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Conserved domains on  [gi|301615846|ref|XP_002937375|]
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ceruloplasmin [Xenopus tropicalis]

Protein Classification

multicopper oxidase( domain architecture ID 10136057)

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

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
CuRO_3_ceruloplasmin cd04224
The third cupredoxin domain of Ceruloplasmin; Ceruloplasmin is a multicopper oxidase essential ...
 370-571 1.64e-126

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: 383.36  E-value: 1.64e-126
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 301615846  370 GRERRYFIAAEEAMWNYAPTDTNQFTGQKIDHPDTESAIFFQRNEVRIGGTYTKAVYVEYTDATFTTRKQRSKDEEHLGI 449
Cdd:cd04224     1 GKVRHYFIAAEEIMWDYAPSGKNLFTGQNLTAPGSDSEVFFQRNETRIGGTYWKVRYVEYTDATFTTRKHRSKEEEHLGI 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 301615846  450 LGPVMIAQVGDSMKVTFKNKASRPYSIQAHGVSYSKNMEGASYRtgnltNDDPSPGSHVAPGDTFTYEWEVSSAVGSTNQ 529
Cdd:cd04224    81 LGPVIRAEVGDTIKVTFRNKASRPFSIQPHGVFYEKNYEGAMYR-----DGDPSPGSHVSPGETFTYEWTVPEGVGPTNQ 155

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|..
gi 301615846  530 NLNCLVWLYFSSVDAIKDTNSGLVGPLLICKSIDANNHQRGI 571
Cdd:cd04224   156 DPPCLTYLYFSAVDPVRDTNSGLVGPLLVCKKGSLNANGRQK 197
CuRO_1_ceruloplasmin cd04222
The first cupredoxin domain of Ceruloplasmin; Ceruloplasmin is a multicopper oxidase essential ...
 22-203 3.13e-122

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


:

Pssm-ID: 259884 [Multi-domain]  Cd Length: 183  Bit Score: 371.37  E-value: 3.13e-122
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 301615846   22 RIFYIGIRETNWDYAPSGNNIISGTSIKDDEDAQTFLVGGPDRIGRVYKKAVYLQYSDDSYSKEIKKPQWLGHLGPILKA 101
Cdd:cd04222     1 REYYIGIRETQWDYAPSGKNLITNQTFDDDEHASVFLKRGPDRIGRVYKKAVYLQYTDDTYRTEIEKPVWLGFLGPILKA 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 301615846  102 EIGDIIIVHLKNFASRPYSIHPHGVQYTKENEGALYPDNASS-GHKDDAIEPGQSYTYRWEAVSEQGPTVQDEDCITRIY 180
Cdd:cd04222    81 EVGDVIVVHLKNFASRPYSLHPHGVFYNKENEGALYPDNTSGfEKADDAVPPGGSYTYTWTVPEEQAPTKADANCLTRIY 160

                         170       180
                  ....*....|....*....|...
gi 301615846  181 HSHIDGPKDVSSGLIGPLIICKK 203
Cdd:cd04222   161 HSHIDAPKDIASGLIGPLIICKK 183
CuRO_5_ceruloplasmin cd04225
The fifth cupredoxin domain of Ceruloplasmin; Ceruloplasmin is a multicopper oxidase essential ...
 727-897 4.59e-113

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: 346.76  E-value: 4.59e-113
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 301615846  727 NTYYIAAEEIEWDYSPNRTWEHERHIHHGESPGDAFLNKGEKFIGSTYKKAVYRQYTDRTFTKRKERNEEEKHLGILGPL 806
Cdd:cd04225     1 RTYYIAAEEVEWDYSPQRTWEQELHNTHEESPGNAFLNKGDKFIGSKYKKVVYREYTDDTFSVPKERTAEEEHLGILGPL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 301615846  807 LIARTHEKVKIVFKNMASRPYSIYAHGVKTDGP-VVQTEPGQTQTYIWKIPERSGPGYhEDVNCVTWAYYSTVDQVKDTY 885
Cdd:cd04225    81 IHAEVGEKVKIVFKNMASRPYSIHAHGVKTDSSwVAPTEPGETQTYTWKIPERSGPGV-EDSNCISWAYYSTVDQIKDLY 159

                         170
                  ....*....|..
gi 301615846  886 SGLIGPLVICKR 897
Cdd:cd04225   160 SGLIGPLVICRR 171
CuRO_4_ceruloplasmin cd11022
The fourth cupredoxin domain of Ceruloplasmin; Ceruloplasmin is a multicopper oxidase ...
 572-715 4.85e-96

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


:

Pssm-ID: 259908 [Multi-domain]  Cd Length: 144  Bit Score: 300.55  E-value: 4.85e-96
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 301615846  572 AHNYFLLPTVFDENESWYLDENIQQFTGTPANVNKEDPDFQESNMMHSINGYMYGNQPGLDMCAGDTVLWHLMGLGNEVD 651
Cdd:cd11022     1 DKEFFLLFTVFDENESWYLDENIQQFTLDPRSVDKEDEDFQESNKMHSINGYMYGNQPGLDMCKGDTVSWHLFGLGTETD 80

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 301615846  652 MHGIHFSGNTIVTHYTRADTASLFPHISYSVMMNPDNEGVFNVECMTTDHYTAGMRQHYRVKSC 715
Cdd:cd11022    81 VHGIYFSGNTFLLQGTRRDTANLFPHTSVTAIMQPDNEGTFEVNCQTTDHYSAGMRQIYTVSQC 144
CuRO_2_ceruloplasmin cd11021
The second cupredoxin domain of Ceruloplasmin; Ceruloplasmin is a multicopper oxidase ...
 214-354 2.57e-94

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: 295.92  E-value: 2.57e-94
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 301615846  214 YKEFVLMFSVIDENLSWYLDENINTFCTEPSSVDKNDTDFQESNKMHSINGYMFGNLPGLSMCEGEHIHWYLFGMGNEAD 293
Cdd:cd11021     1 DREFVLMFSVVDENLSWYLDENIKTYCSEPAKVDKDDEDFQESNKMHSINGYTFGNLPGLSMCAGDRVKWHLFGMGNEVD 80

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 301615846  294 IHSAYFHGQVLTFQMYRVDTLSLFPATMIEGHMVTKNPGKWLLTCQVNDHLAGGMQAIYEV 354
Cdd:cd11021    81 IHSAFFHGQTLTDRGHRTDTINLFPATFVTAEMVAQNPGKWLLSCQVNDHLKAGMQAFYEV 141
Cupredoxin super family cl19115
Cupredoxin superfamily; Cupredoxins contain type I copper centers and are involved in ...
 908-1052 1.90e-92

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


The actual alignment was detected with superfamily member cd11012:

Pssm-ID: 473140 [Multi-domain]  Cd Length: 145  Bit Score: 291.00  E-value: 1.90e-92
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 301615846  908 PKRFALLFLIFDENESWYLDENIKTYSLHPDQVQKEDEDFIESNKMHGINGKLYANLEGLTMHVGDKIYWHLIGLGNEAD 987
Cdd:cd11012     1 KLEFALLFLVFDENESWYLDENIKTYSDHPEKVNKEDEEFIESNKMHAINGKVFGNLQGLTMHVGDEVYWYLMGMGNEID 80

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 301615846  988 IHTMHIHAHSFTYVRGATFHSDVYDLFPGTFKTVEMIARVPGTWLLHCHVTDHIHAGMEVLYTVL 1052
Cdd:cd11012    81 IHTAHFHGHSFDYKHRGVYRSDVFDLFPGTFQTVEMIPRTPGTWLLHCHVTDHIHAGMETTYTVL 145
 
Name Accession Description Interval E-value
CuRO_3_ceruloplasmin cd04224
The third cupredoxin domain of Ceruloplasmin; Ceruloplasmin is a multicopper oxidase essential ...
 370-571 1.64e-126

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: 383.36  E-value: 1.64e-126
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 301615846  370 GRERRYFIAAEEAMWNYAPTDTNQFTGQKIDHPDTESAIFFQRNEVRIGGTYTKAVYVEYTDATFTTRKQRSKDEEHLGI 449
Cdd:cd04224     1 GKVRHYFIAAEEIMWDYAPSGKNLFTGQNLTAPGSDSEVFFQRNETRIGGTYWKVRYVEYTDATFTTRKHRSKEEEHLGI 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 301615846  450 LGPVMIAQVGDSMKVTFKNKASRPYSIQAHGVSYSKNMEGASYRtgnltNDDPSPGSHVAPGDTFTYEWEVSSAVGSTNQ 529
Cdd:cd04224    81 LGPVIRAEVGDTIKVTFRNKASRPFSIQPHGVFYEKNYEGAMYR-----DGDPSPGSHVSPGETFTYEWTVPEGVGPTNQ 155

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|..
gi 301615846  530 NLNCLVWLYFSSVDAIKDTNSGLVGPLLICKSIDANNHQRGI 571
Cdd:cd04224   156 DPPCLTYLYFSAVDPVRDTNSGLVGPLLVCKKGSLNANGRQK 197
CuRO_1_ceruloplasmin cd04222
The first cupredoxin domain of Ceruloplasmin; Ceruloplasmin is a multicopper oxidase essential ...
 22-203 3.13e-122

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


Pssm-ID: 259884 [Multi-domain]  Cd Length: 183  Bit Score: 371.37  E-value: 3.13e-122
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 301615846   22 RIFYIGIRETNWDYAPSGNNIISGTSIKDDEDAQTFLVGGPDRIGRVYKKAVYLQYSDDSYSKEIKKPQWLGHLGPILKA 101
Cdd:cd04222     1 REYYIGIRETQWDYAPSGKNLITNQTFDDDEHASVFLKRGPDRIGRVYKKAVYLQYTDDTYRTEIEKPVWLGFLGPILKA 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 301615846  102 EIGDIIIVHLKNFASRPYSIHPHGVQYTKENEGALYPDNASS-GHKDDAIEPGQSYTYRWEAVSEQGPTVQDEDCITRIY 180
Cdd:cd04222    81 EVGDVIVVHLKNFASRPYSLHPHGVFYNKENEGALYPDNTSGfEKADDAVPPGGSYTYTWTVPEEQAPTKADANCLTRIY 160

                         170       180
                  ....*....|....*....|...
gi 301615846  181 HSHIDGPKDVSSGLIGPLIICKK 203
Cdd:cd04222   161 HSHIDAPKDIASGLIGPLIICKK 183
CuRO_5_ceruloplasmin cd04225
The fifth cupredoxin domain of Ceruloplasmin; Ceruloplasmin is a multicopper oxidase essential ...
 727-897 4.59e-113

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: 346.76  E-value: 4.59e-113
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 301615846  727 NTYYIAAEEIEWDYSPNRTWEHERHIHHGESPGDAFLNKGEKFIGSTYKKAVYRQYTDRTFTKRKERNEEEKHLGILGPL 806
Cdd:cd04225     1 RTYYIAAEEVEWDYSPQRTWEQELHNTHEESPGNAFLNKGDKFIGSKYKKVVYREYTDDTFSVPKERTAEEEHLGILGPL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 301615846  807 LIARTHEKVKIVFKNMASRPYSIYAHGVKTDGP-VVQTEPGQTQTYIWKIPERSGPGYhEDVNCVTWAYYSTVDQVKDTY 885
Cdd:cd04225    81 IHAEVGEKVKIVFKNMASRPYSIHAHGVKTDSSwVAPTEPGETQTYTWKIPERSGPGV-EDSNCISWAYYSTVDQIKDLY 159

                         170
                  ....*....|..
gi 301615846  886 SGLIGPLVICKR 897
Cdd:cd04225   160 SGLIGPLVICRR 171
CuRO_4_ceruloplasmin cd11022
The fourth cupredoxin domain of Ceruloplasmin; Ceruloplasmin is a multicopper oxidase ...
 572-715 4.85e-96

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


Pssm-ID: 259908 [Multi-domain]  Cd Length: 144  Bit Score: 300.55  E-value: 4.85e-96
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 301615846  572 AHNYFLLPTVFDENESWYLDENIQQFTGTPANVNKEDPDFQESNMMHSINGYMYGNQPGLDMCAGDTVLWHLMGLGNEVD 651
Cdd:cd11022     1 DKEFFLLFTVFDENESWYLDENIQQFTLDPRSVDKEDEDFQESNKMHSINGYMYGNQPGLDMCKGDTVSWHLFGLGTETD 80

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 301615846  652 MHGIHFSGNTIVTHYTRADTASLFPHISYSVMMNPDNEGVFNVECMTTDHYTAGMRQHYRVKSC 715
Cdd:cd11022    81 VHGIYFSGNTFLLQGTRRDTANLFPHTSVTAIMQPDNEGTFEVNCQTTDHYSAGMRQIYTVSQC 144
CuRO_2_ceruloplasmin cd11021
The second cupredoxin domain of Ceruloplasmin; Ceruloplasmin is a multicopper oxidase ...
 214-354 2.57e-94

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: 295.92  E-value: 2.57e-94
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 301615846  214 YKEFVLMFSVIDENLSWYLDENINTFCTEPSSVDKNDTDFQESNKMHSINGYMFGNLPGLSMCEGEHIHWYLFGMGNEAD 293
Cdd:cd11021     1 DREFVLMFSVVDENLSWYLDENIKTYCSEPAKVDKDDEDFQESNKMHSINGYTFGNLPGLSMCAGDRVKWHLFGMGNEVD 80

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 301615846  294 IHSAYFHGQVLTFQMYRVDTLSLFPATMIEGHMVTKNPGKWLLTCQVNDHLAGGMQAIYEV 354
Cdd:cd11021    81 IHSAFFHGQTLTDRGHRTDTINLFPATFVTAEMVAQNPGKWLLSCQVNDHLKAGMQAFYEV 141
CuRO_6_ceruloplasmin cd11012
The sixth cupredoxin domain of Ceruloplasmin; Ceruloplasmin is a multicopper oxidase essential ...
 908-1052 1.90e-92

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: 291.00  E-value: 1.90e-92
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 301615846  908 PKRFALLFLIFDENESWYLDENIKTYSLHPDQVQKEDEDFIESNKMHGINGKLYANLEGLTMHVGDKIYWHLIGLGNEAD 987
Cdd:cd11012     1 KLEFALLFLVFDENESWYLDENIKTYSDHPEKVNKEDEEFIESNKMHAINGKVFGNLQGLTMHVGDEVYWYLMGMGNEID 80

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 301615846  988 IHTMHIHAHSFTYVRGATFHSDVYDLFPGTFKTVEMIARVPGTWLLHCHVTDHIHAGMEVLYTVL 1052
Cdd:cd11012    81 IHTAHFHGHSFDYKHRGVYRSDVFDLFPGTFQTVEMIPRTPGTWLLHCHVTDHIHAGMETTYTVL 145
Cu-oxidase_2 pfam07731
Multicopper oxidase; This entry contains many divergent copper oxidase-like domains that are ...
 946-1054 9.74e-15

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: 72.08  E-value: 9.74e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 301615846   946 DFIESNKMHGINGKLY-ANLEGLTMHVGDKIYWHLIGLGNeaDIHTMHIHAHSFtYVRGATFHS---------------- 1008
Cdd:pfam07731   14 SGNFRRNDWAINGLLFpPNTNVITLPYGTVVEWVLQNTTT--GVHPFHLHGHSF-QVLGRGGGPwpeedpktynlvdpvr 90

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*..
gi 301615846  1009 -DVYDLFPGTFKTVEMIARVPGTWLLHCHVTDHIHAGMEVLYTVLEK 1054
Cdd:pfam07731   91 rDTVQVPPGGWVAIRFRADNPGVWLFHCHILWHLDQGMMGQFVVRPG 137
Cu-oxidase_3 pfam07732
Multicopper oxidase; This entry contains many divergent copper oxidase-like domains that are ...
 95-200 8.07e-11

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


Pssm-ID: 462247 [Multi-domain]  Cd Length: 119  Bit Score: 60.34  E-value: 8.07e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 301615846    95 LGPILKAEIGDIIIVHLKNFASRPYSIHPHGVQYTKENegalYPDNAsSGHKDDAIEPGQSYTYRWEAVSEQGptvqded 174
Cdd:pfam07732   25 PGPTIRVREGDTVVVNVTNNLDEPTSIHWHGLQQRGTP----WMDGV-PGVTQCPIPPGQSFTYRFQVKQQAG------- 92

                           90       100
                   ....*....|....*....|....*.
gi 301615846   175 ciTRIYHSHIDGPKdvSSGLIGPLII 200
Cdd:pfam07732   93 --TYWYHSHTSGQQ--AAGLAGAIII 114
SufI COG2132
Multicopper oxidase with three cupredoxin domains (includes cell division protein FtsP and ...
 95-200 1.33e-10

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: 64.57  E-value: 1.33e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 301615846   95 LGPILKAEIGDIIIVHLKNFASRPYSIHPHGvqytkenegaLYPDNASSGHKDDAIEPGQSYTYRWEAvsEQGPTvqded 174
Cdd:COG2132    43 PGPTIRVREGDRVRVRVTNRLPEPTTVHWHG----------LRVPNAMDGVPGDPIAPGETFTYEFPV--PQPAG----- 105

                          90       100
                  ....*....|....*....|....*...
gi 301615846  175 ciTRIYHSHIDG--PKDVSSGLIGPLII 200
Cdd:COG2132   106 --TYWYHPHTHGstAEQVYRGLAGALIV 131
SufI COG2132
Multicopper oxidase with three cupredoxin domains (includes cell division protein FtsP and ...
 953-1045 4.66e-09

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


Pssm-ID: 441735 [Multi-domain]  Cd Length: 423  Bit Score: 59.95  E-value: 4.66e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 301615846  953 MHGINGKLYANLE-GLTMHVGDKIYWHLIGLGNEAdiHTMHIHAHSFTYVR---GATFHS---DVYDLFPGtfKTVEMIA 1025
Cdd:COG2132   317 VWTINGKAFDPDRpDLTVKLGERERWTLVNDTMMP--HPFHLHGHQFQVLSrngKPPPEGgwkDTVLVPPG--ETVRILF 392

                          90       100
                  ....*....|....*....|...
gi 301615846 1026 R---VPGTWLLHCHVTDHIHAGM 1045
Cdd:COG2132   393 RfdnYPGDWMFHCHILEHEDAGM 415
PLN02191 PLN02191
L-ascorbate oxidase
 96-222 5.36e-07

L-ascorbate oxidase


Pssm-ID: 177843 [Multi-domain]  Cd Length: 574  Bit Score: 53.48  E-value: 5.36e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 301615846   96 GPILKAEIGDIIIVHLKN-FASRPYSIHPHGVQytkeNEGALYPDNAsSGHKDDAIEPGQSYTYRWeAVSEQGptvqded 174
Cdd:PLN02191   53 GPTIDAVAGDTIVVHLTNkLTTEGLVIHWHGIR----QKGSPWADGA-AGVTQCAINPGETFTYKF-TVEKPG------- 119

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*....
gi 301615846  175 ciTRIYHSHIDGPKdvSSGLIGPLIICKKGSINavEQHKYK-EFVLMFS 222
Cdd:PLN02191  120 --THFYHGHYGMQR--SAGLYGSLIVDVAKGPK--ERLRYDgEFNLLLS 162
PLN02191 PLN02191
L-ascorbate oxidase
 986-1049 8.67e-06

L-ascorbate oxidase


Pssm-ID: 177843 [Multi-domain]  Cd Length: 574  Bit Score: 49.63  E-value: 8.67e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 301615846  986 ADIHTMHIHAHSFtYVRG------------ATFH------SDVYDLFPGTFKTVEMIARVPGTWLLHCHVTDHIHAGMEV 1047
Cdd:PLN02191  464 SEIHPWHLHGHDF-WVLGygdgkfkpgideKTYNlknpplRNTAILYPYGWTAIRFVTDNPGVWFFHCHIEPHLHMGMGV 542


