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Conserved domains on  [gi|1810777707|ref|XP_032302482|]
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ceruloplasmin isoform X3 [Coturnix japonica]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
CuRO_3_ceruloplasmin cd04224
The third cupredoxin domain of Ceruloplasmin; Ceruloplasmin is a multicopper oxidase essential ...
 623-821 9.95e-125

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: 383.75  E-value: 9.95e-125
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1810777707  623 TKIRQYFIAAEEIIWNYGPSALNHFTGQELTA-DSESSVFFEQSETRIGGSYKKAIYKEYTDGTFTAHKKRLPEEEHLGL 701
Cdd:cd04224      1 GKVRHYFIAAEEIMWDYAPSGKNLFTGQNLTApGSDSEVFFQRNETRIGGTYWKVRYVEYTDATFTTRKHRSKEEEHLGI 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1810777707  702 LGPVIKAEVEESIRVTFRNNASRPFSIQPHGVSYQKSNEGALYRtasRDTESPASHVSPGATFTYEWNVPEDVGPTDQDP 781
Cdd:cd04224     81 LGPVIRAEVGDTIKVTFRNKASRPFSIQPHGVFYEKNYEGAMYR---DGDPSPGSHVSPGETFTYEWTVPEGVGPTNQDP 157

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|
gi 1810777707  782 DCLTWLYYSAVDSVRDTNSGLVGPLLVCRRGALLPSAKQK 821
Cdd:cd04224    158 PCLTYLYFSAVDPVRDTNSGLVGPLLVCKKGSLNANGRQK 197
CuRO_1_ceruloplasmin cd04222
The first cupredoxin domain of Ceruloplasmin; Ceruloplasmin is a multicopper oxidase essential ...
 275-457 3.78e-121

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: 373.68  E-value: 3.78e-121
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1810777707  275 REYYIGIIETAWDYAPGNTDLISGQHFAEEEQAEVFLKRGPQRIGSIYKKAVYTQYTNILYDVIVEKPSWLGFLGPIIKG 354
Cdd:cd04222      1 REYYIGIRETQWDYAPSGKNLITNQTFDDDEHASVFLKRGPDRIGRVYKKAVYLQYTDDTYRTEIEKPVWLGFLGPILKA 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1810777707  355 EVGDSIVIHLKNFASRNYTLHPHGVTYTKENEGAFYPDNTKGFEKRDDAVKPGGQYTYTWDVTEDQGPAKEDADCITRVY 434
Cdd:cd04222     81 EVGDVIVVHLKNFASRPYSLHPHGVFYNKENEGALYPDNTSGFEKADDAVPPGGSYTYTWTVPEEQAPTKADANCLTRIY 160

                          170       180
                   ....*....|....*....|...
gi 1810777707  435 HSHIDAPRDVASGLVGPLIICKK 457
Cdd:cd04222    161 HSHIDAPKDIASGLIGPLIICKK 183
CuRO_5_ceruloplasmin cd04225
The fifth cupredoxin domain of Ceruloplasmin; Ceruloplasmin is a multicopper oxidase essential ...
 981-1151 1.14e-107

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: 336.75  E-value: 1.14e-107
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1810777707  981 KTHYIAAIEVEWDYSPNRTWEFERHQYHEESPGNPFLNKEDKFIGSKYKKVVYREYTDHTFSTPKSRAEEEQHLQIQGPL 1060
Cdd:cd04225      1 RTYYIAAEEVEWDYSPQRTWEQELHNTHEESPGNAFLNKGDKFIGSKYKKVVYREYTDDTFSVPKERTAEEEHLGILGPL 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1810777707 1061 IMSSIGDKINIVFKNLASRPYSIHAHGVKTDSSVVAITNPGETKTYVWKISARSSSERGELHCTAWAYHSTVDIIKDTYS 1140
Cdd:cd04225     81 IHAEVGEKVKIVFKNMASRPYSIHAHGVKTDSSWVAPTEPGETQTYTWKIPERSGPGVEDSNCISWAYYSTVDQIKDLYS 160

                          170
                   ....*....|.
gi 1810777707 1141 GLIGTLVVCPR 1151
Cdd:cd04225    161 GLIGPLVICRR 171
CuRO_4_ceruloplasmin cd11022
The fourth cupredoxin domain of Ceruloplasmin; Ceruloplasmin is a multicopper oxidase ...
 824-967 2.88e-95

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


:

Pssm-ID: 259908 [Multi-domain]  Cd Length: 144  Bit Score: 301.71  E-value: 2.88e-95
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1810777707  824 TREFFLLATVFDENLSWYLDDNILMFALNPNEIDKDNEDFQESNKMHSINGYMYGNQPGLEMCKGEVISWHLMGLGTEVD 903
Cdd:cd11022      1 DKEFFLLFTVFDENESWYLDENIQQFTLDPRSVDKEDEDFQESNKMHSINGYMYGNQPGLDMCKGDTVSWHLFGLGTETD 80

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1810777707  904 VHGIYFSHNTFITKGTRKDTANLFPHTFVTAIMKPDSEGIFEVSCLTTDHYRGGMKQKYKVKPC 967
Cdd:cd11022     81 VHGIYFSGNTFLLQGTRRDTANLFPHTSVTAIMQPDNEGTFEVNCQTTDHYSAGMRQIYTVSQC 144
CuRO_2_ceruloplasmin cd11021
The second cupredoxin domain of Ceruloplasmin; Ceruloplasmin is a multicopper oxidase ...
 469-609 8.30e-95

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


:

Pssm-ID: 259907 [Multi-domain]  Cd Length: 141  Bit Score: 300.16  E-value: 8.30e-95
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1810777707  469 DAEFILMFSVMDENLSWYLEDNIRTYCSEPSKVDKDDEDFQESNKMHSINGYMYGYLPNLTMCAEDKVKWHLFGMGNEAD 548
Cdd:cd11021      1 DREFVLMFSVVDENLSWYLDENIKTYCSEPAKVDKDDEDFQESNKMHSINGYTFGNLPGLSMCAGDRVKWHLFGMGNEVD 80

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1810777707  549 IHSVYFHGQTLIERHHRVDTINLFPATFIDALMIPRNPGEWLLSCQVNDHVEGGMQALFKV 609
Cdd:cd11021     81 IHSAFFHGQTLTDRGHRTDTINLFPATFVTAEMVAQNPGKWLLSCQVNDHLKAGMQAFYEV 141
CuRO_6_ceruloplasmin cd11012
The sixth cupredoxin domain of Ceruloplasmin; Ceruloplasmin is a multicopper oxidase essential ...
 1162-1306 7.58e-94

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: 297.94  E-value: 7.58e-94
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1810777707 1162 KVHFALLFMVFDENESWYLDENIETYSVNPHLVDKENEEFLESNKMHAINGKVFGNLHGLTMHVGDEVSWYLIAMGNEVD 1241
Cdd:cd11012      1 KLEFALLFLVFDENESWYLDENIKTYSDHPEKVNKEDEEFIESNKMHAINGKVFGNLQGLTMHVGDEVYWYLMGMGNEID 80

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1810777707 1242 IHTTHFHGHSFNYKQTGVYRADVFDLFPGTFQTVEMIPQNPGTWLLHCHVTDHIHAGMEAIYTVL 1306
Cdd:cd11012     81 IHTAHFHGHSFDYKHRGVYRSDVFDLFPGTFQTVEMIPRTPGTWLLHCHVTDHIHAGMETTYTVL 145
L6_membrane pfam05805
L6 membrane protein; This family consists of several eukaryotic L6 membrane proteins. L6, ...
 1-106 4.39e-49

L6 membrane protein; This family consists of several eukaryotic L6 membrane proteins. L6, IL-TMP, and TM4SF5 are cell surface proteins predicted to have four transmembrane domains. Previous sequence analysis led to their assignment as members of the tetraspanin superfamily it has now been found that that they are not significantly related to genuine tetraspanins, but instead constitute their own L6 family. Several members of this family have been implicated in human cancer.


:

Pssm-ID: 461745  Cd Length: 192  Bit Score: 172.75  E-value: 4.39e-49
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1810777707    1 MLSSVLAACVGILGSGYCVIISALGLSQGPYCLTRA-ERNWIYPFTQSS-GGYLLEYNEWSKCQEPQNIVQWNVTLFSIL 78
Cdd:pfam05805   85 MFLSILFSAIGVLGAGYCFIVSALALAEGPLCLTNGgSTSWGYPFKNNFnGNYLFNQSLWSVCLEPENIVEWHVTLFSIL 164

                           90       100
                   ....*....|....*....|....*...
gi 1810777707   79 LVLGGIEFILCFIQIVNGILGGVCRLCC 106
Cdd:pfam05805  165 LLVSGLELLLCLIQVVNGLLGCLCGTCK 192
L6_membrane pfam05805
L6 membrane protein; This family consists of several eukaryotic L6 membrane proteins. L6, ...
 129-244 1.93e-38

L6 membrane protein; This family consists of several eukaryotic L6 membrane proteins. L6, IL-TMP, and TM4SF5 are cell surface proteins predicted to have four transmembrane domains. Previous sequence analysis led to their assignment as members of the tetraspanin superfamily it has now been found that that they are not significantly related to genuine tetraspanins, but instead constitute their own L6 family. Several members of this family have been implicated in human cancer.


:

Pssm-ID: 461745  Cd Length: 192  Bit Score: 142.32  E-value: 1.93e-38
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1810777707  129 CCqseSCNKTYRSFISIVLAMLGVAFSGYSCIIFTLGLIQGPFCNSSSG---WDYIFKD-TVGGYLTNYSAWSQCAEPAN 204
Cdd:pfam05805   76 CC---SCGNRCGMFLSILFSAIGVLGAGYCFIVSALALAEGPLCLTNGGstsWGYPFKNnFNGNYLFNQSLWSVCLEPEN 152

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|
gi 1810777707  205 AVEWTIILLSILMTLSGLQLIICFLKAAAELKRALCGTYS 244
Cdd:pfam05805  153 IVEWHVTLFSILLLVSGLELLLCLIQVVNGLLGCLCGTCK 192
 
Name Accession Description Interval E-value
CuRO_3_ceruloplasmin cd04224
The third cupredoxin domain of Ceruloplasmin; Ceruloplasmin is a multicopper oxidase essential ...
 623-821 9.95e-125

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: 383.75  E-value: 9.95e-125
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1810777707  623 TKIRQYFIAAEEIIWNYGPSALNHFTGQELTA-DSESSVFFEQSETRIGGSYKKAIYKEYTDGTFTAHKKRLPEEEHLGL 701
Cdd:cd04224      1 GKVRHYFIAAEEIMWDYAPSGKNLFTGQNLTApGSDSEVFFQRNETRIGGTYWKVRYVEYTDATFTTRKHRSKEEEHLGI 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1810777707  702 LGPVIKAEVEESIRVTFRNNASRPFSIQPHGVSYQKSNEGALYRtasRDTESPASHVSPGATFTYEWNVPEDVGPTDQDP 781
Cdd:cd04224     81 LGPVIRAEVGDTIKVTFRNKASRPFSIQPHGVFYEKNYEGAMYR---DGDPSPGSHVSPGETFTYEWTVPEGVGPTNQDP 157

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|
gi 1810777707  782 DCLTWLYYSAVDSVRDTNSGLVGPLLVCRRGALLPSAKQK 821
Cdd:cd04224    158 PCLTYLYFSAVDPVRDTNSGLVGPLLVCKKGSLNANGRQK 197
CuRO_1_ceruloplasmin cd04222
The first cupredoxin domain of Ceruloplasmin; Ceruloplasmin is a multicopper oxidase essential ...
 275-457 3.78e-121

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: 373.68  E-value: 3.78e-121
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1810777707  275 REYYIGIIETAWDYAPGNTDLISGQHFAEEEQAEVFLKRGPQRIGSIYKKAVYTQYTNILYDVIVEKPSWLGFLGPIIKG 354
Cdd:cd04222      1 REYYIGIRETQWDYAPSGKNLITNQTFDDDEHASVFLKRGPDRIGRVYKKAVYLQYTDDTYRTEIEKPVWLGFLGPILKA 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1810777707  355 EVGDSIVIHLKNFASRNYTLHPHGVTYTKENEGAFYPDNTKGFEKRDDAVKPGGQYTYTWDVTEDQGPAKEDADCITRVY 434
Cdd:cd04222     81 EVGDVIVVHLKNFASRPYSLHPHGVFYNKENEGALYPDNTSGFEKADDAVPPGGSYTYTWTVPEEQAPTKADANCLTRIY 160

                          170       180
                   ....*....|....*....|...
gi 1810777707  435 HSHIDAPRDVASGLVGPLIICKK 457
Cdd:cd04222    161 HSHIDAPKDIASGLIGPLIICKK 183
CuRO_5_ceruloplasmin cd04225
The fifth cupredoxin domain of Ceruloplasmin; Ceruloplasmin is a multicopper oxidase essential ...
 981-1151 1.14e-107

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: 336.75  E-value: 1.14e-107
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1810777707  981 KTHYIAAIEVEWDYSPNRTWEFERHQYHEESPGNPFLNKEDKFIGSKYKKVVYREYTDHTFSTPKSRAEEEQHLQIQGPL 1060
Cdd:cd04225      1 RTYYIAAEEVEWDYSPQRTWEQELHNTHEESPGNAFLNKGDKFIGSKYKKVVYREYTDDTFSVPKERTAEEEHLGILGPL 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1810777707 1061 IMSSIGDKINIVFKNLASRPYSIHAHGVKTDSSVVAITNPGETKTYVWKISARSSSERGELHCTAWAYHSTVDIIKDTYS 1140
Cdd:cd04225     81 IHAEVGEKVKIVFKNMASRPYSIHAHGVKTDSSWVAPTEPGETQTYTWKIPERSGPGVEDSNCISWAYYSTVDQIKDLYS 160

                          170
                   ....*....|.
gi 1810777707 1141 GLIGTLVVCPR 1151
Cdd:cd04225    161 GLIGPLVICRR 171
CuRO_4_ceruloplasmin cd11022
The fourth cupredoxin domain of Ceruloplasmin; Ceruloplasmin is a multicopper oxidase ...
 824-967 2.88e-95

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


Pssm-ID: 259908 [Multi-domain]  Cd Length: 144  Bit Score: 301.71  E-value: 2.88e-95
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1810777707  824 TREFFLLATVFDENLSWYLDDNILMFALNPNEIDKDNEDFQESNKMHSINGYMYGNQPGLEMCKGEVISWHLMGLGTEVD 903
Cdd:cd11022      1 DKEFFLLFTVFDENESWYLDENIQQFTLDPRSVDKEDEDFQESNKMHSINGYMYGNQPGLDMCKGDTVSWHLFGLGTETD 80

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1810777707  904 VHGIYFSHNTFITKGTRKDTANLFPHTFVTAIMKPDSEGIFEVSCLTTDHYRGGMKQKYKVKPC 967
Cdd:cd11022     81 VHGIYFSGNTFLLQGTRRDTANLFPHTSVTAIMQPDNEGTFEVNCQTTDHYSAGMRQIYTVSQC 144
CuRO_2_ceruloplasmin cd11021
The second cupredoxin domain of Ceruloplasmin; Ceruloplasmin is a multicopper oxidase ...
 469-609 8.30e-95

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


Pssm-ID: 259907 [Multi-domain]  Cd Length: 141  Bit Score: 300.16  E-value: 8.30e-95
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1810777707  469 DAEFILMFSVMDENLSWYLEDNIRTYCSEPSKVDKDDEDFQESNKMHSINGYMYGYLPNLTMCAEDKVKWHLFGMGNEAD 548
Cdd:cd11021      1 DREFVLMFSVVDENLSWYLDENIKTYCSEPAKVDKDDEDFQESNKMHSINGYTFGNLPGLSMCAGDRVKWHLFGMGNEVD 80

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1810777707  549 IHSVYFHGQTLIERHHRVDTINLFPATFIDALMIPRNPGEWLLSCQVNDHVEGGMQALFKV 609
Cdd:cd11021     81 IHSAFFHGQTLTDRGHRTDTINLFPATFVTAEMVAQNPGKWLLSCQVNDHLKAGMQAFYEV 141
CuRO_6_ceruloplasmin cd11012
The sixth cupredoxin domain of Ceruloplasmin; Ceruloplasmin is a multicopper oxidase essential ...
 1162-1306 7.58e-94

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: 297.94  E-value: 7.58e-94
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1810777707 1162 KVHFALLFMVFDENESWYLDENIETYSVNPHLVDKENEEFLESNKMHAINGKVFGNLHGLTMHVGDEVSWYLIAMGNEVD 1241
Cdd:cd11012      1 KLEFALLFLVFDENESWYLDENIKTYSDHPEKVNKEDEEFIESNKMHAINGKVFGNLQGLTMHVGDEVYWYLMGMGNEID 80

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1810777707 1242 IHTTHFHGHSFNYKQTGVYRADVFDLFPGTFQTVEMIPQNPGTWLLHCHVTDHIHAGMEAIYTVL 1306
Cdd:cd11012     81 IHTAHFHGHSFDYKHRGVYRSDVFDLFPGTFQTVEMIPRTPGTWLLHCHVTDHIHAGMETTYTVL 145
L6_membrane pfam05805
L6 membrane protein; This family consists of several eukaryotic L6 membrane proteins. L6, ...
 1-106 4.39e-49

L6 membrane protein; This family consists of several eukaryotic L6 membrane proteins. L6, IL-TMP, and TM4SF5 are cell surface proteins predicted to have four transmembrane domains. Previous sequence analysis led to their assignment as members of the tetraspanin superfamily it has now been found that that they are not significantly related to genuine tetraspanins, but instead constitute their own L6 family. Several members of this family have been implicated in human cancer.


Pssm-ID: 461745  Cd Length: 192  Bit Score: 172.75  E-value: 4.39e-49
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1810777707    1 MLSSVLAACVGILGSGYCVIISALGLSQGPYCLTRA-ERNWIYPFTQSS-GGYLLEYNEWSKCQEPQNIVQWNVTLFSIL 78
Cdd:pfam05805   85 MFLSILFSAIGVLGAGYCFIVSALALAEGPLCLTNGgSTSWGYPFKNNFnGNYLFNQSLWSVCLEPENIVEWHVTLFSIL 164

                           90       100
                   ....*....|....*....|....*...
gi 1810777707   79 LVLGGIEFILCFIQIVNGILGGVCRLCC 106
Cdd:pfam05805  165 LLVSGLELLLCLIQVVNGLLGCLCGTCK 192
L6_membrane pfam05805
L6 membrane protein; This family consists of several eukaryotic L6 membrane proteins. L6, ...
 129-244 1.93e-38

L6 membrane protein; This family consists of several eukaryotic L6 membrane proteins. L6, IL-TMP, and TM4SF5 are cell surface proteins predicted to have four transmembrane domains. Previous sequence analysis led to their assignment as members of the tetraspanin superfamily it has now been found that that they are not significantly related to genuine tetraspanins, but instead constitute their own L6 family. Several members of this family have been implicated in human cancer.


