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Conserved domains on  [gi|1949456009|ref|XP_038129966|]
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ferroxidase HEPHL1-like [Cyprinodon tularosa]

Protein Classification

cupredoxin domain-containing protein( domain architecture ID 139548)

cupredoxin domain-containing protein may contain a type I copper center and be involved in inter-molecular electron transfer reactions

CATH:  2.60.40.420
Gene Ontology:  GO:0005507|GO:0009055
PubMed:  21258692|35994119
SCOP:  3000886

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
Cupredoxin super family cl19115
Cupredoxin superfamily; Cupredoxins contain type I copper centers and are involved in ...
 60-241 2.42e-111

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: 344.02  E-value: 2.42e-111
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949456009   60 RVYYIGIIEEDWSYAPSGKNLLNGKPIVEDEHASIFLERGQHRIGSVYKKAMYREYTDATFSHQAPREEWLGYLGPIIRA 139
Cdd:cd04222      1 REYYIGIRETQWDYAPSGKNLITNQTFDDDEHASVFLKRGPDRIGRVYKKAVYLQYTDDTYRTEIEKPVWLGFLGPILKA 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949456009  140 EVNDVIKIHLKNFASRNYSIHPHGLFYKKDAEGALYPDNTSDALKKDDSVPPGGSFTYSWEVKPRFAPTTDDANCLTWVY 219
Cdd:cd04222     81 EVGDVIVVHLKNFASRPYSLHPHGVFYNKENEGALYPDNTSGFEKADDAVPPGGSYTYTWTVPEEQAPTKADANCLTRIY 160

                          170       180
                   ....*....|....*....|..
gi 1949456009  220 HSHVNAPHDIASGLIGPLITCK 241
Cdd:cd04222    161 HSHIDAPKDIASGLIGPLIICK 182
Cupredoxin super family cl19115
Cupredoxin superfamily; Cupredoxins contain type I copper centers and are involved in ...
 768-935 7.32e-91

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 cd04225:

Pssm-ID: 473140 [Multi-domain]  Cd Length: 171  Bit Score: 288.60  E-value: 7.32e-91
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949456009  768 VKYYISAEEIEWDYSPTRDWELENHHTSpEESPGNIFVGKGENRIGSRYKKVVYRQYTDETFQKQKTRP---DHWGILGP 844
Cdd:cd04225      1 RTYYIAAEEVEWDYSPQRTWEQELHNTH-EESPGNAFLNKGDKFIGSKYKKVVYREYTDDTFSVPKERTaeeEHLGILGP 79

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949456009  845 IIHAEVGEQILIIFKNKASRPYSITAHGVKASGSHV-PVEPGRIIELTWDIPESSGPGTSELNCISYVYFSSVDYIKDLY 923
Cdd:cd04225     80 LIHAEVGEKVKIVFKNMASRPYSIHAHGVKTDSSWVaPTEPGETQTYTWKIPERSGPGVEDSNCISWAYYSTVDQIKDLY 159

                          170
                   ....*....|..
gi 1949456009  924 SGLLGPLVICRP 935
Cdd:cd04225    160 SGLIGPLVICRR 171
Cupredoxin super family cl19115
Cupredoxin superfamily; Cupredoxins contain type I copper centers and are involved in ...
 417-608 1.09e-90

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 cd04224:

Pssm-ID: 473140 [Multi-domain]  Cd Length: 197  Bit Score: 289.37  E-value: 1.09e-90
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949456009  417 GVVREFFVAAEKATWNYAPSEKNLFNNESLTEADSASEVFFGKEGGRIGGKYVKVLYRAYTDSTFS---KVITSPSHHGF 493
Cdd:cd04224      1 GKVRHYFIAAEEIMWDYAPSGKNLFTGQNLTAPGSDSEVFFQRNETRIGGTYWKVRYVEYTDATFTtrkHRSKEEEHLGI 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949456009  494 LGPVLRVEEGDILNVTFLNKADRGYSIHPHGLNYDKRFQGTSYEDGIDKPGSNVEPGQRFTYSWQVLEGPSSS--DAPCI 571
Cdd:cd04224     81 LGPVIRAEVGDTIKVTFRNKASRPFSIQPHGVFYEKNYEGAMYRDGDPSPGSHVSPGETFTYEWTVPEGVGPTnqDPPCL 160

                          170       180       190
                   ....*....|....*....|....*....|....*..
gi 1949456009  572 SYLYYSGTDPVKDTNSGLVGPLLVCKRGTLGQNGIQR 608
Cdd:cd04224    161 TYLYFSAVDPVRDTNSGLVGPLLVCKKGSLNANGRQK 197
Cupredoxin super family cl19115
Cupredoxin superfamily; Cupredoxins contain type I copper centers and are involved in ...
 264-403 4.85e-81

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 cd11021:

Pssm-ID: 473140 [Multi-domain]  Cd Length: 141  Bit Score: 260.48  E-value: 4.85e-81
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949456009  264 DRDIYLMFSVVDENLSWYLEDNIKK-CLDPDGVTVDDPDFEESNLMHAINGYTYGNLPGIELCRHHATAWHLFGMGNEVD 342
Cdd:cd11021      1 DREFVLMFSVVDENLSWYLDENIKTyCSEPAKVDKDDEDFQESNKMHSINGYTFGNLPGLSMCAGDRVKWHLFGMGNEVD 80

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1949456009  343 IHSAFFHGNTLLNRGHRTDTISLFPATFVTATMVPKVKGKWLLSCQVNDHLQAGMQAFYKV 403
Cdd:cd11021     81 IHSAFFHGQTLTDRGHRTDTINLFPATFVTAEMVAQNPGKWLLSCQVNDHLKAGMQAFYEV 141
Cupredoxin super family cl19115
Cupredoxin superfamily; Cupredoxins contain type I copper centers and are involved in ...
 611-752 8.23e-80

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 cd11022:

Pssm-ID: 473140 [Multi-domain]  Cd Length: 144  Bit Score: 257.41  E-value: 8.23e-80
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949456009  611 DKEFFLLFSVMDENLSWYLEENIKFFGT--SETNQEDEDFEESNKMHAVNGYMYGNLPMLEMCAGDNVVWHTFGLGTEAD 688
Cdd:cd11022      1 DKEFFLLFTVFDENESWYLDENIQQFTLdpRSVDKEDEDFQESNKMHSINGYMYGNQPGLDMCKGDTVSWHLFGLGTETD 80

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1949456009  689 IHGVYFEGNTFKLQSTTRDTVSLFPHTTAALSMRPNNYGLFEVSCRTTDHFSAGMRQLYRVKPC 752
Cdd:cd11022     81 VHGIYFSGNTFLLQGTRRDTANLFPHTSVTAIMQPDNEGTFEVNCQTTDHYSAGMRQIYTVSQC 144
Cupredoxin super family cl19115
Cupredoxin superfamily; Cupredoxins contain type I copper centers and are involved in ...
 954-1095 2.56e-68

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


The actual alignment was detected with superfamily member cd11012:

Pssm-ID: 473140 [Multi-domain]  Cd Length: 145  Bit Score: 225.52  E-value: 2.56e-68
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949456009  954 EFALLFLVYDENQSWYLEDNIKNYLGVHPDAFTPDEDFEESNLMHGINGRVYGNLHGLVMQQNEKVDWYLLGMGNEVDMH 1033
Cdd:cd11012      3 EFALLFLVFDENESWYLDENIKTYSDHPEKVNKEDEEFIESNKMHAINGKVFGNLQGLTMHVGDEVYWYLMGMGNEIDIH 82

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1949456009 1034 TVHFHAETFIYRTDLVHRGDVVDLFPGTFATVEMVAANPGTWLLHCHVSDHIHAGMETTYTI 1095
Cdd:cd11012     83 TAHFHGHSFDYKHRGVYRSDVFDLFPGTFQTVEMIPRTPGTWLLHCHVTDHIHAGMETTYTV 144
 
Name Accession Description Interval E-value
CuRO_1_ceruloplasmin cd04222
The first cupredoxin domain of Ceruloplasmin; Ceruloplasmin is a multicopper oxidase essential ...
 60-241 2.42e-111

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: 344.02  E-value: 2.42e-111
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949456009   60 RVYYIGIIEEDWSYAPSGKNLLNGKPIVEDEHASIFLERGQHRIGSVYKKAMYREYTDATFSHQAPREEWLGYLGPIIRA 139
Cdd:cd04222      1 REYYIGIRETQWDYAPSGKNLITNQTFDDDEHASVFLKRGPDRIGRVYKKAVYLQYTDDTYRTEIEKPVWLGFLGPILKA 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949456009  140 EVNDVIKIHLKNFASRNYSIHPHGLFYKKDAEGALYPDNTSDALKKDDSVPPGGSFTYSWEVKPRFAPTTDDANCLTWVY 219
Cdd:cd04222     81 EVGDVIVVHLKNFASRPYSLHPHGVFYNKENEGALYPDNTSGFEKADDAVPPGGSYTYTWTVPEEQAPTKADANCLTRIY 160

                          170       180
                   ....*....|....*....|..
gi 1949456009  220 HSHVNAPHDIASGLIGPLITCK 241
Cdd:cd04222    161 HSHIDAPKDIASGLIGPLIICK 182
CuRO_5_ceruloplasmin cd04225
The fifth cupredoxin domain of Ceruloplasmin; Ceruloplasmin is a multicopper oxidase essential ...
 768-935 7.32e-91

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: 288.60  E-value: 7.32e-91
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949456009  768 VKYYISAEEIEWDYSPTRDWELENHHTSpEESPGNIFVGKGENRIGSRYKKVVYRQYTDETFQKQKTRP---DHWGILGP 844
Cdd:cd04225      1 RTYYIAAEEVEWDYSPQRTWEQELHNTH-EESPGNAFLNKGDKFIGSKYKKVVYREYTDDTFSVPKERTaeeEHLGILGP 79

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949456009  845 IIHAEVGEQILIIFKNKASRPYSITAHGVKASGSHV-PVEPGRIIELTWDIPESSGPGTSELNCISYVYFSSVDYIKDLY 923
Cdd:cd04225     80 LIHAEVGEKVKIVFKNMASRPYSIHAHGVKTDSSWVaPTEPGETQTYTWKIPERSGPGVEDSNCISWAYYSTVDQIKDLY 159

                          170
                   ....*....|..
gi 1949456009  924 SGLLGPLVICRP 935
Cdd:cd04225    160 SGLIGPLVICRR 171
CuRO_3_ceruloplasmin cd04224
The third cupredoxin domain of Ceruloplasmin; Ceruloplasmin is a multicopper oxidase essential ...
 417-608 1.09e-90

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: 289.37  E-value: 1.09e-90
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949456009  417 GVVREFFVAAEKATWNYAPSEKNLFNNESLTEADSASEVFFGKEGGRIGGKYVKVLYRAYTDSTFS---KVITSPSHHGF 493
Cdd:cd04224      1 GKVRHYFIAAEEIMWDYAPSGKNLFTGQNLTAPGSDSEVFFQRNETRIGGTYWKVRYVEYTDATFTtrkHRSKEEEHLGI 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949456009  494 LGPVLRVEEGDILNVTFLNKADRGYSIHPHGLNYDKRFQGTSYEDGIDKPGSNVEPGQRFTYSWQVLEGPSSS--DAPCI 571
Cdd:cd04224     81 LGPVIRAEVGDTIKVTFRNKASRPFSIQPHGVFYEKNYEGAMYRDGDPSPGSHVSPGETFTYEWTVPEGVGPTnqDPPCL 160

                          170       180       190
                   ....*....|....*....|....*....|....*..
gi 1949456009  572 SYLYYSGTDPVKDTNSGLVGPLLVCKRGTLGQNGIQR 608
Cdd:cd04224    161 TYLYFSAVDPVRDTNSGLVGPLLVCKKGSLNANGRQK 197
CuRO_2_ceruloplasmin cd11021
The second cupredoxin domain of Ceruloplasmin; Ceruloplasmin is a multicopper oxidase ...
 264-403 4.85e-81

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: 260.48  E-value: 4.85e-81
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949456009  264 DRDIYLMFSVVDENLSWYLEDNIKK-CLDPDGVTVDDPDFEESNLMHAINGYTYGNLPGIELCRHHATAWHLFGMGNEVD 342
Cdd:cd11021      1 DREFVLMFSVVDENLSWYLDENIKTyCSEPAKVDKDDEDFQESNKMHSINGYTFGNLPGLSMCAGDRVKWHLFGMGNEVD 80

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1949456009  343 IHSAFFHGNTLLNRGHRTDTISLFPATFVTATMVPKVKGKWLLSCQVNDHLQAGMQAFYKV 403
Cdd:cd11021     81 IHSAFFHGQTLTDRGHRTDTINLFPATFVTAEMVAQNPGKWLLSCQVNDHLKAGMQAFYEV 141
CuRO_4_ceruloplasmin cd11022
The fourth cupredoxin domain of Ceruloplasmin; Ceruloplasmin is a multicopper oxidase ...
 611-752 8.23e-80

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: 257.41  E-value: 8.23e-80
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949456009  611 DKEFFLLFSVMDENLSWYLEENIKFFGT--SETNQEDEDFEESNKMHAVNGYMYGNLPMLEMCAGDNVVWHTFGLGTEAD 688
Cdd:cd11022      1 DKEFFLLFTVFDENESWYLDENIQQFTLdpRSVDKEDEDFQESNKMHSINGYMYGNQPGLDMCKGDTVSWHLFGLGTETD 80

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1949456009  689 IHGVYFEGNTFKLQSTTRDTVSLFPHTTAALSMRPNNYGLFEVSCRTTDHFSAGMRQLYRVKPC 752
Cdd:cd11022     81 VHGIYFSGNTFLLQGTRRDTANLFPHTSVTAIMQPDNEGTFEVNCQTTDHYSAGMRQIYTVSQC 144
CuRO_6_ceruloplasmin cd11012
The sixth cupredoxin domain of Ceruloplasmin; Ceruloplasmin is a multicopper oxidase essential ...
 954-1095 2.56e-68

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: 225.52  E-value: 2.56e-68
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949456009  954 EFALLFLVYDENQSWYLEDNIKNYLGVHPDAFTPDEDFEESNLMHGINGRVYGNLHGLVMQQNEKVDWYLLGMGNEVDMH 1033
Cdd:cd11012      3 EFALLFLVFDENESWYLDENIKTYSDHPEKVNKEDEEFIESNKMHAINGKVFGNLQGLTMHVGDEVYWYLMGMGNEIDIH 82

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1949456009 1034 TVHFHAETFIYRTDLVHRGDVVDLFPGTFATVEMVAANPGTWLLHCHVSDHIHAGMETTYTI 1095
Cdd:cd11012     83 TAHFHGHSFDYKHRGVYRSDVFDLFPGTFQTVEMIPRTPGTWLLHCHVTDHIHAGMETTYTV 144
Cu-oxidase_2 pfam07731
Multicopper oxidase; This entry contains many divergent copper oxidase-like domains that are ...
 982-1099 5.94e-18

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


Pssm-ID: 462246 [Multi-domain]  Cd Length: 138  Bit Score: 81.33  E-value: 5.94e-18
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949456009  982 PDAFTPDeDFEESNLMHGINGRVYG-NLHGLVMQQNEKVDWYLLGMGNevDMHTVHFHAETFiyrtDLVHRG-------- 1052
Cdd:pfam07731    7 PTLLQIT-SGNFRRNDWAINGLLFPpNTNVITLPYGTVVEWVLQNTTT--GVHPFHLHGHSF----QVLGRGggpwpeed 79

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 1949456009 1053 ------------DVVDLFPGTFATVEMVAANPGTWLLHCHVSDHIHAGMETTYTIKEKS 1099
Cdd:pfam07731   80 pktynlvdpvrrDTVQVPPGGWVAIRFRADNPGVWLFHCHILWHLDQGMMGQFVVRPGD 138
Cu-oxidase_3 pfam07732
Multicopper oxidase; This entry contains many divergent copper oxidase-like domains that are ...
 114-238 4.71e-12

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


Pssm-ID: 462247 [Multi-domain]  Cd Length: 119  Bit Score: 63.80  E-value: 4.71e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949456009  114 EYTDATFSHQAPREEWL---GYLGPIIRAEVNDVIKIHLKNFASRNYSIHPHGLFYKK--DAEGALYpdNTSDALkkdds 188
Cdd:pfam07732    3 TYGTVSPLGGTRQAVIGvngQFPGPTIRVREGDTVVVNVTNNLDEPTSIHWHGLQQRGtpWMDGVPG--VTQCPI----- 75

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|
gi 1949456009  189 vPPGGSFTYSWEVKprfapttdDANCLTWvYHSHvnAPHDIASGLIGPLI 238
Cdd:pfam07732   76 -PPGQSFTYRFQVK--------QQAGTYW-YHSH--TSGQQAAGLAGAII 113
SufI COG2132
Multicopper oxidase with three cupredoxin domains (includes cell division protein FtsP and ...
 997-1097 6.75e-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: 62.64  E-value: 6.75e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949456009  997 MHGINGRVYGNLH-GLVMQQNEKVDWYLlgmGNEVDM-HTVHFHAETF----IYRTDLVHRG--DVVDLFPGTFATVEMV 1068
Cdd:COG2132    317 VWTINGKAFDPDRpDLTVKLGERERWTL---VNDTMMpHPFHLHGHQFqvlsRNGKPPPEGGwkDTVLVPPGETVRILFR 393

                           90       100       110
                   ....*....|....*....|....*....|
gi 1949456009 1069 AAN-PGTWLLHCHVSDHIHAGMETTYTIKE 1097
Cdd:COG2132    394 FDNyPGDWMFHCHILEHEDAGMMGQFEVVP 423
Cu-oxidase_3 pfam07732
Multicopper oxidase; This entry contains many divergent copper oxidase-like domains that are ...
 493-559 1.41e-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: 1.41e-08
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949456009  493 FLGPVLRVEEGDILNVTFLNKADRGYSIHPHGLnydkrFQ-GTSYEDGIDKpGSN--VEPGQRFTYSWQV 559
Cdd:pfam07732   24 FPGPTIRVREGDTVVVNVTNNLDEPTSIHWHGL-----QQrGTPWMDGVPG-VTQcpIPPGQSFTYRFQV 87
SufI COG2132
Multicopper oxidase with three cupredoxin domains (includes cell division protein FtsP and ...
 132-238 1.79e-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: 58.02  E-value: 1.79e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949456009  132 YLGPIIRAEVNDVIKIHLKNFASRNYSIHPHGLFykkdaegalyPDNTSD--AlkkDDSVPPGGSFTYSWEVkprfaptt 209
Cdd:COG2132     42 YPGPTIRVREGDRVRVRVTNRLPEPTTVHWHGLR----------VPNAMDgvP---GDPIAPGETFTYEFPV-------- 100

                           90       100       110
                   ....*....|....*....|....*....|..
gi 1949456009  210 DDANCLTWvYHSHVN---APHdIASGLIGPLI 238
Cdd:COG2132    101 PQPAGTYW-YHPHTHgstAEQ-VYRGLAGALI 130
SufI COG2132
Multicopper oxidase with three cupredoxin domains (includes cell division protein FtsP and ...
 493-595 1.32e-06

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: 52.24  E-value: 1.32e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949456009  493 FLGPVLRVEEGDILNVTFLNKADRGYSIHPHGLNydkrfqgTSYE-DGIdkPGSNVEPGQRFTYSWQVLEGPSssdapci 571
Cdd:COG2132     42 YPGPTIRVREGDRVRVRVTNRLPEPTTVHWHGLR-------VPNAmDGV--PGDPIAPGETFTYEFPVPQPAG------- 105

                           90       100
                   ....*....|....*....|....*.
gi 1949456009  572 SYLYYSGTDPVKDTN--SGLVGPLLV 595
Cdd:COG2132    106 TYWYHPHTHGSTAEQvyRGLAGALIV 131
PLN02191 PLN02191
L-ascorbate oxidase
 980-1093 3.62e-05