                  ..
gi 301615846 1048 LY 1049
Cdd:PLN02191  543 VF 544
Cu-oxidase_3 pfam07732
Multicopper oxidase; This entry contains many divergent copper oxidase-like domains that are ...
 427-558 1.15e-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: 45.70  E-value: 1.15e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 301615846   427 VEYTDATFTTRKQRSKdeehLGI----LGPVMIAQVGDSMKVTFKNKASRPYSIQAHGVSYSKN--MEGASYrtgnLTND 500
Cdd:pfam07732    2 VTYGTVSPLGGTRQAV----IGVngqfPGPTIRVREGDTVVVNVTNNLDEPTSIHWHGLQQRGTpwMDGVPG----VTQC 73

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 301615846   501 dpspgsHVAPGDTFTYEWEVSSAVGSTnqnlnclvWlYFSSVDAIKdtNSGLVGPLLI 558
Cdd:pfam07732   74 ------PIPPGQSFTYRFQVKQQAGTY--------W-YHSHTSGQQ--AAGLAGAIII 114
ascorbase TIGR03388
L-ascorbate oxidase, plant type; Members of this protein family are the copper-containing ...
 96-200 2.28e-05

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


Pssm-ID: 274555 [Multi-domain]  Cd Length: 541  Bit Score: 48.21  E-value: 2.28e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 301615846    96 GPILKAEIGDIIIVHLKN-FASRPYSIHPHGVQytkeNEGALYPDNAsSGHKDDAIEPGQSYTYRWeAVSEQGptvqded 174
Cdd:TIGR03388   31 GPTIRAQAGDTIVVELTNkLHTEGVVIHWHGIR----QIGTPWADGT-AGVTQCAINPGETFIYNF-VVDRPG------- 97

                           90       100
                   ....*....|....*....|....*.
gi 301615846   175 ciTRIYHSHIDGPKdvSSGLIGPLII 200
Cdd:TIGR03388   98 --TYFYHGHYGMQR--SAGLYGSLIV 119
ascorbase TIGR03388
L-ascorbate oxidase, plant type; Members of this protein family are the copper-containing ...
 983-1049 9.52e-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: 46.28  E-value: 9.52e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 301615846   983 GNEADIHTMHIHAHSFtYVRG---ATFHSDV----YDL-----------FPGTFKTVEMIARVPGTWLLHCHVTDHIHAG 1044
Cdd:TIGR03388  438 GNNSETHPWHLHGHDF-WVLGygeGKFRPGVdeksYNLknpplrntvviFPYGWTALRFVADNPGVWAFHCHIEPHLHMG 516


                   ....*
gi 301615846  1045 MEVLY 1049
Cdd:TIGR03388  517 MGVVF 521
Cu-oxidase_2 pfam07731
Multicopper oxidase; This entry contains many divergent copper oxidase-like domains that are ...
 251-355 5.04e-04

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


Pssm-ID: 462246 [Multi-domain]  Cd Length: 138  Bit Score: 41.27  E-value: 5.04e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 301615846   251 TDFQESNKMHSINGYMFG-NLPGLSMCEGEHIHWYLFGMGNeaDIHSAYFHG---QVL----------TFQMYRV----- 311
Cdd:pfam07731   13 TSGNFRRNDWAINGLLFPpNTNVITLPYGTVVEWVLQNTTT--GVHPFHLHGhsfQVLgrgggpwpeeDPKTYNLvdpvr 90

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*
gi 301615846   312 -DTLSLFPATMIEGHMVTKNPGKWLLTCQVNDHLAGGMQAIYEVK 355
Cdd:pfam07731   91 rDTVQVPPGGWVAIRFRADNPGVWLFHCHILWHLDQGMMGQFVVR 135
SufI COG2132
Multicopper oxidase with three cupredoxin domains (includes cell division protein FtsP and ...
 449-520 1.54e-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: 42.23  E-value: 1.54e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 301615846  449 ILGPVMIAQVGDSMKVTFKNKASRPYSIQAHGVsysknmegasyRTGNlTNDDpSPGSHVAPGDTFTYEWEV 520
Cdd:COG2132    42 YPGPTIRVREGDRVRVRVTNRLPEPTTVHWHGL-----------RVPN-AMDG-VPGDPIAPGETFTYEFPV 100
Cu-oxidase_3 pfam07732
Multicopper oxidase; This entry contains many divergent copper oxidase-like domains that are ...
 802-860 2.45e-03

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


Pssm-ID: 462247 [Multi-domain]  Cd Length: 119  Bit Score: 38.77  E-value: 2.45e-03
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 301615846   802 ILGPLLIARTHEKVKIVFKNMASRPYSIYAHGVK------TDGPVVQTE----PGQTQTYIWKIPERSG 860
Cdd:pfam07732   24 FPGPTIRVREGDTVVVNVTNNLDEPTSIHWHGLQqrgtpwMDGVPGVTQcpipPGQSFTYRFQVKQQAG 92
 
Name Accession Description Interval E-value
CuRO_3_ceruloplasmin cd04224
The third cupredoxin domain of Ceruloplasmin; Ceruloplasmin is a multicopper oxidase essential ...
 370-571 1.64e-126

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: 383.36  E-value: 1.64e-126
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 301615846  370 GRERRYFIAAEEAMWNYAPTDTNQFTGQKIDHPDTESAIFFQRNEVRIGGTYTKAVYVEYTDATFTTRKQRSKDEEHLGI 449
Cdd:cd04224     1 GKVRHYFIAAEEIMWDYAPSGKNLFTGQNLTAPGSDSEVFFQRNETRIGGTYWKVRYVEYTDATFTTRKHRSKEEEHLGI 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 301615846  450 LGPVMIAQVGDSMKVTFKNKASRPYSIQAHGVSYSKNMEGASYRtgnltNDDPSPGSHVAPGDTFTYEWEVSSAVGSTNQ 529
Cdd:cd04224    81 LGPVIRAEVGDTIKVTFRNKASRPFSIQPHGVFYEKNYEGAMYR-----DGDPSPGSHVSPGETFTYEWTVPEGVGPTNQ 155

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|..
gi 301615846  530 NLNCLVWLYFSSVDAIKDTNSGLVGPLLICKSIDANNHQRGI 571
Cdd:cd04224   156 DPPCLTYLYFSAVDPVRDTNSGLVGPLLVCKKGSLNANGRQK 197
CuRO_1_ceruloplasmin cd04222
The first cupredoxin domain of Ceruloplasmin; Ceruloplasmin is a multicopper oxidase essential ...
 22-203 3.13e-122

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


Pssm-ID: 259884 [Multi-domain]  Cd Length: 183  Bit Score: 371.37  E-value: 3.13e-122
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 301615846   22 RIFYIGIRETNWDYAPSGNNIISGTSIKDDEDAQTFLVGGPDRIGRVYKKAVYLQYSDDSYSKEIKKPQWLGHLGPILKA 101
Cdd:cd04222     1 REYYIGIRETQWDYAPSGKNLITNQTFDDDEHASVFLKRGPDRIGRVYKKAVYLQYTDDTYRTEIEKPVWLGFLGPILKA 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 301615846  102 EIGDIIIVHLKNFASRPYSIHPHGVQYTKENEGALYPDNASS-GHKDDAIEPGQSYTYRWEAVSEQGPTVQDEDCITRIY 180
Cdd:cd04222    81 EVGDVIVVHLKNFASRPYSLHPHGVFYNKENEGALYPDNTSGfEKADDAVPPGGSYTYTWTVPEEQAPTKADANCLTRIY 160

                         170       180
                  ....*....|....*....|...
gi 301615846  181 HSHIDGPKDVSSGLIGPLIICKK 203
Cdd:cd04222   161 HSHIDAPKDIASGLIGPLIICKK 183
CuRO_5_ceruloplasmin cd04225
The fifth cupredoxin domain of Ceruloplasmin; Ceruloplasmin is a multicopper oxidase essential ...
 727-897 4.59e-113

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: 346.76  E-value: 4.59e-113
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 301615846  727 NTYYIAAEEIEWDYSPNRTWEHERHIHHGESPGDAFLNKGEKFIGSTYKKAVYRQYTDRTFTKRKERNEEEKHLGILGPL 806
Cdd:cd04225     1 RTYYIAAEEVEWDYSPQRTWEQELHNTHEESPGNAFLNKGDKFIGSKYKKVVYREYTDDTFSVPKERTAEEEHLGILGPL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 301615846  807 LIARTHEKVKIVFKNMASRPYSIYAHGVKTDGP-VVQTEPGQTQTYIWKIPERSGPGYhEDVNCVTWAYYSTVDQVKDTY 885
Cdd:cd04225    81 IHAEVGEKVKIVFKNMASRPYSIHAHGVKTDSSwVAPTEPGETQTYTWKIPERSGPGV-EDSNCISWAYYSTVDQIKDLY 159

                         170
                  ....*....|..
gi 301615846  886 SGLIGPLVICKR 897
Cdd:cd04225   160 SGLIGPLVICRR 171
CuRO_4_ceruloplasmin cd11022
The fourth cupredoxin domain of Ceruloplasmin; Ceruloplasmin is a multicopper oxidase ...
 572-715 4.85e-96

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


Pssm-ID: 259908 [Multi-domain]  Cd Length: 144  Bit Score: 300.55  E-value: 4.85e-96
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 301615846  572 AHNYFLLPTVFDENESWYLDENIQQFTGTPANVNKEDPDFQESNMMHSINGYMYGNQPGLDMCAGDTVLWHLMGLGNEVD 651
Cdd:cd11022     1 DKEFFLLFTVFDENESWYLDENIQQFTLDPRSVDKEDEDFQESNKMHSINGYMYGNQPGLDMCKGDTVSWHLFGLGTETD 80

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 301615846  652 MHGIHFSGNTIVTHYTRADTASLFPHISYSVMMNPDNEGVFNVECMTTDHYTAGMRQHYRVKSC 715
Cdd:cd11022    81 VHGIYFSGNTFLLQGTRRDTANLFPHTSVTAIMQPDNEGTFEVNCQTTDHYSAGMRQIYTVSQC 144
CuRO_2_ceruloplasmin cd11021
The second cupredoxin domain of Ceruloplasmin; Ceruloplasmin is a multicopper oxidase ...
 214-354 2.57e-94

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: 295.92  E-value: 2.57e-94
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 301615846  214 YKEFVLMFSVIDENLSWYLDENINTFCTEPSSVDKNDTDFQESNKMHSINGYMFGNLPGLSMCEGEHIHWYLFGMGNEAD 293
Cdd:cd11021     1 DREFVLMFSVVDENLSWYLDENIKTYCSEPAKVDKDDEDFQESNKMHSINGYTFGNLPGLSMCAGDRVKWHLFGMGNEVD 80

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 301615846  294 IHSAYFHGQVLTFQMYRVDTLSLFPATMIEGHMVTKNPGKWLLTCQVNDHLAGGMQAIYEV 354
Cdd:cd11021    81 IHSAFFHGQTLTDRGHRTDTINLFPATFVTAEMVAQNPGKWLLSCQVNDHLKAGMQAFYEV 141
CuRO_6_ceruloplasmin cd11012
The sixth cupredoxin domain of Ceruloplasmin; Ceruloplasmin is a multicopper oxidase essential ...
 908-1052 1.90e-92

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: 291.00  E-value: 1.90e-92
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 301615846  908 PKRFALLFLIFDENESWYLDENIKTYSLHPDQVQKEDEDFIESNKMHGINGKLYANLEGLTMHVGDKIYWHLIGLGNEAD 987
Cdd:cd11012     1 KLEFALLFLVFDENESWYLDENIKTYSDHPEKVNKEDEEFIESNKMHAINGKVFGNLQGLTMHVGDEVYWYLMGMGNEID 80

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 301615846  988 IHTMHIHAHSFTYVRGATFHSDVYDLFPGTFKTVEMIARVPGTWLLHCHVTDHIHAGMEVLYTVL 1052
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 ...
 22-203 2.02e-74

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: 243.08  E-value: 2.02e-74
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 301615846   22 RIFYIGIRETNWDYAPSGnniisgTSIKDDEDAQTFLVGGPDRIGRVYKKAVYLQYSDDSYSKEIKKPQWLGHLGPILKA 101
Cdd:cd04199     1 RHYYIAAEEIDWDYAPSG------LAEKDLSYRNQYLDNGPFRIGRSYKKVVYREYTDESFTTPGPQPEHLGILGPTIRA 74

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 301615846  102 EIGDIIIVHLKNFASRPYSIHPHGVQYTKENEGALYPDNASSGHK-DDAIEPGQSYTYRWEAVSEQGPTVQDEDCITRIY 180
Cdd:cd04199    75 EVGDTIKVHFKNKASRPYSIHPHGVSYEKDSEGASYSDQTGPDEKkDDAVAPGETYTYVWIVTEESGPTKGDPACLTWAY 154

                         170       180
                  ....*....|....*....|...
gi 301615846  181 HSHIDGPKDVSSGLIGPLIICKK 203
Cdd:cd04199   155 YSHVDLEKDINSGLIGPLLICKK 177
CuRO_1_ceruloplasmin_like cd04199
Cupredoxin domains 1, 3, and 5 of ceruloplasmin and similar proteins; This family includes the ...
 373-561 2.62e-70

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: 231.91  E-value: 2.62e-70
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 301615846  373 RRYFIAAEEAMWNYAPTDTNQFtgqkidhPDTESAIFFQRNEVRIGGTYTKAVYVEYTDATFTTRKQRskdEEHLGILGP 452
Cdd:cd04199     1 RHYYIAAEEIDWDYAPSGLAEK-------DLSYRNQYLDNGPFRIGRSYKKVVYREYTDESFTTPGPQ---PEHLGILGP 70

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 301615846  453 VMIAQVGDSMKVTFKNKASRPYSIQAHGVSYSKNMEGASYrtGNLTNDDPSPGSHVAPGDTFTYEWEVSSAVGSTNQNLN 532
Cdd:cd04199    71 TIRAEVGDTIKVHFKNKASRPYSIHPHGVSYEKDSEGASY--SDQTGPDEKKDDAVAPGETYTYVWIVTEESGPTKGDPA 148

                         170       180
                  ....*....|....*....|....*....
gi 301615846  533 CLVWLYFSSVDAIKDTNSGLVGPLLICKS 561
Cdd:cd04199   149 CLTWAYYSHVDLEKDINSGLIGPLLICKK 177
CuRO_1_ceruloplasmin_like cd04199
Cupredoxin domains 1, 3, and 5 of ceruloplasmin and similar proteins; This family includes the ...
 728-897 4.59e-67

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: 222.67  E-value: 4.59e-67
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 301615846  728 TYYIAAEEIEWDYSPNRTWEHERHIHhgespgDAFLNKGEKFIGSTYKKAVYRQYTDRTFTKRKERNEeekHLGILGPLL 807
Cdd:cd04199     2 HYYIAAEEIDWDYAPSGLAEKDLSYR------NQYLDNGPFRIGRSYKKVVYREYTDESFTTPGPQPE---HLGILGPTI 72

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 301615846  808 IARTHEKVKIVFKNMASRPYSIYAHGV-------------------KTDGPVvqtEPGQTQTYIWKIPERSGPGyHEDVN 868
Cdd:cd04199    73 RAEVGDTIKVHFKNKASRPYSIHPHGVsyekdsegasysdqtgpdeKKDDAV---APGETYTYVWIVTEESGPT-KGDPA 148

                         170       180
                  ....*....|....*....|....*....
gi 301615846  869 CVTWAYYSTVDQVKDTYSGLIGPLVICKR 897
Cdd:cd04199   149 CLTWAYYSHVDLEKDINSGLIGPLLICKK 177
CuRO_2_ceruloplasmin_like cd04200
Cupredoxin domains 2, 4, and 6 of ceruloplasmin and similar proteins; This family includes the ...
 215-354 6.55e-65

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: 215.35  E-value: 6.55e-65
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 301615846  215 KEFVLMFSVIDENLSWYLDENINTFCTEPSSVDKNDTDFQESNKMHSINGYMFGNLPGLSMCEGEHIHWYLFGMGNEADI 294
Cdd:cd04200     2 KEFVLLFAVFDENKSWYLEDNIKRFCDNPEKVDKDDEEFQESNKMHAINGYVFGNLPGLTMCAGDRVRWHLLGMGNEVDV 81

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 301615846  295 HSAYFHGQVLTFQMYRVDTLSLFPATMIEGHMVTKNPGKWLLTCQVNDHLAGGMQAIYEV 354
Cdd:cd04200    82 HSIHFHGQTFLYKGYRIDTLTLFPATFETVEMVPSNPGTWLLHCHNSDHRHAGMQAYFLV 141
CuRO_2_ceruloplasmin_like cd04200
Cupredoxin domains 2, 4, and 6 of ceruloplasmin and similar proteins; This family includes the ...
 909-1051 3.42e-62

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: 207.65  E-value: 3.42e-62
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 301615846  909 KRFALLFLIFDENESWYLDENIKTYSLHPDQVQKEDEDFIESNKMHGINGKLYANLEGLTMHVGDKIYWHLIGLGNEADI 988
Cdd:cd04200     2 KEFVLLFAVFDENKSWYLEDNIKRFCDNPEKVDKDDEEFQESNKMHAINGYVFGNLPGLTMCAGDRVRWHLLGMGNEVDV 81

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 301615846  989 HTMHIHAHSFTYvRGatFHSDVYDLFPGTFKTVEMIARVPGTWLLHCHVTDHIHAGMEVLYTV 1051
Cdd:cd04200    82 HSIHFHGQTFLY-KG--YRIDTLTLFPATFETVEMVPSNPGTWLLHCHNSDHRHAGMQAYFLV 141
CuRO_3_ceruloplasmin cd04224
The third cupredoxin domain of Ceruloplasmin; Ceruloplasmin is a multicopper oxidase essential ...
 729-900 3.64e-62

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: 210.02  E-value: 3.64e-62
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 301615846  729 YYIAAEEIEWDYSPNRT--WEHERHIHHGeSPGDAFLNKGEKFIGSTYKKAVYRQYTDRTFTKRKERNEEEKHLGILGPL 806
Cdd:cd04224     6 YFIAAEEIMWDYAPSGKnlFTGQNLTAPG-SDSEVFFQRNETRIGGTYWKVRYVEYTDATFTTRKHRSKEEEHLGILGPV 84

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 301615846  807 LIARTHEKVKIVFKNMASRPYSIYAHGVK----TDG---------PVVQTEPGQTQTYIWKIPERSGPGyHEDVNCVTWA 873
Cdd:cd04224    85 IRAEVGDTIKVTFRNKASRPFSIQPHGVFyeknYEGamyrdgdpsPGSHVSPGETFTYEWTVPEGVGPT-NQDPPCLTYL 163

                         170       180
                  ....*....|....*....|....*..
gi 301615846  874 YYSTVDQVKDTYSGLIGPLVICKRSLL 900
Cdd:cd04224   164 YFSAVDPVRDTNSGLVGPLLVCKKGSL 190
CuRO_3_ceruloplasmin cd04224
The third cupredoxin domain of Ceruloplasmin; Ceruloplasmin is a multicopper oxidase essential ...
 21-208 1.24e-61

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: 208.48  E-value: 1.24e-61
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 301615846   21 ERIFYIGIRETNWDYAPSGNNIISGTSI-KDDEDAQTFLVGGPDRIGRVYKKAVYLQYSDDSYSKE---IKKPQWLGHLG 96
Cdd:cd04224     3 VRHYFIAAEEIMWDYAPSGKNLFTGQNLtAPGSDSEVFFQRNETRIGGTYWKVRYVEYTDATFTTRkhrSKEEEHLGILG 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 301615846   97 PILKAEIGDIIIVHLKNFASRPYSIHPHGVQYTKENEGALYPDnaSSGHKDDAIEPGQSYTYRWEAVSEQGPTVQDEDCI 176
Cdd:cd04224    83 PVIRAEVGDTIKVTFRNKASRPFSIQPHGVFYEKNYEGAMYRD--GDPSPGSHVSPGETFTYEWTVPEGVGPTNQDPPCL 160

                         170       180       190
                  ....*....|....*....|....*....|..
gi 301615846  177 TRIYHSHIDGPKDVSSGLIGPLIICKKGSINA 208
Cdd:cd04224   161 TYLYFSAVDPVRDTNSGLVGPLLVCKKGSLNA 192
CuRO_4_ceruloplasmin cd11022
The fourth cupredoxin domain of Ceruloplasmin; Ceruloplasmin is a multicopper oxidase ...
 215-357 5.54e-61

