NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|1307738778|gb|PKK23530|]
View 

ceruloplasmin (ferroxidase), partial [Columba livia]

Protein Classification

multicopper oxidase( domain architecture ID 10362973)

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

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

List of domain hits

 Name Accession Description Interval E-value
CuRO_3_ceruloplasmin cd04224
The third cupredoxin domain of Ceruloplasmin; Ceruloplasmin is a multicopper oxidase essential ...
 370-565 8.11e-125

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


:

Pssm-ID: 259886 [Multi-domain]  Cd Length: 197  Bit Score: 378.74  E-value: 8.11e-125
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1307738778  370 TRVRRYFIAAEEVIWNYGPSAMNHFTGQELIA-DSESRVFFEQSEMRIGGSYKKAVYKEYTDGSFTEHKKRVAEEAHLGL 448
Cdd:cd04224      1 GKVRHYFIAAEEIMWDYAPSGKNLFTGQNLTApGSDSEVFFQRNETRIGGTYWKVRYVEYTDATFTTRKHRSKEEEHLGI 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1307738778  449 LGPVIKAEVGESIRVTFRNNASRPFSIQPHGLSYRKSDEGASYSRGTDSPASHVSPGATFTYEWNVPEDVGPTDQDPDCL 528
Cdd:cd04224     81 LGPVIRAEVGDTIKVTFRNKASRPFSIQPHGVFYEKNYEGAMYRDGDPSPGSHVSPGETFTYEWTVPEGVGPTNQDPPCL 160

                          170       180       190
                   ....*....|....*....|....*....|....*..
gi 1307738778  529 TWLYYSAVDAVRDTSAGLVGPLLVCRRGALLPSGRQK 565
Cdd:cd04224    161 TYLYFSAVDPVRDTNSGLVGPLLVCKKGSLNANGRQK 197
Cupredoxin super family cl19115
Cupredoxin superfamily; Cupredoxins contain type I copper centers and are involved in ...
 22-204 1.31e-115

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 cd04222:

Pssm-ID: 473140 [Multi-domain]  Cd Length: 183  Bit Score: 354.03  E-value: 1.31e-115
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1307738778   22 REYYIGISETEWSYAPGDASAVSGRRLAEDEQARVFLQRGPHRIGSTYKKAVYTQYTDQLYDVAVDKPSWLGFLGPIIKG 101
Cdd:cd04222      1 REYYIGIRETQWDYAPSGKNLITNQTFDDDEHASVFLKRGPDRIGRVYKKAVYLQYTDDTYRTEIEKPVWLGFLGPILKA 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1307738778  102 EVGDSIIIHLKNFASRNYTLHPHGVTYTKENEGALYPDNTGAVQKRDDAVEPGGQFTYTWDVTEDQGPAEGDADCVTRAY 181
Cdd:cd04222     81 EVGDVIVVHLKNFASRPYSLHPHGVFYNKENEGALYPDNTSGFEKADDAVPPGGSYTYTWTVPEEQAPTKADANCLTRIY 160

                          170       180
                   ....*....|....*....|...
gi 1307738778  182 HSHIDAPRDVASGLVGPLIICRK 204
Cdd:cd04222    161 HSHIDAPKDIASGLIGPLIICKK 183
CuRO_5_ceruloplasmin cd04225
The fifth cupredoxin domain of Ceruloplasmin; Ceruloplasmin is a multicopper oxidase essential ...
 725-895 2.13e-105

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: 326.35  E-value: 2.13e-105
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1307738778  725 KTYYIAAVEVEWDYSPNRTWEFERHQYHEDSPGNQFLNREDRFIGSKYRKVVYREYTDGTFSTPKHRAEEQQHLEIQGPL 804
Cdd:cd04225      1 RTYYIAAEEVEWDYSPQRTWEQELHNTHEESPGNAFLNKGDKFIGSKYKKVVYREYTDDTFSVPKERTAEEEHLGILGPL 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1307738778  805 LMSNIGDKIVIVFKNLASRPYSIHAHGVKTDSSAVAVTNPGETKTYVWKIPARSSSERGDPPCIAWAYHSTVDIVKDTYS 884
Cdd:cd04225     81 IHAEVGEKVKIVFKNMASRPYSIHAHGVKTDSSWVAPTEPGETQTYTWKIPERSGPGVEDSNCISWAYYSTVDQIKDLYS 160

                          170
                   ....*....|.
gi 1307738778  885 GLIGTLVVCHR 895
Cdd:cd04225    161 GLIGPLVICRR 171
CuRO_6_ceruloplasmin cd11012
The sixth cupredoxin domain of Ceruloplasmin; Ceruloplasmin is a multicopper oxidase essential ...
 906-1050 1.22e-96

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


:

Pssm-ID: 259898 [Multi-domain]  Cd Length: 145  Bit Score: 302.17  E-value: 1.22e-96
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1307738778  906 KVQFALLFMVFDENESWYLDENIKTYSPNPHLVDKEDEEFLESNKMHAINGKVFGNLRGLTMHVGDRVSWYLMGMGNEID 985
Cdd:cd11012      1 KLEFALLFLVFDENESWYLDENIKTYSDHPEKVNKEDEEFIESNKMHAINGKVFGNLQGLTMHVGDEVYWYLMGMGNEID 80

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1307738778  986 IHTAHFHGHSFDYKQTGVYRADVFDLFPGTFQTVEMIPRNPGTWLLHCHVTDHVHAGMEATYTVL 1050
Cdd:cd11012     81 IHTAHFHGHSFDYKHRGVYRSDVFDLFPGTFQTVEMIPRTPGTWLLHCHVTDHIHAGMETTYTVL 145
CuRO_2_ceruloplasmin cd11021
The second cupredoxin domain of Ceruloplasmin; Ceruloplasmin is a multicopper oxidase ...
 216-356 2.45e-95

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


:

Pssm-ID: 259907 [Multi-domain]  Cd Length: 141  Bit Score: 298.62  E-value: 2.45e-95
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1307738778  216 DAEFILMFSVMDENLSWYLDDNIRTYCSEPSKVDKDDEDFQESNKMHSINGYMYGYLPNLTMCVEDKVKWHLFGMGNEAD 295
Cdd:cd11021      1 DREFVLMFSVVDENLSWYLDENIKTYCSEPAKVDKDDEDFQESNKMHSINGYTFGNLPGLSMCAGDRVKWHLFGMGNEVD 80

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1307738778  296 IHSAYFHGQTLIERHHRVDTISLFPATFVDAVMTPRNPGEWLLSCQVNDHIQGGMQALFKV 356
Cdd:cd11021     81 IHSAFFHGQTLTDRGHRTDTINLFPATFVTAEMVAQNPGKWLLSCQVNDHLKAGMQAFYEV 141
CuRO_4_ceruloplasmin cd11022
The fourth cupredoxin domain of Ceruloplasmin; Ceruloplasmin is a multicopper oxidase ...
 568-711 2.09e-94

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: 295.93  E-value: 2.09e-94
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1307738778  568 DMEFFLLATVFDENLSWYLDDNILMFTLNPNKIDKDDEDFQESNKMHSINGYMYGNQPGLGMCKGSVVSWHLMGLGSEVD 647
Cdd:cd11022      1 DKEFFLLFTVFDENESWYLDENIQQFTLDPRSVDKEDEDFQESNKMHSINGYMYGNQPGLDMCKGDTVSWHLFGLGTETD 80

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1307738778  648 VHGIYFSENTFTARGTRRDTANLFPHTFLTAIMKPDSEGVFEVSCLTTDHYTGGMKQNYRVKQC 711
Cdd:cd11022     81 VHGIYFSGNTFLLQGTRRDTANLFPHTSVTAIMQPDNEGTFEVNCQTTDHYSAGMRQIYTVSQC 144
 
Name Accession Description Interval E-value
CuRO_3_ceruloplasmin cd04224
The third cupredoxin domain of Ceruloplasmin; Ceruloplasmin is a multicopper oxidase essential ...
 370-565 8.11e-125

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


Pssm-ID: 259886 [Multi-domain]  Cd Length: 197  Bit Score: 378.74  E-value: 8.11e-125
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1307738778  370 TRVRRYFIAAEEVIWNYGPSAMNHFTGQELIA-DSESRVFFEQSEMRIGGSYKKAVYKEYTDGSFTEHKKRVAEEAHLGL 448
Cdd:cd04224      1 GKVRHYFIAAEEIMWDYAPSGKNLFTGQNLTApGSDSEVFFQRNETRIGGTYWKVRYVEYTDATFTTRKHRSKEEEHLGI 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1307738778  449 LGPVIKAEVGESIRVTFRNNASRPFSIQPHGLSYRKSDEGASYSRGTDSPASHVSPGATFTYEWNVPEDVGPTDQDPDCL 528
Cdd:cd04224     81 LGPVIRAEVGDTIKVTFRNKASRPFSIQPHGVFYEKNYEGAMYRDGDPSPGSHVSPGETFTYEWTVPEGVGPTNQDPPCL 160

                          170       180       190
                   ....*....|....*....|....*....|....*..
gi 1307738778  529 TWLYYSAVDAVRDTSAGLVGPLLVCRRGALLPSGRQK 565
Cdd:cd04224    161 TYLYFSAVDPVRDTNSGLVGPLLVCKKGSLNANGRQK 197
CuRO_1_ceruloplasmin cd04222
The first cupredoxin domain of Ceruloplasmin; Ceruloplasmin is a multicopper oxidase essential ...
 22-204 1.31e-115

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: 354.03  E-value: 1.31e-115
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1307738778   22 REYYIGISETEWSYAPGDASAVSGRRLAEDEQARVFLQRGPHRIGSTYKKAVYTQYTDQLYDVAVDKPSWLGFLGPIIKG 101
Cdd:cd04222      1 REYYIGIRETQWDYAPSGKNLITNQTFDDDEHASVFLKRGPDRIGRVYKKAVYLQYTDDTYRTEIEKPVWLGFLGPILKA 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1307738778  102 EVGDSIIIHLKNFASRNYTLHPHGVTYTKENEGALYPDNTGAVQKRDDAVEPGGQFTYTWDVTEDQGPAEGDADCVTRAY 181
Cdd:cd04222     81 EVGDVIVVHLKNFASRPYSLHPHGVFYNKENEGALYPDNTSGFEKADDAVPPGGSYTYTWTVPEEQAPTKADANCLTRIY 160

                          170       180
                   ....*....|....*....|...
gi 1307738778  182 HSHIDAPRDVASGLVGPLIICRK 204
Cdd:cd04222    161 HSHIDAPKDIASGLIGPLIICKK 183
CuRO_5_ceruloplasmin cd04225
The fifth cupredoxin domain of Ceruloplasmin; Ceruloplasmin is a multicopper oxidase essential ...
 725-895 2.13e-105

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: 326.35  E-value: 2.13e-105
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1307738778  725 KTYYIAAVEVEWDYSPNRTWEFERHQYHEDSPGNQFLNREDRFIGSKYRKVVYREYTDGTFSTPKHRAEEQQHLEIQGPL 804
Cdd:cd04225      1 RTYYIAAEEVEWDYSPQRTWEQELHNTHEESPGNAFLNKGDKFIGSKYKKVVYREYTDDTFSVPKERTAEEEHLGILGPL 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1307738778  805 LMSNIGDKIVIVFKNLASRPYSIHAHGVKTDSSAVAVTNPGETKTYVWKIPARSSSERGDPPCIAWAYHSTVDIVKDTYS 884
Cdd:cd04225     81 IHAEVGEKVKIVFKNMASRPYSIHAHGVKTDSSWVAPTEPGETQTYTWKIPERSGPGVEDSNCISWAYYSTVDQIKDLYS 160

                          170
                   ....*....|.
gi 1307738778  885 GLIGTLVVCHR 895
Cdd:cd04225    161 GLIGPLVICRR 171
CuRO_6_ceruloplasmin cd11012
The sixth cupredoxin domain of Ceruloplasmin; Ceruloplasmin is a multicopper oxidase essential ...
 906-1050 1.22e-96

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


Pssm-ID: 259898 [Multi-domain]  Cd Length: 145  Bit Score: 302.17  E-value: 1.22e-96
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1307738778  906 KVQFALLFMVFDENESWYLDENIKTYSPNPHLVDKEDEEFLESNKMHAINGKVFGNLRGLTMHVGDRVSWYLMGMGNEID 985
Cdd:cd11012      1 KLEFALLFLVFDENESWYLDENIKTYSDHPEKVNKEDEEFIESNKMHAINGKVFGNLQGLTMHVGDEVYWYLMGMGNEID 80

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1307738778  986 IHTAHFHGHSFDYKQTGVYRADVFDLFPGTFQTVEMIPRNPGTWLLHCHVTDHVHAGMEATYTVL 1050
Cdd:cd11012     81 IHTAHFHGHSFDYKHRGVYRSDVFDLFPGTFQTVEMIPRTPGTWLLHCHVTDHIHAGMETTYTVL 145
CuRO_2_ceruloplasmin cd11021
The second cupredoxin domain of Ceruloplasmin; Ceruloplasmin is a multicopper oxidase ...
 216-356 2.45e-95

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


Pssm-ID: 259907 [Multi-domain]  Cd Length: 141  Bit Score: 298.62  E-value: 2.45e-95
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1307738778  216 DAEFILMFSVMDENLSWYLDDNIRTYCSEPSKVDKDDEDFQESNKMHSINGYMYGYLPNLTMCVEDKVKWHLFGMGNEAD 295
Cdd:cd11021      1 DREFVLMFSVVDENLSWYLDENIKTYCSEPAKVDKDDEDFQESNKMHSINGYTFGNLPGLSMCAGDRVKWHLFGMGNEVD 80

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1307738778  296 IHSAYFHGQTLIERHHRVDTISLFPATFVDAVMTPRNPGEWLLSCQVNDHIQGGMQALFKV 356
Cdd:cd11021     81 IHSAFFHGQTLTDRGHRTDTINLFPATFVTAEMVAQNPGKWLLSCQVNDHLKAGMQAFYEV 141
CuRO_4_ceruloplasmin cd11022
The fourth cupredoxin domain of Ceruloplasmin; Ceruloplasmin is a multicopper oxidase ...
 568-711 2.09e-94

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: 295.93  E-value: 2.09e-94
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1307738778  568 DMEFFLLATVFDENLSWYLDDNILMFTLNPNKIDKDDEDFQESNKMHSINGYMYGNQPGLGMCKGSVVSWHLMGLGSEVD 647
Cdd:cd11022      1 DKEFFLLFTVFDENESWYLDENIQQFTLDPRSVDKEDEDFQESNKMHSINGYMYGNQPGLDMCKGDTVSWHLFGLGTETD 80

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1307738778  648 VHGIYFSENTFTARGTRRDTANLFPHTFLTAIMKPDSEGVFEVSCLTTDHYTGGMKQNYRVKQC 711
Cdd:cd11022     81 VHGIYFSGNTFLLQGTRRDTANLFPHTSVTAIMQPDNEGTFEVNCQTTDHYSAGMRQIYTVSQC 144
Cu-oxidase_2 pfam07731
Multicopper oxidase; This entry contains many divergent copper oxidase-like domains that are ...
 949-1053 4.34e-19

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


Pssm-ID: 462246 [Multi-domain]  Cd Length: 138  Bit Score: 84.79  E-value: 4.34e-19
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1307738778  949 NKMHAINGKVFG-NLRGLTMHVGDRVSWYLMGMGNeiDIHTAHFHGHSFDYKQTGV----------------YRADVFDL 1011
Cdd:pfam07731   19 RNDWAINGLLFPpNTNVITLPYGTVVEWVLQNTTT--GVHPFHLHGHSFQVLGRGGgpwpeedpktynlvdpVRRDTVQV 96

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|..
gi 1307738778 1012 FPGTFQTVEMIPRNPGTWLLHCHVTDHVHAGMEATYTVLPRE 1053
Cdd:pfam07731   97 PPGGWVAIRFRADNPGVWLFHCHILWHLDQGMMGQFVVRPGD 138
Cu-oxidase_3 pfam07732
Multicopper oxidase; This entry contains many divergent copper oxidase-like domains that are ...
 94-201 8.75e-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: 8.75e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1307738778   94 FLGPIIKGEVGDSIIIHLKNFASRNYTLHPHGVTYTKEnegalyPDNTGAVQKRDDAVEPGGQFTYTWDVTEDQGpaegd 173
Cdd:pfam07732   24 FPGPTIRVREGDTVVVNVTNNLDEPTSIHWHGLQQRGT------PWMDGVPGVTQCPIPPGQSFTYRFQVKQQAG----- 92

                           90       100
                   ....*....|....*....|....*...
gi 1307738778  174 adcvTRAYHSHIDAPRdvASGLVGPLII 201
Cdd:pfam07732   93 ----TYWYHSHTSGQQ--AAGLAGAIII 114
SufI COG2132
Multicopper oxidase with three cupredoxin domains (includes cell division protein FtsP and ...
 951-1051 3.01e-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: 63.80  E-value: 3.01e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1307738778  951 MHAINGKVFGNLR-GLTMHVGDRVSWYLMGMGNeiDIHTAHFHGHSF--------DYKQTGvyRADVFDLFPGtfQTVEM 1021
Cdd:COG2132    317 VWTINGKAFDPDRpDLTVKLGERERWTLVNDTM--MPHPFHLHGHQFqvlsrngkPPPEGG--WKDTVLVPPG--ETVRI 390

                           90       100       110
                   ....*....|....*....|....*....|...
gi 1307738778 1022 I---PRNPGTWLLHCHVTDHVHAGMEATYTVLP 1051
Cdd:COG2132    391 LfrfDNYPGDWMFHCHILEHEDAGMMGQFEVVP 423
Cu-oxidase_3 pfam07732
Multicopper oxidase; This entry contains many divergent copper oxidase-like domains that are ...
 448-552 1.16e-08

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: 54.17  E-value: 1.16e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1307738778  448 LLGPVIKAEVGESIRVTFRNNASRPFSIQPHGLSYRKSdegaSYSRGTD-SPASHVSPGATFTYEWNVPEDVGptdqdpd 526
Cdd:pfam07732   24 FPGPTIRVREGDTVVVNVTNNLDEPTSIHWHGLQQRGT----PWMDGVPgVTQCPIPPGQSFTYRFQVKQQAG------- 92

                           90       100
                   ....*....|....*....|....*.
gi 1307738778  527 clTWLYYSAVDAVRdtSAGLVGPLLV 552
Cdd:pfam07732   93 --TYWYHSHTSGQQ--AAGLAGAIII 114
SufI COG2132
Multicopper oxidase with three cupredoxin domains (includes cell division protein FtsP and ...
 94-224 3.75e-08

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


Pssm-ID: 441735 [Multi-domain]  Cd Length: 423  Bit Score: 56.87  E-value: 3.75e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1307738778   94 FLGPIIKGEVGDSIIIHLKNFASRNYTLHPHGvtytkeneGALYPDNTGAVQkrdDAVEPGGQFTYTWDVteDQGPAegd 173
Cdd:COG2132     42 YPGPTIRVREGDRVRVRVTNRLPEPTTVHWHG--------LRVPNAMDGVPG---DPIAPGETFTYEFPV--PQPAG--- 105

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 1307738778  174 adcvTRAYHSHIDA--PRDVASGLVGPLIIcrkgtmNTDSDK--RFDAEFILMFS 224
Cdd:COG2132    106 ----TYWYHPHTHGstAEQVYRGLAGALIV------EDPEEDlpRYDRDIPLVLQ 150
PLN02191 PLN02191
L-ascorbate oxidase
 94-224 5.02e-08

L-ascorbate oxidase


Pssm-ID: 177843 [Multi-domain]  Cd Length: 574  Bit Score: 56.95  E-value: 5.02e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1307738778   94 FLGPIIKGEVGDSIIIHLKN-FASRNYTLHPHGVtytkENEGALYPDNTGAVQKRddAVEPGGQFTYTWDVtEDQGpaeg 172
Cdd:PLN02191    51 FPGPTIDAVAGDTIVVHLTNkLTTEGLVIHWHGI----RQKGSPWADGAAGVTQC--AINPGETFTYKFTV-EKPG---- 119

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|...
gi 1307738778  173 dadcvTRAYHSHIDAPRdvASGLVGPLIIcrkGTMNTDSDK-RFDAEFILMFS 224
Cdd:PLN02191   120 -----THFYHGHYGMQR--SAGLYGSLIV---DVAKGPKERlRYDGEFNLLLS 162
Cu-oxidase pfam00394
Multicopper oxidase; Many of the proteins in this family contain multiple similar copies of ...
 223-359 6.95e-08

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


Pssm-ID: 395317 [Multi-domain]  Cd Length: 146  Bit Score: 52.70  E-value: 6.95e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1307738778  223 FSVMDENLSWYlDDNIRTYCSEPSKVDKDDEDFQESNKMHSINGYMYGYLPNLTMCVEDKVKWHLFgMGNEADIHSAYFH 302
Cdd:pfam00394    1 EDYVITLSDWY-HKDAKDLEKELLASGKAPTDFPPVPDAVLINGKDGASLATLTVTPGKTYRLRII-NVALDDSLNFSIE 78