L-ascorbate oxidase


Pssm-ID: 177843 [Multi-domain]  Cd Length: 574  Bit Score: 47.70  E-value: 3.62e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949456009  980 VHPDAFTPDEDFEESNLMHGINGRVYG-NLHGLvmqqnekvDWYLLGMGNE-----VDMHTVHFHAETFiyrtdlvhRGD 1053
Cdd:PLN02191   442 VFPFNVTVDVIIQNANVLKGVVSEIHPwHLHGH--------DFWVLGYGDGkfkpgIDEKTYNLKNPPL--------RNT 505

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|
gi 1949456009 1054 VVdLFPGTFATVEMVAANPGTWLLHCHVSDHIHAGMETTY 1093
Cdd:PLN02191   506 AI-LYPYGWTAIRFVTDNPGVWFFHCHIEPHLHMGMGVVF 544
ascorbase TIGR03388
L-ascorbate oxidase, plant type; Members of this protein family are the copper-containing ...
 994-1089 3.97e-04

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: 44.36  E-value: 3.97e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949456009  994 SNLMHGINGRVYG-NLHGLvmqqnekvDWYLLGMGN---EVDMHTVHFHAETFIYRtdlvhrgDVVDLFPGTFATVEMVA 1069
Cdd:TIGR03388  433 ANTLNGNNSETHPwHLHGH--------DFWVLGYGEgkfRPGVDEKSYNLKNPPLR-------NTVVIFPYGWTALRFVA 497

                           90       100
                   ....*....|....*....|
gi 1949456009 1070 ANPGTWLLHCHVSDHIHAGM 1089
Cdd:TIGR03388  498 DNPGVWAFHCHIEPHLHMGM 517
Cu-oxidase_3 pfam07732
Multicopper oxidase; This entry contains many divergent copper oxidase-like domains that are ...
 833-932 7.35e-04

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: 40.31  E-value: 7.35e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949456009  833 KTRPDHWGI----LGPIIHAEVGEQILIIFKNKASRPYSITAHGVKASG----------SHVPVEPGRIIELTWDIPESS 898
Cdd:pfam07732   12 GTRQAVIGVngqfPGPTIRVREGDTVVVNVTNNLDEPTSIHWHGLQQRGtpwmdgvpgvTQCPIPPGQSFTYRFQVKQQA 91

                           90       100       110
                   ....*....|....*....|....*....|....*
gi 1949456009  899 GpgtselnciSYVYFSSvdyIKDLY-SGLLGPLVI 932
Cdd:pfam07732   92 G---------TYWYHSH---TSGQQaAGLAGAIII 114
ascorbase TIGR03388
L-ascorbate oxidase, plant type; Members of this protein family are the copper-containing ...
 134-238 1.21e-03

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: 42.82  E-value: 1.21e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949456009  134 GPIIRAEVNDVIKIHLKN-FASRNYSIHPHGLfykkDAEGALYPDNTSDALKKddSVPPGGSFTYSWEVkprfapttDDA 212
Cdd:TIGR03388   31 GPTIRAQAGDTIVVELTNkLHTEGVVIHWHGI----RQIGTPWADGTAGVTQC--AINPGETFIYNFVV--------DRP 96

                           90       100
                   ....*....|....*....|....*.
gi 1949456009  213 NclTWVYHSHVNAPHdiASGLIGPLI 238
Cdd:TIGR03388   97 G--TYFYHGHYGMQR--SAGLYGSLI 118
 
Name Accession Description Interval E-value
CuRO_1_ceruloplasmin cd04222
The first cupredoxin domain of Ceruloplasmin; Ceruloplasmin is a multicopper oxidase essential ...
 60-241 2.42e-111

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: 344.02  E-value: 2.42e-111
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949456009   60 RVYYIGIIEEDWSYAPSGKNLLNGKPIVEDEHASIFLERGQHRIGSVYKKAMYREYTDATFSHQAPREEWLGYLGPIIRA 139
Cdd:cd04222      1 REYYIGIRETQWDYAPSGKNLITNQTFDDDEHASVFLKRGPDRIGRVYKKAVYLQYTDDTYRTEIEKPVWLGFLGPILKA 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949456009  140 EVNDVIKIHLKNFASRNYSIHPHGLFYKKDAEGALYPDNTSDALKKDDSVPPGGSFTYSWEVKPRFAPTTDDANCLTWVY 219
Cdd:cd04222     81 EVGDVIVVHLKNFASRPYSLHPHGVFYNKENEGALYPDNTSGFEKADDAVPPGGSYTYTWTVPEEQAPTKADANCLTRIY 160

                          170       180
                   ....*....|....*....|..
gi 1949456009  220 HSHVNAPHDIASGLIGPLITCK 241
Cdd:cd04222    161 HSHIDAPKDIASGLIGPLIICK 182
CuRO_5_ceruloplasmin cd04225
The fifth cupredoxin domain of Ceruloplasmin; Ceruloplasmin is a multicopper oxidase essential ...
 768-935 7.32e-91

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: 288.60  E-value: 7.32e-91
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949456009  768 VKYYISAEEIEWDYSPTRDWELENHHTSpEESPGNIFVGKGENRIGSRYKKVVYRQYTDETFQKQKTRP---DHWGILGP 844
Cdd:cd04225      1 RTYYIAAEEVEWDYSPQRTWEQELHNTH-EESPGNAFLNKGDKFIGSKYKKVVYREYTDDTFSVPKERTaeeEHLGILGP 79

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949456009  845 IIHAEVGEQILIIFKNKASRPYSITAHGVKASGSHV-PVEPGRIIELTWDIPESSGPGTSELNCISYVYFSSVDYIKDLY 923
Cdd:cd04225     80 LIHAEVGEKVKIVFKNMASRPYSIHAHGVKTDSSWVaPTEPGETQTYTWKIPERSGPGVEDSNCISWAYYSTVDQIKDLY 159

                          170
                   ....*....|..
gi 1949456009  924 SGLLGPLVICRP 935
Cdd:cd04225    160 SGLIGPLVICRR 171
CuRO_3_ceruloplasmin cd04224
The third cupredoxin domain of Ceruloplasmin; Ceruloplasmin is a multicopper oxidase essential ...
 417-608 1.09e-90

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: 289.37  E-value: 1.09e-90
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949456009  417 GVVREFFVAAEKATWNYAPSEKNLFNNESLTEADSASEVFFGKEGGRIGGKYVKVLYRAYTDSTFS---KVITSPSHHGF 493
Cdd:cd04224      1 GKVRHYFIAAEEIMWDYAPSGKNLFTGQNLTAPGSDSEVFFQRNETRIGGTYWKVRYVEYTDATFTtrkHRSKEEEHLGI 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949456009  494 LGPVLRVEEGDILNVTFLNKADRGYSIHPHGLNYDKRFQGTSYEDGIDKPGSNVEPGQRFTYSWQVLEGPSSS--DAPCI 571
Cdd:cd04224     81 LGPVIRAEVGDTIKVTFRNKASRPFSIQPHGVFYEKNYEGAMYRDGDPSPGSHVSPGETFTYEWTVPEGVGPTnqDPPCL 160

                          170       180       190
                   ....*....|....*....|....*....|....*..
gi 1949456009  572 SYLYYSGTDPVKDTNSGLVGPLLVCKRGTLGQNGIQR 608
Cdd:cd04224    161 TYLYFSAVDPVRDTNSGLVGPLLVCKKGSLNANGRQK 197
CuRO_1_ceruloplasmin_like cd04199
Cupredoxin domains 1, 3, and 5 of ceruloplasmin and similar proteins; This family includes the ...
 60-242 4.69e-81

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: 261.96  E-value: 4.69e-81
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949456009   60 RVYYIGIIEEDWSYAPSGKNllngkpIVEDEHASIFLERGQHRIGSVYKKAMYREYTDATFSHQAPREEWLGYLGPIIRA 139
Cdd:cd04199      1 RHYYIAAEEIDWDYAPSGLA------EKDLSYRNQYLDNGPFRIGRSYKKVVYREYTDESFTTPGPQPEHLGILGPTIRA 74

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949456009  140 EVNDVIKIHLKNFASRNYSIHPHGLFYKKDAEGALYPDNTSDALKKDDSVPPGGSFTYSWEVKPRFAPTTDDANCLTWVY 219
Cdd:cd04199     75 EVGDTIKVHFKNKASRPYSIHPHGVSYEKDSEGASYSDQTGPDEKKDDAVAPGETYTYVWIVTEESGPTKGDPACLTWAY 154

                          170       180
                   ....*....|....*....|...
gi 1949456009  220 HSHVNAPHDIASGLIGPLITCKT 242
Cdd:cd04199    155 YSHVDLEKDINSGLIGPLLICKK 177
CuRO_2_ceruloplasmin cd11021
The second cupredoxin domain of Ceruloplasmin; Ceruloplasmin is a multicopper oxidase ...
 264-403 4.85e-81

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: 260.48  E-value: 4.85e-81
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949456009  264 DRDIYLMFSVVDENLSWYLEDNIKK-CLDPDGVTVDDPDFEESNLMHAINGYTYGNLPGIELCRHHATAWHLFGMGNEVD 342
Cdd:cd11021      1 DREFVLMFSVVDENLSWYLDENIKTyCSEPAKVDKDDEDFQESNKMHSINGYTFGNLPGLSMCAGDRVKWHLFGMGNEVD 80

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1949456009  343 IHSAFFHGNTLLNRGHRTDTISLFPATFVTATMVPKVKGKWLLSCQVNDHLQAGMQAFYKV 403
Cdd:cd11021     81 IHSAFFHGQTLTDRGHRTDTINLFPATFVTAEMVAQNPGKWLLSCQVNDHLKAGMQAFYEV 141
CuRO_4_ceruloplasmin cd11022
The fourth cupredoxin domain of Ceruloplasmin; Ceruloplasmin is a multicopper oxidase ...
 611-752 8.23e-80

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: 257.41  E-value: 8.23e-80
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949456009  611 DKEFFLLFSVMDENLSWYLEENIKFFGT--SETNQEDEDFEESNKMHAVNGYMYGNLPMLEMCAGDNVVWHTFGLGTEAD 688
Cdd:cd11022      1 DKEFFLLFTVFDENESWYLDENIQQFTLdpRSVDKEDEDFQESNKMHSINGYMYGNQPGLDMCKGDTVSWHLFGLGTETD 80

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1949456009  689 IHGVYFEGNTFKLQSTTRDTVSLFPHTTAALSMRPNNYGLFEVSCRTTDHFSAGMRQLYRVKPC 752
Cdd:cd11022     81 VHGIYFSGNTFLLQGTRRDTANLFPHTSVTAIMQPDNEGTFEVNCQTTDHYSAGMRQIYTVSQC 144
CuRO_3_ceruloplasmin cd04224
The third cupredoxin domain of Ceruloplasmin; Ceruloplasmin is a multicopper oxidase essential ...
 57-249 3.07e-69

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: 230.05  E-value: 3.07e-69
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949456009   57 GTERVYYIGIIEEDWSYAPSGKNLLNGKPIVEDEHAS-IFLERGQHRIGSVYKKAMYREYTDATFS---HQAPREEWLGY 132
Cdd:cd04224      1 GKVRHYFIAAEEIMWDYAPSGKNLFTGQNLTAPGSDSeVFFQRNETRIGGTYWKVRYVEYTDATFTtrkHRSKEEEHLGI 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949456009  133 LGPIIRAEVNDVIKIHLKNFASRNYSIHPHGLFYKKDAEGALYPDntsDALKKDDSVPPGGSFTYSWEVKPRFAPTTDDA 212
Cdd:cd04224     81 LGPVIRAEVGDTIKVTFRNKASRPFSIQPHGVFYEKNYEGAMYRD---GDPSPGSHVSPGETFTYEWTVPEGVGPTNQDP 157

                          170       180       190
                   ....*....|....*....|....*....|....*..
gi 1949456009  213 NCLTWVYHSHVNAPHDIASGLIGPLITCKTGILKNLG 249
Cdd:cd04224    158 PCLTYLYFSAVDPVRDTNSGLVGPLLVCKKGSLNANG 194
CuRO_6_ceruloplasmin cd11012
The sixth cupredoxin domain of Ceruloplasmin; Ceruloplasmin is a multicopper oxidase essential ...
 954-1095 2.56e-68

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: 225.52  E-value: 2.56e-68
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949456009  954 EFALLFLVYDENQSWYLEDNIKNYLGVHPDAFTPDEDFEESNLMHGINGRVYGNLHGLVMQQNEKVDWYLLGMGNEVDMH 1033
Cdd:cd11012      3 EFALLFLVFDENESWYLDENIKTYSDHPEKVNKEDEEFIESNKMHAINGKVFGNLQGLTMHVGDEVYWYLMGMGNEIDIH 82

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1949456009 1034 TVHFHAETFIYRTDLVHRGDVVDLFPGTFATVEMVAANPGTWLLHCHVSDHIHAGMETTYTI 1095
Cdd:cd11012     83 TAHFHGHSFDYKHRGVYRSDVFDLFPGTFQTVEMIPRTPGTWLLHCHVTDHIHAGMETTYTV 144
CuRO_2_ceruloplasmin_like cd04200
Cupredoxin domains 2, 4, and 6 of ceruloplasmin and similar proteins; This family includes the ...
 264-403 9.60e-63

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: 209.57  E-value: 9.60e-63
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949456009  264 DRDIYLMFSVVDENLSWYLEDNIKK-CLDPDGVTVDDPDFEESNLMHAINGYTYGNLPGIELCRHHATAWHLFGMGNEVD 342
Cdd:cd04200      1 DKEFVLLFAVFDENKSWYLEDNIKRfCDNPEKVDKDDEEFQESNKMHAINGYVFGNLPGLTMCAGDRVRWHLLGMGNEVD 80

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1949456009  343 IHSAFFHGNTLLNRGHRTDTISLFPATFVTATMVPKVKGKWLLSCQVNDHLQAGMQAFYKV 403
Cdd:cd04200     81 VHSIHFHGQTFLYKGYRIDTLTLFPATFETVEMVPSNPGTWLLHCHNSDHRHAGMQAYFLV 141
CuRO_5_FV_like cd14451
The fifth cupredoxin domain of coagulation factor V and similar proteins; Factor V is an ...
 59-243 1.18e-61

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: 207.77  E-value: 1.18e-61
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949456009   59 ERVYYIGIIEEDWSYAPSGKNLLNGKPIVEDehasiflergqhrigSVYKKAMYREYTDATFSHQAPR---EEWLGYLGP 135
Cdd:cd14451      1 KRRYYIAAEEEEWDYAGYGKSRLDKTQNERD---------------TVFKKVVFRRYLDSTFSTPDIQgeyEEHLGILGP 65

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949456009  136 IIRAEVNDVIKIHLKNFASRNYSIHPHGLFYKKDAEGALYPDNTSDALKKDDSVPPGGSFTYSWEVKPRFAPTTDDANCL 215
Cdd:cd14451     66 VIRAEVDDVIQVFFKNLASRPYSLHAHGLSYEKSSEGLSYDDESPDWFKKDDAVQPNGTYTYVWYANPRSGPENNGSDCR 145

                          170       180
                   ....*....|....*....|....*...
gi 1949456009  216 TWVYHSHVNAPHDIASGLIGPLITCKTG 243
Cdd:cd14451    146 TWAYYSAVNPEKDIHSGLIGPLLICRKG 173
CuRO_1_ceruloplasmin_like cd04199
Cupredoxin domains 1, 3, and 5 of ceruloplasmin and similar proteins; This family includes the ...
 770-934 7.86e-61

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: 205.72  E-value: 7.86e-61
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949456009  770 YYISAEEIEWDYSPTRDWELENHHTspeespgNIFVGKGENRIGSRYKKVVYRQYTDETFQKQKTRPDHWGILGPIIHAE 849
Cdd:cd04199      3 YYIAAEEIDWDYAPSGLAEKDLSYR-------NQYLDNGPFRIGRSYKKVVYREYTDESFTTPGPQPEHLGILGPTIRAE 75

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949456009  850 VGEQILIIFKNKASRPYSITAHGVKASGSHV----------------PVEPGRIIELTWDIPESSGPGTSELNCISYVYF 913
Cdd:cd04199     76 VGDTIKVHFKNKASRPYSIHPHGVSYEKDSEgasysdqtgpdekkddAVAPGETYTYVWIVTEESGPTKGDPACLTWAYY 155

                          170       180
                   ....*....|....*....|.
gi 1949456009  914 SSVDYIKDLYSGLLGPLVICR 934
Cdd:cd04199    156 SHVDLEKDINSGLIGPLLICK 176
CuRO_3_ceruloplasmin cd04224
The third cupredoxin domain of Ceruloplasmin; Ceruloplasmin is a multicopper oxidase essential ...
 765-940 1.16e-59

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


Pssm-ID: 259886 [Multi-domain]  Cd Length: 197  Bit Score: 203.09  E-value: 1.16e-59
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949456009  765 TRIVKYYISAEEIEWDYSPTRDWELENHHTSPEESPGNIFVGKGENRIGSRYKKVVYRQYTDETFQKQKTRP---DHWGI 841
Cdd:cd04224      1 GKVRHYFIAAEEIMWDYAPSGKNLFTGQNLTAPGSDSEVFFQRNETRIGGTYWKVRYVEYTDATFTTRKHRSkeeEHLGI 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949456009  842 LGPIIHAEVGEQILIIFKNKASRPYSITAHGVK---------------ASGSHVpvEPGRIIELTWDIPESSGPGTSELN 906
Cdd:cd04224     81 LGPVIRAEVGDTIKVTFRNKASRPFSIQPHGVFyeknyegamyrdgdpSPGSHV--SPGETFTYEWTVPEGVGPTNQDPP 158

                          170       180       190
                   ....*....|....*....|....*....|....
gi 1949456009  907 CISYVYFSSVDYIKDLYSGLLGPLVICRPGTLGR 940
Cdd:cd04224    159 CLTYLYFSAVDPVRDTNSGLVGPLLVCKKGSLNA 192
CuRO_2_ceruloplasmin_like cd04200
Cupredoxin domains 2, 4, and 6 of ceruloplasmin and similar proteins; This family includes the ...
 953-1095 3.63e-59

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: 199.56  E-value: 3.63e-59
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949456009  953 REFALLFLVYDENQSWYLEDNIKNYLGVHPDAFTPDEDFEESNLMHGINGRVYGNLHGLVMQQNEKVDWYLLGMGNEVDM 1032
Cdd:cd04200      2 KEFVLLFAVFDENKSWYLEDNIKRFCDNPEKVDKDDEEFQESNKMHAINGYVFGNLPGLTMCAGDRVRWHLLGMGNEVDV 81

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1949456009 1033 HTVHFHAETFIYRTdlvHRGDVVDLFPGTFATVEMVAANPGTWLLHCHVSDHIHAGMETTYTI 1095
Cdd:cd04200     82 HSIHFHGQTFLYKG---YRIDTLTLFPATFETVEMVPSNPGTWLLHCHNSDHRHAGMQAYFLV 141
CuRO_4_ceruloplasmin cd11022
The fourth cupredoxin domain of Ceruloplasmin; Ceruloplasmin is a multicopper oxidase ...
 264-406 4.40e-58

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: 196.55  E-value: 4.40e-58
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949456009  264 DRDIYLMFSVVDENLSWYLEDNIKK-CLDPDGVTVDDPDFEESNLMHAINGYTYGNLPGIELCRHHATAWHLFGMGNEVD 342
Cdd:cd11022      1 DKEFFLLFTVFDENESWYLDENIQQfTLDPRSVDKEDEDFQESNKMHSINGYMYGNQPGLDMCKGDTVSWHLFGLGTETD 80

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1949456009  343 IHSAFFHGNTLLNRGHRTDTISLFPATFVTATMVPKVKGKWLLSCQVNDHLQAGMQAFYKVKAC 406
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 ...
 420-598 5.95e-58

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


Pssm-ID: 259862 [Multi-domain]  Cd Length: 177  Bit Score: 197.24  E-value: 5.95e-58
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949456009  420 REFFVAAEKATWNYAPSEKNLFNNESLTeadsaseVFFGKEGGRIGGKYVKVLYRAYTDSTFSKVITSPSHHGFLGPVLR 499
Cdd:cd04199      1 RHYYIAAEEIDWDYAPSGLAEKDLSYRN-------QYLDNGPFRIGRSYKKVVYREYTDESFTTPGPQPEHLGILGPTIR 73