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: 204.64  E-value: 5.54e-61
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 301615846  215 KEFVLMFSVIDENLSWYLDENINTFCTEPSSVDKNDTDFQESNKMHSINGYMFGNLPGLSMCEGEHIHWYLFGMGNEADI 294
Cdd:cd11022     2 KEFFLLFTVFDENESWYLDENIQQFTLDPRSVDKEDEDFQESNKMHSINGYMYGNQPGLDMCKGDTVSWHLFGLGTETDV 81

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 301615846  295 HSAYFHGQVLTFQMYRVDTLSLFPATMIEGHMVTKNPGKWLLTCQVNDHLAGGMQAIYEVKSC 357
Cdd:cd11022    82 HGIYFSGNTFLLQGTRRDTANLFPHTSVTAIMQPDNEGTFEVNCQTTDHYSAGMRQIYTVSQC 144
CuRO_2_ceruloplasmin_like cd04200
Cupredoxin domains 2, 4, and 6 of ceruloplasmin and similar proteins; This family includes the ...
 573-712 3.88e-57

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: 193.40  E-value: 3.88e-57
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 301615846  573 HNYFLLPTVFDENESWYLDENIQQFTGTPANVNKEDPDFQESNMMHSINGYMYGNQPGLDMCAGDTVLWHLMGLGNEVDM 652
Cdd:cd04200     2 KEFVLLFAVFDENKSWYLEDNIKRFCDNPEKVDKDDEEFQESNKMHAINGYVFGNLPGLTMCAGDRVRWHLLGMGNEVDV 81

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 301615846  653 HGIHFSGNTIVTHYTRADTASLFPHISYSVMMNPDNEGVFNVECMTTDHYTAGMRQHYRV 712
Cdd:cd04200    82 HSIHFHGQTFLYKGYRIDTLTLFPATFETVEMVPSNPGTWLLHCHNSDHRHAGMQAYFLV 141
CuRO_1_ceruloplasmin cd04222
The first cupredoxin domain of Ceruloplasmin; Ceruloplasmin is a multicopper oxidase essential ...
 373-560 8.56e-57

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: 194.17  E-value: 8.56e-57
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 301615846  373 RRYFIAAEEAMWNYAPTDTNQFTGQKIDHpDTESAIFFQRNEVRIGGTYTKAVYVEYTDATFTTRKQRSKdeeHLGILGP 452
Cdd:cd04222     1 REYYIGIRETQWDYAPSGKNLITNQTFDD-DEHASVFLKRGPDRIGRVYKKAVYLQYTDDTYRTEIEKPV---WLGFLGP 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 301615846  453 VMIAQVGDSMKVTFKNKASRPYSIQAHGVSYSKNMEGASY---RTGNLTNDDPspgshVAPGDTFTYEWEVSSAVGSTNQ 529
Cdd:cd04222    77 ILKAEVGDVIVVHLKNFASRPYSLHPHGVFYNKENEGALYpdnTSGFEKADDA-----VPPGGSYTYTWTVPEEQAPTKA 151

                         170       180       190
                  ....*....|....*....|....*....|.
gi 301615846  530 NLNCLVWLYFSSVDAIKDTNSGLVGPLLICK 560
Cdd:cd04222   152 DANCLTRIYHSHIDAPKDIASGLIGPLIICK 182
CuRO_5_ceruloplasmin cd04225
The fifth cupredoxin domain of Ceruloplasmin; Ceruloplasmin is a multicopper oxidase essential ...
 373-560 1.09e-55

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: 190.37  E-value: 1.09e-55
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 301615846  373 RRYFIAAEEAMWNYAPTDTNQFTgQKIDHPDTESAIFFQRNEVRIGGTYTKAVYVEYTDATFTTRKQRSKDEEHLGILGP 452
Cdd:cd04225     1 RTYYIAAEEVEWDYSPQRTWEQE-LHNTHEESPGNAFLNKGDKFIGSKYKKVVYREYTDDTFSVPKERTAEEEHLGILGP 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 301615846  453 VMIAQVGDSMKVTFKNKASRPYSIQAHGVSysknmegasyrtgnltnDDPSPGSHVAPGDTFTYEWEVSSAVGSTNQNLN 532
Cdd:cd04225    80 LIHAEVGEKVKIVFKNMASRPYSIHAHGVK-----------------TDSSWVAPTEPGETQTYTWKIPERSGPGVEDSN 142

                         170       180
                  ....*....|....*....|....*...
gi 301615846  533 CLVWLYFSSVDAIKDTNSGLVGPLLICK 560
Cdd:cd04225   143 CISWAYYSTVDQIKDLYSGLIGPLVICR 170
CuRO_3_FV_like cd14450
The third cupredoxin domain of coagulation factor V and similar proteins; Factor V is an ...
 24-202 8.69e-55

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


Pssm-ID: 259992 [Multi-domain]  Cd Length: 181  Bit Score: 188.55  E-value: 8.69e-55
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 301615846   24 FYIGIRETNWDYAPsgnNIISGTsikDDEDAQTFLVGGPDRIGRVYKKAVYLQYSDDSYSK--EIKKPQWLGHLGPILKA 101
Cdd:cd14450     5 YFIAAEEVIWDYAP---SIPENM---DKRYRSQYLDNFSNNIGKKYKKAVFTQYEDGSFTKrlENPRPKEEGILGPVIRA 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 301615846  102 EIGDIIIVHLKNFASRPYSIHPHGVQYTKENEGALYP-DNASSGHKDDAIEPGQSYTYRWEAVSEQGPTVQDEDCITRIY 180
Cdd:cd14450    79 QVRDTIKIVFKNKASRPYSIYPHGVTVSKAAEGASYPpDPRGNETQNKAVQPGETYTYKWNILETDEPTARDPRCLTRMY 158

                         170       180
                  ....*....|....*....|..
gi 301615846  181 HSHIDGPKDVSSGLIGPLIICK 202
Cdd:cd14450   159 HSAVDITRDIASGLIGPLLICK 180
CuRO_5_FV_like cd14451
The fifth cupredoxin domain of coagulation factor V and similar proteins; Factor V is an ...
 372-561 1.06e-54

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: 187.74  E-value: 1.06e-54
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 301615846  372 ERRYFIAAEEAMWNYAPTDTNQFTGQKIDHPdtesaiffqrnevrigGTYTKAVYVEYTDATFTTRKQRSKDEEHLGILG 451
Cdd:cd14451     1 KRRYYIAAEEEEWDYAGYGKSRLDKTQNERD----------------TVFKKVVFRRYLDSTFSTPDIQGEYEEHLGILG 64

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 301615846  452 PVMIAQVGDSMKVTFKNKASRPYSIQAHGVSYSKNMEGASYrtgnltnDDPSP-----GSHVAPGDTFTYEWEVSSAVGS 526
Cdd:cd14451    65 PVIRAEVDDVIQVFFKNLASRPYSLHAHGLSYEKSSEGLSY-------DDESPdwfkkDDAVQPNGTYTYVWYANPRSGP 137

                         170       180       190
                  ....*....|....*....|....*....|....*
gi 301615846  527 TNQNLNCLVWLYFSSVDAIKDTNSGLVGPLLICKS 561
Cdd:cd14451   138 ENNGSDCRTWAYYSAVNPEKDIHSGLIGPLLICRK 172
CuRO_2_ceruloplasmin cd11021
The second cupredoxin domain of Ceruloplasmin; Ceruloplasmin is a multicopper oxidase ...
 909-1051 1.71e-54

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: 186.14  E-value: 1.71e-54
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 301615846  909 KRFALLFLIFDENESWYLDENIKTYSLHPDQVQKEDEDFIESNKMHGINGKLYANLEGLTMHVGDKIYWHLIGLGNEADI 988
Cdd:cd11021     2 REFVLMFSVVDENLSWYLDENIKTYCSEPAKVDKDDEDFQESNKMHSINGYTFGNLPGLSMCAGDRVKWHLFGMGNEVDI 81

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 301615846  989 HTMHIHAHSFTYvRGatFHSDVYDLFPGTFKTVEMIARVPGTWLLHCHVTDHIHAGMEVLYTV 1051
Cdd:cd11021    82 HSAFFHGQTLTD-RG--HRTDTINLFPATFVTAEMVAQNPGKWLLSCQVNDHLKAGMQAFYEV 141
CuRO_1_Ceruloplasmin_like_1 cd04229
cupredoxin domain of ceruloplasmin homologs; Uncharacterized subfamily of ceruloplasmin ...
 373-558 3.24e-54

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: 186.47  E-value: 3.24e-54
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 301615846  373 RRYFIAAEEAMWNYAPTdtnqfTGQKIDHPD--TESAIFFQRNEVRIGGTYTKAVYVEYTDATFTTRKQrskDEEHLGIL 450
Cdd:cd04229     1 RTYYIAAEEVDWDYAPS-----GKNKCCLGDdlEVSTLDSQPGPYTIGSTYTKARYREYTDNSFSTPKP---TPAYLGIL 72

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 301615846  451 GPVMIAQVGDSMKVTFKNKASR-PYSIQAHGVSYSKNMEGASYRtgnltNDDPspgshVAPGDTFTYEWEVSSAVGSTNQ 529
Cdd:cd04229    73 GPVIRAEVGDTIKVVFKNNLDEfPVNMHPHGGLYSKDNEGTTDG-----AGDV-----VAPGETYTYRWIVPEDAGPGPG 142

                         170       180
                  ....*....|....*....|....*....
gi 301615846  530 NLNCLVWLYFSSVDAIKDTNSGLVGPLLI 558
Cdd:cd04229   143 DPSSRLWLYHSHVDVFAHTNAGLVGPIIV 171
CuRO_2_ceruloplasmin cd11021
The second cupredoxin domain of Ceruloplasmin; Ceruloplasmin is a multicopper oxidase ...
 573-712 1.57e-52

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: 180.36  E-value: 1.57e-52
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 301615846  573 HNYFLLPTVFDENESWYLDENIQQFTGTPANVNKEDPDFQESNMMHSINGYMYGNQPGLDMCAGDTVLWHLMGLGNEVDM 652
Cdd:cd11021     2 REFVLMFSVVDENLSWYLDENIKTYCSEPAKVDKDDEDFQESNKMHSINGYTFGNLPGLSMCAGDRVKWHLFGMGNEVDI 81

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 301615846  653 HGIHFSGNTIVTHYTRADTASLFPHISYSVMMNPDNEGVFNVECMTTDHYTAGMRQHYRV 712
Cdd:cd11021    82 HSAFFHGQTLTDRGHRTDTINLFPATFVTAEMVAQNPGKWLLSCQVNDHLKAGMQAFYEV 141
CuRO_1_FV_like cd04226
The first cupredoxin domain of coagulation factor VIII and similar proteins; Factor V is an ...
 22-204 2.88e-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: 180.44  E-value: 2.88e-52
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 301615846   22 RIFYIGIRETNWDYAPSGNNIISgtsikddedaqtflvggpDRIGRVYKKAVYLQYSDDsYSKEIKKPQWLGHLGPILKA 101
Cdd:cd04226     1 REYYIAAQNIDWDYTPQSEELRL------------------KRSEQSFKKIVYREYEEG-FKKEKPADLSSGLLGPTLRA 61

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 301615846  102 EIGDIIIVHLKNFASRPYSIHPHGVQYTKENEGALYPDNASSGHK-DDAIEPGQSYTYRWEAVSEQGPTVQDEDCITRIY 180
Cdd:cd04226    62 EVGDTLIVHFKNMADKPLSIHPQGIAYGKKSEGSLYSDNTSPVEKlDDAVQPGQEYTYVWDITEEVGPTEADPPCLTYIY 141

                         170       180
                  ....*....|....*....|....
gi 301615846  181 HSHIDGPKDVSSGLIGPLIICKKG 204
Cdd:cd04226   142 YSHVNMVRDFNSGLIGALLICKKG 165
CuRO_3_FV_like cd14450
The third cupredoxin domain of coagulation factor V and similar proteins; Factor V is an ...
 375-561 3.72e-52

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: 180.84  E-value: 3.72e-52
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 301615846  375 YFIAAEEAMWNYAPTDTNQFTGQ-KIDHPDTESaiffqrneVRIGGTYTKAVYVEYTDATFTTRKQRSKDEEhLGILGPV 453
Cdd:cd14450     5 YFIAAEEVIWDYAPSIPENMDKRyRSQYLDNFS--------NNIGKKYKKAVFTQYEDGSFTKRLENPRPKE-EGILGPV 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 301615846  454 MIAQVGDSMKVTFKNKASRPYSIQAHGVSYSKNMEGASYR---TGNLTNddpspGSHVAPGDTFTYEWEVSSAVGSTNQN 530
Cdd:cd14450    76 IRAQVRDTIKIVFKNKASRPYSIYPHGVTVSKAAEGASYPpdpRGNETQ-----NKAVQPGETYTYKWNILETDEPTARD 150

                         170       180       190
                  ....*....|....*....|....*....|.
gi 301615846  531 LNCLVWLYFSSVDAIKDTNSGLVGPLLICKS 561
Cdd:cd14450   151 PRCLTRMYHSAVDITRDIASGLIGPLLICKS 181
CuRO_1_FVIII_like cd14452
The first cupredoxin domain of coagulation factor VIII and similar proteins; Factor VIII ...
 22-204 3.27e-51

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: 177.86  E-value: 3.27e-51
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 301615846   22 RIFYIGIRETNWDYAPSgnniisgtsikDDEDAQTFLVGGPDRIGRVYKKAVYLQYSDDSYSKEIKKPQWLGHLGPILKA 101
Cdd:cd14452     1 RRYYIAAVEIGWDYIHS-----------DLGDPASEQRKKPKDIPQKYIKAVFVEYLDATFTVPKPRPAWMGLLGPTIVA 69

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 301615846  102 EIGDIIIVHLKNFASRPYSIHPHGVQYTKENEGALYPDNASSGHK-DDAIEPGQSYTYRWEAVSEQGPTVQDEDCITRIY 180
Cdd:cd14452    70 EVGDTVVITFKNLASQPYSLHAVGVSYWKASEGAGYDDSTSQHEKeDDAVYPGGYHTYVWDISPKDGPTGSDPECLTYSY 149

                         170       180
                  ....*....|....*....|....
gi 301615846  181 HSHIDGPKDVSSGLIGPLIICKKG 204
Cdd:cd14452   150 SSQVDPVKDVNSGLIGALLVCRMG 173
CuRO_4_ceruloplasmin cd11022
The fourth cupredoxin domain of Ceruloplasmin; Ceruloplasmin is a multicopper oxidase ...
 909-1051 1.60e-50

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: 174.59  E-value: 1.60e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 301615846  909 KRFALLFLIFDENESWYLDENIKTYSLHPDQVQKEDEDFIESNKMHGINGKLYANLEGLTMHVGDKIYWHLIGLGNEADI 988
Cdd:cd11022     2 KEFFLLFTVFDENESWYLDENIQQFTLDPRSVDKEDEDFQESNKMHSINGYMYGNQPGLDMCKGDTVSWHLFGLGTETDV 81

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 301615846  989 HTMHIHAHSFTYvRGAtfHSDVYDLFPGTFKTVEMIARVPGTWLLHCHVTDHIHAGMEVLYTV 1051
Cdd:cd11022    82 HGIYFSGNTFLL-QGT--RRDTANLFPHTSVTAIMQPDNEGTFEVNCQTTDHYSAGMRQIYTV 141
CuRO_1_Ceruloplasmin_like_1 cd04229
cupredoxin domain of ceruloplasmin homologs; Uncharacterized subfamily of ceruloplasmin ...
 22-204 9.73e-50

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: 173.76  E-value: 9.73e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 301615846   22 RIFYIGIRETNWDYAPSGNNiiSGTSIKDDEDAQTFLVGGPDRIGRVYKKAVYLQYSDDSYSKEIKKPQWLGHLGPILKA 101
Cdd:cd04229     1 RTYYIAAEEVDWDYAPSGKN--KCCLGDDLEVSTLDSQPGPYTIGSTYTKARYREYTDNSFSTPKPTPAYLGILGPVIRA 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 301615846  102 EIGDIIIVHLKN-FASRPYSIHPHGVQYTKENEGALypdnassGHKDDAIEPGQSYTYRWEAVSEQGPTVQDEDCITRIY 180
Cdd:cd04229    79 EVGDTIKVVFKNnLDEFPVNMHPHGGLYSKDNEGTT-------DGAGDVVAPGETYTYRWIVPEDAGPGPGDPSSRLWLY 151

                         170       180
                  ....*....|....*....|....
gi 301615846  181 HSHIDGPKDVSSGLIGPLIICKKG 204
Cdd:cd04229   152 HSHVDVFAHTNAGLVGPIIVTSKG 175
CuRO_3_FV_like cd14450
The third cupredoxin domain of coagulation factor V and similar proteins; Factor V is an ...
 728-896 2.82e-49

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: 172.75  E-value: 2.82e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 301615846  728 TYYIAAEEIEWDYSPNRTWEHERHIHhgespgDAFLNKGEKFIGSTYKKAVYRQYTDRTFTKRKErNEEEKHLGILGPLL 807
Cdd:cd14450     4 EYFIAAEEVIWDYAPSIPENMDKRYR------SQYLDNFSNNIGKKYKKAVFTQYEDGSFTKRLE-NPRPKEEGILGPVI 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 301615846  808 IARTHEKVKIVFKNMASRPYSIYAHGVKTD-------------GPVVQT---EPGQTQTYIWKIPERSGPGyHEDVNCVT 871
Cdd:cd14450    77 RAQVRDTIKIVFKNKASRPYSIYPHGVTVSkaaegasyppdprGNETQNkavQPGETYTYKWNILETDEPT-ARDPRCLT 155

                         170       180
                  ....*....|....*....|....*
gi 301615846  872 WAYYSTVDQVKDTYSGLIGPLVICK 896
Cdd:cd14450   156 RMYHSAVDITRDIASGLIGPLLICK 180
CuRO_5_FV_like cd14451
The fifth cupredoxin domain of coagulation factor V and similar proteins; Factor V is an ...
 726-897 7.54e-49

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: 171.18  E-value: 7.54e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 301615846  726 TNTYYIAAEEIEWDYSPnrtweherhihhgesPGDAFLNKGEKFIGSTYKKAVYRQYTDRTFTKRKERNEEEKHLGILGP 805
Cdd:cd14451     1 KRRYYIAAEEEEWDYAG---------------YGKSRLDKTQNERDTVFKKVVFRRYLDSTFSTPDIQGEYEEHLGILGP 65

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 301615846  806 LLIARTHEKVKIVFKNMASRPYSIYAHGV-------------------KTDGPVvqtEPGQTQTYIWKIPERSGPgYHED 866
Cdd:cd14451    66 VIRAEVDDVIQVFFKNLASRPYSLHAHGLsyeksseglsyddespdwfKKDDAV---QPNGTYTYVWYANPRSGP-ENNG 141

                         170       180       190
                  ....*....|....*....|....*....|.
gi 301615846  867 VNCVTWAYYSTVDQVKDTYSGLIGPLVICKR 897
Cdd:cd14451   142 SDCRTWAYYSAVNPEKDIHSGLIGPLLICRK 172
CuRO_5_FV_like cd14451
The fifth cupredoxin domain of coagulation factor V and similar proteins; Factor V is an ...
 21-204 1.09e-48

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


Pssm-ID: 259993 [Multi-domain]  Cd Length: 173  Bit Score: 170.79  E-value: 1.09e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 301615846   21 ERIFYIGIRETNWDYAPSGNNiisgTSIKDDEDAQTflvggpdrigrVYKKAVYLQYSDDSYSKEIKKPQW---LGHLGP 97
Cdd:cd14451     1 KRRYYIAAEEEEWDYAGYGKS----RLDKTQNERDT-----------VFKKVVFRRYLDSTFSTPDIQGEYeehLGILGP 65

