7.02e-96
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024429024  571 TREFFLLATVFDENLSWYLDDNILMFTAKPNEIDKDNEDFQESNKMHSINGYMYGNQPGLEMCKGDVISWHLMGLGSEVD 650
Cdd:cd11022      1 DKEFFLLFTVFDENESWYLDENIQQFTLDPRSVDKEDEDFQESNKMHSINGYMYGNQPGLDMCKGDTVSWHLFGLGTETD 80

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2024429024  651 VHGIYFSQNTFVTKGARKDTANLFPHTFVTAIMKPDSEGIFEVSCLTTDHYRGGMKQKYKVKPC 714
Cdd:cd11022     81 VHGIYFSGNTFLLQGTRRDTANLFPHTSVTAIMQPDNEGTFEVNCQTTDHYSAGMRQIYTVSQC 144
Cu-oxidase_2 pfam07731
Multicopper oxidase; This entry contains many divergent copper oxidase-like domains that are ...
 952-1056 3.05e-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: 85.18  E-value: 3.05e-19
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024429024  952 NKMHAINGKVFG-NLHGLTMHVGDEVSWYLMamGNEIDIHTAHFHGHSFD----------YKQTEVY------RADVFDL 1014
Cdd:pfam07731   19 RNDWAINGLLFPpNTNVITLPYGTVVEWVLQ--NTTTGVHPFHLHGHSFQvlgrgggpwpEEDPKTYnlvdpvRRDTVQV 96

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|..
gi 2024429024 1015 FPGTFQTVEMIPQNPGVWLLHCHVTDHIHAGMEATYTVLPKE 1056
Cdd:pfam07731   97 PPGGWVAIRFRADNPGVWLFHCHILWHLDQGMMGQFVVRPGD 138
Cu-oxidase_3 pfam07732
Multicopper oxidase; This entry contains many divergent copper oxidase-like domains that are ...
 76-201 2.07e-11

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: 62.26  E-value: 2.07e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024429024   76 QYTSTLYDVIVEKPSWL---GFLGPIIKGEVGDSIVIHLKNFASRNYTLHPHGVKYTKENEGAFYPDNTKgfekrdDAVK 152
Cdd:pfam07732    3 TYGTVSPLGGTRQAVIGvngQFPGPTIRVREGDTVVVNVTNNLDEPTSIHWHGLQQRGTPWMDGVPGVTQ------CPIP 76

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*....
gi 2024429024  153 PGGQYTYTWDVTEDQGpakgdadciTRVYHSHIDAPRdvASGLVGPLII 201
Cdd:pfam07732   77 PGQSFTYRFQVKQQAG---------TYWYHSHTSGQQ--AAGLAGAIII 114
SufI COG2132
Multicopper oxidase with three cupredoxin domains (includes cell division protein FtsP and ...
 954-1054 4.57e-09

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


Pssm-ID: 441735 [Multi-domain]  Cd Length: 423  Bit Score: 59.95  E-value: 4.57e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024429024  954 MHAINGKVFGNLH-GLTMHVGDEVSWYLMAMGNeiDIHTAHFHGHSF------DYKQTEVYRADVFDLFPGtfQTVEMI- 1025
Cdd:COG2132    317 VWTINGKAFDPDRpDLTVKLGERERWTLVNDTM--MPHPFHLHGHQFqvlsrnGKPPPEGGWKDTVLVPPG--ETVRILf 392

                           90       100       110
                   ....*....|....*....|....*....|.
gi 2024429024 1026 --PQNPGVWLLHCHVTDHIHAGMEATYTVLP 1054
Cdd:COG2132    393 rfDNYPGDWMFHCHILEHEDAGMMGQFEVVP 423
Cu-oxidase pfam00394
Multicopper oxidase; Many of the proteins in this family contain multiple similar copies of ...
 223-359 5.60e-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: 53.09  E-value: 5.60e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024429024  223 FSVMDENLSWYlDDNIRMYCSEPSKVDKDDEDFQESNKMHSINGYMYGYLPDLTMCVEDKVKWHLFgMGNEADIHSAYFH 302
Cdd:pfam00394    1 EDYVITLSDWY-HKDAKDLEKELLASGKAPTDFPPVPDAVLINGKDGASLATLTVTPGKTYRLRII-NVALDDSLNFSIE 78

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2024429024  303 GQ--TLIE---RHH---RVDTINLFPATFIDALMIP-RNPGEWLLSCQVN-DHIEGGMQALFKVEGC 359
Cdd:pfam00394   79 GHkmTVVEvdgVYVnpfTVDSLDIFPGQRYSVLVTAnQDPGNYWIVASPNiPAFDNGTAAAILRYSG 145
SufI COG2132
Multicopper oxidase with three cupredoxin domains (includes cell division protein FtsP and ...
 94-224 1.04e-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: 55.71  E-value: 1.04e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024429024   94 FLGPIIKGEVGDSIVIHLKNFASRNYTLHPHGVKYTKENEGafYPdntkgfekrDDAVKPGGQYTYTWDVteDQGPAkgd 173
Cdd:COG2132     42 YPGPTIRVREGDRVRVRVTNRLPEPTTVHWHGLRVPNAMDG--VP---------GDPIAPGETFTYEFPV--PQPAG--- 105

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 2024429024  174 adciTRVYHSHIDA--PRDVASGLVGPLIIckkgamNKDNDKY--VDAEFILMFS 224
Cdd:COG2132    106 ----TYWYHPHTHGstAEQVYRGLAGALIV------EDPEEDLprYDRDIPLVLQ 150
PLN02191 PLN02191
L-ascorbate oxidase
 94-224 3.04e-07

L-ascorbate oxidase


Pssm-ID: 177843 [Multi-domain]  Cd Length: 574  Bit Score: 54.63  E-value: 3.04e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024429024   94 FLGPIIKGEVGDSIVIHLKN-FASRNYTLHPHGVKytkeNEGAFYPDNTKGFEKRddAVKPGGQYTYTWDVtEDQGpakg 172
Cdd:PLN02191    51 FPGPTIDAVAGDTIVVHLTNkLTTEGLVIHWHGIR----QKGSPWADGAAGVTQC--AINPGETFTYKFTV-EKPG---- 119

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|..
gi 2024429024  173 dadciTRVYHSHIDAPRdvASGLVGPLIIckKGAMNKDNDKYVDAEFILMFS 224
Cdd:PLN02191   120 -----THFYHGHYGMQR--SAGLYGSLIV--DVAKGPKERLRYDGEFNLLLS 162
Cu-oxidase_3 pfam07732
Multicopper oxidase; This entry contains many divergent copper oxidase-like domains that are ...
 448-555 1.56e-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: 1.56e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024429024  448 LLGPVIKAEVGESIRVTFRNNASRPFSIQPHGVSYHKSNE--GALYrtasrdteSPASHVSPGTTFTYEWTVPEDVGptd 525
Cdd:pfam07732   24 FPGPTIRVREGDTVVVNVTNNLDEPTSIHWHGLQQRGTPWmdGVPG--------VTQCPIPPGQSFTYRFQVKQQAG--- 92

                           90       100       110
                   ....*....|....*....|....*....|
gi 2024429024  526 qdpdclTWLYYSAVNSVRdtSSGLVGPLMV 555
Cdd:pfam07732   93 ------TYWYHSHTSGQQ--AAGLAGAIII 114
PLN02191 PLN02191
L-ascorbate oxidase
 988-1046 1.72e-06

L-ascorbate oxidase


Pssm-ID: 177843 [Multi-domain]  Cd Length: 574  Bit Score: 52.32  E-value: 1.72e-06
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2024429024  988 DIHTAHFHGHSF--------------DYKQTEVYRADVFD---LFPGTFQTVEMIPQNPGVWLLHCHVTDHIHAGM 1046
Cdd:PLN02191   465 EIHPWHLHGHDFwvlgygdgkfkpgiDEKTYNLKNPPLRNtaiLYPYGWTAIRFVTDNPGVWFFHCHIEPHLHMGM 540
ascorbase TIGR03388
L-ascorbate oxidase, plant type; Members of this protein family are the copper-containing ...
 94-233 1.97e-06

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: 52.06  E-value: 1.97e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024429024   94 FLGPIIKGEVGDSIVIHLKN-FASRNYTLHPHGVKytkeNEGAFYPDNTKGFEKRddAVKPGGQYTYTWdVTEDQGpakg 172
Cdd:TIGR03388   29 FPGPTIRAQAGDTIVVELTNkLHTEGVVIHWHGIR----QIGTPWADGTAGVTQC--AINPGETFIYNF-VVDRPG---- 97

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2024429024  173 dadciTRVYHSHIDAPRdvASGLVGPLIIcKKGAMNKDNDKYvDAEFILMFSvmdenlSWY 233
Cdd:TIGR03388   98 -----TYFYHGHYGMQR--SAGLYGSLIV-DVPDGEKEPFHY-DGEFNLLLS------DWW 143
ascorbase TIGR03388
L-ascorbate oxidase, plant type; Members of this protein family are the copper-containing ...
 984-1046 2.21e-05

L-ascorbate oxidase, plant type; Members of this protein family are the copper-containing enzyme L-ascorbate oxidase (EC 1.10.3.3), also called ascorbase. This family is found in flowering plants, and shows greater sequence similarity to a family of laccases (EC 1.10.3.2) from plants than to other known ascorbate oxidases.


Pssm-ID: 274555 [Multi-domain]  Cd Length: 541  Bit Score: 48.59  E-value: 2.21e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024429024  984 GNEIDIHTAHFHGHSF------DYKQTEVYRADVFDL-----------FPGTFQTVEMIPQNPGVWLLHCHVTDHIHAGM 1046
Cdd:TIGR03388  438 GNNSETHPWHLHGHDFwvlgygEGKFRPGVDEKSYNLknpplrntvviFPYGWTALRFVADNPGVWAFHCHIEPHLHMGM 517
SufI COG2132
Multicopper oxidase with three cupredoxin domains (includes cell division protein FtsP and ...
 448-577 3.87e-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: 3.87e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024429024  448 LLGPVIKAEVGESIRVTFRNNASRPFSIQPHGVsyHKSNE--GalyrtasrdteSPASHVSPGTTFTYEWTVPEDVGptd 525
Cdd:COG2132     42 YPGPTIRVREGDRVRVRVTNRLPEPTTVHWHGL--RVPNAmdG-----------VPGDPIAPGETFTYEFPVPQPAG--- 105

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....
gi 2024429024  526 qdpdclTWLYYSAVN--SVRDTSSGLVGPLMVCRKGALLPSakqktVTREFFLL 577
Cdd:COG2132    106 ------TYWYHPHTHgsTAEQVYRGLAGALIVEDPEEDLPR-----YDRDIPLV 148
 
Name Accession Description Interval E-value
CuRO_3_ceruloplasmin cd04224
The third cupredoxin domain of Ceruloplasmin; Ceruloplasmin is a multicopper oxidase essential ...
 370-568 2.41e-129

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: 392.61  E-value: 2.41e-129
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024429024  370 TKIRQYFIAAEEIIWNYGPSALNHFTGQELIA-DSESYVFFERSETRIGGSYKKAIYKEYTDGTFTAHKKRLPEEEHLGL 448
Cdd:cd04224      1 GKVRHYFIAAEEIMWDYAPSGKNLFTGQNLTApGSDSEVFFQRNETRIGGTYWKVRYVEYTDATFTTRKHRSKEEEHLGI 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024429024  449 LGPVIKAEVGESIRVTFRNNASRPFSIQPHGVSYHKSNEGALYRtasRDTESPASHVSPGTTFTYEWTVPEDVGPTDQDP 528
Cdd:cd04224     81 LGPVIRAEVGDTIKVTFRNKASRPFSIQPHGVFYEKNYEGAMYR---DGDPSPGSHVSPGETFTYEWTVPEGVGPTNQDP 157

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|
gi 2024429024  529 DCLTWLYYSAVNSVRDTSSGLVGPLMVCRKGALLPSAKQK 568
Cdd:cd04224    158 PCLTYLYFSAVDPVRDTNSGLVGPLLVCKKGSLNANGRQK 197
CuRO_1_ceruloplasmin cd04222
The first cupredoxin domain of Ceruloplasmin; Ceruloplasmin is a multicopper oxidase essential ...
 22-204 5.33e-124

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: 377.92  E-value: 5.33e-124
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024429024   22 REYYIGITETAWDYAPGSTDLISGQRFAEEEQAEVFLKRGPQRIGSTYKKAVYTQYTSTLYDVIVEKPSWLGFLGPIIKG 101
Cdd:cd04222      1 REYYIGIRETQWDYAPSGKNLITNQTFDDDEHASVFLKRGPDRIGRVYKKAVYLQYTDDTYRTEIEKPVWLGFLGPILKA 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024429024  102 EVGDSIVIHLKNFASRNYTLHPHGVKYTKENEGAFYPDNTKGFEKRDDAVKPGGQYTYTWDVTEDQGPAKGDADCITRVY 181
Cdd:cd04222     81 EVGDVIVVHLKNFASRPYSLHPHGVFYNKENEGALYPDNTSGFEKADDAVPPGGSYTYTWTVPEEQAPTKADANCLTRIY 160

                          170       180
                   ....*....|....*....|...
gi 2024429024  182 HSHIDAPRDVASGLVGPLIICKK 204
Cdd:cd04222    161 HSHIDAPKDIASGLIGPLIICKK 183
CuRO_5_ceruloplasmin cd04225
The fifth cupredoxin domain of Ceruloplasmin; Ceruloplasmin is a multicopper oxidase essential ...
 728-898 8.70e-112

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: 344.84  E-value: 8.70e-112
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024429024  728 KTHYIAAVEVEWDYSPNRTWEFERHQYHKESPGNPFLNKDDKFIGSKYKKVVYREYTDQTFSIPKSRAEEEQHLQIQGPL 807
Cdd:cd04225      1 RTYYIAAEEVEWDYSPQRTWEQELHNTHEESPGNAFLNKGDKFIGSKYKKVVYREYTDDTFSVPKERTAEEEHLGILGPL 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024429024  808 IMSSIGDKINIVFKNLASRPYSIHAHGVKTDSSAVAITNPGETKMYVWKISARSGSERGDLHCTAWAYHSMVDIIKDTYS 887
Cdd:cd04225     81 IHAEVGEKVKIVFKNMASRPYSIHAHGVKTDSSWVAPTEPGETQTYTWKIPERSGPGVEDSNCISWAYYSTVDQIKDLYS 160

                          170
                   ....*....|.
gi 2024429024  888 GLIGTLVVCPR 898
Cdd:cd04225    161 GLIGPLVICRR 171
CuRO_2_ceruloplasmin cd11021
The second cupredoxin domain of Ceruloplasmin; Ceruloplasmin is a multicopper oxidase ...
 216-356 1.63e-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: 302.85  E-value: 1.63e-96
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024429024  216 DAEFILMFSVMDENLSWYLDDNIRMYCSEPSKVDKDDEDFQESNKMHSINGYMYGYLPDLTMCVEDKVKWHLFGMGNEAD 295
Cdd:cd11021      1 DREFVLMFSVVDENLSWYLDENIKTYCSEPAKVDKDDEDFQESNKMHSINGYTFGNLPGLSMCAGDRVKWHLFGMGNEVD 80

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2024429024  296 IHSAYFHGQTLIERHHRVDTINLFPATFIDALMIPRNPGEWLLSCQVNDHIEGGMQALFKV 356
Cdd:cd11021     81 IHSAFFHGQTLTDRGHRTDTINLFPATFVTAEMVAQNPGKWLLSCQVNDHLKAGMQAFYEV 141
CuRO_6_ceruloplasmin cd11012
The sixth cupredoxin domain of Ceruloplasmin; Ceruloplasmin is a multicopper oxidase essential ...
 909-1053 5.27e-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: 301.79  E-value: 5.27e-96
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024429024  909 KVRFALLFMVFDENESWYLDENIETYSANPHLVDKENEEFLESNKMHAINGKVFGNLHGLTMHVGDEVSWYLMAMGNEID 988
Cdd:cd11012      1 KLEFALLFLVFDENESWYLDENIKTYSDHPEKVNKEDEEFIESNKMHAINGKVFGNLQGLTMHVGDEVYWYLMGMGNEID 80

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2024429024  989 IHTAHFHGHSFDYKQTEVYRADVFDLFPGTFQTVEMIPQNPGVWLLHCHVTDHIHAGMEATYTVL 1053
Cdd:cd11012     81 IHTAHFHGHSFDYKHRGVYRSDVFDLFPGTFQTVEMIPRTPGTWLLHCHVTDHIHAGMETTYTVL 145
CuRO_4_ceruloplasmin cd11022
The fourth cupredoxin domain of Ceruloplasmin; Ceruloplasmin is a multicopper oxidase ...
 571-714 7.02e-96

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: 301.32  E-value: 7.02e-96
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024429024  571 TREFFLLATVFDENLSWYLDDNILMFTAKPNEIDKDNEDFQESNKMHSINGYMYGNQPGLEMCKGDVISWHLMGLGSEVD 650
Cdd:cd11022      1 DKEFFLLFTVFDENESWYLDENIQQFTLDPRSVDKEDEDFQESNKMHSINGYMYGNQPGLDMCKGDTVSWHLFGLGTETD 80

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2024429024  651 VHGIYFSQNTFVTKGARKDTANLFPHTFVTAIMKPDSEGIFEVSCLTTDHYRGGMKQKYKVKPC 714
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 ...
 22-204 5.98e-79

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


Pssm-ID: 259862 [Multi-domain]  Cd Length: 177  Bit Score: 256.56  E-value: 5.98e-79
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024429024   22 REYYIGITETAWDYAPGSTDLIsgqrfaEEEQAEVFLKRGPQRIGSTYKKAVYTQYTSTLYDVIVEKPSWLGFLGPIIKG 101
Cdd:cd04199      1 RHYYIAAEEIDWDYAPSGLAEK------DLSYRNQYLDNGPFRIGRSYKKVVYREYTDESFTTPGPQPEHLGILGPTIRA 74

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024429024  102 EVGDSIVIHLKNFASRNYTLHPHGVKYTKENEGAFYPDNTKGFEKRDDAVKPGGQYTYTWDVTEDQGPAKGDADCITRVY 181
Cdd:cd04199     75 EVGDTIKVHFKNKASRPYSIHPHGVSYEKDSEGASYSDQTGPDEKKDDAVAPGETYTYVWIVTEESGPTKGDPACLTWAY 154

                          170       180
                   ....*....|....*....|...
gi 2024429024  182 HSHIDAPRDVASGLVGPLIICKK 204
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 ...
 373-558 4.18e-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: 254.25  E-value: 4.18e-78
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024429024  373 RQYFIAAEEIIWNYGPSALNHFTgqeliaDSESYVFFERSETRIGGSYKKAIYKEYTDGTFTahkKRLPEEEHLGLLGPV 452
Cdd:cd04199      1 RHYYIAAEEIDWDYAPSGLAEKD------LSYRNQYLDNGPFRIGRSYKKVVYREYTDESFT---TPGPQPEHLGILGPT 71

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024429024  453 IKAEVGESIRVTFRNNASRPFSIQPHGVSYHKSNEGALYRTASRDTESPASHVSPGTTFTYEWTVPEDVGPTDQDPDCLT 532
Cdd:cd04199     72 IRAEVGDTIKVHFKNKASRPYSIHPHGVSYEKDSEGASYSDQTGPDEKKDDAVAPGETYTYVWIVTEESGPTKGDPACLT 151

                          170       180
                   ....*....|....*....|....*.
gi 2024429024  533 WLYYSAVNSVRDTSSGLVGPLMVCRK 558
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 ...
 216-356 9.65e-71