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1307738778  303 GQ--TLIE---RHH---RVDTISLFPATFVDAVMTP-RNPGEWLLSCQVN-DHIQGGMQALFKVKDC 359
Cdd:pfam00394   79 GHkmTVVEvdgVYVnpfTVDSLDIFPGQRYSVLVTAnQDPGNYWIVASPNiPAFDNGTAAAILRYSG 145
ascorbase TIGR03388
L-ascorbate oxidase, plant type; Members of this protein family are the copper-containing ...
 94-233 8.73e-07

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


Pssm-ID: 274555 [Multi-domain]  Cd Length: 541  Bit Score: 52.83  E-value: 8.73e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1307738778   94 FLGPIIKGEVGDSIIIHLKN-FASRNYTLHPHGVtytkENEGALYPDNTGAVQKRddAVEPGGQFTYTWdVTEDQGpaeg 172
Cdd:TIGR03388   29 FPGPTIRAQAGDTIVVELTNkLHTEGVVIHWHGI----RQIGTPWADGTAGVTQC--AINPGETFIYNF-VVDRPG---- 97

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1307738778  173 dadcvTRAYHSHIDAPRdvASGLVGPLIIcrkgtMNTDSDK---RFDAEFILMFSvmdenlSWY 233
Cdd:TIGR03388   98 -----TYFYHGHYGMQR--SAGLYGSLIV-----DVPDGEKepfHYDGEFNLLLS------DWW 143
SufI COG2132
Multicopper oxidase with three cupredoxin domains (includes cell division protein FtsP and ...
 448-552 1.10e-05

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


Pssm-ID: 441735 [Multi-domain]  Cd Length: 423  Bit Score: 49.16  E-value: 1.10e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1307738778  448 LLGPVIKAEVGESIRVTFRNNASRPFSIQPHGLsyR---KSDegasysrgtDSPASHVSPGATFTYEWNVPEDVGptdqd 524
Cdd:COG2132     42 YPGPTIRVREGDRVRVRVTNRLPEPTTVHWHGL--RvpnAMD---------GVPGDPIAPGETFTYEFPVPQPAG----- 105

                           90       100       110
                   ....*....|....*....|....*....|
gi 1307738778  525 pdclTWLYYSAVDAV--RDTSAGLVGPLLV 552
Cdd:COG2132    106 ----TYWYHPHTHGStaEQVYRGLAGALIV 131
PLN02191 PLN02191
L-ascorbate oxidase
 985-1043 1.25e-05

L-ascorbate oxidase


Pssm-ID: 177843 [Multi-domain]  Cd Length: 574  Bit Score: 49.24  E-value: 1.25e-05
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1307738778  985 DIHTAHFHGHSF--------------DYKQTGVYRADVFD---LFPGTFQTVEMIPRNPGTWLLHCHVTDHVHAGM 1043
Cdd:PLN02191   465 EIHPWHLHGHDFwvlgygdgkfkpgiDEKTYNLKNPPLRNtaiLYPYGWTAIRFVTDNPGVWFFHCHIEPHLHMGM 540
ascorbOXfungal TIGR03390
L-ascorbate oxidase, fungal type; This model describes a family of fungal ascorbate oxidases, ...
 984-1054 2.26e-03

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


Pssm-ID: 132431 [Multi-domain]  Cd Length: 538  Bit Score: 41.75  E-value: 2.26e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1307738778  984 IDIHTAHFHG-HSFDYKQ-TGVYRA---------------DVFDLFPGTFQTVEMIP----------RNPGTWLLHCHVT 1036
Cdd:TIGR03390  439 VDTHPFHAHGrHFYDIGGgDGEYNAtaneaklenytpvlrDTTMLYRYAVKVVPGAPagwrawrirvTNPGVWMMHCHIL 518

                           90
                   ....*....|....*...
gi 1307738778 1037 DHVHAGMEATYTVLPRED 1054
Cdd:TIGR03390  519 QHMVMGMQTVWVFGDAED 536
Cu-oxidase_3 pfam07732
Multicopper oxidase; This entry contains many divergent copper oxidase-like domains that are ...
 802-874 7.67e-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: 37.61  E-value: 7.67e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1307738778  802 GPLLMSNIGDKIVIVFKNLASRPYSIHAHGVKTDSS-----AVAVTN----PGETKTYVWKIParsssergDPPCIAWaY 872
Cdd:pfam07732   26 GPTIRVREGDTVVVNVTNNLDEPTSIHWHGLQQRGTpwmdgVPGVTQcpipPGQSFTYRFQVK--------QQAGTYW-Y 96


                   ..
gi 1307738778  873 HS 874
Cdd:pfam07732   97 HS 98
 
Name Accession Description Interval E-value
CuRO_3_ceruloplasmin cd04224
The third cupredoxin domain of Ceruloplasmin; Ceruloplasmin is a multicopper oxidase essential ...
 370-565 8.11e-125

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


Pssm-ID: 259886 [Multi-domain]  Cd Length: 197  Bit Score: 378.74  E-value: 8.11e-125
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1307738778  370 TRVRRYFIAAEEVIWNYGPSAMNHFTGQELIA-DSESRVFFEQSEMRIGGSYKKAVYKEYTDGSFTEHKKRVAEEAHLGL 448
Cdd:cd04224      1 GKVRHYFIAAEEIMWDYAPSGKNLFTGQNLTApGSDSEVFFQRNETRIGGTYWKVRYVEYTDATFTTRKHRSKEEEHLGI 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1307738778  449 LGPVIKAEVGESIRVTFRNNASRPFSIQPHGLSYRKSDEGASYSRGTDSPASHVSPGATFTYEWNVPEDVGPTDQDPDCL 528
Cdd:cd04224     81 LGPVIRAEVGDTIKVTFRNKASRPFSIQPHGVFYEKNYEGAMYRDGDPSPGSHVSPGETFTYEWTVPEGVGPTNQDPPCL 160

                          170       180       190
                   ....*....|....*....|....*....|....*..
gi 1307738778  529 TWLYYSAVDAVRDTSAGLVGPLLVCRRGALLPSGRQK 565
Cdd:cd04224    161 TYLYFSAVDPVRDTNSGLVGPLLVCKKGSLNANGRQK 197
CuRO_1_ceruloplasmin cd04222
The first cupredoxin domain of Ceruloplasmin; Ceruloplasmin is a multicopper oxidase essential ...
 22-204 1.31e-115

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: 354.03  E-value: 1.31e-115
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1307738778   22 REYYIGISETEWSYAPGDASAVSGRRLAEDEQARVFLQRGPHRIGSTYKKAVYTQYTDQLYDVAVDKPSWLGFLGPIIKG 101
Cdd:cd04222      1 REYYIGIRETQWDYAPSGKNLITNQTFDDDEHASVFLKRGPDRIGRVYKKAVYLQYTDDTYRTEIEKPVWLGFLGPILKA 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1307738778  102 EVGDSIIIHLKNFASRNYTLHPHGVTYTKENEGALYPDNTGAVQKRDDAVEPGGQFTYTWDVTEDQGPAEGDADCVTRAY 181
Cdd:cd04222     81 EVGDVIVVHLKNFASRPYSLHPHGVFYNKENEGALYPDNTSGFEKADDAVPPGGSYTYTWTVPEEQAPTKADANCLTRIY 160

                          170       180
                   ....*....|....*....|...
gi 1307738778  182 HSHIDAPRDVASGLVGPLIICRK 204
Cdd:cd04222    161 HSHIDAPKDIASGLIGPLIICKK 183
CuRO_5_ceruloplasmin cd04225
The fifth cupredoxin domain of Ceruloplasmin; Ceruloplasmin is a multicopper oxidase essential ...
 725-895 2.13e-105

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: 326.35  E-value: 2.13e-105
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1307738778  725 KTYYIAAVEVEWDYSPNRTWEFERHQYHEDSPGNQFLNREDRFIGSKYRKVVYREYTDGTFSTPKHRAEEQQHLEIQGPL 804
Cdd:cd04225      1 RTYYIAAEEVEWDYSPQRTWEQELHNTHEESPGNAFLNKGDKFIGSKYKKVVYREYTDDTFSVPKERTAEEEHLGILGPL 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1307738778  805 LMSNIGDKIVIVFKNLASRPYSIHAHGVKTDSSAVAVTNPGETKTYVWKIPARSSSERGDPPCIAWAYHSTVDIVKDTYS 884
Cdd:cd04225     81 IHAEVGEKVKIVFKNMASRPYSIHAHGVKTDSSWVAPTEPGETQTYTWKIPERSGPGVEDSNCISWAYYSTVDQIKDLYS 160

                          170
                   ....*....|.
gi 1307738778  885 GLIGTLVVCHR 895
Cdd:cd04225    161 GLIGPLVICRR 171
CuRO_6_ceruloplasmin cd11012
The sixth cupredoxin domain of Ceruloplasmin; Ceruloplasmin is a multicopper oxidase essential ...
 906-1050 1.22e-96

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


Pssm-ID: 259898 [Multi-domain]  Cd Length: 145  Bit Score: 302.17  E-value: 1.22e-96
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1307738778  906 KVQFALLFMVFDENESWYLDENIKTYSPNPHLVDKEDEEFLESNKMHAINGKVFGNLRGLTMHVGDRVSWYLMGMGNEID 985
Cdd:cd11012      1 KLEFALLFLVFDENESWYLDENIKTYSDHPEKVNKEDEEFIESNKMHAINGKVFGNLQGLTMHVGDEVYWYLMGMGNEID 80

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1307738778  986 IHTAHFHGHSFDYKQTGVYRADVFDLFPGTFQTVEMIPRNPGTWLLHCHVTDHVHAGMEATYTVL 1050
Cdd:cd11012     81 IHTAHFHGHSFDYKHRGVYRSDVFDLFPGTFQTVEMIPRTPGTWLLHCHVTDHIHAGMETTYTVL 145
CuRO_2_ceruloplasmin cd11021
The second cupredoxin domain of Ceruloplasmin; Ceruloplasmin is a multicopper oxidase ...
 216-356 2.45e-95

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


Pssm-ID: 259907 [Multi-domain]  Cd Length: 141  Bit Score: 298.62  E-value: 2.45e-95
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1307738778  216 DAEFILMFSVMDENLSWYLDDNIRTYCSEPSKVDKDDEDFQESNKMHSINGYMYGYLPNLTMCVEDKVKWHLFGMGNEAD 295
Cdd:cd11021      1 DREFVLMFSVVDENLSWYLDENIKTYCSEPAKVDKDDEDFQESNKMHSINGYTFGNLPGLSMCAGDRVKWHLFGMGNEVD 80

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1307738778  296 IHSAYFHGQTLIERHHRVDTISLFPATFVDAVMTPRNPGEWLLSCQVNDHIQGGMQALFKV 356
Cdd:cd11021     81 IHSAFFHGQTLTDRGHRTDTINLFPATFVTAEMVAQNPGKWLLSCQVNDHLKAGMQAFYEV 141
CuRO_4_ceruloplasmin cd11022
The fourth cupredoxin domain of Ceruloplasmin; Ceruloplasmin is a multicopper oxidase ...
 568-711 2.09e-94

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: 295.93  E-value: 2.09e-94
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1307738778  568 DMEFFLLATVFDENLSWYLDDNILMFTLNPNKIDKDDEDFQESNKMHSINGYMYGNQPGLGMCKGSVVSWHLMGLGSEVD 647
Cdd:cd11022      1 DKEFFLLFTVFDENESWYLDENIQQFTLDPRSVDKEDEDFQESNKMHSINGYMYGNQPGLDMCKGDTVSWHLFGLGTETD 80

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1307738778  648 VHGIYFSENTFTARGTRRDTANLFPHTFLTAIMKPDSEGVFEVSCLTTDHYTGGMKQNYRVKQC 711
Cdd:cd11022     81 VHGIYFSGNTFLLQGTRRDTANLFPHTSVTAIMQPDNEGTFEVNCQTTDHYSAGMRQIYTVSQC 144
CuRO_1_ceruloplasmin_like cd04199
Cupredoxin domains 1, 3, and 5 of ceruloplasmin and similar proteins; This family includes the ...
 22-204 2.27e-78

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


Pssm-ID: 259862 [Multi-domain]  Cd Length: 177  Bit Score: 253.87  E-value: 2.27e-78
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1307738778   22 REYYIGISETEWSYAPGDASAVsgrrlaEDEQARVFLQRGPHRIGSTYKKAVYTQYTDQLYDVAVDKPSWLGFLGPIIKG 101
Cdd:cd04199      1 RHYYIAAEEIDWDYAPSGLAEK------DLSYRNQYLDNGPFRIGRSYKKVVYREYTDESFTTPGPQPEHLGILGPTIRA 74

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1307738778  102 EVGDSIIIHLKNFASRNYTLHPHGVTYTKENEGALYPDNTGAVQKRDDAVEPGGQFTYTWDVTEDQGPAEGDADCVTRAY 181
Cdd:cd04199     75 EVGDTIKVHFKNKASRPYSIHPHGVSYEKDSEGASYSDQTGPDEKKDDAVAPGETYTYVWIVTEESGPTKGDPACLTWAY 154

                          170       180
                   ....*....|....*....|...
gi 1307738778  182 HSHIDAPRDVASGLVGPLIICRK 204
Cdd:cd04199    155 YSHVDLEKDINSGLIGPLLICKK 177
CuRO_1_ceruloplasmin_like cd04199
Cupredoxin domains 1, 3, and 5 of ceruloplasmin and similar proteins; This family includes the ...
 373-555 4.50e-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: 242.31  E-value: 4.50e-74
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1307738778  373 RRYFIAAEEVIWNYGPSAMNHFTgqeliaDSESRVFFEQSEMRIGGSYKKAVYKEYTDGSFTEHKkrvAEEAHLGLLGPV 452
Cdd:cd04199      1 RHYYIAAEEIDWDYAPSGLAEKD------LSYRNQYLDNGPFRIGRSYKKVVYREYTDESFTTPG---PQPEHLGILGPT 71

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1307738778  453 IKAEVGESIRVTFRNNASRPFSIQPHGLSYRKSDEGASYSRGTDS---PASHVSPGATFTYEWNVPEDVGPTDQDPDCLT 529
Cdd:cd04199     72 IRAEVGDTIKVHFKNKASRPYSIHPHGVSYEKDSEGASYSDQTGPdekKDDAVAPGETYTYVWIVTEESGPTKGDPACLT 151

                          170       180
                   ....*....|....*....|....*.
gi 1307738778  530 WLYYSAVDAVRDTSAGLVGPLLVCRR 555
Cdd:cd04199    152 WAYYSHVDLEKDINSGLIGPLLICKK 177
CuRO_2_ceruloplasmin_like cd04200
Cupredoxin domains 2, 4, and 6 of ceruloplasmin and similar proteins; This family includes the ...
 216-356 4.78e-71

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


Pssm-ID: 259863 [Multi-domain]  Cd Length: 141  Bit Score: 232.30  E-value: 4.78e-71
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1307738778  216 DAEFILMFSVMDENLSWYLDDNIRTYCSEPSKVDKDDEDFQESNKMHSINGYMYGYLPNLTMCVEDKVKWHLFGMGNEAD 295
Cdd:cd04200      1 DKEFVLLFAVFDENKSWYLEDNIKRFCDNPEKVDKDDEEFQESNKMHAINGYVFGNLPGLTMCAGDRVRWHLLGMGNEVD 80

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1307738778  296 IHSAYFHGQTLIERHHRVDTISLFPATFVDAVMTPRNPGEWLLSCQVNDHIQGGMQALFKV 356
Cdd:cd04200     81 VHSIHFHGQTFLYKGYRIDTLTLFPATFETVEMVPSNPGTWLLHCHNSDHRHAGMQAYFLV 141
CuRO_2_ceruloplasmin_like cd04200
Cupredoxin domains 2, 4, and 6 of ceruloplasmin and similar proteins; This family includes the ...
 908-1049 8.38e-71

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


Pssm-ID: 259863 [Multi-domain]  Cd Length: 141  Bit Score: 231.92  E-value: 8.38e-71
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1307738778  908 QFALLFMVFDENESWYLDENIKTYSPNPHLVDKEDEEFLESNKMHAINGKVFGNLRGLTMHVGDRVSWYLMGMGNEIDIH 987
Cdd:cd04200      3 EFVLLFAVFDENKSWYLEDNIKRFCDNPEKVDKDDEEFQESNKMHAINGYVFGNLPGLTMCAGDRVRWHLLGMGNEVDVH 82

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1307738778  988 TAHFHGHSFDYKQtgvYRADVFDLFPGTFQTVEMIPRNPGTWLLHCHVTDHVHAGMEATYTV 1049
Cdd:cd04200     83 SIHFHGQTFLYKG---YRIDTLTLFPATFETVEMVPSNPGTWLLHCHNSDHRHAGMQAYFLV 141
CuRO_1_ceruloplasmin cd04222
The first cupredoxin domain of Ceruloplasmin; Ceruloplasmin is a multicopper oxidase essential ...
 373-555 2.49e-66

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


Pssm-ID: 259884 [Multi-domain]  Cd Length: 183  Bit Score: 221.14  E-value: 2.49e-66
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1307738778  373 RRYFIAAEEVIWNYGPSAMNHFTGQELIADSESRVFFEQSEMRIGGSYKKAVYKEYTDGSFTehkKRVAEEAHLGLLGPV 452
Cdd:cd04222      1 REYYIGIRETQWDYAPSGKNLITNQTFDDDEHASVFLKRGPDRIGRVYKKAVYLQYTDDTYR---TEIEKPVWLGFLGPI 77

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1307738778  453 IKAEVGESIRVTFRNNASRPFSIQPHGLSYRKSDEGASYSRGTDSPASH---VSPGATFTYEWNVPEDVGPTDQDPDCLT 529
Cdd:cd04222     78 LKAEVGDVIVVHLKNFASRPYSLHPHGVFYNKENEGALYPDNTSGFEKAddaVPPGGSYTYTWTVPEEQAPTKADANCLT 157

                          170       180
                   ....*....|....*....|....*.
gi 1307738778  530 WLYYSAVDAVRDTSAGLVGPLLVCRR 555
Cdd:cd04222    158 RIYHSHIDAPKDIASGLIGPLIICKK 183
CuRO_1_ceruloplasmin_like cd04199
Cupredoxin domains 1, 3, and 5 of ceruloplasmin and similar proteins; This family includes the ...
 725-895 1.90e-64

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: 215.35  E-value: 1.90e-64
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1307738778  725 KTYYIAAVEVEWDYSPNRTWEFERHQYhedspgNQFLNREDRFIGSKYRKVVYREYTDGTFSTPKhraEEQQHLEIQGPL 804
Cdd:cd04199      1 RHYYIAAEEIDWDYAPSGLAEKDLSYR------NQYLDNGPFRIGRSYKKVVYREYTDESFTTPG---PQPEHLGILGPT 71

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1307738778  805 LMSNIGDKIVIVFKNLASRPYSIHAHGVKTDSSAVAVTN---------------PGETKTYVWKIPARSSSERGDPPCIA 869
Cdd:cd04199     72 IRAEVGDTIKVHFKNKASRPYSIHPHGVSYEKDSEGASYsdqtgpdekkddavaPGETYTYVWIVTEESGPTKGDPACLT 151

                          170       180
                   ....*....|....*....|....*.
gi 1307738778  870 WAYHSTVDIVKDTYSGLIGTLVVCHR 895
Cdd:cd04199    152 WAYYSHVDLEKDINSGLIGPLLICKK 177
CuRO_2_ceruloplasmin cd11021
The second cupredoxin domain of Ceruloplasmin; Ceruloplasmin is a multicopper oxidase ...
 908-1049 1.83e-63

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: 211.18  E-value: 1.83e-63
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1307738778  908 QFALLFMVFDENESWYLDENIKTYSPNPHLVDKEDEEFLESNKMHAINGKVFGNLRGLTMHVGDRVSWYLMGMGNEIDIH 987
Cdd:cd11021      3 EFVLMFSVVDENLSWYLDENIKTYCSEPAKVDKDDEDFQESNKMHSINGYTFGNLPGLSMCAGDRVKWHLFGMGNEVDIH 82

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1307738778  988 TAHFHGHSFDYKQtgvYRADVFDLFPGTFQTVEMIPRNPGTWLLHCHVTDHVHAGMEATYTV 1049
Cdd:cd11021     83 SAFFHGQTLTDRG---HRTDTINLFPATFVTAEMVAQNPGKWLLSCQVNDHLKAGMQAFYEV 141
CuRO_4_ceruloplasmin cd11022
The fourth cupredoxin domain of Ceruloplasmin; Ceruloplasmin is a multicopper oxidase ...
 216-359 4.33e-63

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


Pssm-ID: 259908 [Multi-domain]  Cd Length: 144  Bit Score: 210.42  E-value: 4.33e-63
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1307738778  216 DAEFILMFSVMDENLSWYLDDNIRTYCSEPSKVDKDDEDFQESNKMHSINGYMYGYLPNLTMCVEDKVKWHLFGMGNEAD 295
Cdd:cd11022      1 DKEFFLLFTVFDENESWYLDENIQQFTLDPRSVDKEDEDFQESNKMHSINGYMYGNQPGLDMCKGDTVSWHLFGLGTETD 80

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1307738778  296 IHSAYFHGQTLIERHHRVDTISLFPATFVDAVMTPRNPGEWLLSCQVNDHIQGGMQALFKVKDC 359
Cdd:cd11022     81 VHGIYFSGNTFLLQGTRRDTANLFPHTSVTAIMQPDNEGTFEVNCQTTDHYSAGMRQIYTVSQC 144
CuRO_2_ceruloplasmin_like cd04200
Cupredoxin domains 2, 4, and 6 of ceruloplasmin and similar proteins; This family includes the ...
 568-708 1.68e-60