Pssm-ID: 461745  Cd Length: 192  Bit Score: 142.32  E-value: 1.93e-38
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1810777707  129 CCqseSCNKTYRSFISIVLAMLGVAFSGYSCIIFTLGLIQGPFCNSSSG---WDYIFKD-TVGGYLTNYSAWSQCAEPAN 204
Cdd:pfam05805   76 CC---SCGNRCGMFLSILFSAIGVLGAGYCFIVSALALAEGPLCLTNGGstsWGYPFKNnFNGNYLFNQSLWSVCLEPEN 152

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|
gi 1810777707  205 AVEWTIILLSILMTLSGLQLIICFLKAAAELKRALCGTYS 244
Cdd:pfam05805  153 IVEWHVTLFSILLLVSGLELLLCLIQVVNGLLGCLCGTCK 192
Cu-oxidase_2 pfam07731
Multicopper oxidase; This entry contains many divergent copper oxidase-like domains that are ...
 1205-1309 3.33e-18

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: 82.48  E-value: 3.33e-18
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1810777707 1205 NKMHAINGKVFG-NLHGLTMHVGDEVSWYLIAMGNevDIHTTHFHGHSF----------NYKQTGVY------RADVFDL 1267
Cdd:pfam07731   19 RNDWAINGLLFPpNTNVITLPYGTVVEWVLQNTTT--GVHPFHLHGHSFqvlgrgggpwPEEDPKTYnlvdpvRRDTVQV 96

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|..
gi 1810777707 1268 FPGTFQTVEMIPQNPGTWLLHCHVTDHIHAGMEAIYTVLPEE 1309
Cdd:pfam07731   97 PPGGWVAIRFRADNPGVWLFHCHILWHLDQGMMGQFVVRPGD 138
Cu-oxidase_3 pfam07732
Multicopper oxidase; This entry contains many divergent copper oxidase-like domains that are ...
 329-454 6.48e-12

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


Pssm-ID: 462247 [Multi-domain]  Cd Length: 119  Bit Score: 63.80  E-value: 6.48e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1810777707  329 QYTNILYDVIVEKPSWL---GFLGPIIKGEVGDSIVIHLKNFASRNYTLHPHGVTYTKENEGAFYPDNTKgfekrdDAVK 405
Cdd:pfam07732    3 TYGTVSPLGGTRQAVIGvngQFPGPTIRVREGDTVVVNVTNNLDEPTSIHWHGLQQRGTPWMDGVPGVTQ------CPIP 76

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*....
gi 1810777707  406 PGGQYTYTWDVTEDQGpakedadciTRVYHSHIDAPRdvASGLVGPLII 454
Cdd:pfam07732   77 PGQSFTYRFQVKQQAG---------TYWYHSHTSGQQ--AAGLAGAIII 114
Cu-oxidase pfam00394
Multicopper oxidase; Many of the proteins in this family contain multiple similar copies of ...
 476-612 6.08e-10

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: 58.87  E-value: 6.08e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1810777707  476 FSVMDENLSWYlEDNIRTYCSEPSKVDKDDEDFQESNKMHSINGYMYGYLPNLTMCAEDKVKWHLFGMGNEadiHSVYF- 554
Cdd:pfam00394    1 EDYVITLSDWY-HKDAKDLEKELLASGKAPTDFPPVPDAVLINGKDGASLATLTVTPGKTYRLRIINVALD---DSLNFs 76

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1810777707  555 ---HGQTLIE---RHH---RVDTINLFPATFIDALMIP-RNPGEWLLSCQVN-DHVEGGMQALFKVEDC 612
Cdd:pfam00394   77 iegHKMTVVEvdgVYVnpfTVDSLDIFPGQRYSVLVTAnQDPGNYWIVASPNiPAFDNGTAAAILRYSG 145
SufI COG2132
Multicopper oxidase with three cupredoxin domains (includes cell division protein FtsP and ...
 1207-1307 8.15e-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: 59.56  E-value: 8.15e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1810777707 1207 MHAINGKVFGNLH-GLTMHVGDEVSWYLIAMGNevDIHTTHFHGHSF-----NYKQTGV-YRADVFDLFPGtfQTVEMI- 1278
Cdd:COG2132    317 VWTINGKAFDPDRpDLTVKLGERERWTLVNDTM--MPHPFHLHGHQFqvlsrNGKPPPEgGWKDTVLVPPG--ETVRILf 392

                           90       100       110
                   ....*....|....*....|....*....|.
gi 1810777707 1279 --PQNPGTWLLHCHVTDHIHAGMEAIYTVLP 1307
Cdd:COG2132    393 rfDNYPGDWMFHCHILEHEDAGMMGQFEVVP 423
SufI COG2132
Multicopper oxidase with three cupredoxin domains (includes cell division protein FtsP and ...
 347-477 4.90e-08

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


Pssm-ID: 441735 [Multi-domain]  Cd Length: 423  Bit Score: 56.87  E-value: 4.90e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1810777707  347 FLGPIIKGEVGDSIVIHLKNFASRNYTLHPHGVTYTKENEGafYPdntkgfekrDDAVKPGGQYTYTWDVteDQGPAked 426
Cdd:COG2132     42 YPGPTIRVREGDRVRVRVTNRLPEPTTVHWHGLRVPNAMDG--VP---------GDPIAPGETFTYEFPV--PQPAG--- 105

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 1810777707  427 adciTRVYHSHIDA--PRDVASGLVGPLIIckkgamNKDNDKY--VDAEFILMFS 477
Cdd:COG2132    106 ----TYWYHPHTHGstAEQVYRGLAGALIV------EDPEEDLprYDRDIPLVLQ 150
PLN02191 PLN02191
L-ascorbate oxidase
 347-477 7.31e-07

L-ascorbate oxidase


Pssm-ID: 177843 [Multi-domain]  Cd Length: 574  Bit Score: 53.48  E-value: 7.31e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1810777707  347 FLGPIIKGEVGDSIVIHLKN-FASRNYTLHPHGVtytkENEGAFYPDNTKGFEKRddAVKPGGQYTYTWDVtEDQGpake 425
Cdd:PLN02191    51 FPGPTIDAVAGDTIVVHLTNkLTTEGLVIHWHGI----RQKGSPWADGAAGVTQC--AINPGETFTYKFTV-EKPG---- 119

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|..
gi 1810777707  426 dadciTRVYHSHIDAPRdvASGLVGPLIIckKGAMNKDNDKYVDAEFILMFS 477
Cdd:PLN02191   120 -----THFYHGHYGMQR--SAGLYGSLIV--DVAKGPKERLRYDGEFNLLLS 162
PLN02191 PLN02191
L-ascorbate oxidase
 1241-1303 1.94e-06

L-ascorbate oxidase


Pssm-ID: 177843 [Multi-domain]  Cd Length: 574  Bit Score: 52.32  E-value: 1.94e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1810777707 1241 DIHTTHFHGH-------------------SFNYKQTGVYRADVfdLFPGTFQTVEMIPQNPGTWLLHCHVTDHIHAGMEA 1301
Cdd:PLN02191   465 EIHPWHLHGHdfwvlgygdgkfkpgidekTYNLKNPPLRNTAI--LYPYGWTAIRFVTDNPGVWFFHCHIEPHLHMGMGV 542


                   ..
gi 1810777707 1302 IY 1303
Cdd:PLN02191   543 VF 544
ascorbase TIGR03388
L-ascorbate oxidase, plant type; Members of this protein family are the copper-containing ...
 347-486 4.38e-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: 50.91  E-value: 4.38e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1810777707  347 FLGPIIKGEVGDSIVIHLKN-FASRNYTLHPHGVtytkENEGAFYPDNTKGFEKRddAVKPGGQYTYTWdVTEDQGpake 425
Cdd:TIGR03388   29 FPGPTIRAQAGDTIVVELTNkLHTEGVVIHWHGI----RQIGTPWADGTAGVTQC--AINPGETFIYNF-VVDRPG---- 97

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1810777707  426 dadciTRVYHSHIDAPRdvASGLVGPLIIcKKGAMNKDNDKYvDAEFILMFSvmdenlSWY 486
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 ...
 1237-1303 4.69e-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: 47.82  E-value: 4.69e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1810777707 1237 GNEVDIHTTHFHGHSF---NYKQtGVYRADV----FDL-----------FPGTFQTVEMIPQNPGTWLLHCHVTDHIHAG 1298
Cdd:TIGR03388  438 GNNSETHPWHLHGHDFwvlGYGE-GKFRPGVdeksYNLknpplrntvviFPYGWTALRFVADNPGVWAFHCHIEPHLHMG 516


                   ....*
gi 1810777707 1299 MEAIY 1303
Cdd:TIGR03388  517 MGVVF 521
Cu-oxidase_3 pfam07732
Multicopper oxidase; This entry contains many divergent copper oxidase-like domains that are ...
 701-808 5.84e-05

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: 43.77  E-value: 5.84e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1810777707  701 LLGPVIKAEVEESIRVTFRNNASRPFSIQPHGVsYQKSN---EGALYrtasrdteSPASHVSPGATFTYEWNVPEDVGpt 777
Cdd:pfam07732   24 FPGPTIRVREGDTVVVNVTNNLDEPTSIHWHGL-QQRGTpwmDGVPG--------VTQCPIPPGQSFTYRFQVKQQAG-- 92

                           90       100       110
                   ....*....|....*....|....*....|.
gi 1810777707  778 dqdpdclTWLYYSAVDSVRdtNSGLVGPLLV 808
Cdd:pfam07732   93 -------TYWYHSHTSGQQ--AAGLAGAIII 114
Cu-oxidase_3 pfam07732
Multicopper oxidase; This entry contains many divergent copper oxidase-like domains that are ...
 1055-1130 4.34e-03

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


Pssm-ID: 462247 [Multi-domain]  Cd Length: 119  Bit Score: 38.38  E-value: 4.34e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1810777707 1055 QIQGPLIMSSIGDKINIVFKNLASRPYSIHAHGVKTDSS-----VVAITN----PGETKTYVWKISARSssergelhCTA 1125
Cdd:pfam07732   23 QFPGPTIRVREGDTVVVNVTNNLDEPTSIHWHGLQQRGTpwmdgVPGVTQcpipPGQSFTYRFQVKQQA--------GTY 94


                   ....*
gi 1810777707 1126 WaYHS 1130
Cdd:pfam07732   95 W-YHS 98
SufI COG2132
Multicopper oxidase with three cupredoxin domains (includes cell division protein FtsP and ...
 701-895 6.92e-03

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


Pssm-ID: 441735 [Multi-domain]  Cd Length: 423  Bit Score: 40.30  E-value: 6.92e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1810777707  701 LLGPVIKAEVEESIRVTFRNNASRPFSIQPHG--VSYQksNEGalyrtasrdteSPASHVSPGATFTYEWNVPEDVGptd 778
Cdd:COG2132     42 YPGPTIRVREGDRVRVRVTNRLPEPTTVHWHGlrVPNA--MDG-----------VPGDPIAPGETFTYEFPVPQPAG--- 105

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1810777707  779 qdpdclTWLYYSAVD--SVRDTNSGLVGPLLVCRRGALLPsakqkSVTREFFLLatvfdenlswyLDDnilmFALN-PNE 855
Cdd:COG2132    106 ------TYWYHPHTHgsTAEQVYRGLAGALIVEDPEEDLP-----RYDRDIPLV-----------LQD----WRLDdDGQ 159

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|..
gi 1810777707  856 IDKDNEDFQESN--KMHSINGYMygnQPGLEMCKGEVISWHL 895
Cdd:COG2132    160 LLYPMDAAMGGRlgDTLLVNGRP---NPTLEVRPGERVRLRL 198
 
Name Accession Description Interval E-value
CuRO_3_ceruloplasmin cd04224
The third cupredoxin domain of Ceruloplasmin; Ceruloplasmin is a multicopper oxidase essential ...
 623-821 9.95e-125

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: 383.75  E-value: 9.95e-125
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1810777707  623 TKIRQYFIAAEEIIWNYGPSALNHFTGQELTA-DSESSVFFEQSETRIGGSYKKAIYKEYTDGTFTAHKKRLPEEEHLGL 701
Cdd:cd04224      1 GKVRHYFIAAEEIMWDYAPSGKNLFTGQNLTApGSDSEVFFQRNETRIGGTYWKVRYVEYTDATFTTRKHRSKEEEHLGI 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1810777707  702 LGPVIKAEVEESIRVTFRNNASRPFSIQPHGVSYQKSNEGALYRtasRDTESPASHVSPGATFTYEWNVPEDVGPTDQDP 781
Cdd:cd04224     81 LGPVIRAEVGDTIKVTFRNKASRPFSIQPHGVFYEKNYEGAMYR---DGDPSPGSHVSPGETFTYEWTVPEGVGPTNQDP 157

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|
gi 1810777707  782 DCLTWLYYSAVDSVRDTNSGLVGPLLVCRRGALLPSAKQK 821
Cdd:cd04224    158 PCLTYLYFSAVDPVRDTNSGLVGPLLVCKKGSLNANGRQK 197
CuRO_1_ceruloplasmin cd04222
The first cupredoxin domain of Ceruloplasmin; Ceruloplasmin is a multicopper oxidase essential ...
 275-457 3.78e-121

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: 373.68  E-value: 3.78e-121
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1810777707  275 REYYIGIIETAWDYAPGNTDLISGQHFAEEEQAEVFLKRGPQRIGSIYKKAVYTQYTNILYDVIVEKPSWLGFLGPIIKG 354
Cdd:cd04222      1 REYYIGIRETQWDYAPSGKNLITNQTFDDDEHASVFLKRGPDRIGRVYKKAVYLQYTDDTYRTEIEKPVWLGFLGPILKA 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1810777707  355 EVGDSIVIHLKNFASRNYTLHPHGVTYTKENEGAFYPDNTKGFEKRDDAVKPGGQYTYTWDVTEDQGPAKEDADCITRVY 434
Cdd:cd04222     81 EVGDVIVVHLKNFASRPYSLHPHGVFYNKENEGALYPDNTSGFEKADDAVPPGGSYTYTWTVPEEQAPTKADANCLTRIY 160

                          170       180
                   ....*....|....*....|...
gi 1810777707  435 HSHIDAPRDVASGLVGPLIICKK 457
Cdd:cd04222    161 HSHIDAPKDIASGLIGPLIICKK 183
CuRO_5_ceruloplasmin cd04225
The fifth cupredoxin domain of Ceruloplasmin; Ceruloplasmin is a multicopper oxidase essential ...
 981-1151 1.14e-107

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: 336.75  E-value: 1.14e-107
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1810777707  981 KTHYIAAIEVEWDYSPNRTWEFERHQYHEESPGNPFLNKEDKFIGSKYKKVVYREYTDHTFSTPKSRAEEEQHLQIQGPL 1060
Cdd:cd04225      1 RTYYIAAEEVEWDYSPQRTWEQELHNTHEESPGNAFLNKGDKFIGSKYKKVVYREYTDDTFSVPKERTAEEEHLGILGPL 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1810777707 1061 IMSSIGDKINIVFKNLASRPYSIHAHGVKTDSSVVAITNPGETKTYVWKISARSSSERGELHCTAWAYHSTVDIIKDTYS 1140
Cdd:cd04225     81 IHAEVGEKVKIVFKNMASRPYSIHAHGVKTDSSWVAPTEPGETQTYTWKIPERSGPGVEDSNCISWAYYSTVDQIKDLYS 160

                          170
                   ....*....|.
gi 1810777707 1141 GLIGTLVVCPR 1151
Cdd:cd04225    161 GLIGPLVICRR 171
CuRO_4_ceruloplasmin cd11022
The fourth cupredoxin domain of Ceruloplasmin; Ceruloplasmin is a multicopper oxidase ...
 824-967 2.88e-95

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


Pssm-ID: 259908 [Multi-domain]  Cd Length: 144  Bit Score: 301.71  E-value: 2.88e-95
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1810777707  824 TREFFLLATVFDENLSWYLDDNILMFALNPNEIDKDNEDFQESNKMHSINGYMYGNQPGLEMCKGEVISWHLMGLGTEVD 903
Cdd:cd11022      1 DKEFFLLFTVFDENESWYLDENIQQFTLDPRSVDKEDEDFQESNKMHSINGYMYGNQPGLDMCKGDTVSWHLFGLGTETD 80

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1810777707  904 VHGIYFSHNTFITKGTRKDTANLFPHTFVTAIMKPDSEGIFEVSCLTTDHYRGGMKQKYKVKPC 967
Cdd:cd11022     81 VHGIYFSGNTFLLQGTRRDTANLFPHTSVTAIMQPDNEGTFEVNCQTTDHYSAGMRQIYTVSQC 144
CuRO_2_ceruloplasmin cd11021
The second cupredoxin domain of Ceruloplasmin; Ceruloplasmin is a multicopper oxidase ...
 469-609 8.30e-95

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


Pssm-ID: 259907 [Multi-domain]  Cd Length: 141  Bit Score: 300.16  E-value: 8.30e-95
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1810777707  469 DAEFILMFSVMDENLSWYLEDNIRTYCSEPSKVDKDDEDFQESNKMHSINGYMYGYLPNLTMCAEDKVKWHLFGMGNEAD 548
Cdd:cd11021      1 DREFVLMFSVVDENLSWYLDENIKTYCSEPAKVDKDDEDFQESNKMHSINGYTFGNLPGLSMCAGDRVKWHLFGMGNEVD 80

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1810777707  549 IHSVYFHGQTLIERHHRVDTINLFPATFIDALMIPRNPGEWLLSCQVNDHVEGGMQALFKV 609
Cdd:cd11021     81 IHSAFFHGQTLTDRGHRTDTINLFPATFVTAEMVAQNPGKWLLSCQVNDHLKAGMQAFYEV 141
CuRO_6_ceruloplasmin cd11012
The sixth cupredoxin domain of Ceruloplasmin; Ceruloplasmin is a multicopper oxidase essential ...
 1162-1306 7.58e-94

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: 297.94  E-value: 7.58e-94
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1810777707 1162 KVHFALLFMVFDENESWYLDENIETYSVNPHLVDKENEEFLESNKMHAINGKVFGNLHGLTMHVGDEVSWYLIAMGNEVD 1241
Cdd:cd11012      1 KLEFALLFLVFDENESWYLDENIKTYSDHPEKVNKEDEEFIESNKMHAINGKVFGNLQGLTMHVGDEVYWYLMGMGNEID 80

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1810777707 1242 IHTTHFHGHSFNYKQTGVYRADVFDLFPGTFQTVEMIPQNPGTWLLHCHVTDHIHAGMEAIYTVL 1306
Cdd:cd11012     81 IHTAHFHGHSFDYKHRGVYRSDVFDLFPGTFQTVEMIPRTPGTWLLHCHVTDHIHAGMETTYTVL 145
CuRO_1_ceruloplasmin_like cd04199
Cupredoxin domains 1, 3, and 5 of ceruloplasmin and similar proteins; This family includes the ...
 626-811 9.72e-80

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


Pssm-ID: 259862 [Multi-domain]  Cd Length: 177  Bit Score: 259.65  E-value: 9.72e-80
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1810777707  626 RQYFIAAEEIIWNYGPSALNHFTgqeltaDSESSVFFEQSETRIGGSYKKAIYKEYTDGTFTahkKRLPEEEHLGLLGPV 705
Cdd:cd04199      1 RHYYIAAEEIDWDYAPSGLAEKD------LSYRNQYLDNGPFRIGRSYKKVVYREYTDESFT---TPGPQPEHLGILGPT 71

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1810777707  706 IKAEVEESIRVTFRNNASRPFSIQPHGVSYQKSNEGALYRTASRDTESPASHVSPGATFTYEWNVPEDVGPTDQDPDCLT 785
Cdd:cd04199     72 IRAEVGDTIKVHFKNKASRPYSIHPHGVSYEKDSEGASYSDQTGPDEKKDDAVAPGETYTYVWIVTEESGPTKGDPACLT 151

                          170       180
                   ....*....|....*....|....*.
gi 1810777707  786 WLYYSAVDSVRDTNSGLVGPLLVCRR 811
Cdd:cd04199    152 WAYYSHVDLEKDINSGLIGPLLICKK 177
CuRO_1_ceruloplasmin_like cd04199
Cupredoxin domains 1, 3, and 5 of ceruloplasmin and similar proteins; This family includes the ...
 275-457 1.32e-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: 259.26  E-value: 1.32e-79
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1810777707  275 REYYIGIIETAWDYAPgntdliSGQHFAEEEQAEVFLKRGPQRIGSIYKKAVYTQYTNILYDVIVEKPSWLGFLGPIIKG 354
Cdd:cd04199      1 RHYYIAAEEIDWDYAP------SGLAEKDLSYRNQYLDNGPFRIGRSYKKVVYREYTDESFTTPGPQPEHLGILGPTIRA 74

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1810777707  355 EVGDSIVIHLKNFASRNYTLHPHGVTYTKENEGAFYPDNTKGFEKRDDAVKPGGQYTYTWDVTEDQGPAKEDADCITRVY 434
Cdd:cd04199     75 EVGDTIKVHFKNKASRPYSIHPHGVSYEKDSEGASYSDQTGPDEKKDDAVAPGETYTYVWIVTEESGPTKGDPACLTWAY 154

                          170       180
                   ....*....|....*....|...
gi 1810777707  435 HSHIDAPRDVASGLVGPLIICKK 457
Cdd:cd04199    155 YSHVDLEKDINSGLIGPLLICKK 177
CuRO_2_ceruloplasmin_like cd04200
Cupredoxin domains 2, 4, and 6 of ceruloplasmin and similar proteins; This family includes the ...
 469-609 1.49e-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: 235.00  E-value: 1.49e-71
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1810777707  469 DAEFILMFSVMDENLSWYLEDNIRTYCSEPSKVDKDDEDFQESNKMHSINGYMYGYLPNLTMCAEDKVKWHLFGMGNEAD 548
Cdd:cd04200      1 DKEFVLLFAVFDENKSWYLEDNIKRFCDNPEKVDKDDEEFQESNKMHAINGYVFGNLPGLTMCAGDRVRWHLLGMGNEVD 80

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1810777707  549 IHSVYFHGQTLIERHHRVDTINLFPATFIDALMIPRNPGEWLLSCQVNDHVEGGMQALFKV 609
Cdd:cd04200     81 VHSIHFHGQTFLYKGYRIDTLTLFPATFETVEMVPSNPGTWLLHCHNSDHRHAGMQAYFLV 141
CuRO_2_ceruloplasmin_like cd04200
Cupredoxin domains 2, 4, and 6 of ceruloplasmin and similar proteins; This family includes the ...
 1165-1305 2.43e-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: 225.75  E-value: 2.43e-68
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1810777707 1165 FALLFMVFDENESWYLDENIETYSVNPHLVDKENEEFLESNKMHAINGKVFGNLHGLTMHVGDEVSWYLIAMGNEVDIHT 1244
Cdd:cd04200      4 FVLLFAVFDENKSWYLEDNIKRFCDNPEKVDKDDEEFQESNKMHAINGYVFGNLPGLTMCAGDRVRWHLLGMGNEVDVHS 83

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1810777707 1245 THFHGHSFNYKQtgvYRADVFDLFPGTFQTVEMIPQNPGTWLLHCHVTDHIHAGMEAIYTV 1305
Cdd:cd04200     84 IHFHGQTFLYKG---YRIDTLTLFPATFETVEMVPSNPGTWLLHCHNSDHRHAGMQAYFLV 141
CuRO_1_ceruloplasmin cd04222
The first cupredoxin domain of Ceruloplasmin; Ceruloplasmin is a multicopper oxidase essential ...
 626-811 1.44e-66

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


Pssm-ID: 259884 [Multi-domain]  Cd Length: 183  Bit Score: 222.68  E-value: 1.44e-66
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1810777707  626 RQYFIAAEEIIWNYGPSALNHFTGQELTADSESSVFFEQSETRIGGSYKKAIYKEYTDGTFTahkKRLPEEEHLGLLGPV 705
Cdd:cd04222      1 REYYIGIRETQWDYAPSGKNLITNQTFDDDEHASVFLKRGPDRIGRVYKKAVYLQYTDDTYR---TEIEKPVWLGFLGPI 77

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1810777707  706 IKAEVEESIRVTFRNNASRPFSIQPHGVSYQKSNEGALYRTASRDTESPASHVSPGATFTYEWNVPEDVGPTDQDPDCLT 785
Cdd:cd04222     78 LKAEVGDVIVVHLKNFASRPYSLHPHGVFYNKENEGALYPDNTSGFEKADDAVPPGGSYTYTWTVPEEQAPTKADANCLT 157