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 301615846   98 ILKAEIGDIIIVHLKNFASRPYSIHPHGVQYTKENEGALYPDNASSGHK-DDAIEPGQSYTYRWEAVSEQGPTVQDEDCI 176
Cdd:cd14451    66 VIRAEVDDVIQVFFKNLASRPYSLHAHGLSYEKSSEGLSYDDESPDWFKkDDAVQPNGTYTYVWYANPRSGPENNGSDCR 145

                         170       180
                  ....*....|....*....|....*...
gi 301615846  177 TRIYHSHIDGPKDVSSGLIGPLIICKKG 204
Cdd:cd14451   146 TWAYYSAVNPEKDIHSGLIGPLLICRKG 173
CuRO_6_ceruloplasmin cd11012
The sixth cupredoxin domain of Ceruloplasmin; Ceruloplasmin is a multicopper oxidase essential ...
 215-354 6.38e-48

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: 167.35  E-value: 6.38e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 301615846  215 KEFVLMFSVIDENLSWYLDENINTFCTEPSSVDKNDTDFQESNKMHSINGYMFGNLPGLSMCEGEHIHWYLFGMGNEADI 294
Cdd:cd11012     2 LEFALLFLVFDENESWYLDENIKTYSDHPEKVNKEDEEFIESNKMHAINGKVFGNLQGLTMHVGDEVYWYLMGMGNEIDI 81

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 301615846  295 HSAYFHGQVLTFQ---MYRVDTLSLFPATMIEGHMVTKNPGKWLLTCQVNDHLAGGMQAIYEV 354
Cdd:cd11012    82 HTAHFHGHSFDYKhrgVYRSDVFDLFPGTFQTVEMIPRTPGTWLLHCHVTDHIHAGMETTYTV 144
CuRO_3_FVIII_like cd04227
The third cupredoxin domain of coagulation factor VIII and similar proteins; Factor VIII ...
 24-203 1.35e-46

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


Pssm-ID: 259889 [Multi-domain]  Cd Length: 177  Bit Score: 164.72  E-value: 1.35e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 301615846   24 FYIGIRETNWDYAPSgnniisgTSIKDDEDAQT-FLVGGPDRIGRVYKKAVYLQYSDDSYSKEIKKPQWLGHLGPILKAE 102
Cdd:cd04227     5 HYIAAEELDWDYAPL-------LSSTDDRELQSrYLPTGPQRIGYKYKKVAFVEYTDKTFKRREAKQTEKGILGPLLKGE 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 301615846  103 IGDIIIVHLKNFASRPYSIHPHGVQYTKenegALYPDNASSGHKD---DAIEPGQSYTYRWEAVSEQGPTVQDEDCITRI 179
Cdd:cd04227    78 VGDQIHIMFKNTASRPYNIYPHGLTSVR----PMYRSRNPAGEKDlktMPIGPGETFGYMWELTAEDGPTEEDPRCLTRL 153

                         170       180
                  ....*....|....*....|....
gi 301615846  180 YHSHIDGPKDVSSGLIGPLIICKK 203
Cdd:cd04227   154 YQSTVDPERDLASGLIGPLLICKK 177
CuRO_1_ceruloplasmin cd04222
The first cupredoxin domain of Ceruloplasmin; Ceruloplasmin is a multicopper oxidase essential ...
 728-897 4.24e-46

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: 163.74  E-value: 4.24e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 301615846  728 TYYIAAEEIEWDYSPNRTWEHERHIHHGESPGDAFLNKGEKFIGSTYKKAVYRQYTDRTFTKRKERneeEKHLGILGPLL 807
Cdd:cd04222     2 EYYIGIRETQWDYAPSGKNLITNQTFDDDEHASVFLKRGPDRIGRVYKKAVYLQYTDDTYRTEIEK---PVWLGFLGPIL 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 301615846  808 IARTHEKVKIVFKNMASRPYSIYAHGV-------------------KTDGPVvqtEPGQTQTYIWKIPERSGPGyHEDVN 868
Cdd:cd04222    79 KAEVGDVIVVHLKNFASRPYSLHPHGVfynkenegalypdntsgfeKADDAV---PPGGSYTYTWTVPEEQAPT-KADAN 154

                         170       180
                  ....*....|....*....|....*....
gi 301615846  869 CVTWAYYSTVDQVKDTYSGLIGPLVICKR 897
Cdd:cd04222   155 CLTRIYHSHIDAPKDIASGLIGPLIICKK 183
CuRO_3_FVIII_like cd04227
The third cupredoxin domain of coagulation factor VIII and similar proteins; Factor VIII ...
 725-897 9.13e-44

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


Pssm-ID: 259889 [Multi-domain]  Cd Length: 177  Bit Score: 156.63  E-value: 9.13e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 301615846  725 RTNTYYIAAEEIEWDYSPNRTWEHERHIHhgespgDAFLNKGEKFIGSTYKKAVYRQYTDRTFTKRKERNEEEkhlGILG 804
Cdd:cd04227     1 QTWEHYIAAEELDWDYAPLLSSTDDRELQ------SRYLPTGPQRIGYKYKKVAFVEYTDKTFKRREAKQTEK---GILG 71

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 301615846  805 PLLIARTHEKVKIVFKNMASRPYSIYAHGVKTDGPVVQTE--------------PGQTQTYIWKIPERSGPgYHEDVNCV 870
Cdd:cd04227    72 PLLKGEVGDQIHIMFKNTASRPYNIYPHGLTSVRPMYRSRnpagekdlktmpigPGETFGYMWELTAEDGP-TEEDPRCL 150

                         170       180
                  ....*....|....*....|....*..
gi 301615846  871 TWAYYSTVDQVKDTYSGLIGPLVICKR 897
Cdd:cd04227   151 TRLYQSTVDPERDLASGLIGPLLICKK 177
CuRO_3_FVIII_like cd04227
The third cupredoxin domain of coagulation factor VIII and similar proteins; Factor VIII ...
 375-560 1.16e-43

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


Pssm-ID: 259889 [Multi-domain]  Cd Length: 177  Bit Score: 156.63  E-value: 1.16e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 301615846  375 YFIAAEEAMWNYAPtdtnqftgQKIDHPDTE-SAIFFQRNEVRIGGTYTKAVYVEYTDATFTTRKQRSKDEehlGILGPV 453
Cdd:cd04227     5 HYIAAEELDWDYAP--------LLSSTDDRElQSRYLPTGPQRIGYKYKKVAFVEYTDKTFKRREAKQTEK---GILGPL 73

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 301615846  454 MIAQVGDSMKVTFKNKASRPYSIQAHGVSYSKNMegasYRTGNLTNDDPSPGSHVAPGDTFTYEWEVSSAVGSTNQNLNC 533
Cdd:cd04227    74 LKGEVGDQIHIMFKNTASRPYNIYPHGLTSVRPM----YRSRNPAGEKDLKTMPIGPGETFGYMWELTAEDGPTEEDPRC 149

                         170       180
                  ....*....|....*....|....*..
gi 301615846  534 LVWLYFSSVDAIKDTNSGLVGPLLICK 560
Cdd:cd04227   150 LTRLYQSTVDPERDLASGLIGPLLICK 176
CuRO_5_FVIII_like cd04228
The fifth cupredoxin domain of coagulation factor VIII and similar proteins; Factor VIII ...
 373-560 1.66e-43

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: 155.81  E-value: 1.66e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 301615846  373 RRYFIAAEEAMWNYAPTDTNQFtgqkIDHPDTESAiffQRNEVRiggTYTKAVYVEYTDATFTTRKQRSKDEEHLGILGP 452
Cdd:cd04228     2 RHYFIAAVEVLWDYGMQRPQHF----LRARDPNRG---RRKSVP---QYKKVVFREYLDGSFTQPVYRGELDEHLGILGP 71

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 301615846  453 VMIAQVGDSMKVTFKNKASRPYSIQAHGVSYSKnmEGASYRTGNLtnddpspgshVAPGDTFTYEWEVSSAVGSTNQNLN 532
Cdd:cd04228    72 YIRAEVEDNIMVTFKNLASRPYSFHSSLISYEE--DQRAEPRGNF----------VQPGEVQTYSWKVLHQMAPTKQEFD 139

                         170       180
                  ....*....|....*....|....*...
gi 301615846  533 CLVWLYFSSVDAIKDTNSGLVGPLLICK 560
Cdd:cd04228   140 CKAWAYFSNVDLEKDLHSGLIGPLIICK 167
CuRO_1_Ceruloplasmin_like_1 cd04229
cupredoxin domain of ceruloplasmin homologs; Uncharacterized subfamily of ceruloplasmin ...
 727-894 2.23e-43

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: 155.65  E-value: 2.23e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 301615846  727 NTYYIAAEEIEWDYSPNrtweHERHIHHGESPGDAFL--NKGEKFIGSTYKKAVYRQYTDRTFTKRKernEEEKHLGILG 804
Cdd:cd04229     1 RTYYIAAEEVDWDYAPS----GKNKCCLGDDLEVSTLdsQPGPYTIGSTYTKARYREYTDNSFSTPK---PTPAYLGILG 73

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 301615846  805 PLLIARTHEKVKIVFKN-MASRPYSIYAHGV--------KTDGPVVQTEPGQTQTYIWKIPERSGPGyHEDVNCVTWAYY 875
Cdd:cd04229    74 PVIRAEVGDTIKVVFKNnLDEFPVNMHPHGGlyskdnegTTDGAGDVVAPGETYTYRWIVPEDAGPG-PGDPSSRLWLYH 152

                         170
                  ....*....|....*....
gi 301615846  876 STVDQVKDTYSGLIGPLVI 894
Cdd:cd04229   153 SHVDVFAHTNAGLVGPIIV 171
CuRO_5_FVIII_like cd04228
The fifth cupredoxin domain of coagulation factor VIII and similar proteins; Factor VIII ...
 729-897 9.54e-43

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


Pssm-ID: 259890 [Multi-domain]  Cd Length: 169  Bit Score: 153.50  E-value: 9.54e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 301615846  729 YYIAAEEIEWDYSPNRTWeherHIHHGESPgdaflNKGEKFIGSTYKKAVYRQYTDRTFTKRKERNEEEKHLGILGPLLI 808
Cdd:cd04228     4 YFIAAVEVLWDYGMQRPQ----HFLRARDP-----NRGRRKSVPQYKKVVFREYLDGSFTQPVYRGELDEHLGILGPYIR 74

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 301615846  809 ARTHEKVKIVFKNMASRPYSIYAHGVKTD--------GPVVQtePGQTQTYIWKIPERSGPGYHEdVNCVTWAYYSTVDQ 880
Cdd:cd04228    75 AEVEDNIMVTFKNLASRPYSFHSSLISYEedqraeprGNFVQ--PGEVQTYSWKVLHQMAPTKQE-FDCKAWAYFSNVDL 151

                         170
                  ....*....|....*..
gi 301615846  881 VKDTYSGLIGPLVICKR 897
Cdd:cd04228   152 EKDLHSGLIGPLIICKT 168
CuRO_1_FVIII_like cd14452
The first cupredoxin domain of coagulation factor VIII and similar proteins; Factor VIII ...
 373-560 1.83e-42

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: 152.82  E-value: 1.83e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 301615846  373 RRYFIAAEEAMWNYAPTDTNQFTGQKIDHPDTESAIffqrnevriggtYTKAVYVEYTDATFTTRKQRSKdeeHLGILGP 452
Cdd:cd14452     1 RRYYIAAVEIGWDYIHSDLGDPASEQRKKPKDIPQK------------YIKAVFVEYLDATFTVPKPRPA---WMGLLGP 65

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 301615846  453 VMIAQVGDSMKVTFKNKASRPYSIQAHGVSYSKNMEGASYRtgNLTNDDPSPGSHVAPGDTFTYEWEVSSAVGSTNQNLN 532
Cdd:cd14452    66 TIVAEVGDTVVITFKNLASQPYSLHAVGVSYWKASEGAGYD--DSTSQHEKEDDAVYPGGYHTYVWDISPKDGPTGSDPE 143

                         170       180
                  ....*....|....*....|....*...
gi 301615846  533 CLVWLYFSSVDAIKDTNSGLVGPLLICK 560
Cdd:cd14452   144 CLTYSYSSQVDPVKDVNSGLIGALLVCR 171
CuRO_1_FV_like cd04226
The first cupredoxin domain of coagulation factor VIII and similar proteins; Factor V is an ...
 373-560 4.08e-42

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: 151.55  E-value: 4.08e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 301615846  373 RRYFIAAEEAMWNYaptdTNQFTGQKIDHPDTesaiffqrnevriggTYTKAVYVEYtDATFTTRKQRSKDEehlGILGP 452
Cdd:cd04226     1 REYYIAAQNIDWDY----TPQSEELRLKRSEQ---------------SFKKIVYREY-EEGFKKEKPADLSS---GLLGP 57

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 301615846  453 VMIAQVGDSMKVTFKNKASRPYSIQAHGVSYSKNMEGASYRTGNL---TNDDPspgshVAPGDTFTYEWEVSSAVGSTNQ 529
Cdd:cd04226    58 TLRAEVGDTLIVHFKNMADKPLSIHPQGIAYGKKSEGSLYSDNTSpveKLDDA-----VQPGQEYTYVWDITEEVGPTEA 132

                         170       180       190
                  ....*....|....*....|....*....|.
gi 301615846  530 NLNCLVWLYFSSVDAIKDTNSGLVGPLLICK 560
Cdd:cd04226   133 DPPCLTYIYYSHVNMVRDFNSGLIGALLICK 163
CuRO_5_ceruloplasmin cd04225
The fifth cupredoxin domain of Ceruloplasmin; Ceruloplasmin is a multicopper oxidase essential ...
 22-203 8.13e-42

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


Pssm-ID: 259887 [Multi-domain]  Cd Length: 171  Bit Score: 151.08  E-value: 8.13e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 301615846   22 RIFYIGIRETNWDYAPSGN-----NIISGTSIKDdedaqTFLVGGPDRIGRVYKKAVYLQYSDDSYSKEIKKP---QWLG 93
Cdd:cd04225     1 RTYYIAAEEVEWDYSPQRTweqelHNTHEESPGN-----AFLNKGDKFIGSKYKKVVYREYTDDTFSVPKERTaeeEHLG 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 301615846   94 HLGPILKAEIGDIIIVHLKNFASRPYSIHPHGVQytkenegalypdnaSSGHKDDAIEPGQSYTYRWEAVSEQGPTVQDE 173
Cdd:cd04225    76 ILGPLIHAEVGEKVKIVFKNMASRPYSIHAHGVK--------------TDSSWVAPTEPGETQTYTWKIPERSGPGVEDS 141

                         170       180       190
                  ....*....|....*....|....*....|
gi 301615846  174 DCITRIYHSHIDGPKDVSSGLIGPLIICKK 203
Cdd:cd04225   142 NCISWAYYSTVDQIKDLYSGLIGPLVICRR 171
CuRO_6_ceruloplasmin cd11012
The sixth cupredoxin domain of Ceruloplasmin; Ceruloplasmin is a multicopper oxidase essential ...
 577-712 7.78e-40

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


Pssm-ID: 259898 [Multi-domain]  Cd Length: 145  Bit Score: 144.24  E-value: 7.78e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 301615846  577 LLPTVFDENESWYLDENIQQFTGTPANVNKEDPDFQESNMMHSINGYMYGNQPGLDMCAGDTVLWHLMGLGNEVDMHGIH 656
Cdd:cd11012     6 LLFLVFDENESWYLDENIKTYSDHPEKVNKEDEEFIESNKMHAINGKVFGNLQGLTMHVGDEVYWYLMGMGNEIDIHTAH 85

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 301615846  657 FSGNTI---VTHYTRADTASLFPHISYSVMMNPDNEGVFNVECMTTDHYTAGMRQHYRV 712
Cdd:cd11012    86 FHGHSFdykHRGVYRSDVFDLFPGTFQTVEMIPRTPGTWLLHCHVTDHIHAGMETTYTV 144
CuRO_6_FVIII_like cd11018
The sixth cupredoxin domain of coagulation factor VIII and similar proteins; Factor VIII ...
 909-1051 4.05e-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: 139.24  E-value: 4.05e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 301615846  909 KRFALLFLIFDENESWYLDENIKTYSLHPDQVQKEDEDFIESNKMHGINGKLYANLEGLTMHVGDKIYWHLIGLGNEADI 988
Cdd:cd11018     2 QEFALLFTIFDETKSWYFEENMRRNCRPPCHIQTQDPWFHINNKFHAINGYVADTLPGLVMAQHQRIRWHLLNMGSDEEI 81

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 301615846  989 HTMHIHAHSFTYVRGATFHSDVYDLFPGTFKTVEMIARVPGTWLLHCHVTDHIHAGMEVLYTV 1051
Cdd:cd11018    82 HSVHFHGLPFTVRAKKEYRMGVYNLYPGVFGTVEMRPSTAGIWLVECTVGEHLLAGMSALFLV 144
CuRO_5_FVIII_like cd04228
The fifth cupredoxin domain of coagulation factor VIII and similar proteins; Factor VIII ...
 22-204 9.46e-36

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: 133.47  E-value: 9.46e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 301615846   22 RIFYIGIRETNWDYApsgnniisgtsikdDEDAQTFLVGGPDRIGR-----VYKKAVYLQYSDDSYSKEIKKPQW---LG 93
Cdd:cd04228     2 RHYFIAAVEVLWDYG--------------MQRPQHFLRARDPNRGRrksvpQYKKVVFREYLDGSFTQPVYRGELdehLG 67

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 301615846   94 HLGPILKAEIGDIIIVHLKNFASRPYSIHPHGVQYtkENEGAlypdnasSGHKDDAIEPGQSYTYRWEAVSEQGPTVQDE 173
Cdd:cd04228    68 ILGPYIRAEVEDNIMVTFKNLASRPYSFHSSLISY--EEDQR-------AEPRGNFVQPGEVQTYSWKVLHQMAPTKQEF 138

                         170       180       190
                  ....*....|....*....|....*....|.
gi 301615846  174 DCITRIYHSHIDGPKDVSSGLIGPLIICKKG 204
Cdd:cd04228   139 DCKAWAYFSNVDLEKDLHSGLIGPLIICKTG 169
CuRO_1_FVIII_like cd14452
The first cupredoxin domain of coagulation factor VIII and similar proteins; Factor VIII ...
 729-898 1.15e-35

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


Pssm-ID: 259994 [Multi-domain]  Cd Length: 173  Bit Score: 133.56  E-value: 1.15e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 301615846  729 YYIAAEEIEWDYSpnrtweherHIHHGESPGDAflNKGEKFIGSTYKKAVYRQYTDRTFTKRKERneeEKHLGILGPLLI 808
Cdd:cd14452     3 YYIAAVEIGWDYI---------HSDLGDPASEQ--RKKPKDIPQKYIKAVFVEYLDATFTVPKPR---PAWMGLLGPTIV 68

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 301615846  809 ARTHEKVKIVFKNMASRPYSIYAHGV-------------KTDGPVVQTE---PGQTQTYIWKIPERSGPgYHEDVNCVTW 872
Cdd:cd14452    69 AEVGDTVVITFKNLASQPYSLHAVGVsywkasegagyddSTSQHEKEDDavyPGGYHTYVWDISPKDGP-TGSDPECLTY 147

                         170       180
                  ....*....|....*....|....*.
gi 301615846  873 AYYSTVDQVKDTYSGLIGPLVICKRS 898
Cdd:cd14452   148 SYSSQVDPVKDVNSGLIGALLVCRMG 173
CuRO_4_FVIII_like cd11016
The fourth cupredoxin domain of coagulation factor VIII and similar proteins; Factor VIII ...
 577-715 6.45e-34

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: 127.29  E-value: 6.45e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 301615846  577 LLPTVFDENESWYLDENIQQFTGTPANVNKEDPDFQESNMMHSINGYMYGNQPgLDMCAGDTVLWHLMGLGNEVDMHGIH 656
Cdd:cd11016     6 LLFSVFDENNSWYLKENIHRFTQTPAGVNDTDPDFYASNVMHTINGIVFDRRQ-FVICLTDVAYWYVLSVGAQTDFLSVF 84