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


Pssm-ID: 259863 [Multi-domain]  Cd Length: 141  Bit Score: 203.03  E-value: 1.68e-60
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1307738778  568 DMEFFLLATVFDENLSWYLDDNILMFTLNPNKIDKDDEDFQESNKMHSINGYMYGNQPGLGMCKGSVVSWHLMGLGSEVD 647
Cdd:cd04200      1 DKEFVLLFAVFDENKSWYLEDNIKRFCDNPEKVDKDDEEFQESNKMHAINGYVFGNLPGLTMCAGDRVRWHLLGMGNEVD 80

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1307738778  648 VHGIYFSENTFTARGTRRDTANLFPHTFLTAIMKPDSEGVFEVSCLTTDHYTGGMKQNYRV 708
Cdd:cd04200     81 VHSIHFHGQTFLYKGYRIDTLTLFPATFETVEMVPSNPGTWLLHCHNSDHRHAGMQAYFLV 141
CuRO_2_ceruloplasmin cd11021
The second cupredoxin domain of Ceruloplasmin; Ceruloplasmin is a multicopper oxidase ...
 568-708 3.57e-60

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


Pssm-ID: 259907 [Multi-domain]  Cd Length: 141  Bit Score: 201.93  E-value: 3.57e-60
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1307738778  568 DMEFFLLATVFDENLSWYLDDNILMFTLNPNKIDKDDEDFQESNKMHSINGYMYGNQPGLGMCKGSVVSWHLMGLGSEVD 647
Cdd:cd11021      1 DREFVLMFSVVDENLSWYLDENIKTYCSEPAKVDKDDEDFQESNKMHSINGYTFGNLPGLSMCAGDRVKWHLFGMGNEVD 80

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1307738778  648 VHGIYFSENTFTARGTRRDTANLFPHTFLTAIMKPDSEGVFEVSCLTTDHYTGGMKQNYRV 708
Cdd:cd11021     81 IHSAFFHGQTLTDRGHRTDTINLFPATFVTAEMVAQNPGKWLLSCQVNDHLKAGMQAFYEV 141
CuRO_3_FV_like cd14450
The third cupredoxin domain of coagulation factor V and similar proteins; Factor V is an ...
 375-554 1.72e-59

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: 201.64  E-value: 1.72e-59
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1307738778  375 YFIAAEEVIWNYGPSamnhftgqelIADSESRVF----FEQSEMRIGGSYKKAVYKEYTDGSFTEH--KKRVAEEahlGL 448
Cdd:cd14450      5 YFIAAEEVIWDYAPS----------IPENMDKRYrsqyLDNFSNNIGKKYKKAVFTQYEDGSFTKRleNPRPKEE---GI 71

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1307738778  449 LGPVIKAEVGESIRVTFRNNASRPFSIQPHGLSYRKSDEGASYS---RGTDSPASHVSPGATFTYEWNVPEDVGPTDQDP 525
Cdd:cd14450     72 LGPVIRAQVRDTIKIVFKNKASRPYSIYPHGVTVSKAAEGASYPpdpRGNETQNKAVQPGETYTYKWNILETDEPTARDP 151

                          170       180
                   ....*....|....*....|....*....
gi 1307738778  526 DCLTWLYYSAVDAVRDTSAGLVGPLLVCR 554
Cdd:cd14450    152 RCLTRMYHSAVDITRDIASGLIGPLLICK 180
CuRO_5_ceruloplasmin cd04225
The fifth cupredoxin domain of Ceruloplasmin; Ceruloplasmin is a multicopper oxidase essential ...
 373-555 1.92e-59

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


Pssm-ID: 259887 [Multi-domain]  Cd Length: 171  Bit Score: 201.16  E-value: 1.92e-59
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1307738778  373 RRYFIAAEEVIWNYGPSAMNHFTGQELIADSESRVFFEQSEMRIGGSYKKAVYKEYTDGSFTEHKKRVAEEAHLGLLGPV 452
Cdd:cd04225      1 RTYYIAAEEVEWDYSPQRTWEQELHNTHEESPGNAFLNKGDKFIGSKYKKVVYREYTDDTFSVPKERTAEEEHLGILGPL 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1307738778  453 IKAEVGESIRVTFRNNASRPFSIQPHGLSyrksdegasysrgTDSPA-SHVSPGATFTYEWNVPEDVGPTDQDPDCLTWL 531
Cdd:cd04225     81 IHAEVGEKVKIVFKNMASRPYSIHAHGVK-------------TDSSWvAPTEPGETQTYTWKIPERSGPGVEDSNCISWA 147

                          170       180
                   ....*....|....*....|....
gi 1307738778  532 YYSAVDAVRDTSAGLVGPLLVCRR 555
Cdd:cd04225    148 YYSTVDQIKDLYSGLIGPLVICRR 171
CuRO_3_ceruloplasmin cd04224
The third cupredoxin domain of Ceruloplasmin; Ceruloplasmin is a multicopper oxidase essential ...
 723-893 9.90e-58

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


Pssm-ID: 259886 [Multi-domain]  Cd Length: 197  Bit Score: 197.31  E-value: 9.90e-58
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1307738778  723 HEKTYYIAAVEVEWDYSPNRTWEFERHQY-HEDSPGNQFLNREDRFIGSKYRKVVYREYTDGTFSTPKHRAEEQQHLEIQ 801
Cdd:cd04224      2 KVRHYFIAAEEIMWDYAPSGKNLFTGQNLtAPGSDSEVFFQRNETRIGGTYWKVRYVEYTDATFTTRKHRSKEEEHLGIL 81

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1307738778  802 GPLLMSNIGDKIVIVFKNLASRPYSIHAHGV------------KTDSSAVAVTNPGETKTYVWKIPARSSSERGDPPCIA 869
Cdd:cd04224     82 GPVIRAEVGDTIKVTFRNKASRPFSIQPHGVfyeknyegamyrDGDPSPGSHVSPGETFTYEWTVPEGVGPTNQDPPCLT 161

                          170       180
                   ....*....|....*....|....
gi 1307738778  870 WAYHSTVDIVKDTYSGLIGTLVVC 893
Cdd:cd04224    162 YLYFSAVDPVRDTNSGLVGPLLVC 185
CuRO_1_Ceruloplasmin_like_1 cd04229
cupredoxin domain of ceruloplasmin homologs; Uncharacterized subfamily of ceruloplasmin ...
 373-556 1.11e-57

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


Pssm-ID: 259891 [Multi-domain]  Cd Length: 175  Bit Score: 196.48  E-value: 1.11e-57
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1307738778  373 RRYFIAAEEVIWNYGPSAMNH-FTGQELiadSESRVFFEQSEMRIGGSYKKAVYKEYTDGSFTEhkkRVAEEAHLGLLGP 451
Cdd:cd04229      1 RTYYIAAEEVDWDYAPSGKNKcCLGDDL---EVSTLDSQPGPYTIGSTYTKARYREYTDNSFST---PKPTPAYLGILGP 74

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1307738778  452 VIKAEVGESIRVTFRNNASR-PFSIQPHGLSYRKSDEGASysRGTDSPashVSPGATFTYEWNVPEDVGPTDQDPDCLTW 530
Cdd:cd04229     75 VIRAEVGDTIKVVFKNNLDEfPVNMHPHGGLYSKDNEGTT--DGAGDV---VAPGETYTYRWIVPEDAGPGPGDPSSRLW 149

                          170       180
                   ....*....|....*....|....*.
gi 1307738778  531 LYYSAVDAVRDTSAGLVGPLLVCRRG 556
Cdd:cd04229    150 LYHSHVDVFAHTNAGLVGPIIVTSKG 175
CuRO_4_ceruloplasmin cd11022
The fourth cupredoxin domain of Ceruloplasmin; Ceruloplasmin is a multicopper oxidase ...
 908-1049 1.20e-57

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: 195.01  E-value: 1.20e-57
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1307738778  908 QFALLFMVFDENESWYLDENIKTYSPNPHLVDKEDEEFLESNKMHAINGKVFGNLRGLTMHVGDRVSWYLMGMGNEIDIH 987
Cdd:cd11022      3 EFFLLFTVFDENESWYLDENIQQFTLDPRSVDKEDEDFQESNKMHSINGYMYGNQPGLDMCKGDTVSWHLFGLGTETDVH 82

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1307738778  988 TAHFHGHSFDYKQTgvyRADVFDLFPGTFQTVEMIPRNPGTWLLHCHVTDHVHAGMEATYTV 1049
Cdd:cd11022     83 GIYFSGNTFLLQGT---RRDTANLFPHTSVTAIMQPDNEGTFEVNCQTTDHYSAGMRQIYTV 141
CuRO_3_ceruloplasmin cd04224
The third cupredoxin domain of Ceruloplasmin; Ceruloplasmin is a multicopper oxidase essential ...
 22-210 2.56e-56

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: 193.46  E-value: 2.56e-56
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1307738778   22 REYYIGISETEWSYAPGDASAVSGRRL-AEDEQARVFLQRGPHRIGSTYKKAVYTQYTDQLYDVA---VDKPSWLGFLGP 97
Cdd:cd04224      4 RHYFIAAEEIMWDYAPSGKNLFTGQNLtAPGSDSEVFFQRNETRIGGTYWKVRYVEYTDATFTTRkhrSKEEEHLGILGP 83

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1307738778   98 IIKGEVGDSIIIHLKNFASRNYTLHPHGVTYTKENEGALYPDNTGavqKRDDAVEPGGQFTYTWDVTEDQGPAEGDADCV 177
Cdd:cd04224     84 VIRAEVGDTIKVTFRNKASRPFSIQPHGVFYEKNYEGAMYRDGDP---SPGSHVSPGETFTYEWTVPEGVGPTNQDPPCL 160

                          170       180       190
                   ....*....|....*....|....*....|...
gi 1307738778  178 TRAYHSHIDAPRDVASGLVGPLIICRKGTMNTD 210
Cdd:cd04224    161 TYLYFSAVDPVRDTNSGLVGPLLVCKKGSLNAN 193
CuRO_3_FV_like cd14450
The third cupredoxin domain of coagulation factor V and similar proteins; Factor V is an ...
 23-203 1.58e-54

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: 187.78  E-value: 1.58e-54
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1307738778   23 EYYIGISETEWSYAPGDASAVSGRRLAEdeqarvFLQRGPHRIGSTYKKAVYTQYTDQLYD--VAVDKPSWLGFLGPIIK 100
Cdd:cd14450      4 EYFIAAEEVIWDYAPSIPENMDKRYRSQ------YLDNFSNNIGKKYKKAVFTQYEDGSFTkrLENPRPKEEGILGPVIR 77

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1307738778  101 GEVGDSIIIHLKNFASRNYTLHPHGVTYTKENEGALYPDNTGAVQKRDDAVEPGGQFTYTWDVTEDQGPAEGDADCVTRA 180
Cdd:cd14450     78 AQVRDTIKIVFKNKASRPYSIYPHGVTVSKAAEGASYPPDPRGNETQNKAVQPGETYTYKWNILETDEPTARDPRCLTRM 157

                          170       180
                   ....*....|....*....|...
gi 1307738778  181 YHSHIDAPRDVASGLVGPLIICR 203
Cdd:cd14450    158 YHSAVDITRDIASGLIGPLLICK 180
CuRO_1_FVIII_like cd14452
The first cupredoxin domain of coagulation factor VIII and similar proteins; Factor VIII ...
 22-205 5.02e-54

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: 185.95  E-value: 5.02e-54
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1307738778   22 REYYIGISETEWSYAPGDasavsgrrlaeDEQARVFLQRGPHRIGSTYKKAVYTQYTDQLYDVAVDKPSWLGFLGPIIKG 101
Cdd:cd14452      1 RRYYIAAVEIGWDYIHSD-----------LGDPASEQRKKPKDIPQKYIKAVFVEYLDATFTVPKPRPAWMGLLGPTIVA 69

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1307738778  102 EVGDSIIIHLKNFASRNYTLHPHGVTYTKENEGALYPDNTGAVQKRDDAVEPGGQFTYTWDVTEDQGPAEGDADCVTRAY 181
Cdd:cd14452     70 EVGDTVVITFKNLASQPYSLHAVGVSYWKASEGAGYDDSTSQHEKEDDAVYPGGYHTYVWDISPKDGPTGSDPECLTYSY 149

                          170       180
                   ....*....|....*....|....
gi 1307738778  182 HSHIDAPRDVASGLVGPLIICRKG 205
Cdd:cd14452    150 SSQVDPVKDVNSGLIGALLVCRMG 173
CuRO_5_FV_like cd14451
The fifth cupredoxin domain of coagulation factor V and similar proteins; Factor V is an ...
 373-556 9.34e-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: 185.04  E-value: 9.34e-54
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1307738778  373 RRYFIAAEEVIWNYGPSAmnhftgqeliadsESRVFFEQSEMRigGSYKKAVYKEYTDGSFTEHKKRVAEEAHLGLLGPV 452
Cdd:cd14451      2 RRYYIAAEEEEWDYAGYG-------------KSRLDKTQNERD--TVFKKVVFRRYLDSTFSTPDIQGEYEEHLGILGPV 66

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1307738778  453 IKAEVGESIRVTFRNNASRPFSIQPHGLSYRKSDEGASYSrgTDSPA-----SHVSPGATFTYEWNVPEDVGPTDQDPDC 527
Cdd:cd14451     67 IRAEVDDVIQVFFKNLASRPYSLHAHGLSYEKSSEGLSYD--DESPDwfkkdDAVQPNGTYTYVWYANPRSGPENNGSDC 144

                          170       180
                   ....*....|....*....|....*....
gi 1307738778  528 LTWLYYSAVDAVRDTSAGLVGPLLVCRRG 556
Cdd:cd14451    145 RTWAYYSAVNPEKDIHSGLIGPLLICRKG 173
CuRO_6_ceruloplasmin cd11012
The sixth cupredoxin domain of Ceruloplasmin; Ceruloplasmin is a multicopper oxidase essential ...
 218-356 4.15e-53

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: 181.99  E-value: 4.15e-53
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1307738778  218 EFILMFSVMDENLSWYLDDNIRTYCSEPSKVDKDDEDFQESNKMHSINGYMYGYLPNLTMCVEDKVKWHLFGMGNEADIH 297
Cdd:cd11012      3 EFALLFLVFDENESWYLDENIKTYSDHPEKVNKEDEEFIESNKMHAINGKVFGNLQGLTMHVGDEVYWYLMGMGNEIDIH 82

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1307738778  298 SAYFHGQTLIERH---HRVDTISLFPATFVDAVMTPRNPGEWLLSCQVNDHIQGGMQALFKV 356
Cdd:cd11012     83 TAHFHGHSFDYKHrgvYRSDVFDLFPGTFQTVEMIPRTPGTWLLHCHVTDHIHAGMETTYTV 144
CuRO_1_FV_like cd04226
The first cupredoxin domain of coagulation factor VIII and similar proteins; Factor V is an ...
 22-205 9.89e-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: 178.90  E-value: 9.89e-52
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1307738778   22 REYYIGISETEWSYAPGDasavSGRRLAEDEQarvflqrgphrigsTYKKAVYTQYTDqlyDVAVDKPSWL--GFLGPII 99
Cdd:cd04226      1 REYYIAAQNIDWDYTPQS----EELRLKRSEQ--------------SFKKIVYREYEE---GFKKEKPADLssGLLGPTL 59

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1307738778  100 KGEVGDSIIIHLKNFASRNYTLHPHGVTYTKENEGALYPDNTGAVQKRDDAVEPGGQFTYTWDVTEDQGPAEGDADCVTR 179
Cdd:cd04226     60 RAEVGDTLIVHFKNMADKPLSIHPQGIAYGKKSEGSLYSDNTSPVEKLDDAVQPGQEYTYVWDITEEVGPTEADPPCLTY 139

                          170       180
                   ....*....|....*....|....*.
gi 1307738778  180 AYHSHIDAPRDVASGLVGPLIICRKG 205
Cdd:cd04226    140 IYYSHVNMVRDFNSGLIGALLICKKG 165
CuRO_1_Ceruloplasmin_like_1 cd04229
cupredoxin domain of ceruloplasmin homologs; Uncharacterized subfamily of ceruloplasmin ...
 22-205 1.94e-51

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: 178.76  E-value: 1.94e-51
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1307738778   22 REYYIGISETEWSYAPGDAS-AVSGRRLaedEQARVFLQRGPHRIGSTYKKAVYTQYTDQLYDVAVDKPSWLGFLGPIIK 100
Cdd:cd04229      1 RTYYIAAEEVDWDYAPSGKNkCCLGDDL---EVSTLDSQPGPYTIGSTYTKARYREYTDNSFSTPKPTPAYLGILGPVIR 77

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1307738778  101 GEVGDSIIIHLKN-FASRNYTLHPHGVTYTKENEGALypdntgavQKRDDAVEPGGQFTYTWDVTEDQGPAEGDADCVTR 179
Cdd:cd04229     78 AEVGDTIKVVFKNnLDEFPVNMHPHGGLYSKDNEGTT--------DGAGDVVAPGETYTYRWIVPEDAGPGPGDPSSRLW 149

                          170       180
                   ....*....|....*....|....*.
gi 1307738778  180 AYHSHIDAPRDVASGLVGPLIICRKG 205
Cdd:cd04229    150 LYHSHVDVFAHTNAGLVGPIIVTSKG 175
CuRO_5_FVIII_like cd04228
The fifth cupredoxin domain of coagulation factor VIII and similar proteins; Factor VIII ...
 372-556 3.24e-51

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: 177.77  E-value: 3.24e-51
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1307738778  372 VRRYFIAAEEVIWNYGPSAMNHFTgQELIADSESRVFFEQsemriggsYKKAVYKEYTDGSFTEHKKRVAEEAHLGLLGP 451
Cdd:cd04228      1 IRHYFIAAVEVLWDYGMQRPQHFL-RARDPNRGRRKSVPQ--------YKKVVFREYLDGSFTQPVYRGELDEHLGILGP 71

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1307738778  452 VIKAEVGESIRVTFRNNASRPFSIQPHGLSYRksDEGASYSRGtdspaSHVSPGATFTYEWNVPEDVGPTDQDPDCLTWL 531
Cdd:cd04228     72 YIRAEVEDNIMVTFKNLASRPYSFHSSLISYE--EDQRAEPRG-----NFVQPGEVQTYSWKVLHQMAPTKQEFDCKAWA 144

                          170       180
                   ....*....|....*....|....*
gi 1307738778  532 YYSAVDAVRDTSAGLVGPLLVCRRG 556
Cdd:cd04228    145 YFSNVDLEKDLHSGLIGPLIICKTG 169
CuRO_1_FV_like cd04226
The first cupredoxin domain of coagulation factor VIII and similar proteins; Factor V is an ...
 373-556 5.14e-49

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: 171.20  E-value: 5.14e-49
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1307738778  373 RRYFIAAEEVIWNYGPsamnhftGQEliadsesrvffEQSEMRIGGSYKKAVYKEYTDGsfteHKKRVAEEAHLGLLGPV 452
Cdd:cd04226      1 REYYIAAQNIDWDYTP-------QSE-----------ELRLKRSEQSFKKIVYREYEEG----FKKEKPADLSSGLLGPT 58

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1307738778  453 IKAEVGESIRVTFRNNASRPFSIQPHGLSYRKSDEGASYSRGTdSPASH----VSPGATFTYEWNVPEDVGPTDQDPDCL 528
Cdd:cd04226     59 LRAEVGDTLIVHFKNMADKPLSIHPQGIAYGKKSEGSLYSDNT-SPVEKlddaVQPGQEYTYVWDITEEVGPTEADPPCL 137

                          170       180
                   ....*....|....*....|....*...
gi 1307738778  529 TWLYYSAVDAVRDTSAGLVGPLLVCRRG 556
Cdd:cd04226    138 TYIYYSHVNMVRDFNSGLIGALLICKKG 165
CuRO_5_FV_like cd14451
The fifth cupredoxin domain of coagulation factor V and similar proteins; Factor V is an ...
 21-205 1.12e-47

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


Pssm-ID: 259993 [Multi-domain]  Cd Length: 173  Bit Score: 167.71  E-value: 1.12e-47
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1307738778   21 RREYYIGISETEWSYAPGDASAVSGRRLAEDeqarvflqrgphrigSTYKKAVYTQYTDQLY---DVAVDKPSWLGFLGP 97
Cdd:cd14451      1 KRRYYIAAEEEEWDYAGYGKSRLDKTQNERD---------------TVFKKVVFRRYLDSTFstpDIQGEYEEHLGILGP 65

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1307738778   98 IIKGEVGDSIIIHLKNFASRNYTLHPHGVTYTKENEGALYPDNTGAVQKRDDAVEPGGQFTYTWDVTEDQGPAEGDADCV 177
Cdd:cd14451     66 VIRAEVDDVIQVFFKNLASRPYSLHAHGLSYEKSSEGLSYDDESPDWFKKDDAVQPNGTYTYVWYANPRSGPENNGSDCR 145

                          170       180
                   ....*....|....*....|....*...
gi 1307738778  178 TRAYHSHIDAPRDVASGLVGPLIICRKG 205
Cdd:cd14451    146 TWAYYSAVNPEKDIHSGLIGPLLICRKG 173
CuRO_3_FVIII_like cd04227
The third cupredoxin domain of coagulation factor VIII and similar proteins; Factor VIII ...
 375-555 3.11e-47