                          170       180
                   ....*....|....*....|....*.
gi 1810777707  786 WLYYSAVDSVRDTNSGLVGPLLVCRR 811
Cdd:cd04222    158 RIYHSHIDAPKDIASGLIGPLIICKK 183
CuRO_4_ceruloplasmin cd11022
The fourth cupredoxin domain of Ceruloplasmin; Ceruloplasmin is a multicopper oxidase ...
 469-612 1.53e-64

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: 215.04  E-value: 1.53e-64
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1810777707  469 DAEFILMFSVMDENLSWYLEDNIRTYCSEPSKVDKDDEDFQESNKMHSINGYMYGYLPNLTMCAEDKVKWHLFGMGNEAD 548
Cdd:cd11022      1 DKEFFLLFTVFDENESWYLDENIQQFTLDPRSVDKEDEDFQESNKMHSINGYMYGNQPGLDMCKGDTVSWHLFGLGTETD 80

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1810777707  549 IHSVYFHGQTLIERHHRVDTINLFPATFIDALMIPRNPGEWLLSCQVNDHVEGGMQALFKVEDC 612
Cdd:cd11022     81 VHGIYFSGNTFLLQGTRRDTANLFPHTSVTAIMQPDNEGTFEVNCQTTDHYSAGMRQIYTVSQC 144
CuRO_2_ceruloplasmin cd11021
The second cupredoxin domain of Ceruloplasmin; Ceruloplasmin is a multicopper oxidase ...
 825-964 3.50e-61

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


Pssm-ID: 259907 [Multi-domain]  Cd Length: 141  Bit Score: 205.40  E-value: 3.50e-61
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1810777707  825 REFFLLATVFDENLSWYLDDNILMFALNPNEIDKDNEDFQESNKMHSINGYMYGNQPGLEMCKGEVISWHLMGLGTEVDV 904
Cdd:cd11021      2 REFVLMFSVVDENLSWYLDENIKTYCSEPAKVDKDDEDFQESNKMHSINGYTFGNLPGLSMCAGDRVKWHLFGMGNEVDI 81

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1810777707  905 HGIYFSHNTFITKGTRKDTANLFPHTFVTAIMKPDSEGIFEVSCLTTDHYRGGMKQKYKV 964
Cdd:cd11021     82 HSAFFHGQTLTDRGHRTDTINLFPATFVTAEMVAQNPGKWLLSCQVNDHLKAGMQAFYEV 141
CuRO_2_ceruloplasmin cd11021
The second cupredoxin domain of Ceruloplasmin; Ceruloplasmin is a multicopper oxidase ...
 1165-1305 3.74e-61

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


Pssm-ID: 259907 [Multi-domain]  Cd Length: 141  Bit Score: 205.40  E-value: 3.74e-61
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1810777707 1165 FALLFMVFDENESWYLDENIETYSVNPHLVDKENEEFLESNKMHAINGKVFGNLHGLTMHVGDEVSWYLIAMGNEVDIHT 1244
Cdd:cd11021      4 FVLMFSVVDENLSWYLDENIKTYCSEPAKVDKDDEDFQESNKMHSINGYTFGNLPGLSMCAGDRVKWHLFGMGNEVDIHS 83

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1810777707 1245 THFHGHSFNYKQtgvYRADVFDLFPGTFQTVEMIPQNPGTWLLHCHVTDHIHAGMEAIYTV 1305
Cdd:cd11021     84 AFFHGQTLTDRG---HRTDTINLFPATFVTAEMVAQNPGKWLLSCQVNDHLKAGMQAFYEV 141
CuRO_3_FV_like cd14450
The third cupredoxin domain of coagulation factor V and similar proteins; Factor V is an ...
 624-810 3.78e-61

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: 207.04  E-value: 3.78e-61
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1810777707  624 KIRQYFIAAEEIIWNYGPSALNHFTGQEltadseSSVFFEQSETRIGGSYKKAIYKEYTDGTFTAHKKRlPEEEHLGLLG 703
Cdd:cd14450      1 KNWEYFIAAEEVIWDYAPSIPENMDKRY------RSQYLDNFSNNIGKKYKKAVFTQYEDGSFTKRLEN-PRPKEEGILG 73

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1810777707  704 PVIKAEVEESIRVTFRNNASRPFSIQPHGVSYQKSNEGALYRTASRDTESPASHVSPGATFTYEWNVPEDVGPTDQDPDC 783
Cdd:cd14450     74 PVIRAQVRDTIKIVFKNKASRPYSIYPHGVTVSKAAEGASYPPDPRGNETQNKAVQPGETYTYKWNILETDEPTARDPRC 153

                          170       180
                   ....*....|....*....|....*..
gi 1810777707  784 LTWLYYSAVDSVRDTNSGLVGPLLVCR 810
Cdd:cd14450    154 LTRMYHSAVDITRDIASGLIGPLLICK 180
CuRO_2_ceruloplasmin_like cd04200
Cupredoxin domains 2, 4, and 6 of ceruloplasmin and similar proteins; This family includes the ...
 825-964 8.81e-61

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: 204.18  E-value: 8.81e-61
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1810777707  825 REFFLLATVFDENLSWYLDDNILMFALNPNEIDKDNEDFQESNKMHSINGYMYGNQPGLEMCKGEVISWHLMGLGTEVDV 904
Cdd:cd04200      2 KEFVLLFAVFDENKSWYLEDNIKRFCDNPEKVDKDDEEFQESNKMHAINGYVFGNLPGLTMCAGDRVRWHLLGMGNEVDV 81

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1810777707  905 HGIYFSHNTFITKGTRKDTANLFPHTFVTAIMKPDSEGIFEVSCLTTDHYRGGMKQKYKV 964
Cdd:cd04200     82 HSIHFHGQTFLYKGYRIDTLTLFPATFETVEMVPSNPGTWLLHCHNSDHRHAGMQAYFLV 141
CuRO_5_ceruloplasmin cd04225
The fifth cupredoxin domain of Ceruloplasmin; Ceruloplasmin is a multicopper oxidase essential ...
 626-811 8.84e-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: 202.70  E-value: 8.84e-60
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1810777707  626 RQYFIAAEEIIWNYGPSALNHFTGQELTADSESSVFFEQSETRIGGSYKKAIYKEYTDGTFTAHKKRLPEEEHLGLLGPV 705
Cdd:cd04225      1 RTYYIAAEEVEWDYSPQRTWEQELHNTHEESPGNAFLNKGDKFIGSKYKKVVYREYTDDTFSVPKERTAEEEHLGILGPL 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1810777707  706 IKAEVEESIRVTFRNNASRPFSIQPHGVSyqksnegalyrtasrdTESPA-SHVSPGATFTYEWNVPEDVGPTDQDPDCL 784
Cdd:cd04225     81 IHAEVGEKVKIVFKNMASRPYSIHAHGVK----------------TDSSWvAPTEPGETQTYTWKIPERSGPGVEDSNCI 144

                          170       180
                   ....*....|....*....|....*..
gi 1810777707  785 TWLYYSAVDSVRDTNSGLVGPLLVCRR 811
Cdd:cd04225    145 SWAYYSTVDQIKDLYSGLIGPLVICRR 171
CuRO_1_ceruloplasmin_like cd04199
Cupredoxin domains 1, 3, and 5 of ceruloplasmin and similar proteins; This family includes the ...
 981-1149 7.71e-59

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: 200.32  E-value: 7.71e-59
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1810777707  981 KTHYIAAIEVEWDYSPNRTWEFERHQYheespgNPFLNKEDKFIGSKYKKVVYREYTDHTFSTPKsraEEEQHLQIQGPL 1060
Cdd:cd04199      1 RHYYIAAEEIDWDYAPSGLAEKDLSYR------NQYLDNGPFRIGRSYKKVVYREYTDESFTTPG---PQPEHLGILGPT 71

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1810777707 1061 IMSSIGDKINIVFKNLASRPYSIHAHGV-------------------KTDSSVVaitnPGETKTYVWKISARSSSERGEL 1121
Cdd:cd04199     72 IRAEVGDTIKVHFKNKASRPYSIHPHGVsyekdsegasysdqtgpdeKKDDAVA----PGETYTYVWIVTEESGPTKGDP 147

                          170       180
                   ....*....|....*....|....*...
gi 1810777707 1122 HCTAWAYHSTVDIIKDTYSGLIGTLVVC 1149
Cdd:cd04199    148 ACLTWAYYSHVDLEKDINSGLIGPLLIC 175
CuRO_3_ceruloplasmin cd04224
The third cupredoxin domain of Ceruloplasmin; Ceruloplasmin is a multicopper oxidase essential ...
 275-463 7.59e-58

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


Pssm-ID: 259886 [Multi-domain]  Cd Length: 197  Bit Score: 198.08  E-value: 7.59e-58
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1810777707  275 REYYIGIIETAWDYAPGNTDLISGQ-HFAEEEQAEVFLKRGPQRIGSIYKKAVYTQYTNILYDV---IVEKPSWLGFLGP 350
Cdd:cd04224      4 RHYFIAAEEIMWDYAPSGKNLFTGQnLTAPGSDSEVFFQRNETRIGGTYWKVRYVEYTDATFTTrkhRSKEEEHLGILGP 83

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1810777707  351 IIKGEVGDSIVIHLKNFASRNYTLHPHGVTYTKENEGAFYPDntkGFEKRDDAVKPGGQYTYTWDVTEDQGPAKEDADCI 430
Cdd:cd04224     84 VIRAEVGDTIKVTFRNKASRPFSIQPHGVFYEKNYEGAMYRD---GDPSPGSHVSPGETFTYEWTVPEGVGPTNQDPPCL 160

                          170       180       190
                   ....*....|....*....|....*....|...
gi 1810777707  431 TRVYHSHIDAPRDVASGLVGPLIICKKGAMNKD 463
Cdd:cd04224    161 TYLYFSAVDPVRDTNSGLVGPLLVCKKGSLNAN 193
CuRO_1_Ceruloplasmin_like_1 cd04229
cupredoxin domain of ceruloplasmin homologs; Uncharacterized subfamily of ceruloplasmin ...
 626-812 1.27e-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: 196.48  E-value: 1.27e-57
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1810777707  626 RQYFIAAEEIIWNYGPSALNHFTgqeLTADSE-SSVFFEQSETRIGGSYKKAIYKEYTDGTFTahkKRLPEEEHLGLLGP 704
Cdd:cd04229      1 RTYYIAAEEVDWDYAPSGKNKCC---LGDDLEvSTLDSQPGPYTIGSTYTKARYREYTDNSFS---TPKPTPAYLGILGP 74

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1810777707  705 VIKAEVEESIRVTFRNNASR-PFSIQPHGVSYQKSNEGALYRTASRdtespashVSPGATFTYEWNVPEDVGPTDQDPDC 783
Cdd:cd04229     75 VIRAEVGDTIKVVFKNNLDEfPVNMHPHGGLYSKDNEGTTDGAGDV--------VAPGETYTYRWIVPEDAGPGPGDPSS 146

                          170       180
                   ....*....|....*....|....*....
gi 1810777707  784 LTWLYYSAVDSVRDTNSGLVGPLLVCRRG 812
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 ...
 626-812 3.68e-57

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: 195.44  E-value: 3.68e-57
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1810777707  626 RQYFIAAEEIIWNYGPSALNHFTGQELTADsessvffeqsetrigGSYKKAIYKEYTDGTFTAHKKRLPEEEHLGLLGPV 705
Cdd:cd14451      2 RRYYIAAEEEEWDYAGYGKSRLDKTQNERD---------------TVFKKVVFRRYLDSTFSTPDIQGEYEEHLGILGPV 66

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1810777707  706 IKAEVEESIRVTFRNNASRPFSIQPHGVSYQKSNEGALYRTASRDTESPASHVSPGATFTYEWNVPEDVGPTDQDPDCLT 785
Cdd:cd14451     67 IRAEVDDVIQVFFKNLASRPYSLHAHGLSYEKSSEGLSYDDESPDWFKKDDAVQPNGTYTYVWYANPRSGPENNGSDCRT 146

                          170       180
                   ....*....|....*....|....*..
gi 1810777707  786 WLYYSAVDSVRDTNSGLVGPLLVCRRG 812
Cdd:cd14451    147 WAYYSAVNPEKDIHSGLIGPLLICRKG 173
CuRO_1_FVIII_like cd14452
The first cupredoxin domain of coagulation factor VIII and similar proteins; Factor VIII ...
 275-458 1.00e-56

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


Pssm-ID: 259994 [Multi-domain]  Cd Length: 173  Bit Score: 194.04  E-value: 1.00e-56
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1810777707  275 REYYIGIIETAWDYApgntdlisgqhFAEEEQAEVFLKRGPQRIGSIYKKAVYTQYTNILYDVIVEKPSWLGFLGPIIKG 354
Cdd:cd14452      1 RRYYIAAVEIGWDYI-----------HSDLGDPASEQRKKPKDIPQKYIKAVFVEYLDATFTVPKPRPAWMGLLGPTIVA 69

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1810777707  355 EVGDSIVIHLKNFASRNYTLHPHGVTYTKENEGAFYPDNTKGFEKRDDAVKPGGQYTYTWDVTEDQGPAKEDADCITRVY 434
Cdd:cd14452     70 EVGDTVVITFKNLASQPYSLHAVGVSYWKASEGAGYDDSTSQHEKEDDAVYPGGYHTYVWDISPKDGPTGSDPECLTYSY 149

                          170       180
                   ....*....|....*....|....
gi 1810777707  435 HSHIDAPRDVASGLVGPLIICKKG 458
Cdd:cd14452    150 SSQVDPVKDVNSGLIGALLVCRMG 173
CuRO_4_ceruloplasmin cd11022
The fourth cupredoxin domain of Ceruloplasmin; Ceruloplasmin is a multicopper oxidase ...
 1165-1305 2.73e-56

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: 191.54  E-value: 2.73e-56
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1810777707 1165 FALLFMVFDENESWYLDENIETYSVNPHLVDKENEEFLESNKMHAINGKVFGNLHGLTMHVGDEVSWYLIAMGNEVDIHT 1244
Cdd:cd11022      4 FFLLFTVFDENESWYLDENIQQFTLDPRSVDKEDEDFQESNKMHSINGYMYGNQPGLDMCKGDTVSWHLFGLGTETDVHG 83

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1810777707 1245 THFHGHSFNYKQTgvyRADVFDLFPGTFQTVEMIPQNPGTWLLHCHVTDHIHAGMEAIYTV 1305
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 ...
 276-456 5.13e-56

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: 192.40  E-value: 5.13e-56
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1810777707  276 EYYIGIIETAWDYAPGNTDLISGQHFAEeeqaevFLKRGPQRIGSIYKKAVYTQYTNILYDVIVE--KPSWLGFLGPIIK 353
Cdd:cd14450      4 EYFIAAEEVIWDYAPSIPENMDKRYRSQ------YLDNFSNNIGKKYKKAVFTQYEDGSFTKRLEnpRPKEEGILGPVIR 77

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1810777707  354 GEVGDSIVIHLKNFASRNYTLHPHGVTYTKENEGAFYPDNTKGFEKRDDAVKPGGQYTYTWDVTEDQGPAKEDADCITRV 433
Cdd:cd14450     78 AQVRDTIKIVFKNKASRPYSIYPHGVTVSKAAEGASYPPDPRGNETQNKAVQPGETYTYKWNILETDEPTARDPRCLTRM 157

                          170       180
                   ....*....|....*....|...
gi 1810777707  434 YHSHIDAPRDVASGLVGPLIICK 456
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 ...
 275-458 3.26e-53

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


Pssm-ID: 259888 [Multi-domain]  Cd Length: 165  Bit Score: 183.52  E-value: 3.26e-53
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1810777707  275 REYYIGIIETAWDYAPGNTDLISgqhfaeeeqaevflkrgpQRIGSIYKKAVYTQYTNilyDVIVEKPSWL--GFLGPII 352
Cdd:cd04226      1 REYYIAAQNIDWDYTPQSEELRL------------------KRSEQSFKKIVYREYEE---GFKKEKPADLssGLLGPTL 59

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1810777707  353 KGEVGDSIVIHLKNFASRNYTLHPHGVTYTKENEGAFYPDNTKGFEKRDDAVKPGGQYTYTWDVTEDQGPAKEDADCITR 432
Cdd:cd04226     60 RAEVGDTLIVHFKNMADKPLSIHPQGIAYGKKSEGSLYSDNTSPVEKLDDAVQPGQEYTYVWDITEEVGPTEADPPCLTY 139

                          170       180
                   ....*....|....*....|....*.
gi 1810777707  433 VYHSHIDAPRDVASGLVGPLIICKKG 458
Cdd:cd04226    140 IYYSHVNMVRDFNSGLIGALLICKKG 165
CuRO_1_Ceruloplasmin_like_1 cd04229
cupredoxin domain of ceruloplasmin homologs; Uncharacterized subfamily of ceruloplasmin ...
 275-458 2.09e-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: 181.85  E-value: 2.09e-52
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1810777707  275 REYYIGIIETAWDYAPGNTDLIsgqHFAEE-EQAEVFLKRGPQRIGSIYKKAVYTQYTNILYDVIVEKPSWLGFLGPIIK 353
Cdd:cd04229      1 RTYYIAAEEVDWDYAPSGKNKC---CLGDDlEVSTLDSQPGPYTIGSTYTKARYREYTDNSFSTPKPTPAYLGILGPVIR 77

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1810777707  354 GEVGDSIVIHLKN-FASRNYTLHPHGVTYTKENEGafypdntkGFEKRDDAVKPGGQYTYTWDVTEDQGPAKEDADCITR 432
Cdd:cd04229     78 AEVGDTIKVVFKNnLDEFPVNMHPHGGLYSKDNEG--------TTDGAGDVVAPGETYTYRWIVPEDAGPGPGDPSSRLW 149

                          170       180
                   ....*....|....*....|....*.
gi 1810777707  433 VYHSHIDAPRDVASGLVGPLIICKKG 458
Cdd:cd04229    150 LYHSHVDVFAHTNAGLVGPIIVTSKG 175
CuRO_5_FVIII_like cd04228
The fifth cupredoxin domain of coagulation factor VIII and similar proteins; Factor VIII ...
 625-812 3.12e-52

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: 180.85  E-value: 3.12e-52
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1810777707  625 IRQYFIAAEEIIWNYGPSALNHFTgQELTADSESSVFFEQsetriggsYKKAIYKEYTDGTFTAHKKRLPEEEHLGLLGP 704
Cdd:cd04228      1 IRHYFIAAVEVLWDYGMQRPQHFL-RARDPNRGRRKSVPQ--------YKKVVFREYLDGSFTQPVYRGELDEHLGILGP 71

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1810777707  705 VIKAEVEESIRVTFRNNASRPFSIQPHGVSYQksNEGAlyrtasrdTESPASHVSPGATFTYEWNVPEDVGPTDQDPDCL 784
Cdd:cd04228     72 YIRAEVEDNIMVTFKNLASRPYSFHSSLISYE--EDQR--------AEPRGNFVQPGEVQTYSWKVLHQMAPTKQEFDCK 141

                          170       180
                   ....*....|....*....|....*...
gi 1810777707  785 TWLYYSAVDSVRDTNSGLVGPLLVCRRG 812
Cdd:cd04228    142 AWAYFSNVDLEKDLHSGLIGPLIICKTG 169
CuRO_6_ceruloplasmin cd11012
The sixth cupredoxin domain of Ceruloplasmin; Ceruloplasmin is a multicopper oxidase essential ...
 471-609 3.75e-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: 179.68  E-value: 3.75e-52
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1810777707  471 EFILMFSVMDENLSWYLEDNIRTYCSEPSKVDKDDEDFQESNKMHSINGYMYGYLPNLTMCAEDKVKWHLFGMGNEADIH 550
Cdd:cd11012      3 EFALLFLVFDENESWYLDENIKTYSDHPEKVNKEDEEFIESNKMHAINGKVFGNLQGLTMHVGDEVYWYLMGMGNEIDIH 82

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1810777707  551 SVYFHGQTLIERH---HRVDTINLFPATFIDALMIPRNPGEWLLSCQVNDHVEGGMQALFKV 609
Cdd:cd11012     83 TAHFHGHSFDYKHrgvYRSDVFDLFPGTFQTVEMIPRTPGTWLLHCHVTDHIHAGMETTYTV 144
CuRO_3_ceruloplasmin cd04224
The third cupredoxin domain of Ceruloplasmin; Ceruloplasmin is a multicopper oxidase essential ...
 979-1161 4.26e-52

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: 181.52  E-value: 4.26e-52
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1810777707  979 HEKTHYIAAIEVEWDYSPNRTWEFERHQY-HEESPGNPFLNKEDKFIGSKYKKVVYREYTDHTFSTPKSRAEEEQHLQIQ 1057
Cdd:cd04224      2 KVRHYFIAAEEIMWDYAPSGKNLFTGQNLtAPGSDSEVFFQRNETRIGGTYWKVRYVEYTDATFTTRKHRSKEEEHLGIL 81

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1810777707 1058 GPLIMSSIGDKINIVFKNLASRPYSIHAHGV------------KTDSSVVAITNPGETKTYVWKISARSSSERGELHCTA 1125
Cdd:cd04224     82 GPVIRAEVGDTIKVTFRNKASRPFSIQPHGVfyeknyegamyrDGDPSPGSHVSPGETFTYEWTVPEGVGPTNQDPPCLT 161

                          170       180       190
                   ....*....|....*....|....*....|....*.
gi 1810777707 1126 WAYHSTVDIIKDTYSGLIGTLVVCPRHYLPSSHTRK 1161
Cdd:cd04224    162 YLYFSAVDPVRDTNSGLVGPLLVCKKGSLNANGRQK 197
CuRO_1_FV_like cd04226
The first cupredoxin domain of coagulation factor VIII and similar proteins; Factor V is an ...
 626-812 5.00e-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: 180.06  E-value: 5.00e-52
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1810777707  626 RQYFIAAEEIIWNYGPsalnhftGQEltadsessvffEQSETRIGGSYKKAIYKEYTDGtftaHKKRLPEEEHLGLLGPV 705
Cdd:cd04226      1 REYYIAAQNIDWDYTP-------QSE-----------ELRLKRSEQSFKKIVYREYEEG----FKKEKPADLSSGLLGPT 58

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1810777707  706 IKAEVEESIRVTFRNNASRPFSIQPHGVSYQKSNEGALYRTASRDTESPASHVSPGATFTYEWNVPEDVGPTDQDPDCLT 785
Cdd:cd04226     59 LRAEVGDTLIVHFKNMADKPLSIHPQGIAYGKKSEGSLYSDNTSPVEKLDDAVQPGQEYTYVWDITEEVGPTEADPPCLT 138

                          170       180
                   ....*....|....*....|....*..
gi 1810777707  786 WLYYSAVDSVRDTNSGLVGPLLVCRRG 812
Cdd:cd04226    139 YIYYSHVNMVRDFNSGLIGALLICKKG 165
CuRO_1_FVIII_like cd14452
The first cupredoxin domain of coagulation factor VIII and similar proteins; Factor VIII ...
 626-812 1.89e-49

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


Pssm-ID: 259994 [Multi-domain]  Cd Length: 173  Bit Score: 173.24  E-value: 1.89e-49
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1810777707  626 RQYFIAAEEIIWNYGPSALNhftgqELTADSESSVFFEQSEtriggsYKKAIYKEYTDGTFTAHKKRLPeeeHLGLLGPV 705
Cdd:cd14452      1 RRYYIAAVEIGWDYIHSDLG-----DPASEQRKKPKDIPQK------YIKAVFVEYLDATFTVPKPRPA---WMGLLGPT 66

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1810777707  706 IKAEVEESIRVTFRNNASRPFSIQPHGVSYQKSNEGALYRTASRDTESPASHVSPGATFTYEWNVPEDVGPTDQDPDCLT 785
Cdd:cd14452     67 IVAEVGDTVVITFKNLASQPYSLHAVGVSYWKASEGAGYDDSTSQHEKEDDAVYPGGYHTYVWDISPKDGPTGSDPECLT 146

                          170       180
                   ....*....|....*....|....*..
gi 1810777707  786 WLYYSAVDSVRDTNSGLVGPLLVCRRG 812
Cdd:cd14452    147 YSYSSQVDPVKDVNSGLIGALLVCRMG 173
L6_membrane pfam05805
L6 membrane protein; This family consists of several eukaryotic L6 membrane proteins. L6, ...
 1-106 4.39e-49

L6 membrane protein; This family consists of several eukaryotic L6 membrane proteins. L6, IL-TMP, and TM4SF5 are cell surface proteins predicted to have four transmembrane domains. Previous sequence analysis led to their assignment as members of the tetraspanin superfamily it has now been found that that they are not significantly related to genuine tetraspanins, but instead constitute their own L6 family. Several members of this family have been implicated in human cancer.