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


Pssm-ID: 259863 [Multi-domain]  Cd Length: 141  Bit Score: 231.92  E-value: 9.65e-71
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024429024  216 DAEFILMFSVMDENLSWYLDDNIRMYCSEPSKVDKDDEDFQESNKMHSINGYMYGYLPDLTMCVEDKVKWHLFGMGNEAD 295
Cdd:cd04200      1 DKEFVLLFAVFDENKSWYLEDNIKRFCDNPEKVDKDDEEFQESNKMHAINGYVFGNLPGLTMCAGDRVRWHLLGMGNEVD 80

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2024429024  296 IHSAYFHGQTLIERHHRVDTINLFPATFIDALMIPRNPGEWLLSCQVNDHIEGGMQALFKV 356
Cdd:cd04200     81 VHSIHFHGQTFLYKGYRIDTLTLFPATFETVEMVPSNPGTWLLHCHNSDHRHAGMQAYFLV 141
CuRO_1_ceruloplasmin cd04222
The first cupredoxin domain of Ceruloplasmin; Ceruloplasmin is a multicopper oxidase essential ...
 373-558 5.99e-68

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: 226.15  E-value: 5.99e-68
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024429024  373 RQYFIAAEEIIWNYGPSALNHFTGQELIADSESYVFFERSETRIGGSYKKAIYKEYTDGTFTahkKRLPEEEHLGLLGPV 452
Cdd:cd04222      1 REYYIGIRETQWDYAPSGKNLITNQTFDDDEHASVFLKRGPDRIGRVYKKAVYLQYTDDTYR---TEIEKPVWLGFLGPI 77

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024429024  453 IKAEVGESIRVTFRNNASRPFSIQPHGVSYHKSNEGALYRTASRDTESPASHVSPGTTFTYEWTVPEDVGPTDQDPDCLT 532
Cdd:cd04222     78 LKAEVGDVIVVHLKNFASRPYSLHPHGVFYNKENEGALYPDNTSGFEKADDAVPPGGSYTYTWTVPEEQAPTKADANCLT 157

                          170       180
                   ....*....|....*....|....*.
gi 2024429024  533 WLYYSAVNSVRDTSSGLVGPLMVCRK 558
Cdd:cd04222    158 RIYHSHIDAPKDIASGLIGPLIICKK 183
CuRO_2_ceruloplasmin_like cd04200
Cupredoxin domains 2, 4, and 6 of ceruloplasmin and similar proteins; This family includes the ...
 911-1052 8.35e-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: 223.83  E-value: 8.35e-68
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024429024  911 RFALLFMVFDENESWYLDENIETYSANPHLVDKENEEFLESNKMHAINGKVFGNLHGLTMHVGDEVSWYLMAMGNEIDIH 990
Cdd:cd04200      3 EFVLLFAVFDENKSWYLEDNIKRFCDNPEKVDKDDEEFQESNKMHAINGYVFGNLPGLTMCAGDRVRWHLLGMGNEVDVH 82

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2024429024  991 TAHFHGHSFDYKQtevYRADVFDLFPGTFQTVEMIPQNPGVWLLHCHVTDHIHAGMEATYTV 1052
Cdd:cd04200     83 SIHFHGQTFLYKG---YRIDTLTLFPATFETVEMVPSNPGTWLLHCHNSDHRHAGMQAYFLV 141
CuRO_4_ceruloplasmin cd11022
The fourth cupredoxin domain of Ceruloplasmin; Ceruloplasmin is a multicopper oxidase ...
 216-359 1.60e-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: 211.96  E-value: 1.60e-63
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024429024  216 DAEFILMFSVMDENLSWYLDDNIRMYCSEPSKVDKDDEDFQESNKMHSINGYMYGYLPDLTMCVEDKVKWHLFGMGNEAD 295
Cdd:cd11022      1 DKEFFLLFTVFDENESWYLDENIQQFTLDPRSVDKEDEDFQESNKMHSINGYMYGNQPGLDMCKGDTVSWHLFGLGTETD 80

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2024429024  296 IHSAYFHGQTLIERHHRVDTINLFPATFIDALMIPRNPGEWLLSCQVNDHIEGGMQALFKVEGC 359
Cdd:cd11022     81 VHGIYFSGNTFLLQGTRRDTANLFPHTSVTAIMQPDNEGTFEVNCQTTDHYSAGMRQIYTVSQC 144
CuRO_2_ceruloplasmin cd11021
The second cupredoxin domain of Ceruloplasmin; Ceruloplasmin is a multicopper oxidase ...
 912-1052 9.61e-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: 203.86  E-value: 9.61e-61
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024429024  912 FALLFMVFDENESWYLDENIETYSANPHLVDKENEEFLESNKMHAINGKVFGNLHGLTMHVGDEVSWYLMAMGNEIDIHT 991
Cdd:cd11021      4 FVLMFSVVDENLSWYLDENIKTYCSEPAKVDKDDEDFQESNKMHSINGYTFGNLPGLSMCAGDRVKWHLFGMGNEVDIHS 83

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2024429024  992 AHFHGHSFDYKQtevYRADVFDLFPGTFQTVEMIPQNPGVWLLHCHVTDHIHAGMEATYTV 1052
Cdd:cd11021     84 AFFHGQTLTDRG---HRTDTINLFPATFVTAEMVAQNPGKWLLSCQVNDHLKAGMQAFYEV 141
CuRO_2_ceruloplasmin cd11021
The second cupredoxin domain of Ceruloplasmin; Ceruloplasmin is a multicopper oxidase ...
 572-711 2.40e-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: 202.70  E-value: 2.40e-60
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024429024  572 REFFLLATVFDENLSWYLDDNILMFTAKPNEIDKDNEDFQESNKMHSINGYMYGNQPGLEMCKGDVISWHLMGLGSEVDV 651
Cdd:cd11021      2 REFVLMFSVVDENLSWYLDENIKTYCSEPAKVDKDDEDFQESNKMHSINGYTFGNLPGLSMCAGDRVKWHLFGMGNEVDI 81

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024429024  652 HGIYFSQNTFVTKGARKDTANLFPHTFVTAIMKPDSEGIFEVSCLTTDHYRGGMKQKYKV 711
Cdd:cd11021     82 HSAFFHGQTLTDRGHRTDTINLFPATFVTAEMVAQNPGKWLLSCQVNDHLKAGMQAFYEV 141
CuRO_5_ceruloplasmin cd04225
The fifth cupredoxin domain of Ceruloplasmin; Ceruloplasmin is a multicopper oxidase essential ...
 373-558 5.74e-60

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: 203.08  E-value: 5.74e-60
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024429024  373 RQYFIAAEEIIWNYGPSALNHFTGQELIADSESYVFFERSETRIGGSYKKAIYKEYTDGTFTAHKKRLPEEEHLGLLGPV 452
Cdd:cd04225      1 RTYYIAAEEVEWDYSPQRTWEQELHNTHEESPGNAFLNKGDKFIGSKYKKVVYREYTDDTFSVPKERTAEEEHLGILGPL 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024429024  453 IKAEVGESIRVTFRNNASRPFSIQPHGVSyhksnegalyrtasrdTESPA-SHVSPGTTFTYEWTVPEDVGPTDQDPDCL 531
Cdd:cd04225     81 IHAEVGEKVKIVFKNMASRPYSIHAHGVK----------------TDSSWvAPTEPGETQTYTWKIPERSGPGVEDSNCI 144

                          170       180
                   ....*....|....*....|....*..
gi 2024429024  532 TWLYYSAVNSVRDTSSGLVGPLMVCRK 558
Cdd:cd04225    145 SWAYYSTVDQIKDLYSGLIGPLVICRR 171
CuRO_2_ceruloplasmin_like cd04200
Cupredoxin domains 2, 4, and 6 of ceruloplasmin and similar proteins; This family includes the ...
 572-711 6.65e-60

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


Pssm-ID: 259863 [Multi-domain]  Cd Length: 141  Bit Score: 201.48  E-value: 6.65e-60
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024429024  572 REFFLLATVFDENLSWYLDDNILMFTAKPNEIDKDNEDFQESNKMHSINGYMYGNQPGLEMCKGDVISWHLMGLGSEVDV 651
Cdd:cd04200      2 KEFVLLFAVFDENKSWYLEDNIKRFCDNPEKVDKDDEEFQESNKMHAINGYVFGNLPGLTMCAGDRVRWHLLGMGNEVDV 81

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024429024  652 HGIYFSQNTFVTKGARKDTANLFPHTFVTAIMKPDSEGIFEVSCLTTDHYRGGMKQKYKV 711
Cdd:cd04200     82 HSIHFHGQTFLYKGYRIDTLTLFPATFETVEMVPSNPGTWLLHCHNSDHRHAGMQAYFLV 141
CuRO_3_ceruloplasmin cd04224
The third cupredoxin domain of Ceruloplasmin; Ceruloplasmin is a multicopper oxidase essential ...
 22-210 3.74e-59

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


Pssm-ID: 259886 [Multi-domain]  Cd Length: 197  Bit Score: 201.55  E-value: 3.74e-59
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024429024   22 REYYIGITETAWDYAPGSTDLISGQRF-AEEEQAEVFLKRGPQRIGSTYKKAVYTQYTS---TLYDVIVEKPSWLGFLGP 97
Cdd:cd04224      4 RHYFIAAEEIMWDYAPSGKNLFTGQNLtAPGSDSEVFFQRNETRIGGTYWKVRYVEYTDatfTTRKHRSKEEEHLGILGP 83

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024429024   98 IIKGEVGDSIVIHLKNFASRNYTLHPHGVKYTKENEGAFYPDntkGFEKRDDAVKPGGQYTYTWDVTEDQGPAKGDADCI 177
Cdd:cd04224     84 VIRAEVGDTIKVTFRNKASRPFSIQPHGVFYEKNYEGAMYRD---GDPSPGSHVSPGETFTYEWTVPEGVGPTNQDPPCL 160

                          170       180       190
                   ....*....|....*....|....*....|...
gi 2024429024  178 TRVYHSHIDAPRDVASGLVGPLIICKKGAMNKD 210
Cdd:cd04224    161 TYLYFSAVDPVRDTNSGLVGPLLVCKKGSLNAN 193
CuRO_3_FV_like cd14450
The third cupredoxin domain of coagulation factor V and similar proteins; Factor V is an ...
 371-557 2.19e-58

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: 198.95  E-value: 2.19e-58
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024429024  371 KIRQYFIAAEEIIWNYGP----SALNHFTGQELIADSEsyvffersetRIGGSYKKAIYKEYTDGTFTAHKKRlPEEEHL 446
Cdd:cd14450      1 KNWEYFIAAEEVIWDYAPsipeNMDKRYRSQYLDNFSN----------NIGKKYKKAVFTQYEDGSFTKRLEN-PRPKEE 69

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024429024  447 GLLGPVIKAEVGESIRVTFRNNASRPFSIQPHGVSYHKSNEGALYRTASRDTESPASHVSPGTTFTYEWTVPEDVGPTDQ 526
Cdd:cd14450     70 GILGPVIRAQVRDTIKIVFKNKASRPYSIYPHGVTVSKAAEGASYPPDPRGNETQNKAVQPGETYTYKWNILETDEPTAR 149

                          170       180       190
                   ....*....|....*....|....*....|.
gi 2024429024  527 DPDCLTWLYYSAVNSVRDTSSGLVGPLMVCR 557
Cdd:cd14450    150 DPRCLTRMYHSAVDITRDIASGLIGPLLICK 180
CuRO_1_ceruloplasmin_like cd04199
Cupredoxin domains 1, 3, and 5 of ceruloplasmin and similar proteins; This family includes the ...
 728-896 3.06e-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: 198.40  E-value: 3.06e-58
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024429024  728 KTHYIAAVEVEWDYSPNRTWEFERHQYhkespgNPFLNKDDKFIGSKYKKVVYREYTDQTFSIPKsraEEEQHLQIQGPL 807
Cdd:cd04199      1 RHYYIAAEEIDWDYAPSGLAEKDLSYR------NQYLDNGPFRIGRSYKKVVYREYTDESFTTPG---PQPEHLGILGPT 71

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024429024  808 IMSSIGDKINIVFKNLASRPYSIHAHGVKTDSS------------------AVAitnPGETKMYVWKISARSGSERGDLH 869
Cdd:cd04199     72 IRAEVGDTIKVHFKNKASRPYSIHPHGVSYEKDsegasysdqtgpdekkddAVA---PGETYTYVWIVTEESGPTKGDPA 148

                          170       180
                   ....*....|....*....|....*..
gi 2024429024  870 CTAWAYHSMVDIIKDTYSGLIGTLVVC 896
Cdd:cd04199    149 CLTWAYYSHVDLEKDINSGLIGPLLIC 175
CuRO_1_Ceruloplasmin_like_1 cd04229
cupredoxin domain of ceruloplasmin homologs; Uncharacterized subfamily of ceruloplasmin ...
 373-559 8.48e-57

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


Pssm-ID: 259891 [Multi-domain]  Cd Length: 175  Bit Score: 194.17  E-value: 8.48e-57
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024429024  373 RQYFIAAEEIIWNYGPSALNH-FTGQELiadSESYVFFERSETRIGGSYKKAIYKEYTDGTFTahkKRLPEEEHLGLLGP 451
Cdd:cd04229      1 RTYYIAAEEVDWDYAPSGKNKcCLGDDL---EVSTLDSQPGPYTIGSTYTKARYREYTDNSFS---TPKPTPAYLGILGP 74

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024429024  452 VIKAEVGESIRVTFRNNASR-PFSIQPHGVSYHKSNEGALYRTASRdtespashVSPGTTFTYEWTVPEDVGPTDQDPDC 530
Cdd:cd04229     75 VIRAEVGDTIKVVFKNNLDEfPVNMHPHGGLYSKDNEGTTDGAGDV--------VAPGETYTYRWIVPEDAGPGPGDPSS 146

                          170       180
                   ....*....|....*....|....*....
gi 2024429024  531 LTWLYYSAVNSVRDTSSGLVGPLMVCRKG 559
Cdd:cd04229    147 RLWLYHSHVDVFAHTNAGLVGPIIVTSKG 175
CuRO_5_FV_like cd14451
The fifth cupredoxin domain of coagulation factor V and similar proteins; Factor V is an ...
 373-559 2.80e-56

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


Pssm-ID: 259993 [Multi-domain]  Cd Length: 173  Bit Score: 192.36  E-value: 2.80e-56
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024429024  373 RQYFIAAEEIIWNYGPSALNHFTGQELIADsesyvffersetrigGSYKKAIYKEYTDGTFTAHKKRLPEEEHLGLLGPV 452
Cdd:cd14451      2 RRYYIAAEEEEWDYAGYGKSRLDKTQNERD---------------TVFKKVVFRRYLDSTFSTPDIQGEYEEHLGILGPV 66

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024429024  453 IKAEVGESIRVTFRNNASRPFSIQPHGVSYHKSNEGALYRTASRDTESPASHVSPGTTFTYEWTVPEDVGPTDQDPDCLT 532
Cdd:cd14451     67 IRAEVDDVIQVFFKNLASRPYSLHAHGLSYEKSSEGLSYDDESPDWFKKDDAVQPNGTYTYVWYANPRSGPENNGSDCRT 146

                          170       180
                   ....*....|....*....|....*..
gi 2024429024  533 WLYYSAVNSVRDTSSGLVGPLMVCRKG 559
Cdd:cd14451    147 WAYYSAVNPEKDIHSGLIGPLLICRKG 173
CuRO_1_FVIII_like cd14452
The first cupredoxin domain of coagulation factor VIII and similar proteins; Factor VIII ...
 22-205 1.03e-55

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: 190.96  E-value: 1.03e-55
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024429024   22 REYYIGITETAWDYApgstdlisgqrFAEEEQAEVFLKRGPQRIGSTYKKAVYTQYTSTLYDVIVEKPSWLGFLGPIIKG 101
Cdd:cd14452      1 RRYYIAAVEIGWDYI-----------HSDLGDPASEQRKKPKDIPQKYIKAVFVEYLDATFTVPKPRPAWMGLLGPTIVA 69

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024429024  102 EVGDSIVIHLKNFASRNYTLHPHGVKYTKENEGAFYPDNTKGFEKRDDAVKPGGQYTYTWDVTEDQGPAKGDADCITRVY 181
Cdd:cd14452     70 EVGDTVVITFKNLASQPYSLHAVGVSYWKASEGAGYDDSTSQHEKEDDAVYPGGYHTYVWDISPKDGPTGSDPECLTYSY 149

                          170       180
                   ....*....|....*....|....
gi 2024429024  182 HSHIDAPRDVASGLVGPLIICKKG 205
Cdd:cd14452    150 SSQVDPVKDVNSGLIGALLVCRMG 173
CuRO_4_ceruloplasmin cd11022
The fourth cupredoxin domain of Ceruloplasmin; Ceruloplasmin is a multicopper oxidase ...
 912-1052 4.32e-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: 4.32e-55
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024429024  912 FALLFMVFDENESWYLDENIETYSANPHLVDKENEEFLESNKMHAINGKVFGNLHGLTMHVGDEVSWYLMAMGNEIDIHT 991
Cdd:cd11022      4 FFLLFTVFDENESWYLDENIQQFTLDPRSVDKEDEDFQESNKMHSINGYMYGNQPGLDMCKGDTVSWHLFGLGTETDVHG 83

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2024429024  992 AHFHGHSFDYKQTevyRADVFDLFPGTFQTVEMIPQNPGVWLLHCHVTDHIHAGMEATYTV 1052
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 ...
 23-203 5.62e-55

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


Pssm-ID: 259992 [Multi-domain]  Cd Length: 181  Bit Score: 188.93  E-value: 5.62e-55
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024429024   23 EYYIGITETAWDYAPGSTDLISGQRFAEeeqaevFLKRGPQRIGSTYKKAVYTQYTSTLYDVIVE--KPSWLGFLGPIIK 100
Cdd:cd14450      4 EYFIAAEEVIWDYAPSIPENMDKRYRSQ------YLDNFSNNIGKKYKKAVFTQYEDGSFTKRLEnpRPKEEGILGPVIR 77

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024429024  101 GEVGDSIVIHLKNFASRNYTLHPHGVKYTKENEGAFYPDNTKGFEKRDDAVKPGGQYTYTWDVTEDQGPAKGDADCITRV 180
Cdd:cd14450     78 AQVRDTIKIVFKNKASRPYSIYPHGVTVSKAAEGASYPPDPRGNETQNKAVQPGETYTYKWNILETDEPTARDPRCLTRM 157

                          170       180
                   ....*....|....*....|...
gi 2024429024  181 YHSHIDAPRDVASGLVGPLIICK 203
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 ...
 22-205 4.99e-54

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: 185.83  E-value: 4.99e-54
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024429024   22 REYYIGITETAWDYAPGSTDLISgqrfaeeeqaevflkrgpQRIGSTYKKAVYTQYTStlyDVIVEKPSWL--GFLGPII 99
Cdd:cd04226      1 REYYIAAQNIDWDYTPQSEELRL------------------KRSEQSFKKIVYREYEE---GFKKEKPADLssGLLGPTL 59

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024429024  100 KGEVGDSIVIHLKNFASRNYTLHPHGVKYTKENEGAFYPDNTKGFEKRDDAVKPGGQYTYTWDVTEDQGPAKGDADCITR 179
Cdd:cd04226     60 RAEVGDTLIVHFKNMADKPLSIHPQGIAYGKKSEGSLYSDNTSPVEKLDDAVQPGQEYTYVWDITEEVGPTEADPPCLTY 139