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


Pssm-ID: 259889 [Multi-domain]  Cd Length: 177  Bit Score: 166.64  E-value: 3.11e-47
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1307738778  375 YFIAAEEVIWNYGPsamnhftgqeLIADSESR----VFFEQSEMRIGGSYKKAVYKEYTDGSFtehKKRVAEEAHLGLLG 450
Cdd:cd04227      5 HYIAAEELDWDYAP----------LLSSTDDRelqsRYLPTGPQRIGYKYKKVAFVEYTDKTF---KRREAKQTEKGILG 71

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1307738778  451 PVIKAEVGESIRVTFRNNASRPFSIQPHGLS----YRKSDEGASYSRGTDSPashVSPGATFTYEWNVPEDVGPTDQDPD 526
Cdd:cd04227     72 PLLKGEVGDQIHIMFKNTASRPYNIYPHGLTsvrpMYRSRNPAGEKDLKTMP---IGPGETFGYMWELTAEDGPTEEDPR 148

                          170       180
                   ....*....|....*....|....*....
gi 1307738778  527 CLTWLYYSAVDAVRDTSAGLVGPLLVCRR 555
Cdd:cd04227    149 CLTRLYQSTVDPERDLASGLIGPLLICKK 177
CuRO_1_FVIII_like cd14452
The first cupredoxin domain of coagulation factor VIII and similar proteins; Factor VIII ...
 373-556 1.53e-46

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: 164.38  E-value: 1.53e-46
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1307738778  373 RRYFIAAEEVIWNYgpsamNHFTGQELIADSESRVFFEQSEmriggsYKKAVYKEYTDGSFTEHKKRvaeEAHLGLLGPV 452
Cdd:cd14452      1 RRYYIAAVEIGWDY-----IHSDLGDPASEQRKKPKDIPQK------YIKAVFVEYLDATFTVPKPR---PAWMGLLGPT 66

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1307738778  453 IKAEVGESIRVTFRNNASRPFSIQPHGLSYRKSDEGASYSRGTDSPASH---VSPGATFTYEWNVPEDVGPTDQDPDCLT 529
Cdd:cd14452     67 IVAEVGDTVVITFKNLASQPYSLHAVGVSYWKASEGAGYDDSTSQHEKEddaVYPGGYHTYVWDISPKDGPTGSDPECLT 146

                          170       180
                   ....*....|....*....|....*..
gi 1307738778  530 WLYYSAVDAVRDTSAGLVGPLLVCRRG 556
Cdd:cd14452    147 YSYSSQVDPVKDVNSGLIGALLVCRMG 173
CuRO_3_FVIII_like cd04227
The third cupredoxin domain of coagulation factor VIII and similar proteins; Factor VIII ...
 23-204 2.40e-45

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


Pssm-ID: 259889 [Multi-domain]  Cd Length: 177  Bit Score: 161.25  E-value: 2.40e-45
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1307738778   23 EYYIGISETEWSYAPGDASAVsgrrlaEDEQARVFLQRGPHRIGSTYKKAVYTQYTDQLYDVAVDKPSWLGFLGPIIKGE 102
Cdd:cd04227      4 EHYIAAEELDWDYAPLLSSTD------DRELQSRYLPTGPQRIGYKYKKVAFVEYTDKTFKRREAKQTEKGILGPLLKGE 77

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1307738778  103 VGDSIIIHLKNFASRNYTLHPHGVTYTKenegALYPDNTGAVQK--RDDAVEPGGQFTYTWDVTEDQGPAEGDADCVTRA 180
Cdd:cd04227     78 VGDQIHIMFKNTASRPYNIYPHGLTSVR----PMYRSRNPAGEKdlKTMPIGPGETFGYMWELTAEDGPTEEDPRCLTRL 153

                          170       180
                   ....*....|....*....|....
gi 1307738778  181 YHSHIDAPRDVASGLVGPLIICRK 204
Cdd:cd04227    154 YQSTVDPERDLASGLIGPLLICKK 177
CuRO_1_Ceruloplasmin_like_1 cd04229
cupredoxin domain of ceruloplasmin homologs; Uncharacterized subfamily of ceruloplasmin ...
 725-892 5.38e-45

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: 160.27  E-value: 5.38e-45
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1307738778  725 KTYYIAAVEVEWDYSPNrtweferHQYHEDSPGNQ-----FLNREDRFIGSKYRKVVYREYTDGTFSTPKhraEEQQHLE 799
Cdd:cd04229      1 RTYYIAAEEVDWDYAPS-------GKNKCCLGDDLevstlDSQPGPYTIGSTYTKARYREYTDNSFSTPK---PTPAYLG 70

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1307738778  800 IQGPLLMSNIGDKIVIVFKN-LASRPYSIHAHGV-------KTDSSAVAVTNPGETKTYVWKIPARSSSERGDPPCIAWA 871
Cdd:cd04229     71 ILGPVIRAEVGDTIKVVFKNnLDEFPVNMHPHGGlyskdneGTTDGAGDVVAPGETYTYRWIVPEDAGPGPGDPSSRLWL 150

                          170       180
                   ....*....|....*....|.
gi 1307738778  872 YHSTVDIVKDTYSGLIGTLVV 892
Cdd:cd04229    151 YHSHVDVFAHTNAGLVGPIIV 171
CuRO_5_FV_like cd14451
The fifth cupredoxin domain of coagulation factor V and similar proteins; Factor V is an ...
 724-895 8.59e-45

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


Pssm-ID: 259993 [Multi-domain]  Cd Length: 173  Bit Score: 159.62  E-value: 8.59e-45
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1307738778  724 EKTYYIAAVEVEWDYSPnrtweferhqyhedsPGNQFLNREDRFIGSKYRKVVYREYTDGTFSTPKHRAEEQQHLEIQGP 803
Cdd:cd14451      1 KRRYYIAAEEEEWDYAG---------------YGKSRLDKTQNERDTVFKKVVFRRYLDSTFSTPDIQGEYEEHLGILGP 65

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1307738778  804 LLMSNIGDKIVIVFKNLASRPYSIHAHGVKTDSSAVAVT---------------NPGETKTYVWKIPARSSSERGDPPCI 868
Cdd:cd14451     66 VIRAEVDDVIQVFFKNLASRPYSLHAHGLSYEKSSEGLSyddespdwfkkddavQPNGTYTYVWYANPRSGPENNGSDCR 145

                          170       180
                   ....*....|....*....|....*..
gi 1307738778  869 AWAYHSTVDIVKDTYSGLIGTLVVCHR 895
Cdd:cd14451    146 TWAYYSAVNPEKDIHSGLIGPLLICRK 172
CuRO_1_ceruloplasmin cd04222
The first cupredoxin domain of Ceruloplasmin; Ceruloplasmin is a multicopper oxidase essential ...
 725-895 1.92e-44

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: 158.74  E-value: 1.92e-44
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1307738778  725 KTYYIAAVEVEWDYSPNRTWEFERHQYHEDSPGNQFLNREDRFIGSKYRKVVYREYTDGTFSTpkhRAEEQQHLEIQGPL 804
Cdd:cd04222      1 REYYIGIRETQWDYAPSGKNLITNQTFDDDEHASVFLKRGPDRIGRVYKKAVYLQYTDDTYRT---EIEKPVWLGFLGPI 77

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1307738778  805 LMSNIGDKIVIVFKNLASRPYSIHAHGV---KTDSSAVAVTN------------PGETKTYVWKIPARSSSERGDPPCIA 869
Cdd:cd04222     78 LKAEVGDVIVVHLKNFASRPYSLHPHGVfynKENEGALYPDNtsgfekaddavpPGGSYTYTWTVPEEQAPTKADANCLT 157

                          170       180
                   ....*....|....*....|....*.
gi 1307738778  870 WAYHSTVDIVKDTYSGLIGTLVVCHR 895
Cdd:cd04222    158 RIYHSHIDAPKDIASGLIGPLIICKK 183
CuRO_5_FVIII_like cd04228
The fifth cupredoxin domain of coagulation factor VIII and similar proteins; Factor VIII ...
 727-895 4.90e-44

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


Pssm-ID: 259890 [Multi-domain]  Cd Length: 169  Bit Score: 157.36  E-value: 4.90e-44
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1307738778  727 YYIAAVEVEWDYSPNRTWEFERHQYhedspgnqfLNREDRFIGSKYRKVVYREYTDGTFSTPKHRAEEQQHLEIQGPLLM 806
Cdd:cd04228      4 YFIAAVEVLWDYGMQRPQHFLRARD---------PNRGRRKSVPQYKKVVFREYLDGSFTQPVYRGELDEHLGILGPYIR 74

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1307738778  807 SNIGDKIVIVFKNLASRPYSIHAHGVKTDSSAVA-----VTNPGETKTYVWKIPARSSSERGDPPCIAWAYHSTVDIVKD 881
Cdd:cd04228     75 AEVEDNIMVTFKNLASRPYSFHSSLISYEEDQRAeprgnFVQPGEVQTYSWKVLHQMAPTKQEFDCKAWAYFSNVDLEKD 154

                          170
                   ....*....|....
gi 1307738778  882 TYSGLIGTLVVCHR 895
Cdd:cd04228    155 LHSGLIGPLIICKT 168
CuRO_5_ceruloplasmin cd04225
The fifth cupredoxin domain of Ceruloplasmin; Ceruloplasmin is a multicopper oxidase essential ...
 22-204 6.90e-44

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


Pssm-ID: 259887 [Multi-domain]  Cd Length: 171  Bit Score: 156.86  E-value: 6.90e-44
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1307738778   22 REYYIGISETEWSYAPGDASAVSGRRLAEDEQARVFLQRGPHRIGSTYKKAVYTQYTDQLYDVAVDKPS---WLGFLGPI 98
Cdd:cd04225      1 RTYYIAAEEVEWDYSPQRTWEQELHNTHEESPGNAFLNKGDKFIGSKYKKVVYREYTDDTFSVPKERTAeeeHLGILGPL 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1307738778   99 IKGEVGDSIIIHLKNFASRNYTLHPHGVtytKENEGALYPdntgavqkrddaVEPGGQFTYTWDVTEDQGPAEGDADCVT 178
Cdd:cd04225     81 IHAEVGEKVKIVFKNMASRPYSIHAHGV---KTDSSWVAP------------TEPGETQTYTWKIPERSGPGVEDSNCIS 145

                          170       180
                   ....*....|....*....|....*.
gi 1307738778  179 RAYHSHIDAPRDVASGLVGPLIICRK 204
Cdd:cd04225    146 WAYYSTVDQIKDLYSGLIGPLVICRR 171
CuRO_3_FV_like cd14450
The third cupredoxin domain of coagulation factor V and similar proteins; Factor V is an ...
 726-893 5.56e-42

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: 151.95  E-value: 5.56e-42
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1307738778  726 TYYIAAVEVEWDYSPNRTWEFERHQYhedspgNQFLNREDRFIGSKYRKVVYREYTDGTFstpKHRAEEQQHLE--IQGP 803
Cdd:cd14450      4 EYFIAAEEVIWDYAPSIPENMDKRYR------SQYLDNFSNNIGKKYKKAVFTQYEDGSF---TKRLENPRPKEegILGP 74

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1307738778  804 LLMSNIGDKIVIVFKNLASRPYSIHAHGVKTDSSAVAVT---------------NPGETKTYVWKIPARSSSERGDPPCI 868
Cdd:cd14450     75 VIRAQVRDTIKIVFKNKASRPYSIYPHGVTVSKAAEGASyppdprgnetqnkavQPGETYTYKWNILETDEPTARDPRCL 154

                          170       180
                   ....*....|....*....|....*
gi 1307738778  869 AWAYHSTVDIVKDTYSGLIGTLVVC 893
Cdd:cd14450    155 TRMYHSAVDITRDIASGLIGPLLIC 179
CuRO_6_FVIII_like cd11018
The sixth cupredoxin domain of coagulation factor VIII and similar proteins; Factor VIII ...
 908-1049 9.13e-42

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


Pssm-ID: 259904 [Multi-domain]  Cd Length: 144  Bit Score: 149.65  E-value: 9.13e-42
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1307738778  908 QFALLFMVFDENESWYLDENIKTYSPNPHLVDKEDEEFLESNKMHAINGKVFGNLRGLTMHVGDRVSWYLMGMGNEIDIH 987
Cdd:cd11018      3 EFALLFTIFDETKSWYFEENMRRNCRPPCHIQTQDPWFHINNKFHAINGYVADTLPGLVMAQHQRIRWHLLNMGSDEEIH 82

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1307738778  988 TAHFHGHSFDYKQTGVYRADVFDLFPGTFQTVEMIPRNPGTWLLHCHVTDHVHAGMEATYTV 1049
Cdd:cd11018     83 SVHFHGLPFTVRAKKEYRMGVYNLYPGVFGTVEMRPSTAGIWLVECTVGEHLLAGMSALFLV 144
CuRO_6_ceruloplasmin cd11012
The sixth cupredoxin domain of Ceruloplasmin; Ceruloplasmin is a multicopper oxidase essential ...
 570-708 2.63e-41

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


Pssm-ID: 259898 [Multi-domain]  Cd Length: 145  Bit Score: 148.48  E-value: 2.63e-41
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1307738778  570 EFFLLATVFDENLSWYLDDNILMFTLNPNKIDKDDEDFQESNKMHSINGYMYGNQPGLGMCKGSVVSWHLMGLGSEVDVH 649
Cdd:cd11012      3 EFALLFLVFDENESWYLDENIKTYSDHPEKVNKEDEEFIESNKMHAINGKVFGNLQGLTMHVGDEVYWYLMGMGNEIDIH 82

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1307738778  650 GIYFSENTFTARGT---RRDTANLFPHTFLTAIMKPDSEGVFEVSCLTTDHYTGGMKQNYRV 708
Cdd:cd11012     83 TAHFHGHSFDYKHRgvyRSDVFDLFPGTFQTVEMIPRTPGTWLLHCHVTDHIHAGMETTYTV 144
CuRO_3_FVIII_like cd04227
The third cupredoxin domain of coagulation factor VIII and similar proteins; Factor VIII ...
 726-895 1.53e-39

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: 144.69  E-value: 1.53e-39
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1307738778  726 TYYIAAVEVEWDYSPNRTWEFERhqyhedSPGNQFLNREDRFIGSKYRKVVYREYTDGTFstpKHRAEEQQHLEIQGPLL 805
Cdd:cd04227      4 EHYIAAEELDWDYAPLLSSTDDR------ELQSRYLPTGPQRIGYKYKKVAFVEYTDKTF---KRREAKQTEKGILGPLL 74

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1307738778  806 MSNIGDKIVIVFKNLASRPYSIHAHGVKTDSSAVAVTN-------------PGETKTYVWKIPARSSSERGDPPCIAWAY 872
Cdd:cd04227     75 KGEVGDQIHIMFKNTASRPYNIYPHGLTSVRPMYRSRNpagekdlktmpigPGETFGYMWELTAEDGPTEEDPRCLTRLY 154

                          170       180
                   ....*....|....*....|...
gi 1307738778  873 HSTVDIVKDTYSGLIGTLVVCHR 895
Cdd:cd04227    155 QSTVDPERDLASGLIGPLLICKK 177
CuRO_6_FVIII_like cd11018
The sixth cupredoxin domain of coagulation factor VIII and similar proteins; Factor VIII ...
 218-356 9.65e-37

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


Pssm-ID: 259904 [Multi-domain]  Cd Length: 144  Bit Score: 135.39  E-value: 9.65e-37
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1307738778  218 EFILMFSVMDENLSWYLDDNIRTYCSEPSKVDKDDEDFQESNKMHSINGYMYGYLPNLTMCVEDKVKWHLFGMGNEADIH 297
Cdd:cd11018      3 EFALLFTIFDETKSWYFEENMRRNCRPPCHIQTQDPWFHINNKFHAINGYVADTLPGLVMAQHQRIRWHLLNMGSDEEIH 82

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1307738778  298 SAYFHGQTLIER---HHRVDTISLFPATFVDAVMTPRNPGEWLLSCQVNDHIQGGMQALFKV 356
Cdd:cd11018     83 SVHFHGLPFTVRakkEYRMGVYNLYPGVFGTVEMRPSTAGIWLVECTVGEHLLAGMSALFLV 144
CuRO_2_ceruloplasmin_like_2 cd11023
cupredoxin domain of ceruloplasmin homologs; Uncharacterized subfamily of ceruloplasmin ...
 915-1049 8.85e-36

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: 131.58  E-value: 8.85e-36
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1307738778  915 VFDENESWYLDENIKtyspnphlvdkedeeflESNKMHAINGKVFGNLRGLTMHVGDRVSWYLMGMGNEIDIHTAHFHGH 994
Cdd:cd11023      3 EFIENSSIFLDLNVE-----------------EAGLMHSINGYVFGNLPGVTIAKGKRVRWHLVAYGNEVDFHTPHWHGQ 65

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 1307738778  995 SFDYKQTGvyRADVFDLFPGTFQTVEMIPRNPGTWLLHCHVTDHVHAGMEATYTV 1049
Cdd:cd11023     66 TVEADKSR--RTDVAELMPASMRVADMTAADVGTWLLHCHVHDHYMAGMMTQFAV 118
CuRO_6_FV_like cd14455
The sixth cupredoxin domain of coagulation factor V and similar proteins; Factor V is an ...
 908-1049 1.16e-35

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


Pssm-ID: 259997 [Multi-domain]  Cd Length: 140  Bit Score: 132.30  E-value: 1.16e-35
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1307738778  908 QFALLFMVFDENESWYLDENIKTYSPNphlVDKEDEEFLESNKMHAINGKVFgNLRGLTMHVGDRVSWYLMGMGNEIDIH 987
Cdd:cd14455      3 EFVLLFMTFDEEKSWYYEKNRKRTCRE---NRVKDPNVQDNHTFHAINGIIY-NLKGLRMYTNELVRWHLINMGGPKDLH 78

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1307738778  988 TAHFHGHSFDYKQTGVYRADVFDLFPGTFQTVEMIPRNPGTWLLHCHVTDHVHAGMEATYTV 1049
Cdd:cd14455     79 VVHFHGQTFTEKGLKDHQLGVYPLLPGSFATLEMKPSKPGLWLLETEVGESQQRGMQTLFLV 140
CuRO_1_FVIII_like cd14452
The first cupredoxin domain of coagulation factor VIII and similar proteins; Factor VIII ...
 725-893 2.32e-33

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


Pssm-ID: 259994 [Multi-domain]  Cd Length: 173  Bit Score: 126.63  E-value: 2.32e-33
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1307738778  725 KTYYIAAVEVEWDYSpnrtweferHQYHEDSPGNQFLNREDrfIGSKYRKVVYREYTDGTFSTPKHRAEeqqHLEIQGPL 804
Cdd:cd14452      1 RRYYIAAVEIGWDYI---------HSDLGDPASEQRKKPKD--IPQKYIKAVFVEYLDATFTVPKPRPA---WMGLLGPT 66

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1307738778  805 LMSNIGDKIVIVFKNLASRPYSIHAHGVK----------TDSSAVA-----VTNPGETKTYVWKIPARSSSERGDPPCIA 869
Cdd:cd14452     67 IVAEVGDTVVITFKNLASQPYSLHAVGVSywkasegagyDDSTSQHekeddAVYPGGYHTYVWDISPKDGPTGSDPECLT 146

                          170       180
                   ....*....|....*....|....
gi 1307738778  870 WAYHSTVDIVKDTYSGLIGTLVVC 893
Cdd:cd14452    147 YSYSSQVDPVKDVNSGLIGALLVC 170
CuRO_5_FVIII_like cd04228
The fifth cupredoxin domain of coagulation factor VIII and similar proteins; Factor VIII ...
 22-205 3.02e-33

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


Pssm-ID: 259890 [Multi-domain]  Cd Length: 169  Bit Score: 126.15  E-value: 3.02e-33
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1307738778   22 REYYIGISETEWSYapGDASAVSGRRLAEDEQARvflqRGPHRigsTYKKAVYTQYTDQLYDVAVDK---PSWLGFLGPI 98
Cdd:cd04228      2 RHYFIAAVEVLWDY--GMQRPQHFLRARDPNRGR----RKSVP---QYKKVVFREYLDGSFTQPVYRgelDEHLGILGPY 72

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1307738778   99 IKGEVGDSIIIHLKNFASRNYTLHPHGVTYtkenegalypDNTGAVQKRDDAVEPGGQFTYTWDVTEDQGPAEGDADCVT 178
Cdd:cd04228     73 IRAEVEDNIMVTFKNLASRPYSFHSSLISY----------EEDQRAEPRGNFVQPGEVQTYSWKVLHQMAPTKQEFDCKA 142

                          170       180
                   ....*....|....*....|....*..
gi 1307738778  179 RAYHSHIDAPRDVASGLVGPLIICRKG 205
Cdd:cd04228    143 WAYFSNVDLEKDLHSGLIGPLIICKTG 169
CuRO_2_FV_like cd14453
The second cupredoxin domain of coagulation factor V and similar proteins; Factor V is an ...
 216-356 3.32e-33