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 301615846  657 FSGNTIVTHYTRADTASLFPHISYSVMMNPDNEGVFNVECMTTDHYTAGMRQHYRVKSC 715
Cdd:cd11016    85 FSGNTFKHQMVYEDVLTLFPFSGETVSMSPEVPGEWELGCFNGDFRSRGMSAQYTVSTC 143
CuRO_6_FVIII_like cd11018
The sixth cupredoxin domain of coagulation factor VIII and similar proteins; Factor VIII ...
 215-354 1.43e-33

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: 126.15  E-value: 1.43e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 301615846  215 KEFVLMFSVIDENLSWYLDENINTFCTEPSSVDKNDTDFQESNKMHSINGYMFGNLPGLSMCEGEHIHWYLFGMGNEADI 294
Cdd:cd11018     2 QEFALLFTIFDETKSWYFEENMRRNCRPPCHIQTQDPWFHINNKFHAINGYVADTLPGLVMAQHQRIRWHLLNMGSDEEI 81

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 301615846  295 HSAYFHGQVLTF---QMYRVDTLSLFPATMIEGHMVTKNPGKWLLTCQVNDHLAGGMQAIYEV 354
Cdd:cd11018    82 HSVHFHGLPFTVrakKEYRMGVYNLYPGVFGTVEMRPSTAGIWLVECTVGEHLLAGMSALFLV 144
CuRO_4_FVIII_like cd11016
The fourth cupredoxin domain of coagulation factor VIII and similar proteins; Factor VIII ...
 215-357 2.25e-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: 125.75  E-value: 2.25e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 301615846  215 KEFVLMFSVIDENLSWYLDENINTFCTEPSSVDKNDTDFQESNKMHSINGYMFGNLPgLSMCEGEHIHWYLFGMGNEADI 294
Cdd:cd11016     2 KDWSLLFSVFDENNSWYLKENIHRFTQTPAGVNDTDPDFYASNVMHTINGIVFDRRQ-FVICLTDVAYWYVLSVGAQTDF 80

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 301615846  295 HSAYFHGQVLTFQMYRVDTLSLFPATMIEGHMVTKNPGKWLLTCQVNDHLAGGMQAIYEVKSC 357
Cdd:cd11016    81 LSVFFSGNTFKHQMVYEDVLTLFPFSGETVSMSPEVPGEWELGCFNGDFRSRGMSAQYTVSTC 143
CuRO_1_FV_like cd04226
The first cupredoxin domain of coagulation factor VIII and similar proteins; Factor V is an ...
 729-897 9.69e-33

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: 124.59  E-value: 9.69e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 301615846  729 YYIAAEEIEWDYSPNRtwEHERHIHhgespgdaflnkgekfIGSTYKKAVYRQYtDRTFTKRKERNEEEkhlGILGPLLI 808
Cdd:cd04226     3 YYIAAQNIDWDYTPQS--EELRLKR----------------SEQSFKKIVYREY-EEGFKKEKPADLSS---GLLGPTLR 60

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 301615846  809 ARTHEKVKIVFKNMASRPYSIYAHGVK----------TDG--PVVQTE----PGQTQTYIWKIPERSGPGyHEDVNCVTW 872
Cdd:cd04226    61 AEVGDTLIVHFKNMADKPLSIHPQGIAygkksegslySDNtsPVEKLDdavqPGQEYTYVWDITEEVGPT-EADPPCLTY 139

                         170       180
                  ....*....|....*....|....*
gi 301615846  873 AYYSTVDQVKDTYSGLIGPLVICKR 897
Cdd:cd04226   140 IYYSHVNMVRDFNSGLIGALLICKK 164
CuRO_6_FV_like cd14455
The sixth cupredoxin domain of coagulation factor V and similar proteins; Factor V is an ...
 909-1051 5.19e-32

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


Pssm-ID: 259997 [Multi-domain]  Cd Length: 140  Bit Score: 121.51  E-value: 5.19e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 301615846  909 KRFALLFLIFDENESWYLDENIKTYSLhpdQVQKEDEDFIESNKMHGINGKLYaNLEGLTMHVGDKIYWHLIGLGNEADI 988
Cdd:cd14455     2 REFVLLFMTFDEEKSWYYEKNRKRTCR---ENRVKDPNVQDNHTFHAINGIIY-NLKGLRMYTNELVRWHLINMGGPKDL 77

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 301615846  989 HTMHIHAHSFTYVRGATFHSDVYDLFPGTFKTVEMIARVPGTWLLHCHVTDHIHAGMEVLYTV 1051
Cdd:cd14455    78 HVVHFHGQTFTEKGLKDHQLGVYPLLPGSFATLEMKPSKPGLWLLETEVGESQQRGMQTLFLV 140
CuRO_2_ceruloplasmin_like_2 cd11023
cupredoxin domain of ceruloplasmin homologs; Uncharacterized subfamily of ceruloplasmin ...
 249-354 2.23e-31

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: 118.87  E-value: 2.23e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 301615846  249 NDTDFQESNKMHSINGYMFGNLPGLSMCEGEHIHWYLFGMGNEADIHSAYFHGQ-VLTFQMYRVDTLSLFPATMIEGHMV 327
Cdd:cd11023    12 LDLNVEEAGLMHSINGYVFGNLPGVTIAKGKRVRWHLVAYGNEVDFHTPHWHGQtVEADKSRRTDVAELMPASMRVADMT 91

                          90       100
                  ....*....|....*....|....*..
gi 301615846  328 TKNPGKWLLTCQVNDHLAGGMQAIYEV 354
Cdd:cd11023    92 AADVGTWLLHCHVHDHYMAGMMTQFAV 118
CuRO_4_FV_like cd14454
The fourth cupredoxin domain of coagulation factor V and similar proteins; Factor V is an ...
 580-715 1.71e-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: 1.71e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 301615846  580 TVFDENESWYLDENIQQFTGTPANVNKEDPDFQESNMMHSINGYMYGNQPGLDMCAGDTVLWHLMGLGNEVDMHGIHFSG 659
Cdd:cd14454     9 AVFDENKSWYLEENINKYCSNPNNVKKDDPKFYKSNIMPTINGYAYESSAPLGFCHSEVVQWHISSVGTQDEIITVHLSG 88

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 301615846  660 NTIVTHYTRADTASLFPHISYSVMMNPDNEGVFNVECMTTDHYTAGMRQHYRVKSC 715
Cdd:cd14454    89 HTFRYKGKHEDTLNLFPMSGESITVTMDNLGTWLLGSFGSSKKSKGLRVRFTDVIC 144
CuRO_2_ceruloplasmin_like_2 cd11023
cupredoxin domain of ceruloplasmin homologs; Uncharacterized subfamily of ceruloplasmin ...
 918-1051 4.84e-30

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: 115.40  E-value: 4.84e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 301615846  918 FDENESWYLDENIKtyslhpdqvqkededfiESNKMHGINGKLYANLEGLTMHVGDKIYWHLIGLGNEADIHTMHIHAHS 997
Cdd:cd11023     4 FIENSSIFLDLNVE-----------------EAGLMHSINGYVFGNLPGVTIAKGKRVRWHLVAYGNEVDFHTPHWHGQT 66

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....
gi 301615846  998 FTyvRGATFHSDVYDLFPGTFKTVEMIARVPGTWLLHCHVTDHIHAGMEVLYTV 1051
Cdd:cd11023    67 VE--ADKSRRTDVAELMPASMRVADMTAADVGTWLLHCHVHDHYMAGMMTQFAV 118
CuRO_6_FVIII_like cd11018
The sixth cupredoxin domain of coagulation factor VIII and similar proteins; Factor VIII ...
 577-712 1.96e-29

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


Pssm-ID: 259904 [Multi-domain]  Cd Length: 144  Bit Score: 114.59  E-value: 1.96e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 301615846  577 LLPTVFDENESWYLDENIQQFTGTPANVNKEDPDFQESNMMHSINGYMYGNQPGLDMCAGDTVLWHLMGLGNEVDMHGIH 656
Cdd:cd11018     6 LLFTIFDETKSWYFEENMRRNCRPPCHIQTQDPWFHINNKFHAINGYVADTLPGLVMAQHQRIRWHLLNMGSDEEIHSVH 85

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 301615846  657 FSGNTIVTHYT---RADTASLFPHISYSVMMNPDNEGVFNVECMTTDHYTAGMRQHYRV 712
Cdd:cd11018    86 FHGLPFTVRAKkeyRMGVYNLYPGVFGTVEMRPSTAGIWLVECTVGEHLLAGMSALFLV 144
CuRO_2_FV_like cd14453
The second cupredoxin domain of coagulation factor V and similar proteins; Factor V is an ...
 214-354 7.59e-29

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: 111.87  E-value: 7.59e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 301615846  214 YKEFVLMFSVIDENLSWYldenintfctepssvdknDTDFQESNKMHSINGYMFGNLPGLSMCEGEHIHWYLFGMGNEAD 293
Cdd:cd14453     1 YKEYVLMFGVFDENKSWY------------------KQNASVDSVKYTINGYTNGTLPDVSICAYDHVSWHLLGMSSEPE 62

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 301615846  294 IHSAYFHGQVLTFQMYRVDTLSLFPATMIEGHMVTKNPGKWLLTCQVNDHLAGGMQAIYEV 354
Cdd:cd14453    63 LFSVHFNGQVLEQNGHKVSAVGLVSGSSTTASMTVVHTGRWLISSLIMKHLQAGMYGYLNI 123
CuRO_6_FV_like cd14455
The sixth cupredoxin domain of coagulation factor V and similar proteins; Factor V is an ...
 215-354 1.69e-27

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: 108.80  E-value: 1.69e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 301615846  215 KEFVLMFSVIDENLSWYLDENINTFCTEPSSVDKNdtdFQESNKMHSINGYMFgNLPGLSMCEGEHIHWYLFGMGNEADI 294
Cdd:cd14455     2 REFVLLFMTFDEEKSWYYEKNRKRTCRENRVKDPN---VQDNHTFHAINGIIY-NLKGLRMYTNELVRWHLINMGGPKDL 77

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 301615846  295 HSAYFHGQVLT---FQMYRVDTLSLFPATMIEGHMVTKNPGKWLLTCQVNDHLAGGMQAIYEV 354
Cdd:cd14455    78 HVVHFHGQTFTekgLKDHQLGVYPLLPGSFATLEMKPSKPGLWLLETEVGESQQRGMQTLFLV 140
CuRO_4_FV_like cd14454
The fourth cupredoxin domain of coagulation factor V and similar proteins; Factor V is an ...
 209-337 1.94e-27

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


Pssm-ID: 259996 [Multi-domain]  Cd Length: 144  Bit Score: 108.81  E-value: 1.94e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 301615846  209 VEQHKykefvlMFSVIDENLSWYLDENINTFCTEPSSVDKNDTDFQESNKMHSINGYMFGNLPGLSMCEGEHIHWYLFGM 288
Cdd:cd14454     2 LEQHA------VFAVFDENKSWYLEENINKYCSNPNNVKKDDPKFYKSNIMPTINGYAYESSAPLGFCHSEVVQWHISSV 75

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*....
gi 301615846  289 GNEADIHSAYFHGQVLTFQMYRVDTLSLFPATMIEGHMVTKNPGKWLLT 337
Cdd:cd14454    76 GTQDEIITVHLSGHTFRYKGKHEDTLNLFPMSGESITVTMDNLGTWLLG 124
CuRO_2_ceruloplasmin_like_2 cd11023
cupredoxin domain of ceruloplasmin homologs; Uncharacterized subfamily of ceruloplasmin ...
 581-712 1.20e-26

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: 105.38  E-value: 1.20e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 301615846  581 VFDENESWYLDENIQqftgtpanvnkedpdfqESNMMHSINGYMYGNQPGLDMCAGDTVLWHLMGLGNEVDMHGIHFSGN 660
Cdd:cd11023     3 EFIENSSIFLDLNVE-----------------EAGLMHSINGYVFGNLPGVTIAKGKRVRWHLVAYGNEVDFHTPHWHGQ 65

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|...
gi 301615846  661 TIVTHYT-RADTASLFPHISYSVMMNPDNEGVFNVECMTTDHYTAGMRQHYRV 712
Cdd:cd11023    66 TVEADKSrRTDVAELMPASMRVADMTAADVGTWLLHCHVHDHYMAGMMTQFAV 118
CuRO_4_FV_like cd14454
The fourth cupredoxin domain of coagulation factor V and similar proteins; Factor V is an ...
 914-1053 4.94e-26

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: 104.57  E-value: 4.94e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 301615846  914 LFLIFDENESWYLDENIKTYSLHPDQVQKEDEDFIESNKMHGINGKLYANLEGLTMHVGDKIYWHLIGLGNEADIHTMHI 993
Cdd:cd14454     7 VFAVFDENKSWYLEENINKYCSNPNNVKKDDPKFYKSNIMPTINGYAYESSAPLGFCHSEVVQWHISSVGTQDEIITVHL 86

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 301615846  994 HAHSFTYvrgATFHSDVYDLFPGTFKTVEMIARVPGTWLLHCHVTDHIHAGMEVLYTVLE 1053
Cdd:cd14454    87 SGHTFRY---KGKHEDTLNLFPMSGESITVTMDNLGTWLLGSFGSSKKSKGLRVRFTDVI 143
CuRO_4_FVIII_like cd11016
The fourth cupredoxin domain of coagulation factor VIII and similar proteins; Factor VIII ...
 909-1053 2.18e-25

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: 103.02  E-value: 2.18e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 301615846  909 KRFALLFLIFDENESWYLDENIKTYSLHPDQVQKEDEDFIESNKMHGINGKLYANLEgLTMHVGDKIYWHLIGLGNEADI 988
Cdd:cd11016     2 KDWSLLFSVFDENNSWYLKENIHRFTQTPAGVNDTDPDFYASNVMHTINGIVFDRRQ-FVICLTDVAYWYVLSVGAQTDF 80

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 301615846  989 HTMHIHAHSFTYvrgATFHSDVYDLFPGTFKTVEMIARVPGTWLLHCHVTDHIHAGMEVLYTVLE 1053
Cdd:cd11016    81 LSVFFSGNTFKH---QMVYEDVLTLFPFSGETVSMSPEVPGEWELGCFNGDFRSRGMSAQYTVST 142
CuRO_2_FVIII_like cd11015
The second cupredoxin domain of coagulation factor VIII and similar proteins; Factor VIII ...
 215-354 8.41e-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: 100.75  E-value: 8.41e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 301615846  215 KEFVLMFSVIDENLSWYLDENintfctEPSSVDKNDTDfQESNKMHSINGYMFGNLPGLSMCEGEHIHWYLFGMGNEADI 294
Cdd:cd11015     2 QAFVLLFAVFDEGKSWYSEVG------ERKSRDKFKRA-DSRKEFHTINGYINASLPGLKICQRKPVIWHVIGMGTAPEV 74

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 301615846  295 HSAYFHGQVLTFQMYRVDTLSLFPATMIEGHMVTKNPGKWLLTCQVNDHLAGGMQAIYEV 354
Cdd:cd11015    75 HSIFFEGHTFLVRTHRKVSLEISPMTFLTAQTKPATVGSFLIFCQIHSHQHDGMEAMVKV 134
CuRO_2_FVIII_like cd11015
The second cupredoxin domain of coagulation factor VIII and similar proteins; Factor VIII ...
 909-1051 3.18e-19

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: 84.96  E-value: 3.18e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 301615846  909 KRFALLFLIFDENESWYLDENiktYSLHPDQVQKEDEdfieSNKMHGINGKLYANLEGLTMHVGDKIYWHLIGLGNEADI 988
Cdd:cd11015     2 QAFVLLFAVFDEGKSWYSEVG---ERKSRDKFKRADS----RKEFHTINGYINASLPGLKICQRKPVIWHVIGMGTAPEV 74

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 301615846  989 HTMHIHAHSFTyVRgaTFHSDVYDLFPGTFKTVEMIARVPGTWLLHCHVTDHIHAGMEVLYTV 1051
Cdd:cd11015    75 HSIFFEGHTFL-VR--THRKVSLEISPMTFLTAQTKPATVGSFLIFCQIHSHQHDGMEAMVKV 134
CuRO_2_FV_like cd14453
The second cupredoxin domain of coagulation factor V and similar proteins; Factor V is an ...
 573-706 7.94e-18

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


Pssm-ID: 259995 [Multi-domain]  Cd Length: 123  Bit Score: 80.67  E-value: 7.94e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 301615846  573 HNYFLLPTVFDENESWYldeniqqftgtpanvnkeDPDFQESNMMHSINGYMYGNQPGLDMCAGDTVLWHLMGLGNEVDM 652
Cdd:cd14453     2 KEYVLMFGVFDENKSWY------------------KQNASVDSVKYTINGYTNGTLPDVSICAYDHVSWHLLGMSSEPEL 63

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....
gi 301615846  653 HGIHFSGNTIVTHYTRADTASLFPHISYSVMMNPDNEGVFNVECMTTDHYTAGM 706
Cdd:cd14453    64 FSVHFNGQVLEQNGHKVSAVGLVSGSSTTASMTVVHTGRWLISSLIMKHLQAGM 117
CuRO_2_FVIII_like cd11015
The second cupredoxin domain of coagulation factor VIII and similar proteins; Factor VIII ...
 573-712 6.18e-17

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: 78.41  E-value: 6.18e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 301615846  573 HNYFLLPTVFDENESWYLDeniqqfTGTPANVNKEDPDFQESNMmHSINGYMYGNQPGLDMCAGDTVLWHLMGLGNEVDM 652
Cdd:cd11015     2 QAFVLLFAVFDEGKSWYSE------VGERKSRDKFKRADSRKEF-HTINGYINASLPGLKICQRKPVIWHVIGMGTAPEV 74

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 301615846  653 HGIHFSGNTIVTHYTRADTASLFPHISYSVMMNPDNEGVFNVECMTTDHYTAGMRQHYRV 712
Cdd:cd11015    75 HSIFFEGHTFLVRTHRKVSLEISPMTFLTAQTKPATVGSFLIFCQIHSHQHDGMEAMVKV 134
CuRO_6_FV_like cd14455
The sixth cupredoxin domain of coagulation factor V and similar proteins; Factor V is an ...
 575-712 4.06e-16

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: 76.06  E-value: 4.06e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 301615846  575 YFLLPTVFDENESWYLDENIQQftgTPANVNKEDPDFQESNMMHSINGYMYgNQPGLDMCAGDTVLWHLMGLGNEVDMHG 654
Cdd:cd14455     4 FVLLFMTFDEEKSWYYEKNRKR---TCRENRVKDPNVQDNHTFHAINGIIY-NLKGLRMYTNELVRWHLINMGGPKDLHV 79

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 301615846  655 IHFSGNTIVTHYTRADTASLFPHIS---YSVMMNPDNEGVFNVECMTTDHYTAGMRQHYRV 712
Cdd:cd14455    80 VHFHGQTFTEKGLKDHQLGVYPLLPgsfATLEMKPSKPGLWLLETEVGESQQRGMQTLFLV 140
CuRO_1_LCC_like cd04206
Cupredoxin domain 1 of laccase-like multicopper oxidases; including laccase, CueO, spore coat ...
 95-201 4.43e-16

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


Pssm-ID: 259869 [Multi-domain]  Cd Length: 120  Bit Score: 75.40  E-value: 4.43e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 301615846   95 LGPILKAEIGDIIIVHLKN-FASRPYSIHPHGVQYTKENEGalypdNASSGHKDDAIEPGQSYTYRWEAvseqgptvqDE 173
Cdd:cd04206    29 PGPTIRVKEGDTVEVTVTNnLPNEPTSIHWHGLRQPGTNDG-----DGVAGLTQCPIPPGESFTYRFTV---------DD 94

                          90       100
                  ....*....|....*....|....*...
gi 301615846  174 DCITRIYHSHIDGpkDVSSGLIGPLIIC 201
Cdd:cd04206    95 QAGTFWYHSHVGG--QRADGLYGPLIVE 120
CuRO_D2_2dMcoN_like cd04202
The second cupredoxin domain of bacterial two domain multicopper oxidase McoN and similar ...
 956-1045 3.05e-15