                          170       180
                   ....*....|....*....|....*.
gi 2024429024  180 VYHSHIDAPRDVASGLVGPLIICKKG 205
Cdd:cd04226    140 IYYSHVNMVRDFNSGLIGALLICKKG 165
CuRO_1_Ceruloplasmin_like_1 cd04229
cupredoxin domain of ceruloplasmin homologs; Uncharacterized subfamily of ceruloplasmin ...
 22-205 2.08e-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: 181.46  E-value: 2.08e-52
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024429024   22 REYYIGITETAWDYAPGSTDLISGQRFAEEEQaeVFLKRGPQRIGSTYKKAVYTQYTSTLYDVIVEKPSWLGFLGPIIKG 101
Cdd:cd04229      1 RTYYIAAEEVDWDYAPSGKNKCCLGDDLEVST--LDSQPGPYTIGSTYTKARYREYTDNSFSTPKPTPAYLGILGPVIRA 78

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024429024  102 EVGDSIVIHLKN-FASRNYTLHPHGVKYTKENEGafypdntkGFEKRDDAVKPGGQYTYTWDVTEDQGPAKGDADCITRV 180
Cdd:cd04229     79 EVGDTIKVVFKNnLDEFPVNMHPHGGLYSKDNEG--------TTDGAGDVVAPGETYTYRWIVPEDAGPGPGDPSSRLWL 150

                          170       180
                   ....*....|....*....|....*
gi 2024429024  181 YHSHIDAPRDVASGLVGPLIICKKG 205
Cdd:cd04229    151 YHSHVDVFAHTNAGLVGPIIVTSKG 175
CuRO_6_ceruloplasmin cd11012
The sixth cupredoxin domain of Ceruloplasmin; Ceruloplasmin is a multicopper oxidase essential ...
 218-356 5.39e-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: 179.29  E-value: 5.39e-52
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024429024  218 EFILMFSVMDENLSWYLDDNIRMYCSEPSKVDKDDEDFQESNKMHSINGYMYGYLPDLTMCVEDKVKWHLFGMGNEADIH 297
Cdd:cd11012      3 EFALLFLVFDENESWYLDENIKTYSDHPEKVNKEDEEFIESNKMHAINGKVFGNLQGLTMHVGDEVYWYLMGMGNEIDIH 82

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2024429024  298 SAYFHGQTLIERH---HRVDTINLFPATFIDALMIPRNPGEWLLSCQVNDHIEGGMQALFKV 356
Cdd:cd11012     83 TAHFHGHSFDYKHrgvYRSDVFDLFPGTFQTVEMIPRTPGTWLLHCHVTDHIHAGMETTYTV 144
CuRO_1_FV_like cd04226
The first cupredoxin domain of coagulation factor VIII and similar proteins; Factor V is an ...
 373-559 8.27e-52

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: 179.28  E-value: 8.27e-52
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024429024  373 RQYFIAAEEIIWNYGPsalnhftGQEliadsesyvffERSETRIGGSYKKAIYKEYTDGtftaHKKRLPEEEHLGLLGPV 452
Cdd:cd04226      1 REYYIAAQNIDWDYTP-------QSE-----------ELRLKRSEQSFKKIVYREYEEG----FKKEKPADLSSGLLGPT 58

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024429024  453 IKAEVGESIRVTFRNNASRPFSIQPHGVSYHKSNEGALYRTASRDTESPASHVSPGTTFTYEWTVPEDVGPTDQDPDCLT 532
Cdd:cd04226     59 LRAEVGDTLIVHFKNMADKPLSIHPQGIAYGKKSEGSLYSDNTSPVEKLDDAVQPGQEYTYVWDITEEVGPTEADPPCLT 138

                          170       180
                   ....*....|....*....|....*..
gi 2024429024  533 WLYYSAVNSVRDTSSGLVGPLMVCRKG 559
Cdd:cd04226    139 YIYYSHVNMVRDFNSGLIGALLICKKG 165
CuRO_3_ceruloplasmin cd04224
The third cupredoxin domain of Ceruloplasmin; Ceruloplasmin is a multicopper oxidase essential ...
 726-908 3.96e-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: 178.82  E-value: 3.96e-51
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024429024  726 HEKTHYIAAVEVEWDYSPNRTWEFERHQY-HKESPGNPFLNKDDKFIGSKYKKVVYREYTDQTFSIPKSRAEEEQHLQIQ 804
Cdd:cd04224      2 KVRHYFIAAEEIMWDYAPSGKNLFTGQNLtAPGSDSEVFFQRNETRIGGTYWKVRYVEYTDATFTTRKHRSKEEEHLGIL 81

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024429024  805 GPLIMSSIGDKINIVFKNLASRPYSIHAHGV------------KTDSSAVAITNPGETKMYVWKISARSGSERGDLHCTA 872
Cdd:cd04224     82 GPVIRAEVGDTIKVTFRNKASRPFSIQPHGVfyeknyegamyrDGDPSPGSHVSPGETFTYEWTVPEGVGPTNQDPPCLT 161

                          170       180       190
                   ....*....|....*....|....*....|....*.
gi 2024429024  873 WAYHSMVDIIKDTYSGLIGTLVVCPRHYLPSSHTRK 908
Cdd:cd04224    162 YLYFSAVDPVRDTNSGLVGPLLVCKKGSLNANGRQK 197
CuRO_5_FV_like cd14451
The fifth cupredoxin domain of coagulation factor V and similar proteins; Factor V is an ...
 21-205 3.35e-48

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: 169.25  E-value: 3.35e-48
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024429024   21 TREYYIGITETAWDYAP-GSTDLISGQRFAEeeqaevflkrgpqrigSTYKKAVYTQY---TSTLYDVIVEKPSWLGFLG 96
Cdd:cd14451      1 KRRYYIAAEEEEWDYAGyGKSRLDKTQNERD----------------TVFKKVVFRRYldsTFSTPDIQGEYEEHLGILG 64

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024429024   97 PIIKGEVGDSIVIHLKNFASRNYTLHPHGVKYTKENEGAFYPDNTKGFEKRDDAVKPGGQYTYTWDVTEDQGPAKGDADC 176
Cdd:cd14451     65 PVIRAEVDDVIQVFFKNLASRPYSLHAHGLSYEKSSEGLSYDDESPDWFKKDDAVQPNGTYTYVWYANPRSGPENNGSDC 144

                          170       180
                   ....*....|....*....|....*....
gi 2024429024  177 ITRVYHSHIDAPRDVASGLVGPLIICKKG 205
Cdd:cd14451    145 RTWAYYSAVNPEKDIHSGLIGPLLICRKG 173
CuRO_1_FVIII_like cd14452
The first cupredoxin domain of coagulation factor VIII and similar proteins; Factor VIII ...
 373-559 4.62e-48

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


Pssm-ID: 259994 [Multi-domain]  Cd Length: 173  Bit Score: 169.00  E-value: 4.62e-48
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024429024  373 RQYFIAAEEIIWNYGPSALNhftgqELIADSESYVFfersetRIGGSYKKAIYKEYTDGTFTAHKKRLPeeeHLGLLGPV 452
Cdd:cd14452      1 RRYYIAAVEIGWDYIHSDLG-----DPASEQRKKPK------DIPQKYIKAVFVEYLDATFTVPKPRPA---WMGLLGPT 66

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024429024  453 IKAEVGESIRVTFRNNASRPFSIQPHGVSYHKSNEGALYRTASRDTESPASHVSPGTTFTYEWTVPEDVGPTDQDPDCLT 532
Cdd:cd14452     67 IVAEVGDTVVITFKNLASQPYSLHAVGVSYWKASEGAGYDDSTSQHEKEDDAVYPGGYHTYVWDISPKDGPTGSDPECLT 146

                          170       180
                   ....*....|....*....|....*..
gi 2024429024  533 WLYYSAVNSVRDTSSGLVGPLMVCRKG 559
Cdd:cd14452    147 YSYSSQVDPVKDVNSGLIGALLVCRMG 173
CuRO_5_FVIII_like cd04228
The fifth cupredoxin domain of coagulation factor VIII and similar proteins; Factor VIII ...
 372-559 8.30e-48

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


Pssm-ID: 259890 [Multi-domain]  Cd Length: 169  Bit Score: 168.14  E-value: 8.30e-48
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024429024  372 IRQYFIAAEEIIWNYGPSALNHFtgqeLIADSESyvffeRSETRIGGSYKKAIYKEYTDGTFTAHKKRLPEEEHLGLLGP 451
Cdd:cd04228      1 IRHYFIAAVEVLWDYGMQRPQHF----LRARDPN-----RGRRKSVPQYKKVVFREYLDGSFTQPVYRGELDEHLGILGP 71

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024429024  452 VIKAEVGESIRVTFRNNASRPFSIQPHGVSYHksNEGAlyrtasrdTESPASHVSPGTTFTYEWTVPEDVGPTDQDPDCL 531
Cdd:cd04228     72 YIRAEVEDNIMVTFKNLASRPYSFHSSLISYE--EDQR--------AEPRGNFVQPGEVQTYSWKVLHQMAPTKQEFDCK 141

                          170       180
                   ....*....|....*....|....*...
gi 2024429024  532 TWLYYSAVNSVRDTSSGLVGPLMVCRKG 559
Cdd:cd04228    142 AWAYFSNVDLEKDLHSGLIGPLIICKTG 169
CuRO_3_FVIII_like cd04227
The third cupredoxin domain of coagulation factor VIII and similar proteins; Factor VIII ...
 371-558 1.17e-46

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: 165.10  E-value: 1.17e-46
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024429024  371 KIRQYFIAAEEIIWNYGPsalnhftgQELIADSESY--VFFERSETRIGGSYKKAIYKEYTDGTFtahKKRLPEEEHLGL 448
Cdd:cd04227      1 QTWEHYIAAEELDWDYAP--------LLSSTDDRELqsRYLPTGPQRIGYKYKKVAFVEYTDKTF---KRREAKQTEKGI 69

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024429024  449 LGPVIKAEVGESIRVTFRNNASRPFSIQPHGVSYHKSnegaLYRTASRDTESPASH--VSPGTTFTYEWTVPEDVGPTDQ 526
Cdd:cd04227     70 LGPLLKGEVGDQIHIMFKNTASRPYNIYPHGLTSVRP----MYRSRNPAGEKDLKTmpIGPGETFGYMWELTAEDGPTEE 145

                          170       180       190
                   ....*....|....*....|....*....|..
gi 2024429024  527 DPDCLTWLYYSAVNSVRDTSSGLVGPLMVCRK 558
Cdd:cd04227    146 DPRCLTRLYQSTVDPERDLASGLIGPLLICKK 177
CuRO_5_FV_like cd14451
The fifth cupredoxin domain of coagulation factor V and similar proteins; Factor V is an ...
 727-896 1.02e-44

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: 159.24  E-value: 1.02e-44
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024429024  727 EKTHYIAAVEVEWDYSPnrtweferhqyhkesPGNPFLNKDDKFIGSKYKKVVYREYTDQTFSIPKSRAEEEQHLQIQGP 806
Cdd:cd14451      1 KRRYYIAAEEEEWDYAG---------------YGKSRLDKTQNERDTVFKKVVFRRYLDSTFSTPDIQGEYEEHLGILGP 65

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024429024  807 LIMSSIGDKINIVFKNLASRPYSIHAHGVKTDSSAVAIT---------------NPGETKMYVWKISARSGSERGDLHCT 871
Cdd:cd14451     66 VIRAEVDDVIQVFFKNLASRPYSLHAHGLSYEKSSEGLSyddespdwfkkddavQPNGTYTYVWYANPRSGPENNGSDCR 145

                          170       180
                   ....*....|....*....|....*
gi 2024429024  872 AWAYHSMVDIIKDTYSGLIGTLVVC 896
Cdd:cd14451    146 TWAYYSAVNPEKDIHSGLIGPLLIC 170
CuRO_3_FVIII_like cd04227
The third cupredoxin domain of coagulation factor VIII and similar proteins; Factor VIII ...
 20-204 1.95e-44

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


Pssm-ID: 259889 [Multi-domain]  Cd Length: 177  Bit Score: 158.94  E-value: 1.95e-44
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024429024   20 VTREYYIGITETAWDYAP--GSTDlisgqrfaEEEQAEVFLKRGPQRIGSTYKKAVYTQYTSTLYDVIVEKPSWLGFLGP 97
Cdd:cd04227      1 QTWEHYIAAEELDWDYAPllSSTD--------DRELQSRYLPTGPQRIGYKYKKVAFVEYTDKTFKRREAKQTEKGILGP 72

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024429024   98 IIKGEVGDSIVIHLKNFASRNYTLHPHGVKYTKENEGAFYPDNTKgfEKRDDAVKPGGQYTYTWDVTEDQGPAKGDADCI 177
Cdd:cd04227     73 LLKGEVGDQIHIMFKNTASRPYNIYPHGLTSVRPMYRSRNPAGEK--DLKTMPIGPGETFGYMWELTAEDGPTEEDPRCL 150

                          170       180
                   ....*....|....*....|....*..
gi 2024429024  178 TRVYHSHIDAPRDVASGLVGPLIICKK 204
Cdd:cd04227    151 TRLYQSTVDPERDLASGLIGPLLICKK 177
CuRO_5_ceruloplasmin cd04225
The fifth cupredoxin domain of Ceruloplasmin; Ceruloplasmin is a multicopper oxidase essential ...
 22-204 4.69e-43

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: 154.55  E-value: 4.69e-43
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024429024   22 REYYIGITETAWDYAPGSTDLISGQRFAEEEQAEVFLKRGPQRIGSTYKKAVYTQYTSTLYDVIVEKPS---WLGFLGPI 98
Cdd:cd04225      1 RTYYIAAEEVEWDYSPQRTWEQELHNTHEESPGNAFLNKGDKFIGSKYKKVVYREYTDDTFSVPKERTAeeeHLGILGPL 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024429024   99 IKGEVGDSIVIHLKNFASRNYTLHPHGVKytkenegafypdnTKGFEKRddAVKPGGQYTYTWDVTEDQGPAKGDADCIT 178
Cdd:cd04225     81 IHAEVGEKVKIVFKNMASRPYSIHAHGVK-------------TDSSWVA--PTEPGETQTYTWKIPERSGPGVEDSNCIS 145

                          170       180
                   ....*....|....*....|....*.
gi 2024429024  179 RVYHSHIDAPRDVASGLVGPLIICKK 204
Cdd:cd04225    146 WAYYSTVDQIKDLYSGLIGPLVICRR 171
CuRO_5_FVIII_like cd04228
The fifth cupredoxin domain of coagulation factor VIII and similar proteins; Factor VIII ...
 730-898 5.50e-42

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


Pssm-ID: 259890 [Multi-domain]  Cd Length: 169  Bit Score: 151.58  E-value: 5.50e-42
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024429024  730 HYIAAVEVEWDYSPNRTWEFERHQYHKESPGNPFlnkddkfigSKYKKVVYREYTDQTFSIPKSRAEEEQHLQIQGPLIM 809
Cdd:cd04228      4 YFIAAVEVLWDYGMQRPQHFLRARDPNRGRRKSV---------PQYKKVVFREYLDGSFTQPVYRGELDEHLGILGPYIR 74

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024429024  810 SSIGDKINIVFKNLASRPYSIHAHGVKTDSSAVA-----ITNPGETKMYVWKISARSGSERGDLHCTAWAYHSMVDIIKD 884
Cdd:cd04228     75 AEVEDNIMVTFKNLASRPYSFHSSLISYEEDQRAeprgnFVQPGEVQTYSWKVLHQMAPTKQEFDCKAWAYFSNVDLEKD 154

                          170
                   ....*....|....
gi 2024429024  885 TYSGLIGTLVVCPR 898
Cdd:cd04228    155 LHSGLIGPLIICKT 168
CuRO_6_FVIII_like cd11018
The sixth cupredoxin domain of coagulation factor VIII and similar proteins; Factor VIII ...
 912-1052 7.34e-42

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


Pssm-ID: 259904 [Multi-domain]  Cd Length: 144  Bit Score: 150.03  E-value: 7.34e-42
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024429024  912 FALLFMVFDENESWYLDENIETYSANPHLVDKENEEFLESNKMHAINGKVFGNLHGLTMHVGDEVSWYLMAMGNEIDIHT 991
Cdd:cd11018      4 FALLFTIFDETKSWYFEENMRRNCRPPCHIQTQDPWFHINNKFHAINGYVADTLPGLVMAQHQRIRWHLLNMGSDEEIHS 83

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2024429024  992 AHFHGHSFDYKQTEVYRADVFDLFPGTFQTVEMIPQNPGVWLLHCHVTDHIHAGMEATYTV 1052
Cdd:cd11018     84 VHFHGLPFTVRAKKEYRMGVYNLYPGVFGTVEMRPSTAGIWLVECTVGEHLLAGMSALFLV 144
CuRO_1_Ceruloplasmin_like_1 cd04229
cupredoxin domain of ceruloplasmin homologs; Uncharacterized subfamily of ceruloplasmin ...
 728-895 2.41e-40

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


Pssm-ID: 259891 [Multi-domain]  Cd Length: 175  Bit Score: 146.79  E-value: 2.41e-40
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024429024  728 KTHYIAAVEVEWDYSP-NRTWEFERHQYHKESPGnpfLNKDDKFIGSKYKKVVYREYTDQTFSIPKSraeEEQHLQIQGP 806
Cdd:cd04229      1 RTYYIAAEEVDWDYAPsGKNKCCLGDDLEVSTLD---SQPGPYTIGSTYTKARYREYTDNSFSTPKP---TPAYLGILGP 74

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024429024  807 LIMSSIGDKINIVFKN-LASRPYSIHAHGV-------KTDSSAVAITNPGETKMYVWKISARSGSERGDLHCTAWAYHSM 878
Cdd:cd04229     75 VIRAEVGDTIKVVFKNnLDEFPVNMHPHGGlyskdneGTTDGAGDVVAPGETYTYRWIVPEDAGPGPGDPSSRLWLYHSH 154

                          170
                   ....*....|....*..
gi 2024429024  879 VDIIKDTYSGLIGTLVV 895
Cdd:cd04229    155 VDVFAHTNAGLVGPIIV 171
CuRO_6_ceruloplasmin cd11012
The sixth cupredoxin domain of Ceruloplasmin; Ceruloplasmin is a multicopper oxidase essential ...
 573-711 2.65e-40

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: 145.78  E-value: 2.65e-40
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024429024  573 EFFLLATVFDENLSWYLDDNILMFTAKPNEIDKDNEDFQESNKMHSINGYMYGNQPGLEMCKGDVISWHLMGLGSEVDVH 652
Cdd:cd11012      3 EFALLFLVFDENESWYLDENIKTYSDHPEKVNKEDEEFIESNKMHAINGKVFGNLQGLTMHVGDEVYWYLMGMGNEIDIH 82

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2024429024  653 GIYFSQNTF---VTKGARKDTANLFPHTFVTAIMKPDSEGIFEVSCLTTDHYRGGMKQKYKV 711
Cdd:cd11012     83 TAHFHGHSFdykHRGVYRSDVFDLFPGTFQTVEMIPRTPGTWLLHCHVTDHIHAGMETTYTV 144
CuRO_1_ceruloplasmin cd04222
The first cupredoxin domain of Ceruloplasmin; Ceruloplasmin is a multicopper oxidase essential ...
 728-898 2.73e-38