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


Pssm-ID: 259995 [Multi-domain]  Cd Length: 123  Bit Score: 124.59  E-value: 3.32e-33
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1307738778  216 DAEFILMFSVMDENLSWYlddnirtycsepskvdkdDEDFQESNKMHSINGYMYGYLPNLTMCVEDKVKWHLFGMGNEAD 295
Cdd:cd14453      1 YKEYVLMFGVFDENKSWY------------------KQNASVDSVKYTINGYTNGTLPDVSICAYDHVSWHLLGMSSEPE 62

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1307738778  296 IHSAYFHGQTLIERHHRVDTISLFPATFVDAVMTPRNPGEWLLSCQVNDHIQGGMQALFKV 356
Cdd:cd14453     63 LFSVHFNGQVLEQNGHKVSAVGLVSGSSTTASMTVVHTGRWLISSLIMKHLQAGMYGYLNI 123
CuRO_1_FV_like cd04226
The first cupredoxin domain of coagulation factor VIII and similar proteins; Factor V is an ...
 727-893 5.08e-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: 125.36  E-value: 5.08e-33
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1307738778  727 YYIAAVEVEWDYSPnrtweferhQYHEdspgnqflNREDRFiGSKYRKVVYREYTDGtFSTPKHRAEEQQHLeiqGPLLM 806
Cdd:cd04226      3 YYIAAQNIDWDYTP---------QSEE--------LRLKRS-EQSFKKIVYREYEEG-FKKEKPADLSSGLL---GPTLR 60

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1307738778  807 SNIGDKIVIVFKNLASRPYSIHAHGVK----------TDSSAVA-----VTNPGETKTYVWKIPARSSSERGDPPCIAWA 871
Cdd:cd04226     61 AEVGDTLIVHFKNMADKPLSIHPQGIAygkksegslySDNTSPVeklddAVQPGQEYTYVWDITEEVGPTEADPPCLTYI 140

                          170       180
                   ....*....|....*....|..
gi 1307738778  872 YHSTVDIVKDTYSGLIGTLVVC 893
Cdd:cd04226    141 YYSHVNMVRDFNSGLIGALLIC 162
CuRO_6_FV_like cd14455
The sixth cupredoxin domain of coagulation factor V and similar proteins; Factor V is an ...
 218-356 5.24e-33

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


Pssm-ID: 259997 [Multi-domain]  Cd Length: 140  Bit Score: 124.59  E-value: 5.24e-33
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1307738778  218 EFILMFSVMDENLSWYLDDNIRTYCSEpskVDKDDEDFQESNKMHSINGYMYGyLPNLTMCVEDKVKWHLFGMGNEADIH 297
Cdd:cd14455      3 EFVLLFMTFDEEKSWYYEKNRKRTCRE---NRVKDPNVQDNHTFHAINGIIYN-LKGLRMYTNELVRWHLINMGGPKDLH 78

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1307738778  298 SAYFHGQTLIE---RHHRVDTISLFPATFVDAVMTPRNPGEWLLSCQVNDHIQGGMQALFKV 356
Cdd:cd14455     79 VVHFHGQTFTEkglKDHQLGVYPLLPGSFATLEMKPSKPGLWLLETEVGESQQRGMQTLFLV 140
CuRO_2_ceruloplasmin_like_2 cd11023
cupredoxin domain of ceruloplasmin homologs; Uncharacterized subfamily of ceruloplasmin ...
 251-356 7.08e-33

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


Pssm-ID: 259909 [Multi-domain]  Cd Length: 118  Bit Score: 123.49  E-value: 7.08e-33
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1307738778  251 DDEDFQESNKMHSINGYMYGYLPNLTMCVEDKVKWHLFGMGNEADIHSAYFHGQTL-IERHHRVDTISLFPATFVDAVMT 329
Cdd:cd11023     12 LDLNVEEAGLMHSINGYVFGNLPGVTIAKGKRVRWHLVAYGNEVDFHTPHWHGQTVeADKSRRTDVAELMPASMRVADMT 91

                           90       100
                   ....*....|....*....|....*..
gi 1307738778  330 PRNPGEWLLSCQVNDHIQGGMQALFKV 356
Cdd:cd11023     92 AADVGTWLLHCHVHDHYMAGMMTQFAV 118
CuRO_4_FVIII_like cd11016
The fourth cupredoxin domain of coagulation factor VIII and similar proteins; Factor VIII ...
 216-359 9.94e-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: 123.82  E-value: 9.94e-33
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1307738778  216 DAEFILMFSVMDENLSWYLDDNIRTYCSEPSKVDKDDEDFQESNKMHSINGYMYGYLpNLTMCVEDKVKWHLFGMGNEAD 295
Cdd:cd11016      1 DKDWSLLFSVFDENNSWYLKENIHRFTQTPAGVNDTDPDFYASNVMHTINGIVFDRR-QFVICLTDVAYWYVLSVGAQTD 79

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1307738778  296 IHSAYFHGQTLIERHHRVDTISLFPATFVDAVMTPRNPGEWLLSCQVNDHIQGGMQALFKVKDC 359
Cdd:cd11016     80 FLSVFFSGNTFKHQMVYEDVLTLFPFSGETVSMSPEVPGEWELGCFNGDFRSRGMSAQYTVSTC 143
CuRO_4_FVIII_like cd11016
The fourth cupredoxin domain of coagulation factor VIII and similar proteins; Factor VIII ...
 568-711 1.78e-32

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


Pssm-ID: 259902 [Multi-domain]  Cd Length: 143  Bit Score: 123.05  E-value: 1.78e-32
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1307738778  568 DMEFFLLATVFDENLSWYLDDNILMFTLNPNKIDKDDEDFQESNKMHSINGYMYGNQPgLGMCKGSVVSWHLMGLGSEVD 647
Cdd:cd11016      1 DKDWSLLFSVFDENNSWYLKENIHRFTQTPAGVNDTDPDFYASNVMHTINGIVFDRRQ-FVICLTDVAYWYVLSVGAQTD 79

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1307738778  648 VHGIYFSENTFTARGTRRDTANLFPHTFLTAIMKPDSEGVFEVSCLTTDHYTGGMKQNYRVKQC 711
Cdd:cd11016     80 FLSVFFSGNTFKHQMVYEDVLTLFPFSGETVSMSPEVPGEWELGCFNGDFRSRGMSAQYTVSTC 143
CuRO_4_FV_like cd14454
The fourth cupredoxin domain of coagulation factor V and similar proteins; Factor V is an ...
 216-359 3.30e-32

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: 122.29  E-value: 3.30e-32
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1307738778  216 DAEFILMFSVMDENLSWYLDDNIRTYCSEPSKVDKDDEDFQESNKMHSINGYMYGYLPNLTMCVEDKVKWHLFGMGNEAD 295
Cdd:cd14454      1 DLEQHAVFAVFDENKSWYLEENINKYCSNPNNVKKDDPKFYKSNIMPTINGYAYESSAPLGFCHSEVVQWHISSVGTQDE 80

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1307738778  296 IHSAYFHGQTLIERHHRVDTISLFPATFVDAVMTPRNPGEWLLSCQVNDHIQGGMQALFKVKDC 359
Cdd:cd14454     81 IITVHLSGHTFRYKGKHEDTLNLFPMSGESITVTMDNLGTWLLGSFGSSKKSKGLRVRFTDVIC 144
CuRO_2_FVIII_like cd11015
The second cupredoxin domain of coagulation factor VIII and similar proteins; Factor VIII ...
 218-356 7.78e-32

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


Pssm-ID: 259901 [Multi-domain]  Cd Length: 134  Bit Score: 120.78  E-value: 7.78e-32
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1307738778  218 EFILMFSVMDENLSWYLDDnirtycSEPSKVDKDDEDfQESNKMHSINGYMYGYLPNLTMCVEDKVKWHLFGMGNEADIH 297
Cdd:cd11015      3 AFVLLFAVFDEGKSWYSEV------GERKSRDKFKRA-DSRKEFHTINGYINASLPGLKICQRKPVIWHVIGMGTAPEVH 75

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 1307738778  298 SAYFHGQTLIERHHRVDTISLFPATFVDAVMTPRNPGEWLLSCQVNDHIQGGMQALFKV 356
Cdd:cd11015     76 SIFFEGHTFLVRTHRKVSLEISPMTFLTAQTKPATVGSFLIFCQIHSHQHDGMEAMVKV 134
CuRO_4_FVIII_like cd11016
The fourth cupredoxin domain of coagulation factor VIII and similar proteins; Factor VIII ...
 911-1050 5.87e-31

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


Pssm-ID: 259902 [Multi-domain]  Cd Length: 143  Bit Score: 118.82  E-value: 5.87e-31
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1307738778  911 LLFMVFDENESWYLDENIKTYSPNPHLVDKEDEEFLESNKMHAINGKVFGNLRgLTMHVGDRVSWYLMGMGNEIDIHTAH 990
Cdd:cd11016      6 LLFSVFDENNSWYLKENIHRFTQTPAGVNDTDPDFYASNVMHTINGIVFDRRQ-FVICLTDVAYWYVLSVGAQTDFLSVF 84

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1307738778  991 FHGHSFdyKQTGVYRaDVFDLFPGTFQTVEMIPRNPGTWLLHCHVTDHVHAGMEATYTVL 1050
Cdd:cd11016     85 FSGNTF--KHQMVYE-DVLTLFPFSGETVSMSPEVPGEWELGCFNGDFRSRGMSAQYTVS 141
CuRO_4_FV_like cd14454
The fourth cupredoxin domain of coagulation factor V and similar proteins; Factor V is an ...
 568-711 2.71e-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: 116.89  E-value: 2.71e-30
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1307738778  568 DMEFFLLATVFDENLSWYLDDNILMFTLNPNKIDKDDEDFQESNKMHSINGYMYGNQPGLGMCKGSVVSWHLMGLGSEVD 647
Cdd:cd14454      1 DLEQHAVFAVFDENKSWYLEENINKYCSNPNNVKKDDPKFYKSNIMPTINGYAYESSAPLGFCHSEVVQWHISSVGTQDE 80

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1307738778  648 VHGIYFSENTFTARGTRRDTANLFPHTFLTAIMKPDSEGVFEVSCLTTDHYTGGMKQNYRVKQC 711
Cdd:cd14454     81 IITVHLSGHTFRYKGKHEDTLNLFPMSGESITVTMDNLGTWLLGSFGSSKKSKGLRVRFTDVIC 144
CuRO_4_FV_like cd14454
The fourth cupredoxin domain of coagulation factor V and similar proteins; Factor V is an ...
 912-1031 1.54e-28

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: 111.89  E-value: 1.54e-28
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1307738778  912 LFMVFDENESWYLDENIKTYSPNPHLVDKEDEEFLESNKMHAINGKVFGNLRGLTMHVGDRVSWYLMGMGNEIDIHTAHF 991
Cdd:cd14454      7 VFAVFDENKSWYLEENINKYCSNPNNVKKDDPKFYKSNIMPTINGYAYESSAPLGFCHSEVVQWHISSVGTQDEIITVHL 86

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|
gi 1307738778  992 HGHSFDYKQTgvyRADVFDLFPGTFQTVEMIPRNPGTWLL 1031
Cdd:cd14454     87 SGHTFRYKGK---HEDTLNLFPMSGESITVTMDNLGTWLL 123
CuRO_6_FVIII_like cd11018
The sixth cupredoxin domain of coagulation factor VIII and similar proteins; Factor VIII ...
 570-708 2.90e-28

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


Pssm-ID: 259904 [Multi-domain]  Cd Length: 144  Bit Score: 111.13  E-value: 2.90e-28
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1307738778  570 EFFLLATVFDENLSWYLDDNILMFTLNPNKIDKDDEDFQESNKMHSINGYMYGNQPGLGMCKGSVVSWHLMGLGSEVDVH 649
Cdd:cd11018      3 EFALLFTIFDETKSWYFEENMRRNCRPPCHIQTQDPWFHINNKFHAINGYVADTLPGLVMAQHQRIRWHLLNMGSDEEIH 82

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1307738778  650 GIYFSENTFTARGT---RRDTANLFPHTFLTAIMKPDSEGVFEVSCLTTDHYTGGMKQNYRV 708
Cdd:cd11018     83 SVHFHGLPFTVRAKkeyRMGVYNLYPGVFGTVEMRPSTAGIWLVECTVGEHLLAGMSALFLV 144
CuRO_2_ceruloplasmin_like_2 cd11023
cupredoxin domain of ceruloplasmin homologs; Uncharacterized subfamily of ceruloplasmin ...
 603-708 3.06e-24

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


Pssm-ID: 259909 [Multi-domain]  Cd Length: 118  Bit Score: 98.84  E-value: 3.06e-24
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1307738778  603 DDEDFQESNKMHSINGYMYGNQPGLGMCKGSVVSWHLMGLGSEVDVHGIYFSENTFTARGTRR-DTANLFPHTFLTAIMK 681
Cdd:cd11023     12 LDLNVEEAGLMHSINGYVFGNLPGVTIAKGKRVRWHLVAYGNEVDFHTPHWHGQTVEADKSRRtDVAELMPASMRVADMT 91

                           90       100
                   ....*....|....*....|....*..
gi 1307738778  682 PDSEGVFEVSCLTTDHYTGGMKQNYRV 708
Cdd:cd11023     92 AADVGTWLLHCHVHDHYMAGMMTQFAV 118
CuRO_2_FVIII_like cd11015
The second cupredoxin domain of coagulation factor VIII and similar proteins; Factor VIII ...
 570-708 1.97e-23

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


Pssm-ID: 259901 [Multi-domain]  Cd Length: 134  Bit Score: 96.90  E-value: 1.97e-23
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1307738778  570 EFFLLATVFDENLSWYLDdnilmfTLNPNKIDKDDEDfQESNKMHSINGYMYGNQPGLGMCKGSVVSWHLMGLGSEVDVH 649
Cdd:cd11015      3 AFVLLFAVFDEGKSWYSE------VGERKSRDKFKRA-DSRKEFHTINGYINASLPGLKICQRKPVIWHVIGMGTAPEVH 75

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 1307738778  650 GIYFSENTFTARGTRRDTANLFPHTFLTAIMKPDSEGVFEVSCLTTDHYTGGMKQNYRV 708
Cdd:cd11015     76 SIFFEGHTFLVRTHRKVSLEISPMTFLTAQTKPATVGSFLIFCQIHSHQHDGMEAMVKV 134
CuRO_2_FVIII_like cd11015
The second cupredoxin domain of coagulation factor VIII and similar proteins; Factor VIII ...
 908-1049 8.96e-22

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


Pssm-ID: 259901 [Multi-domain]  Cd Length: 134  Bit Score: 92.28  E-value: 8.96e-22
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1307738778  908 QFALLFMVFDENESWYLDENiktyspNPHLVDKEDEEFlESNKMHAINGKVFGNLRGLTMHVGDRVSWYLMGMGNEIDIH 987
Cdd:cd11015      3 AFVLLFAVFDEGKSWYSEVG------ERKSRDKFKRAD-SRKEFHTINGYINASLPGLKICQRKPVIWHVIGMGTAPEVH 75

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1307738778  988 TAHFHGHSFDYKQtgvYRADVFDLFPGTFQTVEMIPRNPGTWLLHCHVTDHVHAGMEATYTV 1049
Cdd:cd11015     76 SIFFEGHTFLVRT---HRKVSLEISPMTFLTAQTKPATVGSFLIFCQIHSHQHDGMEAMVKV 134
CuRO_2_FV_like cd14453
The second cupredoxin domain of coagulation factor V and similar proteins; Factor V is an ...
 908-1045 2.24e-19

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: 84.91  E-value: 2.24e-19
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1307738778  908 QFALLFMVFDENESWYldeniKTYSPNPHLvdkedeeflesnkMHAINGKVFGNLRGLTMHVGDRVSWYLMGMGNEIDIH 987
Cdd:cd14453      3 EYVLMFGVFDENKSWY-----KQNASVDSV-------------KYTINGYTNGTLPDVSICAYDHVSWHLLGMSSEPELF 64

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 1307738778  988 TAHFHGHSFDYKQtgvYRADVFDLFPGTFQTVEMIPRNPGTWLLHCHVTDHVHAGMEA 1045
Cdd:cd14453     65 SVHFNGQVLEQNG---HKVSAVGLVSGSSTTASMTVVHTGRWLISSLIMKHLQAGMYG 119
Cu-oxidase_2 pfam07731
Multicopper oxidase; This entry contains many divergent copper oxidase-like domains that are ...
 949-1053 4.34e-19

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


Pssm-ID: 462246 [Multi-domain]  Cd Length: 138  Bit Score: 84.79  E-value: 4.34e-19
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1307738778  949 NKMHAINGKVFG-NLRGLTMHVGDRVSWYLMGMGNeiDIHTAHFHGHSFDYKQTGV----------------YRADVFDL 1011
Cdd:pfam07731   19 RNDWAINGLLFPpNTNVITLPYGTVVEWVLQNTTT--GVHPFHLHGHSFQVLGRGGgpwpeedpktynlvdpVRRDTVQV 96

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|..
gi 1307738778 1012 FPGTFQTVEMIPRNPGTWLLHCHVTDHVHAGMEATYTVLPRE 1053
Cdd:pfam07731   97 PPGGWVAIRFRADNPGVWLFHCHILWHLDQGMMGQFVVRPGD 138
CuRO_6_FV_like cd14455
The sixth cupredoxin domain of coagulation factor V and similar proteins; Factor V is an ...
 570-686 3.16e-18

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


Pssm-ID: 259997 [Multi-domain]  Cd Length: 140  Bit Score: 82.22  E-value: 3.16e-18
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1307738778  570 EFFLLATVFDENLSWYLDDNIlmfTLNPNKIDKDDEDFQESNKMHSINGYMYgNQPGLGMCKGSVVSWHLMGLGSEVDVH 649
Cdd:cd14455      3 EFVLLFMTFDEEKSWYYEKNR---KRTCRENRVKDPNVQDNHTFHAINGIIY-NLKGLRMYTNELVRWHLINMGGPKDLH 78

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|
gi 1307738778  650 GIYFSENTFTARGT---RRDTANLFPHTFLTAIMKPDSEG 686
Cdd:cd14455     79 VVHFHGQTFTEKGLkdhQLGVYPLLPGSFATLEMKPSKPG 118
CuRO_1_LCC_like cd04206
Cupredoxin domain 1 of laccase-like multicopper oxidases; including laccase, CueO, spore coat ...
 93-202 5.51e-17

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


Pssm-ID: 259869 [Multi-domain]  Cd Length: 120  Bit Score: 78.10  E-value: 5.51e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1307738778   93 GFLGPIIKGEVGDSIIIHLKN-FASRNYTLHPHGVTYTKENEGalypdnTGAVQKRDDAVEPGGQFTYTWDVTEDQGpae 171
Cdd:cd04206     27 QFPGPTIRVKEGDTVEVTVTNnLPNEPTSIHWHGLRQPGTNDG------DGVAGLTQCPIPPGESFTYRFTVDDQAG--- 97

                           90       100       110
                   ....*....|....*....|....*....|.
gi 1307738778  172 gdadcvTRAYHSHIDAprDVASGLVGPLIIC 202
Cdd:cd04206     98 ------TFWYHSHVGG--QRADGLYGPLIVE 120
CuRO_2_FV_like cd14453
The second cupredoxin domain of coagulation factor V and similar proteins; Factor V is an ...
 568-702 1.58e-16

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: 76.82  E-value: 1.58e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1307738778  568 DMEFFLLATVFDENLSWYlddnilmfTLNPnkidkddedfQESNKMHSINGYMYGNQPGLGMCKGSVVSWHLMGLGSEVD 647
Cdd:cd14453      1 YKEYVLMFGVFDENKSWY--------KQNA----------SVDSVKYTINGYTNGTLPDVSICAYDHVSWHLLGMSSEPE 62

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 1307738778  648 VHGIYFSENTFTARGTRRDTANLFPHTFLTAIMKPDSEGVFEVSCLTTDHYTGGM 702
Cdd:cd14453     63 LFSVHFNGQVLEQNGHKVSAVGLVSGSSTTASMTVVHTGRWLISSLIMKHLQAGM 117
CuRO_1_LCC_like cd04206
Cupredoxin domain 1 of laccase-like multicopper oxidases; including laccase, CueO, spore coat ...
 447-553 8.16e-15

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


Pssm-ID: 259869 [Multi-domain]  Cd Length: 120  Bit Score: 71.93  E-value: 8.16e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1307738778  447 GLLGPVIKAEVGESIRVTFRNN-ASRPFSIQPHGLSYRKSDEGASYSRGTdspASHVSPGATFTYEWNVPEDVGptdqdp 525
Cdd:cd04206     27 QFPGPTIRVKEGDTVEVTVTNNlPNEPTSIHWHGLRQPGTNDGDGVAGLT---QCPIPPGESFTYRFTVDDQAG------ 97

                           90       100
                   ....*....|....*....|....*...
gi 1307738778  526 dclTWLYYSAVDAVRDtsAGLVGPLLVC 553
Cdd:cd04206     98 ---TFWYHSHVGGQRA--DGLYGPLIVE 120
CuRO_3_LCC_like cd04207
Cupredoxin domain 3 of laccase-like multicopper oxidases; including laccase, CueO, spore coat ...
 953-1048 2.98e-14