Pssm-ID: 461745  Cd Length: 192  Bit Score: 172.75  E-value: 4.39e-49
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1810777707    1 MLSSVLAACVGILGSGYCVIISALGLSQGPYCLTRA-ERNWIYPFTQSS-GGYLLEYNEWSKCQEPQNIVQWNVTLFSIL 78
Cdd:pfam05805   85 MFLSILFSAIGVLGAGYCFIVSALALAEGPLCLTNGgSTSWGYPFKNNFnGNYLFNQSLWSVCLEPENIVEWHVTLFSIL 164

                           90       100
                   ....*....|....*....|....*...
gi 1810777707   79 LVLGGIEFILCFIQIVNGILGGVCRLCC 106
Cdd:pfam05805  165 LLVSGLELLLCLIQVVNGLLGCLCGTCK 192
CuRO_5_FV_like cd14451
The fifth cupredoxin domain of coagulation factor V and similar proteins; Factor V is an ...
 274-458 3.27e-47

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


Pssm-ID: 259993 [Multi-domain]  Cd Length: 173  Bit Score: 166.94  E-value: 3.27e-47
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1810777707  274 TREYYIGIIETAWDYAP-GNTDLISGQHFAEeeqaevflkrgpqrigSIYKKAVYTQYTNILY---DVIVEKPSWLGFLG 349
Cdd:cd14451      1 KRRYYIAAEEEEWDYAGyGKSRLDKTQNERD----------------TVFKKVVFRRYLDSTFstpDIQGEYEEHLGILG 64

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1810777707  350 PIIKGEVGDSIVIHLKNFASRNYTLHPHGVTYTKENEGAFYPDNTKGFEKRDDAVKPGGQYTYTWDVTEDQGPAKEDADC 429
Cdd:cd14451     65 PVIRAEVDDVIQVFFKNLASRPYSLHAHGLSYEKSSEGLSYDDESPDWFKKDDAVQPNGTYTYVWYANPRSGPENNGSDC 144

                          170       180
                   ....*....|....*....|....*....
gi 1810777707  430 ITRVYHSHIDAPRDVASGLVGPLIICKKG 458
Cdd:cd14451    145 RTWAYYSAVNPEKDIHSGLIGPLLICRKG 173
CuRO_3_FVIII_like cd04227
The third cupredoxin domain of coagulation factor VIII and similar proteins; Factor VIII ...
 624-811 4.99e-47

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


Pssm-ID: 259889 [Multi-domain]  Cd Length: 177  Bit Score: 166.26  E-value: 4.99e-47
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1810777707  624 KIRQYFIAAEEIIWNYGPSALnhftgqeLTADSE-SSVFFEQSETRIGGSYKKAIYKEYTDGTFtahKKRLPEEEHLGLL 702
Cdd:cd04227      1 QTWEHYIAAEELDWDYAPLLS-------STDDRElQSRYLPTGPQRIGYKYKKVAFVEYTDKTF---KRREAKQTEKGIL 70

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1810777707  703 GPVIKAEVEESIRVTFRNNASRPFSIQPHGVSYQKSnegaLYRTASRDTESPASH--VSPGATFTYEWNVPEDVGPTDQD 780
Cdd:cd04227     71 GPLLKGEVGDQIHIMFKNTASRPYNIYPHGLTSVRP----MYRSRNPAGEKDLKTmpIGPGETFGYMWELTAEDGPTEED 146

                          170       180       190
                   ....*....|....*....|....*....|.
gi 1810777707  781 PDCLTWLYYSAVDSVRDTNSGLVGPLLVCRR 811
Cdd:cd04227    147 PRCLTRLYQSTVDPERDLASGLIGPLLICKK 177
CuRO_3_FVIII_like cd04227
The third cupredoxin domain of coagulation factor VIII and similar proteins; Factor VIII ...
 273-457 1.01e-45

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: 162.79  E-value: 1.01e-45
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1810777707  273 VTREYYIGIIETAWDYAPgntdLISGQhfAEEEQAEVFLKRGPQRIGSIYKKAVYTQYTNILYDVIVEKPSWLGFLGPII 352
Cdd:cd04227      1 QTWEHYIAAEELDWDYAP----LLSST--DDRELQSRYLPTGPQRIGYKYKKVAFVEYTDKTFKRREAKQTEKGILGPLL 74

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1810777707  353 KGEVGDSIVIHLKNFASRNYTLHPHGVTYTKENEGAFYPDNTKgfEKRDDAVKPGGQYTYTWDVTEDQGPAKEDADCITR 432
Cdd:cd04227     75 KGEVGDQIHIMFKNTASRPYNIYPHGLTSVRPMYRSRNPAGEK--DLKTMPIGPGETFGYMWELTAEDGPTEEDPRCLTR 152

                          170       180
                   ....*....|....*....|....*
gi 1810777707  433 VYHSHIDAPRDVASGLVGPLIICKK 457
Cdd:cd04227    153 LYQSTVDPERDLASGLIGPLLICKK 177
CuRO_5_FV_like cd14451
The fifth cupredoxin domain of coagulation factor V and similar proteins; Factor V is an ...
 980-1149 2.52e-45

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


Pssm-ID: 259993 [Multi-domain]  Cd Length: 173  Bit Score: 161.55  E-value: 2.52e-45
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1810777707  980 EKTHYIAAIEVEWDYSPnrtweferhqyheesPGNPFLNKEDKFIGSKYKKVVYREYTDHTFSTPKSRAEEEQHLQIQGP 1059
Cdd:cd14451      1 KRRYYIAAEEEEWDYAG---------------YGKSRLDKTQNERDTVFKKVVFRRYLDSTFSTPDIQGEYEEHLGILGP 65

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1810777707 1060 LIMSSIGDKINIVFKNLASRPYSIHAHGVKTDSSVVAIT---------------NPGETKTYVWKISARSSSERGELHCT 1124
Cdd:cd14451     66 VIRAEVDDVIQVFFKNLASRPYSLHAHGLSYEKSSEGLSyddespdwfkkddavQPNGTYTYVWYANPRSGPENNGSDCR 145

                          170       180
                   ....*....|....*....|....*
gi 1810777707 1125 AWAYHSTVDIIKDTYSGLIGTLVVC 1149
Cdd:cd14451    146 TWAYYSAVNPEKDIHSGLIGPLLIC 170
CuRO_5_FVIII_like cd04228
The fifth cupredoxin domain of coagulation factor VIII and similar proteins; Factor VIII ...
 983-1151 6.82e-44

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: 156.97  E-value: 6.82e-44
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1810777707  983 HYIAAIEVEWDYSPNRTWEFERHQYHEESPGNPFlnkedkfigSKYKKVVYREYTDHTFSTPKSRAEEEQHLQIQGPLIM 1062
Cdd:cd04228      4 YFIAAVEVLWDYGMQRPQHFLRARDPNRGRRKSV---------PQYKKVVFREYLDGSFTQPVYRGELDEHLGILGPYIR 74

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1810777707 1063 SSIGDKINIVFKNLASRPYSIHAHGVKTDSSVVA-----ITNPGETKTYVWKISARSSSERGELHCTAWAYHSTVDIIKD 1137
Cdd:cd04228     75 AEVEDNIMVTFKNLASRPYSFHSSLISYEEDQRAeprgnFVQPGEVQTYSWKVLHQMAPTKQEFDCKAWAYFSNVDLEKD 154

                          170
                   ....*....|....
gi 1810777707 1138 TYSGLIGTLVVCPR 1151
Cdd:cd04228    155 LHSGLIGPLIICKT 168
CuRO_5_ceruloplasmin cd04225
The fifth cupredoxin domain of Ceruloplasmin; Ceruloplasmin is a multicopper oxidase essential ...
 275-457 1.24e-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: 156.47  E-value: 1.24e-43
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1810777707  275 REYYIGIIETAWDYAPGNTDLISGQHFAEEEQAEVFLKRGPQRIGSIYKKAVYTQYTNILYDVIVEKPS---WLGFLGPI 351
Cdd:cd04225      1 RTYYIAAEEVEWDYSPQRTWEQELHNTHEESPGNAFLNKGDKFIGSKYKKVVYREYTDDTFSVPKERTAeeeHLGILGPL 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1810777707  352 IKGEVGDSIVIHLKNFASRNYTLHPHGVtytKENEGAFYPdntkgfekrddaVKPGGQYTYTWDVTEDQGPAKEDADCIT 431
Cdd:cd04225     81 IHAEVGEKVKIVFKNMASRPYSIHAHGV---KTDSSWVAP------------TEPGETQTYTWKIPERSGPGVEDSNCIS 145

                          170       180
                   ....*....|....*....|....*.
gi 1810777707  432 RVYHSHIDAPRDVASGLVGPLIICKK 457
Cdd:cd04225    146 WAYYSTVDQIKDLYSGLIGPLVICRR 171
CuRO_6_FVIII_like cd11018
The sixth cupredoxin domain of coagulation factor VIII and similar proteins; Factor VIII ...
 1165-1305 2.56e-41

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


Pssm-ID: 259904 [Multi-domain]  Cd Length: 144  Bit Score: 148.87  E-value: 2.56e-41
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1810777707 1165 FALLFMVFDENESWYLDENIETYSVNPHLVDKENEEFLESNKMHAINGKVFGNLHGLTMHVGDEVSWYLIAMGNEVDIHT 1244
Cdd:cd11018      4 FALLFTIFDETKSWYFEENMRRNCRPPCHIQTQDPWFHINNKFHAINGYVADTLPGLVMAQHQRIRWHLLNMGSDEEIHS 83

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1810777707 1245 THFHGHSFNYKQTGVYRADVFDLFPGTFQTVEMIPQNPGTWLLHCHVTDHIHAGMEAIYTV 1305
Cdd:cd11018     84 VHFHGLPFTVRAKKEYRMGVYNLYPGVFGTVEMRPSTAGIWLVECTVGEHLLAGMSALFLV 144
CuRO_6_ceruloplasmin cd11012
The sixth cupredoxin domain of Ceruloplasmin; Ceruloplasmin is a multicopper oxidase essential ...
 826-964 5.14e-41

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


Pssm-ID: 259898 [Multi-domain]  Cd Length: 145  Bit Score: 148.09  E-value: 5.14e-41
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1810777707  826 EFFLLATVFDENLSWYLDDNILMFALNPNEIDKDNEDFQESNKMHSINGYMYGNQPGLEMCKGEVISWHLMGLGTEVDVH 905
Cdd:cd11012      3 EFALLFLVFDENESWYLDENIKTYSDHPEKVNKEDEEFIESNKMHAINGKVFGNLQGLTMHVGDEVYWYLMGMGNEIDIH 82

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1810777707  906 GIYFSHNTFITKGT---RKDTANLFPHTFVTAIMKPDSEGIFEVSCLTTDHYRGGMKQKYKV 964
Cdd:cd11012     83 TAHFHGHSFDYKHRgvyRSDVFDLFPGTFQTVEMIPRTPGTWLLHCHVTDHIHAGMETTYTV 144
CuRO_1_Ceruloplasmin_like_1 cd04229
cupredoxin domain of ceruloplasmin homologs; Uncharacterized subfamily of ceruloplasmin ...
 981-1148 3.70e-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: 3.70e-40
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1810777707  981 KTHYIAAIEVEWDYSP-NRTWEFERHQYHEESPGnpfLNKEDKFIGSKYKKVVYREYTDHTFSTPKSraeEEQHLQIQGP 1059
Cdd:cd04229      1 RTYYIAAEEVDWDYAPsGKNKCCLGDDLEVSTLD---SQPGPYTIGSTYTKARYREYTDNSFSTPKP---TPAYLGILGP 74

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1810777707 1060 LIMSSIGDKINIVFKN-LASRPYSIHAHGV-------KTDSSVVAITNPGETKTYVWKISARSSSERGELHCTAWAYHST 1131
Cdd:cd04229     75 VIRAEVGDTIKVVFKNnLDEFPVNMHPHGGlyskdneGTTDGAGDVVAPGETYTYRWIVPEDAGPGPGDPSSRLWLYHSH 154

                          170
                   ....*....|....*..
gi 1810777707 1132 VDIIKDTYSGLIGTLVV 1148
Cdd:cd04229    155 VDVFAHTNAGLVGPIIV 171
CuRO_1_ceruloplasmin cd04222
The first cupredoxin domain of Ceruloplasmin; Ceruloplasmin is a multicopper oxidase essential ...
 981-1151 9.36e-39

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


Pssm-ID: 259884 [Multi-domain]  Cd Length: 183  Bit Score: 142.94  E-value: 9.36e-39
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1810777707  981 KTHYIAAIEVEWDYSPNRTWEFERHQYHEESPGNPFLNKEDKFIGSKYKKVVYREYTDHTFSTpksRAEEEQHLQIQGPL 1060
Cdd:cd04222      1 REYYIGIRETQWDYAPSGKNLITNQTFDDDEHASVFLKRGPDRIGRVYKKAVYLQYTDDTYRT---EIEKPVWLGFLGPI 77

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1810777707 1061 IMSSIGDKINIVFKNLASRPYSIHAHGV-------------------KTDSSVvaitNPGETKTYVWKISARSSSERGEL 1121
Cdd:cd04222     78 LKAEVGDVIVVHLKNFASRPYSLHPHGVfynkenegalypdntsgfeKADDAV----PPGGSYTYTWTVPEEQAPTKADA 153

                          170       180       190
                   ....*....|....*....|....*....|
gi 1810777707 1122 HCTAWAYHSTVDIIKDTYSGLIGTLVVCPR 1151
Cdd:cd04222    154 NCLTRIYHSHIDAPKDIASGLIGPLIICKK 183
L6_membrane pfam05805
L6 membrane protein; This family consists of several eukaryotic L6 membrane proteins. L6, ...
 129-244 1.93e-38

L6 membrane protein; This family consists of several eukaryotic L6 membrane proteins. L6, IL-TMP, and TM4SF5 are cell surface proteins predicted to have four transmembrane domains. Previous sequence analysis led to their assignment as members of the tetraspanin superfamily it has now been found that that they are not significantly related to genuine tetraspanins, but instead constitute their own L6 family. Several members of this family have been implicated in human cancer.


Pssm-ID: 461745  Cd Length: 192  Bit Score: 142.32  E-value: 1.93e-38
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1810777707  129 CCqseSCNKTYRSFISIVLAMLGVAFSGYSCIIFTLGLIQGPFCNSSSG---WDYIFKD-TVGGYLTNYSAWSQCAEPAN 204
Cdd:pfam05805   76 CC---SCGNRCGMFLSILFSAIGVLGAGYCFIVSALALAEGPLCLTNGGstsWGYPFKNnFNGNYLFNQSLWSVCLEPEN 152

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|
gi 1810777707  205 AVEWTIILLSILMTLSGLQLIICFLKAAAELKRALCGTYS 244
Cdd:pfam05805  153 IVEWHVTLFSILLLVSGLELLLCLIQVVNGLLGCLCGTCK 192
CuRO_6_FVIII_like cd11018
The sixth cupredoxin domain of coagulation factor VIII and similar proteins; Factor VIII ...
 471-609 2.26e-38

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


Pssm-ID: 259904 [Multi-domain]  Cd Length: 144  Bit Score: 140.40  E-value: 2.26e-38
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1810777707  471 EFILMFSVMDENLSWYLEDNIRTYCSEPSKVDKDDEDFQESNKMHSINGYMYGYLPNLTMCAEDKVKWHLFGMGNEADIH 550
Cdd:cd11018      3 EFALLFTIFDETKSWYFEENMRRNCRPPCHIQTQDPWFHINNKFHAINGYVADTLPGLVMAQHQRIRWHLLNMGSDEEIH 82

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1810777707  551 SVYFHGQTLIER---HHRVDTINLFPATFIDALMIPRNPGEWLLSCQVNDHVEGGMQALFKV 609
Cdd:cd11018     83 SVHFHGLPFTVRakkEYRMGVYNLYPGVFGTVEMRPSTAGIWLVECTVGEHLLAGMSALFLV 144
CuRO_3_FVIII_like cd04227
The third cupredoxin domain of coagulation factor VIII and similar proteins; Factor VIII ...
 982-1149 1.60e-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: 139.29  E-value: 1.60e-37
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1810777707  982 THYIAAIEVEWDYSPNRTWEFERhqyheeSPGNPFLNKEDKFIGSKYKKVVYREYTDHTFSTPKSRAEEEQhlqIQGPLI 1061
Cdd:cd04227      4 EHYIAAEELDWDYAPLLSSTDDR------ELQSRYLPTGPQRIGYKYKKVAFVEYTDKTFKRREAKQTEKG---ILGPLL 74

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1810777707 1062 MSSIGDKINIVFKNLASRPYSIHAHGVKTDSSVVAITN-------------PGETKTYVWKISARSSSERGELHCTAWAY 1128
Cdd:cd04227     75 KGEVGDQIHIMFKNTASRPYNIYPHGLTSVRPMYRSRNpagekdlktmpigPGETFGYMWELTAEDGPTEEDPRCLTRLY 154

                          170       180
                   ....*....|....*....|.
gi 1810777707 1129 HSTVDIIKDTYSGLIGTLVVC 1149
Cdd:cd04227    155 QSTVDPERDLASGLIGPLLIC 175
CuRO_3_FV_like cd14450
The third cupredoxin domain of coagulation factor V and similar proteins; Factor V is an ...
 982-1149 1.78e-37

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: 139.24  E-value: 1.78e-37
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1810777707  982 THYIAAIEVEWDYSPNRTWEFERhQYHEEspgnpFLNKEDKFIGSKYKKVVYREYTDHTFsTPKSRAEEEQHLQIQGPLI 1061
Cdd:cd14450      4 EYFIAAEEVIWDYAPSIPENMDK-RYRSQ-----YLDNFSNNIGKKYKKAVFTQYEDGSF-TKRLENPRPKEEGILGPVI 76

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1810777707 1062 MSSIGDKINIVFKNLASRPYSIHAHGVKTDSSVVAIT---------------NPGETKTYVWKISARSSSERGELHCTAW 1126
Cdd:cd14450     77 RAQVRDTIKIVFKNKASRPYSIYPHGVTVSKAAEGASyppdprgnetqnkavQPGETYTYKWNILETDEPTARDPRCLTR 156

                          170       180
                   ....*....|....*....|...
gi 1810777707 1127 AYHSTVDIIKDTYSGLIGTLVVC 1149
Cdd:cd14450    157 MYHSAVDITRDIASGLIGPLLIC 179
CuRO_2_ceruloplasmin_like_2 cd11023
cupredoxin domain of ceruloplasmin homologs; Uncharacterized subfamily of ceruloplasmin ...
 1171-1305 1.86e-35

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


Pssm-ID: 259909 [Multi-domain]  Cd Length: 118  Bit Score: 130.81  E-value: 1.86e-35
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1810777707 1171 VFDENESWYLDENIEtysvnphlvdkeneeflESNKMHAINGKVFGNLHGLTMHVGDEVSWYLIAMGNEVDIHTTHFHGH 1250
Cdd:cd11023      3 EFIENSSIFLDLNVE-----------------EAGLMHSINGYVFGNLPGVTIAKGKRVRWHLVAYGNEVDFHTPHWHGQ 65