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949456009  500 VEEGDILNVTFLNKADRGYSIHPHGLNYDKRFQGTSYEDGI---DKPGSNVEPGQRFTYSWQVLE--GPSSSDAPCISYL 574
Cdd:cd04199     74 AEVGDTIKVHFKNKASRPYSIHPHGVSYEKDSEGASYSDQTgpdEKKDDAVAPGETYTYVWIVTEesGPTKGDPACLTWA 153

                          170       180
                   ....*....|....*....|....
gi 1949456009  575 YYSGTDPVKDTNSGLVGPLLVCKR 598
Cdd:cd04199    154 YYSHVDLEKDINSGLIGPLLICKK 177
CuRO_1_Ceruloplasmin_like_1 cd04229
cupredoxin domain of ceruloplasmin homologs; Uncharacterized subfamily of ceruloplasmin ...
 60-238 6.69e-56

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: 191.48  E-value: 6.69e-56
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949456009   60 RVYYIGIIEEDWSYAPSGKNllNGKPIVEDEHASIFLERGQHRIGSVYKKAMYREYTDATFSHQAPREEWLGYLGPIIRA 139
Cdd:cd04229      1 RTYYIAAEEVDWDYAPSGKN--KCCLGDDLEVSTLDSQPGPYTIGSTYTKARYREYTDNSFSTPKPTPAYLGILGPVIRA 78

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949456009  140 EVNDVIKIHLKN-FASRNYSIHPHGLFYKKDAEGAlypdntsdALKKDDSVPPGGSFTYSWEVKPRFAPTTDDANCLTWV 218
Cdd:cd04229     79 EVGDTIKVVFKNnLDEFPVNMHPHGGLYSKDNEGT--------TDGAGDVVAPGETYTYRWIVPEDAGPGPGDPSSRLWL 150

                          170       180
                   ....*....|....*....|
gi 1949456009  219 YHSHVNAPHDIASGLIGPLI 238
Cdd:cd04229    151 YHSHVDVFAHTNAGLVGPII 170
CuRO_2_ceruloplasmin cd11021
The second cupredoxin domain of Ceruloplasmin; Ceruloplasmin is a multicopper oxidase ...
 611-749 1.22e-55

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: 189.22  E-value: 1.22e-55
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949456009  611 DKEFFLLFSVMDENLSWYLEENIKFFGT--SETNQEDEDFEESNKMHAVNGYMYGNLPMLEMCAGDNVVWHTFGLGTEAD 688
Cdd:cd11021      1 DREFVLMFSVVDENLSWYLDENIKTYCSepAKVDKDDEDFQESNKMHSINGYTFGNLPGLSMCAGDRVKWHLFGMGNEVD 80

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1949456009  689 IHGVYFEGNTFKLQSTTRDTVSLFPHTTAALSMRPNNYGLFEVSCRTTDHFSAGMRQLYRV 749
Cdd:cd11021     81 IHSAFFHGQTLTDRGHRTDTINLFPATFVTAEMVAQNPGKWLLSCQVNDHLKAGMQAFYEV 141
CuRO_2_ceruloplasmin cd11021
The second cupredoxin domain of Ceruloplasmin; Ceruloplasmin is a multicopper oxidase ...
 953-1095 4.18e-55

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: 187.68  E-value: 4.18e-55
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949456009  953 REFALLFLVYDENQSWYLEDNIKNYLGVHPDAFTPDEDFEESNLMHGINGRVYGNLHGLVMQQNEKVDWYLLGMGNEVDM 1032
Cdd:cd11021      2 REFVLMFSVVDENLSWYLDENIKTYCSEPAKVDKDDEDFQESNKMHSINGYTFGNLPGLSMCAGDRVKWHLFGMGNEVDI 81

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1949456009 1033 HTVHFHAETFIYRTdlvHRGDVVDLFPGTFATVEMVAANPGTWLLHCHVSDHIHAGMETTYTI 1095
Cdd:cd11021     82 HSAFFHGQTLTDRG---HRTDTINLFPATFVTAEMVAQNPGKWLLSCQVNDHLKAGMQAFYEV 141
CuRO_3_FV_like cd14450
The third cupredoxin domain of coagulation factor V and similar proteins; Factor V is an ...
 62-242 4.57e-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: 186.62  E-value: 4.57e-54
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949456009   62 YYIGIIEEDWSYAPSGKNLLNGKpivedeHASIFLERGQHRIGSVYKKAMYREYTDATFSH--QAPREEWLGYLGPIIRA 139
Cdd:cd14450      5 YFIAAEEVIWDYAPSIPENMDKR------YRSQYLDNFSNNIGKKYKKAVFTQYEDGSFTKrlENPRPKEEGILGPVIRA 78

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949456009  140 EVNDVIKIHLKNFASRNYSIHPHGLFYKKDAEGALYPDNTSDALKKDDSVPPGGSFTYSWEVKPRFAPTTDDANCLTWVY 219
Cdd:cd14450     79 QVRDTIKIVFKNKASRPYSIYPHGVTVSKAAEGASYPPDPRGNETQNKAVQPGETYTYKWNILETDEPTARDPRCLTRMY 158

                          170       180
                   ....*....|....*....|...
gi 1949456009  220 HSHVNAPHDIASGLIGPLITCKT 242
Cdd:cd14450    159 HSAVDITRDIASGLIGPLLICKS 181
CuRO_1_ceruloplasmin cd04222
The first cupredoxin domain of Ceruloplasmin; Ceruloplasmin is a multicopper oxidase essential ...
 420-598 4.58e-54

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: 186.47  E-value: 4.58e-54
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949456009  420 REFFVAAEKATWNYAPSEKNLFNNESLTEaDSASEVFFGKEGGRIGGKYVKVLYRAYTDSTFSKVITSPSHHGFLGPVLR 499
Cdd:cd04222      1 REYYIGIRETQWDYAPSGKNLITNQTFDD-DEHASVFLKRGPDRIGRVYKKAVYLQYTDDTYRTEIEKPVWLGFLGPILK 79

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949456009  500 VEEGDILNVTFLNKADRGYSIHPHGLNYDKRFQGTSYEDGIDKPGSN---VEPGQRFTYSWQVLE--GPSSSDAPCISYL 574
Cdd:cd04222     80 AEVGDVIVVHLKNFASRPYSLHPHGVFYNKENEGALYPDNTSGFEKAddaVPPGGSYTYTWTVPEeqAPTKADANCLTRI 159

                          170       180
                   ....*....|....*....|....
gi 1949456009  575 YYSGTDPVKDTNSGLVGPLLVCKR 598
Cdd:cd04222    160 YHSHIDAPKDIASGLIGPLIICKK 183
CuRO_1_FV_like cd04226
The first cupredoxin domain of coagulation factor VIII and similar proteins; Factor V is an ...
 60-243 2.07e-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: 181.21  E-value: 2.07e-52
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949456009   60 RVYYIGIIEEDWSYAPsgknllngkpivEDEHASIflergqHRIGSVYKKAMYREYtDATFSHQAPREEWLGYLGPIIRA 139
Cdd:cd04226      1 REYYIAAQNIDWDYTP------------QSEELRL------KRSEQSFKKIVYREY-EEGFKKEKPADLSSGLLGPTLRA 61

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949456009  140 EVNDVIKIHLKNFASRNYSIHPHGLFYKKDAEGALYPDNTSDALKKDDSVPPGGSFTYSWEVKPRFAPTTDDANCLTWVY 219
Cdd:cd04226     62 EVGDTLIVHFKNMADKPLSIHPQGIAYGKKSEGSLYSDNTSPVEKLDDAVQPGQEYTYVWDITEEVGPTEADPPCLTYIY 141

                          170       180
                   ....*....|....*....|....
gi 1949456009  220 HSHVNAPHDIASGLIGPLITCKTG 243
Cdd:cd04226    142 YSHVNMVRDFNSGLIGALLICKKG 165
CuRO_1_FVIII_like cd14452
The first cupredoxin domain of coagulation factor VIII and similar proteins; Factor VIII ...
 60-243 1.75e-51

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


Pssm-ID: 259994 [Multi-domain]  Cd Length: 173  Bit Score: 178.63  E-value: 1.75e-51
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949456009   60 RVYYIGIIEEDWSYAPSGknllNGKPIVEDEhasifleRGQHRIGSVYKKAMYREYTDATFSHQAPREEWLGYLGPIIRA 139
Cdd:cd14452      1 RRYYIAAVEIGWDYIHSD----LGDPASEQR-------KKPKDIPQKYIKAVFVEYLDATFTVPKPRPAWMGLLGPTIVA 69

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949456009  140 EVNDVIKIHLKNFASRNYSIHPHGLFYKKDAEGALYPDNTSDALKKDDSVPPGGSFTYSWEVKPRFAPTTDDANCLTWVY 219
Cdd:cd14452     70 EVGDTVVITFKNLASQPYSLHAVGVSYWKASEGAGYDDSTSQHEKEDDAVYPGGYHTYVWDISPKDGPTGSDPECLTYSY 149

                          170       180
                   ....*....|....*....|....
gi 1949456009  220 HSHVNAPHDIASGLIGPLITCKTG 243
Cdd:cd14452    150 SSQVDPVKDVNSGLIGALLVCRMG 173
CuRO_2_ceruloplasmin_like cd04200
Cupredoxin domains 2, 4, and 6 of ceruloplasmin and similar proteins; This family includes the ...
 611-749 3.22e-50

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: 173.75  E-value: 3.22e-50
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949456009  611 DKEFFLLFSVMDENLSWYLEENIKFFGTS--ETNQEDEDFEESNKMHAVNGYMYGNLPMLEMCAGDNVVWHTFGLGTEAD 688
Cdd:cd04200      1 DKEFVLLFAVFDENKSWYLEDNIKRFCDNpeKVDKDDEEFQESNKMHAINGYVFGNLPGLTMCAGDRVRWHLLGMGNEVD 80

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1949456009  689 IHGVYFEGNTFKLQSTTRDTVSLFPHTTAALSMRPNNYGLFEVSCRTTDHFSAGMRQLYRV 749
Cdd:cd04200     81 VHSIHFHGQTFLYKGYRIDTLTLFPATFETVEMVPSNPGTWLLHCHNSDHRHAGMQAYFLV 141
CuRO_1_ceruloplasmin cd04222
The first cupredoxin domain of Ceruloplasmin; Ceruloplasmin is a multicopper oxidase essential ...
 770-934 2.05e-48

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: 170.29  E-value: 2.05e-48
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949456009  770 YYISAEEIEWDYSPTRDwELENHHTSPEESPGNIFVGKGENRIGSRYKKVVYRQYTDETFQKQKTRPDHWGILGPIIHAE 849
Cdd:cd04222      3 YYIGIRETQWDYAPSGK-NLITNQTFDDDEHASVFLKRGPDRIGRVYKKAVYLQYTDDTYRTEIEKPVWLGFLGPILKAE 81

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949456009  850 VGEQILIIFKNKASRPYSITAHGVK----ASGSHVP------------VEPGRIIELTWDIPESSGPGTSELNCISYVYF 913
Cdd:cd04222     82 VGDVIVVHLKNFASRPYSLHPHGVFynkeNEGALYPdntsgfekaddaVPPGGSYTYTWTVPEEQAPTKADANCLTRIYH 161

                          170       180
                   ....*....|....*....|.
gi 1949456009  914 SSVDYIKDLYSGLLGPLVICR 934
Cdd:cd04222    162 SHIDAPKDIASGLIGPLIICK 182
CuRO_1_Ceruloplasmin_like_1 cd04229
cupredoxin domain of ceruloplasmin homologs; Uncharacterized subfamily of ceruloplasmin ...
 420-599 1.90e-47

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: 167.21  E-value: 1.90e-47
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949456009  420 REFFVAAEKATWNYAPSEknlFNNESLTEADSASEVFFGKEGGRIGGKYVKVLYRAYTDSTFSKVITSPSHHGFLGPVLR 499
Cdd:cd04229      1 RTYYIAAEEVDWDYAPSG---KNKCCLGDDLEVSTLDSQPGPYTIGSTYTKARYREYTDNSFSTPKPTPAYLGILGPVIR 77

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949456009  500 VEEGDILNVTFLNKADRG-YSIHPHGLNYDKRFQGTSyeDGIDKPgsnVEPGQRFTYSWQVLE--GPSSSDAPCISYLYY 576
Cdd:cd04229     78 AEVGDTIKVVFKNNLDEFpVNMHPHGGLYSKDNEGTT--DGAGDV---VAPGETYTYRWIVPEdaGPGPGDPSSRLWLYH 152

                          170       180
                   ....*....|....*....|...
gi 1949456009  577 SGTDPVKDTNSGLVGPLLVCKRG 599
Cdd:cd04229    153 SHVDVFAHTNAGLVGPIIVTSKG 175
CuRO_3_FV_like cd14450
The third cupredoxin domain of coagulation factor V and similar proteins; Factor V is an ...
 421-597 2.61e-46

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: 164.28  E-value: 2.61e-46
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949456009  421 EFFVAAEKATWNYAPSEKnlfnnESLTEADSASEVFFGKEggRIGGKYVKVLYRAYTDSTFSK--VITSPSHHGFLGPVL 498
Cdd:cd14450      4 EYFIAAEEVIWDYAPSIP-----ENMDKRYRSQYLDNFSN--NIGKKYKKAVFTQYEDGSFTKrlENPRPKEEGILGPVI 76

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949456009  499 RVEEGDILNVTFLNKADRGYSIHPHGLNYDKRFQGTSYEDgiDKPGSN-----VEPGQRFTYSWQVLEG--PSSSDAPCI 571
Cdd:cd14450     77 RAQVRDTIKIVFKNKASRPYSIYPHGVTVSKAAEGASYPP--DPRGNEtqnkaVQPGETYTYKWNILETdePTARDPRCL 154

                          170       180
                   ....*....|....*....|....*.
gi 1949456009  572 SYLYYSGTDPVKDTNSGLVGPLLVCK 597
Cdd:cd14450    155 TRMYHSAVDITRDIASGLIGPLLICK 180
CuRO_5_ceruloplasmin cd04225
The fifth cupredoxin domain of Ceruloplasmin; Ceruloplasmin is a multicopper oxidase essential ...
 60-241 4.06e-46

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: 163.41  E-value: 4.06e-46
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949456009   60 RVYYIGIIEEDWSYAPS---GKNLLNGKpivEDEHASIFLERGQHRIGSVYKKAMYREYTDATFSHQAPR---EEWLGYL 133
Cdd:cd04225      1 RTYYIAAEEVEWDYSPQrtwEQELHNTH---EESPGNAFLNKGDKFIGSKYKKVVYREYTDDTFSVPKERtaeEEHLGIL 77

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949456009  134 GPIIRAEVNDVIKIHLKNFASRNYSIHPHGLfykkdaegalypdntsdalKKDDSVP----PGGSFTYSWEVKPRFAPTT 209
Cdd:cd04225     78 GPLIHAEVGEKVKIVFKNMASRPYSIHAHGV-------------------KTDSSWVaptePGETQTYTWKIPERSGPGV 138

                          170       180       190
                   ....*....|....*....|....*....|..
gi 1949456009  210 DDANCLTWVYHSHVNAPHDIASGLIGPLITCK 241
Cdd:cd04225    139 EDSNCISWAYYSTVDQIKDLYSGLIGPLVICR 170
CuRO_3_FV_like cd14450
The third cupredoxin domain of coagulation factor V and similar proteins; Factor V is an ...
 770-934 6.22e-46

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: 163.12  E-value: 6.22e-46
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949456009  770 YYISAEEIEWDYSPTRDWELENHHTSPeespgniFVGKGENRIGSRYKKVVYRQYTDETFQK--QKTRPDHWGILGPIIH 847
Cdd:cd14450      5 YFIAAEEVIWDYAPSIPENMDKRYRSQ-------YLDNFSNNIGKKYKKAVFTQYEDGSFTKrlENPRPKEEGILGPVIR 77

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949456009  848 AEVGEQILIIFKNKASRPYSITAHGVK----ASGSHVP------------VEPGRIIELTWDIPESSGPGTSELNCISYV 911
Cdd:cd14450     78 AQVRDTIKIVFKNKASRPYSIYPHGVTvskaAEGASYPpdprgnetqnkaVQPGETYTYKWNILETDEPTARDPRCLTRM 157

                          170       180
                   ....*....|....*....|...
gi 1949456009  912 YFSSVDYIKDLYSGLLGPLVICR 934
Cdd:cd14450    158 YHSAVDITRDIASGLIGPLLICK 180
CuRO_4_ceruloplasmin cd11022
The fourth cupredoxin domain of Ceruloplasmin; Ceruloplasmin is a multicopper oxidase ...
 952-1096 2.17e-45

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: 160.34  E-value: 2.17e-45
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949456009  952 NREFALLFLVYDENQSWYLEDNIKNYLGvHPDAFTP-DEDFEESNLMHGINGRVYGNLHGLVMQQNEKVDWYLLGMGNEV 1030
Cdd:cd11022      1 DKEFFLLFTVFDENESWYLDENIQQFTL-DPRSVDKeDEDFQESNKMHSINGYMYGNQPGLDMCKGDTVSWHLFGLGTET 79

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1949456009 1031 DMHTVHFHAETFIYRTDlvhRGDVVDLFPGTFATVEMVAANPGTWLLHCHVSDHIHAGMETTYTIK 1096
Cdd:cd11022     80 DVHGIYFSGNTFLLQGT---RRDTANLFPHTSVTAIMQPDNEGTFEVNCQTTDHYSAGMRQIYTVS 142
CuRO_5_ceruloplasmin cd04225
The fifth cupredoxin domain of Ceruloplasmin; Ceruloplasmin is a multicopper oxidase essential ...
 420-598 1.55e-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: 158.78  E-value: 1.55e-44
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949456009  420 REFFVAAEKATWNYAPS---EKNLFNneslTEADSASEVFFGKEGGRIGGKYVKVLYRAYTDSTFSKVI--TSPSHH-GF 493
Cdd:cd04225      1 RTYYIAAEEVEWDYSPQrtwEQELHN----THEESPGNAFLNKGDKFIGSKYKKVVYREYTDDTFSVPKerTAEEEHlGI 76

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949456009  494 LGPVLRVEEGDILNVTFLNKADRGYSIHPHGLNydkrfqgtsyEDGIDKpgSNVEPGQRFTYSWQVLE--GPSSSDAPCI 571
Cdd:cd04225     77 LGPLIHAEVGEKVKIVFKNMASRPYSIHAHGVK----------TDSSWV--APTEPGETQTYTWKIPErsGPGVEDSNCI 144

                          170       180
                   ....*....|....*....|....*..
gi 1949456009  572 SYLYYSGTDPVKDTNSGLVGPLLVCKR 598
Cdd:cd04225    145 SWAYYSTVDQIKDLYSGLIGPLVICRR 171
CuRO_1_FV_like cd04226
The first cupredoxin domain of coagulation factor VIII and similar proteins; Factor V is an ...
 420-599 1.98e-44

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: 158.10  E-value: 1.98e-44
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949456009  420 REFFVAAEKATWNYAPSEKNLfnneSLTEADSAsevffgkeggriggkYVKVLYRAYtDSTFSKVITSPSHHGFLGPVLR 499
Cdd:cd04226      1 REYYIAAQNIDWDYTPQSEEL----RLKRSEQS---------------FKKIVYREY-EEGFKKEKPADLSSGLLGPTLR 60

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949456009  500 VEEGDILNVTFLNKADRGYSIHPHGLNYDKRFQGTSYEDG---IDKPGSNVEPGQRFTYSWQVLE--GPSSSDAPCISYL 574
Cdd:cd04226     61 AEVGDTLIVHFKNMADKPLSIHPQGIAYGKKSEGSLYSDNtspVEKLDDAVQPGQEYTYVWDITEevGPTEADPPCLTYI 140

                          170       180
                   ....*....|....*....|....*
gi 1949456009  575 YYSGTDPVKDTNSGLVGPLLVCKRG 599
Cdd:cd04226    141 YYSHVNMVRDFNSGLIGALLICKKG 165
CuRO_3_FVIII_like cd04227
The third cupredoxin domain of coagulation factor VIII and similar proteins; Factor VIII ...
 61-241 2.20e-43