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


Pssm-ID: 259870 [Multi-domain]  Cd Length: 132  Bit Score: 70.57  E-value: 2.98e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1307738778  953 AINGKVF----GNLRGLTMHVGDRVSWYLMGMGNEIDIHTAHFHGHSF------------DYKQTGVYRADVFDLFPGTF 1016
Cdd:cd04207     21 VINGMPFkegdANTDIFSVEAGDVVEIVLINAGNHDMQHPFHLHGHSFwvlgsgggpfdaPLNLTNPPWRDTVLVPPGGW 100

                           90       100       110
                   ....*....|....*....|....*....|..
gi 1307738778 1017 QTVEMIPRNPGTWLLHCHVTDHVHAGMEATYT 1048
Cdd:cd04207    101 VVIRFKADNPGVWMLHCHILEHEDAGMMTVFE 132
CuRO_D2_2dMcoN_like cd04202
The second cupredoxin domain of bacterial two domain multicopper oxidase McoN and similar ...
 951-1043 2.94e-13

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: 68.05  E-value: 2.94e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1307738778  951 MHAINGKVFGNLRGLTMHVGDRVSWYLMGMGNeiDIHTAHFHGHSFDYKQT-GV-------YRADVFDLFPGTFQTVEMI 1022
Cdd:cd04202     29 YFTINGKSFPATPPLVVKEGDRVRIRLINLSM--DHHPMHLHGHFFLVTATdGGpipgsapWPKDTLNVAPGERYDIEFV 106

                           90       100
                   ....*....|....*....|.
gi 1307738778 1023 PRNPGTWLLHCHVTDHVHAGM 1043
Cdd:cd04202    107 ADNPGDWMFHCHKLHHAMNGM 127
CuRO_1_2DMCO_NIR_like_2 cd14449
The cupredoxin domain 1 of a two-domain laccase related to nitrite reductase; The two-domain ...
 96-204 5.03e-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: 5.03e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1307738778   96 GPIIKGEVGDSIIIHLKNFASRNYTLHPHGVTYTKENEGALYPDNtgavqkrddAVEPGGQFTYTWDVTEDQGPAEGDAD 175
Cdd:cd14449     29 GPVIEVREGDTLKILFRNTLDVPASLHPHGVDYTTASDGTGMNAS---------IVAPGDTRIYTWRTHGGYRRADGSWA 99

                           90       100       110
                   ....*....|....*....|....*....|....*.
gi 1307738778  176 CVTRA---YHSHI----DAPRDVASGLVGPLIICRK 204
Cdd:cd14449    100 EGTAGywhYHDHVfgteHGTEGLSRGLYGALIVRRV 135
Cu-oxidase_3 pfam07732
Multicopper oxidase; This entry contains many divergent copper oxidase-like domains that are ...
 94-201 8.75e-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: 8.75e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1307738778   94 FLGPIIKGEVGDSIIIHLKNFASRNYTLHPHGVTYTKEnegalyPDNTGAVQKRDDAVEPGGQFTYTWDVTEDQGpaegd 173
Cdd:pfam07732   24 FPGPTIRVREGDTVVVNVTNNLDEPTSIHWHGLQQRGT------PWMDGVPGVTQCPIPPGQSFTYRFQVKQQAG----- 92

                           90       100
                   ....*....|....*....|....*...
gi 1307738778  174 adcvTRAYHSHIDAPRdvASGLVGPLII 201
Cdd:pfam07732   93 ----TYWYHSHTSGQQ--AAGLAGAIII 114
CuRO_1_2DMCO_NIR_like_2 cd14449
The cupredoxin domain 1 of a two-domain laccase related to nitrite reductase; The two-domain ...
 450-555 2.46e-10

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


Pssm-ID: 259991 [Multi-domain]  Cd Length: 135  Bit Score: 59.59  E-value: 2.46e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1307738778  450 GPVIKAEVGESIRVTFRNNASRPFSIQPHGLSYRKSdegasySRGTDSPASHVSPGATFTYEWNVPEDVGPTDQDPDCLT 529
Cdd:cd14449     29 GPVIEVREGDTLKILFRNTLDVPASLHPHGVDYTTA------SDGTGMNASIVAPGDTRIYTWRTHGGYRRADGSWAEGT 102

                           90       100       110
                   ....*....|....*....|....*....|...
gi 1307738778  530 ---WLYYSAV----DAVRDTSAGLVGPLLVCRR 555
Cdd:cd14449    103 agyWHYHDHVfgteHGTEGLSRGLYGALIVRRV 135
SufI COG2132
Multicopper oxidase with three cupredoxin domains (includes cell division protein FtsP and ...
 951-1051 3.01e-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: 63.80  E-value: 3.01e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1307738778  951 MHAINGKVFGNLR-GLTMHVGDRVSWYLMGMGNeiDIHTAHFHGHSF--------DYKQTGvyRADVFDLFPGtfQTVEM 1021
Cdd:COG2132    317 VWTINGKAFDPDRpDLTVKLGERERWTLVNDTM--MPHPFHLHGHQFqvlsrngkPPPEGG--WKDTVLVPPG--ETVRI 390

                           90       100       110
                   ....*....|....*....|....*....|...
gi 1307738778 1022 I---PRNPGTWLLHCHVTDHVHAGMEATYTVLP 1051
Cdd:COG2132    391 LfrfDNYPGDWMFHCHILEHEDAGMMGQFEVVP 423
CuRO_3_CopA cd13896
The third cupredoxin domain of CopA copper resistance protein family; CopA is a multicopper ...
 954-1043 5.52e-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: 57.65  E-value: 5.52e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1307738778  954 INGKVFGNLRGLTMHVGDRVswylmgmgnEIDI-------HTAHFHGHSFDYKQ-TGVYRA--DVFDLFPGTFQTVEMIP 1023
Cdd:cd13896     19 INGKAYPDADPLRVREGERV---------RIVFvndtmmaHPMHLHGHFFQVENgNGEYGPrkDTVLVPPGETVSVDFDA 89

                           90       100
                   ....*....|....*....|
gi 1307738778 1024 RNPGTWLLHCHVTDHVHAGM 1043
Cdd:cd13896     90 DNPGRWAFHCHNLYHMEAGM 109
CuRO_3_CumA_like cd13906
The third cupredoxin domain of CumA like multicopper oxidase; This multicopper oxidase (MCO) ...
 953-1049 6.74e-10

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


Pssm-ID: 259973 [Multi-domain]  Cd Length: 138  Bit Score: 58.16  E-value: 6.74e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1307738778  953 AINGKVFGNLRG-------LTMHVGDrvsWYLMGMGNEID-IHTAHFHGHSF-----DYKQTGV-YRADVFDLFPGtfQT 1018
Cdd:cd13906     30 AINGTSWTGGDHshlppplATLKRGR---SYVLRLVNETAfLHPMHLHGHFFrvlsrNGRPVPEpFWRDTVLLGPK--ET 104

                           90       100       110
                   ....*....|....*....|....*....|...
gi 1307738778 1019 VE--MIPRNPGTWLLHCHVTDHVHAGMEATYTV 1049
Cdd:cd13906    105 VDiaFVADNPGDWMFHCHILEHQETGMMGVIRV 137
CuRO_1_2DMCO_NIR_like cd11024
The cupredoxin domain 1 of a two-domain laccase related to nitrite reductase; The two-domain ...
 96-201 4.46e-09

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


Pssm-ID: 259910 [Multi-domain]  Cd Length: 119  Bit Score: 55.35  E-value: 4.46e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1307738778   96 GPIIKGEVGDSIIIHLKNFASRNYTLHPHGVTYTKEnegalypDNTGAvqkrdDAVEPGGQFTYTWDVTedqgPAeGdad 175
Cdd:cd11024     32 GPTLRATEGDLVRIHFINTGDHPHTIHFHGIHDAAM-------DGTGL-----GPIMPGESFTYEFVAE----PA-G--- 91

                           90       100
                   ....*....|....*....|....*...
gi 1307738778  176 cvTRAYHSHIdAP--RDVASGLVGPLII 201
Cdd:cd11024     92 --THLYHCHV-QPlkEHIAMGLYGAFIV 116
CuRO_1_Diphenol_Ox cd13857
The first cupredoxin domain of fungal laccase, diphenol oxidase; Diphenol oxidase belongs to ...
 94-201 7.30e-09

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


Pssm-ID: 259926 [Multi-domain]  Cd Length: 119  Bit Score: 54.57  E-value: 7.30e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1307738778   94 FLGPIIKGEVGDSIIIHLKNFASRNYTLHPHGVTytkeNEGALYPDNTGAVQKRddAVEPGGQFTYTWDVTEDQGpaegd 173
Cdd:cd13857     28 FPGPLIEANQGDRIVVHVTNELDEPTSIHWHGLF----QNGTNWMDGTAGITQC--PIPPGGSFTYNFTVDGQYG----- 96

                           90       100
                   ....*....|....*....|....*...
gi 1307738778  174 adcvTRAYHSHIDAprDVASGLVGPLII 201
Cdd:cd13857     97 ----TYWYHSHYST--QYADGLVGPLIV 118
CuRO_1_CumA_like cd13861
The first cupredoxin domain of CumA like multicopper oxidase; This multicopper oxidase (MCO) ...
 93-201 8.10e-09

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


Pssm-ID: 259930 [Multi-domain]  Cd Length: 119  Bit Score: 54.55  E-value: 8.10e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1307738778   93 GFLGPIIKGEVGDSIIIHLKNFASRNYTLHPHGVTYtkENEgalyPDNTGAVQKrdDAVEPGGQFTYTWdVTEDQGpaeg 172
Cdd:cd13861     28 QVPGPELRVRQGDTLRVRLTNRLPEPTTIHWHGLRL--PNA----MDGVPGLTQ--PPVPPGESFTYEF-TPPDAG---- 94

                           90       100
                   ....*....|....*....|....*....
gi 1307738778  173 dadcvTRAYHSHIDAPRDVASGLVGPLII 201
Cdd:cd13861     95 -----TYWYHPHVGSQEQLDRGLYGPLIV 118
Cu-oxidase_3 pfam07732
Multicopper oxidase; This entry contains many divergent copper oxidase-like domains that are ...
 448-552 1.16e-08

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: 54.17  E-value: 1.16e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1307738778  448 LLGPVIKAEVGESIRVTFRNNASRPFSIQPHGLSYRKSdegaSYSRGTD-SPASHVSPGATFTYEWNVPEDVGptdqdpd 526
Cdd:pfam07732   24 FPGPTIRVREGDTVVVNVTNNLDEPTSIHWHGLQQRGT----PWMDGVPgVTQCPIPPGQSFTYRFQVKQQAG------- 92

                           90       100
                   ....*....|....*....|....*.
gi 1307738778  527 clTWLYYSAVDAVRdtSAGLVGPLLV 552
Cdd:pfam07732   93 --TYWYHSHTSGQQ--AAGLAGAIII 114
CuRO_1_CumA_like cd13861
The first cupredoxin domain of CumA like multicopper oxidase; This multicopper oxidase (MCO) ...
 447-552 1.28e-08

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


Pssm-ID: 259930 [Multi-domain]  Cd Length: 119  Bit Score: 54.16  E-value: 1.28e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1307738778  447 GLLGPVIKAEVGESIRVTFRNNASRPFSIQPHGLSYRKSDEGASYSrgTDSPashVSPGATFTYEWNVPeDVGptdqdpd 526
Cdd:cd13861     28 QVPGPELRVRQGDTLRVRLTNRLPEPTTIHWHGLRLPNAMDGVPGL--TQPP---VPPGESFTYEFTPP-DAG------- 94

                           90       100
                   ....*....|....*....|....*.
gi 1307738778  527 clTWLYYSAVDAVRDTSAGLVGPLLV 552
Cdd:cd13861     95 --TYWYHPHVGSQEQLDRGLYGPLIV 118
CuRO_3_CumA_like cd13906
The third cupredoxin domain of CumA like multicopper oxidase; This multicopper oxidase (MCO) ...
 284-357 3.32e-08

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


Pssm-ID: 259973 [Multi-domain]  Cd Length: 138  Bit Score: 53.54  E-value: 3.32e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1307738778  284 KWHLFGMGNEAD-IHSAYFHG----------QTLIERHHRvDTISLFPATFVDAVMTPRNPGEWLLSCQVNDHIQGGMQA 352
Cdd:cd13906     55 RSYVLRLVNETAfLHPMHLHGhffrvlsrngRPVPEPFWR-DTVLLGPKETVDIAFVADNPGDWMFHCHILEHQETGMMG 133


                   ....*
gi 1307738778  353 LFKVK 357
Cdd:cd13906    134 VIRVA 138
SufI COG2132
Multicopper oxidase with three cupredoxin domains (includes cell division protein FtsP and ...
 94-224 3.75e-08

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


Pssm-ID: 441735 [Multi-domain]  Cd Length: 423  Bit Score: 56.87  E-value: 3.75e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1307738778   94 FLGPIIKGEVGDSIIIHLKNFASRNYTLHPHGvtytkeneGALYPDNTGAVQkrdDAVEPGGQFTYTWDVteDQGPAegd 173
Cdd:COG2132     42 YPGPTIRVREGDRVRVRVTNRLPEPTTVHWHG--------LRVPNAMDGVPG---DPIAPGETFTYEFPV--PQPAG--- 105

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 1307738778  174 adcvTRAYHSHIDA--PRDVASGLVGPLIIcrkgtmNTDSDK--RFDAEFILMFS 224
Cdd:COG2132    106 ----TYWYHPHTHGstAEQVYRGLAGALIV------EDPEEDlpRYDRDIPLVLQ 150
CuRO_3_Fet3p cd13899
The third Cupredoxin domain of multicopper oxidase Fet3p; Fet3p catalyzes the ferroxidase ...
 987-1051 4.32e-08

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


Pssm-ID: 259966 [Multi-domain]  Cd Length: 160  Bit Score: 53.80  E-value: 4.32e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1307738778  987 HTAHFHGHSFD--YKQTGVY----------------RADVFDLFPGTFQTVEMIPRNPGTWLLHCHVTDHVHAGMEATYT 1048
Cdd:cd13899     78 HPFHLHGHKFQvvQRSPDVAsddpnppinefpenpmRRDTVMVPPGGSVVIRFRADNPGVWFFHCHIEWHLEAGLAATFI 157


                   ...
gi 1307738778 1049 VLP 1051
Cdd:cd13899    158 EAP 160
PLN02191 PLN02191
L-ascorbate oxidase
 94-224 5.02e-08

L-ascorbate oxidase


Pssm-ID: 177843 [Multi-domain]  Cd Length: 574  Bit Score: 56.95  E-value: 5.02e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1307738778   94 FLGPIIKGEVGDSIIIHLKN-FASRNYTLHPHGVtytkENEGALYPDNTGAVQKRddAVEPGGQFTYTWDVtEDQGpaeg 172
Cdd:PLN02191    51 FPGPTIDAVAGDTIVVHLTNkLTTEGLVIHWHGI----RQKGSPWADGAAGVTQC--AINPGETFTYKFTV-EKPG---- 119

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|...
gi 1307738778  173 dadcvTRAYHSHIDAPRdvASGLVGPLIIcrkGTMNTDSDK-RFDAEFILMFS 224
Cdd:PLN02191   120 -----THFYHGHYGMQR--SAGLYGSLIV---DVAKGPKERlRYDGEFNLLLS 162
CuRO_1_2dMco_1 cd13860
The first cupredoxin domain of bacteria two domain multicopper oxidase; This subfamily ...
 96-201 5.20e-08

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


Pssm-ID: 259929 [Multi-domain]  Cd Length: 119  Bit Score: 52.20  E-value: 5.20e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1307738778   96 GPIIKGEVGDSIIIHLKNFASRNYTLHPHGVTYTKENEGAlyPDNTGavqkrdDAVEPGGQFTYTWDVTEdqgpaEGdad 175
Cdd:cd13860     31 GPTIEVTEGDRVRILVTNELPEPTTVHWHGLPVPNGMDGV--PGITQ------PPIQPGETFTYEFTAKQ-----AG--- 94

                           90       100
                   ....*....|....*....|....*.
gi 1307738778  176 cvTRAYHSHIDAPRDVASGLVGPLII 201
Cdd:cd13860     95 --TYMYHSHVDEAKQEDMGLYGAFIV 118
CuRO_D1_2dMcoN_like cd13859
The first cupredoxin domain of bacterial two domain multicopper oxidase McoN and similar ...
 96-201 5.73e-08

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


Pssm-ID: 259928 [Multi-domain]  Cd Length: 122  Bit Score: 52.48  E-value: 5.73e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1307738778   96 GPIIKGEVGDSIIIHLKNFASRNYTLHPHGV--TYTKENEGAlypdnTGAVQKrddAVEPGGQFTYTWDVtEDQGpaegd 173
Cdd:cd13859     31 GPLIHVKEGDDLVVHVTNNTTLPHTIHWHGVlqMGSWKMDGV-----PGVTQP---AIEPGESFTYKFKA-ERPG----- 96

                           90       100
                   ....*....|....*....|....*....
gi 1307738778  174 adcvTRAYHSHIDAPRDVA-SGLVGPLII 201
Cdd:cd13859     97 ----TLWYHCHVNVNEHVGmRGMWGPLIV 121
CuRO_1_2DMCO_NIR_like cd11024
The cupredoxin domain 1 of a two-domain laccase related to nitrite reductase; The two-domain ...
 450-552 6.23e-08

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


Pssm-ID: 259910 [Multi-domain]  Cd Length: 119  Bit Score: 51.89  E-value: 6.23e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1307738778  450 GPVIKAEVGESIRVTFRNNASRPFSIQPHGLSYRKSDegasysrgtDSPASHVSPGATFTYEWnVPEDVGptdqdpdclT 529
Cdd:cd11024     32 GPTLRATEGDLVRIHFINTGDHPHTIHFHGIHDAAMD---------GTGLGPIMPGESFTYEF-VAEPAG---------T 92

                           90       100
                   ....*....|....*....|....
gi 1307738778  530 WLYYSAVDAVRD-TSAGLVGPLLV 552
Cdd:cd11024     93 HLYHCHVQPLKEhIAMGLYGAFIV 116
CuRO_3_MaLCC_like cd13901
The third cupredoxin domain of the fungal laccases similar to Ma-LCC from Melanocarpus ...
 967-1043 6.38e-08

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


Pssm-ID: 259968 [Multi-domain]  Cd Length: 157  Bit Score: 53.00  E-value: 6.38e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1307738778  967 MHVGDRVSWYLMGMGNEIDI-HTAHFHGHSFdY--KQ-TGVY-------------RADVFDLFPGTFQTVEMIPRNPGTW 1029
Cdd:cd13901     60 IELPKANKWVYIVIQNNSPLpHPIHLHGHDF-YilAQgTGTFdddgtilnlnnppRRDVAMLPAGGYLVIAFKTDNPGAW 138

                           90
                   ....*....|....
gi 1307738778 1030 LLHCHVTDHVHAGM 1043
Cdd:cd13901    139 LMHCHIAWHASGGL 152
Cu-oxidase pfam00394
Multicopper oxidase; Many of the proteins in this family contain multiple similar copies of ...
 223-359 6.95e-08

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


Pssm-ID: 395317 [Multi-domain]  Cd Length: 146  Bit Score: 52.70  E-value: 6.95e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1307738778  223 FSVMDENLSWYlDDNIRTYCSEPSKVDKDDEDFQESNKMHSINGYMYGYLPNLTMCVEDKVKWHLFgMGNEADIHSAYFH 302
Cdd:pfam00394    1 EDYVITLSDWY-HKDAKDLEKELLASGKAPTDFPPVPDAVLINGKDGASLATLTVTPGKTYRLRII-NVALDDSLNFSIE 78

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1307738778  303 GQ--TLIE---RHH---RVDTISLFPATFVDAVMTP-RNPGEWLLSCQVN-DHIQGGMQALFKVKDC 359
Cdd:pfam00394   79 GHkmTVVEvdgVYVnpfTVDSLDIFPGQRYSVLVTAnQDPGNYWIVASPNiPAFDNGTAAAILRYSG 145
CuRO_1_Diphenol_Ox cd13857
The first cupredoxin domain of fungal laccase, diphenol oxidase; Diphenol oxidase belongs to ...
 450-552 8.08e-08

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: 51.88  E-value: 8.08e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1307738778  450 GPVIKAEVGESIRVTFRNNASRPFSIQPHGLSYRksdeGASYSRGTdspaSHVS-----PGATFTYEWNVPEDVGptdqd 524
Cdd:cd13857     30 GPLIEANQGDRIVVHVTNELDEPTSIHWHGLFQN----GTNWMDGT----AGITqcpipPGGSFTYNFTVDGQYG----- 96

                           90       100
                   ....*....|....*....|....*...
gi 1307738778  525 pdclTWLYYSAVDAvrDTSAGLVGPLLV 552
Cdd:cd13857     97 ----TYWYHSHYST--QYADGLVGPLIV 118
CuRO_1_2DMCO_NIR_like_2 cd14449
The cupredoxin domain 1 of a two-domain laccase related to nitrite reductase; The two-domain ...
 800-876 1.02e-07

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


Pssm-ID: 259991 [Multi-domain]  Cd Length: 135  Bit Score: 51.88  E-value: 1.02e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1307738778  800 IQGPLLMSNIGDKIVIVFKNLASRPYSIHAHGVKTDSSAVAVTN------PGETKTYVWK--IPARSSSERGDPPCIA-W 870
Cdd:cd14449     27 VPGPVIEVREGDTLKILFRNTLDVPASLHPHGVDYTTASDGTGMnasivaPGDTRIYTWRthGGYRRADGSWAEGTAGyW 106