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: 73.44  E-value: 3.05e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 301615846  956 INGKLYANLEGLTMHVGDKIYWHLIGLGNeaDIHTMHIHAHSFTYV--------RGATFHSDVYDLFPGTFKTVEMIARV 1027
Cdd:cd04202    32 INGKSFPATPPLVVKEGDRVRIRLINLSM--DHHPMHLHGHFFLVTatdggpipGSAPWPKDTLNVAPGERYDIEFVADN 109

                          90
                  ....*....|....*...
gi 301615846 1028 PGTWLLHCHVTDHIHAGM 1045
Cdd:cd04202   110 PGDWMFHCHKLHHAMNGM 127
Cu-oxidase_2 pfam07731
Multicopper oxidase; This entry contains many divergent copper oxidase-like domains that are ...
 946-1054 9.74e-15

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: 72.08  E-value: 9.74e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 301615846   946 DFIESNKMHGINGKLY-ANLEGLTMHVGDKIYWHLIGLGNeaDIHTMHIHAHSFtYVRGATFHS---------------- 1008
Cdd:pfam07731   14 SGNFRRNDWAINGLLFpPNTNVITLPYGTVVEWVLQNTTT--GVHPFHLHGHSF-QVLGRGGGPwpeedpktynlvdpvr 90

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*..
gi 301615846  1009 -DVYDLFPGTFKTVEMIARVPGTWLLHCHVTDHIHAGMEVLYTVLEK 1054
Cdd:pfam07731   91 rDTVQVPPGGWVAIRFRADNPGVWLFHCHILWHLDQGMMGQFVVRPG 137
CuRO_2_FV_like cd14453
The second cupredoxin domain of coagulation factor V and similar proteins; Factor V is an ...
 909-1045 4.97e-14

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: 69.50  E-value: 4.97e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 301615846  909 KRFALLFLIFDENESWYlDENIKTYSLhpdqvqkededfiesnkMHGINGKLYANLEGLTMHVGDKIYWHLIGLGNEADI 988
Cdd:cd14453     2 KEYVLMFGVFDENKSWY-KQNASVDSV-----------------KYTINGYTNGTLPDVSICAYDHVSWHLLGMSSEPEL 63

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 301615846  989 HTMHIHahsftyvrGATFHSDVY-----DLFPGTFKTVEMIARVPGTWLLHCHVTDHIHAGM 1045
Cdd:cd14453    64 FSVHFN--------GQVLEQNGHkvsavGLVSGSSTTASMTVVHTGRWLISSLIMKHLQAGM 117
CuRO_3_LCC_like cd04207
Cupredoxin domain 3 of laccase-like multicopper oxidases; including laccase, CueO, spore coat ...
 956-1050 6.16e-12

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: 64.02  E-value: 6.16e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 301615846  956 INGK----LYANLEGLTMHVGDKIYWHLIGLGNEADIHTMHIHAHSFTYVRGATFHS------------DVYDLFPGTFK 1019
Cdd:cd04207    22 INGMpfkeGDANTDIFSVEAGDVVEIVLINAGNHDMQHPFHLHGHSFWVLGSGGGPFdaplnltnppwrDTVLVPPGGWV 101

                          90       100       110
                  ....*....|....*....|....*....|.
gi 301615846 1020 TVEMIARVPGTWLLHCHVTDHIHAGMEVLYT 1050
Cdd:cd04207   102 VIRFKADNPGVWMLHCHILEHEDAGMMTVFE 132
CuRO_1_2DMCO_NIR_like_2 cd14449
The cupredoxin domain 1 of a two-domain laccase related to nitrite reductase; The two-domain ...
 96-200 4.64e-11

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


Pssm-ID: 259991 [Multi-domain]  Cd Length: 135  Bit Score: 61.51  E-value: 4.64e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 301615846   96 GPILKAEIGDIIIVHLKNFASRPYSIHPHGVQYTKENEGALYPDNassghkddAIEPGQSYTYRWEAvseQGPTVQDEDC 175
Cdd:cd14449    29 GPVIEVREGDTLKILFRNTLDVPASLHPHGVDYTTASDGTGMNAS--------IVAPGDTRIYTWRT---HGGYRRADGS 97

                          90       100       110
                  ....*....|....*....|....*....|....*
gi 301615846  176 I------TRIYHSHI----DGPKDVSSGLIGPLII 200
Cdd:cd14449    98 WaegtagYWHYHDHVfgteHGTEGLSRGLYGALIV 132
Cu-oxidase_3 pfam07732
Multicopper oxidase; This entry contains many divergent copper oxidase-like domains that are ...
 95-200 8.07e-11

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


Pssm-ID: 462247 [Multi-domain]  Cd Length: 119  Bit Score: 60.34  E-value: 8.07e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 301615846    95 LGPILKAEIGDIIIVHLKNFASRPYSIHPHGVQYTKENegalYPDNAsSGHKDDAIEPGQSYTYRWEAVSEQGptvqded 174
Cdd:pfam07732   25 PGPTIRVREGDTVVVNVTNNLDEPTSIHWHGLQQRGTP----WMDGV-PGVTQCPIPPGQSFTYRFQVKQQAG------- 92

                           90       100
                   ....*....|....*....|....*.
gi 301615846   175 ciTRIYHSHIDGPKdvSSGLIGPLII 200
Cdd:pfam07732   93 --TYWYHSHTSGQQ--AAGLAGAIII 114
CuRO_1_CumA_like cd13861
The first cupredoxin domain of CumA like multicopper oxidase; This multicopper oxidase (MCO) ...
 96-200 1.10e-10

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: 59.94  E-value: 1.10e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 301615846   96 GPILKAEIGDIIIVHLKNFASRPYSIHPHGVQytkenegalyPDNASSG---HKDDAIEPGQSYTYRWEAVseqgptvqd 172
Cdd:cd13861    31 GPELRVRQGDTLRVRLTNRLPEPTTIHWHGLR----------LPNAMDGvpgLTQPPVPPGESFTYEFTPP--------- 91

                          90       100
                  ....*....|....*....|....*...
gi 301615846  173 eDCITRIYHSHIDGPKDVSSGLIGPLII 200
Cdd:cd13861    92 -DAGTYWYHPHVGSQEQLDRGLYGPLIV 118
CuRO_D1_2dMcoN_like cd13859
The first cupredoxin domain of bacterial two domain multicopper oxidase McoN and similar ...
 96-200 1.14e-10

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: 60.18  E-value: 1.14e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 301615846   96 GPILKAEIGDIIIVHLKNFASRPYSIHPHGVQYTK--ENEGAlypdnasSGHKDDAIEPGQSYTYRWEAvseqgptvqdE 173
Cdd:cd13859    31 GPLIHVKEGDDLVVHVTNNTTLPHTIHWHGVLQMGswKMDGV-------PGVTQPAIEPGESFTYKFKA----------E 93

                          90       100
                  ....*....|....*....|....*...
gi 301615846  174 DCITRIYHSHIDGPKDVS-SGLIGPLII 200
Cdd:cd13859    94 RPGTLWYHCHVNVNEHVGmRGMWGPLIV 121
SufI COG2132
Multicopper oxidase with three cupredoxin domains (includes cell division protein FtsP and ...
 95-200 1.33e-10

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: 64.57  E-value: 1.33e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 301615846   95 LGPILKAEIGDIIIVHLKNFASRPYSIHPHGvqytkenegaLYPDNASSGHKDDAIEPGQSYTYRWEAvsEQGPTvqded 174
Cdd:COG2132    43 PGPTIRVREGDRVRVRVTNRLPEPTTVHWHG----------LRVPNAMDGVPGDPIAPGETFTYEFPV--PQPAG----- 105

                          90       100
                  ....*....|....*....|....*...
gi 301615846  175 ciTRIYHSHIDG--PKDVSSGLIGPLII 200
Cdd:COG2132   106 --TYWYHPHTHGstAEQVYRGLAGALIV 131
CuRO_3_CopA cd13896
The third cupredoxin domain of CopA copper resistance protein family; CopA is a multicopper ...
 955-1045 2.58e-10

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


Pssm-ID: 259963 [Multi-domain]  Cd Length: 115  Bit Score: 58.81  E-value: 2.58e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 301615846  955 GINGKLYANLEGLTMHVGDKIywhLIGLGNEADI-HTMHIHAHSFTYVRGATFHS---DVYDLFPGTFKTVEMIARVPGT 1030
Cdd:cd13896    18 TINGKAYPDADPLRVREGERV---RIVFVNDTMMaHPMHLHGHFFQVENGNGEYGprkDTVLVPPGETVSVDFDADNPGR 94

                          90
                  ....*....|....*
gi 301615846 1031 WLLHCHVTDHIHAGM 1045
Cdd:cd13896    95 WAFHCHNLYHMEAGM 109
CuRO_1_2DMCO_NIR_like cd11024
The cupredoxin domain 1 of a two-domain laccase related to nitrite reductase; The two-domain ...
 96-200 3.00e-10

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


Pssm-ID: 259910 [Multi-domain]  Cd Length: 119  Bit Score: 58.82  E-value: 3.00e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 301615846   96 GPILKAEIGDIIIVHLKNFASRPYSIHPHGVQYTKENEGALYPdnassghkddaIEPGQSYTYRWEAvseqgptvqdEDC 175
Cdd:cd11024    32 GPTLRATEGDLVRIHFINTGDHPHTIHFHGIHDAAMDGTGLGP-----------IMPGESFTYEFVA----------EPA 90

                          90       100
                  ....*....|....*....|....*.
gi 301615846  176 ITRIYHSHIDGPKD-VSSGLIGPLII 200
Cdd:cd11024    91 GTHLYHCHVQPLKEhIAMGLYGAFIV 116
CuRO_1_Diphenol_Ox cd13857
The first cupredoxin domain of fungal laccase, diphenol oxidase; Diphenol oxidase belongs to ...
 96-200 3.30e-10

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


Pssm-ID: 259926 [Multi-domain]  Cd Length: 119  Bit Score: 58.42  E-value: 3.30e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 301615846   96 GPILKAEIGDIIIVHLKNFASRPYSIHPHGVQytkeNEGALYPDNAsSGHKDDAIEPGQSYTYRWEAVSEQGptvqdedc 175
Cdd:cd13857    30 GPLIEANQGDRIVVHVTNELDEPTSIHWHGLF----QNGTNWMDGT-AGITQCPIPPGGSFTYNFTVDGQYG-------- 96

                          90       100
                  ....*....|....*....|....*
gi 301615846  176 iTRIYHSHIDGPKdvSSGLIGPLII 200
Cdd:cd13857    97 -TYWYHSHYSTQY--ADGLVGPLIV 118
CuRO_1_LCC_like cd04206
Cupredoxin domain 1 of laccase-like multicopper oxidases; including laccase, CueO, spore coat ...
 448-559 7.94e-10

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: 57.68  E-value: 7.94e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 301615846  448 GILGPVMIAQVGDSMKVTFKNK-ASRPYSIQAHGVSYSKNMEGasyrtgnltndDPSPG---SHVAPGDTFTYEWEVSSA 523
Cdd:cd04206    27 QFPGPTIRVKEGDTVEVTVTNNlPNEPTSIHWHGLRQPGTNDG-----------DGVAGltqCPIPPGESFTYRFTVDDQ 95

                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 301615846  524 VGStnqnlnclvWLYFSSVDAikDTNSGLVGPLLIC 559
Cdd:cd04206    96 AGT---------FWYHSHVGG--QRADGLYGPLIVE 120
CuRO_3_CumA_like cd13906
The third cupredoxin domain of CumA like multicopper oxidase; This multicopper oxidase (MCO) ...
 967-1045 2.67e-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: 2.67e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 301615846  967 LTMHVGDkiyWHLIGLGNEAD-IHTMHIHAHSFTYVR--GAT----FHSDVYDLFPGTFKTVEMIARVPGTWLLHCHVTD 1039
Cdd:cd13906    49 ATLKRGR---SYVLRLVNETAfLHPMHLHGHFFRVLSrnGRPvpepFWRDTVLLGPKETVDIAFVADNPGDWMFHCHILE 125


                  ....*.
gi 301615846 1040 HIHAGM 1045
Cdd:cd13906   126 HQETGM 131
SufI COG2132
Multicopper oxidase with three cupredoxin domains (includes cell division protein FtsP and ...
 953-1045 4.66e-09

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


Pssm-ID: 441735 [Multi-domain]  Cd Length: 423  Bit Score: 59.95  E-value: 4.66e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 301615846  953 MHGINGKLYANLE-GLTMHVGDKIYWHLIGLGNEAdiHTMHIHAHSFTYVR---GATFHS---DVYDLFPGtfKTVEMIA 1025
Cdd:COG2132   317 VWTINGKAFDPDRpDLTVKLGERERWTLVNDTMMP--HPFHLHGHQFQVLSrngKPPPEGgwkDTVLVPPG--ETVRILF 392

                          90       100
                  ....*....|....*....|...
gi 301615846 1026 R---VPGTWLLHCHVTDHIHAGM 1045
Cdd:COG2132   393 RfdnYPGDWMFHCHILEHEDAGM 415
CuRO_1_Abr2_like cd13850
The first cupredoxin domain of a group of fungal Laccases similar to Abr2 from Aspergillus ...
 96-200 5.04e-09

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: 55.00  E-value: 5.04e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 301615846   96 GPILKAEIGDIIIVHLKNFASRPYSIHPHGV--QYTKENEGAlyPdnassGHKDDAIEPGQSYTYRWEAVSEQGptvqde 173
Cdd:cd13850    28 GPPIILDEGDEVEILVTNNLPVNTTIHFHGIlqRGTPWSDGV--P-----GVTQWPIQPGGSFTYRWKAEDQYG------ 94

                          90       100
                  ....*....|....*....|....*..
gi 301615846  174 dciTRIYHSHIDGpkDVSSGLIGPLII 200
Cdd:cd13850    95 ---LYWYHSHYRG--YYMDGLYGPIYI 116
CuRO_3_LCC_like cd04207
Cupredoxin domain 3 of laccase-like multicopper oxidases; including laccase, CueO, spore coat ...
 249-353 3.21e-08

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


Pssm-ID: 259870 [Multi-domain]  Cd Length: 132  Bit Score: 53.23  E-value: 3.21e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 301615846  249 NDTDFQESNKMHSINGYMF----GNLPGLSMCEGEHIHWYLFGMGNEADIHSAYFHG---QVL-------------TFQM 308
Cdd:cd04207     9 SQTGAPDGTTRWVINGMPFkegdANTDIFSVEAGDVVEIVLINAGNHDMQHPFHLHGhsfWVLgsgggpfdaplnlTNPP 88

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
gi 301615846  309 YRvDTLSLFPATMIEGHMVTKNPGKWLLTCQVNDHLAGGMQAIYE 353
Cdd:cd04207    89 WR-DTVLVPPGGWVVIRFKADNPGVWMLHCHILEHEDAGMMTVFE 132
CuRO_1_2DMCO_NIR_like_2 cd14449
The cupredoxin domain 1 of a two-domain laccase related to nitrite reductase; The two-domain ...
 451-519 4.05e-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: 53.04  E-value: 4.05e-08
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 301615846  451 GPVMIAQVGDSMKVTFKNKASRPYSIQAHGVSYSKNMEGASyrtgnltnddpSPGSHVAPGDTFTYEWE 519
Cdd:cd14449    29 GPVIEVREGDTLKILFRNTLDVPASLHPHGVDYTTASDGTG-----------MNASIVAPGDTRIYTWR 86
CuRO_1_McoP_like cd13852
The first cupredoxin domain of multicopper oxidase McoP and similar proteins; This family ...
 95-200 6.17e-08

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: 51.91  E-value: 6.17e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 301615846   95 LGPILKAEIGDIIIVHLKNFASRPYSIHPHGvqytkenegaLYPDNASSGHKDDAIEPGQSYTYRWEAVSEQGptvqded 174
Cdd:cd13852    23 LGPILRLRKGQKVRITFKNNLPEPTIIHWHG----------LHVPAAMDGHPRYAIDPGETYVYEFEVLNRAG------- 85

                          90       100
                  ....*....|....*....|....*...
gi 301615846  175 ciTRIYHSHIDG--PKDVSSGLIGPLII 200
Cdd:cd13852    86 --TYWYHPHPHGltAKQVYRGLAGLFLV 111
CuRO_1_MaLCC_like cd13854
The first cupredoxin domain of the fungal laccases similar to Ma-LCC from Melanocarpus ...
 96-200 6.35e-08

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: 52.24  E-value: 6.35e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 301615846   96 GPILKAEIGDIIIVHLKNfaSRPY---SIHPHGVQ--YTKENEGAlypdnasSGHKDDAIEPGQSYTYRWEAvSEQGptv 170
Cdd:cd13854    33 GPLIEANWGDTIEVTVIN--KLQDngtSIHWHGIRqlNTNWQDGV-------PGVTECPIAPGDTRTYRFRA-TQYG--- 99

                          90       100       110
                  ....*....|....*....|....*....|
gi 301615846  171 qdedciTRIYHSHIDGpkDVSSGLIGPLII 200
Cdd:cd13854   100 ------TSWYHSHYSA--QYGDGVVGPIVI 121
CuRO_1_2dMco_1 cd13860
The first cupredoxin domain of bacteria two domain multicopper oxidase; This subfamily ...
 96-200 1.07e-07

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


Pssm-ID: 259929 [Multi-domain]  Cd Length: 119  Bit Score: 51.43  E-value: 1.07e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 301615846   96 GPILKAEIGDIIIVHLKNFASRPYSIHPHGVQYTKENEGAlypdnasSGHKDDAIEPGQSYTYRwEAVSEQGptvqdedc 175
Cdd:cd13860    31 GPTIEVTEGDRVRILVTNELPEPTTVHWHGLPVPNGMDGV-------PGITQPPIQPGETFTYE-FTAKQAG-------- 94

                          90       100
                  ....*....|....*....|....*
gi 301615846  176 iTRIYHSHIDGPKDVSSGLIGPLII 200
Cdd:cd13860    95 -TYMYHSHVDEAKQEDMGLYGAFIV 118
CuRO_3_Tv-LCC_like cd13903
The third cupredoxin domain of the fungal laccases similar to Tv-LCC from Trametes Versicolor; ...
 983-1047 2.53e-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: 51.13  E-value: 2.53e-07
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 301615846  983 GNEADIHTMHIHAHSFTYVRGATFHS---------DVYDL-FPGTFKTVEMIARVPGTWLLHCHVTDHIHAGMEV 1047
Cdd:cd13903    67 GAIGGPHPFHLHGHAFSVVRSAGSNTynyvnpvrrDVVSVgTPGDGVTIRFVTDNPGPWFLHCHIDWHLEAGLAV 141
CuRO_1_LCC_like cd04206
Cupredoxin domain 1 of laccase-like multicopper oxidases; including laccase, CueO, spore coat ...
 801-895 2.83e-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: 50.36  E-value: 2.83e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 301615846  801 GILGPLLIARTHEKVKIVFKN-MASRPYSIYAHGVKT------DGPVVQT----EPGQTQTYIWKIPERSGpgyhedvnc 869
Cdd:cd04206    27 QFPGPTIRVKEGDTVEVTVTNnLPNEPTSIHWHGLRQpgtndgDGVAGLTqcpiPPGESFTYRFTVDDQAG--------- 97

                          90       100
                  ....*....|....*....|....*.
gi 301615846  870 vTWAYYSTVDQvkDTYSGLIGPLVIC 895
Cdd:cd04206    98 -TFWYHSHVGG--QRADGLYGPLIVE 120
PLN02191 PLN02191
L-ascorbate oxidase
 96-222 5.36e-07

L-ascorbate oxidase


Pssm-ID: 177843 [Multi-domain]  Cd Length: 574  Bit Score: 53.48  E-value: 5.36e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 301615846   96 GPILKAEIGDIIIVHLKN-FASRPYSIHPHGVQytkeNEGALYPDNAsSGHKDDAIEPGQSYTYRWeAVSEQGptvqded 174
Cdd:PLN02191   53 GPTIDAVAGDTIVVHLTNkLTTEGLVIHWHGIR----QKGSPWADGA-AGVTQCAINPGETFTYKF-TVEKPG------- 119