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


Pssm-ID: 259889 [Multi-domain]  Cd Length: 177  Bit Score: 155.86  E-value: 2.20e-43
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949456009   61 VYYIGIIEEDWSYAPSgknllngKPIVED-EHASIFLERGQHRIGSVYKKAMYREYTDATFSHQAPREEWLGYLGPIIRA 139
Cdd:cd04227      4 EHYIAAEELDWDYAPL-------LSSTDDrELQSRYLPTGPQRIGYKYKKVAFVEYTDKTFKRREAKQTEKGILGPLLKG 76

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949456009  140 EVNDVIKIHLKNFASRNYSIHPHGLFYKKDAEGALYPDNTSDAlkKDDSVPPGGSFTYSWEVKPRFAPTTDDANCLTWVY 219
Cdd:cd04227     77 EVGDQIHIMFKNTASRPYNIYPHGLTSVRPMYRSRNPAGEKDL--KTMPIGPGETFGYMWELTAEDGPTEEDPRCLTRLY 154

                          170       180
                   ....*....|....*....|..
gi 1949456009  220 HSHVNAPHDIASGLIGPLITCK 241
Cdd:cd04227    155 QSTVDPERDLASGLIGPLLICK 176
CuRO_1_Ceruloplasmin_like_1 cd04229
cupredoxin domain of ceruloplasmin homologs; Uncharacterized subfamily of ceruloplasmin ...
 770-936 3.00e-43

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


Pssm-ID: 259891 [Multi-domain]  Cd Length: 175  Bit Score: 155.27  E-value: 3.00e-43
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949456009  770 YYISAEEIEWDYSPTRDwelENHHTSPEESPGNIFVGKGENRIGSRYKKVVYRQYTDETFQKQKTRPDHWGILGPIIHAE 849
Cdd:cd04229      3 YYIAAEEVDWDYAPSGK---NKCCLGDDLEVSTLDSQPGPYTIGSTYTKARYREYTDNSFSTPKPTPAYLGILGPVIRAE 79

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949456009  850 VGEQILIIFKNKASR-PYSITAHGV--------KASGSHVPVEPGRIIELTWDIPESSGPGTSELNCISYVYFSSVDYIK 920
Cdd:cd04229     80 VGDTIKVVFKNNLDEfPVNMHPHGGlyskdnegTTDGAGDVVAPGETYTYRWIVPEDAGPGPGDPSSRLWLYHSHVDVFA 159

                          170
                   ....*....|....*.
gi 1949456009  921 DLYSGLLGPLVICRPG 936
Cdd:cd04229    160 HTNAGLVGPIIVTSKG 175
CuRO_5_FV_like cd14451
The fifth cupredoxin domain of coagulation factor V and similar proteins; Factor V is an ...
 420-599 3.19e-43

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: 155.00  E-value: 3.19e-43
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949456009  420 REFFVAAEKATWNYAPSEKNLFNNESLTEAdsasevffgkeggrigGKYVKVLYRAYTDSTFSKVITS---PSHHGFLGP 496
Cdd:cd14451      2 RRYYIAAEEEEWDYAGYGKSRLDKTQNERD----------------TVFKKVVFRRYLDSTFSTPDIQgeyEEHLGILGP 65

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949456009  497 VLRVEEGDILNVTFLNKADRGYSIHPHGLNYDKRFQGTSYEDGID---KPGSNVEPGQRFTYSWQV--LEGPSSSDAPCI 571
Cdd:cd14451     66 VIRAEVDDVIQVFFKNLASRPYSLHAHGLSYEKSSEGLSYDDESPdwfKKDDAVQPNGTYTYVWYAnpRSGPENNGSDCR 145

                          170       180
                   ....*....|....*....|....*...
gi 1949456009  572 SYLYYSGTDPVKDTNSGLVGPLLVCKRG 599
Cdd:cd14451    146 TWAYYSAVNPEKDIHSGLIGPLLICRKG 173
CuRO_3_FVIII_like cd04227
The third cupredoxin domain of coagulation factor VIII and similar proteins; Factor VIII ...
 770-934 3.30e-43

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


Pssm-ID: 259889 [Multi-domain]  Cd Length: 177  Bit Score: 155.09  E-value: 3.30e-43
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949456009  770 YYISAEEIEWDYSPtrdwelenHHTSPEESP-GNIFVGKGENRIGSRYKKVVYRQYTDETFQKQKTRPDHWGILGPIIHA 848
Cdd:cd04227      5 HYIAAEELDWDYAP--------LLSSTDDRElQSRYLPTGPQRIGYKYKKVAFVEYTDKTFKRREAKQTEKGILGPLLKG 76

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949456009  849 EVGEQILIIFKNKASRPYSITAHGV-----------KASGSHV---PVEPGRIIELTWDIPESSGPGTSELNCISYVYFS 914
Cdd:cd04227     77 EVGDQIHIMFKNTASRPYNIYPHGLtsvrpmyrsrnPAGEKDLktmPIGPGETFGYMWELTAEDGPTEEDPRCLTRLYQS 156

                          170       180
                   ....*....|....*....|
gi 1949456009  915 SVDYIKDLYSGLLGPLVICR 934
Cdd:cd04227    157 TVDPERDLASGLIGPLLICK 176
CuRO_5_FV_like cd14451
The fifth cupredoxin domain of coagulation factor V and similar proteins; Factor V is an ...
 769-936 3.10e-41

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: 149.61  E-value: 3.10e-41
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949456009  769 KYYISAEEIEWDYSPtrdwelenhhtspeesPGNIFVGKGENRIGSRYKKVVYRQYTDETFQKQKTR---PDHWGILGPI 845
Cdd:cd14451      3 RYYIAAEEEEWDYAG----------------YGKSRLDKTQNERDTVFKKVVFRRYLDSTFSTPDIQgeyEEHLGILGPV 66

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949456009  846 IHAEVGEQILIIFKNKASRPYSITAHGVKASGSHV----------------PVEPGRIIELTWDIPESSGPGTSELNCIS 909
Cdd:cd14451     67 IRAEVDDVIQVFFKNLASRPYSLHAHGLSYEKSSEglsyddespdwfkkddAVQPNGTYTYVWYANPRSGPENNGSDCRT 146

                          170       180
                   ....*....|....*....|....*..
gi 1949456009  910 YVYFSSVDYIKDLYSGLLGPLVICRPG 936
Cdd:cd14451    147 WAYYSAVNPEKDIHSGLIGPLLICRKG 173
CuRO_6_ceruloplasmin cd11012
The sixth cupredoxin domain of Ceruloplasmin; Ceruloplasmin is a multicopper oxidase essential ...
 269-403 4.03e-41

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


Pssm-ID: 259898 [Multi-domain]  Cd Length: 145  Bit Score: 148.09  E-value: 4.03e-41
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949456009  269 LMFSVVDENLSWYLEDNIKK-CLDPDGVTVDDPDFEESNLMHAINGYTYGNLPGIELCRHHATAWHLFGMGNEVDIHSAF 347
Cdd:cd11012      6 LLFLVFDENESWYLDENIKTySDHPEKVNKEDEEFIESNKMHAINGKVFGNLQGLTMHVGDEVYWYLMGMGNEIDIHTAH 85

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 1949456009  348 FHGNTL---LNRGHRTDTISLFPATFVTATMVPKVKGKWLLSCQVNDHLQAGMQAFYKV 403
Cdd:cd11012     86 FHGHSFdykHRGVYRSDVFDLFPGTFQTVEMIPRTPGTWLLHCHVTDHIHAGMETTYTV 144
CuRO_5_FVIII_like cd04228
The fifth cupredoxin domain of coagulation factor VIII and similar proteins; Factor VIII ...
 767-936 2.19e-39

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: 143.87  E-value: 2.19e-39
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949456009  767 IVKYYISAEEIEWDYSPTRDWelenHHTSPEEspgnifVGKGENRIGSRYKKVVYRQYTDETFQKQKTRPD---HWGILG 843
Cdd:cd04228      1 IRHYFIAAVEVLWDYGMQRPQ----HFLRARD------PNRGRRKSVPQYKKVVFREYLDGSFTQPVYRGEldeHLGILG 70

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949456009  844 PIIHAEVGEQILIIFKNKASRPYSITAHGVKASGSHV------PVEPGRIIELTWDIPESSGPGTSELNCISYVYFSSVD 917
Cdd:cd04228     71 PYIRAEVEDNIMVTFKNLASRPYSFHSSLISYEEDQRaeprgnFVQPGEVQTYSWKVLHQMAPTKQEFDCKAWAYFSNVD 150

                          170
                   ....*....|....*....
gi 1949456009  918 YIKDLYSGLLGPLVICRPG 936
Cdd:cd04228    151 LEKDLHSGLIGPLIICKTG 169
CuRO_6_FVIII_like cd11018
The sixth cupredoxin domain of coagulation factor VIII and similar proteins; Factor VIII ...
 953-1095 2.52e-39

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: 142.71  E-value: 2.52e-39
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949456009  953 REFALLFLVYDENQSWYLEDNIKNYLGVHPDAFTPDEDFEESNLMHGINGRVYGNLHGLVMQQNEKVDWYLLGMGNEVDM 1032
Cdd:cd11018      2 QEFALLFTIFDETKSWYFEENMRRNCRPPCHIQTQDPWFHINNKFHAINGYVADTLPGLVMAQHQRIRWHLLNMGSDEEI 81

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1949456009 1033 HTVHFHAETFIYRTDLVHRGDVVDLFPGTFATVEMVAANPGTWLLHCHVSDHIHAGMETTYTI 1095
Cdd:cd11018     82 HSVHFHGLPFTVRAKKEYRMGVYNLYPGVFGTVEMRPSTAGIWLVECTVGEHLLAGMSALFLV 144
CuRO_2_ceruloplasmin_like_2 cd11023
cupredoxin domain of ceruloplasmin homologs; Uncharacterized subfamily of ceruloplasmin ...
 988-1095 2.58e-39

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


Pssm-ID: 259909 [Multi-domain]  Cd Length: 118  Bit Score: 141.98  E-value: 2.58e-39
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949456009  988 DEDFEESNLMHGINGRVYGNLHGLVMQQNEKVDWYLLGMGNEVDMHTVHFHAETFIyrTDLVHRGDVVDLFPGTFATVEM 1067
Cdd:cd11023     13 DLNVEEAGLMHSINGYVFGNLPGVTIAKGKRVRWHLVAYGNEVDFHTPHWHGQTVE--ADKSRRTDVAELMPASMRVADM 90

                           90       100
                   ....*....|....*....|....*...
gi 1949456009 1068 VAANPGTWLLHCHVSDHIHAGMETTYTI 1095
Cdd:cd11023     91 TAADVGTWLLHCHVHDHYMAGMMTQFAV 118
CuRO_1_FVIII_like cd14452
The first cupredoxin domain of coagulation factor VIII and similar proteins; Factor VIII ...
 420-599 1.22e-38

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: 142.04  E-value: 1.22e-38
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949456009  420 REFFVAAEKATWNYAPSEknlfnnesltEADSASEVffGKEGGRIGGKYVKVLYRAYTDSTFSKVITSPSHHGFLGPVLR 499
Cdd:cd14452      1 RRYYIAAVEIGWDYIHSD----------LGDPASEQ--RKKPKDIPQKYIKAVFVEYLDATFTVPKPRPAWMGLLGPTIV 68

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949456009  500 VEEGDILNVTFLNKADRGYSIHPHGLNYDKRFQGTSYED---GIDKPGSNVEPGQRFTYSWQVLE--GPSSSDAPCISYL 574
Cdd:cd14452     69 AEVGDTVVITFKNLASQPYSLHAVGVSYWKASEGAGYDDstsQHEKEDDAVYPGGYHTYVWDISPkdGPTGSDPECLTYS 148

                          170       180
                   ....*....|....*....|....*
gi 1949456009  575 YYSGTDPVKDTNSGLVGPLLVCKRG 599
Cdd:cd14452    149 YSSQVDPVKDVNSGLIGALLVCRMG 173
CuRO_6_ceruloplasmin cd11012
The sixth cupredoxin domain of Ceruloplasmin; Ceruloplasmin is a multicopper oxidase essential ...
 612-749 5.44e-38

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: 139.23  E-value: 5.44e-38
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949456009  612 KEFFLLFSVMDENLSWYLEENIKFFGTS--ETNQEDEDFEESNKMHAVNGYMYGNLPMLEMCAGDNVVWHTFGLGTEADI 689
Cdd:cd11012      2 LEFALLFLVFDENESWYLDENIKTYSDHpeKVNKEDEEFIESNKMHAINGKVFGNLQGLTMHVGDEVYWYLMGMGNEIDI 81

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1949456009  690 HGVYFEGNTF--KLQSTTR-DTVSLFPHTTAALSMRPNNYGLFEVSCRTTDHFSAGMRQLYRV 749
Cdd:cd11012     82 HTAHFHGHSFdyKHRGVYRsDVFDLFPGTFQTVEMIPRTPGTWLLHCHVTDHIHAGMETTYTV 144
CuRO_3_FVIII_like cd04227
The third cupredoxin domain of coagulation factor VIII and similar proteins; Factor VIII ...
 418-598 1.60e-37

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


Pssm-ID: 259889 [Multi-domain]  Cd Length: 177  Bit Score: 138.91  E-value: 1.60e-37
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949456009  418 VVREFFVAAEKATWNYAPseknlfnNESLTEADSASEVFFGKEGGRIGGKYVKVLYRAYTDSTFSKVITSPSHHGFLGPV 497
Cdd:cd04227      1 QTWEHYIAAEELDWDYAP-------LLSSTDDRELQSRYLPTGPQRIGYKYKKVAFVEYTDKTFKRREAKQTEKGILGPL 73

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949456009  498 LRVEEGDILNVTFLNKADRGYSIHPHGLN----YDKRFQGTSYEDGIDKPgsnVEPGQRFTYSWQVL--EGPSSSDAPCI 571
Cdd:cd04227     74 LKGEVGDQIHIMFKNTASRPYNIYPHGLTsvrpMYRSRNPAGEKDLKTMP---IGPGETFGYMWELTaeDGPTEEDPRCL 150

                          170       180
                   ....*....|....*....|....*..
gi 1949456009  572 SYLYYSGTDPVKDTNSGLVGPLLVCKR 598
Cdd:cd04227    151 TRLYQSTVDPERDLASGLIGPLLICKK 177
CuRO_1_FVIII_like cd14452
The first cupredoxin domain of coagulation factor VIII and similar proteins; Factor VIII ...
 769-936 1.82e-37

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: 138.57  E-value: 1.82e-37
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949456009  769 KYYISAEEIEWDYSPTRDWELEnhhTSPEESPGNIFVgkgenrigsRYKKVVYRQYTDETFQKQKTRPDHWGILGPIIHA 848
Cdd:cd14452      2 RYYIAAVEIGWDYIHSDLGDPA---SEQRKKPKDIPQ---------KYIKAVFVEYLDATFTVPKPRPAWMGLLGPTIVA 69

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949456009  849 EVGEQILIIFKNKASRPYSITAHGV---KAS-GSHV------------PVEPGRIIELTWDIPESSGPGTSELNCISYVY 912
Cdd:cd14452     70 EVGDTVVITFKNLASQPYSLHAVGVsywKASeGAGYddstsqhekeddAVYPGGYHTYVWDISPKDGPTGSDPECLTYSY 149

                          170       180
                   ....*....|....*....|....
gi 1949456009  913 FSSVDYIKDLYSGLLGPLVICRPG 936
Cdd:cd14452    150 SSQVDPVKDVNSGLIGALLVCRMG 173
CuRO_5_FVIII_like cd04228
The fifth cupredoxin domain of coagulation factor VIII and similar proteins; Factor VIII ...
 60-243 2.55e-37

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: 138.10  E-value: 2.55e-37
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949456009   60 RVYYIGIIEEDWSYApsgknllNGKPivedEH--ASIFLERGQHRIGSVYKKAMYREYTDATFSHQAPR---EEWLGYLG 134
Cdd:cd04228      2 RHYFIAAVEVLWDYG-------MQRP----QHflRARDPNRGRRKSVPQYKKVVFREYLDGSFTQPVYRgelDEHLGILG 70

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949456009  135 PIIRAEVNDVIKIHLKNFASRNYSIHPHGLFYKkdaegalypdNTSDALKKDDSVPPGGSFTYSWEVKPRFAPTTDDANC 214
Cdd:cd04228     71 PYIRAEVEDNIMVTFKNLASRPYSFHSSLISYE----------EDQRAEPRGNFVQPGEVQTYSWKVLHQMAPTKQEFDC 140

                          170       180
                   ....*....|....*....|....*....
gi 1949456009  215 LTWVYHSHVNAPHDIASGLIGPLITCKTG 243
Cdd:cd04228    141 KAWAYFSNVDLEKDLHSGLIGPLIICKTG 169
CuRO_6_FV_like cd14455
The sixth cupredoxin domain of coagulation factor V and similar proteins; Factor V is an ...
 953-1095 4.59e-37

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: 136.15  E-value: 4.59e-37
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949456009  953 REFALLFLVYDENQSWYLEDNIKNylgVHPDAFTPDEDFEESNLMHGINGRVYgNLHGLVMQQNEKVDWYLLGMGNEVDM 1032
Cdd:cd14455      2 REFVLLFMTFDEEKSWYYEKNRKR---TCRENRVKDPNVQDNHTFHAINGIIY-NLKGLRMYTNELVRWHLINMGGPKDL 77

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1949456009 1033 HTVHFHAETFIYRTDLVHRGDVVDLFPGTFATVEMVAANPGTWLLHCHVSDHIHAGMETTYTI 1095
Cdd:cd14455     78 HVVHFHGQTFTEKGLKDHQLGVYPLLPGSFATLEMKPSKPGLWLLETEVGESQQRGMQTLFLV 140
CuRO_1_FV_like cd04226
The first cupredoxin domain of coagulation factor VIII and similar proteins; Factor V is an ...
 770-936 3.05e-36

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: 134.99  E-value: 3.05e-36
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949456009  770 YYISAEEIEWDYSPtrdwelENHHTSPEESpgnifvgkgenriGSRYKKVVYRQYtDETFQKQKTRPDHWGILGPIIHAE 849
Cdd:cd04226      3 YYIAAQNIDWDYTP------QSEELRLKRS-------------EQSFKKIVYREY-EEGFKKEKPADLSSGLLGPTLRAE 62

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949456009  850 VGEQILIIFKNKASRPYSITAHGV----KASGSH-----VPVE-------PGRIIELTWDIPESSGPGTSELNCISYVYF 913
Cdd:cd04226     63 VGDTLIVHFKNMADKPLSIHPQGIaygkKSEGSLysdntSPVEklddavqPGQEYTYVWDITEEVGPTEADPPCLTYIYY 142

                          170       180
                   ....*....|....*....|...
gi 1949456009  914 SSVDYIKDLYSGLLGPLVICRPG 936
Cdd:cd04226    143 SHVNMVRDFNSGLIGALLICKKG 165
CuRO_4_FVIII_like cd11016
The fourth cupredoxin domain of coagulation factor VIII and similar proteins; Factor VIII ...
 264-406 4.98e-34

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


Pssm-ID: 259902 [Multi-domain]  Cd Length: 143  Bit Score: 127.68  E-value: 4.98e-34
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949456009  264 DRDIYLMFSVVDENLSWYLEDNIKK-CLDPDGVTVDDPDFEESNLMHAINGYTYGNLPgIELCRHHATAWHLFGMGNEVD 342
Cdd:cd11016      1 DKDWSLLFSVFDENNSWYLKENIHRfTQTPAGVNDTDPDFYASNVMHTINGIVFDRRQ-FVICLTDVAYWYVLSVGAQTD 79

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1949456009  343 IHSAFFHGNTLLNRGHRTDTISLFPATFVTATMVPKVKGKWLLSCQVNDHLQAGMQAFYKVKAC 406
Cdd:cd11016     80 FLSVFFSGNTFKHQMVYEDVLTLFPFSGETVSMSPEVPGEWELGCFNGDFRSRGMSAQYTVSTC 143
CuRO_4_FVIII_like cd11016
The fourth cupredoxin domain of coagulation factor VIII and similar proteins; Factor VIII ...
 611-752 3.68e-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: 122.28  E-value: 3.68e-32
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949456009  611 DKEFFLLFSVMDENLSWYLEENIKFFGTSET--NQEDEDFEESNKMHAVNGYMYGNLpMLEMCAGDNVVWHTFGLGTEAD 688
Cdd:cd11016      1 DKDWSLLFSVFDENNSWYLKENIHRFTQTPAgvNDTDPDFYASNVMHTINGIVFDRR-QFVICLTDVAYWYVLSVGAQTD 79