                   ....*.
gi 1307738778  871 AYHSTV 876
Cdd:cd14449    107 HYHDHV 112
CuRO_1_Abr2_like cd13850
The first cupredoxin domain of a group of fungal Laccases similar to Abr2 from Aspergillus ...
 94-201 1.24e-07

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


Pssm-ID: 259919 [Multi-domain]  Cd Length: 117  Bit Score: 51.14  E-value: 1.24e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1307738778   94 FLGPIIKGEVGDSIIIHLKNFASRNYTLHPHGVtytkENEGALYPDNTGAVQKRddAVEPGGQFTYTWDVTEDQGpaegd 173
Cdd:cd13850     26 FPGPPIILDEGDEVEILVTNNLPVNTTIHFHGI----LQRGTPWSDGVPGVTQW--PIQPGGSFTYRWKAEDQYG----- 94

                           90       100
                   ....*....|....*....|....*....
gi 1307738778  174 adcvTRAYHSHIdapRDVAS-GLVGPLII 201
Cdd:cd13850     95 ----LYWYHSHY---RGYYMdGLYGPIYI 116
CuRO_3_McoC_like cd13902
The third cupredoxin domain of a multicopper oxidase McoC and similar proteins; This family ...
 951-1049 1.29e-07

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


Pssm-ID: 259969 [Multi-domain]  Cd Length: 125  Bit Score: 51.25  E-value: 1.29e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1307738778  951 MHAINGKVFGNLR-GLTMHVGDRVSWYLMgmgNEIDI-HTAHFHGHSF------DYKQTGVYRA--DVFDLFPGTFQTVE 1020
Cdd:cd13902     20 MFLINGKTFDMNRiDFVAKVGEVEVWEVT---NTSHMdHPFHLHGTQFqvleidGNPQKPEYRAwkDTVNLPPGEAVRIA 96

                           90       100
                   ....*....|....*....|....*....
gi 1307738778 1021 MIPRNPGTWLLHCHVTDHVHAGMEATYTV 1049
Cdd:cd13902     97 TRQDDPGMWMYHCHILEHEDAGMMGMLHV 125
CuRO_3_MCO_like_3 cd13909
The third cupredoxin domain of uncharacterized multicopper oxidase; Multicopper Oxidases (MCOs) ...
 987-1043 1.71e-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: 51.37  E-value: 1.71e-07
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1307738778  987 HTAHFHGHSF-----DYkQTGVYRaDVFDLFPGTFQTVEMIPRNPGTWLLHCHVTDHVHAGM 1043
Cdd:cd13909     71 HGMHLHGHHFrailpNG-ALGPWR-DTLLMDRGETREIAFVADNPGDWLLHCHMLEHAAAGM 130
CuRO_1_LCC_like cd04206
Cupredoxin domain 1 of laccase-like multicopper oxidases; including laccase, CueO, spore coat ...
 802-893 1.73e-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: 50.75  E-value: 1.73e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1307738778  802 GPLLMSNIGDKIVIVFKN-LASRPYSIHAHGVK----TDSSAVAVTN-----PGETKTYVWKIParsssergDPPCIAWa 871
Cdd:cd04206     30 GPTIRVKEGDTVEVTVTNnLPNEPTSIHWHGLRqpgtNDGDGVAGLTqcpipPGESFTYRFTVD--------DQAGTFW- 100

                           90       100
                   ....*....|....*....|..
gi 1307738778  872 YHSTVDIvkDTYSGLIGTLVVC 893
Cdd:cd04206    101 YHSHVGG--QRADGLYGPLIVE 120
CuRO_1_AAO cd13845
The first cupredoxin domain of plant Ascorbate oxidase; Ascorbate oxidase catalyzes the ...
 93-201 1.75e-07

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


Pssm-ID: 259914 [Multi-domain]  Cd Length: 120  Bit Score: 50.91  E-value: 1.75e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1307738778   93 GFLGPIIKGEVGDSIIIHLKN-FASRNYTLHPHGVtytkENEGALYPDNTGAVQKRddAVEPGGQFTYTWDVteDQgPAe 171
Cdd:cd13845     27 QFPGPTIRATAGDTIVVELENkLPTEGVAIHWHGI----RQRGTPWADGTASVSQC--PINPGETFTYQFVV--DR-PG- 96

                           90       100       110
                   ....*....|....*....|....*....|
gi 1307738778  172 gdadcvTRAYHSHIDAPRdvASGLVGPLII 201
Cdd:cd13845     97 ------TYFYHGHYGMQR--SAGLYGSLIV 118
CuRO_1_Fet3p cd13851
The first Cupredoxin domain of multicopper oxidase Fet3P; Fet3p catalyzes the ferroxidase ...
 97-201 3.02e-07

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: 50.34  E-value: 3.02e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1307738778   97 PIIKGEVGDSIIIHLKN-FASRNYTLHPHGVTYTkeneGALYPDntGAVQKRDDAVEPGGQFTYTWDVTEDQGpaegdad 175
Cdd:cd13851     32 PPIEVNKGDTVVIHATNsLGDQPTSLHFHGLFQN----GTNYMD--GPVGVTQCPIPPGQSFTYEFTVDTQVG------- 98

                           90       100
                   ....*....|....*....|....*.
gi 1307738778  176 cvTRAYHSHIDAprDVASGLVGPLII 201
Cdd:cd13851     99 --TYWYHSHDGG--QYPDGLRGPFII 120
CuRO_3_LCC_like cd04207
Cupredoxin domain 3 of laccase-like multicopper oxidases; including laccase, CueO, spore coat ...
 263-354 3.26e-07

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: 50.54  E-value: 3.26e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1307738778  263 SING----YMYGYLPNLTMCVEDKVKWHLFGMGNEADIHSAYFHGQtlierHHRV--------------------DTISL 318
Cdd:cd04207     21 VINGmpfkEGDANTDIFSVEAGDVVEIVLINAGNHDMQHPFHLHGH-----SFWVlgsgggpfdaplnltnppwrDTVLV 95

                           90       100       110
                   ....*....|....*....|....*....|....*.
gi 1307738778  319 FPATFVDAVMTPRNPGEWLLSCQVNDHIQGGMQALF 354
Cdd:cd04207     96 PPGGWVVIRFKADNPGVWMLHCHILEHEDAGMMTVF 131
CuRO_1_Tv-LCC_like cd13856
The first cupredoxin domain of fungal laccases similar to Tv-LCC from Trametes versicolor; ...
 94-201 4.22e-07

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: 50.03  E-value: 4.22e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1307738778   94 FLGPIIKGEVGDSIIIHLKNFAS-----RNYTLHPHGVTYTKENegalYPDNTGAVQKRddAVEPGGQFTYTWDVTEDQG 168
Cdd:cd13856     28 FPGPLITANKGDTFRITVVNQLTdptmrRSTSIHWHGIFQHGTN----YADGPAFVTQC--PIAPNHSFTYDFTAGDQAG 101

                           90       100       110
                   ....*....|....*....|....*....|...
gi 1307738778  169 paegdadcvTRAYHSHIDAprDVASGLVGPLII 201
Cdd:cd13856    102 ---------TFWYHSHLST--QYCDGLRGPLVI 123
CuRO_3_MCO_like_2 cd13908
The third cupredoxin domain of uncharacterized multicopper oxidase; Multicopper Oxidases (MCOs) ...
 954-1045 4.82e-07

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


Pssm-ID: 259975 [Multi-domain]  Cd Length: 122  Bit Score: 49.76  E-value: 4.82e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1307738778  954 INGKVFGNL-RGLTMHVGDRvswYLMGMGNEI-DIHTAHFHGHSF-----DYKQTGVYRADVFDLFPGTFQTVEMIPRNP 1026
Cdd:cd13908     23 INGKSYPDEdPPLVVQQGRR---YRLVFRNASdDAHPMHLHRHTFevtriDGKPTSGLRKDVVMLGGYQRVEVDFVADNP 99

                           90
                   ....*....|....*....
gi 1307738778 1027 GTWLLHCHVTDHVHAGMEA 1045
Cdd:cd13908    100 GLTLFHCHQQLHMDYGFMA 118
ascorbase TIGR03388
L-ascorbate oxidase, plant type; Members of this protein family are the copper-containing ...
 94-233 8.73e-07

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


Pssm-ID: 274555 [Multi-domain]  Cd Length: 541  Bit Score: 52.83  E-value: 8.73e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1307738778   94 FLGPIIKGEVGDSIIIHLKN-FASRNYTLHPHGVtytkENEGALYPDNTGAVQKRddAVEPGGQFTYTWdVTEDQGpaeg 172
Cdd:TIGR03388   29 FPGPTIRAQAGDTIVVELTNkLHTEGVVIHWHGI----RQIGTPWADGTAGVTQC--AINPGETFIYNF-VVDRPG---- 97

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1307738778  173 dadcvTRAYHSHIDAPRdvASGLVGPLIIcrkgtMNTDSDK---RFDAEFILMFSvmdenlSWY 233
Cdd:TIGR03388   98 -----TYFYHGHYGMQR--SAGLYGSLIV-----DVPDGEKepfHYDGEFNLLLS------DWW 143
CuRO_1_2dMco_1 cd13860
The first cupredoxin domain of bacteria two domain multicopper oxidase; This subfamily ...
 450-552 1.03e-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: 48.73  E-value: 1.03e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1307738778  450 GPVIKAEVGESIRVTFRNNASRPFSIQPHGLSYRKSDEGASysrgtDSPASHVSPGATFTYEWNVpEDVGptdqdpdclT 529
Cdd:cd13860     31 GPTIEVTEGDRVRILVTNELPEPTTVHWHGLPVPNGMDGVP-----GITQPPIQPGETFTYEFTA-KQAG---------T 95

                           90       100
                   ....*....|....*....|...
gi 1307738778  530 WLYYSAVDAVRDTSAGLVGPLLV 552
Cdd:cd13860     96 YMYHSHVDEAKQEDMGLYGAFIV 118
CuRO_3_Tv-LCC_like cd13903
The third cupredoxin domain of the fungal laccases similar to Tv-LCC from Trametes Versicolor; ...
 981-1043 1.08e-06

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


Pssm-ID: 259970 [Multi-domain]  Cd Length: 147  Bit Score: 49.20  E-value: 1.08e-06
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1307738778  981 GNEIDIHTAHFHGHSFDYKQ---TGVY------RADVFDL-FPGTFQTVEMIPRNPGTWLLHCHVTDHVHAGM 1043
Cdd:cd13903     67 GAIGGPHPFHLHGHAFSVVRsagSNTYnyvnpvRRDVVSVgTPGDGVTIRFVTDNPGPWFLHCHIDWHLEAGL 139
CuRO_1_MaLCC_like cd13854
The first cupredoxin domain of the fungal laccases similar to Ma-LCC from Melanocarpus ...
 96-201 1.10e-06

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


Pssm-ID: 259923 [Multi-domain]  Cd Length: 122  Bit Score: 48.78  E-value: 1.10e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1307738778   96 GPIIKGEVGDSIIIHLKNFASRNYT-LHPHGVT--YTKENEGAlypdnTGAVQKrddAVEPGGQFTYTWDVTEdQGpaeg 172
Cdd:cd13854     33 GPLIEANWGDTIEVTVINKLQDNGTsIHWHGIRqlNTNWQDGV-----PGVTEC---PIAPGDTRTYRFRATQ-YG---- 99

                           90       100
                   ....*....|....*....|....*....
gi 1307738778  173 dadcvTRAYHSHIDAprDVASGLVGPLII 201
Cdd:cd13854    100 -----TSWYHSHYSA--QYGDGVVGPIVI 121
CuRO_3_AAO cd13893
The third cupredoxin domain of plant Ascorbate oxidase; Ascorbate oxidase catalyzes the ...
 982-1043 5.63e-06

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


Pssm-ID: 259960 [Multi-domain]  Cd Length: 155  Bit Score: 47.41  E-value: 5.63e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1307738778  982 NEIDIHTAHFHGHSF---DYKqTGVYRA---------------DVFDLFPGTFQTVEMIPRNPGTWLLHCHVTDHVHAGM 1043
Cdd:cd13893     62 NASEQHPWHLHGHDFwvlGYG-LGGFDPaadpsslnlvnppmrNTVTIFPYGWTALRFKADNPGVWAFHCHIEWHFHMGM 140
CuRO_1_2DMCO_NIR_like cd11024
The cupredoxin domain 1 of a two-domain laccase related to nitrite reductase; The two-domain ...
 800-892 6.09e-06

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


Pssm-ID: 259910 [Multi-domain]  Cd Length: 119  Bit Score: 46.49  E-value: 6.09e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1307738778  800 IQGPLLMSNIGDKIVIVFKNLASRPYSIHAHGV---KTDSSAVAVTNPGETKTYVWkiPARsssergdpPCIAWAYHSTV 876
Cdd:cd11024     30 VPGPTLRATEGDLVRIHFINTGDHPHTIHFHGIhdaAMDGTGLGPIMPGESFTYEF--VAE--------PAGTHLYHCHV 99

                           90
                   ....*....|....*..
gi 1307738778  877 DIVKD-TYSGLIGTLVV 892
Cdd:cd11024    100 QPLKEhIAMGLYGAFIV 116
CuRO_1_Tv-LCC_like cd13856
The first cupredoxin domain of fungal laccases similar to Tv-LCC from Trametes versicolor; ...
 450-552 7.23e-06

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


Pssm-ID: 259925 [Multi-domain]  Cd Length: 125  Bit Score: 46.18  E-value: 7.23e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1307738778  450 GPVIKAEVGESIRVTFRNNAS-----RPFSIQPHGLSYRKS--DEGASYSrgTDSPashVSPGATFTYEWNVPEDVGptd 522
Cdd:cd13856     30 GPLITANKGDTFRITVVNQLTdptmrRSTSIHWHGIFQHGTnyADGPAFV--TQCP---IAPNHSFTYDFTAGDQAG--- 101

                           90       100       110
                   ....*....|....*....|....*....|
gi 1307738778  523 qdpdclTWLYYSAVDAvrDTSAGLVGPLLV 552
Cdd:cd13856    102 ------TFWYHSHLST--QYCDGLRGPLVI 123
CuRO_D2_2dMcoN_like cd04202
The second cupredoxin domain of bacterial two domain multicopper oxidase McoN and similar ...
 216-357 9.83e-06

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: 46.09  E-value: 9.83e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1307738778  216 DAEFILMFSvmdenlSWYLDDNirtycSEPSKVDKDDEDFqesnkmHSINGYMYGYLPNLTMCVEDKVKWHLFGMGNeaD 295
Cdd:cd04202      1 DRDYTLVLQ------EWFVDPG-----TTPMPPEGMDFNY------FTINGKSFPATPPLVVKEGDRVRIRLINLSM--D 61

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1307738778  296 IHSAYFHGQT---------LIERHHRV--DTISLFPATFVDAVMTPRNPGEWLLSCQVNDHI----QGGMQALFKVK 357
Cdd:cd04202     62 HHPMHLHGHFflvtatdggPIPGSAPWpkDTLNVAPGERYDIEFVADNPGDWMFHCHKLHHAmngmGGGMMTLIGYE 138
SufI COG2132
Multicopper oxidase with three cupredoxin domains (includes cell division protein FtsP and ...
 448-552 1.10e-05

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


Pssm-ID: 441735 [Multi-domain]  Cd Length: 423  Bit Score: 49.16  E-value: 1.10e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1307738778  448 LLGPVIKAEVGESIRVTFRNNASRPFSIQPHGLsyR---KSDegasysrgtDSPASHVSPGATFTYEWNVPEDVGptdqd 524
Cdd:COG2132     42 YPGPTIRVREGDRVRVRVTNRLPEPTTVHWHGL--RvpnAMD---------GVPGDPIAPGETFTYEFPVPQPAG----- 105

                           90       100       110
                   ....*....|....*....|....*....|
gi 1307738778  525 pdclTWLYYSAVDAV--RDTSAGLVGPLLV 552
Cdd:COG2132    106 ----TYWYHPHTHGStaEQVYRGLAGALIV 131
PLN02191 PLN02191
L-ascorbate oxidase
 985-1043 1.25e-05

L-ascorbate oxidase


Pssm-ID: 177843 [Multi-domain]  Cd Length: 574  Bit Score: 49.24  E-value: 1.25e-05
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1307738778  985 DIHTAHFHGHSF--------------DYKQTGVYRADVFD---LFPGTFQTVEMIPRNPGTWLLHCHVTDHVHAGM 1043
Cdd:PLN02191   465 EIHPWHLHGHDFwvlgygdgkfkpgiDEKTYNLKNPPLRNtaiLYPYGWTAIRFVTDNPGVWFFHCHIEPHLHMGM 540
CuRO_1_AAO cd13845
The first cupredoxin domain of plant Ascorbate oxidase; Ascorbate oxidase catalyzes the ...
 450-552 1.45e-05

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: 45.51  E-value: 1.45e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1307738778  450 GPVIKAEVGESIRVTFRNN-ASRPFSIQPHGLSYRksdeGASYSRGTDSPAS-HVSPGATFTYEWNVpedvgptDQDPdc 527
Cdd:cd13845     30 GPTIRATAGDTIVVELENKlPTEGVAIHWHGIRQR----GTPWADGTASVSQcPINPGETFTYQFVV-------DRPG-- 96

                           90       100
                   ....*....|....*....|....*
gi 1307738778  528 lTWLYYSAVDAVRdtSAGLVGPLLV 552
Cdd:cd13845     97 -TYFYHGHYGMQR--SAGLYGSLIV 118
CuRO_1_2DMCO_NIR_like cd11024
The cupredoxin domain 1 of a two-domain laccase related to nitrite reductase; The two-domain ...
 950-1052 1.71e-05

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


Pssm-ID: 259910 [Multi-domain]  Cd Length: 119  Bit Score: 44.95  E-value: 1.71e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1307738778  950 KMHAINGKVFG-NLRgltMHVGDRVSWYLMGMGNeiDIHTAHFHGHSFDYKQTGVYRadvfDLFPGTFQTVEMIPRNPGT 1028
Cdd:cd11024     22 KAWTYNGTVPGpTLR---ATEGDLVRIHFINTGD--HPHTIHFHGIHDAAMDGTGLG----PIMPGESFTYEFVAEPAGT 92

                           90       100
                   ....*....|....*....|....*..
gi 1307738778 1029 WLLHCHV---TDHVHAGMEATYTVLPR 1052
Cdd:cd11024     93 HLYHCHVqplKEHIAMGLYGAFIVDPK 119
CuRO_1_CuNIR_like cd04201
Cupredoxin domain 1 of Copper-containing nitrite reductase and two-domain laccase; ...
 955-1052 1.88e-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: 45.17  E-value: 1.88e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1307738778  955 NGKVFGNLrgLTMHVGDRVSWYLMGMGNEIDIHTAHFHGHSfdyKQTGVYRADVFDlfPGTFQTVEMIPRNPGTWLLHCH 1034
Cdd:cd04201     27 DGDIPGPM--LRVREGDTVELHFSNNPSSTMPHNIDFHAAT---GAGGGAGATFIA--PGETSTFSFKATQPGLYVYHCA 99

                           90       100
                   ....*....|....*....|.
gi 1307738778 1035 VTD---HVHAGMEATYTVLPR 1052
Cdd:cd04201    100 VAPvpmHIANGMYGLILVEPK 120
CuRO_1_LCC_plant cd13849
The first cupredoxin domain of plant laccases; Laccase is a blue multicopper oxidase (MCO) ...
 94-201 2.11e-05

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


Pssm-ID: 259918 [Multi-domain]  Cd Length: 117  Bit Score: 44.94  E-value: 2.11e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1307738778   94 FLGPIIKGEVGDSIIIHLKNFASRNYTLHPHGVtYTKENEGAlypDNTGAVQKRddAVEPGGQFTYTWDVTEDQGpaegd 173
Cdd:cd13849     26 FPGPTIRVHEGDTVVVNVTNRSPYNITIHWHGI-RQLRSGWA---DGPAYITQC--PIQPGQSYTYRFTVTGQEG----- 94

                           90       100
                   ....*....|....*....|....*...
gi 1307738778  174 adcvTRAYHSHIDAPRdvaSGLVGPLII 201
Cdd:cd13849     95 ----TLWWHAHISWLR---ATVYGAFII 115
CuRO_D1_2dMcoN_like cd13859
The first cupredoxin domain of bacterial two domain multicopper oxidase McoN and similar ...
 799-892 2.83e-05

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


Pssm-ID: 259928 [Multi-domain]  Cd Length: 122  Bit Score: 44.39  E-value: 2.83e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1307738778  799 EIQGPLLMSNIGDKIVIVFKNLASRPYSIHAHGV-KTDS----SAVAVTN----PGETKTYVWKiparssserGDPPCIA 869
Cdd:cd13859     28 QVPGPLIHVKEGDDLVVHVTNNTTLPHTIHWHGVlQMGSwkmdGVPGVTQpaiePGESFTYKFK---------AERPGTL 98

                           90       100
                   ....*....|....*....|....
gi 1307738778  870 WaYHSTVDIVK-DTYSGLIGTLVV 892
Cdd:cd13859     99 W-YHCHVNVNEhVGMRGMWGPLIV 121
CuRO_1_CumA_like cd13861
The first cupredoxin domain of CumA like multicopper oxidase; This multicopper oxidase (MCO) ...
 802-892 5.95e-05

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: 43.38  E-value: 5.95e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1307738778  802 GPLLMSNIGDKIVIVFKNLASRPYSIHAHGVKTDS----------SAVAvtnPGETKTYVWKIParsssergdPPCIAWa 871
Cdd:cd13861     31 GPELRVRQGDTLRVRLTNRLPEPTTIHWHGLRLPNamdgvpgltqPPVP---PGESFTYEFTPP---------DAGTYW- 97

                           90       100
                   ....*....|....*....|.
gi 1307738778  872 YHSTVDIVKDTYSGLIGTLVV 892
Cdd:cd13861     98 YHPHVGSQEQLDRGLYGPLIV 118
CuRO_3_tcLLC2_insect_like cd13905
The third cupredoxin domain of the insect laccases similar to laccase 2 in Tribolium castaneum; ...
 987-1044 6.19e-05

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


Pssm-ID: 259972 [Multi-domain]  Cd Length: 174  Bit Score: 44.59  E-value: 6.19e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1307738778  987 HTAHFHGHSF--------DY-KQTGVY--------RADVFDLFPGTFQ------TVeMIPR-----------NPGTWLLH 1032
Cdd:cd13905     70 HPFHLHGHSFyvlgmgfpGYnSTTGEIlsqnwnnkLLDRGGLPGRNLVnpplkdTV-VVPNggyvvirfradNPGYWLLH 148

                           90
                   ....*....|..
gi 1307738778 1033 CHVTDHVHAGME 1044
Cdd:cd13905    149 CHIEFHLLEGMA 160
CuRO_1_CueO_FtsP cd04232
The first Cupredoxin domain of the multicopper oxidase CueO, the cell division protein FtsP, ...
 94-201 7.54e-05

The first Cupredoxin domain of the multicopper oxidase CueO, the cell division protein FtsP, and similar proteins; CueO is a multicopper oxidase (MCO) that is part of the copper-regulatory cue operon, which employs a cytosolic metalloregulatory protein CueR that induces expression of CopA and CueO under copper stress conditions. CueO is a periplasmic multicopper oxidase that is stimulated by exogenous copper(II). FtsP (also named SufI) is a component of the cell division apparatus. It is involved in protecting or stabilizing the assembly of divisomes under stress conditions. FtsP belongs to the multicopper oxidase superfamily but lacks metal cofactors. The protein is localized at septal rings and may serve as a scaffolding function. Members of this subfamily contain three cupredoxin domains and this model represents the first domain. Although MCOs have diverse functions, majority of them have three cupredoxin domain repeats that include one mononuclear and one trinuclear copper center. The copper ions are bound in several sites: Type 1, Type 2, and/or Type 3. The ensemble of types 2 and 3 copper is called a trinuclear cluster. MCOs oxidize their substrate by accepting electrons at a mononuclear copper center and transferring them to the active site trinuclear copper center. The cupredoxin domain 1 of 3-domain MCOs contains part the trinuclear copper binding site, which is located at the interface of domains 1 and 3. FtsP does not contain any copper binding sites.