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: 141.40  E-value: 2.73e-38
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024429024  728 KTHYIAAVEVEWDYSPNRTWEFERHQYHKESPGNPFLNKDDKFIGSKYKKVVYREYTDQTFSIpksRAEEEQHLQIQGPL 807
Cdd:cd04222      1 REYYIGIRETQWDYAPSGKNLITNQTFDDDEHASVFLKRGPDRIGRVYKKAVYLQYTDDTYRT---EIEKPVWLGFLGPI 77

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024429024  808 IMSSIGDKINIVFKNLASRPYSIHAHGV---KTDSSAVAITN------------PGETKMYVWKISARSGSERGDLHCTA 872
Cdd:cd04222     78 LKAEVGDVIVVHLKNFASRPYSLHPHGVfynKENEGALYPDNtsgfekaddavpPGGSYTYTWTVPEEQAPTKADANCLT 157

                          170       180
                   ....*....|....*....|....*.
gi 2024429024  873 WAYHSMVDIIKDTYSGLIGTLVVCPR 898
Cdd:cd04222    158 RIYHSHIDAPKDIASGLIGPLIICKK 183
CuRO_3_FV_like cd14450
The third cupredoxin domain of coagulation factor V and similar proteins; Factor V is an ...
 729-896 9.30e-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: 139.63  E-value: 9.30e-38
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024429024  729 THYIAAVEVEWDYSPNRTWEFERHQYHKespgnpFLNKDDKFIGSKYKKVVYREYTDQTFSIPkSRAEEEQHLQIQGPLI 808
Cdd:cd14450      4 EYFIAAEEVIWDYAPSIPENMDKRYRSQ------YLDNFSNNIGKKYKKAVFTQYEDGSFTKR-LENPRPKEEGILGPVI 76

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024429024  809 MSSIGDKINIVFKNLASRPYSIHAHGVKTDSSAVAIT---------------NPGETKMYVWKISARSGSERGDLHCTAW 873
Cdd:cd14450     77 RAQVRDTIKIVFKNKASRPYSIYPHGVTVSKAAEGASyppdprgnetqnkavQPGETYTYKWNILETDEPTARDPRCLTR 156

                          170       180
                   ....*....|....*....|...
gi 2024429024  874 AYHSMVDIIKDTYSGLIGTLVVC 896
Cdd:cd14450    157 MYHSAVDITRDIASGLIGPLLIC 179
CuRO_3_FVIII_like cd04227
The third cupredoxin domain of coagulation factor VIII and similar proteins; Factor VIII ...
 729-896 1.83e-37

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: 138.91  E-value: 1.83e-37
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024429024  729 THYIAAVEVEWDYSPNRTWEFERhqyhkeSPGNPFLNKDDKFIGSKYKKVVYREYTDQTFsipKSRAEEEQHLQIQGPLI 808
Cdd:cd04227      4 EHYIAAEELDWDYAPLLSSTDDR------ELQSRYLPTGPQRIGYKYKKVAFVEYTDKTF---KRREAKQTEKGILGPLL 74

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024429024  809 MSSIGDKINIVFKNLASRPYSIHAHGV--------------KTDSSAVAITnPGETKMYVWKISARSGSERGDLHCTAWA 874
Cdd:cd04227     75 KGEVGDQIHIMFKNTASRPYNIYPHGLtsvrpmyrsrnpagEKDLKTMPIG-PGETFGYMWELTAEDGPTEEDPRCLTRL 153

                          170       180
                   ....*....|....*....|..
gi 2024429024  875 YHSMVDIIKDTYSGLIGTLVVC 896
Cdd:cd04227    154 YQSTVDPERDLASGLIGPLLIC 175
CuRO_6_FVIII_like cd11018
The sixth cupredoxin domain of coagulation factor VIII and similar proteins; Factor VIII ...
 218-356 9.51e-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: 135.39  E-value: 9.51e-37
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024429024  218 EFILMFSVMDENLSWYLDDNIRMYCSEPSKVDKDDEDFQESNKMHSINGYMYGYLPDLTMCVEDKVKWHLFGMGNEADIH 297
Cdd:cd11018      3 EFALLFTIFDETKSWYFEENMRRNCRPPCHIQTQDPWFHINNKFHAINGYVADTLPGLVMAQHQRIRWHLLNMGSDEEIH 82

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2024429024  298 SAYFHGQTLIER---HHRVDTINLFPATFIDALMIPRNPGEWLLSCQVNDHIEGGMQALFKV 356
Cdd:cd11018     83 SVHFHGLPFTVRakkEYRMGVYNLYPGVFGTVEMRPSTAGIWLVECTVGEHLLAGMSALFLV 144
CuRO_6_FV_like cd14455
The sixth cupredoxin domain of coagulation factor V and similar proteins; Factor V is an ...
 912-1052 4.80e-34

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


Pssm-ID: 259997 [Multi-domain]  Cd Length: 140  Bit Score: 127.67  E-value: 4.80e-34
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024429024  912 FALLFMVFDENESWYLDENIETYSANPHLVDKEneeFLESNKMHAINGKVFgNLHGLTMHVGDEVSWYLMAMGNEIDIHT 991
Cdd:cd14455      4 FVLLFMTFDEEKSWYYEKNRKRTCRENRVKDPN---VQDNHTFHAINGIIY-NLKGLRMYTNELVRWHLINMGGPKDLHV 79

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2024429024  992 AHFHGHSFDYKQTEVYRADVFDLFPGTFQTVEMIPQNPGVWLLHCHVTDHIHAGMEATYTV 1052
Cdd:cd14455     80 VHFHGQTFTEKGLKDHQLGVYPLLPGSFATLEMKPSKPGLWLLETEVGESQQRGMQTLFLV 140
CuRO_2_ceruloplasmin_like_2 cd11023
cupredoxin domain of ceruloplasmin homologs; Uncharacterized subfamily of ceruloplasmin ...
 918-1052 4.88e-34

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


Pssm-ID: 259909 [Multi-domain]  Cd Length: 118  Bit Score: 126.57  E-value: 4.88e-34
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024429024  918 VFDENESWYLDENIEtysanphlvdkeneeflESNKMHAINGKVFGNLHGLTMHVGDEVSWYLMAMGNEIDIHTAHFHGH 997
Cdd:cd11023      3 EFIENSSIFLDLNVE-----------------EAGLMHSINGYVFGNLPGVTIAKGKRVRWHLVAYGNEVDFHTPHWHGQ 65

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 2024429024  998 SFDYKQTEvyRADVFDLFPGTFQTVEMIPQNPGVWLLHCHVTDHIHAGMEATYTV 1052
Cdd:cd11023     66 TVEADKSR--RTDVAELMPASMRVADMTAADVGTWLLHCHVHDHYMAGMMTQFAV 118
CuRO_2_ceruloplasmin_like_2 cd11023
cupredoxin domain of ceruloplasmin homologs; Uncharacterized subfamily of ceruloplasmin ...
 251-356 5.74e-33

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


Pssm-ID: 259909 [Multi-domain]  Cd Length: 118  Bit Score: 123.87  E-value: 5.74e-33
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024429024  251 DDEDFQESNKMHSINGYMYGYLPDLTMCVEDKVKWHLFGMGNEADIHSAYFHGQTL-IERHHRVDTINLFPATFIDALMI 329
Cdd:cd11023     12 LDLNVEEAGLMHSINGYVFGNLPGVTIAKGKRVRWHLVAYGNEVDFHTPHWHGQTVeADKSRRTDVAELMPASMRVADMT 91

                           90       100
                   ....*....|....*....|....*..
gi 2024429024  330 PRNPGEWLLSCQVNDHIEGGMQALFKV 356
Cdd:cd11023     92 AADVGTWLLHCHVHDHYMAGMMTQFAV 118
CuRO_2_FV_like cd14453
The second cupredoxin domain of coagulation factor V and similar proteins; Factor V is an ...
 216-356 6.14e-33

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


Pssm-ID: 259995 [Multi-domain]  Cd Length: 123  Bit Score: 123.81  E-value: 6.14e-33
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024429024  216 DAEFILMFSVMDENLSWYlddnirmycsepskvdkdDEDFQESNKMHSINGYMYGYLPDLTMCVEDKVKWHLFGMGNEAD 295
Cdd:cd14453      1 YKEYVLMFGVFDENKSWY------------------KQNASVDSVKYTINGYTNGTLPDVSICAYDHVSWHLLGMSSEPE 62

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2024429024  296 IHSAYFHGQTLIERHHRVDTINLFPATFIDALMIPRNPGEWLLSCQVNDHIEGGMQALFKV 356
Cdd:cd14453     63 LFSVHFNGQVLEQNGHKVSAVGLVSGSSTTASMTVVHTGRWLISSLIMKHLQAGMYGYLNI 123
CuRO_1_FVIII_like cd14452
The first cupredoxin domain of coagulation factor VIII and similar proteins; Factor VIII ...
 728-896 9.78e-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: 125.09  E-value: 9.78e-33
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024429024  728 KTHYIAAVEVEWDYSpnrtweferHQYHKESPGNPflNKDDKFIGSKYKKVVYREYTDQTFSIPKSRAEeeqHLQIQGPL 807
Cdd:cd14452      1 RRYYIAAVEIGWDYI---------HSDLGDPASEQ--RKKPKDIPQKYIKAVFVEYLDATFTVPKPRPA---WMGLLGPT 66

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024429024  808 IMSSIGDKINIVFKNLASRPYSIHAHGVK----------TDSSAVA-----ITNPGETKMYVWKISARSGSERGDLHCTA 872
Cdd:cd14452     67 IVAEVGDTVVITFKNLASQPYSLHAVGVSywkasegagyDDSTSQHekeddAVYPGGYHTYVWDISPKDGPTGSDPECLT 146

                          170       180
                   ....*....|....*....|....
gi 2024429024  873 WAYHSMVDIIKDTYSGLIGTLVVC 896
Cdd:cd14452    147 YSYSSQVDPVKDVNSGLIGALLVC 170
CuRO_5_FVIII_like cd04228
The fifth cupredoxin domain of coagulation factor VIII and similar proteins; Factor VIII ...
 21-205 1.38e-32

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: 124.61  E-value: 1.38e-32
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024429024   21 TREYYIGITETAWDYAPGS-------TDLISGQRfaeeeqaevflKRGPQrigstYKKAVYTQYTSTLYDVIV---EKPS 90
Cdd:cd04228      1 IRHYFIAAVEVLWDYGMQRpqhflraRDPNRGRR-----------KSVPQ-----YKKVVFREYLDGSFTQPVyrgELDE 64

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024429024   91 WLGFLGPIIKGEVGDSIVIHLKNFASRNYTLHPHGVKYtkenegafypDNTKGFEKRDDAVKPGGQYTYTWDVTEDQGPA 170
Cdd:cd04228     65 HLGILGPYIRAEVEDNIMVTFKNLASRPYSFHSSLISY----------EEDQRAEPRGNFVQPGEVQTYSWKVLHQMAPT 134

                          170       180       190
                   ....*....|....*....|....*....|....*
gi 2024429024  171 KGDADCITRVYHSHIDAPRDVASGLVGPLIICKKG 205
Cdd:cd04228    135 KQEFDCKAWAYFSNVDLEKDLHSGLIGPLIICKTG 169
CuRO_6_FV_like cd14455
The sixth cupredoxin domain of coagulation factor V and similar proteins; Factor V is an ...
 218-356 1.33e-31

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: 120.74  E-value: 1.33e-31
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024429024  218 EFILMFSVMDENLSWYLDDNIRMYCSEpskVDKDDEDFQESNKMHSINGYMYGyLPDLTMCVEDKVKWHLFGMGNEADIH 297
Cdd:cd14455      3 EFVLLFMTFDEEKSWYYEKNRKRTCRE---NRVKDPNVQDNHTFHAINGIIYN-LKGLRMYTNELVRWHLINMGGPKDLH 78

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2024429024  298 SAYFHGQTLIE---RHHRVDTINLFPATFIDALMIPRNPGEWLLSCQVNDHIEGGMQALFKV 356
Cdd:cd14455     79 VVHFHGQTFTEkglKDHQLGVYPLLPGSFATLEMKPSKPGLWLLETEVGESQQRGMQTLFLV 140
CuRO_4_FVIII_like cd11016
The fourth cupredoxin domain of coagulation factor VIII and similar proteins; Factor VIII ...
 216-359 1.79e-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: 120.36  E-value: 1.79e-31
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024429024  216 DAEFILMFSVMDENLSWYLDDNIRMYCSEPSKVDKDDEDFQESNKMHSINGYMYGYLpDLTMCVEDKVKWHLFGMGNEAD 295
Cdd:cd11016      1 DKDWSLLFSVFDENNSWYLKENIHRFTQTPAGVNDTDPDFYASNVMHTINGIVFDRR-QFVICLTDVAYWYVLSVGAQTD 79

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2024429024  296 IHSAYFHGQTLIERHHRVDTINLFPATFIDALMIPRNPGEWLLSCQVNDHIEGGMQALFKVEGC 359
Cdd:cd11016     80 FLSVFFSGNTFKHQMVYEDVLTLFPFSGETVSMSPEVPGEWELGCFNGDFRSRGMSAQYTVSTC 143
CuRO_4_FVIII_like cd11016
The fourth cupredoxin domain of coagulation factor VIII and similar proteins; Factor VIII ...
 576-714 3.11e-31

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


Pssm-ID: 259902 [Multi-domain]  Cd Length: 143  Bit Score: 119.59  E-value: 3.11e-31
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024429024  576 LLATVFDENLSWYLDDNILMFTAKPNEIDKDNEDFQESNKMHSINGYMYGNQPgLEMCKGDVISWHLMGLGSEVDVHGIY 655
Cdd:cd11016      6 LLFSVFDENNSWYLKENIHRFTQTPAGVNDTDPDFYASNVMHTINGIVFDRRQ-FVICLTDVAYWYVLSVGAQTDFLSVF 84

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 2024429024  656 FSQNTFVTKGARKDTANLFPHTFVTAIMKPDSEGIFEVSCLTTDHYRGGMKQKYKVKPC 714
Cdd:cd11016     85 FSGNTFKHQMVYEDVLTLFPFSGETVSMSPEVPGEWELGCFNGDFRSRGMSAQYTVSTC 143
CuRO_4_FV_like cd14454
The fourth cupredoxin domain of coagulation factor V and similar proteins; Factor V is an ...
 216-355 2.38e-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: 117.28  E-value: 2.38e-30
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024429024  216 DAEFILMFSVMDENLSWYLDDNIRMYCSEPSKVDKDDEDFQESNKMHSINGYMYGYLPDLTMCVEDKVKWHLFGMGNEAD 295
Cdd:cd14454      1 DLEQHAVFAVFDENKSWYLEENINKYCSNPNNVKKDDPKFYKSNIMPTINGYAYESSAPLGFCHSEVVQWHISSVGTQDE 80

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024429024  296 IHSAYFHGQTLIERHHRVDTINLFPATFIDALMIPRNPGEWLLSCQVNDHIEGGMQALFK 355
Cdd:cd14454     81 IITVHLSGHTFRYKGKHEDTLNLFPMSGESITVTMDNLGTWLLGSFGSSKKSKGLRVRFT 140
CuRO_2_FVIII_like cd11015
The second cupredoxin domain of coagulation factor VIII and similar proteins; Factor VIII ...
 218-356 2.58e-30

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: 116.54  E-value: 2.58e-30
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024429024  218 EFILMFSVMDENLSWYLDDnirmycSEPSKVDKDDEDfQESNKMHSINGYMYGYLPDLTMCVEDKVKWHLFGMGNEADIH 297
Cdd:cd11015      3 AFVLLFAVFDEGKSWYSEV------GERKSRDKFKRA-DSRKEFHTINGYINASLPGLKICQRKPVIWHVIGMGTAPEVH 75

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 2024429024  298 SAYFHGQTLIERHHRVDTINLFPATFIDALMIPRNPGEWLLSCQVNDHIEGGMQALFKV 356
Cdd:cd11015     76 SIFFEGHTFLVRTHRKVSLEISPMTFLTAQTKPATVGSFLIFCQIHSHQHDGMEAMVKV 134
CuRO_4_FVIII_like cd11016
The fourth cupredoxin domain of coagulation factor VIII and similar proteins; Factor VIII ...
 911-1053 2.01e-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: 114.58  E-value: 2.01e-29
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024429024  911 RFALLFMVFDENESWYLDENIETYSANPHLVDKENEEFLESNKMHAINGKVFGNLHgLTMHVGDEVSWYLMAMGNEIDIH 990
Cdd:cd11016      3 DWSLLFSVFDENNSWYLKENIHRFTQTPAGVNDTDPDFYASNVMHTINGIVFDRRQ-FVICLTDVAYWYVLSVGAQTDFL 81

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2024429024  991 TAHFHGHSFDYKQteVYRaDVFDLFPGTFQTVEMIPQNPGVWLLHCHVTDHIHAGMEATYTVL 1053
Cdd:cd11016     82 SVFFSGNTFKHQM--VYE-DVLTLFPFSGETVSMSPEVPGEWELGCFNGDFRSRGMSAQYTVS 141
CuRO_4_FV_like cd14454
The fourth cupredoxin domain of coagulation factor V and similar proteins; Factor V is an ...
 579-714 7.13e-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: 113.04  E-value: 7.13e-29
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024429024  579 TVFDENLSWYLDDNILMFTAKPNEIDKDNEDFQESNKMHSINGYMYGNQPGLEMCKGDVISWHLMGLGSEVDVHGIYFSQ 658
Cdd:cd14454      9 AVFDENKSWYLEENINKYCSNPNNVKKDDPKFYKSNIMPTINGYAYESSAPLGFCHSEVVQWHISSVGTQDEIITVHLSG 88

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 2024429024  659 NTFVTKGARKDTANLFPHTFVTAIMKPDSEGIFEVSCLTTDHYRGGMKQKYKVKPC 714
Cdd:cd14454     89 HTFRYKGKHEDTLNLFPMSGESITVTMDNLGTWLLGSFGSSKKSKGLRVRFTDVIC 144
CuRO_6_FVIII_like cd11018
The sixth cupredoxin domain of coagulation factor VIII and similar proteins; Factor VIII ...
 572-711 7.73e-29

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: 112.67  E-value: 7.73e-29
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024429024  572 REFFLLATVFDENLSWYLDDNILMFTAKPNEIDKDNEDFQESNKMHSINGYMYGNQPGLEMCKGDVISWHLMGLGSEVDV 651
Cdd:cd11018      2 QEFALLFTIFDETKSWYFEENMRRNCRPPCHIQTQDPWFHINNKFHAINGYVADTLPGLVMAQHQRIRWHLLNMGSDEEI 81

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2024429024  652 HGIYFSQNTFVTKGA---RKDTANLFPHTFVTAIMKPDSEGIFEVSCLTTDHYRGGMKQKYKV 711
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 ...
 915-1034 1.42e-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: 109.19  E-value: 1.42e-27
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024429024  915 LFMVFDENESWYLDENIETYSANPHLVDKENEEFLESNKMHAINGKVFGNLHGLTMHVGDEVSWYLMAMGNEIDIHTAHF 994
Cdd:cd14454      7 VFAVFDENKSWYLEENINKYCSNPNNVKKDDPKFYKSNIMPTINGYAYESSAPLGFCHSEVVQWHISSVGTQDEIITVHL 86

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|
gi 2024429024  995 HGHSFDYKQTEvyrADVFDLFPGTFQTVEMIPQNPGVWLL 1034
Cdd:cd14454     87 SGHTFRYKGKH---EDTLNLFPMSGESITVTMDNLGTWLL 123
CuRO_1_FV_like cd04226
The first cupredoxin domain of coagulation factor VIII and similar proteins; Factor V is an ...
 730-896 2.87e-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: 2.87e-27
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024429024  730 HYIAAVEVEWDYSPnrtweferhQYHKESPgnpflnkddKFIGSKYKKVVYREYtDQTFSIPKSRAEEEQHLqiqGPLIM 809
Cdd:cd04226      3 YYIAAQNIDWDYTP---------QSEELRL---------KRSEQSFKKIVYREY-EEGFKKEKPADLSSGLL---GPTLR 60