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1949456009  689 IHGVYFEGNTFKLQSTTRDTVSLFPHTTAALSMRPNNYGLFEVSCRTTDHFSAGMRQLYRVKPC 752
Cdd:cd11016     80 FLSVFFSGNTFKHQMVYEDVLTLFPFSGETVSMSPEVPGEWELGCFNGDFRSRGMSAQYTVSTC 143
CuRO_2_ceruloplasmin_like_2 cd11023
cupredoxin domain of ceruloplasmin homologs; Uncharacterized subfamily of ceruloplasmin ...
 298-403 4.38e-32

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: 121.18  E-value: 4.38e-32
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949456009  298 DDPDFEESNLMHAINGYTYGNLPGIELCRHHATAWHLFGMGNEVDIHSAFFHGNTLLNRGH-RTDTISLFPATFVTATMV 376
Cdd:cd11023     12 LDLNVEEAGLMHSINGYVFGNLPGVTIAKGKRVRWHLVAYGNEVDFHTPHWHGQTVEADKSrRTDVAELMPASMRVADMT 91

                           90       100
                   ....*....|....*....|....*..
gi 1949456009  377 PKVKGKWLLSCQVNDHLQAGMQAFYKV 403
Cdd:cd11023     92 AADVGTWLLHCHVHDHYMAGMMTQFAV 118
CuRO_6_FVIII_like cd11018
The sixth cupredoxin domain of coagulation factor VIII and similar proteins; Factor VIII ...
 269-403 4.52e-32

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: 121.91  E-value: 4.52e-32
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949456009  269 LMFSVVDENLSWYLEDNIKK-CLDPDGVTVDDPDFEESNLMHAINGYTYGNLPGIELCRHHATAWHLFGMGNEVDIHSAF 347
Cdd:cd11018      6 LLFTIFDETKSWYFEENMRRnCRPPCHIQTQDPWFHINNKFHAINGYVADTLPGLVMAQHQRIRWHLLNMGSDEEIHSVH 85

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 1949456009  348 FHGNTLLNRG---HRTDTISLFPATFVTATMVPKVKGKWLLSCQVNDHLQAGMQAFYKV 403
Cdd:cd11018     86 FHGLPFTVRAkkeYRMGVYNLYPGVFGTVEMRPSTAGIWLVECTVGEHLLAGMSALFLV 144
CuRO_5_FVIII_like cd04228
The fifth cupredoxin domain of coagulation factor VIII and similar proteins; Factor VIII ...
 419-599 4.36e-31

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: 120.38  E-value: 4.36e-31
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949456009  419 VREFFVAAEKATWNYAPSEKNLFNNEslTEADSASEVFFGKeggriggkYVKVLYRAYTDSTFSKVITS---PSHHGFLG 495
Cdd:cd04228      1 IRHYFIAAVEVLWDYGMQRPQHFLRA--RDPNRGRRKSVPQ--------YKKVVFREYLDGSFTQPVYRgelDEHLGILG 70

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949456009  496 PVLRVEEGDILNVTFLNKADRGYSIHPHGLNYDkrfqgtsyEDGIDKPGSN-VEPGQRFTYSWQVLE--GPSSSDAPCIS 572
Cdd:cd04228     71 PYIRAEVEDNIMVTFKNLASRPYSFHSSLISYE--------EDQRAEPRGNfVQPGEVQTYSWKVLHqmAPTKQEFDCKA 142

                          170       180
                   ....*....|....*....|....*..
gi 1949456009  573 YLYYSGTDPVKDTNSGLVGPLLVCKRG 599
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 ...
 264-403 1.03e-30

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: 117.27  E-value: 1.03e-30
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949456009  264 DRDIYLMFSVVDENLSWYlednikkcldpdgvtvdDPDFEESNLMHAINGYTYGNLPGIELCRHHATAWHLFGMGNEVDI 343
Cdd:cd14453      1 YKEYVLMFGVFDENKSWY-----------------KQNASVDSVKYTINGYTNGTLPDVSICAYDHVSWHLLGMSSEPEL 63

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949456009  344 HSAFFHGNTLLNRGHRTDTISLFPATFVTATMVPKVKGKWLLSCQVNDHLQAGMQAFYKV 403
Cdd:cd14453     64 FSVHFNGQVLEQNGHKVSAVGLVSGSSTTASMTVVHTGRWLISSLIMKHLQAGMYGYLNI 123
CuRO_2_FVIII_like cd11015
The second cupredoxin domain of coagulation factor VIII and similar proteins; Factor VIII ...
 269-403 1.44e-30

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


Pssm-ID: 259901 [Multi-domain]  Cd Length: 134  Bit Score: 117.31  E-value: 1.44e-30
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949456009  269 LMFSVVDENLSWYLEDNIKKCLDPDGVTVDDPDfeesnlMHAINGYTYGNLPGIELCRHHATAWHLFGMGNEVDIHSAFF 348
Cdd:cd11015      6 LLFAVFDEGKSWYSEVGERKSRDKFKRADSRKE------FHTINGYINASLPGLKICQRKPVIWHVIGMGTAPEVHSIFF 79

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 1949456009  349 HGNTLLNRGHRTDTISLFPATFVTATMVPKVKGKWLLSCQVNDHLQAGMQAFYKV 403
Cdd:cd11015     80 EGHTFLVRTHRKVSLEISPMTFLTAQTKPATVGSFLIFCQIHSHQHDGMEAMVKV 134
CuRO_6_FV_like cd14455
The sixth cupredoxin domain of coagulation factor V and similar proteins; Factor V is an ...
 265-403 8.17e-28

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: 109.57  E-value: 8.17e-28
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949456009  265 RDIYLMFSVVDENLSWYLEDNIKK-CLDpdgVTVDDPDFEESNLMHAINGYTYgNLPGIELCRHHATAWHLFGMGNEVDI 343
Cdd:cd14455      2 REFVLLFMTFDEEKSWYYEKNRKRtCRE---NRVKDPNVQDNHTFHAINGIIY-NLKGLRMYTNELVRWHLINMGGPKDL 77

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1949456009  344 HSAFFHGNTLLNRG---HRTDTISLFPATFVTATMVPKVKGKWLLSCQVNDHLQAGMQAFYKV 403
Cdd:cd14455     78 HVVHFHGQTFTEKGlkdHQLGVYPLLPGSFATLEMKPSKPGLWLLETEVGESQQRGMQTLFLV 140
CuRO_4_FV_like cd14454
The fourth cupredoxin domain of coagulation factor V and similar proteins; Factor V is an ...
 264-386 3.66e-27

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


Pssm-ID: 259996 [Multi-domain]  Cd Length: 144  Bit Score: 108.04  E-value: 3.66e-27
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949456009  264 DRDIYLMFSVVDENLSWYLEDNIKK-CLDPDGVTVDDPDFEESNLMHAINGYTYGNLPGIELCRHHATAWHLFGMGNEVD 342
Cdd:cd14454      1 DLEQHAVFAVFDENKSWYLEENINKyCSNPNNVKKDDPKFYKSNIMPTINGYAYESSAPLGFCHSEVVQWHISSVGTQDE 80

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....
gi 1949456009  343 IHSAFFHGNTLLNRGHRTDTISLFPATFVTATMVPKVKGKWLLS 386
Cdd:cd14454     81 IITVHLSGHTFRYKGKHEDTLNLFPMSGESITVTMDNLGTWLLG 124
CuRO_6_FVIII_like cd11018
The sixth cupredoxin domain of coagulation factor VIII and similar proteins; Factor VIII ...
 612-749 2.08e-25

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: 103.04  E-value: 2.08e-25
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949456009  612 KEFFLLFSVMDENLSWYLEENIKFF--GTSETNQEDEDFEESNKMHAVNGYMYGNLPMLEMCAGDNVVWHTFGLGTEADI 689
Cdd:cd11018      2 QEFALLFTIFDETKSWYFEENMRRNcrPPCHIQTQDPWFHINNKFHAINGYVADTLPGLVMAQHQRIRWHLLNMGSDEEI 81

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1949456009  690 HGVYFEGNTFKLQSTTRDTV---SLFPHTTAALSMRPNNYGLFEVSCRTTDHFSAGMRQLYRV 749
Cdd:cd11018     82 HSVHFHGLPFTVRAKKEYRMgvyNLYPGVFGTVEMRPSTAGIWLVECTVGEHLLAGMSALFLV 144
CuRO_4_FV_like cd14454
The fourth cupredoxin domain of coagulation factor V and similar proteins; Factor V is an ...
 611-744 2.57e-25

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: 102.64  E-value: 2.57e-25
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949456009  611 DKEFFLLFSVMDENLSWYLEENIKFF--GTSETNQEDEDFEESNKMHAVNGYMYGNLPMLEMCAGDNVVWHTFGLGTEAD 688
Cdd:cd14454      1 DLEQHAVFAVFDENKSWYLEENINKYcsNPNNVKKDDPKFYKSNIMPTINGYAYESSAPLGFCHSEVVQWHISSVGTQDE 80

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 1949456009  689 IHGVYFEGNTFKLQSTTRDTVSLFPHTTAALSMRPNNYGLFEVSCRTTDHFSAGMR 744
Cdd:cd14454     81 IITVHLSGHTFRYKGKHEDTLNLFPMSGESITVTMDNLGTWLLGSFGSSKKSKGLR 136
CuRO_4_FVIII_like cd11016
The fourth cupredoxin domain of coagulation factor VIII and similar proteins; Factor VIII ...
 952-1095 6.40e-25

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


Pssm-ID: 259902 [Multi-domain]  Cd Length: 143  Bit Score: 101.48  E-value: 6.40e-25
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949456009  952 NREFALLFLVYDENQSWYLEDNIKNYLGVHPDAFTPDEDFEESNLMHGINGRVYGNLHgLVMQQNEKVDWYLLGMGNEVD 1031
Cdd:cd11016      1 DKDWSLLFSVFDENNSWYLKENIHRFTQTPAGVNDTDPDFYASNVMHTINGIVFDRRQ-FVICLTDVAYWYVLSVGAQTD 79

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1949456009 1032 MHTVHFHAETFiyrtdlVHRG---DVVDLFPGTFATVEMVAANPGTWLLHCHVSDHIHAGMETTYTI 1095
Cdd:cd11016     80 FLSVFFSGNTF------KHQMvyeDVLTLFPFSGETVSMSPEVPGEWELGCFNGDFRSRGMSAQYTV 140
CuRO_2_FVIII_like cd11015
The second cupredoxin domain of coagulation factor VIII and similar proteins; Factor VIII ...
 952-1090 1.66e-24

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


Pssm-ID: 259901 [Multi-domain]  Cd Length: 134  Bit Score: 99.98  E-value: 1.66e-24
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949456009  952 NREFALLFLVYDENQSWYLEdnIKNYLGvhPDAFTPDEDFEEsnlMHGINGRVYGNLHGLVMQQNEKVDWYLLGMGNEVD 1031
Cdd:cd11015      1 NQAFVLLFAVFDEGKSWYSE--VGERKS--RDKFKRADSRKE---FHTINGYINASLPGLKICQRKPVIWHVIGMGTAPE 73

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 1949456009 1032 MHTVHFHAETFIYRTdlvHRGDVVDLFPGTFATVEMVAANPGTWLLHCHVSDHIHAGME 1090
Cdd:cd11015     74 VHSIFFEGHTFLVRT---HRKVSLEISPMTFLTAQTKPATVGSFLIFCQIHSHQHDGME 129
CuRO_2_FVIII_like cd11015
The second cupredoxin domain of coagulation factor VIII and similar proteins; Factor VIII ...
 612-749 2.68e-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: 96.51  E-value: 2.68e-23
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949456009  612 KEFFLLFSVMDENLSWYLEEnikffGTSETNQEDEDFEESNKMHAVNGYMYGNLPMLEMCAGDNVVWHTFGLGTEADIHG 691
Cdd:cd11015      2 QAFVLLFAVFDEGKSWYSEV-----GERKSRDKFKRADSRKEFHTINGYINASLPGLKICQRKPVIWHVIGMGTAPEVHS 76

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 1949456009  692 VYFEGNTFKLQSTTRDTVSLFPHTTAALSMRPNNYGLFEVSCRTTDHFSAGMRQLYRV 749
Cdd:cd11015     77 IFFEGHTFLVRTHRKVSLEISPMTFLTAQTKPATVGSFLIFCQIHSHQHDGMEAMVKV 134
CuRO_4_FV_like cd14454
The fourth cupredoxin domain of coagulation factor V and similar proteins; Factor V is an ...
 958-1094 5.05e-21

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: 90.32  E-value: 5.05e-21
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949456009  958 LFLVYDENQSWYLEDNIKNYLGVHPDAFTPDEDFEESNLMHGINGRVYGNLHGLVMQQNEKVDWYLLGMGNEVDMHTVHF 1037
Cdd:cd14454      7 VFAVFDENKSWYLEENINKYCSNPNNVKKDDPKFYKSNIMPTINGYAYESSAPLGFCHSEVVQWHISSVGTQDEIITVHL 86

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 1949456009 1038 HAETFIYRTdlvHRGDVVDLFPGTFATVEMVAANPGTWLLHCHVSDHIHAGMETTYT 1094
Cdd:cd14454     87 SGHTFRYKG---KHEDTLNLFPMSGESITVTMDNLGTWLLGSFGSSKKSKGLRVRFT 140
CuRO_2_FV_like cd14453
The second cupredoxin domain of coagulation factor V and similar proteins; Factor V is an ...
 952-1089 2.10e-20

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: 87.99  E-value: 2.10e-20
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949456009  952 NREFALLFLVYDENQSWYledniknylgvhpdaftpDEDFEESNLMHGINGRVYGNLHGLVMQQNEKVDWYLLGMGNEVD 1031
Cdd:cd14453      1 YKEYVLMFGVFDENKSWY------------------KQNASVDSVKYTINGYTNGTLPDVSICAYDHVSWHLLGMSSEPE 62

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 1949456009 1032 MHTVHFHAETFIYRTdlvHRGDVVDLFPGTFATVEMVAANPGTWLLHCHVSDHIHAGM 1089
Cdd:cd14453     63 LFSVHFNGQVLEQNG---HKVSAVGLVSGSSTTASMTVVHTGRWLISSLIMKHLQAGM 117
CuRO_2_ceruloplasmin_like_2 cd11023
cupredoxin domain of ceruloplasmin homologs; Uncharacterized subfamily of ceruloplasmin ...
 645-749 2.29e-20

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: 87.67  E-value: 2.29e-20
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949456009  645 DEDFEESNKMHAVNGYMYGNLPMLEMCAGDNVVWHTFGLGTEADIHGVYFEGNTFKLQSTTR-DTVSLFPHTTAALSMRP 723
Cdd:cd11023     13 DLNVEEAGLMHSINGYVFGNLPGVTIAKGKRVRWHLVAYGNEVDFHTPHWHGQTVEADKSRRtDVAELMPASMRVADMTA 92

                           90       100
                   ....*....|....*....|....*.
gi 1949456009  724 NNYGLFEVSCRTTDHFSAGMRQLYRV 749
Cdd:cd11023     93 ADVGTWLLHCHVHDHYMAGMMTQFAV 118
CuRO_6_FV_like cd14455
The sixth cupredoxin domain of coagulation factor V and similar proteins; Factor V is an ...
 612-749 3.24e-20

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


Pssm-ID: 259997 [Multi-domain]  Cd Length: 140  Bit Score: 88.00  E-value: 3.24e-20
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949456009  612 KEFFLLFSVMDENLSWYLEENIKffGTSETNQE-DEDFEESNKMHAVNGYMYgNLPMLEMCAGDNVVWHTFGLGTEADIH 690
Cdd:cd14455      2 REFVLLFMTFDEEKSWYYEKNRK--RTCRENRVkDPNVQDNHTFHAINGIIY-NLKGLRMYTNELVRWHLINMGGPKDLH 78

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1949456009  691 GVYFEGNTF---KLQSTTRDTVSLFPHTTAALSMRPNNYGLFEVSCRTTDHFSAGMRQLYRV 749
Cdd:cd14455     79 VVHFHGQTFtekGLKDHQLGVYPLLPGSFATLEMKPSKPGLWLLETEVGESQQRGMQTLFLV 140
Cu-oxidase_2 pfam07731
Multicopper oxidase; This entry contains many divergent copper oxidase-like domains that are ...
 982-1099 5.94e-18

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


Pssm-ID: 462246 [Multi-domain]  Cd Length: 138  Bit Score: 81.33  E-value: 5.94e-18
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949456009  982 PDAFTPDeDFEESNLMHGINGRVYG-NLHGLVMQQNEKVDWYLLGMGNevDMHTVHFHAETFiyrtDLVHRG-------- 1052
Cdd:pfam07731    7 PTLLQIT-SGNFRRNDWAINGLLFPpNTNVITLPYGTVVEWVLQNTTT--GVHPFHLHGHSF----QVLGRGggpwpeed 79

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 1949456009 1053 ------------DVVDLFPGTFATVEMVAANPGTWLLHCHVSDHIHAGMETTYTIKEKS 1099
Cdd:pfam07731   80 pktynlvdpvrrDTVQVPPGGWVAIRFRADNPGVWLFHCHILWHLDQGMMGQFVVRPGD 138
CuRO_1_LCC_like cd04206
Cupredoxin domain 1 of laccase-like multicopper oxidases; including laccase, CueO, spore coat ...
 133-238 7.67e-18

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: 80.41  E-value: 7.67e-18
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949456009  133 LGPIIRAEVNDVIKIHLKN-FASRNYSIHPHGLFYKKDAEGALYPDNTSDAlkkddsVPPGGSFTYSWEVKPRfapttdd 211
Cdd:cd04206     29 PGPTIRVKEGDTVEVTVTNnLPNEPTSIHWHGLRQPGTNDGDGVAGLTQCP------IPPGESFTYRFTVDDQ------- 95

                           90       100
                   ....*....|....*....|....*..
gi 1949456009  212 anCLTWVYHSHVNapHDIASGLIGPLI 238
Cdd:cd04206     96 --AGTFWYHSHVG--GQRADGLYGPLI 118
CuRO_2_FV_like cd14453
The second cupredoxin domain of coagulation factor V and similar proteins; Factor V is an ...
 611-743 4.74e-17

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


Pssm-ID: 259995 [Multi-domain]  Cd Length: 123  Bit Score: 78.36  E-value: 4.74e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949456009  611 DKEFFLLFSVMDENLSWYleenikffgtsetNQEDEdfeESNKMHAVNGYMYGNLPMLEMCAGDNVVWHTFGLGTEADIH 690
Cdd:cd14453      1 YKEYVLMFGVFDENKSWY-------------KQNAS---VDSVKYTINGYTNGTLPDVSICAYDHVSWHLLGMSSEPELF 64

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|...
gi 1949456009  691 GVYFEGNTFKLQSTTRDTVSLFPHTTAALSMRPNNYGLFEVSCRTTDHFSAGM 743
Cdd:cd14453     65 SVHFNGQVLEQNGHKVSAVGLVSGSSTTASMTVVHTGRWLISSLIMKHLQAGM 117
CuRO_3_LCC_like cd04207
Cupredoxin domain 3 of laccase-like multicopper oxidases; including laccase, CueO, spore coat ...
 989-1094 1.60e-13

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


Pssm-ID: 259870 [Multi-domain]  Cd Length: 132  Bit Score: 68.64  E-value: 1.60e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949456009  989 EDFEESNLMH-GINGRVY----GNLHGLVMQQNEKVDWYLLGMGNEVDMHTVHFHAETF-------------IYRTDLVH 1050
Cdd:cd04207     10 QTGAPDGTTRwVINGMPFkegdANTDIFSVEAGDVVEIVLINAGNHDMQHPFHLHGHSFwvlgsgggpfdapLNLTNPPW 89