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 1810777707 1251 SFNYKQTGvyRADVFDLFPGTFQTVEMIPQNPGTWLLHCHVTDHIHAGMEAIYTV 1305
Cdd:cd11023     66 TVEADKSR--RTDVAELMPASMRVADMTAADVGTWLLHCHVHDHYMAGMMTQFAV 118
CuRO_6_FV_like cd14455
The sixth cupredoxin domain of coagulation factor V and similar proteins; Factor V is an ...
 1165-1305 3.12e-35

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


Pssm-ID: 259997 [Multi-domain]  Cd Length: 140  Bit Score: 131.14  E-value: 3.12e-35
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1810777707 1165 FALLFMVFDENESWYLDENietysvnPHLVDKENE----EFLESNKMHAINGKVFgNLHGLTMHVGDEVSWYLIAMGNEV 1240
Cdd:cd14455      4 FVLLFMTFDEEKSWYYEKN-------RKRTCRENRvkdpNVQDNHTFHAINGIIY-NLKGLRMYTNELVRWHLINMGGPK 75

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1810777707 1241 DIHTTHFHGHSFNYKQTGVYRADVFDLFPGTFQTVEMIPQNPGTWLLHCHVTDHIHAGMEAIYTV 1305
Cdd:cd14455     76 DLHVVHFHGQTFTEKGLKDHQLGVYPLLPGSFATLEMKPSKPGLWLLETEVGESQQRGMQTLFLV 140
CuRO_5_FVIII_like cd04228
The fifth cupredoxin domain of coagulation factor VIII and similar proteins; Factor VIII ...
 274-458 2.09e-34

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: 130.01  E-value: 2.09e-34
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1810777707  274 TREYYIGIIETAWDYapGNTdliSGQHFAEEEQaevfLKRGPQRIGSIYKKAVYTQYTNILYDVIV---EKPSWLGFLGP 350
Cdd:cd04228      1 IRHYFIAAVEVLWDY--GMQ---RPQHFLRARD----PNRGRRKSVPQYKKVVFREYLDGSFTQPVyrgELDEHLGILGP 71

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1810777707  351 IIKGEVGDSIVIHLKNFASRNYTLHPHGVTYtkenegafypDNTKGFEKRDDAVKPGGQYTYTWDVTEDQGPAKEDADCI 430
Cdd:cd04228     72 YIRAEVEDNIMVTFKNLASRPYSFHSSLISY----------EEDQRAEPRGNFVQPGEVQTYSWKVLHQMAPTKQEFDCK 141

                          170       180
                   ....*....|....*....|....*...
gi 1810777707  431 TRVYHSHIDAPRDVASGLVGPLIICKKG 458
Cdd:cd04228    142 AWAYFSNVDLEKDLHSGLIGPLIICKTG 169
CuRO_2_ceruloplasmin_like_2 cd11023
cupredoxin domain of ceruloplasmin homologs; Uncharacterized subfamily of ceruloplasmin ...
 504-609 1.16e-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: 125.80  E-value: 1.16e-33
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1810777707  504 DDEDFQESNKMHSINGYMYGYLPNLTMCAEDKVKWHLFGMGNEADIHSVYFHGQTL-IERHHRVDTINLFPATFIDALMI 582
Cdd:cd11023     12 LDLNVEEAGLMHSINGYVFGNLPGVTIAKGKRVRWHLVAYGNEVDFHTPHWHGQTVeADKSRRTDVAELMPASMRVADMT 91

                           90       100
                   ....*....|....*....|....*..
gi 1810777707  583 PRNPGEWLLSCQVNDHVEGGMQALFKV 609
Cdd:cd11023     92 AADVGTWLLHCHVHDHYMAGMMTQFAV 118
CuRO_6_FV_like cd14455
The sixth cupredoxin domain of coagulation factor V and similar proteins; Factor V is an ...
 471-609 1.30e-33

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


Pssm-ID: 259997 [Multi-domain]  Cd Length: 140  Bit Score: 126.52  E-value: 1.30e-33
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1810777707  471 EFILMFSVMDENLSWYLEDNIRTYCSEpskVDKDDEDFQESNKMHSINGYMYGyLPNLTMCAEDKVKWHLFGMGNEADIH 550
Cdd:cd14455      3 EFVLLFMTFDEEKSWYYEKNRKRTCRE---NRVKDPNVQDNHTFHAINGIIYN-LKGLRMYTNELVRWHLINMGGPKDLH 78

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1810777707  551 SVYFHGQTLIE---RHHRVDTINLFPATFIDALMIPRNPGEWLLSCQVNDHVEGGMQALFKV 609
Cdd:cd14455     79 VVHFHGQTFTEkglKDHQLGVYPLLPGSFATLEMKPSKPGLWLLETEVGESQQRGMQTLFLV 140
CuRO_2_FV_like cd14453
The second cupredoxin domain of coagulation factor V and similar proteins; Factor V is an ...
 469-605 2.43e-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: 124.97  E-value: 2.43e-33
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1810777707  469 DAEFILMFSVMDENLSWYlednirtycsepskvdkdDEDFQESNKMHSINGYMYGYLPNLTMCAEDKVKWHLFGMGNEAD 548
Cdd:cd14453      1 YKEYVLMFGVFDENKSWY------------------KQNASVDSVKYTINGYTNGTLPDVSICAYDHVSWHLLGMSSEPE 62

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 1810777707  549 IHSVYFHGQTLIERHHRVDTINLFPATFIDALMIPRNPGEWLLSCQVNDHVEGGMQA 605
Cdd:cd14453     63 LFSVHFNGQVLEQNGHKVSAVGLVSGSSTTASMTVVHTGRWLISSLIMKHLQAGMYG 119
CuRO_4_FVIII_like cd11016
The fourth cupredoxin domain of coagulation factor VIII and similar proteins; Factor VIII ...
 469-612 7.83e-33

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: 124.60  E-value: 7.83e-33
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1810777707  469 DAEFILMFSVMDENLSWYLEDNIRTYCSEPSKVDKDDEDFQESNKMHSINGYMYGYLpNLTMCAEDKVKWHLFGMGNEAD 548
Cdd:cd11016      1 DKDWSLLFSVFDENNSWYLKENIHRFTQTPAGVNDTDPDFYASNVMHTINGIVFDRR-QFVICLTDVAYWYVLSVGAQTD 79

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1810777707  549 IHSVYFHGQTLIERHHRVDTINLFPATFIDALMIPRNPGEWLLSCQVNDHVEGGMQALFKVEDC 612
Cdd:cd11016     80 FLSVFFSGNTFKHQMVYEDVLTLFPFSGETVSMSPEVPGEWELGCFNGDFRSRGMSAQYTVSTC 143
CuRO_1_FVIII_like cd14452
The first cupredoxin domain of coagulation factor VIII and similar proteins; Factor VIII ...
 981-1149 1.72e-32

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: 124.71  E-value: 1.72e-32
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1810777707  981 KTHYIAAIEVEWDYSpnrtweferHQYHEESPGNPflNKEDKFIGSKYKKVVYREYTDHTFSTPKSRAEeeqHLQIQGPL 1060
Cdd:cd14452      1 RRYYIAAVEIGWDYI---------HSDLGDPASEQ--RKKPKDIPQKYIKAVFVEYLDATFTVPKPRPA---WMGLLGPT 66

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1810777707 1061 IMSSIGDKINIVFKNLASRPYSIHAHGV-------------------KTDSSVvaitNPGETKTYVWKISARSSSERGEL 1121
Cdd:cd14452     67 IVAEVGDTVVITFKNLASQPYSLHAVGVsywkasegagyddstsqheKEDDAV----YPGGYHTYVWDISPKDGPTGSDP 142

                          170       180
                   ....*....|....*....|....*...
gi 1810777707 1122 HCTAWAYHSTVDIIKDTYSGLIGTLVVC 1149
Cdd:cd14452    143 ECLTYSYSSQVDPVKDVNSGLIGALLVC 170
CuRO_2_FVIII_like cd11015
The second cupredoxin domain of coagulation factor VIII and similar proteins; Factor VIII ...
 471-609 7.42e-32

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


Pssm-ID: 259901 [Multi-domain]  Cd Length: 134  Bit Score: 121.17  E-value: 7.42e-32
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1810777707  471 EFILMFSVMDENLSWYLEDnirtycSEPSKVDKDDEDfQESNKMHSINGYMYGYLPNLTMCAEDKVKWHLFGMGNEADIH 550
Cdd:cd11015      3 AFVLLFAVFDEGKSWYSEV------GERKSRDKFKRA-DSRKEFHTINGYINASLPGLKICQRKPVIWHVIGMGTAPEVH 75

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 1810777707  551 SVYFHGQTLIERHHRVDTINLFPATFIDALMIPRNPGEWLLSCQVNDHVEGGMQALFKV 609
Cdd:cd11015     76 SIFFEGHTFLVRTHRKVSLEISPMTFLTAQTKPATVGSFLIFCQIHSHQHDGMEAMVKV 134
CuRO_4_FV_like cd14454
The fourth cupredoxin domain of coagulation factor V and similar proteins; Factor V is an ...
 469-612 1.04e-31

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


Pssm-ID: 259996 [Multi-domain]  Cd Length: 144  Bit Score: 121.13  E-value: 1.04e-31
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1810777707  469 DAEFILMFSVMDENLSWYLEDNIRTYCSEPSKVDKDDEDFQESNKMHSINGYMYGYLPNLTMCAEDKVKWHLFGMGNEAD 548
Cdd:cd14454      1 DLEQHAVFAVFDENKSWYLEENINKYCSNPNNVKKDDPKFYKSNIMPTINGYAYESSAPLGFCHSEVVQWHISSVGTQDE 80

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1810777707  549 IHSVYFHGQTLIERHHRVDTINLFPATFIDALMIPRNPGEWLLSCQVNDHVEGGMQALFKVEDC 612
Cdd:cd14454     81 IITVHLSGHTFRYKGKHEDTLNLFPMSGESITVTMDNLGTWLLGSFGSSKKSKGLRVRFTDVIC 144
CuRO_4_FVIII_like cd11016
The fourth cupredoxin domain of coagulation factor VIII and similar proteins; Factor VIII ...
 829-967 3.85e-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: 3.85e-31
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1810777707  829 LLATVFDENLSWYLDDNILMFALNPNEIDKDNEDFQESNKMHSINGYMYGNQPgLEMCKGEVISWHLMGLGTEVDVHGIY 908
Cdd:cd11016      6 LLFSVFDENNSWYLKENIHRFTQTPAGVNDTDPDFYASNVMHTINGIVFDRRQ-FVICLTDVAYWYVLSVGAQTDFLSVF 84

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 1810777707  909 FSHNTFITKGTRKDTANLFPHTFVTAIMKPDSEGIFEVSCLTTDHYRGGMKQKYKVKPC 967
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 ...
 832-967 2.03e-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: 117.67  E-value: 2.03e-30
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1810777707  832 TVFDENLSWYLDDNILMFALNPNEIDKDNEDFQESNKMHSINGYMYGNQPGLEMCKGEVISWHLMGLGTEVDVHGIYFSH 911
Cdd:cd14454      9 AVFDENKSWYLEENINKYCSNPNNVKKDDPKFYKSNIMPTINGYAYESSAPLGFCHSEVVQWHISSVGTQDEIITVHLSG 88

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 1810777707  912 NTFITKGTRKDTANLFPHTFVTAIMKPDSEGIFEVSCLTTDHYRGGMKQKYKVKPC 967
Cdd:cd14454     89 HTFRYKGKHEDTLNLFPMSGESITVTMDNLGTWLLGSFGSSKKSKGLRVRFTDVIC 144
CuRO_4_FVIII_like cd11016
The fourth cupredoxin domain of coagulation factor VIII and similar proteins; Factor VIII ...
 1167-1306 2.90e-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: 114.19  E-value: 2.90e-29
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1810777707 1167 LLFMVFDENESWYLDENIETYSVNPHLVDKENEEFLESNKMHAINGKVFGNLHgLTMHVGDEVSWYLIAMGNEVDIHTTH 1246
Cdd:cd11016      6 LLFSVFDENNSWYLKENIHRFTQTPAGVNDTDPDFYASNVMHTINGIVFDRRQ-FVICLTDVAYWYVLSVGAQTDFLSVF 84

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1810777707 1247 FHGHSFNYKqtGVYRaDVFDLFPGTFQTVEMIPQNPGTWLLHCHVTDHIHAGMEAIYTVL 1306
Cdd:cd11016     85 FSGNTFKHQ--MVYE-DVLTLFPFSGETVSMSPEVPGEWELGCFNGDFRSRGMSAQYTVS 141
CuRO_6_FVIII_like cd11018
The sixth cupredoxin domain of coagulation factor VIII and similar proteins; Factor VIII ...
 825-964 6.08e-28

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


Pssm-ID: 259904 [Multi-domain]  Cd Length: 144  Bit Score: 110.36  E-value: 6.08e-28
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1810777707  825 REFFLLATVFDENLSWYLDDNILMFALNPNEIDKDNEDFQESNKMHSINGYMYGNQPGLEMCKGEVISWHLMGLGTEVDV 904
Cdd:cd11018      2 QEFALLFTIFDETKSWYFEENMRRNCRPPCHIQTQDPWFHINNKFHAINGYVADTLPGLVMAQHQRIRWHLLNMGSDEEI 81

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1810777707  905 HGIYFSHNTFITKGT---RKDTANLFPHTFVTAIMKPDSEGIFEVSCLTTDHYRGGMKQKYKV 964
Cdd:cd11018     82 HSVHFHGLPFTVRAKkeyRMGVYNLYPGVFGTVEMRPSTAGIWLVECTVGEHLLAGMSALFLV 144
CuRO_1_FV_like cd04226
The first cupredoxin domain of coagulation factor VIII and similar proteins; Factor V is an ...
 983-1149 3.49e-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: 3.49e-27
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1810777707  983 HYIAAIEVEWDYSPnrtweferhQYHEespgnpflnKEDKFIGSKYKKVVYREYtDHTFSTPKSRAEEEQHLqiqGPLIM 1062
Cdd:cd04226      3 YYIAAQNIDWDYTP---------QSEE---------LRLKRSEQSFKKIVYREY-EEGFKKEKPADLSSGLL---GPTLR 60

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1810777707 1063 SSIGDKINIVFKNLASRPYSIHAHGV-------------------KTDSSVVaitnPGETKTYVWKISARSSSERGELHC 1123
Cdd:cd04226     61 AEVGDTLIVHFKNMADKPLSIHPQGIaygkksegslysdntspveKLDDAVQ----PGQEYTYVWDITEEVGPTEADPPC 136

                          170       180
                   ....*....|....*....|....*.
gi 1810777707 1124 TAWAYHSTVDIIKDTYSGLIGTLVVC 1149
Cdd:cd04226    137 LTYIYYSHVNMVRDFNSGLIGALLIC 162
CuRO_4_FV_like cd14454
The fourth cupredoxin domain of coagulation factor V and similar proteins; Factor V is an ...
 1168-1287 6.95e-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: 107.65  E-value: 6.95e-27
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1810777707 1168 LFMVFDENESWYLDENIETYSVNPHLVDKENEEFLESNKMHAINGKVFGNLHGLTMHVGDEVSWYLIAMGNEVDIHTTHF 1247
Cdd:cd14454      7 VFAVFDENKSWYLEENINKYCSNPNNVKKDDPKFYKSNIMPTINGYAYESSAPLGFCHSEVVQWHISSVGTQDEIITVHL 86

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|
gi 1810777707 1248 HGHSFNYKQTgvyRADVFDLFPGTFQTVEMIPQNPGTWLL 1287
Cdd:cd14454     87 SGHTFRYKGK---HEDTLNLFPMSGESITVTMDNLGTWLL 123
CuRO_2_FVIII_like cd11015
The second cupredoxin domain of coagulation factor VIII and similar proteins; Factor VIII ...
 825-964 5.73e-25

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: 101.52  E-value: 5.73e-25
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1810777707  825 REFFLLATVFDENLSWYLDDNilmfalNPNEIDKDNEDfQESNKMHSINGYMYGNQPGLEMCKGEVISWHLMGLGTEVDV 904
Cdd:cd11015      2 QAFVLLFAVFDEGKSWYSEVG------ERKSRDKFKRA-DSRKEFHTINGYINASLPGLKICQRKPVIWHVIGMGTAPEV 74

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1810777707  905 HGIYFSHNTFITKGTRKDTANLFPHTFVTAIMKPDSEGIFEVSCLTTDHYRGGMKQKYKV 964
Cdd:cd11015     75 HSIFFEGHTFLVRTHRKVSLEISPMTFLTAQTKPATVGSFLIFCQIHSHQHDGMEAMVKV 134
CuRO_2_ceruloplasmin_like_2 cd11023
cupredoxin domain of ceruloplasmin homologs; Uncharacterized subfamily of ceruloplasmin ...
 859-964 1.20e-24

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


Pssm-ID: 259909 [Multi-domain]  Cd Length: 118  Bit Score: 99.99  E-value: 1.20e-24
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1810777707  859 DNEDFQESNKMHSINGYMYGNQPGLEMCKGEVISWHLMGLGTEVDVHGIYFSHNTFITKGTRK-DTANLFPHTFVTAIMK 937
Cdd:cd11023     12 LDLNVEEAGLMHSINGYVFGNLPGVTIAKGKRVRWHLVAYGNEVDFHTPHWHGQTVEADKSRRtDVAELMPASMRVADMT 91

                           90       100
                   ....*....|....*....|....*..
gi 1810777707  938 PDSEGIFEVSCLTTDHYRGGMKQKYKV 964
Cdd:cd11023     92 AADVGTWLLHCHVHDHYMAGMMTQFAV 118
CuRO_2_FVIII_like cd11015
The second cupredoxin domain of coagulation factor VIII and similar proteins; Factor VIII ...
 1165-1305 9.33e-22

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: 92.28  E-value: 9.33e-22
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1810777707 1165 FALLFMVFDENESWYLDENietysvNPHLVDKENEEFlESNKMHAINGKVFGNLHGLTMHVGDEVSWYLIAMGNEVDIHT 1244
Cdd:cd11015      4 FVLLFAVFDEGKSWYSEVG------ERKSRDKFKRAD-SRKEFHTINGYINASLPGLKICQRKPVIWHVIGMGTAPEVHS 76

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1810777707 1245 THFHGHSFNYKQtgvYRADVFDLFPGTFQTVEMIPQNPGTWLLHCHVTDHIHAGMEAIYTV 1305
Cdd:cd11015     77 IFFEGHTFLVRT---HRKVSLEISPMTFLTAQTKPATVGSFLIFCQIHSHQHDGMEAMVKV 134
CuRO_6_FV_like cd14455
The sixth cupredoxin domain of coagulation factor V and similar proteins; Factor V is an ...
 825-964 8.90e-20

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


Pssm-ID: 259997 [Multi-domain]  Cd Length: 140  Bit Score: 86.84  E-value: 8.90e-20
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1810777707  825 REFFLLATVFDENLSWYLDDNILMFALNPNEIDKDnedFQESNKMHSINGYMYgNQPGLEMCKGEVISWHLMGLGTEVDV 904
Cdd:cd14455      2 REFVLLFMTFDEEKSWYYEKNRKRTCRENRVKDPN---VQDNHTFHAINGIIY-NLKGLRMYTNELVRWHLINMGGPKDL 77

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1810777707  905 HGIYFSHNTFITKGTRKDTAN---LFPHTFVTAIMKPDSEGIFEVSCLTTDHYRGGMKQKYKV 964
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 ...
 1165-1301 1.64e-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: 82.60  E-value: 1.64e-18
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1810777707 1165 FALLFMVFDENESWYldenietySVNPHlvdkeneeflESNKMHAINGKVFGNLHGLTMHVGDEVSWYLIAMGNEVDIHT 1244
Cdd:cd14453      4 YVLMFGVFDENKSWY--------KQNAS----------VDSVKYTINGYTNGTLPDVSICAYDHVSWHLLGMSSEPELFS 65

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 1810777707 1245 THFHGHSFNYKQtgvYRADVFDLFPGTFQTVEMIPQNPGTWLLHCHVTDHIHAGMEA 1301
Cdd:cd14453     66 VHFNGQVLEQNG---HKVSAVGLVSGSSTTASMTVVHTGRWLISSLIMKHLQAGMYG 119
Cu-oxidase_2 pfam07731
Multicopper oxidase; This entry contains many divergent copper oxidase-like domains that are ...
 1205-1309 3.33e-18

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: 82.48  E-value: 3.33e-18
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1810777707 1205 NKMHAINGKVFG-NLHGLTMHVGDEVSWYLIAMGNevDIHTTHFHGHSF----------NYKQTGVY------RADVFDL 1267
Cdd:pfam07731   19 RNDWAINGLLFPpNTNVITLPYGTVVEWVLQNTTT--GVHPFHLHGHSFqvlgrgggpwPEEDPKTYnlvdpvRRDTVQV 96

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|..
gi 1810777707 1268 FPGTFQTVEMIPQNPGTWLLHCHVTDHIHAGMEAIYTVLPEE 1309
Cdd:pfam07731   97 PPGGWVAIRFRADNPGVWLFHCHILWHLDQGMMGQFVVRPGD 138
CuRO_1_LCC_like cd04206
Cupredoxin domain 1 of laccase-like multicopper oxidases; including laccase, CueO, spore coat ...
 346-455 1.77e-17

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


Pssm-ID: 259869 [Multi-domain]  Cd Length: 120  Bit Score: 79.64  E-value: 1.77e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1810777707  346 GFLGPIIKGEVGDSIVIHLKN-FASRNYTLHPHGVTYTKENEGAFYPDNTKgfekrdDAVKPGGQYTYTWDVTEDQGpak 424
Cdd:cd04206     27 QFPGPTIRVKEGDTVEVTVTNnLPNEPTSIHWHGLRQPGTNDGDGVAGLTQ------CPIPPGESFTYRFTVDDQAG--- 97