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024429024  810 SSIGDKINIVFKNLASRPYSIHAHGVK----------TDSS--------AVAitnPGETKMYVWKISARSGSERGDLHCT 871
Cdd:cd04226     61 AEVGDTLIVHFKNMADKPLSIHPQGIAygkksegslySDNTspveklddAVQ---PGQEYTYVWDITEEVGPTEADPPCL 137

                          170       180
                   ....*....|....*....|....*
gi 2024429024  872 AWAYHSMVDIIKDTYSGLIGTLVVC 896
Cdd:cd04226    138 TYIYYSHVNMVRDFNSGLIGALLIC 162
CuRO_2_ceruloplasmin_like_2 cd11023
cupredoxin domain of ceruloplasmin homologs; Uncharacterized subfamily of ceruloplasmin ...
 606-711 6.74e-24

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


Pssm-ID: 259909 [Multi-domain]  Cd Length: 118  Bit Score: 97.68  E-value: 6.74e-24
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024429024  606 DNEDFQESNKMHSINGYMYGNQPGLEMCKGDVISWHLMGLGSEVDVHGIYFSQNTFVTKGARK-DTANLFPHTFVTAIMK 684
Cdd:cd11023     12 LDLNVEEAGLMHSINGYVFGNLPGVTIAKGKRVRWHLVAYGNEVDFHTPHWHGQTVEADKSRRtDVAELMPASMRVADMT 91

                           90       100
                   ....*....|....*....|....*..
gi 2024429024  685 PDSEGIFEVSCLTTDHYRGGMKQKYKV 711
Cdd:cd11023     92 AADVGTWLLHCHVHDHYMAGMMTQFAV 118
CuRO_2_FVIII_like cd11015
The second cupredoxin domain of coagulation factor VIII and similar proteins; Factor VIII ...
 572-711 1.25e-23

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


Pssm-ID: 259901 [Multi-domain]  Cd Length: 134  Bit Score: 97.67  E-value: 1.25e-23
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024429024  572 REFFLLATVFDENLSWYLDdnilmfTAKPNEIDKDNEDfQESNKMHSINGYMYGNQPGLEMCKGDVISWHLMGLGSEVDV 651
Cdd:cd11015      2 QAFVLLFAVFDEGKSWYSE------VGERKSRDKFKRA-DSRKEFHTINGYINASLPGLKICQRKPVIWHVIGMGTAPEV 74

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024429024  652 HGIYFSQNTFVTKGARKDTANLFPHTFVTAIMKPDSEGIFEVSCLTTDHYRGGMKQKYKV 711
Cdd:cd11015     75 HSIFFEGHTFLVRTHRKVSLEISPMTFLTAQTKPATVGSFLIFCQIHSHQHDGMEAMVKV 134
CuRO_2_FVIII_like cd11015
The second cupredoxin domain of coagulation factor VIII and similar proteins; Factor VIII ...
 911-1052 1.56e-20

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: 88.81  E-value: 1.56e-20
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024429024  911 RFALLFMVFDENESWYLDenietySANPHLVDKENEEFlESNKMHAINGKVFGNLHGLTMHVGDEVSWYLMAMGNEIDIH 990
Cdd:cd11015      3 AFVLLFAVFDEGKSWYSE------VGERKSRDKFKRAD-SRKEFHTINGYINASLPGLKICQRKPVIWHVIGMGTAPEVH 75

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2024429024  991 TAHFHGHSFDYKQtevYRADVFDLFPGTFQTVEMIPQNPGVWLLHCHVTDHIHAGMEATYTV 1052
Cdd:cd11015     76 SIFFEGHTFLVRT---HRKVSLEISPMTFLTAQTKPATVGSFLIFCQIHSHQHDGMEAMVKV 134
Cu-oxidase_2 pfam07731
Multicopper oxidase; This entry contains many divergent copper oxidase-like domains that are ...
 952-1056 3.05e-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: 85.18  E-value: 3.05e-19
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024429024  952 NKMHAINGKVFG-NLHGLTMHVGDEVSWYLMamGNEIDIHTAHFHGHSFD----------YKQTEVY------RADVFDL 1014
Cdd:pfam07731   19 RNDWAINGLLFPpNTNVITLPYGTVVEWVLQ--NTTTGVHPFHLHGHSFQvlgrgggpwpEEDPKTYnlvdpvRRDTVQV 96

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|..
gi 2024429024 1015 FPGTFQTVEMIPQNPGVWLLHCHVTDHIHAGMEATYTVLPKE 1056
Cdd:pfam07731   97 PPGGWVAIRFRADNPGVWLFHCHILWHLDQGMMGQFVVRPGD 138
CuRO_6_FV_like cd14455
The sixth cupredoxin domain of coagulation factor V and similar proteins; Factor V is an ...
 572-711 1.79e-18

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


Pssm-ID: 259997 [Multi-domain]  Cd Length: 140  Bit Score: 82.99  E-value: 1.79e-18
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024429024  572 REFFLLATVFDENLSWYLDDNILMFTAKPNEIDKDnedFQESNKMHSINGYMYgNQPGLEMCKGDVISWHLMGLGSEVDV 651
Cdd:cd14455      2 REFVLLFMTFDEEKSWYYEKNRKRTCRENRVKDPN---VQDNHTFHAINGIIY-NLKGLRMYTNELVRWHLINMGGPKDL 77

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2024429024  652 HGIYFSQNTFVTKGARKDTAN---LFPHTFVTAIMKPDSEGIFEVSCLTTDHYRGGMKQKYKV 711
Cdd:cd14455     78 HVVHFHGQTFTEKGLKDHQLGvypLLPGSFATLEMKPSKPGLWLLETEVGESQQRGMQTLFLV 140
CuRO_2_FV_like cd14453
The second cupredoxin domain of coagulation factor V and similar proteins; Factor V is an ...
 572-705 2.49e-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: 82.21  E-value: 2.49e-18
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024429024  572 REFFLLATVFDENLSWYlddnilmftakpneidkdNEDFQESNKMHSINGYMYGNQPGLEMCKGDVISWHLMGLGSEVDV 651
Cdd:cd14453      2 KEYVLMFGVFDENKSWY------------------KQNASVDSVKYTINGYTNGTLPDVSICAYDHVSWHLLGMSSEPEL 63

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....
gi 2024429024  652 HGIYFSQNTFVTKGARKDTANLFPHTFVTAIMKPDSEGIFEVSCLTTDHYRGGM 705
Cdd:cd14453     64 FSVHFNGQVLEQNGHKVSAVGLVSGSSTTASMTVVHTGRWLISSLIMKHLQAGM 117
CuRO_2_FV_like cd14453
The second cupredoxin domain of coagulation factor V and similar proteins; Factor V is an ...
 912-1048 6.45e-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: 81.06  E-value: 6.45e-18
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024429024  912 FALLFMVFDENESWYldenietysanphlvdkeNEEFLESNKMHAINGKVFGNLHGLTMHVGDEVSWYLMAMGNEIDIHT 991
Cdd:cd14453      4 YVLMFGVFDENKSWY------------------KQNASVDSVKYTINGYTNGTLPDVSICAYDHVSWHLLGMSSEPELFS 65

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 2024429024  992 AHFHGHSFDYKQtevYRADVFDLFPGTFQTVEMIPQNPGVWLLHCHVTDHIHAGMEA 1048
Cdd:cd14453     66 VHFNGQVLEQNG---HKVSAVGLVSGSSTTASMTVVHTGRWLISSLIMKHLQAGMYG 119
CuRO_1_LCC_like cd04206
Cupredoxin domain 1 of laccase-like multicopper oxidases; including laccase, CueO, spore coat ...
 93-202 3.18e-17

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


Pssm-ID: 259869 [Multi-domain]  Cd Length: 120  Bit Score: 78.87  E-value: 3.18e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024429024   93 GFLGPIIKGEVGDSIVIHLKN-FASRNYTLHPHGVKYTKENEGAFYPDNTKgfekrdDAVKPGGQYTYTWDVTEDQGpak 171
Cdd:cd04206     27 QFPGPTIRVKEGDTVEVTVTNnLPNEPTSIHWHGLRQPGTNDGDGVAGLTQ------CPIPPGESFTYRFTVDDQAG--- 97

                           90       100       110
                   ....*....|....*....|....*....|.
gi 2024429024  172 gdadciTRVYHSHIDAprDVASGLVGPLIIC 202
Cdd:cd04206     98 ------TFWYHSHVGG--QRADGLYGPLIVE 120
CuRO_1_LCC_like cd04206
Cupredoxin domain 1 of laccase-like multicopper oxidases; including laccase, CueO, spore coat ...
 435-556 2.26e-16

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: 76.17  E-value: 2.26e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024429024  435 AHKKRLPEEEHLGLLGPVIKAEVGESIRVTFRNN-ASRPFSIQPHGVSYHKSNE--GALYRTASrdtespasHVSPGTTF 511
Cdd:cd04206     15 DGVLRQVITVNGQFPGPTIRVKEGDTVEVTVTNNlPNEPTSIHWHGLRQPGTNDgdGVAGLTQC--------PIPPGESF 86

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*
gi 2024429024  512 TYEWTVPEDVGptdqdpdclTWLYYSAVNSVRDTssGLVGPLMVC 556
Cdd:cd04206     87 TYRFTVDDQAG---------TFWYHSHVGGQRAD--GLYGPLIVE 120
CuRO_3_LCC_like cd04207
Cupredoxin domain 3 of laccase-like multicopper oxidases; including laccase, CueO, spore coat ...
 956-1051 3.17e-14

Cupredoxin domain 3 of laccase-like multicopper oxidases; including laccase, CueO, spore coat protein A, ascorbate oxidase and similar proteins; Laccase-like multicopper oxidases (MCOs) in this family contain three cupredoxin domains. They are able to couple oxidation of substrates with reduction of dioxygen to water. MCOs are capable of oxidizing a vast range of substrates, varying from aromatic to inorganic compounds such as metals. Although the members of this family have diverse functions, majority of them have three cupredoxin domain repeats. The copper ions are bound in several sites; Type 1, Type 2, and/or Type 3. The ensemble of types 2 and 3 copper is called a trinuclear cluster. MCOs oxidize their substrate by accepting electrons at a mononuclear copper center and transferring them to the active site trinuclear copper center. The cupredoxin domain 3 of 3-domain MCOs contains the Type 1 (T1) copper binding site and part the trinuclear copper binding site, which is located at the interface of domains 1 and 3. Also included in this family are cupredoxin domains 2, 4, and 6 of the 6-domain MCO ceruloplasmin and similar proteins.


Pssm-ID: 259870 [Multi-domain]  Cd Length: 132  Bit Score: 70.57  E-value: 3.17e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024429024  956 AINGKVF----GNLHGLTMHVGDEVSWYLMAMGNEIDIHTAHFHGHSF------------DYKQTEVYRADVFDLFPGTF 1019
Cdd:cd04207     21 VINGMPFkegdANTDIFSVEAGDVVEIVLINAGNHDMQHPFHLHGHSFwvlgsgggpfdaPLNLTNPPWRDTVLVPPGGW 100

                           90       100       110
                   ....*....|....*....|....*....|..
gi 2024429024 1020 QTVEMIPQNPGVWLLHCHVTDHIHAGMEATYT 1051
Cdd:cd04207    101 VVIRFKADNPGVWMLHCHILEHEDAGMMTVFE 132
CuRO_1_2DMCO_NIR_like_2 cd14449
The cupredoxin domain 1 of a two-domain laccase related to nitrite reductase; The two-domain ...
 450-558 1.85e-11

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


Pssm-ID: 259991 [Multi-domain]  Cd Length: 135  Bit Score: 62.67  E-value: 1.85e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024429024  450 GPVIKAEVGESIRVTFRNNASRPFSIQPHGVSYHKSNEGALyrtasrdteSPASHVSPGTTFTYEWTVPEDVGPTDQDPD 529
Cdd:cd14449     29 GPVIEVREGDTLKILFRNTLDVPASLHPHGVDYTTASDGTG---------MNASIVAPGDTRIYTWRTHGGYRRADGSWA 99

                           90       100       110
                   ....*....|....*....|....*....|....*.
gi 2024429024  530 CLT---WLYYSAV----NSVRDTSSGLVGPLMVCRK 558
Cdd:cd14449    100 EGTagyWHYHDHVfgteHGTEGLSRGLYGALIVRRV 135
Cu-oxidase_3 pfam07732
Multicopper oxidase; This entry contains many divergent copper oxidase-like domains that are ...
 76-201 2.07e-11

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: 62.26  E-value: 2.07e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024429024   76 QYTSTLYDVIVEKPSWL---GFLGPIIKGEVGDSIVIHLKNFASRNYTLHPHGVKYTKENEGAFYPDNTKgfekrdDAVK 152
Cdd:pfam07732    3 TYGTVSPLGGTRQAVIGvngQFPGPTIRVREGDTVVVNVTNNLDEPTSIHWHGLQQRGTPWMDGVPGVTQ------CPIP 76

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*....
gi 2024429024  153 PGGQYTYTWDVTEDQGpakgdadciTRVYHSHIDAPRdvASGLVGPLII 201
Cdd:pfam07732   77 PGQSFTYRFQVKQQAG---------TYWYHSHTSGQQ--AAGLAGAIII 114
CuRO_D2_2dMcoN_like cd04202
The second cupredoxin domain of bacterial two domain multicopper oxidase McoN and similar ...
 954-1046 3.09e-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: 62.27  E-value: 3.09e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024429024  954 MHAINGKVFGNLHGLTMHVGDEVSWYLMAMGNeiDIHTAHFHGHSF-----DYKQTEV---YRADVFDLFPGTFQTVEMI 1025
Cdd:cd04202     29 YFTINGKSFPATPPLVVKEGDRVRIRLINLSM--DHHPMHLHGHFFlvtatDGGPIPGsapWPKDTLNVAPGERYDIEFV 106

                           90       100
                   ....*....|....*....|.
gi 2024429024 1026 PQNPGVWLLHCHVTDHIHAGM 1046
Cdd:cd04202    107 ADNPGDWMFHCHKLHHAMNGM 127
CuRO_3_CumA_like cd13906
The third cupredoxin domain of CumA like multicopper oxidase; This multicopper oxidase (MCO) ...
 956-1052 5.77e-11

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: 61.63  E-value: 5.77e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024429024  956 AINGKVFGNLHG-------LTMHVGDevsWYLMAMGNEID-IHTAHFHGHSF-----DYKQTEV-YRADVFDLFPGtfQT 1021
Cdd:cd13906     30 AINGTSWTGGDHshlppplATLKRGR---SYVLRLVNETAfLHPMHLHGHFFrvlsrNGRPVPEpFWRDTVLLGPK--ET 104

                           90       100       110
                   ....*....|....*....|....*....|...
gi 2024429024 1022 VE--MIPQNPGVWLLHCHVTDHIHAGMEATYTV 1052
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 ...
 96-201 3.85e-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: 3.85e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024429024   96 GPIIKGEVGDSIVIHLKNFASRNYTLHPHGVKYTKENEGAFYPDNtkgfekrddAVKPGGQYTYTWDVTEDQGPAKGDAD 175
Cdd:cd14449     29 GPVIEVREGDTLKILFRNTLDVPASLHPHGVDYTTASDGTGMNAS---------IVAPGDTRIYTWRTHGGYRRADGSWA 99

                           90       100       110
                   ....*....|....*....|....*....|...
gi 2024429024  176 CITR---VYHSHI----DAPRDVASGLVGPLII 201
Cdd:cd14449    100 EGTAgywHYHDHVfgteHGTEGLSRGLYGALIV 132
CuRO_1_Diphenol_Ox cd13857
The first cupredoxin domain of fungal laccase, diphenol oxidase; Diphenol oxidase belongs to ...
 94-201 2.70e-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: 56.11  E-value: 2.70e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024429024   94 FLGPIIKGEVGDSIVIHLKNFASRNYTLHPHGVKytkeNEGAFYPDNTKGFEKRddAVKPGGQYTYTWDVTEDQGpakgd 173
Cdd:cd13857     28 FPGPLIEANQGDRIVVHVTNELDEPTSIHWHGLF----QNGTNWMDGTAGITQC--PIPPGGSFTYNFTVDGQYG----- 96

                           90       100
                   ....*....|....*....|....*...
gi 2024429024  174 adciTRVYHSHIDAprDVASGLVGPLII 201
Cdd:cd13857     97 ----TYWYHSHYST--QYADGLVGPLIV 118
CuRO_1_CumA_like cd13861
The first cupredoxin domain of CumA like multicopper oxidase; This multicopper oxidase (MCO) ...
 447-555 2.71e-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: 2.71e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024429024  447 GLLGPVIKAEVGESIRVTFRNNASRPFSIQPHGVsyhksnegalyRTASR-D-----TESPashVSPGTTFTYEWTVPeD 520
Cdd:cd13861     28 QVPGPELRVRQGDTLRVRLTNRLPEPTTIHWHGL-----------RLPNAmDgvpglTQPP---VPPGESFTYEFTPP-D 92

                           90       100       110
                   ....*....|....*....|....*....|....*
gi 2024429024  521 VGptdqdpdclTWLYYSAVNSVRDTSSGLVGPLMV 555
Cdd:cd13861     93 AG---------TYWYHPHVGSQEQLDRGLYGPLIV 118
SufI COG2132
Multicopper oxidase with three cupredoxin domains (includes cell division protein FtsP and ...
 954-1054 4.57e-09

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


Pssm-ID: 441735 [Multi-domain]  Cd Length: 423  Bit Score: 59.95  E-value: 4.57e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024429024  954 MHAINGKVFGNLH-GLTMHVGDEVSWYLMAMGNeiDIHTAHFHGHSF------DYKQTEVYRADVFDLFPGtfQTVEMI- 1025
Cdd:COG2132    317 VWTINGKAFDPDRpDLTVKLGERERWTLVNDTM--MPHPFHLHGHQFqvlsrnGKPPPEGGWKDTVLVPPG--ETVRILf 392

                           90       100       110
                   ....*....|....*....|....*....|.
gi 2024429024 1026 --PQNPGVWLLHCHVTDHIHAGMEATYTVLP 1054
Cdd:COG2132    393 rfDNYPGDWMFHCHILEHEDAGMMGQFEVVP 423
CuRO_3_Fet3p cd13899
The third Cupredoxin domain of multicopper oxidase Fet3p; Fet3p catalyzes the ferroxidase ...
 990-1054 8.71e-09

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: 55.72  E-value: 8.71e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024429024  990 HTAHFHGHSFD--YKQTEVY----------------RADVFDLFPGTFQTVEMIPQNPGVWLLHCHVTDHIHAGMEATYT 1051
Cdd:cd13899     78 HPFHLHGHKFQvvQRSPDVAsddpnppinefpenpmRRDTVMVPPGGSVVIRFRADNPGVWFFHCHIEWHLEAGLAATFI 157


                   ...
gi 2024429024 1052 VLP 1054
Cdd:cd13899    158 EAP 160
CuRO_3_McoC_like cd13902
The third cupredoxin domain of a multicopper oxidase McoC and similar proteins; This family ...
 954-1052 9.87e-09