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*....
gi 301615846  175 ciTRIYHSHIDGPKdvSSGLIGPLIICKKGSINavEQHKYK-EFVLMFS 222
Cdd:PLN02191  120 --THFYHGHYGMQR--SAGLYGSLIVDVAKGPK--ERLRYDgEFNLLLS 162
CuRO_3_MCO_like_3 cd13909
The third cupredoxin domain of uncharacterized multicopper oxidase; Multicopper Oxidases (MCOs) ...
 989-1045 6.13e-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: 259976 [Multi-domain]  Cd Length: 137  Bit Score: 49.82  E-value: 6.13e-07
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 301615846  989 HTMHIHAHSFTYV--RGAT--FHsDVYDLFPGTFKTVEMIARVPGTWLLHCHVTDHIHAGM 1045
Cdd:cd13909    71 HGMHLHGHHFRAIlpNGALgpWR-DTLLMDRGETREIAFVADNPGDWLLHCHMLEHAAAGM 130
CuRO_1_2DMCO_NIR_like_2 cd14449
The cupredoxin domain 1 of a two-domain laccase related to nitrite reductase; The two-domain ...
 804-894 7.73e-07

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


Pssm-ID: 259991 [Multi-domain]  Cd Length: 135  Bit Score: 49.57  E-value: 7.73e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 301615846  804 GPLLIARTHEKVKIVFKNMASRPYSIYAHGVK-------TDGPVVQTEPGQTQTYIWK--IPERSGPGYHEDVNCVTWAY 874
Cdd:cd14449    29 GPVIEVREGDTLKILFRNTLDVPASLHPHGVDyttasdgTGMNASIVAPGDTRIYTWRthGGYRRADGSWAEGTAGYWHY 108

                          90       100
                  ....*....|....*....|....
gi 301615846  875 YSTV----DQVKDTYSGLIGPLVI 894
Cdd:cd14449   109 HDHVfgteHGTEGLSRGLYGALIV 132
CuRO_1_CumA_like cd13861
The first cupredoxin domain of CumA like multicopper oxidase; This multicopper oxidase (MCO) ...
 448-558 9.24e-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: 48.77  E-value: 9.24e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 301615846  448 GILGPVMIAQVGDSMKVTFKNKASRPYSIQAHGVSYSKNMEGasyrTGNLTNDdpspgsHVAPGDTFTYEWEVSSAvGSt 527
Cdd:cd13861    28 QVPGPELRVRQGDTLRVRLTNRLPEPTTIHWHGLRLPNAMDG----VPGLTQP------PVPPGESFTYEFTPPDA-GT- 95

                          90       100       110
                  ....*....|....*....|....*....|.
gi 301615846  528 nqnlnclvWLYFSSVDAIKDTNSGLVGPLLI 558
Cdd:cd13861    96 --------YWYHPHVGSQEQLDRGLYGPLIV 118
CuRO_1_2DMCO_NIR_like cd11024
The cupredoxin domain 1 of a two-domain laccase related to nitrite reductase; The two-domain ...
 972-1045 9.28e-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: 48.81  E-value: 9.28e-07
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 301615846  972 GDKIYWHLIGLGNeaDIHTMHIHAHSFTYVRGATFHsdvyDLFPGTFKTVEMIARVPGTWLLHCHV---TDHIHAGM 1045
Cdd:cd11024    40 GDLVRIHFINTGD--HPHTIHFHGIHDAAMDGTGLG----PIMPGESFTYEFVAEPAGTHLYHCHVqplKEHIAMGL 110
CuRO_1_2DMCO_NIR_like cd11024
The cupredoxin domain 1 of a two-domain laccase related to nitrite reductase; The two-domain ...
 451-518 1.02e-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: 48.42  E-value: 1.02e-06
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 301615846  451 GPVMIAQVGDSMKVTFKNKASRPYSIQAHGVSYSKnmegasyrtgnltNDDPSPGShVAPGDTFTYEW 518
Cdd:cd11024    32 GPTLRATEGDLVRIHFINTGDHPHTIHFHGIHDAA-------------MDGTGLGP-IMPGESFTYEF 85
CuRO_1_Fet3p cd13851
The first Cupredoxin domain of multicopper oxidase Fet3P; Fet3p catalyzes the ferroxidase ...
 97-200 2.42e-06

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: 47.65  E-value: 2.42e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 301615846   97 PILKAEIGDIIIVHLKN-FASRPYSIHPHGVQYTkeneGALYPDNAsSGHKDDAIEPGQSYTYRWEAVSEQGptvqdedc 175
Cdd:cd13851    32 PPIEVNKGDTVVIHATNsLGDQPTSLHFHGLFQN----GTNYMDGP-VGVTQCPIPPGQSFTYEFTVDTQVG-------- 98

                          90       100
                  ....*....|....*....|....*
gi 301615846  176 iTRIYHSHIDGpkDVSSGLIGPLII 200
Cdd:cd13851    99 -TYWYHSHDGG--QYPDGLRGPFII 120
CuRO_1_AAO cd13845
The first cupredoxin domain of plant Ascorbate oxidase; Ascorbate oxidase catalyzes the ...
 96-200 2.69e-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: 47.44  E-value: 2.69e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 301615846   96 GPILKAEIGDIIIVHLKN-FASRPYSIHPHGVQytkeNEGALYPDNASSGHKdDAIEPGQSYTYRWeAVSEQGptvqded 174
Cdd:cd13845    30 GPTIRATAGDTIVVELENkLPTEGVAIHWHGIR----QRGTPWADGTASVSQ-CPINPGETFTYQF-VVDRPG------- 96

                          90       100
                  ....*....|....*....|....*.
gi 301615846  175 ciTRIYHSHIDGPKdvSSGLIGPLII 200
Cdd:cd13845    97 --TYFYHGHYGMQR--SAGLYGSLIV 118
CuRO_3_Fet3p cd13899
The third Cupredoxin domain of multicopper oxidase Fet3p; Fet3p catalyzes the ferroxidase ...
 984-1045 3.31e-06

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: 48.02  E-value: 3.31e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 301615846  984 NEADIHTMHIHAHSFTYV-RGATFHSDVYD-----------------LFPGTFKTVEMIARVPGTWLLHCHVTDHIHAGM 1045
Cdd:cd13899    73 WDAGKHPFHLHGHKFQVVqRSPDVASDDPNppinefpenpmrrdtvmVPPGGSVVIRFRADNPGVWFFHCHIEWHLEAGL 152
PLN02191 PLN02191
L-ascorbate oxidase
 986-1049 8.67e-06

L-ascorbate oxidase


Pssm-ID: 177843 [Multi-domain]  Cd Length: 574  Bit Score: 49.63  E-value: 8.67e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 301615846  986 ADIHTMHIHAHSFtYVRG------------ATFH------SDVYDLFPGTFKTVEMIARVPGTWLLHCHVTDHIHAGMEV 1047
Cdd:PLN02191  464 SEIHPWHLHGHDF-WVLGygdgkfkpgideKTYNlknpplRNTAILYPYGWTAIRFVTDNPGVWFFHCHIEPHLHMGMGV 542


                  ..
gi 301615846 1048 LY 1049
Cdd:PLN02191  543 VF 544
CuRO_1_2dMco_1 cd13860
The first cupredoxin domain of bacteria two domain multicopper oxidase; This subfamily ...
 451-558 9.23e-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: 46.04  E-value: 9.23e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 301615846  451 GPVMIAQVGDSMKVTFKNKASRPYSIQAHGVSYSKNMEGASYRTGNltnddpspgsHVAPGDTFTYEWEVSSAvGStnqn 530
Cdd:cd13860    31 GPTIEVTEGDRVRILVTNELPEPTTVHWHGLPVPNGMDGVPGITQP----------PIQPGETFTYEFTAKQA-GT---- 95

                          90       100
                  ....*....|....*....|....*...
gi 301615846  531 lnclvWLYFSSVDAIKDTNSGLVGPLLI 558
Cdd:cd13860    96 -----YMYHSHVDEAKQEDMGLYGAFIV 118
Cu-oxidase_3 pfam07732
Multicopper oxidase; This entry contains many divergent copper oxidase-like domains that are ...
 427-558 1.15e-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: 45.70  E-value: 1.15e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 301615846   427 VEYTDATFTTRKQRSKdeehLGI----LGPVMIAQVGDSMKVTFKNKASRPYSIQAHGVSYSKN--MEGASYrtgnLTND 500
Cdd:pfam07732    2 VTYGTVSPLGGTRQAV----IGVngqfPGPTIRVREGDTVVVNVTNNLDEPTSIHWHGLQQRGTpwMDGVPG----VTQC 73

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 301615846   501 dpspgsHVAPGDTFTYEWEVSSAVGSTnqnlnclvWlYFSSVDAIKdtNSGLVGPLLI 558
Cdd:pfam07732   74 ------PIPPGQSFTYRFQVKQQAGTY--------W-YHSHTSGQQ--AAGLAGAIII 114
CuRO_1_CuNIR_like cd04201
Cupredoxin domain 1 of Copper-containing nitrite reductase and two-domain laccase; ...
 967-1054 1.39e-05

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


Pssm-ID: 259864 [Multi-domain]  Cd Length: 120  Bit Score: 45.56  E-value: 1.39e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 301615846  967 LTMHVGDKIYWHLIGLGNEADIHTMHIH-AHSFTYVRGATFHSdvydlfPGTFKTVEMIARVPGTWLLHCHVTD---HIH 1042
Cdd:cd04201    35 LRVREGDTVELHFSNNPSSTMPHNIDFHaATGAGGGAGATFIA------PGETSTFSFKATQPGLYVYHCAVAPvpmHIA 108

                          90
                  ....*....|..
gi 301615846 1043 AGMEVLYTVLEK 1054
Cdd:cd04201   109 NGMYGLILVEPK 120
CuRO_3_AAO cd13893
The third cupredoxin domain of plant Ascorbate oxidase; Ascorbate oxidase catalyzes the ...
 984-1049 1.96e-05

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: 45.87  E-value: 1.96e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 301615846  984 NEADIHTMHIHAHSF------TYVRGATFHSDVYDL-----------FPGTFKTVEMIARVPGTWLLHCHVTDHIHAGME 1046
Cdd:cd13893    62 NASEQHPWHLHGHDFwvlgygLGGFDPAADPSSLNLvnppmrntvtiFPYGWTALRFKADNPGVWAFHCHIEWHFHMGMG 141


                  ...
gi 301615846 1047 VLY 1049
Cdd:cd13893   142 VVF 144
CuRO_1_McoC_like cd13855
The first cupredoxin domain of a multicopper oxidase McoC and similar proteins; This family ...
 804-894 1.97e-05

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


Pssm-ID: 259924 [Multi-domain]  Cd Length: 121  Bit Score: 45.16  E-value: 1.97e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 301615846  804 GPLLIARTHEKVKIVFKNMASRPYSIYAHGV----KTDG-PVVQTEPGQTQTYIWKIPERSGPGYhedvncvtW----AY 874
Cdd:cd13855    32 GPLIEVFEGDTVEITFRNRLPEPTTVHWHGLpvppDQDGnPHDPVAPGNDRVYRFTLPQDSAGTY--------WyhphPH 103

                          90       100
                  ....*....|....*....|
gi 301615846  875 YSTVDQVkdtYSGLIGPLVI 894
Cdd:cd13855   104 GHTAEQV---YRGLAGAFVV 120
ascorbase TIGR03388
L-ascorbate oxidase, plant type; Members of this protein family are the copper-containing ...
 96-200 2.28e-05

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


Pssm-ID: 274555 [Multi-domain]  Cd Length: 541  Bit Score: 48.21  E-value: 2.28e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 301615846    96 GPILKAEIGDIIIVHLKN-FASRPYSIHPHGVQytkeNEGALYPDNAsSGHKDDAIEPGQSYTYRWeAVSEQGptvqded 174
Cdd:TIGR03388   31 GPTIRAQAGDTIVVELTNkLHTEGVVIHWHGIR----QIGTPWADGT-AGVTQCAINPGETFIYNF-VVDRPG------- 97

                           90       100
                   ....*....|....*....|....*.
gi 301615846   175 ciTRIYHSHIDGPKdvSSGLIGPLII 200
Cdd:TIGR03388   98 --TYFYHGHYGMQR--SAGLYGSLIV 119
CuRO_3_MCO_like_2 cd13908
The third cupredoxin domain of uncharacterized multicopper oxidase; Multicopper Oxidases (MCOs) ...
 987-1049 2.39e-05

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: 44.75  E-value: 2.39e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 301615846  987 DIHTMHIHAHSFTYVR-----GATFHSDVYDLFPGTFKTVEMIARVPGTWLLHCHVTDHIHAGMEVLY 1049
Cdd:cd13908    53 DAHPMHLHRHTFEVTRidgkpTSGLRKDVVMLGGYQRVEVDFVADNPGLTLFHCHQQLHMDYGFMALF 120
CuRO_1_LCC_plant cd13849
The first cupredoxin domain of plant laccases; Laccase is a blue multicopper oxidase (MCO) ...
 96-185 2.68e-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: 44.56  E-value: 2.68e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 301615846   96 GPILKAEIGDIIIVHLKNFASRPYSIHPHGVQ--YTKENEGALYPDNASsghkddaIEPGQSYTYRWEAVSEQGptvqde 173
Cdd:cd13849    28 GPTIRVHEGDTVVVNVTNRSPYNITIHWHGIRqlRSGWADGPAYITQCP-------IQPGQSYTYRFTVTGQEG------ 94

                          90
                  ....*....|..
gi 301615846  174 dciTRIYHSHID 185
Cdd:cd13849    95 ---TLWWHAHIS 103
CuRO_1_tcLCC2_insect_like cd13858
The first cupredoxin domain of insect laccases similar to laccase 2 in Tribolium castaneum; ...
 96-200 3.00e-05

The first cupredoxin domain of 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 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: 259927 [Multi-domain]  Cd Length: 105  Bit Score: 44.07  E-value: 3.00e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 301615846   96 GPILKAEIGDIIIVHLKN-FASRPYSIHPHGvQYTKENegalyPdnassgHKDDA-------IEPGQSYTYRWEAvSEQG 167
Cdd:cd13858    16 GPSIEVCEGDTVVVDVKNrLPGESTTIHWHG-IHQRGT-----P------YMDGVpmvtqcpILPGQTFRYKFKA-DPAG 82

                          90       100       110
                  ....*....|....*....|....*....|...
gi 301615846  168 ptvqdedciTRIYHSHIDGpkDVSSGLIGPLII 200
Cdd:cd13858    83 ---------THWYHSHSGT--QRADGLFGALIV 104
CuRO_3_MaLCC_like cd13901
The third cupredoxin domain of the fungal laccases similar to Ma-LCC from Melanocarpus ...
 989-1045 3.05e-05

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: 45.29  E-value: 3.05e-05
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 301615846  989 HTMHIHAHSFtYVRGA---TFHS-------------DVYDLFPGTFKTVEMIARVPGTWLLHCHVTDHIHAGM 1045
Cdd:cd13901    81 HPIHLHGHDF-YILAQgtgTFDDdgtilnlnnpprrDVAMLPAGGYLVIAFKTDNPGAWLMHCHIAWHASGGL 152
CuRO_1_CuNIR cd11020
Cupredoxin domain 1 of Copper-containing nitrite reductase; Copper-containing nitrite ...
 966-1045 3.12e-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: 44.51  E-value: 3.12e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 301615846  966 GLTMHV--GDKIYWHLIGLGNEADIHTMHIHAhsfTYVRGATFHSDVYdlfPGTFKTVEMIARVPGTWLLHC---HVTDH 1040
Cdd:cd11020    32 GPVIRVreGDTVELTLTNPGTNTMPHSIDFHA---ATGPGGGEFTTIA---PGETKTFSFKALYPGVFMYHCataPVLMH 105


                  ....*
gi 301615846 1041 IHAGM 1045
Cdd:cd11020   106 IANGM 110
CuRO_1_Tv-LCC_like cd13856
The first cupredoxin domain of fungal laccases similar to Tv-LCC from Trametes versicolor; ...
 94-200 5.58e-05

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


Pssm-ID: 259925 [Multi-domain]  Cd Length: 125  Bit Score: 43.87  E-value: 5.58e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 301615846   94 HLGPILKAEIGDIIIVHLKNFAS-----RPYSIHPHGVQYTKENegalYPDNASSGHKdDAIEPGQSYTYRWEAVSEQGp 168
Cdd:cd13856    28 FPGPLITANKGDTFRITVVNQLTdptmrRSTSIHWHGIFQHGTN----YADGPAFVTQ-CPIAPNHSFTYDFTAGDQAG- 101

                          90       100       110
                  ....*....|....*....|....*....|..
gi 301615846  169 tvqdedciTRIYHSHIDgpKDVSSGLIGPLII 200
Cdd:cd13856   102 --------TFWYHSHLS--TQYCDGLRGPLVI 123
Cu-oxidase pfam00394
Multicopper oxidase; Many of the proteins in this family contain multiple similar copies of ...
 915-1038 8.08e-05

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


Pssm-ID: 395317 [Multi-domain]  Cd Length: 146  Bit Score: 43.85  E-value: 8.08e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 301615846   915 FLIFDENESWYlDENIKTYSLHPDQVQKEDEDFIESNKMHGINGKLYANLEGLTMHVGDKIYWHLIGLGNEaDIHTMHIH 994
Cdd:pfam00394    1 EDYVITLSDWY-HKDAKDLEKELLASGKAPTDFPPVPDAVLINGKDGASLATLTVTPGKTYRLRIINVALD-DSLNFSIE 78

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|.
gi 301615846   995 AHSFTYVrGATFH------SDVYDLFPGTFKTVEMIA-RVPGTWLLHCHVT 1038
Cdd:pfam00394   79 GHKMTVV-EVDGVyvnpftVDSLDIFPGQRYSVLVTAnQDPGNYWIVASPN 128
ascorbase TIGR03388
L-ascorbate oxidase, plant type; Members of this protein family are the copper-containing ...
 983-1049 9.52e-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: 46.28  E-value: 9.52e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 301615846   983 GNEADIHTMHIHAHSFtYVRG---ATFHSDV----YDL-----------FPGTFKTVEMIARVPGTWLLHCHVTDHIHAG 1044
Cdd:TIGR03388  438 GNNSETHPWHLHGHDF-WVLGygeGKFRPGVdeksYNLknpplrntvviFPYGWTALRFVADNPGVWAFHCHIEPHLHMG 516


                   ....*
gi 301615846  1045 MEVLY 1049
Cdd:TIGR03388  517 MGVVF 521
CuRO_3_LCC_plant cd13897
The third cupredoxin domain of the plant laccases; Laccase is a blue multicopper oxidase (MCO) ...
 986-1051 1.17e-04

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


Pssm-ID: 259964 [Multi-domain]  Cd Length: 139  Bit Score: 43.02  E-value: 1.17e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 301615846  986 ADIHTMHIHAHSFtYVRGATF-----HSDV--YDLF-----------PGTFKTVEMIARVPGTWLLHCHVTDHIHAGMEV 1047
Cdd:cd13897    54 AENHPMHLHGFDF-YVVGRGFgnfdpSTDPatFNLVdpplrntvgvpRGGWAAIRFVADNPGVWFMHCHFERHTSWGMAT 132


                  ....
gi 301615846 1048 LYTV 1051
Cdd:cd13897   133 VFIV 136
CuRO_3_Tth-MCO_like cd13900
The third cupredoxin domain of the bacterial laccases similar to Tth-MCO from Thermus ...
 956-1045 1.28e-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: 1.28e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 301615846  956 INGKLYA-NLEGLTMHVGDKIYWHLIGLGNEAdiHTMHIHAHSFTYVRGatfhSDVYDLFPGTFKTV------EMIARVP 1028
Cdd:cd13900    22 INGKPFDpDRPDRTVRLGTVEEWTLINTSGED--HPFHIHVNPFQVVSI----NGKPGLPPVWRDTVnvpaggSVTIRTR 95