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....
gi 1949456009 1051 RgDVVDLFPGTFATVEMVAANPGTWLLHCHVSDHIHAGMETTYT 1094
Cdd:cd04207     90 R-DTVLVPPGGWVVIRFKADNPGVWMLHCHILEHEDAGMMTVFE 132
CuRO_1_LCC_like cd04206
Cupredoxin domain 1 of laccase-like multicopper oxidases; including laccase, CueO, spore coat ...
 492-596 3.32e-13

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


Pssm-ID: 259869 [Multi-domain]  Cd Length: 120  Bit Score: 67.31  E-value: 3.32e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949456009  492 GFLGPVLRVEEGDILNVTFLNKAD-RGYSIHPHGLnydkRFQGTSYEDGIDKPGSN-VEPGQRFTYSWQVlegpsssDAP 569
Cdd:cd04206     27 QFPGPTIRVKEGDTVEVTVTNNLPnEPTSIHWHGL----RQPGTNDGDGVAGLTQCpIPPGESFTYRFTV-------DDQ 95

                           90       100
                   ....*....|....*....|....*..
gi 1949456009  570 CISYLYYSGTDPVKDTnsGLVGPLLVC 596
Cdd:cd04206     96 AGTFWYHSHVGGQRAD--GLYGPLIVE 120
CuRO_1_CumA_like cd13861
The first cupredoxin domain of CumA like multicopper oxidase; This multicopper oxidase (MCO) ...
 134-238 4.52e-12

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: 63.79  E-value: 4.52e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949456009  134 GPIIRAEVNDVIKIHLKNFASRNYSIHPHGLFYKKDAEGAlyPDNTSDAlkkddsVPPGGSFTYswevkpRFapTTDDAN 213
Cdd:cd13861     31 GPELRVRQGDTLRVRLTNRLPEPTTIHWHGLRLPNAMDGV--PGLTQPP------VPPGESFTY------EF--TPPDAG 94

                           90       100
                   ....*....|....*....|....*
gi 1949456009  214 clTWVYHSHVNAPHDIASGLIGPLI 238
Cdd:cd13861     95 --TYWYHPHVGSQEQLDRGLYGPLI 117
Cu-oxidase_3 pfam07732
Multicopper oxidase; This entry contains many divergent copper oxidase-like domains that are ...
 114-238 4.71e-12

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


Pssm-ID: 462247 [Multi-domain]  Cd Length: 119  Bit Score: 63.80  E-value: 4.71e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949456009  114 EYTDATFSHQAPREEWL---GYLGPIIRAEVNDVIKIHLKNFASRNYSIHPHGLFYKK--DAEGALYpdNTSDALkkdds 188
Cdd:pfam07732    3 TYGTVSPLGGTRQAVIGvngQFPGPTIRVREGDTVVVNVTNNLDEPTSIHWHGLQQRGtpWMDGVPG--VTQCPI----- 75

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|
gi 1949456009  189 vPPGGSFTYSWEVKprfapttdDANCLTWvYHSHvnAPHDIASGLIGPLI 238
Cdd:pfam07732   76 -PPGQSFTYRFQVK--------QQAGTYW-YHSH--TSGQQAAGLAGAII 113
CuRO_1_2DMCO_NIR_like_2 cd14449
The cupredoxin domain 1 of a two-domain laccase related to nitrite reductase; The two-domain ...
 495-595 2.01e-11

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


Pssm-ID: 259991 [Multi-domain]  Cd Length: 135  Bit Score: 62.67  E-value: 2.01e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949456009  495 GPVLRVEEGDILNVTFLNKADRGYSIHPHGLNYDkrfqgtSYEDGIDKPGSNVEPGQRFTYSWQVLEGPSSSDAPCIS-- 572
Cdd:cd14449     29 GPVIEVREGDTLKILFRNTLDVPASLHPHGVDYT------TASDGTGMNASIVAPGDTRIYTWRTHGGYRRADGSWAEgt 102

                           90       100       110
                   ....*....|....*....|....*....|...
gi 1949456009  573 --YLYY--------SGTDPVKdtnSGLVGPLLV 595
Cdd:cd14449    103 agYWHYhdhvfgteHGTEGLS---RGLYGALIV 132
CuRO_1_Diphenol_Ox cd13857
The first cupredoxin domain of fungal laccase, diphenol oxidase; Diphenol oxidase belongs to ...
 132-238 2.92e-11

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: 61.51  E-value: 2.92e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949456009  132 YLGPIIRAEVNDVIKIHLKNFASRNYSIHPHGLFYkkdaEGALYPDNTSDALKKddSVPPGGSFTYSWevkprfapTTDD 211
Cdd:cd13857     28 FPGPLIEANQGDRIVVHVTNELDEPTSIHWHGLFQ----NGTNWMDGTAGITQC--PIPPGGSFTYNF--------TVDG 93

                           90       100
                   ....*....|....*....|....*..
gi 1949456009  212 ANCLTWvYHSHVNAPHdiASGLIGPLI 238
Cdd:cd13857     94 QYGTYW-YHSHYSTQY--ADGLVGPLI 117
CuRO_3_CopA cd13896
The third cupredoxin domain of CopA copper resistance protein family; CopA is a multicopper ...
 999-1092 9.23e-11

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: 59.96  E-value: 9.23e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949456009  999 GINGRVYGNLHGLVMQQNEKVdwyLLGMGNEVDM-HTVHFHAETFIYRTDLVHRG---DVVDLFPGTFATVEMVAANPGT 1074
Cdd:cd13896     18 TINGKAYPDADPLRVREGERV---RIVFVNDTMMaHPMHLHGHFFQVENGNGEYGprkDTVLVPPGETVSVDFDADNPGR 94

                           90
                   ....*....|....*...
gi 1949456009 1075 WLLHCHVSDHIHAGMETT 1092
Cdd:cd13896     95 WAFHCHNLYHMEAGMMRV 112
SufI COG2132
Multicopper oxidase with three cupredoxin domains (includes cell division protein FtsP and ...
 997-1097 6.75e-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: 62.64  E-value: 6.75e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949456009  997 MHGINGRVYGNLH-GLVMQQNEKVDWYLlgmGNEVDM-HTVHFHAETF----IYRTDLVHRG--DVVDLFPGTFATVEMV 1068
Cdd:COG2132    317 VWTINGKAFDPDRpDLTVKLGERERWTL---VNDTMMpHPFHLHGHQFqvlsRNGKPPPEGGwkDTVLVPPGETVRILFR 393

                           90       100       110
                   ....*....|....*....|....*....|
gi 1949456009 1069 AAN-PGTWLLHCHVSDHIHAGMETTYTIKE 1097
Cdd:COG2132    394 FDNyPGDWMFHCHILEHEDAGMMGQFEVVP 423
CuRO_D2_2dMcoN_like cd04202
The second cupredoxin domain of bacterial two domain multicopper oxidase McoN and similar ...
 953-1089 6.76e-10

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: 58.42  E-value: 6.76e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949456009  953 REFALLFlvydenQSWYledniknylgVHPDAFTPDEDFEESNlMHGINGRVYGNLHGLVMQQNEKVDWYLLGMGNEVdm 1032
Cdd:cd04202      2 RDYTLVL------QEWF----------VDPGTTPMPPEGMDFN-YFTINGKSFPATPPLVVKEGDRVRIRLINLSMDH-- 62

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1949456009 1033 HTVHFHAETF-IYRTDLV-------HRGDVVDLFPGTFATVEMVAANPGTWLLHCHVSDHIHAGM 1089
Cdd:cd04202     63 HPMHLHGHFFlVTATDGGpipgsapWPKDTLNVAPGERYDIEFVADNPGDWMFHCHKLHHAMNGM 127
CuRO_D1_2dMcoN_like cd13859
The first cupredoxin domain of bacterial two domain multicopper oxidase McoN and similar ...
 134-238 9.51e-10

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


Pssm-ID: 259928 [Multi-domain]  Cd Length: 122  Bit Score: 57.49  E-value: 9.51e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949456009  134 GPIIRAEVNDVIKIHLKNFASRNYSIHPHGLFYKKDAEGALYPDNTSDALKkddsvpPGGSFTYSWEVKPrfaPTTddan 213
Cdd:cd13859     31 GPLIHVKEGDDLVVHVTNNTTLPHTIHWHGVLQMGSWKMDGVPGVTQPAIE------PGESFTYKFKAER---PGT---- 97

                           90       100
                   ....*....|....*....|....*.
gi 1949456009  214 clTWvYHSHVNAP-HDIASGLIGPLI 238
Cdd:cd13859     98 --LW-YHCHVNVNeHVGMRGMWGPLI 120
CuRO_1_2DMCO_NIR_like cd11024
The cupredoxin domain 1 of a two-domain laccase related to nitrite reductase; The two-domain ...
 134-238 1.14e-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: 57.28  E-value: 1.14e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949456009  134 GPIIRAEVNDVIKIHLKNFASRNYSIHPHGLFY-KKDAEGAlypdntsdalkkdDSVPPGGSFTYSWEVKPrFApttdda 212
Cdd:cd11024     32 GPTLRATEGDLVRIHFINTGDHPHTIHFHGIHDaAMDGTGL-------------GPIMPGESFTYEFVAEP-AG------ 91

                           90       100
                   ....*....|....*....|....*...
gi 1949456009  213 nclTWVYHSHV--NAPHdIASGLIGPLI 238
Cdd:cd11024     92 ---THLYHCHVqpLKEH-IAMGLYGAFI 115
CuRO_1_CumA_like cd13861
The first cupredoxin domain of CumA like multicopper oxidase; This multicopper oxidase (MCO) ...
 492-595 1.17e-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: 57.24  E-value: 1.17e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949456009  492 GFLGPVLRVEEGDILNVTFLNKADRGYSIHPHGLNYDKRFQGTsyeDGIDKPGsnVEPGQRFTYSWQVlegPsssDAPci 571
Cdd:cd13861     28 QVPGPELRVRQGDTLRVRLTNRLPEPTTIHWHGLRLPNAMDGV---PGLTQPP--VPPGESFTYEFTP---P---DAG-- 94

                           90       100
                   ....*....|....*....|....
gi 1949456009  572 SYLYYSGTDPVKDTNSGLVGPLLV 595
Cdd:cd13861     95 TYWYHPHVGSQEQLDRGLYGPLIV 118
CuRO_3_CumA_like cd13906
The third cupredoxin domain of CumA like multicopper oxidase; This multicopper oxidase (MCO) ...
 1020-1096 1.46e-09

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


Pssm-ID: 259973 [Multi-domain]  Cd Length: 138  Bit Score: 57.39  E-value: 1.46e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949456009 1020 DWYLLGMGNEVD-MHTVHFHAETFIY------RTDLVHRGDVVDLFPGTFATVEMVAANPGTWLLHCHVSDHIHAGMETT 1092
Cdd:cd13906     55 RSYVLRLVNETAfLHPMHLHGHFFRVlsrngrPVPEPFWRDTVLLGPKETVDIAFVADNPGDWMFHCHILEHQETGMMGV 134


                   ....
gi 1949456009 1093 YTIK 1096
Cdd:cd13906    135 IRVA 138
CuRO_1_2DMCO_NIR_like_2 cd14449
The cupredoxin domain 1 of a two-domain laccase related to nitrite reductase; The two-domain ...
 134-238 3.93e-09

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


Pssm-ID: 259991 [Multi-domain]  Cd Length: 135  Bit Score: 56.12  E-value: 3.93e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949456009  134 GPIIRAEVNDVIKIHLKNFASRNYSIHPHGLFYKKDAEGALYPDNtsdalkkddSVPPGGSFTYSWEV---KPRFAPTTD 210
Cdd:cd14449     29 GPVIEVREGDTLKILFRNTLDVPASLHPHGVDYTTASDGTGMNAS---------IVAPGDTRIYTWRThggYRRADGSWA 99

                           90       100       110
                   ....*....|....*....|....*....|..
gi 1949456009  211 DANCLTWVYHSHV----NAPHDIASGLIGPLI 238
Cdd:cd14449    100 EGTAGYWHYHDHVfgteHGTEGLSRGLYGALI 131
CuRO_1_Diphenol_Ox cd13857
The first cupredoxin domain of fungal laccase, diphenol oxidase; Diphenol oxidase belongs to ...
 493-595 5.29e-09

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


Pssm-ID: 259926 [Multi-domain]  Cd Length: 119  Bit Score: 55.34  E-value: 5.29e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949456009  493 FLGPVLRVEEGDILNVTFLNKADRGYSIHPHGLnydkRFQGTSYEDGIdkPGSN---VEPGQRFTYSWQVlegpsssDAP 569
Cdd:cd13857     28 FPGPLIEANQGDRIVVHVTNELDEPTSIHWHGL----FQNGTNWMDGT--AGITqcpIPPGGSFTYNFTV-------DGQ 94

                           90       100       110
                   ....*....|....*....|....*....|.
gi 1949456009  570 CISYLYYS-----GTDpvkdtnsGLVGPLLV 595
Cdd:cd13857     95 YGTYWYHShystqYAD-------GLVGPLIV 118
CuRO_1_2DMCO_NIR_like cd11024
The cupredoxin domain 1 of a two-domain laccase related to nitrite reductase; The two-domain ...
 495-557 5.40e-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: 5.40e-09
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1949456009  495 GPVLRVEEGDILNVTFLNKADRGYSIHPHGLNYDKRfQGTSYEDgidkpgsnVEPGQRFTYSW 557
Cdd:cd11024     32 GPTLRATEGDLVRIHFINTGDHPHTIHFHGIHDAAM-DGTGLGP--------IMPGESFTYEF 85
CuRO_3_Fet3p cd13899
The third Cupredoxin domain of multicopper oxidase Fet3p; Fet3p catalyzes the ferroxidase ...
 998-1089 1.00e-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: 55.72  E-value: 1.00e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949456009  998 HGINGRVYG-NLHGLVMQQNEKVDwylLGMGNEvDM--HTVHFHAETF--IYRTDLVH----------------RGDVVD 1056
Cdd:cd13899     44 DALDPAIYGpQTNAFVLNHGEVVE---LVVNNW-DAgkHPFHLHGHKFqvVQRSPDVAsddpnppinefpenpmRRDTVM 119

                           90       100       110
                   ....*....|....*....|....*....|...
gi 1949456009 1057 LFPGTFATVEMVAANPGTWLLHCHVSDHIHAGM 1089
Cdd:cd13899    120 VPPGGSVVIRFRADNPGVWFFHCHIEWHLEAGL 152
CuRO_1_2dMco_1 cd13860
The first cupredoxin domain of bacteria two domain multicopper oxidase; This subfamily ...
 134-238 1.11e-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: 54.12  E-value: 1.11e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949456009  134 GPIIRAEVNDVIKIHLKNFASRNYSIHPHGLFYKKDAEGAlyPDNTSDAlkkddsVPPGGSFTYSWEVKPRFapttddan 213
Cdd:cd13860     31 GPTIEVTEGDRVRILVTNELPEPTTVHWHGLPVPNGMDGV--PGITQPP------IQPGETFTYEFTAKQAG-------- 94

                           90       100
                   ....*....|....*....|....*
gi 1949456009  214 clTWVYHSHVNAPHDIASGLIGPLI 238
Cdd:cd13860     95 --TYMYHSHVDEAKQEDMGLYGAFI 117
Cu-oxidase_3 pfam07732
Multicopper oxidase; This entry contains many divergent copper oxidase-like domains that are ...
 493-559 1.41e-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: 1.41e-08
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949456009  493 FLGPVLRVEEGDILNVTFLNKADRGYSIHPHGLnydkrFQ-GTSYEDGIDKpGSN--VEPGQRFTYSWQV 559
Cdd:pfam07732   24 FPGPTIRVREGDTVVVNVTNNLDEPTSIHWHGL-----QQrGTPWMDGVPG-VTQcpIPPGQSFTYRFQV 87
CuRO_3_McoC_like cd13902
The third cupredoxin domain of a multicopper oxidase McoC and similar proteins; This family ...
 995-1089 1.64e-08

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


Pssm-ID: 259969 [Multi-domain]  Cd Length: 125  Bit Score: 53.94  E-value: 1.64e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949456009  995 NLMHGINGRVYG-NLHGLVMQQNEKVDWYLLgmgNEVDM-HTVHFHAETF--IYRTDLVHRG------DVVDLFPGTFAT 1064
Cdd:cd13902     18 GMMFLINGKTFDmNRIDFVAKVGEVEVWEVT---NTSHMdHPFHLHGTQFqvLEIDGNPQKPeyrawkDTVNLPPGEAVR 94

                           90       100
                   ....*....|....*....|....*
gi 1949456009 1065 VEMVAANPGTWLLHCHVSDHIHAGM 1089
Cdd:cd13902     95 IATRQDDPGMWMYHCHILEHEDAGM 119
SufI COG2132
Multicopper oxidase with three cupredoxin domains (includes cell division protein FtsP and ...
 132-238 1.79e-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: 58.02  E-value: 1.79e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949456009  132 YLGPIIRAEVNDVIKIHLKNFASRNYSIHPHGLFykkdaegalyPDNTSD--AlkkDDSVPPGGSFTYSWEVkprfaptt 209
Cdd:COG2132     42 YPGPTIRVREGDRVRVRVTNRLPEPTTVHWHGLR----------VPNAMDgvP---GDPIAPGETFTYEFPV-------- 100

                           90       100       110
                   ....*....|....*....|....*....|..
gi 1949456009  210 DDANCLTWvYHSHVN---APHdIASGLIGPLI 238
Cdd:COG2132    101 PQPAGTYW-YHPHTHgstAEQ-VYRGLAGALI 130
CuRO_1_Fet3p cd13851
The first Cupredoxin domain of multicopper oxidase Fet3P; Fet3p catalyzes the ferroxidase ...
 135-238 1.66e-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: 51.11  E-value: 1.66e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949456009  135 PIIRAEVNDVIKIHLKN-FASRNYSIHPHGLFYKkdaeGALYPDNTSDALKKDdsVPPGGSFTYSWevkprfapTTDDAN 213
Cdd:cd13851     32 PPIEVNKGDTVVIHATNsLGDQPTSLHFHGLFQN----GTNYMDGPVGVTQCP--IPPGQSFTYEF--------TVDTQV 97

                           90       100
                   ....*....|....*....|....*
gi 1949456009  214 CLTWvYHSHVNAPHdiASGLIGPLI 238
Cdd:cd13851     98 GTYW-YHSHDGGQY--PDGLRGPFI 119
CuRO_3_MCO_like_2 cd13908
The third cupredoxin domain of uncharacterized multicopper oxidase; Multicopper Oxidases (MCOs) ...
 1000-1088 2.08e-07

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


Pssm-ID: 259975 [Multi-domain]  Cd Length: 122  Bit Score: 50.91  E-value: 2.08e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949456009 1000 INGRVYGNLHG-LVMQQNEKvdwYLLGMGNEV-DMHTVHFHAETF----IYRTDLVH-RGDVVDLFPGTFATVEMVAANP 1072
Cdd:cd13908     23 INGKSYPDEDPpLVVQQGRR---YRLVFRNASdDAHPMHLHRHTFevtrIDGKPTSGlRKDVVMLGGYQRVEVDFVADNP 99

                           90
                   ....*....|....*.
gi 1949456009 1073 GTWLLHCHVSDHIHAG 1088
Cdd:cd13908    100 GLTLFHCHQQLHMDYG 115
CuRO_3_MaLCC_like cd13901
The third cupredoxin domain of the fungal laccases similar to Ma-LCC from Melanocarpus ...
 958-1089 2.11e-07

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: 51.84  E-value: 2.11e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949456009  958 LFLVYDENQS-WYLEDN--------------IKNYLGV-HPdaftpdedfeesnlMHgingrvygnLHGLvmqqnekvDW 1021
Cdd:cd13901     42 LLLVADGNTStFPPEWNvielpkankwvyivIQNNSPLpHP--------------IH---------LHGH--------DF 90

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1949456009 1022 YLLGMGnevdmhTVHFHAETFIYRTDLVHRGDVVDLFPGTFATVEMVAANPGTWLLHCHVSDHIHAGM 1089
Cdd:cd13901     91 YILAQG------TGTFDDDGTILNLNNPPRRDVAMLPAGGYLVIAFKTDNPGAWLMHCHIAWHASGGL 152
CuRO_1_2dMco_1 cd13860
The first cupredoxin domain of bacteria two domain multicopper oxidase; This subfamily ...
 495-595 9.59e-07