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: 54.71  E-value: 9.87e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024429024  954 MHAINGKVFG-NLHGLTMHVGDEVSWYLMamgNEIDI-HTAHFHGHSF------DYKQTEVYRA--DVFDLFPGTFQTVE 1023
Cdd:cd13902     20 MFLINGKTFDmNRIDFVAKVGEVEVWEVT---NTSHMdHPFHLHGTQFqvleidGNPQKPEYRAwkDTVNLPPGEAVRIA 96

                           90       100
                   ....*....|....*....|....*....
gi 2024429024 1024 MIPQNPGVWLLHCHVTDHIHAGMEATYTV 1052
Cdd:cd13902     97 TRQDDPGMWMYHCHILEHEDAGMMGMLHV 125
CuRO_3_CumA_like cd13906
The third cupredoxin domain of CumA like multicopper oxidase; This multicopper oxidase (MCO) ...
 284-356 1.70e-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: 1.70e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024429024  284 KWHLFGMGNEAD-IHSAYFHG----------QTLIERHHRvDTINLFPATFIDALMIPRNPGEWLLSCQVNDHIEGGMQA 352
Cdd:cd13906     55 RSYVLRLVNETAfLHPMHLHGhffrvlsrngRPVPEPFWR-DTVLLGPKETVDIAFVADNPGDWMFHCHILEHQETGMMG 133


                   ....
gi 2024429024  353 LFKV 356
Cdd:cd13906    134 VIRV 137
CuRO_3_LCC_like cd04207
Cupredoxin domain 3 of laccase-like multicopper oxidases; including laccase, CueO, spore coat ...
 263-354 2.46e-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: 53.62  E-value: 2.46e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024429024  263 SING----YMYGYLPDLTMCVEDKVKWHLFGMGNEADIHSAYFHGQtlierHHRV--------------------DTINL 318
Cdd:cd04207     21 VINGmpfkEGDANTDIFSVEAGDVVEIVLINAGNHDMQHPFHLHGH-----SFWVlgsgggpfdaplnltnppwrDTVLV 95

                           90       100       110
                   ....*....|....*....|....*....|....*.
gi 2024429024  319 FPATFIDALMIPRNPGEWLLSCQVNDHIEGGMQALF 354
Cdd:cd04207     96 PPGGWVVIRFKADNPGVWMLHCHILEHEDAGMMTVF 131
CuRO_1_2DMCO_NIR_like cd11024
The cupredoxin domain 1 of a two-domain laccase related to nitrite reductase; The two-domain ...
 96-201 3.17e-08

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


Pssm-ID: 259910 [Multi-domain]  Cd Length: 119  Bit Score: 53.04  E-value: 3.17e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024429024   96 GPIIKGEVGDSIVIHLKNFASRNYTLHPHGVKYTKENEGAFYPdntkgfekrddaVKPGGQYTYTWDVTedqgPAKgdad 175
Cdd:cd11024     32 GPTLRATEGDLVRIHFINTGDHPHTIHFHGIHDAAMDGTGLGP------------IMPGESFTYEFVAE----PAG---- 91

                           90       100
                   ....*....|....*....|....*...
gi 2024429024  176 ciTRVYHSHIdAP--RDVASGLVGPLII 201
Cdd:cd11024     92 --THLYHCHV-QPlkEHIAMGLYGAFIV 116
CuRO_1_LCC_like cd04206
Cupredoxin domain 1 of laccase-like multicopper oxidases; including laccase, CueO, spore coat ...
 802-896 3.61e-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: 53.06  E-value: 3.61e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024429024  802 QIQGPLIMSSIGDKINIVFKN-LASRPYSIHAHGVK----TDSSAVAITN-----PGETKMYVWKISARSGsergdlhcT 871
Cdd:cd04206     27 QFPGPTIRVKEGDTVEVTVTNnLPNEPTSIHWHGLRqpgtNDGDGVAGLTqcpipPGESFTYRFTVDDQAG--------T 98

                           90       100
                   ....*....|....*....|....*
gi 2024429024  872 AWaYHSMVDIikDTYSGLIGTLVVC 896
Cdd:cd04206     99 FW-YHSHVGG--QRADGLYGPLIVE 120
CuRO_1_CumA_like cd13861
The first cupredoxin domain of CumA like multicopper oxidase; This multicopper oxidase (MCO) ...
 93-201 3.69e-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: 53.01  E-value: 3.69e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024429024   93 GFLGPIIKGEVGDSIVIHLKNFASRNYTLHPHGVKYTKENEGAfyPDNTKgfekrdDAVKPGGQYTYTWdVTEDQGpakg 172
Cdd:cd13861     28 QVPGPELRVRQGDTLRVRLTNRLPEPTTIHWHGLRLPNAMDGV--PGLTQ------PPVPPGESFTYEF-TPPDAG---- 94

                           90       100
                   ....*....|....*....|....*....
gi 2024429024  173 dadciTRVYHSHIDAPRDVASGLVGPLII 201
Cdd:cd13861     95 -----TYWYHPHVGSQEQLDRGLYGPLIV 118
CuRO_1_Abr2_like cd13850
The first cupredoxin domain of a group of fungal Laccases similar to Abr2 from Aspergillus ...
 87-201 4.33e-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: 52.69  E-value: 4.33e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024429024   87 EKPSWLG---FLGPIIKGEVGDSIVIHLKNFASRNYTLHPHGVkytkENEGAFYPDNTKGFEKRddAVKPGGQYTYTWDV 163
Cdd:cd13850     16 EREVILIngqFPGPPIILDEGDEVEILVTNNLPVNTTIHFHGI----LQRGTPWSDGVPGVTQW--PIQPGGSFTYRWKA 89

                           90       100       110
                   ....*....|....*....|....*....|....*....
gi 2024429024  164 TEDQGpakgdadciTRVYHSHIdapRDVAS-GLVGPLII 201
Cdd:cd13850     90 EDQYG---------LYWYHSHY---RGYYMdGLYGPIYI 116
CuRO_3_MaLCC_like cd13901
The third cupredoxin domain of the fungal laccases similar to Ma-LCC from Melanocarpus ...
 970-1046 5.35e-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: 53.38  E-value: 5.35e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024429024  970 MHVGDEVSWYLMAMGNEIDI-HTAHFHGHSF----------DYKQTEVY-----RADVFDLFPGTFQTVEMIPQNPGVWL 1033
Cdd:cd13901     60 IELPKANKWVYIVIQNNSPLpHPIHLHGHDFyilaqgtgtfDDDGTILNlnnppRRDVAMLPAGGYLVIAFKTDNPGAWL 139

                           90
                   ....*....|...
gi 2024429024 1034 LHCHVTDHIHAGM 1046
Cdd:cd13901    140 MHCHIAWHASGGL 152
Cu-oxidase pfam00394
Multicopper oxidase; Many of the proteins in this family contain multiple similar copies of ...
 223-359 5.60e-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: 53.09  E-value: 5.60e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024429024  223 FSVMDENLSWYlDDNIRMYCSEPSKVDKDDEDFQESNKMHSINGYMYGYLPDLTMCVEDKVKWHLFgMGNEADIHSAYFH 302
Cdd:pfam00394    1 EDYVITLSDWY-HKDAKDLEKELLASGKAPTDFPPVPDAVLINGKDGASLATLTVTPGKTYRLRII-NVALDDSLNFSIE 78

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2024429024  303 GQ--TLIE---RHH---RVDTINLFPATFIDALMIP-RNPGEWLLSCQVN-DHIEGGMQALFKVEGC 359
Cdd:pfam00394   79 GHkmTVVEvdgVYVnpfTVDSLDIFPGQRYSVLVTAnQDPGNYWIVASPNiPAFDNGTAAAILRYSG 145
CuRO_D1_2dMcoN_like cd13859
The first cupredoxin domain of bacterial two domain multicopper oxidase McoN and similar ...
 96-201 5.64e-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: 5.64e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024429024   96 GPIIKGEVGDSIVIHLKNFASRNYTLHPHGVKYTkeneGAFYPDNTKGFEKRddAVKPGGQYTYTWDVtEDQGpakgdad 175
Cdd:cd13859     31 GPLIHVKEGDDLVVHVTNNTTLPHTIHWHGVLQM----GSWKMDGVPGVTQP--AIEPGESFTYKFKA-ERPG------- 96

                           90       100
                   ....*....|....*....|....*..
gi 2024429024  176 ciTRVYHSHIDAPRDVA-SGLVGPLII 201
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 ...
 450-535 8.52e-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: 51.89  E-value: 8.52e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024429024  450 GPVIKAEVGESIRVTFRNNASRPFSIQPHGVsyhksnegalYRTASRDTESPAshVSPGTTFTYEWtVPEDVGptdqdpd 529
Cdd:cd11024     32 GPTLRATEGDLVRIHFINTGDHPHTIHFHGI----------HDAAMDGTGLGP--IMPGESFTYEF-VAEPAG------- 91


                   ....*.
gi 2024429024  530 clTWLY 535
Cdd:cd11024     92 --THLY 95
SufI COG2132
Multicopper oxidase with three cupredoxin domains (includes cell division protein FtsP and ...
 94-224 1.04e-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: 55.71  E-value: 1.04e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024429024   94 FLGPIIKGEVGDSIVIHLKNFASRNYTLHPHGVKYTKENEGafYPdntkgfekrDDAVKPGGQYTYTWDVteDQGPAkgd 173
Cdd:COG2132     42 YPGPTIRVREGDRVRVRVTNRLPEPTTVHWHGLRVPNAMDG--VP---------GDPIAPGETFTYEFPV--PQPAG--- 105

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 2024429024  174 adciTRVYHSHIDA--PRDVASGLVGPLIIckkgamNKDNDKY--VDAEFILMFS 224
Cdd:COG2132    106 ----TYWYHPHTHGstAEQVYRGLAGALIV------EDPEEDLprYDRDIPLVLQ 150
CuRO_3_MCO_like_2 cd13908
The third cupredoxin domain of uncharacterized multicopper oxidase; Multicopper Oxidases (MCOs) ...
 928-1048 1.54e-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: 51.30  E-value: 1.54e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024429024  928 DENIE-TYSANPHLVDKENeeflesnkMHAINGKVFGNLHG-LTMHVGDEvswYLMAMGNEI-DIHTAHFHGHSF----- 999
Cdd:cd13908      1 DETIDmTFEKRNAGDGGFN--------LWTINGKSYPDEDPpLVVQQGRR---YRLVFRNASdDAHPMHLHRHTFevtri 69

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*....
gi 2024429024 1000 DYKQTEVYRADVFDLFPGTFQTVEMIPQNPGVWLLHCHVTDHIHAGMEA 1048
Cdd:cd13908     70 DGKPTSGLRKDVVMLGGYQRVEVDFVADNPGLTLFHCHQQLHMDYGFMA 118
CuRO_1_2DMCO_NIR_like_2 cd14449
The cupredoxin domain 1 of a two-domain laccase related to nitrite reductase; The two-domain ...
 803-879 1.60e-07

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


Pssm-ID: 259991 [Multi-domain]  Cd Length: 135  Bit Score: 51.50  E-value: 1.60e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024429024  803 IQGPLIMSSIGDKINIVFKNLASRPYSIHAHGVKTDSSAV------AITNPGETKMYVWKISARSGSERGDLHCTA---W 873
Cdd:cd14449     27 VPGPVIEVREGDTLKILFRNTLDVPASLHPHGVDYTTASDgtgmnaSIVAPGDTRIYTWRTHGGYRRADGSWAEGTagyW 106


                   ....*.
gi 2024429024  874 AYHSMV 879
Cdd:cd14449    107 HYHDHV 112
CuRO_1_2dMco_1 cd13860
The first cupredoxin domain of bacteria two domain multicopper oxidase; This subfamily ...
 96-201 2.04e-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: 50.66  E-value: 2.04e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024429024   96 GPIIKGEVGDSIVIHLKNFASRNYTLHPHGVKYTKENEGAfyPDNTKgfekrdDAVKPGGQYTYTWDVTEdQGpakgdad 175
Cdd:cd13860     31 GPTIEVTEGDRVRILVTNELPEPTTVHWHGLPVPNGMDGV--PGITQ------PPIQPGETFTYEFTAKQ-AG------- 94

                           90       100
                   ....*....|....*....|....*.
gi 2024429024  176 ciTRVYHSHIDAPRDVASGLVGPLII 201
Cdd:cd13860     95 --TYMYHSHVDEAKQEDMGLYGAFIV 118
CuRO_3_CopA cd13896
The third cupredoxin domain of CopA copper resistance protein family; CopA is a multicopper ...
 957-1046 2.19e-07

The third cupredoxin domain of CopA copper resistance protein family; CopA is a multicopper oxidase (MCO) related to laccase and L-ascorbate oxidase, both copper-containing enzymes. It is part of the copper-regulatory cue operon, which employs a cytosolic metalloregulatory protein CueR that induces expression of CopA and CueO under copper stress conditions. CopA is a copper efflux P-type ATPase that is located in the inner cell membrane and is is involved in copper resistance in bacteria. CopA mutant causes a loss of function including copper tolerance and oxidase activity and copA transcription is inducible in the presence of copper. Although MCOs have diverse functions, majority of them have three cupredoxin domain repeats that include one mononuclear and one trinuclear copper center. The copper ions are bound in several sites: Type 1, Type 2, and/or Type 3. The ensemble of types 2 and 3 copper is called a trinuclear cluster. MCOs oxidize their substrate by accepting electrons at a mononuclear copper center and transferring them to the active site trinuclear copper center. The cupredoxin domain 3 of 3-domain MCOs contains the Type 1 (T1) copper binding site and part the trinuclear copper binding site, which is located at the interface of domains 1 and 3.


Pssm-ID: 259963 [Multi-domain]  Cd Length: 115  Bit Score: 50.33  E-value: 2.19e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024429024  957 INGKVFGNLHGLTMHVGDEVswyLMAMGNEIDI-HTAHFHGHSFDY---KQTEVYRADVFDLFPGTFQTVEMIPQNPGVW 1032
Cdd:cd13896     19 INGKAYPDADPLRVREGERV---RIVFVNDTMMaHPMHLHGHFFQVengNGEYGPRKDTVLVPPGETVSVDFDADNPGRW 95

                           90
                   ....*....|....
gi 2024429024 1033 LLHCHVTDHIHAGM 1046
Cdd:cd13896     96 AFHCHNLYHMEAGM 109
PLN02191 PLN02191
L-ascorbate oxidase
 94-224 3.04e-07

L-ascorbate oxidase


Pssm-ID: 177843 [Multi-domain]  Cd Length: 574  Bit Score: 54.63  E-value: 3.04e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024429024   94 FLGPIIKGEVGDSIVIHLKN-FASRNYTLHPHGVKytkeNEGAFYPDNTKGFEKRddAVKPGGQYTYTWDVtEDQGpakg 172
Cdd:PLN02191    51 FPGPTIDAVAGDTIVVHLTNkLTTEGLVIHWHGIR----QKGSPWADGAAGVTQC--AINPGETFTYKFTV-EKPG---- 119

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|..
gi 2024429024  173 dadciTRVYHSHIDAPRdvASGLVGPLIIckKGAMNKDNDKYVDAEFILMFS 224
Cdd:PLN02191   120 -----THFYHGHYGMQR--SAGLYGSLIV--DVAKGPKERLRYDGEFNLLLS 162
CuRO_1_MaLCC_like cd13854
The first cupredoxin domain of the fungal laccases similar to Ma-LCC from Melanocarpus ...
 96-201 3.51e-07

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


Pssm-ID: 259923 [Multi-domain]  Cd Length: 122  Bit Score: 49.93  E-value: 3.51e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024429024   96 GPIIKGEVGDSIVIHLKNFASRNYT-LHPHGV--KYTKENEGAfyPDNTKGfekrddAVKPGGQYTYTWDVTEdQGpakg 172
Cdd:cd13854     33 GPLIEANWGDTIEVTVINKLQDNGTsIHWHGIrqLNTNWQDGV--PGVTEC------PIAPGDTRTYRFRATQ-YG---- 99

                           90       100
                   ....*....|....*....|....*....
gi 2024429024  173 dadciTRVYHSHIDAprDVASGLVGPLII 201
Cdd:cd13854    100 -----TSWYHSHYSA--QYGDGVVGPIVI 121
CuRO_D2_2dMcoN_like cd04202
The second cupredoxin domain of bacterial two domain multicopper oxidase McoN and similar ...
 216-357 4.55e-07

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


Pssm-ID: 259865 [Multi-domain]  Cd Length: 138  Bit Score: 50.33  E-value: 4.55e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024429024  216 DAEFILMFSvmdenlSWYLDDNirmycSEPSKVDKDDEDFqesnkmHSINGYMYGYLPDLTMCVEDKVKWHLFGMGNeaD 295
Cdd:cd04202      1 DRDYTLVLQ------EWFVDPG-----TTPMPPEGMDFNY------FTINGKSFPATPPLVVKEGDRVRIRLINLSM--D 61

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2024429024  296 IHSAYFHGQT---------LIERHHRV--DTINLFPATFIDALMIPRNPGEWLLSCQVNDHIE----GGMQALFKVE 357
Cdd:cd04202     62 HHPMHLHGHFflvtatdggPIPGSAPWpkDTLNVAPGERYDIEFVADNPGDWMFHCHKLHHAMngmgGGMMTLIGYE 138
CuRO_1_AAO cd13845
The first cupredoxin domain of plant Ascorbate oxidase; Ascorbate oxidase catalyzes the ...
 93-201 6.70e-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: 49.37  E-value: 6.70e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024429024   93 GFLGPIIKGEVGDSIVIHLKN-FASRNYTLHPHGVKytkeNEGAFYPDNTKGFEKRddAVKPGGQYTYTWDVteDQgPAk 171
Cdd:cd13845     27 QFPGPTIRATAGDTIVVELENkLPTEGVAIHWHGIR----QRGTPWADGTASVSQC--PINPGETFTYQFVV--DR-PG- 96

                           90       100       110
                   ....*....|....*....|....*....|
gi 2024429024  172 gdadciTRVYHSHIDAPRdvASGLVGPLII 201
Cdd:cd13845     97 ------TYFYHGHYGMQR--SAGLYGSLIV 118
CuRO_1_Diphenol_Ox cd13857
The first cupredoxin domain of fungal laccase, diphenol oxidase; Diphenol oxidase belongs to ...
 450-555 7.39e-07

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


Pssm-ID: 259926 [Multi-domain]  Cd Length: 119  Bit Score: 49.18  E-value: 7.39e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024429024  450 GPVIKAEVGESIRVTFRNNASRPFSIQPHGVSYHKSNEgalYRTASRDTESPashVSPGTTFTYEWTVPEDVGptdqdpd 529
Cdd:cd13857     30 GPLIEANQGDRIVVHVTNELDEPTSIHWHGLFQNGTNW---MDGTAGITQCP---IPPGGSFTYNFTVDGQYG------- 96

                           90       100
                   ....*....|....*....|....*.
gi 2024429024  530 clTWLYYSAVNSvrDTSSGLVGPLMV 555
Cdd:cd13857     97 --TYWYHSHYST--QYADGLVGPLIV 118
CuRO_3_MCO_like_3 cd13909
The third cupredoxin domain of uncharacterized multicopper oxidase; Multicopper Oxidases (MCOs) ...
 990-1046 9.72e-07