Pssm-ID: 259894 [Multi-domain]  Cd Length: 120  Bit Score: 43.33  E-value: 7.54e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1307738778   94 FLGPIIKGEVGDSIIIHLKNFASRNYTLHPHGVTYTKENEGalypdntGAVQkrddAVEPGGQFTYTWDVteDQGPAegd 173
Cdd:cd04232     29 YLGPTIRVKKGDTVRINVTNNLDEETTVHWHGLHVPGEMDG-------GPHQ----PIAPGQTWSPTFTI--DQPAA--- 92

                           90       100       110
                   ....*....|....*....|....*....|
gi 1307738778  174 adcvTRAYHSHIDA--PRDVASGLVGPLII 201
Cdd:cd04232     93 ----TLWYHPHTHGktAEQVYRGLAGLFII 118
CuRO_1_McoC_like cd13855
The first cupredoxin domain of a multicopper oxidase McoC and similar proteins; This family ...
 447-517 9.65e-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: 42.85  E-value: 9.65e-05
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1307738778  447 GLLGPVIKAEVGESIRVTFRNNASRPFSIQPHGLSYRKSDEGasysrgtdSPASHVSPGATFTYEWNVPED 517
Cdd:cd13855     29 SVPGPLIEVFEGDTVEITFRNRLPEPTTVHWHGLPVPPDQDG--------NPHDPVAPGNDRVYRFTLPQD 91
CuRO_1_Diphenol_Ox cd13857
The first cupredoxin domain of fungal laccase, diphenol oxidase; Diphenol oxidase belongs to ...
 802-892 1.12e-04

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


Pssm-ID: 259926 [Multi-domain]  Cd Length: 119  Bit Score: 42.63  E-value: 1.12e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1307738778  802 GPLLMSNIGDKIVIVFKNLASRPYSIHAHGVKTDSS-----AVAVTN----PGETKTYVWKIPARSSSergdppciAWaY 872
Cdd:cd13857     30 GPLIEANQGDRIVVHVTNELDEPTSIHWHGLFQNGTnwmdgTAGITQcpipPGGSFTYNFTVDGQYGT--------YW-Y 100

                           90       100
                   ....*....|....*....|.
gi 1307738778  873 HSTVDIvkdTYS-GLIGTLVV 892
Cdd:cd13857    101 HSHYST---QYAdGLVGPLIV 118
CuRO_1_McoC_like cd13855
The first cupredoxin domain of a multicopper oxidase McoC and similar proteins; This family ...
 96-201 1.33e-04

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


Pssm-ID: 259924 [Multi-domain]  Cd Length: 121  Bit Score: 42.46  E-value: 1.33e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1307738778   96 GPIIKGEVGDSIIIHLKNFASRNYTLHPHGVTYTKENEGALYpdntgavqkrdDAVEPGGQFTYTWDVTEDQGPaegdad 175
Cdd:cd13855     32 GPLIEVFEGDTVEITFRNRLPEPTTVHWHGLPVPPDQDGNPH-----------DPVAPGNDRVYRFTLPQDSAG------ 94

                           90       100
                   ....*....|....*....|....*...
gi 1307738778  176 cvTRAY--HSHIDAPRDVASGLVGPLII 201
Cdd:cd13855     95 --TYWYhpHPHGHTAEQVYRGLAGAFVV 120
CuRO_1_McoC_like cd13855
The first cupredoxin domain of a multicopper oxidase McoC and similar proteins; This family ...
 802-892 3.88e-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: 41.31  E-value: 3.88e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1307738778  802 GPLLMSNIGDKIVIVFKNLASRPYSIHAHGV----KTDSSAVAVTNPGETKTYVWKIPARSSSERGDPPciawayHSTVD 877
Cdd:cd13855     32 GPLIEVFEGDTVEITFRNRLPEPTTVHWHGLpvppDQDGNPHDPVAPGNDRVYRFTLPQDSAGTYWYHP------HPHGH 105

                           90
                   ....*....|....*
gi 1307738778  878 IVKDTYSGLIGTLVV 892
Cdd:cd13855    106 TAEQVYRGLAGAFVV 120
CuRO_D1_2dMcoN_like cd13859
The first cupredoxin domain of bacterial two domain multicopper oxidase McoN and similar ...
 450-519 4.39e-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: 41.31  E-value: 4.39e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1307738778  450 GPVIKAEVGESIRVTFRNNASRPFSIQPHGLSYRKS--DEGASysrGTDSPAshVSPGATFTYEW--------------N 513
Cdd:cd13859     31 GPLIHVKEGDDLVVHVTNNTTLPHTIHWHGVLQMGSwkMDGVP---GVTQPA--IEPGESFTYKFkaerpgtlwyhchvN 105


                   ....*.
gi 1307738778  514 VPEDVG 519
Cdd:cd13859    106 VNEHVG 111
CuRO_3_Abr2_like cd13898
The third cupredoxin domain of a group of fungal Laccases similar to Abr2 from Aspergillus ...
 1004-1043 4.88e-04

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


Pssm-ID: 259965 [Multi-domain]  Cd Length: 164  Bit Score: 41.86  E-value: 4.88e-04
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....
gi 1307738778 1004 YRaDVFDLFPGTFQTVEMIPR----NPGTWLLHCHVTDHVHAGM 1043
Cdd:cd13898    115 LR-DTFTTPPSTEGPSWLVIRyhvvNPGAWLLHCHIQSHLAGGM 157
CuRO_3_LCC_plant cd13897
The third cupredoxin domain of the plant laccases; Laccase is a blue multicopper oxidase (MCO) ...
 985-1049 4.89e-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: 41.48  E-value: 4.89e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1307738778  985 DIHTAHFHGHSFdY---KQTGVYRA--DV--FDLF-PGTFQTVeMIPR-----------NPGTWLLHCHVTDHVHAGMEA 1045
Cdd:cd13897     55 ENHPMHLHGFDF-YvvgRGFGNFDPstDPatFNLVdPPLRNTV-GVPRggwaairfvadNPGVWFMHCHFERHTSWGMAT 132


                   ....
gi 1307738778 1046 TYTV 1049
Cdd:cd13897    133 VFIV 136
Cu-oxidase_2 pfam07731
Multicopper oxidase; This entry contains many divergent copper oxidase-like domains that are ...
 254-358 6.54e-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: 40.88  E-value: 6.54e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1307738778  254 DFQESNKMHSINGYMYGYLPN-LTMCVEDKVKWHLFGMGNeaDIHSAYFHGQT--LIERHH-----------------RV 313
Cdd:pfam07731   14 SGNFRRNDWAINGLLFPPNTNvITLPYGTVVEWVLQNTTT--GVHPFHLHGHSfqVLGRGGgpwpeedpktynlvdpvRR 91

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*
gi 1307738778  314 DTISLFPATFVDAVMTPRNPGEWLLSCQVNDHIQGGMQALFKVKD 358
Cdd:pfam07731   92 DTVQVPPGGWVAIRFRADNPGVWLFHCHILWHLDQGMMGQFVVRP 136
CuRO_3_MCO_like_4 cd13910
The third cupredoxin domain of uncharacterized multicopper oxidase; Multicopper Oxidases (MCOs) ...
 987-1043 6.94e-04

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


Pssm-ID: 259977 [Multi-domain]  Cd Length: 166  Bit Score: 41.51  E-value: 6.94e-04
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1307738778  987 HTAHFHGHSF-------DYKQTGVYRADVFDLFPGTFQ----TVEmIPR-----------NPGTWLLHCHVTDHVHAGM 1043
Cdd:cd13910     83 HPFHLHGHKFwvlgsgdGRYGGGGYTAPDGTSLNTTNPlrrdTVS-VPGfgwavlrfvadNPGLWAFHCHILWHMAAGM 160
CuRO_1_Abr2_like cd13850
The first cupredoxin domain of a group of fungal Laccases similar to Abr2 from Aspergillus ...
 450-514 1.00e-03

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


Pssm-ID: 259919 [Multi-domain]  Cd Length: 117  Bit Score: 39.97  E-value: 1.00e-03
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1307738778  450 GPVIKAEVGESIRVTFRNNASRPFSIQPHGLSYRksdeGASYSRG----TDSPashVSPGATFTYEWNV 514
Cdd:cd13850     28 GPPIILDEGDEVEILVTNNLPVNTTIHFHGILQR----GTPWSDGvpgvTQWP---IQPGGSFTYRWKA 89
CuRO_1_MaLCC_like cd13854
The first cupredoxin domain of the fungal laccases similar to Ma-LCC from Melanocarpus ...
 802-892 1.10e-03

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


Pssm-ID: 259923 [Multi-domain]  Cd Length: 122  Bit Score: 39.92  E-value: 1.10e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1307738778  802 GPLLMSNIGDKIVI-VFKNLASRPYSIHAHGVK-----TDSSAVAVTN----PGETKTYVWKIPARSSSergdppciaWa 871
Cdd:cd13854     33 GPLIEANWGDTIEVtVINKLQDNGTSIHWHGIRqlntnWQDGVPGVTEcpiaPGDTRTYRFRATQYGTS---------W- 102

                           90       100
                   ....*....|....*....|..
gi 1307738778  872 YHSTVDIvkdTYS-GLIGTLVV 892
Cdd:cd13854    103 YHSHYSA---QYGdGVVGPIVI 121
CuRO_1_Tth-MCO_like cd13853
The first cupredoxin domain of the bacterial laccases similar to Tth-MCO from Thermus ...
 94-201 1.33e-03

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


Pssm-ID: 259922 [Multi-domain]  Cd Length: 139  Bit Score: 40.31  E-value: 1.33e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1307738778   94 FLGPIIKGEVGDSIIIHLKN----------------FASRNYT-LHPHGVTYTKENEGalypDNtgaVQKRddaVEPGGQ 156
Cdd:cd13853     29 IPGPTLRVRPGDTLRITLKNdlppegaaneapapntPHCPNTTnLHFHGLHVSPTGNS----DN---VFLT---IAPGES 98

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*...
gi 1307738778  157 FTYTWDVTEDQGPaeGdadcvTRAYHSHID---APrDVASGLVGPLII 201
Cdd:cd13853     99 FTYEYDIPADHPP--G-----TYWYHPHLHgstAL-QVAGGMAGALVV 138
Cu-oxidase pfam00394
Multicopper oxidase; Many of the proteins in this family contain multiple similar copies of ...
 915-1047 1.41e-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: 40.38  E-value: 1.41e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1307738778  915 VFDENESWYlDENIKTYSPNPHLVDKEDEEF-LESNKmHAINGKVFGNLRGLTMHVGDRVSWYLMgMGNEIDIHTAHFHG 993
Cdd:pfam00394    3 YVITLSDWY-HKDAKDLEKELLASGKAPTDFpPVPDA-VLINGKDGASLATLTVTPGKTYRLRII-NVALDDSLNFSIEG 79

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1307738778  994 HSF-----DYKQTGVYRADVFDLFPGTFQTVeMI--PRNPGTWLLHCHVT-DHVHAGMEATY 1047
Cdd:pfam00394   80 HKMtvvevDGVYVNPFTVDSLDIFPGQRYSV-LVtaNQDPGNYWIVASPNiPAFDNGTAAAI 140
CuRO_1_Fet3p cd13851
The first Cupredoxin domain of multicopper oxidase Fet3P; Fet3p catalyzes the ferroxidase ...
 451-519 1.80e-03

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


Pssm-ID: 259920 [Multi-domain]  Cd Length: 121  Bit Score: 39.17  E-value: 1.80e-03
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1307738778  451 PVIKAEVGESIRVTFRNN-ASRPFSIQPHGLsyrksdegasYSRGT---DSPAS----HVSPGATFTYEWNVPEDVG 519
Cdd:cd13851     32 PPIEVNKGDTVVIHATNSlGDQPTSLHFHGL----------FQNGTnymDGPVGvtqcPIPPGQSFTYEFTVDTQVG 98
Cupredoxin cd00920
Cupredoxin superfamily; Cupredoxins contain type I copper centers and are involved in ...
 965-1046 2.02e-03

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


Pssm-ID: 259860 [Multi-domain]  Cd Length: 110  Bit Score: 39.14  E-value: 2.02e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1307738778  965 LTMHVGDRVSWYL---MGMGNEIDIHTAHFHGHSFDYKQTGVYRADVFdLFPGTFQTVEMIPRNPGTWLLHCHVTDHVHA 1041
Cdd:cd00920     25 LVVPVGDTVRVQFvnkLGENHSVTIAGFGVPVVAMAGGANPGLVNTLV-IGPGESAEVTFTTDQAGVYWFYCTIPGHNHA 103


                   ....*
gi 1307738778 1042 GMEAT 1046
Cdd:cd00920    104 GMVGT 108
ascorbOXfungal TIGR03390
L-ascorbate oxidase, fungal type; This model describes a family of fungal ascorbate oxidases, ...
 984-1054 2.26e-03

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


Pssm-ID: 132431 [Multi-domain]  Cd Length: 538  Bit Score: 41.75  E-value: 2.26e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1307738778  984 IDIHTAHFHG-HSFDYKQ-TGVYRA---------------DVFDLFPGTFQTVEMIP----------RNPGTWLLHCHVT 1036
Cdd:TIGR03390  439 VDTHPFHAHGrHFYDIGGgDGEYNAtaneaklenytpvlrDTTMLYRYAVKVVPGAPagwrawrirvTNPGVWMMHCHIL 518

                           90
                   ....*....|....*...
gi 1307738778 1037 DHVHAGMEATYTVLPRED 1054
Cdd:TIGR03390  519 QHMVMGMQTVWVFGDAED 536
CuRO_1_McoP_like cd13852
The first cupredoxin domain of multicopper oxidase McoP and similar proteins; This family ...
 449-514 2.70e-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: 38.81  E-value: 2.70e-03
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1307738778  449 LGPVIKAEVGESIRVTFRNNASRPFSIQPHGLSYRKSDEGasysrgtdSPASHVSPGATFTYEWNV 514
Cdd:cd13852     23 LGPILRLRKGQKVRITFKNNLPEPTIIHWHGLHVPAAMDG--------HPRYAIDPGETYVYEFEV 80
CuRO_1_CuNIR_like cd04201
Cupredoxin domain 1 of Copper-containing nitrite reductase and two-domain laccase; ...
 800-853 3.17e-03

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


Pssm-ID: 259864 [Multi-domain]  Cd Length: 120  Bit Score: 38.63  E-value: 3.17e-03
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 1307738778  800 IQGPLLMSNIGDKIVIVFKNLASR--PYSIHAHGV--KTDSSAVAVTNPGETKTYVWK 853
Cdd:cd04201     30 IPGPMLRVREGDTVELHFSNNPSStmPHNIDFHAAtgAGGGAGATFIAPGETSTFSFK 87
CuRO_3_Tth-MCO_like cd13900
The third cupredoxin domain of the bacterial laccases similar to Tth-MCO from Thermus ...
 954-1043 4.06e-03

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


Pssm-ID: 259967 [Multi-domain]  Cd Length: 123  Bit Score: 38.38  E-value: 4.06e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1307738778  954 INGKVFGNLR-GLTMHVGDRVSWYLMGMGNEIdiHTAHFHGHSF-------DYKQTGVYRaDVFDLFPGTFQTVEMIPRN 1025
Cdd:cd13900     22 INGKPFDPDRpDRTVRLGTVEEWTLINTSGED--HPFHIHVNPFqvvsingKPGLPPVWR-DTVNVPAGGSVTIRTRFRD 98

                           90
                   ....*....|....*....
gi 1307738778 1026 P-GTWLLHCHVTDHVHAGM 1043
Cdd:cd13900     99 FtGEFVLHCHILDHEDQGM 117
CuRO_1_CuNIR cd11020
Cupredoxin domain 1 of Copper-containing nitrite reductase; Copper-containing nitrite ...
 802-853 5.09e-03

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


Pssm-ID: 259906 [Multi-domain]  Cd Length: 119  Bit Score: 37.96  E-value: 5.09e-03
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 1307738778  802 GPLLMSNIGDKIVIVFKNLASR--PYSIHAHGVKTDSSAVAVT-NPGETKTYVWK 853
Cdd:cd11020     32 GPVIRVREGDTVELTLTNPGTNtmPHSIDFHAATGPGGGEFTTiAPGETKTFSFK 86
PLN02604 PLN02604
oxidoreductase
 982-1047 5.63e-03

oxidoreductase


Pssm-ID: 215324 [Multi-domain]  Cd Length: 566  Bit Score: 40.61  E-value: 5.63e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1307738778  982 NEIDIHTAHFHGHsfDYKQTGvYRADVFDLF--PGTFQTVEMIPRN------------------PGTWLLHCHVTDHVHA 1041
Cdd:PLN02604   462 NNSETHPWHLHGH--DFWVLG-YGEGKFNMSsdPKKYNLVDPIMKNtvpvhpygwtalrfradnPGVWAFHCHIESHFFM 538


                   ....*.
gi 1307738778 1042 GMEATY 1047
Cdd:PLN02604   539 GMGVVF 544
CuRO_1_2dMco_1 cd13860
The first cupredoxin domain of bacteria two domain multicopper oxidase; This subfamily ...
 802-892 6.61e-03

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: 37.56  E-value: 6.61e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1307738778  802 GPLLMSNIGDKIVIVFKNLASRPYSIHAHGVKTDSSAVAVTN-------PGETKTYVWKIparsssergDPPCIAWaYHS 874
Cdd:cd13860     31 GPTIEVTEGDRVRILVTNELPEPTTVHWHGLPVPNGMDGVPGitqppiqPGETFTYEFTA---------KQAGTYM-YHS 100

                           90
                   ....*....|....*...
gi 1307738778  875 TVDIVKDTYSGLIGTLVV 892
Cdd:cd13860    101 HVDEAKQEDMGLYGAFIV 118
Cu-oxidase_3 pfam07732
Multicopper oxidase; This entry contains many divergent copper oxidase-like domains that are ...
 802-874 7.67e-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: 37.61  E-value: 7.67e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1307738778  802 GPLLMSNIGDKIVIVFKNLASRPYSIHAHGVKTDSS-----AVAVTN----PGETKTYVWKIParsssergDPPCIAWaY 872
Cdd:pfam07732   26 GPTIRVREGDTVVVNVTNNLDEPTSIHWHGLQQRGTpwmdgVPGVTQcpipPGQSFTYRFQVK--------QQAGTYW-Y 96


                   ..
gi 1307738778  873 HS 874
Cdd:pfam07732   97 HS 98
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

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