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


Pssm-ID: 259929 [Multi-domain]  Cd Length: 119  Bit Score: 48.73  E-value: 9.59e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949456009  495 GPVLRVEEGDILNVTFLNKADRGYSIHPHGLNYDKRFqgtsyeDGIdkPGSN---VEPGQRFTYSWQV-LEGpsssdapc 570
Cdd:cd13860     31 GPTIEVTEGDRVRILVTNELPEPTTVHWHGLPVPNGM------DGV--PGITqppIQPGETFTYEFTAkQAG-------- 94

                           90       100
                   ....*....|....*....|....*
gi 1949456009  571 iSYLYYSGTDPVKDTNSGLVGPLLV 595
Cdd:cd13860     95 -TYMYHSHVDEAKQEDMGLYGAFIV 118
SufI COG2132
Multicopper oxidase with three cupredoxin domains (includes cell division protein FtsP and ...
 493-595 1.32e-06

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: 52.24  E-value: 1.32e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949456009  493 FLGPVLRVEEGDILNVTFLNKADRGYSIHPHGLNydkrfqgTSYE-DGIdkPGSNVEPGQRFTYSWQVLEGPSssdapci 571
Cdd:COG2132     42 YPGPTIRVREGDRVRVRVTNRLPEPTTVHWHGLR-------VPNAmDGV--PGDPIAPGETFTYEFPVPQPAG------- 105

                           90       100
                   ....*....|....*....|....*.
gi 1949456009  572 SYLYYSGTDPVKDTN--SGLVGPLLV 595
Cdd:COG2132    106 TYWYHPHTHGSTAEQvyRGLAGALIV 131
CuRO_3_MCO_like_3 cd13909
The third cupredoxin domain of uncharacterized multicopper oxidase; Multicopper Oxidases (MCOs) ...
 1032-1091 1.63e-06

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: 48.67  E-value: 1.63e-06
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949456009 1032 MHTVHFHAETFIYRTDLVHrgDVVDLFPGTFATVEMVAANPGTWLLHCHVSDHIHAGMET 1091
Cdd:cd13909     75 LHGHHFRAILPNGALGPWR--DTLLMDRGETREIAFVADNPGDWLLHCHMLEHAAAGMMS 132
CuRO_1_Abr2_like cd13850
The first cupredoxin domain of a group of fungal Laccases similar to Abr2 from Aspergillus ...
 493-559 2.21e-06

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: 47.68  E-value: 2.21e-06
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949456009  493 FLGPVLRVEEGDILNVTFLNKADRGYSIHPHGLnydkRFQGTSYEDGIdkPG---SNVEPGQRFTYSWQV 559
Cdd:cd13850     26 FPGPPIILDEGDEVEILVTNNLPVNTTIHFHGI----LQRGTPWSDGV--PGvtqWPIQPGGSFTYRWKA 89
CuRO_1_AAO cd13845
The first cupredoxin domain of plant Ascorbate oxidase; Ascorbate oxidase catalyzes the ...
 131-238 4.41e-06

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


Pssm-ID: 259914 [Multi-domain]  Cd Length: 120  Bit Score: 47.06  E-value: 4.41e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949456009  131 GYLGPIIRAEVNDVIKIHLKN-FASRNYSIHPHGLFYKkdaeGALYPDNTSDALKKddSVPPGGSFTYSWEVkprfaptt 209
Cdd:cd13845     27 QFPGPTIRATAGDTIVVELENkLPTEGVAIHWHGIRQR----GTPWADGTASVSQC--PINPGETFTYQFVV-------- 92

                           90       100
                   ....*....|....*....|....*....
gi 1949456009  210 DDANclTWVYHSHVNAPHdiASGLIGPLI 238
Cdd:cd13845     93 DRPG--TYFYHGHYGMQR--SAGLYGSLI 117
CuRO_1_MaLCC_like cd13854
The first cupredoxin domain of the fungal laccases similar to Ma-LCC from Melanocarpus ...
 132-238 5.20e-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: 46.85  E-value: 5.20e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949456009  132 YLGPIIRAEVNDVIKIHLKNFASRN-YSIHPHGL--FYKKDAEGAlyPDNTSDAlkkddsVPPGGSFTYSWEVkprfapt 208
Cdd:cd13854     31 YPGPLIEANWGDTIEVTVINKLQDNgTSIHWHGIrqLNTNWQDGV--PGVTECP------IAPGDTRTYRFRA------- 95

                           90       100       110
                   ....*....|....*....|....*....|
gi 1949456009  209 tdDANCLTWvYHSHVNAPHdiASGLIGPLI 238
Cdd:cd13854     96 --TQYGTSW-YHSHYSAQY--GDGVVGPIV 120
CuRO_1_Abr2_like cd13850
The first cupredoxin domain of a group of fungal Laccases similar to Abr2 from Aspergillus ...
 124-237 6.60e-06

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: 46.14  E-value: 6.60e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949456009  124 APREEWLG---YLGPIIRAEVNDVIKIHLKNFASRNYSIHPHGLFYKKDAEGALYPDNTSDALkkddsvPPGGSFTYSWe 200
Cdd:cd13850     15 GEREVILIngqFPGPPIILDEGDEVEILVTNNLPVNTTIHFHGILQRGTPWSDGVPGVTQWPI------QPGGSFTYRW- 87

                           90       100       110
                   ....*....|....*....|....*....|....*..
gi 1949456009  201 vkprfapTTDDANCLTWvYHSHVNAphDIASGLIGPL 237
Cdd:cd13850     88 -------KAEDQYGLYW-YHSHYRG--YYMDGLYGPI 114
CuRO_1_2DMCO_NIR_like cd11024
The cupredoxin domain 1 of a two-domain laccase related to nitrite reductase; The two-domain ...
 1033-1098 7.10e-06

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


Pssm-ID: 259910 [Multi-domain]  Cd Length: 119  Bit Score: 46.11  E-value: 7.10e-06
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1949456009 1033 HTVHFHaetfiyrtdLVHR----GDVV-DLFPGTFATVEMVAANPGTWLLHCHV---SDHIHAGMETTYTIKEK 1098
Cdd:cd11024     55 HTIHFH---------GIHDaamdGTGLgPIMPGESFTYEFVAEPAGTHLYHCHVqplKEHIAMGLYGAFIVDPK 119
CuRO_1_MaLCC_like cd13854
The first cupredoxin domain of the fungal laccases similar to Ma-LCC from Melanocarpus ...
 495-558 9.21e-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: 46.08  E-value: 9.21e-06
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1949456009  495 GPVLRVEEGDILNVTFLNK-ADRGYSIHPHGLnydkRFQGTSYEDGIdkPGSN---VEPGQRFTYSWQ 558
Cdd:cd13854     33 GPLIEANWGDTIEVTVINKlQDNGTSIHWHGI----RQLNTNWQDGV--PGVTecpIAPGDTRTYRFR 94
CuRO_3_AAO cd13893
The third cupredoxin domain of plant Ascorbate oxidase; Ascorbate oxidase catalyzes the ...
 1053-1089 1.13e-05

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


Pssm-ID: 259960 [Multi-domain]  Cd Length: 155  Bit Score: 46.64  E-value: 1.13e-05
                           10        20        30
                   ....*....|....*....|....*....|....*..
gi 1949456009 1053 DVVDLFPGTFATVEMVAANPGTWLLHCHVSDHIHAGM 1089
Cdd:cd13893    104 NTVTIFPYGWTALRFKADNPGVWAFHCHIEWHFHMGM 140
CuRO_1_AAO cd13845
The first cupredoxin domain of plant Ascorbate oxidase; Ascorbate oxidase catalyzes the ...
 470-595 1.49e-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: 1.49e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949456009  470 KVLYRAYTDSTFSKVITSpSHHGFLGPVLRVEEGDILNVTFLNK-ADRGYSIHPHGLnydkRFQGTSYEDGIDKPGS-NV 547
Cdd:cd13845      6 KVEYMFWAPDCVEKLVIG-INGQFPGPTIRATAGDTIVVELENKlPTEGVAIHWHGI----RQRGTPWADGTASVSQcPI 80

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*...
gi 1949456009  548 EPGQRFTYSWQVlegpsssDAPCiSYLYYSGTDPVKdtNSGLVGPLLV 595
Cdd:cd13845     81 NPGETFTYQFVV-------DRPG-TYFYHGHYGMQR--SAGLYGSLIV 118
CuRO_1_Tv-LCC_like cd13856
The first cupredoxin domain of fungal laccases similar to Tv-LCC from Trametes versicolor; ...
 132-238 1.51e-05

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


Pssm-ID: 259925 [Multi-domain]  Cd Length: 125  Bit Score: 45.41  E-value: 1.51e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949456009  132 YLGPIIRAEVNDVIKIHLKNFAS-----RNYSIHPHGLFYKKDAegalYPDNTSDALKKddSVPPGGSFTYSWevkprfa 206
Cdd:cd13856     28 FPGPLITANKGDTFRITVVNQLTdptmrRSTSIHWHGIFQHGTN----YADGPAFVTQC--PIAPNHSFTYDF------- 94

                           90       100       110
                   ....*....|....*....|....*....|..
gi 1949456009  207 PTTDDANclTWVYHSHVNAPHdiASGLIGPLI 238
Cdd:cd13856     95 TAGDQAG--TFWYHSHLSTQY--CDGLRGPLV 122
CuRO_3_Tv-LCC_like cd13903
The third cupredoxin domain of the fungal laccases similar to Tv-LCC from Trametes Versicolor; ...
 1051-1089 1.58e-05

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: 46.12  E-value: 1.58e-05
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|
gi 1949456009 1051 RGDVVDL-FPGTFATVEMVAANPGTWLLHCHVSDHIHAGM 1089
Cdd:cd13903    100 RRDVVSVgTPGDGVTIRFVTDNPGPWFLHCHIDWHLEAGL 139
CuRO_1_CuNIR cd11020
Cupredoxin domain 1 of Copper-containing nitrite reductase; Copper-containing nitrite ...
 495-582 1.61e-05

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


Pssm-ID: 259906 [Multi-domain]  Cd Length: 119  Bit Score: 45.28  E-value: 1.61e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949456009  495 GPVLRVEEGDILNVTFLNKADRGYsihPHGLNYDkrfqgTSYEDGiDKPGSNVEPGQRFTYSWQVLEgpsssdaPCIsYL 574
Cdd:cd11020     32 GPVIRVREGDTVELTLTNPGTNTM---PHSIDFH-----AATGPG-GGEFTTIAPGETKTFSFKALY-------PGV-FM 94


                   ....*...
gi 1949456009  575 YYSGTDPV 582
Cdd:cd11020     95 YHCATAPV 102
CuRO_1_CuNIR cd11020
Cupredoxin domain 1 of Copper-containing nitrite reductase; Copper-containing nitrite ...
 114-238 2.51e-05

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


Pssm-ID: 259906 [Multi-domain]  Cd Length: 119  Bit Score: 44.51  E-value: 2.51e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949456009  114 EYTDATFSHQAPreewlgylGPIIRAEVNDVIKIHLKNFASRNYsihPHGLfykkDAEGAlypdnTSDALKKDDSVPPGG 193
Cdd:cd11020     20 TYTAWTFNGQVP--------GPVIRVREGDTVELTLTNPGTNTM---PHSI----DFHAA-----TGPGGGEFTTIAPGE 79

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*.
gi 1949456009  194 SFTYSWevKPRFAPttddanclTWVYH-SHVNAPHDIASGLIGPLI 238
Cdd:cd11020     80 TKTFSF--KALYPG--------VFMYHcATAPVLMHIANGMYGAII 115
CuRO_1_Fet3p cd13851
The first Cupredoxin domain of multicopper oxidase Fet3P; Fet3p catalyzes the ferroxidase ...
 496-559 2.80e-05

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


Pssm-ID: 259920 [Multi-domain]  Cd Length: 121  Bit Score: 44.57  E-value: 2.80e-05
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1949456009  496 PVLRVEEGDILNVTFLNK-ADRGYSIHPHGLnydkrFQ-GTSYEDGidKPGSN---VEPGQRFTYSWQV 559
Cdd:cd13851     32 PPIEVNKGDTVVIHATNSlGDQPTSLHFHGL-----FQnGTNYMDG--PVGVTqcpIPPGQSFTYEFTV 93
CuRO_3_LCC_plant cd13897
The third cupredoxin domain of the plant laccases; Laccase is a blue multicopper oxidase (MCO) ...
 1059-1097 2.87e-05

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


Pssm-ID: 259964 [Multi-domain]  Cd Length: 139  Bit Score: 44.94  E-value: 2.87e-05
                           10        20        30
                   ....*....|....*....|....*....|....*....
gi 1949456009 1059 PGTFATVEMVAANPGTWLLHCHVSDHIHAGMETTYTIKE 1097
Cdd:cd13897    100 RGGWAAIRFVADNPGVWFMHCHFERHTSWGMATVFIVKN 138
PLN02191 PLN02191
L-ascorbate oxidase
 980-1093 3.62e-05

L-ascorbate oxidase


Pssm-ID: 177843 [Multi-domain]  Cd Length: 574  Bit Score: 47.70  E-value: 3.62e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949456009  980 VHPDAFTPDEDFEESNLMHGINGRVYG-NLHGLvmqqnekvDWYLLGMGNE-----VDMHTVHFHAETFiyrtdlvhRGD 1053
Cdd:PLN02191   442 VFPFNVTVDVIIQNANVLKGVVSEIHPwHLHGH--------DFWVLGYGDGkfkpgIDEKTYNLKNPPL--------RNT 505

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|
gi 1949456009 1054 VVdLFPGTFATVEMVAANPGTWLLHCHVSDHIHAGMETTY 1093
Cdd:PLN02191   506 AI-LYPYGWTAIRFVTDNPGVWFFHCHIEPHLHMGMGVVF 544
CuRO_1_McoC_like cd13855
The first cupredoxin domain of a multicopper oxidase McoC and similar proteins; This family ...
 495-562 4.04e-05

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


Pssm-ID: 259924 [Multi-domain]  Cd Length: 121  Bit Score: 44.00  E-value: 4.04e-05
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1949456009  495 GPVLRVEEGDILNVTFLNKADRGYSIHPHGLNYDKRFQGTsyedgidkPGSNVEPGQRFTYSWQVLEG 562
Cdd:cd13855     32 GPLIEVFEGDTVEITFRNRLPEPTTVHWHGLPVPPDQDGN--------PHDPVAPGNDRVYRFTLPQD 91
CuRO_1_McoP_like cd13852
The first cupredoxin domain of multicopper oxidase McoP and similar proteins; This family ...
 492-560 4.75e-05

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: 43.82  E-value: 4.75e-05
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1949456009  492 GFLGPVLRVEEGDILNVTFLNKADRGYSIHPHGLNYDKRFQGtsyedgidKPGSNVEPGQRFTYSWQVL 560
Cdd:cd13852     21 SYLGPILRLRKGQKVRITFKNNLPEPTIIHWHGLHVPAAMDG--------HPRYAIDPGETYVYEFEVL 81
Cupredoxin cd00920
Cupredoxin superfamily; Cupredoxins contain type I copper centers and are involved in ...
 1001-1092 5.36e-05

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: 43.37  E-value: 5.36e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949456009 1001 NGRVYGNLHgLVMQQNEKVDWYL---LGMGNEVDMHT--VHFHAETFIYRTDLVHrgdVVDLFPGTFATVEMVAANPGTW 1075
Cdd:cd00920     16 GVLLFGPPV-LVVPVGDTVRVQFvnkLGENHSVTIAGfgVPVVAMAGGANPGLVN---TLVIGPGESAEVTFTTDQAGVY 91

                           90
                   ....*....|....*..
gi 1949456009 1076 LLHCHVSDHIHAGMETT 1092
Cdd:cd00920     92 WFYCTIPGHNHAGMVGT 108
CuRO_1_McoC_like cd13855
The first cupredoxin domain of a multicopper oxidase McoC and similar proteins; This family ...
 134-238 6.30e-05

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


Pssm-ID: 259924 [Multi-domain]  Cd Length: 121  Bit Score: 43.62  E-value: 6.30e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949456009  134 GPIIRAEVNDVIKIHLKNFASRNYSIHPHGLFYKKDAEGalypdNTSDAlkkddsVPPGGSFTYSWEVKPRFAPTtddan 213
Cdd:cd13855     32 GPLIEVFEGDTVEITFRNRLPEPTTVHWHGLPVPPDQDG-----NPHDP------VAPGNDRVYRFTLPQDSAGT----- 95

                           90       100       110
                   ....*....|....*....|....*....|
gi 1949456009  214 clTWvYHSHvnaPHDIAS-----GLIGPLI 238
Cdd:cd13855     96 --YW-YHPH---PHGHTAeqvyrGLAGAFV 119
Cupredoxin cd00920
Cupredoxin superfamily; Cupredoxins contain type I copper centers and are involved in ...
 484-560 8.62e-05

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: 42.99  E-value: 8.62e-05
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1949456009  484 VITSPSHHGFLGPVLRVEEGDILNVTFLNKADRGYSIHPHGLNYDKRFQGTSYeDGIDKPGSNVEPGQRFTYSWQVL 560
Cdd:cd00920     11 SFTYNGVLLFGPPVLVVPVGDTVRVQFVNKLGENHSVTIAGFGVPVVAMAGGA-NPGLVNTLVIGPGESAEVTFTTD 86
CuRO_1_CueO_FtsP cd04232
The first Cupredoxin domain of the multicopper oxidase CueO, the cell division protein FtsP, ...
 132-238 1.09e-04

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


Pssm-ID: 259894 [Multi-domain]  Cd Length: 120  Bit Score: 42.95  E-value: 1.09e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949456009  132 YLGPIIRAEVNDVIKIHLKNFASRNYSIHPHGLFYKKDAEGAlyPDNTsdalkkddsVPPGGsftySWevKPRFAPTTDD 211
Cdd:cd04232     29 YLGPTIRVKKGDTVRINVTNNLDEETTVHWHGLHVPGEMDGG--PHQP---------IAPGQ----TW--SPTFTIDQPA 91

                           90       100       110
                   ....*....|....*....|....*....|
gi 1949456009  212 ANCltWvYHSHV---NAPHdIASGLIGPLI 238
Cdd:cd04232     92 ATL--W-YHPHThgkTAEQ-VYRGLAGLFI 117
CuRO_3_LCC_like cd04207
Cupredoxin domain 3 of laccase-like multicopper oxidases; including laccase, CueO, spore coat ...
 332-401 1.15e-04

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: 43.22  E-value: 1.15e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949456009  332 WHLFGMGNEVDIHSAFFHGNT--LLNRGH-------------RTDTISLFPATFVTATMVPKVKGKWLLSCQVNDHLQAG 396
Cdd:cd04207     47 IVLINAGNHDMQHPFHLHGHSfwVLGSGGgpfdaplnltnppWRDTVLVPPGGWVVIRFKADNPGVWMLHCHILEHEDAG 126


                   ....*
gi 1949456009  397 MQAFY 401
Cdd:cd04207    127 MMTVF 131
CuRO_1_CuNIR_like cd04201
Cupredoxin domain 1 of Copper-containing nitrite reductase and two-domain laccase; ...
 495-595 1.49e-04

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


Pssm-ID: 259864 [Multi-domain]  Cd Length: 120  Bit Score: 42.48  E-value: 1.49e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949456009  495 GPVLRVEEGDILNVTFLNKADrgySIHPHGLNydkrFQGTSYEDGiDKPGSNVEPGQRFTYSWQVLegpsssdaPCISYL 574
Cdd:cd04201     32 GPMLRVREGDTVELHFSNNPS---STMPHNID----FHAATGAGG-GAGATFIAPGETSTFSFKAT--------QPGLYV 95

                           90       100
                   ....*....|....*....|..
gi 1949456009  575 YYSGTDPVK-DTNSGLVGPLLV 595
Cdd:cd04201     96 YHCAVAPVPmHIANGMYGLILV 117
CuRO_1_CopA cd13848
The first cupredoxin domain of CopA copper resistance protein family; CopA is a multicopper ...
 495-559 1.54e-04