                           90       100       110
                   ....*....|....*....|....*....|.
gi 1810777707  425 edadciTRVYHSHIDAprDVASGLVGPLIIC 455
Cdd:cd04206     98 ------TFWYHSHVGG--QRADGLYGPLIVE 120
CuRO_2_FV_like cd14453
The second cupredoxin domain of coagulation factor V and similar proteins; Factor V is an ...
 825-958 5.98e-17

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


Pssm-ID: 259995 [Multi-domain]  Cd Length: 123  Bit Score: 78.36  E-value: 5.98e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1810777707  825 REFFLLATVFDENLSWYlddnilmfalnpneidkdNEDFQESNKMHSINGYMYGNQPGLEMCKGEVISWHLMGLGTEVDV 904
Cdd:cd14453      2 KEYVLMFGVFDENKSWY------------------KQNASVDSVKYTINGYTNGTLPDVSICAYDHVSWHLLGMSSEPEL 63

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....
gi 1810777707  905 HGIYFSHNTFITKGTRKDTANLFPHTFVTAIMKPDSEGIFEVSCLTTDHYRGGM 958
Cdd:cd14453     64 FSVHFNGQVLEQNGHKVSAVGLVSGSSTTASMTVVHTGRWLISSLIMKHLQAGM 117
CuRO_3_LCC_like cd04207
Cupredoxin domain 3 of laccase-like multicopper oxidases; including laccase, CueO, spore coat ...
 1209-1304 6.51e-15

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: 72.88  E-value: 6.51e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1810777707 1209 AINGKVF----GNLHGLTMHVGDEVSWYLIAMGNEVDIHTTHFHGHSF------------NYKQTGVYRADVFDLFPGTF 1272
Cdd:cd04207     21 VINGMPFkegdANTDIFSVEAGDVVEIVLINAGNHDMQHPFHLHGHSFwvlgsgggpfdaPLNLTNPPWRDTVLVPPGGW 100

                           90       100       110
                   ....*....|....*....|....*....|..
gi 1810777707 1273 QTVEMIPQNPGTWLLHCHVTDHIHAGMEAIYT 1304
Cdd:cd04207    101 VVIRFKADNPGVWMLHCHILEHEDAGMMTVFE 132
CuRO_1_LCC_like cd04206
Cupredoxin domain 1 of laccase-like multicopper oxidases; including laccase, CueO, spore coat ...
 688-809 2.82e-13

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: 67.70  E-value: 2.82e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1810777707  688 AHKKRLPEEEHLGLLGPVIKAEVEESIRVTFRNN-ASRPFSIQPHGVSYQKSNE--GALYRTASrdtespasHVSPGATF 764
Cdd:cd04206     15 DGVLRQVITVNGQFPGPTIRVKEGDTVEVTVTNNlPNEPTSIHWHGLRQPGTNDgdGVAGLTQC--------PIPPGESF 86

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*
gi 1810777707  765 TYEWNVPEDVGptdqdpdclTWLYYSAVDSVRDTnsGLVGPLLVC 809
Cdd:cd04206     87 TYRFTVDDQAG---------TFWYHSHVGGQRAD--GLYGPLIVE 120
CuRO_D2_2dMcoN_like cd04202
The second cupredoxin domain of bacterial two domain multicopper oxidase McoN and similar ...
 1207-1299 5.63e-12

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: 64.58  E-value: 5.63e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1810777707 1207 MHAINGKVFGNLHGLTMHVGDEVSWYLIAMGNevDIHTTHFHGHSFNYKQT-GV-------YRADVFDLFPGTFQTVEMI 1278
Cdd:cd04202     29 YFTINGKSFPATPPLVVKEGDRVRIRLINLSM--DHHPMHLHGHFFLVTATdGGpipgsapWPKDTLNVAPGERYDIEFV 106

                           90       100
                   ....*....|....*....|.
gi 1810777707 1279 PQNPGTWLLHCHVTDHIHAGM 1299
Cdd:cd04202    107 ADNPGDWMFHCHKLHHAMNGM 127
Cu-oxidase_3 pfam07732
Multicopper oxidase; This entry contains many divergent copper oxidase-like domains that are ...
 329-454 6.48e-12

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


Pssm-ID: 462247 [Multi-domain]  Cd Length: 119  Bit Score: 63.80  E-value: 6.48e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1810777707  329 QYTNILYDVIVEKPSWL---GFLGPIIKGEVGDSIVIHLKNFASRNYTLHPHGVTYTKENEGAFYPDNTKgfekrdDAVK 405
Cdd:pfam07732    3 TYGTVSPLGGTRQAVIGvngQFPGPTIRVREGDTVVVNVTNNLDEPTSIHWHGLQQRGTPWMDGVPGVTQ------CPIP 76

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*....
gi 1810777707  406 PGGQYTYTWDVTEDQGpakedadciTRVYHSHIDAPRdvASGLVGPLII 454
Cdd:pfam07732   77 PGQSFTYRFQVKQQAG---------TYWYHSHTSGQQ--AAGLAGAIII 114
CuRO_3_CumA_like cd13906
The third cupredoxin domain of CumA like multicopper oxidase; This multicopper oxidase (MCO) ...
 1209-1299 7.80e-12

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: 64.33  E-value: 7.80e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1810777707 1209 AINGKVFGNLHG-------LTMHVGDevsWYLIAMGNEVD-IHTTHFHGHSF-----NYKQTGV-YRADVFDLFPGtfQT 1274
Cdd:cd13906     30 AINGTSWTGGDHshlppplATLKRGR---SYVLRLVNETAfLHPMHLHGHFFrvlsrNGRPVPEpFWRDTVLLGPK--ET 104

                           90       100
                   ....*....|....*....|....*..
gi 1810777707 1275 VE--MIPQNPGTWLLHCHVTDHIHAGM 1299
Cdd:cd13906    105 VDiaFVADNPGDWMFHCHILEHQETGM 131
CuRO_1_2DMCO_NIR_like_2 cd14449
The cupredoxin domain 1 of a two-domain laccase related to nitrite reductase; The two-domain ...
 703-811 4.89e-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: 58.82  E-value: 4.89e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1810777707  703 GPVIKAEVEESIRVTFRNNASRPFSIQPHGVSYQKSNEGALyrtasrdteSPASHVSPGATFTYEWNVPEDVGPTDQDPD 782
Cdd:cd14449     29 GPVIEVREGDTLKILFRNTLDVPASLHPHGVDYTTASDGTG---------MNASIVAPGDTRIYTWRTHGGYRRADGSWA 99

                           90       100       110
                   ....*....|....*....|....*....|....*.
gi 1810777707  783 CLT---WLYYSAV----DSVRDTNSGLVGPLLVCRR 811
Cdd:cd14449    100 EGTagyWHYHDHVfgteHGTEGLSRGLYGALIVRRV 135
Cu-oxidase pfam00394
Multicopper oxidase; Many of the proteins in this family contain multiple similar copies of ...
 476-612 6.08e-10

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: 58.87  E-value: 6.08e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1810777707  476 FSVMDENLSWYlEDNIRTYCSEPSKVDKDDEDFQESNKMHSINGYMYGYLPNLTMCAEDKVKWHLFGMGNEadiHSVYF- 554
Cdd:pfam00394    1 EDYVITLSDWY-HKDAKDLEKELLASGKAPTDFPPVPDAVLINGKDGASLATLTVTPGKTYRLRIINVALD---DSLNFs 76

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1810777707  555 ---HGQTLIE---RHH---RVDTINLFPATFIDALMIP-RNPGEWLLSCQVN-DHVEGGMQALFKVEDC 612
Cdd:pfam00394   77 iegHKMTVVEvdgVYVnpfTVDSLDIFPGQRYSVLVTAnQDPGNYWIVASPNiPAFDNGTAAAILRYSG 145
CuRO_3_CumA_like cd13906
The third cupredoxin domain of CumA like multicopper oxidase; This multicopper oxidase (MCO) ...
 537-609 3.14e-09

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


Pssm-ID: 259973 [Multi-domain]  Cd Length: 138  Bit Score: 56.62  E-value: 3.14e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1810777707  537 KWHLFGMGNEAD-IHSVYFHG----------QTLIERHHRvDTINLFPATFIDALMIPRNPGEWLLSCQVNDHVEGGMQA 605
Cdd:cd13906     55 RSYVLRLVNETAfLHPMHLHGhffrvlsrngRPVPEPFWR-DTVLLGPKETVDIAFVADNPGDWMFHCHILEHQETGMMG 133


                   ....
gi 1810777707  606 LFKV 609
Cdd:cd13906    134 VIRV 137
CuRO_1_2DMCO_NIR_like_2 cd14449
The cupredoxin domain 1 of a two-domain laccase related to nitrite reductase; The two-domain ...
 349-454 3.71e-09

The cupredoxin domain 1 of a two-domain laccase related to nitrite reductase; The two-domain laccase (small laccase) in this family differs significantly from all laccases. It resembles the two domain nitrite reductase in both sequence and structure. It consists of two cupredoxin domains and forms trimers, and hence resembles the quaternary structure of nitrite reductases more than that of large laccases. There are three trinuclear copper clusters in the enzyme localized between domains 1 and 2 of each pair of neighbor chains. 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: 56.51  E-value: 3.71e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1810777707  349 GPIIKGEVGDSIVIHLKNFASRNYTLHPHGVTYTKENEGAFYPDNtkgfekrddAVKPGGQYTYTWDVtedQGPAKEDAD 428
Cdd:cd14449     29 GPVIEVREGDTLKILFRNTLDVPASLHPHGVDYTTASDGTGMNAS---------IVAPGDTRIYTWRT---HGGYRRADG 96

                           90       100       110
                   ....*....|....*....|....*....|....*.
gi 1810777707  429 CI------TRVYHSHI----DAPRDVASGLVGPLII 454
Cdd:cd14449     97 SWaegtagYWHYHDHVfgteHGTEGLSRGLYGALIV 132
CuRO_3_LCC_like cd04207
Cupredoxin domain 3 of laccase-like multicopper oxidases; including laccase, CueO, spore coat ...
 516-607 4.11e-09

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: 56.31  E-value: 4.11e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1810777707  516 SING----YMYGYLPNLTMCAEDKVKWHLFGMGNEADIHSVYFHGQtlierHHRV--------------------DTINL 571
Cdd:cd04207     21 VINGmpfkEGDANTDIFSVEAGDVVEIVLINAGNHDMQHPFHLHGH-----SFWVlgsgggpfdaplnltnppwrDTVLV 95

                           90       100       110
                   ....*....|....*....|....*....|....*.
gi 1810777707  572 FPATFIDALMIPRNPGEWLLSCQVNDHVEGGMQALF 607
Cdd:cd04207     96 PPGGWVVIRFKADNPGVWMLHCHILEHEDAGMMTVF 131
CuRO_1_Diphenol_Ox cd13857
The first cupredoxin domain of fungal laccase, diphenol oxidase; Diphenol oxidase belongs to ...
 347-454 4.44e-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: 55.73  E-value: 4.44e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1810777707  347 FLGPIIKGEVGDSIVIHLKNFASRNYTLHPHGVTytkeNEGAFYPDNTKGFEKRddAVKPGGQYTYTWDVTEDQGpaked 426
Cdd:cd13857     28 FPGPLIEANQGDRIVVHVTNELDEPTSIHWHGLF----QNGTNWMDGTAGITQC--PIPPGGSFTYNFTVDGQYG----- 96

                           90       100
                   ....*....|....*....|....*...
gi 1810777707  427 adciTRVYHSHIDAprDVASGLVGPLII 454
Cdd:cd13857     97 ----TYWYHSHYST--QYADGLVGPLIV 118
SufI COG2132
Multicopper oxidase with three cupredoxin domains (includes cell division protein FtsP and ...
 1207-1307 8.15e-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: 59.56  E-value: 8.15e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1810777707 1207 MHAINGKVFGNLH-GLTMHVGDEVSWYLIAMGNevDIHTTHFHGHSF-----NYKQTGV-YRADVFDLFPGtfQTVEMI- 1278
Cdd:COG2132    317 VWTINGKAFDPDRpDLTVKLGERERWTLVNDTM--MPHPFHLHGHQFqvlsrNGKPPPEgGWKDTVLVPPG--ETVRILf 392

                           90       100       110
                   ....*....|....*....|....*....|.
gi 1810777707 1279 --PQNPGTWLLHCHVTDHIHAGMEAIYTVLP 1307
Cdd:COG2132    393 rfDNYPGDWMFHCHILEHEDAGMMGQFEVVP 423
CuRO_3_CopA cd13896
The third cupredoxin domain of CopA copper resistance protein family; CopA is a multicopper ...
 1210-1299 1.06e-08

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


Pssm-ID: 259963 [Multi-domain]  Cd Length: 115  Bit Score: 54.57  E-value: 1.06e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1810777707 1210 INGKVFGNLHGLTMHVGDEVswyLIAMGNEVDI-HTTHFHGHSF---NYKQTGVYRADVFDLFPGTFQTVEMIPQNPGTW 1285
Cdd:cd13896     19 INGKAYPDADPLRVREGERV---RIVFVNDTMMaHPMHLHGHFFqveNGNGEYGPRKDTVLVPPGETVSVDFDADNPGRW 95

                           90
                   ....*....|....
gi 1810777707 1286 LLHCHVTDHIHAGM 1299
Cdd:cd13896     96 AFHCHNLYHMEAGM 109
CuRO_3_McoC_like cd13902
The third cupredoxin domain of a multicopper oxidase McoC and similar proteins; This family ...
 1207-1305 1.67e-08

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


Pssm-ID: 259969 [Multi-domain]  Cd Length: 125  Bit Score: 54.33  E-value: 1.67e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1810777707 1207 MHAINGKVFG-NLHGLTMHVGDEVSWYLIamgNEVDI-HTTHFHGHSFN------YKQTGVYRA--DVFDLFPGTFQTVE 1276
Cdd:cd13902     20 MFLINGKTFDmNRIDFVAKVGEVEVWEVT---NTSHMdHPFHLHGTQFQvleidgNPQKPEYRAwkDTVNLPPGEAVRIA 96

                           90       100
                   ....*....|....*....|....*....
gi 1810777707 1277 MIPQNPGTWLLHCHVTDHIHAGMEAIYTV 1305
Cdd:cd13902     97 TRQDDPGMWMYHCHILEHEDAGMMGMLHV 125
CuRO_3_MCO_like_3 cd13909
The third cupredoxin domain of uncharacterized multicopper oxidase; Multicopper Oxidases (MCOs) ...
 1234-1299 2.16e-08

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


Pssm-ID: 259976 [Multi-domain]  Cd Length: 137  Bit Score: 54.06  E-value: 2.16e-08
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1810777707 1234 IAMGNEVDI-HTTHFHGHSF-----NYkQTGVYRaDVFDLFPGTFQTVEMIPQNPGTWLLHCHVTDHIHAGM 1299
Cdd:cd13909     61 IEMVNNTGFpHGMHLHGHHFrailpNG-ALGPWR-DTLLMDRGETREIAFVADNPGDWLLHCHMLEHAAAGM 130
CuRO_1_2DMCO_NIR_like cd11024
The cupredoxin domain 1 of a two-domain laccase related to nitrite reductase; The two-domain ...
 349-454 2.45e-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: 53.43  E-value: 2.45e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1810777707  349 GPIIKGEVGDSIVIHLKNFASRNYTLHPHGVTYTKENEGAFYPdntkgfekrddaVKPGGQYTYTWDVTedqgPAKedad 428
Cdd:cd11024     32 GPTLRATEGDLVRIHFINTGDHPHTIHFHGIHDAAMDGTGLGP------------IMPGESFTYEFVAE----PAG---- 91

                           90       100
                   ....*....|....*....|....*...
gi 1810777707  429 ciTRVYHSHIdAP--RDVASGLVGPLII 454
Cdd:cd11024     92 --THLYHCHV-QPlkEHIAMGLYGAFIV 116
CuRO_D1_2dMcoN_like cd13859
The first cupredoxin domain of bacterial two domain multicopper oxidase McoN and similar ...
 349-454 2.67e-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: 53.64  E-value: 2.67e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1810777707  349 GPIIKGEVGDSIVIHLKNFASRNYTLHPHGVTYTkeneGAFYPDNTKGFEKRddAVKPGGQYTYTWDVtEDQGpakedad 428
Cdd:cd13859     31 GPLIHVKEGDDLVVHVTNNTTLPHTIHWHGVLQM----GSWKMDGVPGVTQP--AIEPGESFTYKFKA-ERPG------- 96

                           90       100
                   ....*....|....*....|....*..
gi 1810777707  429 ciTRVYHSHIDAPRDVA-SGLVGPLII 454
Cdd:cd13859     97 --TLWYHCHVNVNEHVGmRGMWGPLIV 121
CuRO_1_2DMCO_NIR_like_2 cd14449
The cupredoxin domain 1 of a two-domain laccase related to nitrite reductase; The two-domain ...
 1056-1151 3.35e-08

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


Pssm-ID: 259991 [Multi-domain]  Cd Length: 135  Bit Score: 53.81  E-value: 3.35e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1810777707 1056 IQGPLIMSSIGDKINIVFKNLASRPYSIHAHGVKTD-SSVVAITN-----PGETKTYVW---KISARSSSERGELHCTAW 1126
Cdd:cd14449     27 VPGPVIEVREGDTLKILFRNTLDVPASLHPHGVDYTtASDGTGMNasivaPGDTRIYTWrthGGYRRADGSWAEGTAGYW 106

                           90       100
                   ....*....|....*....|....*....
gi 1810777707 1127 AYHSTV----DIIKDTYSGLIGTLVVCPR 1151
Cdd:cd14449    107 HYHDHVfgteHGTEGLSRGLYGALIVRRV 135
CuRO_3_MaLCC_like cd13901
The third cupredoxin domain of the fungal laccases similar to Ma-LCC from Melanocarpus ...
 1223-1299 3.49e-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: 54.15  E-value: 3.49e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1810777707 1223 MHVGDEVSWYLIAMGNEVDI-HTTHFHGHSFN--YKQTGVY-------------RADVFDLFPGTFQTVEMIPQNPGTWL 1286
Cdd:cd13901     60 IELPKANKWVYIVIQNNSPLpHPIHLHGHDFYilAQGTGTFdddgtilnlnnppRRDVAMLPAGGYLVIAFKTDNPGAWL 139

                           90
                   ....*....|...
gi 1810777707 1287 LHCHVTDHIHAGM 1299
Cdd:cd13901    140 MHCHIAWHASGGL 152
CuRO_1_Abr2_like cd13850
The first cupredoxin domain of a group of fungal Laccases similar to Abr2 from Aspergillus ...
 340-454 4.30e-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: 4.30e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1810777707  340 EKPSWLG---FLGPIIKGEVGDSIVIHLKNFASRNYTLHPHGVtytkENEGAFYPDNTKGFEKRddAVKPGGQYTYTWDV 416
Cdd:cd13850     16 EREVILIngqFPGPPIILDEGDEVEILVTNNLPVNTTIHFHGI----LQRGTPWSDGVPGVTQW--PIQPGGSFTYRWKA 89

                           90       100       110
                   ....*....|....*....|....*....|....*....
gi 1810777707  417 TEDQGpakedadciTRVYHSHIdapRDVAS-GLVGPLII 454
Cdd:cd13850     90 EDQYG---------LYWYHSHY---RGYYMdGLYGPIYI 116
SufI COG2132
Multicopper oxidase with three cupredoxin domains (includes cell division protein FtsP and ...
 347-477 4.90e-08

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


Pssm-ID: 441735 [Multi-domain]  Cd Length: 423  Bit Score: 56.87  E-value: 4.90e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1810777707  347 FLGPIIKGEVGDSIVIHLKNFASRNYTLHPHGVTYTKENEGafYPdntkgfekrDDAVKPGGQYTYTWDVteDQGPAked 426
Cdd:COG2132     42 YPGPTIRVREGDRVRVRVTNRLPEPTTVHWHGLRVPNAMDG--VP---------GDPIAPGETFTYEFPV--PQPAG--- 105

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 1810777707  427 adciTRVYHSHIDA--PRDVASGLVGPLIIckkgamNKDNDKY--VDAEFILMFS 477
Cdd:COG2132    106 ----TYWYHPHTHGstAEQVYRGLAGALIV------EDPEEDLprYDRDIPLVLQ 150
CuRO_1_CumA_like cd13861
The first cupredoxin domain of CumA like multicopper oxidase; This multicopper oxidase (MCO) ...
 346-454 8.53e-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: 51.85  E-value: 8.53e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1810777707  346 GFLGPIIKGEVGDSIVIHLKNFASRNYTLHPHGVTYTKENEGAfyPDNTKgfekrdDAVKPGGQYTYTWdVTEDQGpake 425
Cdd:cd13861     28 QVPGPELRVRQGDTLRVRLTNRLPEPTTIHWHGLRLPNAMDGV--PGLTQ------PPVPPGESFTYEF-TPPDAG---- 94

                           90       100
                   ....*....|....*....|....*....
gi 1810777707  426 dadciTRVYHSHIDAPRDVASGLVGPLII 454
Cdd:cd13861     95 -----TYWYHPHVGSQEQLDRGLYGPLIV 118
CuRO_3_Fet3p cd13899
The third Cupredoxin domain of multicopper oxidase Fet3p; Fet3p catalyzes the ferroxidase ...
 1243-1307 8.58e-08

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


Pssm-ID: 259966 [Multi-domain]  Cd Length: 160  Bit Score: 53.03  E-value: 8.58e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1810777707 1243 HTTHFHGHSFN--YKQTGVY----------------RADVFDLFPGTFQTVEMIPQNPGTWLLHCHVTDHIHAGMEAIYT 1304
Cdd:cd13899     78 HPFHLHGHKFQvvQRSPDVAsddpnppinefpenpmRRDTVMVPPGGSVVIRFRADNPGVWFFHCHIEWHLEAGLAATFI 157