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


Pssm-ID: 259976 [Multi-domain]  Cd Length: 137  Bit Score: 49.44  E-value: 9.72e-07
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2024429024  990 HTAHFHGHSFdyKQTEVYRA-----DVFDLFPGTFQTVEMIPQNPGVWLLHCHVTDHIHAGM 1046
Cdd:cd13909     71 HGMHLHGHHF--RAILPNGAlgpwrDTLLMDRGETREIAFVADNPGDWLLHCHMLEHAAAGM 130
CuRO_3_Tv-LCC_like cd13903
The third cupredoxin domain of the fungal laccases similar to Tv-LCC from Trametes Versicolor; ...
 984-1046 1.28e-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: 49.20  E-value: 1.28e-06
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2024429024  984 GNEIDIHTAHFHGHSFDYKQ---TEVY------RADVFDL-FPGTFQTVEMIPQNPGVWLLHCHVTDHIHAGM 1046
Cdd:cd13903     67 GAIGGPHPFHLHGHAFSVVRsagSNTYnyvnpvRRDVVSVgTPGDGVTIRFVTDNPGPWFLHCHIDWHLEAGL 139
Cu-oxidase_3 pfam07732
Multicopper oxidase; This entry contains many divergent copper oxidase-like domains that are ...
 448-555 1.56e-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: 1.56e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024429024  448 LLGPVIKAEVGESIRVTFRNNASRPFSIQPHGVSYHKSNE--GALYrtasrdteSPASHVSPGTTFTYEWTVPEDVGptd 525
Cdd:pfam07732   24 FPGPTIRVREGDTVVVNVTNNLDEPTSIHWHGLQQRGTPWmdGVPG--------VTQCPIPPGQSFTYRFQVKQQAG--- 92

                           90       100       110
                   ....*....|....*....|....*....|
gi 2024429024  526 qdpdclTWLYYSAVNSVRdtSSGLVGPLMV 555
Cdd:pfam07732   93 ------TYWYHSHTSGQQ--AAGLAGAIII 114
CuRO_1_2dMco_1 cd13860
The first cupredoxin domain of bacteria two domain multicopper oxidase; This subfamily ...
 450-555 1.64e-06

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


Pssm-ID: 259929 [Multi-domain]  Cd Length: 119  Bit Score: 47.96  E-value: 1.64e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024429024  450 GPVIKAEVGESIRVTFRNNASRPFSIQPHGVSYHKSNEGAlyrtasrdTESPASHVSPGTTFTYEWTVpEDVGptdqdpd 529
Cdd:cd13860     31 GPTIEVTEGDRVRILVTNELPEPTTVHWHGLPVPNGMDGV--------PGITQPPIQPGETFTYEFTA-KQAG------- 94

                           90       100
                   ....*....|....*....|....*.
gi 2024429024  530 clTWLYYSAVNSVRDTSSGLVGPLMV 555
Cdd:cd13860     95 --TYMYHSHVDEAKQEDMGLYGAFIV 118
PLN02191 PLN02191
L-ascorbate oxidase
 988-1046 1.72e-06

L-ascorbate oxidase


Pssm-ID: 177843 [Multi-domain]  Cd Length: 574  Bit Score: 52.32  E-value: 1.72e-06
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2024429024  988 DIHTAHFHGHSF--------------DYKQTEVYRADVFD---LFPGTFQTVEMIPQNPGVWLLHCHVTDHIHAGM 1046
Cdd:PLN02191   465 EIHPWHLHGHDFwvlgygdgkfkpgiDEKTYNLKNPPLRNtaiLYPYGWTAIRFVTDNPGVWFFHCHIEPHLHMGM 540
ascorbase TIGR03388
L-ascorbate oxidase, plant type; Members of this protein family are the copper-containing ...
 94-233 1.97e-06

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: 52.06  E-value: 1.97e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024429024   94 FLGPIIKGEVGDSIVIHLKN-FASRNYTLHPHGVKytkeNEGAFYPDNTKGFEKRddAVKPGGQYTYTWdVTEDQGpakg 172
Cdd:TIGR03388   29 FPGPTIRAQAGDTIVVELTNkLHTEGVVIHWHGIR----QIGTPWADGTAGVTQC--AINPGETFIYNF-VVDRPG---- 97

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2024429024  173 dadciTRVYHSHIDAPRdvASGLVGPLIIcKKGAMNKDNDKYvDAEFILMFSvmdenlSWY 233
Cdd:TIGR03388   98 -----TYFYHGHYGMQR--SAGLYGSLIV-DVPDGEKEPFHY-DGEFNLLLS------DWW 143
CuRO_3_AAO cd13893
The third cupredoxin domain of plant Ascorbate oxidase; Ascorbate oxidase catalyzes the ...
 985-1046 2.54e-06

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


Pssm-ID: 259960 [Multi-domain]  Cd Length: 155  Bit Score: 48.57  E-value: 2.54e-06
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2024429024  985 NEIDIHTAHFHGHSF------DYKQTEVYRA-----------DVFDLFPGTFQTVEMIPQNPGVWLLHCHVTDHIHAGM 1046
Cdd:cd13893     62 NASEQHPWHLHGHDFwvlgygLGGFDPAADPsslnlvnppmrNTVTIFPYGWTALRFKADNPGVWAFHCHIEWHFHMGM 140
CuRO_1_Tv-LCC_like cd13856
The first cupredoxin domain of fungal laccases similar to Tv-LCC from Trametes versicolor; ...
 94-201 4.35e-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: 46.95  E-value: 4.35e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024429024   94 FLGPIIKGEVGDSIVIHLKNFAS-----RNYTLHPHGVKYTKENegafYPDNTKGFEKRddAVKPGGQYTYTWDVTEDQG 168
Cdd:cd13856     28 FPGPLITANKGDTFRITVVNQLTdptmrRSTSIHWHGIFQHGTN----YADGPAFVTQC--PIAPNHSFTYDFTAGDQAG 101

                           90       100       110
                   ....*....|....*....|....*....|...
gi 2024429024  169 pakgdadciTRVYHSHIDAprDVASGLVGPLII 201
Cdd:cd13856    102 ---------TFWYHSHLST--QYCDGLRGPLVI 123
CuRO_1_2DMCO_NIR_like cd11024
The cupredoxin domain 1 of a two-domain laccase related to nitrite reductase; The two-domain ...
 990-1055 8.41e-06

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


Pssm-ID: 259910 [Multi-domain]  Cd Length: 119  Bit Score: 46.11  E-value: 8.41e-06
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2024429024  990 HTAHFHGHSFDYKQTEVYRadvfDLFPGTFQTVEMIPQNPGVWLLHCHV---TDHIHAGMEATYTVLPK 1055
Cdd:cd11024     55 HTIHFHGIHDAAMDGTGLG----PIMPGESFTYEFVAEPAGTHLYHCHVqplKEHIAMGLYGAFIVDPK 119
CuRO_1_Tv-LCC_like cd13856
The first cupredoxin domain of fungal laccases similar to Tv-LCC from Trametes versicolor; ...
 450-555 8.47e-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: 46.18  E-value: 8.47e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024429024  450 GPVIKAEVGESIRVTFRNNAS-----RPFSIQPHGVSYHKSN--EGALYRtasrdTESPashVSPGTTFTYEWTVPEDVG 522
Cdd:cd13856     30 GPLITANKGDTFRITVVNQLTdptmrRSTSIHWHGIFQHGTNyaDGPAFV-----TQCP---IAPNHSFTYDFTAGDQAG 101

                           90       100       110
                   ....*....|....*....|....*....|...
gi 2024429024  523 ptdqdpdclTWLYYSAVNSvrDTSSGLVGPLMV 555
Cdd:cd13856    102 ---------TFWYHSHLST--QYCDGLRGPLVI 123
CuRO_1_LCC_plant cd13849
The first cupredoxin domain of plant laccases; Laccase is a blue multicopper oxidase (MCO) ...
 94-201 1.14e-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: 1.14e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024429024   94 FLGPIIKGEVGDSIVIHLKNFASRNYTLHPHGVKYTKENegafYPDNTKGFEKRddAVKPGGQYTYTWDVTEDQGpakgd 173
Cdd:cd13849     26 FPGPTIRVHEGDTVVVNVTNRSPYNITIHWHGIRQLRSG----WADGPAYITQC--PIQPGQSYTYRFTVTGQEG----- 94

                           90       100
                   ....*....|....*....|....*...
gi 2024429024  174 adciTRVYHSHIDAPRdvaSGLVGPLII 201
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, ...
 94-201 1.15e-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: 45.64  E-value: 1.15e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024429024   94 FLGPIIKGEVGDSIVIHLKNFASRNYTLHPHGVKYTKENEGAfyPDNTkgfekrddaVKPGGQYTYTWDVteDQGPAkgd 173
Cdd:cd04232     29 YLGPTIRVKKGDTVRINVTNNLDEETTVHWHGLHVPGEMDGG--PHQP---------IAPGQTWSPTFTI--DQPAA--- 92

                           90       100       110
                   ....*....|....*....|....*....|
gi 2024429024  174 adciTRVYHSHIDA--PRDVASGLVGPLII 201
Cdd:cd04232     93 ----TLWYHPHTHGktAEQVYRGLAGLFII 118
CuRO_1_Fet3p cd13851
The first Cupredoxin domain of multicopper oxidase Fet3P; Fet3p catalyzes the ferroxidase ...
 97-201 1.43e-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: 45.34  E-value: 1.43e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024429024   97 PIIKGEVGDSIVIHLKN-FASRNYTLHPHGV--KYTKENEGAFY----PdntkgfekrddaVKPGGQYTYTWDVTEDQGp 169
Cdd:cd13851     32 PPIEVNKGDTVVIHATNsLGDQPTSLHFHGLfqNGTNYMDGPVGvtqcP------------IPPGQSFTYEFTVDTQVG- 98

                           90       100       110
                   ....*....|....*....|....*....|..
gi 2024429024  170 akgdadciTRVYHSHIDAprDVASGLVGPLII 201
Cdd:cd13851     99 --------TYWYHSHDGG--QYPDGLRGPFII 120
CuRO_1_Diphenol_Ox cd13857
The first cupredoxin domain of fungal laccase, diphenol oxidase; Diphenol oxidase belongs to ...
 802-895 1.54e-05

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


Pssm-ID: 259926 [Multi-domain]  Cd Length: 119  Bit Score: 45.33  E-value: 1.54e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024429024  802 QIQGPLIMSSIGDKINIVFKNLASRPYSIHAHGVKTDSS-----AVAITN----PGETKMYVWKISARSGsergdlhcTA 872
Cdd:cd13857     27 QFPGPLIEANQGDRIVVHVTNELDEPTSIHWHGLFQNGTnwmdgTAGITQcpipPGGSFTYNFTVDGQYG--------TY 98

                           90       100
                   ....*....|....*....|....
gi 2024429024  873 WaYHSMVDIikdTYS-GLIGTLVV 895
Cdd:cd13857     99 W-YHSHYST---QYAdGLVGPLIV 118
ascorbase TIGR03388
L-ascorbate oxidase, plant type; Members of this protein family are the copper-containing ...
 984-1046 2.21e-05

L-ascorbate oxidase, plant type; Members of this protein family are the copper-containing enzyme L-ascorbate oxidase (EC 1.10.3.3), also called ascorbase. This family is found in flowering plants, and shows greater sequence similarity to a family of laccases (EC 1.10.3.2) from plants than to other known ascorbate oxidases.


Pssm-ID: 274555 [Multi-domain]  Cd Length: 541  Bit Score: 48.59  E-value: 2.21e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024429024  984 GNEIDIHTAHFHGHSF------DYKQTEVYRADVFDL-----------FPGTFQTVEMIPQNPGVWLLHCHVTDHIHAGM 1046
Cdd:TIGR03388  438 GNNSETHPWHLHGHDFwvlgygEGKFRPGVDEKSYNLknpplrntvviFPYGWTALRFVADNPGVWAFHCHIEPHLHMGM 517
SufI COG2132
Multicopper oxidase with three cupredoxin domains (includes cell division protein FtsP and ...
 448-577 3.87e-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: 3.87e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024429024  448 LLGPVIKAEVGESIRVTFRNNASRPFSIQPHGVsyHKSNE--GalyrtasrdteSPASHVSPGTTFTYEWTVPEDVGptd 525
Cdd:COG2132     42 YPGPTIRVREGDRVRVRVTNRLPEPTTVHWHGL--RVPNAmdG-----------VPGDPIAPGETFTYEFPVPQPAG--- 105

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....
gi 2024429024  526 qdpdclTWLYYSAVN--SVRDTSSGLVGPLMVCRKGALLPSakqktVTREFFLL 577
Cdd:COG2132    106 ------TYWYHPHTHgsTAEQVYRGLAGALIVEDPEEDLPR-----YDRDIPLV 148
CuRO_1_McoC_like cd13855
The first cupredoxin domain of a multicopper oxidase McoC and similar proteins; This family ...
 447-520 8.38e-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: 43.23  E-value: 8.38e-05
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2024429024  447 GLLGPVIKAEVGESIRVTFRNNASRPFSIQPHGVSYHKSNEGalyrtasrdteSPASHVSPGTTFTYEWTVPED 520
Cdd:cd13855     29 SVPGPLIEVFEGDTVEITFRNRLPEPTTVHWHGLPVPPDQDG-----------NPHDPVAPGNDRVYRFTLPQD 91
Cu-oxidase pfam00394
Multicopper oxidase; Many of the proteins in this family contain multiple similar copies of ...
 918-1050 8.47e-05

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: 43.85  E-value: 8.47e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024429024  918 VFDENESWYlDENIETYSANPHLVDKENEEF-LESNKmHAINGKVFGNLHGLTMHVGDEVSWYLmAMGNEIDIHTAHFHG 996
Cdd:pfam00394    3 YVITLSDWY-HKDAKDLEKELLASGKAPTDFpPVPDA-VLINGKDGASLATLTVTPGKTYRLRI-INVALDDSLNFSIEG 79

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2024429024  997 HSF-----DYKQTEVYRADVFDLFPGTFQTVeMI--PQNPGVWLLHCHVT-DHIHAGMEATY 1050
Cdd:pfam00394   80 HKMtvvevDGVYVNPFTVDSLDIFPGQRYSV-LVtaNQDPGNYWIVASPNiPAFDNGTAAAI 140
CuRO_3_tcLLC2_insect_like cd13905
The third cupredoxin domain of the insect laccases similar to laccase 2 in Tribolium castaneum; ...
 973-1047 8.93e-05

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


Pssm-ID: 259972 [Multi-domain]  Cd Length: 174  Bit Score: 44.21  E-value: 8.93e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024429024  973 GDEVSWYLMAMGNEIDI-HTAHFHGHSFdykqtEVYRADVFDLFPGTFQTVE---------------------------M 1024
Cdd:cd13905     52 NSVVEIVLINEGPGPGLsHPFHLHGHSF-----YVLGMGFPGYNSTTGEILSqnwnnklldrgglpgrnlvnpplkdtvV 126

                           90       100       110
                   ....*....|....*....|....*....|....
gi 2024429024 1025 IP-----------QNPGVWLLHCHVTDHIHAGME 1047
Cdd:cd13905    127 VPnggyvvirfraDNPGYWLLHCHIEFHLLEGMA 160
CuRO_D1_2dMcoN_like cd13859
The first cupredoxin domain of bacterial two domain multicopper oxidase McoN and similar ...
 802-895 1.37e-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: 42.85  E-value: 1.37e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024429024  802 QIQGPLIMSSIGDKINIVFKNLASRPYSIHAHGV-KTDS---------SAVAITnPGETKMYVWKiSARSGsergdlhcT 871
Cdd:cd13859     28 QVPGPLIHVKEGDDLVVHVTNNTTLPHTIHWHGVlQMGSwkmdgvpgvTQPAIE-PGESFTYKFK-AERPG--------T 97

                           90       100
                   ....*....|....*....|....*
gi 2024429024  872 AWaYHSMVDIIK-DTYSGLIGTLVV 895
Cdd:cd13859     98 LW-YHCHVNVNEhVGMRGMWGPLIV 121
CuRO_1_McoC_like cd13855
The first cupredoxin domain of a multicopper oxidase McoC and similar proteins; This family ...
 802-895 1.73e-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: 42.46  E-value: 1.73e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024429024  802 QIQGPLIMSSIGDKINIVFKNLASRPYSIHAHGV----KTDSSAVAITNPGETKMYVWKISARSGSergdlhcTAWAY-H 876
Cdd:cd13855     29 SVPGPLIEVFEGDTVEITFRNRLPEPTTVHWHGLpvppDQDGNPHDPVAPGNDRVYRFTLPQDSAG-------TYWYHpH 101

                           90
                   ....*....|....*....
gi 2024429024  877 SMVDIIKDTYSGLIGTLVV 895
Cdd:cd13855    102 PHGHTAEQVYRGLAGAFVV 120
CuRO_3_AAO_like_2 cd13895
The third cupredoxin domain of Ascorbate oxidase homologs; This family includes fungal ...
 988-1049 1.73e-04

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: 43.84  E-value: 1.73e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024429024  988 DIHTAHFHG-HSFD-------YKQTEVYRA-----------DVFDLFPGTFQTVEMIP-------------QNPGVWLLH 1035
Cdd:cd13895     91 DAHPWHAHGaHYYDlgsglgtYSATALANEeklrgynpirrDTTMLYRYGGKGYYPPPgtgsgwrawrlrvDDPGVWMLH 170

                           90
                   ....*....|....
gi 2024429024 1036 CHVTDHIHAGMEAT 1049
Cdd:cd13895    171 CHILQHMIMGMQTV 184
Cu-oxidase_2 pfam07731
Multicopper oxidase; This entry contains many divergent copper oxidase-like domains that are ...
 254-357 2.08e-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: 2.08e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024429024  254 DFQESNKMHSINGYMYGY-LPDLTMCVEDKVKWHLFGMGNeaDIHSAYFHGQT--LIERHH-----------------RV 313
Cdd:pfam07731   14 SGNFRRNDWAINGLLFPPnTNVITLPYGTVVEWVLQNTTT--GVHPFHLHGHSfqVLGRGGgpwpeedpktynlvdpvRR 91

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....
gi 2024429024  314 DTINLFPATFIDALMIPRNPGEWLLSCQVNDHIEGGMQALFKVE 357
Cdd:pfam07731   92 DTVQVPPGGWVAIRFRADNPGVWLFHCHILWHLDQGMMGQFVVR 135
CuRO_3_LCC_plant cd13897
The third cupredoxin domain of the plant laccases; Laccase is a blue multicopper oxidase (MCO) ...
 988-1052 2.16e-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: 2.16e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024429024  988 DIHTAHFHGHSF--------DYKQTEVYRAdvFDLF-PGTFQTVeMIPQ-----------NPGVWLLHCHVTDHIHAGME 1047
Cdd:cd13897     55 ENHPMHLHGFDFyvvgrgfgNFDPSTDPAT--FNLVdPPLRNTV-GVPRggwaairfvadNPGVWFMHCHFERHTSWGMA 131


                   ....*
gi 2024429024 1048 ATYTV 1052
Cdd:cd13897    132 TVFIV 136
CuRO_1_CuNIR_like cd04201
Cupredoxin domain 1 of Copper-containing nitrite reductase and two-domain laccase; ...
 958-1055 2.72e-04

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


Pssm-ID: 259864 [Multi-domain]  Cd Length: 120  Bit Score: 41.71  E-value: 2.72e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024429024  958 NGKVFGNLhgLTMHVGDEVSWYLMAMGNEIDIHTAHFHGHSfdyKQTEVYRADVFDlfPGTFQTVEMIPQNPGVWLLHCH 1037
Cdd:cd04201     27 DGDIPGPM--LRVREGDTVELHFSNNPSSTMPHNIDFHAAT---GAGGGAGATFIA--PGETSTFSFKATQPGLYVYHCA 99