                          90       100
                  ....*....|....*....|..
gi 301615846 1029 -----GTWLLHCHVTDHIHAGM 1045
Cdd:cd13900    96 frdftGEFVLHCHILDHEDQGM 117
laccase TIGR03389
laccase, plant; Members of this protein family include the copper-containing enzyme laccase ...
 96-222 1.42e-04

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


Pssm-ID: 274556 [Multi-domain]  Cd Length: 539  Bit Score: 45.88  E-value: 1.42e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 301615846    96 GPILKAEIGDIIIVHLKNFASRPYSIHPHGV-QY-TKENEGALY----PdnassghkddaIEPGQSYTYRWEAVSEQGpt 169
Cdd:TIGR03389   33 GPTLYAREGDTVIVNVTNNVQYNVTIHWHGVrQLrNGWADGPAYitqcP-----------IQPGQSYVYNFTITGQRG-- 99

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....
gi 301615846   170 vqdedciTRIYHSHIDGPKdvsSGLIGPLIIC-KKGSINAVEQhKYKEFVLMFS 222
Cdd:TIGR03389  100 -------TLWWHAHISWLR---ATVYGAIVILpKPGVPYPFPK-PDREVPIILG 142
CuRO_1_McoC_like cd13855
The first cupredoxin domain of a multicopper oxidase McoC and similar proteins; This family ...
 96-200 2.06e-04

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


Pssm-ID: 259924 [Multi-domain]  Cd Length: 121  Bit Score: 42.08  E-value: 2.06e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 301615846   96 GPILKAEIGDIIIVHLKNFASRPYSIHPHGVQYTKENEGalypdnassgHKDDAIEPGQSYTYRWeavseqgpTVQDEDC 175
Cdd:cd13855    32 GPLIEVFEGDTVEITFRNRLPEPTTVHWHGLPVPPDQDG----------NPHDPVAPGNDRVYRF--------TLPQDSA 93

                          90       100
                  ....*....|....*....|....*..
gi 301615846  176 ITRIYHSHIDG--PKDVSSGLIGPLII 200
Cdd:cd13855    94 GTYWYHPHPHGhtAEQVYRGLAGAFVV 120
CuRO_3_McoC_like cd13902
The third cupredoxin domain of a multicopper oxidase McoC and similar proteins; This family ...
 953-1045 2.83e-04

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: 41.62  E-value: 2.83e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 301615846  953 MHGINGKLYA-NLEGLTMHVGDKIYWHLIglgNEADI-HTMHIHAHSFTYV--RGATFHS------DVYDLFPGTFKTVE 1022
Cdd:cd13902    20 MFLINGKTFDmNRIDFVAKVGEVEVWEVT---NTSHMdHPFHLHGTQFQVLeiDGNPQKPeyrawkDTVNLPPGEAVRIA 96

                          90       100
                  ....*....|....*....|...
gi 301615846 1023 MIARVPGTWLLHCHVTDHIHAGM 1045
Cdd:cd13902    97 TRQDDPGMWMYHCHILEHEDAGM 119
CuRO_1_LCC_like_3 cd13865
The second cupredoxin domain of uncharacterized multicopper oxidase; Multicopper Oxidases ...
 99-200 3.13e-04

The second 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 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: 259933 [Multi-domain]  Cd Length: 115  Bit Score: 41.53  E-value: 3.13e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 301615846   99 LKAEIGDIIIVHLKNFASRPYSIHPHGvqytkenegaLYPDNASSGHKDD---AIEPGQSYTYRWEAVsEQGptvqdedc 175
Cdd:cd13865    31 LRLTEGDRFDVELENRLDEPTTIHWHG----------LIPPNLQDGVPDVtqpPIPPGQSQRYDFPLV-QPG-------- 91

                          90       100
                  ....*....|....*....|....*
gi 301615846  176 iTRIYHSHIdgPKDVSSGLIGPLII 200
Cdd:cd13865    92 -TFWMHSHY--GLQEQKLLAAPLII 113
CuRO_1_CuNIR_like cd04201
Cupredoxin domain 1 of Copper-containing nitrite reductase and two-domain laccase; ...
 96-200 3.21e-04

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


Pssm-ID: 259864 [Multi-domain]  Cd Length: 120  Bit Score: 41.32  E-value: 3.21e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 301615846   96 GPILKAEIGDIIIVHLKNfasRPYSIHPHGVQYtkenegalypdNASSGHKDDA----IEPGQSYTYRWEAVSEQgptvq 171
Cdd:cd04201    32 GPMLRVREGDTVELHFSN---NPSSTMPHNIDF-----------HAATGAGGGAgatfIAPGETSTFSFKATQPG----- 92

                          90       100       110
                  ....*....|....*....|....*....|
gi 301615846  172 dedciTRIYHSHIDG-PKDVSSGLIGPLII 200
Cdd:cd04201    93 -----LYVYHCAVAPvPMHIANGMYGLILV 117
CuRO_D1_2dMcoN_like cd13859
The first cupredoxin domain of bacterial two domain multicopper oxidase McoN and similar ...
 451-520 3.28e-04

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


Pssm-ID: 259928 [Multi-domain]  Cd Length: 122  Bit Score: 41.69  E-value: 3.28e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 301615846  451 GPVMIAQVGDSMKVTFKNKASRPYSIQAHGVsysknmegasYRTGNLTNDDPSPGSH--VAPGDTFTYEWEV 520
Cdd:cd13859    31 GPLIHVKEGDDLVVHVTNNTTLPHTIHWHGV----------LQMGSWKMDGVPGVTQpaIEPGESFTYKFKA 92
CuRO_1_CueO_FtsP cd04232
The first Cupredoxin domain of the multicopper oxidase CueO, the cell division protein FtsP, ...
 94-200 3.67e-04

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: 41.40  E-value: 3.67e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 301615846   94 HLGPILKAEIGDIIIVHLKNFASRPYSIHPHGVQYTKENEGalypdnasSGHKddAIEPGQSYTYRWeavseqgpTVQDE 173
Cdd:cd04232    29 YLGPTIRVKKGDTVRINVTNNLDEETTVHWHGLHVPGEMDG--------GPHQ--PIAPGQTWSPTF--------TIDQP 90

                          90       100
                  ....*....|....*....|....*....
gi 301615846  174 DCiTRIYHSHIDG--PKDVSSGLIGPLII 200
Cdd:cd04232    91 AA-TLWYHPHTHGktAEQVYRGLAGLFII 118
CuRO_1_CumA_like cd13861
The first cupredoxin domain of CumA like multicopper oxidase; This multicopper oxidase (MCO) ...
 801-894 4.30e-04

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: 41.07  E-value: 4.30e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 301615846  801 GILGPLLIARTHEKVKIVFKNMASRPYSIYAHGV----KTDG--PVVQ--TEPGQTQTYIWKIPErsgPGyhedvncvTW 872
Cdd:cd13861    28 QVPGPELRVRQGDTLRVRLTNRLPEPTTIHWHGLrlpnAMDGvpGLTQppVPPGESFTYEFTPPD---AG--------TY 96

                          90       100
                  ....*....|....*....|..
gi 301615846  873 AYYSTVDQVKDTYSGLIGPLVI 894
Cdd:cd13861    97 WYHPHVGSQEQLDRGLYGPLIV 118
Cu-oxidase_2 pfam07731
Multicopper oxidase; This entry contains many divergent copper oxidase-like domains that are ...
 251-355 5.04e-04

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


Pssm-ID: 462246 [Multi-domain]  Cd Length: 138  Bit Score: 41.27  E-value: 5.04e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 301615846   251 TDFQESNKMHSINGYMFG-NLPGLSMCEGEHIHWYLFGMGNeaDIHSAYFHG---QVL----------TFQMYRV----- 311
Cdd:pfam07731   13 TSGNFRRNDWAINGLLFPpNTNVITLPYGTVVEWVLQNTTT--GVHPFHLHGhsfQVLgrgggpwpeeDPKTYNLvdpvr 90

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*
gi 301615846   312 -DTLSLFPATMIEGHMVTKNPGKWLLTCQVNDHLAGGMQAIYEVK 355
Cdd:pfam07731   91 rDTVQVPPGGWVAIRFRADNPGVWLFHCHILWHLDQGMMGQFVVR 135
CuRO_1_CopA cd13848
The first cupredoxin domain of CopA copper resistance protein family; CopA is a multicopper ...
 96-200 5.34e-04

The first 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 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 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: 259917 [Multi-domain]  Cd Length: 116  Bit Score: 40.73  E-value: 5.34e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 301615846   96 GPILKAEIGDIIIVHLKNFASRPYSIHPHGVqytkenegaLYPDN--ASSGHKDDAIEPGQSYTYRWeavseqgPTVQDE 173
Cdd:cd13848    30 GPLLRFKEGDDATIRVHNRLDEDTSIHWHGL---------LLPNDmdGVPGLSFPGIKPGETFTYRF-------PVRQSG 93

                          90       100
                  ....*....|....*....|....*..
gi 301615846  174 dciTRIYHSHIDGPKdvSSGLIGPLII 200
Cdd:cd13848    94 ---TYWYHSHSGLQE--QTGLYGPIII 115
CuRO_3_CumA_like cd13906
The third cupredoxin domain of CumA like multicopper oxidase; This multicopper oxidase (MCO) ...
 283-355 8.84e-04

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: 40.83  E-value: 8.84e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 301615846  283 WYLFGMGNEAD-IHSAYFHGQvlTFQM-----------YRVDTLSLFPATMIEGHMVTKNPGKWLLTCQVNDHLAGGMQA 350
Cdd:cd13906    56 SYVLRLVNETAfLHPMHLHGH--FFRVlsrngrpvpepFWRDTVLLGPKETVDIAFVADNPGDWMFHCHILEHQETGMMG 133


                  ....*
gi 301615846  351 IYEVK 355
Cdd:cd13906   134 VIRVA 138
Cupredoxin cd00920
Cupredoxin superfamily; Cupredoxins contain type I copper centers and are involved in ...
 965-1048 9.55e-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: 39.91  E-value: 9.55e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 301615846  965 EGLTMHVGDKIYWHLIGLGNEAdiHTMHIHAHSFTYV--RGATFHSDVYDLFPGTFKTVEMI--ARVPGTWLLHCHVTDH 1040
Cdd:cd00920    23 PVLVVPVGDTVRVQFVNKLGEN--HSVTIAGFGVPVVamAGGANPGLVNTLVIGPGESAEVTftTDQAGVYWFYCTIPGH 100


                  ....*...
gi 301615846 1041 IHAGMEVL 1048
Cdd:cd00920   101 NHAGMVGT 108
CuRO_1_McoP_like cd13852
The first cupredoxin domain of multicopper oxidase McoP and similar proteins; This family ...
 450-520 1.13e-03

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


Pssm-ID: 259921 [Multi-domain]  Cd Length: 114  Bit Score: 39.58  E-value: 1.13e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 301615846  450 LGPVMIAQVGDSMKVTFKNKASRPYSIQAHGVSYSKNMEGasyrtgnltnddpSPGSHVAPGDTFTYEWEV 520
Cdd:cd13852    23 LGPILRLRKGQKVRITFKNNLPEPTIIHWHGLHVPAAMDG-------------HPRYAIDPGETYVYEFEV 80
CuRO_1_Diphenol_Ox cd13857
The first cupredoxin domain of fungal laccase, diphenol oxidase; Diphenol oxidase belongs to ...
 451-558 1.27e-03

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: 39.55  E-value: 1.27e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 301615846  451 GPVMIAQVGDSMKVTFKNKASRPYSIQAHGVSysknMEGASYRTGnltnddpSPG---SHVAPGDTFTYEWEVSSAVGST 527
Cdd:cd13857    30 GPLIEANQGDRIVVHVTNELDEPTSIHWHGLF----QNGTNWMDG-------TAGitqCPIPPGGSFTYNFTVDGQYGTY 98

                          90       100       110
                  ....*....|....*....|....*....|..
gi 301615846  528 nqnlnclvWlYFSSVDAikdTNS-GLVGPLLI 558
Cdd:cd13857    99 --------W-YHSHYST---QYAdGLVGPLIV 118
CuRO_3_tcLLC2_insect_like cd13905
The third cupredoxin domain of the insect laccases similar to laccase 2 in Tribolium castaneum; ...
 1028-1056 1.41e-03

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: 40.74  E-value: 1.41e-03
                          10        20
                  ....*....|....*....|....*....
gi 301615846 1028 PGTWLLHCHVTDHIHAGMEVLYTVLEKKQ 1056
Cdd:cd13905   142 PGYWLLHCHIEFHLLEGMALVLKVGEPSD 170
SufI COG2132
Multicopper oxidase with three cupredoxin domains (includes cell division protein FtsP and ...
 449-520 1.54e-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: 42.23  E-value: 1.54e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 301615846  449 ILGPVMIAQVGDSMKVTFKNKASRPYSIQAHGVsysknmegasyRTGNlTNDDpSPGSHVAPGDTFTYEWEV 520
Cdd:COG2132    42 YPGPTIRVREGDRVRVRVTNRLPEPTTVHWHGL-----------RVPN-AMDG-VPGDPIAPGETFTYEFPV 100
Cu-oxidase pfam00394
Multicopper oxidase; Many of the proteins in this family contain multiple similar copies of ...
 221-350 2.21e-03

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: 39.61  E-value: 2.21e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 301615846   221 FSVIDENLSWYlDENINTFCTEPSSVDKNDTDFQESNKMHSINGYMFGNLPGLSMCEGEHIHWYLFgMGNEADIHSAYFH 300
Cdd:pfam00394    1 EDYVITLSDWY-HKDAKDLEKELLASGKAPTDFPPVPDAVLINGKDGASLATLTVTPGKTYRLRII-NVALDDSLNFSIE 78

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 301615846   301 GQVLTF--------QMYRVDTLSLFPATMIEGHMVTKN-PGKWLLTCQVN-DHLAGGMQA 350
Cdd:pfam00394   79 GHKMTVvevdgvyvNPFTVDSLDIFPGQRYSVLVTANQdPGNYWIVASPNiPAFDNGTAA 138
CuRO_3_MCO_like_3 cd13909
The third cupredoxin domain of uncharacterized multicopper oxidase; Multicopper Oxidases (MCOs) ...
 312-354 2.42e-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: 2.42e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|...
gi 301615846  312 DTLSLFPATMIEGHMVTKNPGKWLLTCQVNDHLAGGMQAIYEV 354
Cdd:cd13909    94 DTLLMDRGETREIAFVADNPGDWLLHCHMLEHAAAGMMSWFRV 136
Cu-oxidase_3 pfam07732
Multicopper oxidase; This entry contains many divergent copper oxidase-like domains that are ...
 802-860 2.45e-03

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


Pssm-ID: 462247 [Multi-domain]  Cd Length: 119  Bit Score: 38.77  E-value: 2.45e-03
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 301615846   802 ILGPLLIARTHEKVKIVFKNMASRPYSIYAHGVK------TDGPVVQTE----PGQTQTYIWKIPERSG 860
Cdd:pfam07732   24 FPGPTIRVREGDTVVVNVTNNLDEPTSIHWHGLQqrgtpwMDGVPGVTQcpipPGQSFTYRFQVKQQAG 92
CuRO_1_McoP_like cd13852
The first cupredoxin domain of multicopper oxidase McoP and similar proteins; This family ...
 788-894 3.14e-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: 3.14e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 301615846  788 TKRKERNEEEKHLGILGPLLIARTHEKVKIVFKNMASRPYSIYAHGV----KTDG-PVVQTEPGQTQTYIWKIPERSGpg 862
Cdd:cd13852     8 LKGDPAALQNLPDSYLGPILRLRKGQKVRITFKNNLPEPTIIHWHGLhvpaAMDGhPRYAIDPGETYVYEFEVLNRAG-- 85

                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 301615846  863 yhedvncvTWAYYS-----TVDQVkdtYSGLIGPLVI 894
Cdd:cd13852    86 --------TYWYHPhphglTAKQV---YRGLAGLFLV 111
PLN02604 PLN02604
oxidoreductase
 67-200 4.66e-03

oxidoreductase


Pssm-ID: 215324 [Multi-domain]  Cd Length: 566  Bit Score: 41.00  E-value: 4.66e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 301615846   67 RVYKKAVYLQY-SDDSYSKEI-----KKPqwlghlGPILKAEIGDIIIVHLKN-FASRPYSIHPHGVQYTkeneGALYPD 139
Cdd:PLN02604   25 RRYKWEVKYEYkSPDCFKKLVitingRSP------GPTILAQQGDTVIVELKNsLLTENVAIHWHGIRQI----GTPWFD 94

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 301615846  140 nASSGHKDDAIEPGQSYTYRWeAVSEQGptvqdedciTRIYHSHIDGPKDvsSGLIGPLII 200
Cdd:PLN02604   95 -GTEGVTQCPILPGETFTYEF-VVDRPG---------TYLYHAHYGMQRE--AGLYGSIRV 142
CuRO_D2_2dMcoN_like cd04202
The second cupredoxin domain of bacterial two domain multicopper oxidase McoN and similar ...
 215-348 5.00e-03

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: 38.39  E-value: 5.00e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 301615846  215 KEFVLMFSvidenlSWYLDENintfcTEPSSVDKNDTDFqesnkmHSINGYMFGNLPGLSMCEGEHIHWYLFGMGNeaDI 294
Cdd:cd04202     2 RDYTLVLQ------EWFVDPG-----TTPMPPEGMDFNY------FTINGKSFPATPPLVVKEGDRVRIRLINLSM--DH 62

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 301615846  295 HSAYFHG---QVLT--------FQMYRVDTLSLFPATMIEGHMVTKNPGKWLLTCQVNDHLAGGM 348
Cdd:cd04202    63 HPMHLHGhffLVTAtdggpipgSAPWPKDTLNVAPGERYDIEFVADNPGDWMFHCHKLHHAMNGM 127
PLN02604 PLN02604
oxidoreductase
 984-1049 5.67e-03

oxidoreductase


Pssm-ID: 215324 [Multi-domain]  Cd Length: 566  Bit Score: 40.61  E-value: 5.67e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 301615846  984 NEADIHTMHIHAHSFtYVRGatFHSDVYDLF--PGTFKTVEMI------------------ARVPGTWLLHCHVTDHIHA 1043
Cdd:PLN02604  462 NNSETHPWHLHGHDF-WVLG--YGEGKFNMSsdPKKYNLVDPImkntvpvhpygwtalrfrADNPGVWAFHCHIESHFFM 538


                  ....*.
gi 301615846 1044 GMEVLY 1049
Cdd:PLN02604  539 GMGVVF 544
CuRO_D1_2dMcoN_like cd13859
The first cupredoxin domain of bacterial two domain multicopper oxidase McoN and similar ...
 804-868 5.96e-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: 5.96e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 301615846  804 GPLLIARTHEKVKIVFKNMASRPYSIYAHGV------KTDGPVVQT----EPGQTQTYIWKIpERSGP-GYHEDVN 868
Cdd:cd13859    31 GPLIHVKEGDDLVVHVTNNTTLPHTIHWHGVlqmgswKMDGVPGVTqpaiEPGESFTYKFKA-ERPGTlWYHCHVN 105
CuRO_1_Diphenol_Ox cd13857
The first cupredoxin domain of fungal laccase, diphenol oxidase; Diphenol oxidase belongs to ...
 804-894 7.66e-03

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: 37.62  E-value: 7.66e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 301615846  804 GPLLIARTHEKVKIVFKNMASRPYSIYAHGVKT------DGPVVQTE----PGQTQTYIWKIPERSGpgyhedvncVTW- 872
Cdd:cd13857    30 GPLIEANQGDRIVVHVTNELDEPTSIHWHGLFQngtnwmDGTAGITQcpipPGGSFTYNFTVDGQYG---------TYWy 100

                          90       100
                  ....*....|....*....|....
gi 301615846  873 -AYYSTvdqvkdTYS-GLIGPLVI 894
Cdd:cd13857   101 hSHYST------QYAdGLVGPLIV 118
 
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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