                   ...
gi 1810777707 1305 VLP 1307
Cdd:cd13899    158 EAP 160
CuRO_1_2dMco_1 cd13860
The first cupredoxin domain of bacteria two domain multicopper oxidase; This subfamily ...
 349-454 8.59e-08

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


Pssm-ID: 259929 [Multi-domain]  Cd Length: 119  Bit Score: 51.81  E-value: 8.59e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1810777707  349 GPIIKGEVGDSIVIHLKNFASRNYTLHPHGVTYTKENEGAfyPDNTKgfekrdDAVKPGGQYTYTWDVTEdQGpakedad 428
Cdd:cd13860     31 GPTIEVTEGDRVRILVTNELPEPTTVHWHGLPVPNGMDGV--PGITQ------PPIQPGETFTYEFTAKQ-AG------- 94

                           90       100
                   ....*....|....*....|....*.
gi 1810777707  429 ciTRVYHSHIDAPRDVASGLVGPLII 454
Cdd:cd13860     95 --TYMYHSHVDEAKQEDMGLYGAFIV 118
CuRO_1_LCC_like cd04206
Cupredoxin domain 1 of laccase-like multicopper oxidases; including laccase, CueO, spore coat ...
 1055-1149 1.33e-07

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: 51.52  E-value: 1.33e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1810777707 1055 QIQGPLIMSSIGDKINIVFKN-LASRPYSIHAHGVKTDSS-----VVAIT----NPGETKTYVWKISARSsserGelhcT 1124
Cdd:cd04206     27 QFPGPTIRVKEGDTVEVTVTNnLPNEPTSIHWHGLRQPGTndgdgVAGLTqcpiPPGESFTYRFTVDDQA----G----T 98

                           90       100
                   ....*....|....*....|....*
gi 1810777707 1125 AWaYHSTVDIikDTYSGLIGTLVVC 1149
Cdd:cd04206     99 FW-YHSHVGG--QRADGLYGPLIVE 120
CuRO_D2_2dMcoN_like cd04202
The second cupredoxin domain of bacterial two domain multicopper oxidase McoN and similar ...
 469-610 1.77e-07

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


Pssm-ID: 259865 [Multi-domain]  Cd Length: 138  Bit Score: 51.49  E-value: 1.77e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1810777707  469 DAEFILMFSvmdenlSWYLEDNirtycSEPSKVDKDDEDFqesnkmHSINGYMYGYLPNLTMCAEDKVKWHLFGMGNeaD 548
Cdd:cd04202      1 DRDYTLVLQ------EWFVDPG-----TTPMPPEGMDFNY------FTINGKSFPATPPLVVKEGDRVRIRLINLSM--D 61

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1810777707  549 IHSVYFHGQT---------LIERHHRV--DTINLFPATFIDALMIPRNPGEWLLSCQVNDHVE----GGMQALFKVE 610
Cdd:cd04202     62 HHPMHLHGHFflvtatdggPIPGSAPWpkDTLNVAPGERYDIEFVADNPGDWMFHCHKLHHAMngmgGGMMTLIGYE 138
CuRO_1_2DMCO_NIR_like cd11024
The cupredoxin domain 1 of a two-domain laccase related to nitrite reductase; The two-domain ...
 703-808 2.03e-07

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


Pssm-ID: 259910 [Multi-domain]  Cd Length: 119  Bit Score: 50.73  E-value: 2.03e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1810777707  703 GPVIKAEVEESIRVTFRNNASRPFSIQPHGVsyqksnegalYRTASRDTESPAshVSPGATFTYEWnVPEDVGptdqdpd 782
Cdd:cd11024     32 GPTLRATEGDLVRIHFINTGDHPHTIHFHGI----------HDAAMDGTGLGP--IMPGESFTYEF-VAEPAG------- 91

                           90       100
                   ....*....|....*....|....*..
gi 1810777707  783 clTWLYYSAVDSVRD-TNSGLVGPLLV 808
Cdd:cd11024     92 --THLYHCHVQPLKEhIAMGLYGAFIV 116
CuRO_1_CumA_like cd13861
The first cupredoxin domain of CumA like multicopper oxidase; This multicopper oxidase (MCO) ...
 700-808 3.34e-07

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


Pssm-ID: 259930 [Multi-domain]  Cd Length: 119  Bit Score: 50.31  E-value: 3.34e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1810777707  700 GLLGPVIKAEVEESIRVTFRNNASRPFSIQPHGVsyqksnegalyRTASR-D-----TESPashVSPGATFTYEWNVPeD 773
Cdd:cd13861     28 QVPGPELRVRQGDTLRVRLTNRLPEPTTIHWHGL-----------RLPNAmDgvpglTQPP---VPPGESFTYEFTPP-D 92

                           90       100       110
                   ....*....|....*....|....*....|....*
gi 1810777707  774 VGptdqdpdclTWLYYSAVDSVRDTNSGLVGPLLV 808
Cdd:cd13861     93 AG---------TYWYHPHVGSQEQLDRGLYGPLIV 118
CuRO_3_MCO_like_2 cd13908
The third cupredoxin domain of uncharacterized multicopper oxidase; Multicopper Oxidases (MCOs) ...
 1181-1303 4.13e-07

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


Pssm-ID: 259975 [Multi-domain]  Cd Length: 122  Bit Score: 50.14  E-value: 4.13e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1810777707 1181 DENIE-TYSVNPHLVDKENeeflesnkMHAINGKVFGNLHG-LTMHVGDEvswYLIAMGNEV-DIHTTHFHGHSFNY--- 1254
Cdd:cd13908      1 DETIDmTFEKRNAGDGGFN--------LWTINGKSYPDEDPpLVVQQGRR---YRLVFRNASdDAHPMHLHRHTFEVtri 69

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|.
gi 1810777707 1255 --KQTGVYRADVFDLFPGTFQTVEMIPQNPGTWLLHCHVTDHIHAGMEAIY 1303
Cdd:cd13908     70 dgKPTSGLRKDVVMLGGYQRVEVDFVADNPGLTLFHCHQQLHMDYGFMALF 120
PLN02191 PLN02191
L-ascorbate oxidase
 347-477 7.31e-07

L-ascorbate oxidase


Pssm-ID: 177843 [Multi-domain]  Cd Length: 574  Bit Score: 53.48  E-value: 7.31e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1810777707  347 FLGPIIKGEVGDSIVIHLKN-FASRNYTLHPHGVtytkENEGAFYPDNTKGFEKRddAVKPGGQYTYTWDVtEDQGpake 425
Cdd:PLN02191    51 FPGPTIDAVAGDTIVVHLTNkLTTEGLVIHWHGI----RQKGSPWADGAAGVTQC--AINPGETFTYKFTV-EKPG---- 119

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|..
gi 1810777707  426 dadciTRVYHSHIDAPRdvASGLVGPLIIckKGAMNKDNDKYVDAEFILMFS 477
Cdd:PLN02191   120 -----THFYHGHYGMQR--SAGLYGSLIV--DVAKGPKERLRYDGEFNLLLS 162
CuRO_3_Tv-LCC_like cd13903
The third cupredoxin domain of the fungal laccases similar to Tv-LCC from Trametes Versicolor; ...
 1234-1303 7.84e-07

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


Pssm-ID: 259970 [Multi-domain]  Cd Length: 147  Bit Score: 49.97  E-value: 7.84e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1810777707 1234 IAMGNEVDIHTTHFHGHSF-----------NYKQTgvYRADVFDL-FPGTFQTVEMIPQNPGTWLLHCHVTDHIHAGMEA 1301
Cdd:cd13903     64 IPGGAIGGPHPFHLHGHAFsvvrsagsntyNYVNP--VRRDVVSVgTPGDGVTIRFVTDNPGPWFLHCHIDWHLEAGLAV 141


                   ..
gi 1810777707 1302 IY 1303
Cdd:cd13903    142 VF 143
CuRO_1_MaLCC_like cd13854
The first cupredoxin domain of the fungal laccases similar to Ma-LCC from Melanocarpus ...
 349-454 1.26e-06

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: 48.78  E-value: 1.26e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1810777707  349 GPIIKGEVGDSIVIHLKNFASRNYT-LHPHGVT--YTKENEGAfyPDNTKGfekrddAVKPGGQYTYTWDVTEdQGpake 425
Cdd:cd13854     33 GPLIEANWGDTIEVTVINKLQDNGTsIHWHGIRqlNTNWQDGV--PGVTEC------PIAPGDTRTYRFRATQ-YG---- 99

                           90       100
                   ....*....|....*....|....*....
gi 1810777707  426 dadciTRVYHSHIDAprDVASGLVGPLII 454
Cdd:cd13854    100 -----TSWYHSHYSA--QYGDGVVGPIVI 121
CuRO_3_tcLLC2_insect_like cd13905
The third cupredoxin domain of the insect laccases similar to laccase 2 in Tribolium castaneum; ...
 1226-1305 1.56e-06

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: 49.60  E-value: 1.56e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1810777707 1226 GDEVSWYLIAMGNEVDI-HTTHFHGHSF---------NYKQTGVY--------RADVFDLFPGTFQ------TVeMIP-- 1279
Cdd:cd13905     52 NSVVEIVLINEGPGPGLsHPFHLHGHSFyvlgmgfpgYNSTTGEIlsqnwnnkLLDRGGLPGRNLVnpplkdTV-VVPng 130

                           90       100       110
                   ....*....|....*....|....*....|....*
gi 1810777707 1280 ---------QNPGTWLLHCHVTDHIHAGMEAIYTV 1305
Cdd:cd13905    131 gyvvirfraDNPGYWLLHCHIEFHLLEGMALVLKV 165
CuRO_1_AAO cd13845
The first cupredoxin domain of plant Ascorbate oxidase; Ascorbate oxidase catalyzes the ...
 346-454 1.58e-06

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: 48.60  E-value: 1.58e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1810777707  346 GFLGPIIKGEVGDSIVIHLKN-FASRNYTLHPHGVtytkENEGAFYPDNTKGFEKRddAVKPGGQYTYTWDVteDQgPAk 424
Cdd:cd13845     27 QFPGPTIRATAGDTIVVELENkLPTEGVAIHWHGI----RQRGTPWADGTASVSQC--PINPGETFTYQFVV--DR-PG- 96

                           90       100       110
                   ....*....|....*....|....*....|
gi 1810777707  425 edadciTRVYHSHIDAPRdvASGLVGPLII 454
Cdd:cd13845     97 ------TYFYHGHYGMQR--SAGLYGSLIV 118
CuRO_1_CuNIR_like cd04201
Cupredoxin domain 1 of Copper-containing nitrite reductase and two-domain laccase; ...
 1211-1308 1.74e-06

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: 48.26  E-value: 1.74e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1810777707 1211 NGKVFGNLhgLTMHVGDEVSWYLIAMGNEVDIHTTHFHGHSfnyKQTGVYRADVFDlfPGTFQTVEMIPQNPGTWLLHCH 1290
Cdd:cd04201     27 DGDIPGPM--LRVREGDTVELHFSNNPSSTMPHNIDFHAAT---GAGGGAGATFIA--PGETSTFSFKATQPGLYVYHCA 99

                           90       100
                   ....*....|....*....|.
gi 1810777707 1291 VTD---HIHAGMEAIYTVLPE 1308
Cdd:cd04201    100 VAPvpmHIANGMYGLILVEPK 120
CuRO_3_AAO cd13893
The third cupredoxin domain of plant Ascorbate oxidase; Ascorbate oxidase catalyzes the ...
 1238-1299 1.91e-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: 48.96  E-value: 1.91e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1810777707 1238 NEVDIHTTHFHGHSF---NYKqTGVYRA---------------DVFDLFPGTFQTVEMIPQNPGTWLLHCHVTDHIHAGM 1299
Cdd:cd13893     62 NASEQHPWHLHGHDFwvlGYG-LGGFDPaadpsslnlvnppmrNTVTIFPYGWTALRFKADNPGVWAFHCHIEWHFHMGM 140
PLN02191 PLN02191
L-ascorbate oxidase
 1241-1303 1.94e-06

L-ascorbate oxidase


Pssm-ID: 177843 [Multi-domain]  Cd Length: 574  Bit Score: 52.32  E-value: 1.94e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1810777707 1241 DIHTTHFHGH-------------------SFNYKQTGVYRADVfdLFPGTFQTVEMIPQNPGTWLLHCHVTDHIHAGMEA 1301
Cdd:PLN02191   465 EIHPWHLHGHdfwvlgygdgkfkpgidekTYNLKNPPLRNTAI--LYPYGWTAIRFVTDNPGVWFFHCHIEPHLHMGMGV 542


                   ..
gi 1810777707 1302 IY 1303
Cdd:PLN02191   543 VF 544
CuRO_1_Tv-LCC_like cd13856
The first cupredoxin domain of fungal laccases similar to Tv-LCC from Trametes versicolor; ...
 347-454 4.33e-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: 47.33  E-value: 4.33e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1810777707  347 FLGPIIKGEVGDSIVIHLKNFAS-----RNYTLHPHGVTYTKENegafYPDNTKGFEKRddAVKPGGQYTYTWDVTEDQG 421
Cdd:cd13856     28 FPGPLITANKGDTFRITVVNQLTdptmrRSTSIHWHGIFQHGTN----YADGPAFVTQC--PIAPNHSFTYDFTAGDQAG 101

                           90       100       110
                   ....*....|....*....|....*....|...
gi 1810777707  422 pakedadciTRVYHSHIDAprDVASGLVGPLII 454
Cdd:cd13856    102 ---------TFWYHSHLST--QYCDGLRGPLVI 123
ascorbase TIGR03388
L-ascorbate oxidase, plant type; Members of this protein family are the copper-containing ...
 347-486 4.38e-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: 50.91  E-value: 4.38e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1810777707  347 FLGPIIKGEVGDSIVIHLKN-FASRNYTLHPHGVtytkENEGAFYPDNTKGFEKRddAVKPGGQYTYTWdVTEDQGpake 425
Cdd:TIGR03388   29 FPGPTIRAQAGDTIVVELTNkLHTEGVVIHWHGI----RQIGTPWADGTAGVTQC--AINPGETFIYNF-VVDRPG---- 97

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1810777707  426 dadciTRVYHSHIDAPRdvASGLVGPLIIcKKGAMNKDNDKYvDAEFILMFSvmdenlSWY 486
Cdd:TIGR03388   98 -----TYFYHGHYGMQR--SAGLYGSLIV-DVPDGEKEPFHY-DGEFNLLLS------DWW 143
CuRO_1_2dMco_1 cd13860
The first cupredoxin domain of bacteria two domain multicopper oxidase; This subfamily ...
 1055-1148 4.93e-06

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


Pssm-ID: 259929 [Multi-domain]  Cd Length: 119  Bit Score: 46.81  E-value: 4.93e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1810777707 1055 QIQGPLIMSSIGDKINIVFKNLASRPYSIHAHGVKTDSS---VVAITN----PGETKTYVWKIsarsssergELHCTAWa 1127
Cdd:cd13860     28 SVPGPTIEVTEGDRVRILVTNELPEPTTVHWHGLPVPNGmdgVPGITQppiqPGETFTYEFTA---------KQAGTYM- 97

                           90       100
                   ....*....|....*....|.
gi 1810777707 1128 YHSTVDIIKDTYSGLIGTLVV 1148
Cdd:cd13860     98 YHSHVDEAKQEDMGLYGAFIV 118
CuRO_1_2DMCO_NIR_like cd11024
The cupredoxin domain 1 of a two-domain laccase related to nitrite reductase; The two-domain ...
 1226-1307 5.16e-06

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


Pssm-ID: 259910 [Multi-domain]  Cd Length: 119  Bit Score: 46.88  E-value: 5.16e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1810777707 1226 GDEVSWYLIAMGNevDIHTTHFHGHSFNYKQTGVYRadvfDLFPGTFQTVEMIPQNPGTWLLHCHV---TDHIHAGMEAI 1302
Cdd:cd11024     40 GDLVRIHFINTGD--HPHTIHFHGIHDAAMDGTGLG----PIMPGESFTYEFVAEPAGTHLYHCHVqplKEHIAMGLYGA 113


                   ....*
gi 1810777707 1303 YTVLP 1307
Cdd:cd11024    114 FIVDP 118
CuRO_1_2DMCO_NIR_like cd11024
The cupredoxin domain 1 of a two-domain laccase related to nitrite reductase; The two-domain ...
 1055-1151 7.74e-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: 46.49  E-value: 7.74e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1810777707 1055 QIQGPLIMSSIGDKINIVFKNLASRPYSIHAHGV---KTDSSVVAITNPGETKTYVWKisarsSSERGelhctAWAYHST 1131
Cdd:cd11024     29 TVPGPTLRATEGDLVRIHFINTGDHPHTIHFHGIhdaAMDGTGLGPIMPGESFTYEFV-----AEPAG-----THLYHCH 98

                           90       100
                   ....*....|....*....|.
gi 1810777707 1132 VDIIKD-TYSGLIGTLVVCPR 1151
Cdd:cd11024     99 VQPLKEhIAMGLYGAFIVDPK 119
CuRO_1_Diphenol_Ox cd13857
The first cupredoxin domain of fungal laccase, diphenol oxidase; Diphenol oxidase belongs to ...
 1055-1148 1.06e-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: 46.10  E-value: 1.06e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1810777707 1055 QIQGPLIMSSIGDKINIVFKNLASRPYSIHAHGVKTDSS-----VVAITN----PGETKTYVWKISARSSsergelhcTA 1125
Cdd:cd13857     27 QFPGPLIEANQGDRIVVHVTNELDEPTSIHWHGLFQNGTnwmdgTAGITQcpipPGGSFTYNFTVDGQYG--------TY 98

                           90       100
                   ....*....|....*....|....
gi 1810777707 1126 WaYHSTVDIikdTYS-GLIGTLVV 1148
Cdd:cd13857     99 W-YHSHYST---QYAdGLVGPLIV 118
CuRO_D1_2dMcoN_like cd13859
The first cupredoxin domain of bacterial two domain multicopper oxidase McoN and similar ...
 1055-1148 1.13e-05

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


Pssm-ID: 259928 [Multi-domain]  Cd Length: 122  Bit Score: 45.93  E-value: 1.13e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1810777707 1055 QIQGPLIMSSIGDKINIVFKNLASRPYSIHAHGV-KTDS----SVVAITN----PGETKTYVWKisarssserGELHCTA 1125
Cdd:cd13859     28 QVPGPLIHVKEGDDLVVHVTNNTTLPHTIHWHGVlQMGSwkmdGVPGVTQpaiePGESFTYKFK---------AERPGTL 98

                           90       100
                   ....*....|....*....|....
gi 1810777707 1126 WaYHSTVDIIK-DTYSGLIGTLVV 1148
Cdd:cd13859     99 W-YHCHVNVNEhVGMRGMWGPLIV 121
CuRO_1_Fet3p cd13851
The first Cupredoxin domain of multicopper oxidase Fet3P; Fet3p catalyzes the ferroxidase ...
 350-454 1.32e-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: 45.72  E-value: 1.32e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1810777707  350 PIIKGEVGDSIVIHLKN-FASRNYTLHPHGV--TYTKENEGAFY----PdntkgfekrddaVKPGGQYTYTWDVTEDQGp 422
Cdd:cd13851     32 PPIEVNKGDTVVIHATNsLGDQPTSLHFHGLfqNGTNYMDGPVGvtqcP------------IPPGQSFTYEFTVDTQVG- 98

                           90       100       110
                   ....*....|....*....|....*....|..
gi 1810777707  423 akedadciTRVYHSHIDAprDVASGLVGPLII 454
Cdd:cd13851     99 --------TYWYHSHDGG--QYPDGLRGPFII 120
Cu-oxidase_2 pfam07731
Multicopper oxidase; This entry contains many divergent copper oxidase-like domains that are ...
 507-611 1.88e-05

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: 45.89  E-value: 1.88e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1810777707  507 DFQESNKMHSINGYMYGYLPN-LTMCAEDKVKWHLFGMGNeaDIHSVYFHGQT--LIERHH-----------------RV 566
Cdd:pfam07731   14 SGNFRRNDWAINGLLFPPNTNvITLPYGTVVEWVLQNTTT--GVHPFHLHGHSfqVLGRGGgpwpeedpktynlvdpvRR 91

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*
gi 1810777707  567 DTINLFPATFIDALMIPRNPGEWLLSCQVNDHVEGGMQALFKVED 611
Cdd:pfam07731   92 DTVQVPPGGWVAIRFRADNPGVWLFHCHILWHLDQGMMGQFVVRP 136
CuRO_1_CuNIR cd11020
Cupredoxin domain 1 of Copper-containing nitrite reductase; Copper-containing nitrite ...
 1055-1151 1.99e-05

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: 45.28  E-value: 1.99e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1810777707 1055 QIQGPLIMSSIGDKINIVFKNLASR--PYSIHAHGVKTDSSVVAIT-NPGETKTYVWKIsarsssergeLHCTAWAYH-S 1130
Cdd:cd11020     29 QVPGPVIRVREGDTVELTLTNPGTNtmPHSIDFHAATGPGGGEFTTiAPGETKTFSFKA----------LYPGVFMYHcA 98

                           90       100
                   ....*....|....*....|.
gi 1810777707 1131 TVDIIKDTYSGLIGTLVVCPR 1151
Cdd:cd11020     99 TAPVLMHIANGMYGAIIVEPK 119
CuRO_1_LCC_plant cd13849
The first cupredoxin domain of plant laccases; Laccase is a blue multicopper oxidase (MCO) ...
 347-454 2.71e-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: 44.94  E-value: 2.71e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1810777707  347 FLGPIIKGEVGDSIVIHLKNFASRNYTLHPHGVtYTKENEGAfypDNTKGFEKRddAVKPGGQYTYTWDVTEDQGpaked 426
Cdd:cd13849     26 FPGPTIRVHEGDTVVVNVTNRSPYNITIHWHGI-RQLRSGWA---DGPAYITQC--PIQPGQSYTYRFTVTGQEG----- 94