                           90       100
                   ....*....|....*....|.
gi 2024429024 1038 VTD---HIHAGMEATYTVLPK 1055
Cdd:cd04201    100 VAPvpmHIANGMYGLILVEPK 120
CuRO_1_2DMCO_NIR_like cd11024
The cupredoxin domain 1 of a two-domain laccase related to nitrite reductase; The two-domain ...
 802-856 4.35e-04

The cupredoxin domain 1 of a two-domain laccase related to nitrite reductase; The two-domain laccase (small laccase) in this family differs significantly from all laccases. It resembles the two domain nitrite reductase in both sequence and structure. It consists of two cupredoxin domains and forms trimers and hence resembles the quaternary structure of nitrite reductases more than that of large laccases. There are three trinuclear copper clusters in the enzyme localized between domains 1 and 2 of each pair of neighbor chains. 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: 41.10  E-value: 4.35e-04
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 2024429024  802 QIQGPLIMSSIGDKINIVFKNLASRPYSIHAHGV---KTDSSAVAITNPGETKMYVWK 856
Cdd:cd11024     29 TVPGPTLRATEGDLVRIHFINTGDHPHTIHFHGIhdaAMDGTGLGPIMPGESFTYEFV 86
CuRO_1_2dMco_1 cd13860
The first cupredoxin domain of bacteria two domain multicopper oxidase; This subfamily ...
 802-895 4.85e-04

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


Pssm-ID: 259929 [Multi-domain]  Cd Length: 119  Bit Score: 41.03  E-value: 4.85e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024429024  802 QIQGPLIMSSIGDKINIVFKNLASRPYSIHAHG--VKTDSSAVA-ITN----PGETKMYVWKISarsgsergdLHCTAWa 874
Cdd:cd13860     28 SVPGPTIEVTEGDRVRILVTNELPEPTTVHWHGlpVPNGMDGVPgITQppiqPGETFTYEFTAK---------QAGTYM- 97

                           90       100
                   ....*....|....*....|.
gi 2024429024  875 YHSMVDIIKDTYSGLIGTLVV 895
Cdd:cd13860     98 YHSHVDEAKQEDMGLYGAFIV 118
CuRO_3_MCO_like_4 cd13910
The third cupredoxin domain of uncharacterized multicopper oxidase; Multicopper Oxidases (MCOs) ...
 1028-1046 6.86e-04

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


Pssm-ID: 259977 [Multi-domain]  Cd Length: 166  Bit Score: 41.51  E-value: 6.86e-04
                           10
                   ....*....|....*....
gi 2024429024 1028 NPGVWLLHCHVTDHIHAGM 1046
Cdd:cd13910    142 NPGLWAFHCHILWHMAAGM 160
CuRO_1_McoC_like cd13855
The first cupredoxin domain of a multicopper oxidase McoC and similar proteins; This family ...
 96-201 7.72e-04

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


Pssm-ID: 259924 [Multi-domain]  Cd Length: 121  Bit Score: 40.54  E-value: 7.72e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024429024   96 GPIIKGEVGDSIVIHLKNFASRNYTLHPHGVKYTKENEGafYPdntkgfekrDDAVKPGGQYTYTWDVTEDQGPakgdad 175
Cdd:cd13855     32 GPLIEVFEGDTVEITFRNRLPEPTTVHWHGLPVPPDQDG--NP---------HDPVAPGNDRVYRFTLPQDSAG------ 94

                           90       100
                   ....*....|....*....|....*...
gi 2024429024  176 ciTRVY--HSHIDAPRDVASGLVGPLII 201
Cdd:cd13855     95 --TYWYhpHPHGHTAEQVYRGLAGAFVV 120
CuRO_3_Diphenol_Ox cd13904
The third cupredoxin domain of fungal laccase, diphenol oxidase; Diphenol oxidase belongs to ...
 990-1045 8.18e-04

The third 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 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: 259971 [Multi-domain]  Cd Length: 158  Bit Score: 41.13  E-value: 8.18e-04
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2024429024  990 HTAHFHGHSF------------------DYKQTEVYRADVFDLFPGTFQTVEMIPQNPGVWLLHCHVTDHIHAG 1045
Cdd:cd13904     78 HPYHLHGVDFhivargsgtltleqlanvQYNTTNPLRRDTIVIPGGSWAVLRIPADNPGVWALHCHIGWHLAAG 151
CuRO_D1_2dMcoN_like cd13859
The first cupredoxin domain of bacterial two domain multicopper oxidase McoN and similar ...
 450-555 8.57e-04

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


Pssm-ID: 259928 [Multi-domain]  Cd Length: 122  Bit Score: 40.54  E-value: 8.57e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024429024  450 GPVIKAEVGESIRVTFRNNASRPFSIQPHGV----SYHksNEGAlyrtasRDTESPAshVSPGTTFTYEWTVpedvgptd 525
Cdd:cd13859     31 GPLIHVKEGDDLVVHVTNNTTLPHTIHWHGVlqmgSWK--MDGV------PGVTQPA--IEPGESFTYKFKA-------- 92

                           90       100       110
                   ....*....|....*....|....*....|.
gi 2024429024  526 qDPDCLTWlYYSAVN-SVRDTSSGLVGPLMV 555
Cdd:cd13859     93 -ERPGTLW-YHCHVNvNEHVGMRGMWGPLIV 121
CuRO_1_Fet3p cd13851
The first Cupredoxin domain of multicopper oxidase Fet3P; Fet3p catalyzes the ferroxidase ...
 451-522 1.00e-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: 40.33  E-value: 1.00e-03
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2024429024  451 PVIKAEVGESIRVTFRNN-ASRPFSIQPHGVSYHKSNEgalYRTASRDTESPashVSPGTTFTYEWTVPEDVG 522
Cdd:cd13851     32 PPIEVNKGDTVVIHATNSlGDQPTSLHFHGLFQNGTNY---MDGPVGVTQCP---IPPGQSFTYEFTVDTQVG 98
CuRO_1_CuNIR cd11020
Cupredoxin domain 1 of Copper-containing nitrite reductase; Copper-containing nitrite ...
 802-856 1.11e-03

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


Pssm-ID: 259906 [Multi-domain]  Cd Length: 119  Bit Score: 39.89  E-value: 1.11e-03
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 2024429024  802 QIQGPLIMSSIGDKINIVFKNLASR--PYSIHAHGVKTDSSAVAIT-NPGETKMYVWK 856
Cdd:cd11020     29 QVPGPVIRVREGDTVELTLTNPGTNtmPHSIDFHAATGPGGGEFTTiAPGETKTFSFK 86
ascorbOXfungal TIGR03390
L-ascorbate oxidase, fungal type; This model describes a family of fungal ascorbate oxidases, ...
 987-1052 1.20e-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: 42.91  E-value: 1.20e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024429024  987 IDIHTAHFHG-HSFD-------YKQTE-------------------VYRADVFDLFPGTFQTVEMIPQNPGVWLLHCHVT 1039
Cdd:TIGR03390  439 VDTHPFHAHGrHFYDigggdgeYNATAneaklenytpvlrdttmlyRYAVKVVPGAPAGWRAWRIRVTNPGVWMMHCHIL 518

                           90
                   ....*....|...
gi 2024429024 1040 DHIHAGMEATYTV 1052
Cdd:TIGR03390  519 QHMVMGMQTVWVF 531
PLN02604 PLN02604
oxidoreductase
 985-1065 1.44e-03

oxidoreductase


Pssm-ID: 215324 [Multi-domain]  Cd Length: 566  Bit Score: 42.54  E-value: 1.44e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024429024  985 NEIDIHTAHFHGHSFdykQTEVYRADVFDLF--PGTFQTVEMIPQ------------------NPGVWLLHCHVTDHIHA 1044
Cdd:PLN02604   462 NNSETHPWHLHGHDF---WVLGYGEGKFNMSsdPKKYNLVDPIMKntvpvhpygwtalrfradNPGVWAFHCHIESHFFM 538

                           90       100
                   ....*....|....*....|.
gi 2024429024 1045 GMEATYTVLPKEGKSLSTLIM 1065
Cdd:PLN02604   539 GMGVVFEEGIERVGKLPSSIM 559
CuRO_3_Abr2_like cd13898
The third cupredoxin domain of a group of fungal Laccases similar to Abr2 from Aspergillus ...
 1007-1046 1.81e-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: 40.32  E-value: 1.81e-03
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....
gi 2024429024 1007 YRaDVFDLFPGTFQTVEMI----PQNPGVWLLHCHVTDHIHAGM 1046
Cdd:cd13898    115 LR-DTFTTPPSTEGPSWLViryhVVNPGAWLLHCHIQSHLAGGM 157
CuRO_1_McoP_like cd13852
The first cupredoxin domain of multicopper oxidase McoP and similar proteins; This family ...
 449-517 1.97e-03

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


Pssm-ID: 259921 [Multi-domain]  Cd Length: 114  Bit Score: 39.19  E-value: 1.97e-03
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2024429024  449 LGPVIKAEVGESIRVTFRNNASRPFSIQPHGVSYHKSNEGalyrtasrdteSPASHVSPGTTFTYEWTV 517
Cdd:cd13852     23 LGPILRLRKGQKVRITFKNNLPEPTIIHWHGLHVPAAMDG-----------HPRYAIDPGETYVYEFEV 80
CuRO_1_CuNIR cd11020
Cupredoxin domain 1 of Copper-containing nitrite reductase; Copper-containing nitrite ...
 450-516 2.06e-03

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


Pssm-ID: 259906 [Multi-domain]  Cd Length: 119  Bit Score: 39.12  E-value: 2.06e-03
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2024429024  450 GPVIKAEVGESIRVTFRNnasRPFSIQPHGVSYHksnegalyrTASRDTESPASHVSPGTTFTYEWT 516
Cdd:cd11020     32 GPVIRVREGDTVELTLTN---PGTNTMPHSIDFH---------AATGPGGGEFTTIAPGETKTFSFK 86
laccase TIGR03389
laccase, plant; Members of this protein family include the copper-containing enzyme laccase ...
 1028-1063 2.10e-03

laccase, plant; Members of this protein family include the copper-containing enzyme laccase (EC 1.10.3.2), often several from a single plant species, and additional, uncharacterized, closely related plant proteins termed laccase-like multicopper oxidases. This protein family shows considerable sequence similarity to the L-ascorbate oxidase (EC 1.10.3.3) family. Laccases are enzymes of rather broad specificity, and classification of all proteins scoring about the trusted cutoff of this model as laccases may be appropriate.


Pssm-ID: 274556 [Multi-domain]  Cd Length: 539  Bit Score: 42.03  E-value: 2.10e-03
                           10        20        30
                   ....*....|....*....|....*....|....*.
gi 2024429024 1028 NPGVWLLHCHVTDHIHAGMEATYTVLPKEGKSLSTL 1063
Cdd:TIGR03389  495 NPGVWFMHCHLEVHTTWGLKMAFLVDNGKGPNQSLL 530
Cupredoxin cd00920
Cupredoxin superfamily; Cupredoxins contain type I copper centers and are involved in ...
 958-1049 2.25e-03

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


Pssm-ID: 259860 [Multi-domain]  Cd Length: 110  Bit Score: 38.75  E-value: 2.25e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024429024  958 NGKVFGNLHgLTMHVGDEVSWYLMAMGNEIdiHTAHFHGHSFDYKQTEV--YRADVFDLFPGTFQTVEMI--PQNPGVWL 1033
Cdd:cd00920     16 GVLLFGPPV-LVVPVGDTVRVQFVNKLGEN--HSVTIAGFGVPVVAMAGgaNPGLVNTLVIGPGESAEVTftTDQAGVYW 92

                           90
                   ....*....|....*.
gi 2024429024 1034 LHCHVTDHIHAGMEAT 1049
Cdd:cd00920     93 FYCTIPGHNHAGMVGT 108
CuRO_1_AAO cd13845
The first cupredoxin domain of plant Ascorbate oxidase; Ascorbate oxidase catalyzes the ...
 450-555 2.34e-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: 38.97  E-value: 2.34e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024429024  450 GPVIKAEVGESIRVTFRNN-ASRPFSIQPHGVsyHKSNEGALYRTASRdTESPashVSPGTTFTYEWTVpedvgptDQDP 528
Cdd:cd13845     30 GPTIRATAGDTIVVELENKlPTEGVAIHWHGI--RQRGTPWADGTASV-SQCP---INPGETFTYQFVV-------DRPG 96

                           90       100
                   ....*....|....*....|....*..
gi 2024429024  529 dclTWLYYSAVNSVRdtSSGLVGPLMV 555
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 ...
 802-895 2.86e-03

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


Pssm-ID: 259923 [Multi-domain]  Cd Length: 122  Bit Score: 38.76  E-value: 2.86e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024429024  802 QIQGPLIMSSIGDKINI-VFKNLASRPYSIHAHGVK-----TDSSAVAITN----PGETKMYVWkisarsgseRGDLHCT 871
Cdd:cd13854     30 QYPGPLIEANWGDTIEVtVINKLQDNGTSIHWHGIRqlntnWQDGVPGVTEcpiaPGDTRTYRF---------RATQYGT 100

                           90       100
                   ....*....|....*....|....*
gi 2024429024  872 AWaYHSMVDIikdTYS-GLIGTLVV 895
Cdd:cd13854    101 SW-YHSHYSA---QYGdGVVGPIVI 121
CuRO_1_CuNIR_like cd04201
Cupredoxin domain 1 of Copper-containing nitrite reductase and two-domain laccase; ...
 450-555 3.31e-03

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


Pssm-ID: 259864 [Multi-domain]  Cd Length: 120  Bit Score: 38.63  E-value: 3.31e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024429024  450 GPVIKAEVGESIRVTFRNNasrPFSIQPHGVSYHKSNeGALYRTAsrdtespASHVSPGTTFTYEW--TVPEdvgptdqd 527
Cdd:cd04201     32 GPMLRVREGDTVELHFSNN---PSSTMPHNIDFHAAT-GAGGGAG-------ATFIAPGETSTFSFkaTQPG-------- 92

                           90       100
                   ....*....|....*....|....*....
gi 2024429024  528 pdclTWLYYSAVNSV-RDTSSGLVGPLMV 555
Cdd:cd04201     93 ----LYVYHCAVAPVpMHIANGMYGLILV 117
CuRO_1_McoP_like cd13852
The first cupredoxin domain of multicopper oxidase McoP and similar proteins; This family ...
 93-201 4.56e-03

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


Pssm-ID: 259921 [Multi-domain]  Cd Length: 114  Bit Score: 38.04  E-value: 4.56e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024429024   93 GFLGPIIKGEVGDSIVIHLKNFASRNYTLHPHGVKYTKENEGafYPDNtkgfekrddAVKPGGQYTYTWDVTEDQGpakg 172
Cdd:cd13852     21 SYLGPILRLRKGQKVRITFKNNLPEPTIIHWHGLHVPAAMDG--HPRY---------AIDPGETYVYEFEVLNRAG---- 85

                           90       100       110
                   ....*....|....*....|....*....|.
gi 2024429024  173 dadciTRVYHSHID--APRDVASGLVGPLII 201
Cdd:cd13852     86 -----TYWYHPHPHglTAKQVYRGLAGLFLV 111
CuRO_3_Tth-MCO_like cd13900
The third cupredoxin domain of the bacterial laccases similar to Tth-MCO from Thermus ...
 957-1046 6.91e-03

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


Pssm-ID: 259967 [Multi-domain]  Cd Length: 123  Bit Score: 38.00  E-value: 6.91e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024429024  957 INGKVFG-NLHGLTMHVGDEVSWYLMAMGNEIdiHTAHFHGHSF-------DYKQTEVYRaDVFDLFPGTFQTVEMIPQN 1028
Cdd:cd13900     22 INGKPFDpDRPDRTVRLGTVEEWTLINTSGED--HPFHIHVNPFqvvsingKPGLPPVWR-DTVNVPAGGSVTIRTRFRD 98

                           90
                   ....*....|....*....
gi 2024429024 1029 P-GVWLLHCHVTDHIHAGM 1046
Cdd:cd13900     99 FtGEFVLHCHILDHEDQGM 117
CuRO_3_McoC_like cd13902
The third cupredoxin domain of a multicopper oxidase McoC and similar proteins; This family ...
 261-356 7.30e-03

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: 37.76  E-value: 7.30e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024429024  261 MHSINGYMYG-YLPDLTMCVEDKVKWHLFgmgNEADI-HSAYFHGQ--TLIERHHRV---------DTINLFPATFIDAL 327
Cdd:cd13902     20 MFLINGKTFDmNRIDFVAKVGEVEVWEVT---NTSHMdHPFHLHGTqfQVLEIDGNPqkpeyrawkDTVNLPPGEAVRIA 96

                           90       100
                   ....*....|....*....|....*....
gi 2024429024  328 MIPRNPGEWLLSCQVNDHIEGGMQALFKV 356
Cdd:cd13902     97 TRQDDPGMWMYHCHILEHEDAGMMGMLHV 125
CuRO_1_Tth-MCO_like cd13853
The first cupredoxin domain of the bacterial laccases similar to Tth-MCO from Thermus ...
 94-201 8.50e-03

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


Pssm-ID: 259922 [Multi-domain]  Cd Length: 139  Bit Score: 38.00  E-value: 8.50e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024429024   94 FLGPIIKGEVGDSIVIHLKN----------------FASRNYT-LHPHGVKYTKENEGafypdntkgfekrDD---AVKP 153
Cdd:cd13853     29 IPGPTLRVRPGDTLRITLKNdlppegaaneapapntPHCPNTTnLHFHGLHVSPTGNS-------------DNvflTIAP 95

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|.
gi 2024429024  154 GGQYTYTWDVTEDQGPakGdadciTRVYHSHID---APrDVASGLVGPLII 201
Cdd:cd13853     96 GESFTYEYDIPADHPP--G-----TYWYHPHLHgstAL-QVAGGMAGALVV 138
CuRO_1_McoP_like cd13852
The first cupredoxin domain of multicopper oxidase McoP and similar proteins; This family ...
 804-895 9.24e-03

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


Pssm-ID: 259921 [Multi-domain]  Cd Length: 114  Bit Score: 37.27  E-value: 9.24e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024429024  804 QGPLIMSSIGDKINIVFKNLASRPYSIHAHGV----KTDSSAVAITNPGETKMYVWKISARSGsergdlhcTAWaYHSMV 879
Cdd:cd13852     23 LGPILRLRKGQKVRITFKNNLPEPTIIHWHGLhvpaAMDGHPRYAIDPGETYVYEFEVLNRAG--------TYW-YHPHP 93

                           90
                   ....*....|....*...
gi 2024429024  880 D--IIKDTYSGLIGTLVV 895
Cdd:cd13852     94 HglTAKQVYRGLAGLFLV 111
CuRO_1_CuNIR_like cd04201
Cupredoxin domain 1 of Copper-containing nitrite reductase and two-domain laccase; ...
 803-898 9.83e-03

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


Pssm-ID: 259864 [Multi-domain]  Cd Length: 120  Bit Score: 37.47  E-value: 9.83e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024429024  803 IQGPLIMSSIGDKINIVFKNLASR--PYSIHAHGV--KTDSSAVAITNPGETKMYVWKiSARSGsergdlhctAWAYHSM 878
Cdd:cd04201     30 IPGPMLRVREGDTVELHFSNNPSStmPHNIDFHAAtgAGGGAGATFIAPGETSTFSFK-ATQPG---------LYVYHCA 99

                           90       100
                   ....*....|....*....|.
gi 2024429024  879 VD-IIKDTYSGLIGTLVVCPR 898
Cdd:cd04201    100 VApVPMHIANGMYGLILVEPK 120
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

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