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


Pssm-ID: 259917 [Multi-domain]  Cd Length: 116  Bit Score: 42.27  E-value: 1.54e-04
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1949456009  495 GPVLRVEEGDILNVTFLNKADRGYSIHPHGLNYDKRFQGTsyeDGIDKPGsnVEPGQRFTYSWQV 559
Cdd:cd13848     30 GPLLRFKEGDDATIRVHNRLDEDTSIHWHGLLLPNDMDGV---PGLSFPG--IKPGETFTYRFPV 89
CuRO_3_tcLLC2_insect_like cd13905
The third cupredoxin domain of the insect laccases similar to laccase 2 in Tribolium castaneum; ...
 1063-1103 2.34e-04

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


Pssm-ID: 259972 [Multi-domain]  Cd Length: 174  Bit Score: 43.05  E-value: 2.34e-04
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|.
gi 1949456009 1063 ATVEMVAANPGTWLLHCHVSDHIHAGMETTYTIKEKSLPAP 1103
Cdd:cd13905    133 VVIRFRADNPGYWLLHCHIEFHLLEGMALVLKVGEPSDPPP 173
CuRO_1_McoP_like cd13852
The first cupredoxin domain of multicopper oxidase McoP and similar proteins; This family ...
 131-227 2.85e-04

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: 41.50  E-value: 2.85e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949456009  131 GYLGPIIRAEVNDVIKIHLKNFASRNYSIHPHGLFYKKDAEGalYPDNTsdalkkddsVPPGGSFTYSWEVKPRFApttd 210
Cdd:cd13852     21 SYLGPILRLRKGQKVRITFKNNLPEPTIIHWHGLHVPAAMDG--HPRYA---------IDPGETYVYEFEVLNRAG---- 85

                           90
                   ....*....|....*..
gi 1949456009  211 danclTWVYHSHvnaPH 227
Cdd:cd13852     86 -----TYWYHPH---PH 94
CuRO_D1_2dMcoN_like cd13859
The first cupredoxin domain of bacterial two domain multicopper oxidase McoN and similar ...
 495-559 3.83e-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: 3.83e-04
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1949456009  495 GPVLRVEEGDILNVTFLNKADRGYSIHPHGLnydkrFQ-GTSYEDGIdkPGSN---VEPGQRFTYSWQV 559
Cdd:cd13859     31 GPLIHVKEGDDLVVHVTNNTTLPHTIHWHGV-----LQmGSWKMDGV--PGVTqpaIEPGESFTYKFKA 92
ascorbase TIGR03388
L-ascorbate oxidase, plant type; Members of this protein family are the copper-containing ...
 994-1089 3.97e-04

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: 44.36  E-value: 3.97e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949456009  994 SNLMHGINGRVYG-NLHGLvmqqnekvDWYLLGMGN---EVDMHTVHFHAETFIYRtdlvhrgDVVDLFPGTFATVEMVA 1069
Cdd:TIGR03388  433 ANTLNGNNSETHPwHLHGH--------DFWVLGYGEgkfRPGVDEKSYNLKNPPLR-------NTVVIFPYGWTALRFVA 497

                           90       100
                   ....*....|....*....|
gi 1949456009 1070 ANPGTWLLHCHVSDHIHAGM 1089
Cdd:TIGR03388  498 DNPGVWAFHCHIEPHLHMGM 517
CuRO_1_Tth-MCO_like cd13853
The first cupredoxin domain of the bacterial laccases similar to Tth-MCO from Thermus ...
 463-559 5.41e-04

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: 41.47  E-value: 5.41e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949456009  463 RIGGKYVKVlyRAYTDStfskvitspshhgFLGPVLRVEEGDILNVTFLNKADRGYS-----------------IHPHGL 525
Cdd:cd13853     14 TLAGLPVTL--RTYNGS-------------IPGPTLRVRPGDTLRITLKNDLPPEGAaneapapntphcpnttnLHFHGL 78

                           90       100       110
                   ....*....|....*....|....*....|....
gi 1949456009  526 NydkrfqgTSYEDGIDKPGSNVEPGQRFTYSWQV 559
Cdd:cd13853     79 H-------VSPTGNSDNVFLTIAPGESFTYEYDI 105
Cu-oxidase_3 pfam07732
Multicopper oxidase; This entry contains many divergent copper oxidase-like domains that are ...
 833-932 7.35e-04

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: 40.31  E-value: 7.35e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949456009  833 KTRPDHWGI----LGPIIHAEVGEQILIIFKNKASRPYSITAHGVKASG----------SHVPVEPGRIIELTWDIPESS 898
Cdd:pfam07732   12 GTRQAVIGVngqfPGPTIRVREGDTVVVNVTNNLDEPTSIHWHGLQQRGtpwmdgvpgvTQCPIPPGQSFTYRFQVKQQA 91

                           90       100       110
                   ....*....|....*....|....*....|....*
gi 1949456009  899 GpgtselnciSYVYFSSvdyIKDLY-SGLLGPLVI 932
Cdd:pfam07732   92 G---------TYWYHSH---TSGQQaAGLAGAIII 114
laccase TIGR03389
laccase, plant; Members of this protein family include the copper-containing enzyme laccase ...
 1060-1105 7.68e-04

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


Pssm-ID: 274556 [Multi-domain]  Cd Length: 539  Bit Score: 43.57  E-value: 7.68e-04
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|.
gi 1949456009 1060 GTFATVEMVAANPGTWLLHCHVSDHIHAGMETTYTIK-----EKSLPAPAS 1105
Cdd:TIGR03389  484 GGWAAIRFVADNPGVWFMHCHLEVHTTWGLKMAFLVDngkgpNQSLLPPPS 534
CuRO_1_LCC_like cd04206
Cupredoxin domain 1 of laccase-like multicopper oxidases; including laccase, CueO, spore coat ...
 840-933 7.95e-04

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: 40.35  E-value: 7.95e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949456009  840 GILGPIIHAEVGEQILIIFKNK-ASRPYSITAHGVK----------ASGSHVPVEPGRIIELTWDIPESsgPGTselnci 908
Cdd:cd04206     27 QFPGPTIRVKEGDTVEVTVTNNlPNEPTSIHWHGLRqpgtndgdgvAGLTQCPIPPGESFTYRFTVDDQ--AGT------ 98

                           90       100
                   ....*....|....*....|....*
gi 1949456009  909 sYVYFSSVDYikDLYSGLLGPLVIC 933
Cdd:cd04206     99 -FWYHSHVGG--QRADGLYGPLIVE 120
CuRO_1_CueO_FtsP cd04232
The first Cupredoxin domain of the multicopper oxidase CueO, the cell division protein FtsP, ...
 493-559 8.19e-04

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


Pssm-ID: 259894 [Multi-domain]  Cd Length: 120  Bit Score: 40.25  E-value: 8.19e-04
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1949456009  493 FLGPVLRVEEGDILNVTFLNKADRGYSIHPHGLnydkrfQGTSYEDGidKPGSNVEPGQRFTYSWQV 559
Cdd:cd04232     29 YLGPTIRVKKGDTVRINVTNNLDEETTVHWHGL------HVPGEMDG--GPHQPIAPGQTWSPTFTI 87
CuRO_1_Tv-LCC_like cd13856
The first cupredoxin domain of fungal laccases similar to Tv-LCC from Trametes versicolor; ...
 493-559 8.47e-04

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


Pssm-ID: 259925 [Multi-domain]  Cd Length: 125  Bit Score: 40.40  E-value: 8.47e-04
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1949456009  493 FLGPVLRVEEGDILNVTFLNK-----ADRGYSIHPHGLnydkrFQ-GTSYEDGIDK----PgsnVEPGQRFTYSWQV 559
Cdd:cd13856     28 FPGPLITANKGDTFRITVVNQltdptMRRSTSIHWHGI-----FQhGTNYADGPAFvtqcP---IAPNHSFTYDFTA 96
CuRO_1_MCO_like_1 cd13862
The first cupredoxin domain of uncharacterized multicopper oxidase; Multicopper Oxidases (MCOs) ...
 134-238 9.79e-04

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


Pssm-ID: 259931 [Multi-domain]  Cd Length: 123  Bit Score: 40.19  E-value: 9.79e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949456009  134 GPIIRAEVNDVIKIHLKNFASRNYSIHPHGLFYKKDAEGALyPDNTSdalkkddSVPPGGSFTYSweVKPRFAPTtddan 213
Cdd:cd13862     31 GPLLRMRQGVSVTVDVFNDTDIPEYVHWHGLPLPADVDGAM-EEGTP-------SVPPHGHRRYR--MTPRPAGF----- 95

                           90       100
                   ....*....|....*....|....*....
gi 1949456009  214 clTWvYHSHVNAPHDIA----SGLIGPLI 238
Cdd:cd13862     96 --RW-YHTHVMTMDDLTrgqySGLFGFVY 121
CuRO_1_CuNIR cd11020
Cupredoxin domain 1 of Copper-containing nitrite reductase; Copper-containing nitrite ...
 1001-1089 1.10e-03

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


Pssm-ID: 259906 [Multi-domain]  Cd Length: 119  Bit Score: 39.89  E-value: 1.10e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949456009 1001 NGRVYGNLhgLVMQQNEKVDWYLLGMGNEVDMHTVHFHAETfiyrTDLVhrGDVVDLFPGTFATVEMVAANPGTWLLHC- 1079
Cdd:cd11020     27 NGQVPGPV--IRVREGDTVELTLTNPGTNTMPHSIDFHAAT----GPGG--GEFTTIAPGETKTFSFKALYPGVFMYHCa 98

                           90
                   ....*....|..
gi 1949456009 1080 --HVSDHIHAGM 1089
Cdd:cd11020     99 taPVLMHIANGM 110
ascorbase TIGR03388
L-ascorbate oxidase, plant type; Members of this protein family are the copper-containing ...
 134-238 1.21e-03

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: 42.82  E-value: 1.21e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949456009  134 GPIIRAEVNDVIKIHLKN-FASRNYSIHPHGLfykkDAEGALYPDNTSDALKKddSVPPGGSFTYSWEVkprfapttDDA 212
Cdd:TIGR03388   31 GPTIRAQAGDTIVVELTNkLHTEGVVIHWHGI----RQIGTPWADGTAGVTQC--AINPGETFIYNFVV--------DRP 96

                           90       100
                   ....*....|....*....|....*.
gi 1949456009  213 NclTWVYHSHVNAPHdiASGLIGPLI 238
Cdd:TIGR03388   97 G--TYFYHGHYGMQR--SAGLYGSLI 118
CuRO_1_McoC_like cd13855
The first cupredoxin domain of a multicopper oxidase McoC and similar proteins; This family ...
 843-932 1.21e-03

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


Pssm-ID: 259924 [Multi-domain]  Cd Length: 121  Bit Score: 39.77  E-value: 1.21e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949456009  843 GPIIHAEVGEQILIIFKNKASRPYSITAHGV----KASGS-HVPVEPGRIIELTWDIPESSGpGTselncisYVYFSSVD 917
Cdd:cd13855     32 GPLIEVFEGDTVEITFRNRLPEPTTVHWHGLpvppDQDGNpHDPVAPGNDRVYRFTLPQDSA-GT-------YWYHPHPH 103

                           90
                   ....*....|....*..
gi 1949456009  918 YI--KDLYSGLLGPLVI 932
Cdd:cd13855    104 GHtaEQVYRGLAGAFVV 120
CuRO_3_MCO_like_4 cd13910
The third cupredoxin domain of uncharacterized multicopper oxidase; Multicopper Oxidases (MCOs) ...
 1068-1089 1.33e-03

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


Pssm-ID: 259977 [Multi-domain]  Cd Length: 166  Bit Score: 40.74  E-value: 1.33e-03
                           10        20
                   ....*....|....*....|..
gi 1949456009 1068 VAANPGTWLLHCHVSDHIHAGM 1089
Cdd:cd13910    139 VADNPGLWAFHCHILWHMAAGM 160
CuRO_3_Diphenol_Ox cd13904
The third cupredoxin domain of fungal laccase, diphenol oxidase; Diphenol oxidase belongs to ...
 1044-1088 1.38e-03

The third cupredoxin domain of fungal laccase, diphenol oxidase; Diphenol oxidase belongs to the laccase family. It catalyzes the initial steps in melanin biosynthesis from diphenols. Melanin is one of the virulence factors of infectious fungi. In the pathogenesis of C. neoformans, melanin pigments have been shown to protect the fungal cells from oxidative and microbicidal activities of host defense systems. Laccase is a blue multicopper oxidase (MCO) which catalyzes the oxidation of a variety aromatic - notably phenolic and inorganic substances coupled to the reduction of molecular oxygen to water. It has been implicated in a wide spectrum of biological activities and, in particular, plays a key role in morphogenesis, development and lignin metabolism. Although MCOs have diverse functions, majority of them have three cupredoxin domain repeats that include one mononuclear and one trinuclear copper center. The copper ions are bound in several sites: Type 1, Type 2, and/or Type 3. The ensemble of types 2 and 3 copper is called a trinuclear cluster. MCOs oxidize their substrate by accepting electrons at a mononuclear copper center and transferring them to the active site trinuclear copper center. The cupredoxin domain 3 of 3-domain MCOs contains the Type 1 (T1) copper binding site and part the trinuclear copper binding site, which is located at the interface of domains 1 and 3.


Pssm-ID: 259971 [Multi-domain]  Cd Length: 158  Bit Score: 40.74  E-value: 1.38e-03
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*
gi 1949456009 1044 YRTDLVHRGDVVDLFPGTFATVEMVAANPGTWLLHCHVSDHIHAG 1088
Cdd:cd13904    107 YNTTNPLRRDTIVIPGGSWAVLRIPADNPGVWALHCHIGWHLAAG 151
CuRO_1_CuNIR_like cd04201
Cupredoxin domain 1 of Copper-containing nitrite reductase and two-domain laccase; ...
 114-238 1.44e-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: 39.78  E-value: 1.44e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949456009  114 EYTDATFSHQAPreewlgylGPIIRAEVNDVIKIHLKNFASrnySIHPHGLfykkDAEGALYPDNTSDAlkkdDSVPPGG 193
Cdd:cd04201     20 EYRYWTFDGDIP--------GPMLRVREGDTVELHFSNNPS---STMPHNI----DFHAATGAGGGAGA----TFIAPGE 80

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*..
gi 1949456009  194 SFTYSWEVKPRFapttddanclTWVYHSHVN--APHdIASGLIGPLI 238
Cdd:cd04201     81 TSTFSFKATQPG----------LYVYHCAVApvPMH-IANGMYGLIL 116
CuRO_3_Abr2_like cd13898
The third cupredoxin domain of a group of fungal Laccases similar to Abr2 from Aspergillus ...
 1068-1089 1.47e-03

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


Pssm-ID: 259965 [Multi-domain]  Cd Length: 164  Bit Score: 40.70  E-value: 1.47e-03
                           10        20
                   ....*....|....*....|..
gi 1949456009 1068 VAANPGTWLLHCHVSDHIHAGM 1089
Cdd:cd13898    136 HVVNPGAWLLHCHIQSHLAGGM 157
CuRO_1_CuNIR_like cd04201
Cupredoxin domain 1 of Copper-containing nitrite reductase and two-domain laccase; ...
 1001-1089 1.52e-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: 39.78  E-value: 1.52e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949456009 1001 NGRVYGNLhgLVMQQNEKVDWYLLGMGNEVDMHTVHFHAetfiyrtdlVHR--GDVVDLF--PGTFATVEMVAANPGTWL 1076
Cdd:cd04201     27 DGDIPGPM--LRVREGDTVELHFSNNPSSTMPHNIDFHA---------ATGagGGAGATFiaPGETSTFSFKATQPGLYV 95

                           90
                   ....*....|....*.
gi 1949456009 1077 LHCHVSD---HIHAGM 1089
Cdd:cd04201     96 YHCAVAPvpmHIANGM 111
ascorbOXfungal TIGR03390
L-ascorbate oxidase, fungal type; This model describes a family of fungal ascorbate oxidases, ...
 1041-1095 2.67e-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: 2.67e-03
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 1949456009 1041 TFIYRtdlvHRGDVVDLFPGTFATVEMVAANPGTWLLHCHVSDHIHAGMETTYTI 1095
Cdd:TIGR03390  481 TMLYR----YAVKVVPGAPAGWRAWRIRVTNPGVWMMHCHILQHMVMGMQTVWVF 531
CuRO_1_LCC_plant cd13849
The first cupredoxin domain of plant laccases; Laccase is a blue multicopper oxidase (MCO) ...
 493-555 2.78e-03

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


Pssm-ID: 259918 [Multi-domain]  Cd Length: 117  Bit Score: 38.78  E-value: 2.78e-03
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1949456009  493 FLGPVLRVEEGDILNVTFLNKADRGYSIHPHGlNYDKRfqgTSYEDGidkPG----SNVEPGQRFTY 555
Cdd:cd13849     26 FPGPTIRVHEGDTVVVNVTNRSPYNITIHWHG-IRQLR---SGWADG---PAyitqCPIQPGQSYTY 85
CuRO_1_tcLCC2_insect_like cd13858
The first cupredoxin domain of insect laccases similar to laccase 2 in Tribolium castaneum; ...
 495-559 3.65e-03

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


Pssm-ID: 259927 [Multi-domain]  Cd Length: 105  Bit Score: 38.29  E-value: 3.65e-03
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1949456009  495 GPVLRVEEGDILNVTFLNKAD-RGYSIHPHGLnydkrFQ-GTSYEDGIDK----PgsnVEPGQRFTYSWQV 559
Cdd:cd13858     16 GPSIEVCEGDTVVVDVKNRLPgESTTIHWHGI-----HQrGTPYMDGVPMvtqcP---ILPGQTFRYKFKA 78
CuRO_3_AAO_like_2 cd13895
The third cupredoxin domain of Ascorbate oxidase homologs; This family includes fungal ...
 1022-1095 3.66e-03

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


Pssm-ID: 259962 [Multi-domain]  Cd Length: 188  Bit Score: 39.99  E-value: 3.66e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949456009 1022 YLLGMGNEVDMHTVHFHAETF-----IYR-TDLVHRGDVVDLFPGTFA-----TVEMVAANPGTWLLHCHVSDHIHAGME 1090
Cdd:cd13895    103 YDLGSGLGTYSATALANEEKLrgynpIRRdTTMLYRYGGKGYYPPPGTgsgwrAWRLRVDDPGVWMLHCHILQHMIMGMQ 182


                   ....*
gi 1949456009 1091 TTYTI 1095
Cdd:cd13895    183 TVWVF 187
CuRO_3_CumA_like cd13906
The third cupredoxin domain of CumA like multicopper oxidase; This multicopper oxidase (MCO) ...
 332-404 3.79e-03

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: 38.90  E-value: 3.79e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949456009  332 WHLFGMGNEVD-IHSAFFHGNT--LLNR-------GHRTDTISLFPATFVTATMVPKVKGKWLLSCQVNDHLQAGMQAFY 401
Cdd:cd13906     56 SYVLRLVNETAfLHPMHLHGHFfrVLSRngrpvpePFWRDTVLLGPKETVDIAFVADNPGDWMFHCHILEHQETGMMGVI 135


                   ...
gi 1949456009  402 KVK 404
Cdd:cd13906    136 RVA 138
CuRO_1_AAO_like_1 cd13846
The first cupredoxin domain of plant Ascorbate oxidase homologs; This subfamily is composed of ...
 493-559 4.66e-03

The first cupredoxin domain of plant Ascorbate oxidase homologs; This subfamily is composed of plant pollen multicopper oxidase homologous to 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. This subfamily does not harbor trinuclear copper binding histidines.


Pssm-ID: 259915 [Multi-domain]  Cd Length: 118  Bit Score: 38.16  E-value: 4.66e-03
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1949456009  493 FLGPVLRVEEGDILNVTFLNKADRGYSIHPHGLNYDKrfqgTSYEDGIdkPGSN--VEPGQRFTYSWQV 559
Cdd:cd13846     28 FPGPTINVTTNDNVVVNVFNSLDEPLLLTWNGIQQRR----NSWQDGV--LGTNcpIPPGWNWTYKFQV 90
 
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.
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