                           90       100
                   ....*....|....*....|....*...
gi 1810777707  427 adciTRVYHSHIDAPRdvaSGLVGPLII 454
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, ...
 347-454 3.90e-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: 44.49  E-value: 3.90e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1810777707  347 FLGPIIKGEVGDSIVIHLKNFASRNYTLHPHGVTYTKENEGAfyPDNTkgfekrddaVKPGGQYTYTWDVteDQGPAked 426
Cdd:cd04232     29 YLGPTIRVKKGDTVRINVTNNLDEETTVHWHGLHVPGEMDGG--PHQP---------IAPGQTWSPTFTI--DQPAA--- 92

                           90       100       110
                   ....*....|....*....|....*....|
gi 1810777707  427 adciTRVYHSHIDA--PRDVASGLVGPLII 454
Cdd:cd04232     93 ----TLWYHPHTHGktAEQVYRGLAGLFII 118
ascorbase TIGR03388
L-ascorbate oxidase, plant type; Members of this protein family are the copper-containing ...
 1237-1303 4.69e-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: 47.82  E-value: 4.69e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1810777707 1237 GNEVDIHTTHFHGHSF---NYKQtGVYRADV----FDL-----------FPGTFQTVEMIPQNPGTWLLHCHVTDHIHAG 1298
Cdd:TIGR03388  438 GNNSETHPWHLHGHDFwvlGYGE-GKFRPGVdeksYNLknpplrntvviFPYGWTALRFVADNPGVWAFHCHIEPHLHMG 516


                   ....*
gi 1810777707 1299 MEAIY 1303
Cdd:TIGR03388  517 MGVVF 521
Cu-oxidase_3 pfam07732
Multicopper oxidase; This entry contains many divergent copper oxidase-like domains that are ...
 701-808 5.84e-05

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: 43.77  E-value: 5.84e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1810777707  701 LLGPVIKAEVEESIRVTFRNNASRPFSIQPHGVsYQKSN---EGALYrtasrdteSPASHVSPGATFTYEWNVPEDVGpt 777
Cdd:pfam07732   24 FPGPTIRVREGDTVVVNVTNNLDEPTSIHWHGL-QQRGTpwmDGVPG--------VTQCPIPPGQSFTYRFQVKQQAG-- 92

                           90       100       110
                   ....*....|....*....|....*....|.
gi 1810777707  778 dqdpdclTWLYYSAVDSVRdtNSGLVGPLLV 808
Cdd:pfam07732   93 -------TYWYHSHTSGQQ--AAGLAGAIII 114
CuRO_1_MaLCC_like cd13854
The first cupredoxin domain of the fungal laccases similar to Ma-LCC from Melanocarpus ...
 1055-1148 7.01e-05

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: 43.77  E-value: 7.01e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1810777707 1055 QIQGPLIMSSIGDKINI-VFKNLASRPYSIHAHGVK-----TDSSVVAITN----PGETKTYVWkisarssseRGELHCT 1124
Cdd:cd13854     30 QYPGPLIEANWGDTIEVtVINKLQDNGTSIHWHGIRqlntnWQDGVPGVTEcpiaPGDTRTYRF---------RATQYGT 100

                           90       100
                   ....*....|....*....|....*
gi 1810777707 1125 AWaYHSTVDIikdTYS-GLIGTLVV 1148
Cdd:cd13854    101 SW-YHSHYSA---QYGdGVVGPIVI 121
CuRO_1_McoC_like cd13855
The first cupredoxin domain of a multicopper oxidase McoC and similar proteins; This family ...
 1055-1148 7.22e-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: 43.62  E-value: 7.22e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1810777707 1055 QIQGPLIMSSIGDKINIVFKNLASRPYSIHAHGV----KTDSSVVAITNPGETKTYVWKISARSSSergelhcTAWAY-H 1129
Cdd:cd13855     29 SVPGPLIEVFEGDTVEITFRNRLPEPTTVHWHGLpvppDQDGNPHDPVAPGNDRVYRFTLPQDSAG-------TYWYHpH 101

                           90
                   ....*....|....*....
gi 1810777707 1130 STVDIIKDTYSGLIGTLVV 1148
Cdd:cd13855    102 PHGHTAEQVYRGLAGAFVV 120
CuRO_1_2dMco_1 cd13860
The first cupredoxin domain of bacteria two domain multicopper oxidase; This subfamily ...
 703-808 7.26e-05

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


Pssm-ID: 259929 [Multi-domain]  Cd Length: 119  Bit Score: 43.72  E-value: 7.26e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1810777707  703 GPVIKAEVEESIRVTFRNNASRPFSIQPHGVSYQKSNEGAlyrtasrdTESPASHVSPGATFTYEWNVpEDVGptdqdpd 782
Cdd:cd13860     31 GPTIEVTEGDRVRILVTNELPEPTTVHWHGLPVPNGMDGV--------PGITQPPIQPGETFTYEFTA-KQAG------- 94

                           90       100
                   ....*....|....*....|....*.
gi 1810777707  783 clTWLYYSAVDSVRDTNSGLVGPLLV 808
Cdd:cd13860     95 --TYMYHSHVDEAKQEDMGLYGAFIV 118
CuRO_3_LCC_plant cd13897
The third cupredoxin domain of the plant laccases; Laccase is a blue multicopper oxidase (MCO) ...
 1241-1305 9.56e-05

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


Pssm-ID: 259964 [Multi-domain]  Cd Length: 139  Bit Score: 43.79  E-value: 9.56e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1810777707 1241 DIHTTHFHGHSF--------NYKQTGVYRAdvFDLF-PGTFQTVeMIPQ-----------NPGTWLLHCHVTDHIHAGME 1300
Cdd:cd13897     55 ENHPMHLHGFDFyvvgrgfgNFDPSTDPAT--FNLVdPPLRNTV-GVPRggwaairfvadNPGVWFMHCHFERHTSWGMA 131


                   ....*
gi 1810777707 1301 AIYTV 1305
Cdd:cd13897    132 TVFIV 136
Cu-oxidase pfam00394
Multicopper oxidase; Many of the proteins in this family contain multiple similar copies of ...
 1171-1301 1.25e-04

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


Pssm-ID: 395317 [Multi-domain]  Cd Length: 146  Bit Score: 43.46  E-value: 1.25e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1810777707 1171 VFDENESWYlDENIETYSVNPHLVDKENEEF-LESNKmHAINGKVFGNLHGLTMHVGDEVSWYLIaMGNEVDIHTTHFHG 1249
Cdd:pfam00394    3 YVITLSDWY-HKDAKDLEKELLASGKAPTDFpPVPDA-VLINGKDGASLATLTVTPGKTYRLRII-NVALDDSLNFSIEG 79

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1810777707 1250 HSFNYKQ-TGVY----RADVFDLFPGTFQTVeMI--PQNPGTWLLHCHVT-DHIHAGMEA 1301
Cdd:pfam00394   80 HKMTVVEvDGVYvnpfTVDSLDIFPGQRYSV-LVtaNQDPGNYWIVASPNiPAFDNGTAA 138
CuRO_3_Tth-MCO_like cd13900
The third cupredoxin domain of the bacterial laccases similar to Tth-MCO from Thermus ...
 1210-1299 1.55e-04

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


Pssm-ID: 259967 [Multi-domain]  Cd Length: 123  Bit Score: 42.62  E-value: 1.55e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1810777707 1210 INGKVFG-NLHGLTMHVGDEVSWYLIAMGNEvdIHTTHFHGHSF-----NYK--QTGVYRaDVFDLFPGTFQTVEMIPQN 1281
Cdd:cd13900     22 INGKPFDpDRPDRTVRLGTVEEWTLINTSGE--DHPFHIHVNPFqvvsiNGKpgLPPVWR-DTVNVPAGGSVTIRTRFRD 98

                           90
                   ....*....|....*....
gi 1810777707 1282 P-GTWLLHCHVTDHIHAGM 1299
Cdd:cd13900     99 FtGEFVLHCHILDHEDQGM 117
CuRO_1_Diphenol_Ox cd13857
The first cupredoxin domain of fungal laccase, diphenol oxidase; Diphenol oxidase belongs to ...
 703-808 2.44e-04

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: 42.25  E-value: 2.44e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1810777707  703 GPVIKAEVEESIRVTFRNNASRPFSIQPHGVsYQKSnegalyrTASRD-----TESPashVSPGATFTYEWNVPEDVGpt 777
Cdd:cd13857     30 GPLIEANQGDRIVVHVTNELDEPTSIHWHGL-FQNG-------TNWMDgtagiTQCP---IPPGGSFTYNFTVDGQYG-- 96

                           90       100       110
                   ....*....|....*....|....*....|..
gi 1810777707  778 dqdpdclTWLYYSAVDSvrdTNS-GLVGPLLV 808
Cdd:cd13857     97 -------TYWYHSHYST---QYAdGLVGPLIV 118
CuRO_1_Tv-LCC_like cd13856
The first cupredoxin domain of fungal laccases similar to Tv-LCC from Trametes versicolor; ...
 703-808 2.62e-04

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: 42.32  E-value: 2.62e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1810777707  703 GPVIKAEVEESIRVTFRNNAS-----RPFSIQPHGVsYQKsnegalyRTASRD-----TESPashVSPGATFTYEWNVPE 772
Cdd:cd13856     30 GPLITANKGDTFRITVVNQLTdptmrRSTSIHWHGI-FQH-------GTNYADgpafvTQCP---IAPNHSFTYDFTAGD 98

                           90       100       110
                   ....*....|....*....|....*....|....*.
gi 1810777707  773 DVGptdqdpdclTWLYYSAVDSvrDTNSGLVGPLLV 808
Cdd:cd13856     99 QAG---------TFWYHSHLST--QYCDGLRGPLVI 123
Cupredoxin cd00920
Cupredoxin superfamily; Cupredoxins contain type I copper centers and are involved in ...
 1211-1299 4.57e-04

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: 41.06  E-value: 4.57e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1810777707 1211 NGKVFGNLHgLTMHVGDEVSWYLI---AMGNEVDIHTTHFHGHSFNYKQTGVYRADVFdLFPGTFQTVEMIPQNPGTWLL 1287
Cdd:cd00920     16 GVLLFGPPV-LVVPVGDTVRVQFVnklGENHSVTIAGFGVPVVAMAGGANPGLVNTLV-IGPGESAEVTFTTDQAGVYWF 93

                           90
                   ....*....|..
gi 1810777707 1288 HCHVTDHIHAGM 1299
Cdd:cd00920     94 YCTIPGHNHAGM 105
ascorbOXfungal TIGR03390
L-ascorbate oxidase, fungal type; This model describes a family of fungal ascorbate oxidases, ...
 1240-1310 4.75e-04

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


Pssm-ID: 132431 [Multi-domain]  Cd Length: 538  Bit Score: 44.45  E-value: 4.75e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1810777707 1240 VDIHTTHFHGHSF--------------------NYK----QTGV---YRADVFDLFPGTFQTVEMIPQNPGTWLLHCHVT 1292
Cdd:TIGR03390  439 VDTHPFHAHGRHFydigggdgeynataneakleNYTpvlrDTTMlyrYAVKVVPGAPAGWRAWRIRVTNPGVWMMHCHIL 518

                           90
                   ....*....|....*...
gi 1810777707 1293 DHIHAGMEAIYTVLPEED 1310
Cdd:TIGR03390  519 QHMVMGMQTVWVFGDAED 536
CuRO_1_McoC_like cd13855
The first cupredoxin domain of a multicopper oxidase McoC and similar proteins; This family ...
 349-454 6.04e-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: 40.92  E-value: 6.04e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1810777707  349 GPIIKGEVGDSIVIHLKNFASRNYTLHPHGVTYTKENEGafYPdntkgfekrDDAVKPGGQYTYTWDVTEDQGPakedad 428
Cdd:cd13855     32 GPLIEVFEGDTVEITFRNRLPEPTTVHWHGLPVPPDQDG--NP---------HDPVAPGNDRVYRFTLPQDSAG------ 94

                           90       100
                   ....*....|....*....|....*...
gi 1810777707  429 ciTRVY--HSHIDAPRDVASGLVGPLII 454
Cdd:cd13855     95 --TYWYhpHPHGHTAEQVYRGLAGAFVV 120
CuRO_3_MCO_like_4 cd13910
The third cupredoxin domain of uncharacterized multicopper oxidase; Multicopper Oxidases (MCOs) ...
 1204-1299 1.26e-03

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


Pssm-ID: 259977 [Multi-domain]  Cd Length: 166  Bit Score: 41.13  E-value: 1.26e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1810777707 1204 SNKMHAINGKVFGNLHGLTMHVGDEVSWyliamgneVDI---------HTTHFHGHSF-------NYKQTGVYRADVFDL 1267
Cdd:cd13910     43 AEEVAAGNGLSTFDGNQLVITVDDIDKV--------VDLvinnlddgdHPFHLHGHKFwvlgsgdGRYGGGGYTAPDGTS 114

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*..
gi 1810777707 1268 FPGTFQ----TVEmIPQ-----------NPGTWLLHCHVTDHIHAGM 1299
Cdd:cd13910    115 LNTTNPlrrdTVS-VPGfgwavlrfvadNPGLWAFHCHILWHMAAGM 160
CuRO_3_Abr2_like cd13898
The third cupredoxin domain of a group of fungal Laccases similar to Abr2 from Aspergillus ...
 1243-1302 1.75e-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: 40.70  E-value: 1.75e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1810777707 1243 HTTHFHGH----------SFNYK---------------QTGVYRaDVFDLFPGTFQTVEMI----PQNPGTWLLHCHVTD 1293
Cdd:cd13898     73 HPIHKHGNkafvigtgtgPFNWSsvaeaaeaapenfnlVNPPLR-DTFTTPPSTEGPSWLViryhVVNPGAWLLHCHIQS 151


                   ....*....
gi 1810777707 1294 HIHAGMEAI 1302
Cdd:cd13898    152 HLAGGMAVV 160
CuRO_1_Tth-MCO_like cd13853
The first cupredoxin domain of the bacterial laccases similar to Tth-MCO from Thermus ...
 347-454 1.94e-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: 39.93  E-value: 1.94e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1810777707  347 FLGPIIKGEVGDSIVIHLKN----------------FASRNYT-LHPHGVTYTKENEGafypdntkgfekrDD---AVKP 406
Cdd:cd13853     29 IPGPTLRVRPGDTLRITLKNdlppegaaneapapntPHCPNTTnLHFHGLHVSPTGNS-------------DNvflTIAP 95

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|.
gi 1810777707  407 GGQYTYTWDVTEDQGPAkedadciTRVYHSHID---APrDVASGLVGPLII 454
Cdd:cd13853     96 GESFTYEYDIPADHPPG-------TYWYHPHLHgstAL-QVAGGMAGALVV 138
CuRO_D1_2dMcoN_like cd13859
The first cupredoxin domain of bacterial two domain multicopper oxidase McoN and similar ...
 1204-1303 2.11e-03

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: 39.38  E-value: 2.11e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1810777707 1204 SNKMHAINGKVFGNLhgltMHV--GDEVswyLIAMGNEVDI-HTTHFHGhsfnYKQTGVYRADVFD------LFPGTFQT 1274
Cdd:cd13859     19 DFKTFAFNGQVPGPL----IHVkeGDDL---VVHVTNNTTLpHTIHWHG----VLQMGSWKMDGVPgvtqpaIEPGESFT 87

                           90       100
                   ....*....|....*....|....*....
gi 1810777707 1275 VEMIPQNPGTWLLHCHVTDHIHAGMEAIY 1303
Cdd:cd13859     88 YKFKAERPGTLWYHCHVNVNEHVGMRGMW 116
CuRO_3_McoC_like cd13902
The third cupredoxin domain of a multicopper oxidase McoC and similar proteins; This family ...
 507-609 2.76e-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: 39.31  E-value: 2.76e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1810777707  507 DFQE--SNKMHS----INGYMYGylpnltMCAEDKVK-------WHLFgmgNEADI-HSVYFHGQ--TLIERHHRV---- 566
Cdd:cd13902      7 VFSEgmSMGAGGmmflINGKTFD------MNRIDFVAkvgevevWEVT---NTSHMdHPFHLHGTqfQVLEIDGNPqkpe 77

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*...
gi 1810777707  567 -----DTINLFPATFIDALMIPRNPGEWLLSCQVNDHVEGGMQALFKV 609
Cdd:cd13902     78 yrawkDTVNLPPGEAVRIATRQDDPGMWMYHCHILEHEDAGMMGMLHV 125
CuRO_3_MCO_like_3 cd13909
The third cupredoxin domain of uncharacterized multicopper oxidase; Multicopper Oxidases (MCOs) ...
 550-609 2.95e-03

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


Pssm-ID: 259976 [Multi-domain]  Cd Length: 137  Bit Score: 39.42  E-value: 2.95e-03
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1810777707  550 HSVYFHGQtlierHHRVDTINLFPATFIDALMIPR-----------NPGEWLLSCQVNDHVEGGMQALFKV 609
Cdd:cd13909     71 HGMHLHGH-----HFRAILPNGALGPWRDTLLMDRgetreiafvadNPGDWLLHCHMLEHAAAGMMSWFRV 136
Cu-oxidase_3 pfam07732
Multicopper oxidase; This entry contains many divergent copper oxidase-like domains that are ...
 1055-1130 4.34e-03

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


Pssm-ID: 462247 [Multi-domain]  Cd Length: 119  Bit Score: 38.38  E-value: 4.34e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1810777707 1055 QIQGPLIMSSIGDKINIVFKNLASRPYSIHAHGVKTDSS-----VVAITN----PGETKTYVWKISARSssergelhCTA 1125
Cdd:pfam07732   23 QFPGPTIRVREGDTVVVNVTNNLDEPTSIHWHGLQQRGTpwmdgVPGVTQcpipPGQSFTYRFQVKQQA--------GTY 94


                   ....*
gi 1810777707 1126 WaYHS 1130
Cdd:pfam07732   95 W-YHS 98
CuRO_1_McoP_like cd13852
The first cupredoxin domain of multicopper oxidase McoP and similar proteins; This family ...
 346-454 4.41e-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: 38.42  E-value: 4.41e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1810777707  346 GFLGPIIKGEVGDSIVIHLKNFASRNYTLHPHGVTYTKENEGafYPDNtkgfekrddAVKPGGQYTYTWDVTEDQGpake 425
Cdd:cd13852     21 SYLGPILRLRKGQKVRITFKNNLPEPTIIHWHGLHVPAAMDG--HPRY---------AIDPGETYVYEFEVLNRAG---- 85

                           90       100       110
                   ....*....|....*....|....*....|.
gi 1810777707  426 dadciTRVYHSHID--APRDVASGLVGPLII 454
Cdd:cd13852     86 -----TYWYHPHPHglTAKQVYRGLAGLFLV 111
CuRO_3_AAO_like_2 cd13895
The third cupredoxin domain of Ascorbate oxidase homologs; This family includes fungal ...
 1237-1302 5.42e-03

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


Pssm-ID: 259962 [Multi-domain]  Cd Length: 188  Bit Score: 39.61  E-value: 5.42e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1810777707 1237 GNEVDIHTTHFHGHSF--------NYKQTGVYRA-----------DVFDLFPGTFQTVEMIP-------------QNPGT 1284
Cdd:cd13895     87 TGGLDAHPWHAHGAHYydlgsglgTYSATALANEeklrgynpirrDTTMLYRYGGKGYYPPPgtgsgwrawrlrvDDPGV 166

                           90
                   ....*....|....*...
gi 1810777707 1285 WLLHCHVTDHIHAGMEAI 1302
Cdd:cd13895    167 WMLHCHILQHMIMGMQTV 184
SufI COG2132
Multicopper oxidase with three cupredoxin domains (includes cell division protein FtsP and ...
 701-895 6.92e-03

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


Pssm-ID: 441735 [Multi-domain]  Cd Length: 423  Bit Score: 40.30  E-value: 6.92e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1810777707  701 LLGPVIKAEVEESIRVTFRNNASRPFSIQPHG--VSYQksNEGalyrtasrdteSPASHVSPGATFTYEWNVPEDVGptd 778
Cdd:COG2132     42 YPGPTIRVREGDRVRVRVTNRLPEPTTVHWHGlrVPNA--MDG-----------VPGDPIAPGETFTYEFPVPQPAG--- 105

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1810777707  779 qdpdclTWLYYSAVD--SVRDTNSGLVGPLLVCRRGALLPsakqkSVTREFFLLatvfdenlswyLDDnilmFALN-PNE 855
Cdd:COG2132    106 ------TYWYHPHTHgsTAEQVYRGLAGALIVEDPEEDLP-----RYDRDIPLV-----------LQD----WRLDdDGQ 159

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|..
gi 1810777707  856 IDKDNEDFQESN--KMHSINGYMygnQPGLEMCKGEVISWHL 895
Cdd:COG2132    160 LLYPMDAAMGGRlgDTLLVNGRP---NPTLEVRPGERVRLRL 198
CuRO_D1_2dMcoN_like cd13859
The first cupredoxin domain of bacterial two domain multicopper oxidase McoN and similar ...
 703-775 7.54e-03

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: 37.84  E-value: 7.54e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1810777707  703 GPVIKAEVEESIRVTFRNNASRPFSIQPHGVsYQKsneGALYRTASRDTESPAshVSPGATFTYEW-------------- 768
Cdd:cd13859     31 GPLIHVKEGDDLVVHVTNNTTLPHTIHWHGV-LQM---GSWKMDGVPGVTQPA--IEPGESFTYKFkaerpgtlwyhchv 104


                   ....*..
gi 1810777707  769 NVPEDVG 775
Cdd:cd13859    105 NVNEHVG 111
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

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