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Conserved domains on  [gi|564399494|ref|XP_006257111|]
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hephaestin isoform X1 [Rattus norvegicus]

Protein Classification

multicopper oxidase; multicopper oxidase domain-containing protein( domain architecture ID 10136072)

multicopper oxidase (MCO) that couples the oxidation of a substrate with a four-electron reduction of molecular oxygen to water, and which may contain three cupredoxin domains that include one mononuclear and one trinuclear copper center| multicopper oxidase domain-containing protein that may contain type I Cu center(s) and be involved in inter-molecular electron transfer; contains a cupredoxin domain similar to the first cupredoxin domain of bacterial laccases similar to a hyperthermophilic multicopper oxidase (MCO) from thermus thermophilus HB27; may be a partial protein

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
CuRO_1_ceruloplasmin cd04222
The first cupredoxin domain of Ceruloplasmin; Ceruloplasmin is a multicopper oxidase essential ...
 26-208 3.47e-119

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: 365.20  E-value: 3.47e-119
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564399494   26 RNYYLGIQDIQWNYAPKGRNVITNQTLNNDTVASSFLKSGKNRIGGTYKKTVYKEYSDGTYTNEIAKPAWLGFLGPLLKA 105
Cdd:cd04222     1 REYYIGIRETQWDYAPSGKNLITNQTFDDDEHASVFLKRGPDRIGRVYKKAVYLQYTDDTYRTEIEKPVWLGFLGPILKA 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564399494  106 EMGDVILIHLKNFASRPYTIHPHGVFYEKDSEGSLYPDGSSGYLKADDSVPPGGSHVYNWSIPEGHAPTEADPACLTWIY 185
Cdd:cd04222    81 EVGDVIVVHLKNFASRPYSLHPHGVFYNKENEGALYPDNTSGFEKADDAVPPGGSYTYTWTVPEEQAPTKADANCLTRIY 160

                         170       180
                  ....*....|....*....|...
gi 564399494  186 HSHVDAPRDIATGLIGPLITCKR 208
Cdd:cd04222   161 HSHIDAPKDIASGLIGPLIICKK 183
CuRO_3_ceruloplasmin cd04224
The third cupredoxin domain of Ceruloplasmin; Ceruloplasmin is a multicopper oxidase essential ...
 377-571 2.22e-116

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: 358.32  E-value: 2.22e-116
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564399494  377 GKVRQYFIQAHEIQWDYGPIGHDGRTGKSLREPGSGPDKYFQKSSSRIGGTYWKVRYEAFQDETFQERLHQ-EEETHLGI 455
Cdd:cd04224     1 GKVRHYFIAAEEIMWDYAPSGKNLFTGQNLTAPGSDSEVFFQRNETRIGGTYWKVRYVEYTDATFTTRKHRsKEEEHLGI 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564399494  456 LGPVIRAEVGDTIQVVFYNRASQPFSIQPHGVFYEKSSEGTVYNDGTSYPK-VAKSFEKVTYYWTVPPHAGPTAEDPACL 534
Cdd:cd04224    81 LGPVIRAEVGDTIKVTFRNKASRPFSIQPHGVFYEKNYEGAMYRDGDPSPGsHVSPGETFTYEWTVPEGVGPTNQDPPCL 160

                         170       180       190
                  ....*....|....*....|....*....|....*..
gi 564399494  535 TWMYFSAADPTRDTNSGLVGPLLVCKAGALGEDGKQK 571
Cdd:cd04224   161 TYLYFSAVDPVRDTNSGLVGPLLVCKKGSLNANGRQK 197
CuRO_5_ceruloplasmin cd04225
The fifth cupredoxin domain of Ceruloplasmin; Ceruloplasmin is a multicopper oxidase essential ...
 732-903 1.04e-103

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: 323.65  E-value: 1.04e-103
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564399494  732 RVYYIMAEEIEWDYCPDRSWELEWYNTSEKdSYGHVFLSNKDGLLGSKYKKAVFREYTDGTFRIPQPRSGPEEHLGILGP 811
Cdd:cd04225     1 RTYYIAAEEVEWDYSPQRTWEQELHNTHEE-SPGNAFLNKGDKFIGSKYKKVVYREYTDDTFSVPKERTAEEEHLGILGP 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564399494  812 LIRGEVGDILTVVFKNKASRPYSIHAHGVLESSTgWPQAAEPGEVLTYQWNIPERSGPGPSDSACVSWIYYSAVDPIKDM 891
Cdd:cd04225    80 LIHAEVGEKVKIVFKNMASRPYSIHAHGVKTDSS-WVAPTEPGETQTYTWKIPERSGPGVEDSNCISWAYYSTVDQIKDL 158

                         170
                  ....*....|..
gi 564399494  892 YSGLVGPLVICR 903
Cdd:cd04225   159 YSGLIGPLVICR 170
Cupredoxin super family cl19115
Cupredoxin superfamily; Cupredoxins contain type I copper centers and are involved in ...
 223-363 6.23e-86

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: 274.35  E-value: 6.23e-86
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564399494  223 DHNFFLLFSVIDENLSWHLDDNIATYCSDPASVDKEDGPFQDSNRMHAINGFVFGNLPELSMCAQKHVAWHLFGMGNEID 302
Cdd:cd11021     1 DREFVLMFSVVDENLSWYLDENIKTYCSEPAKVDKDDEDFQESNKMHSINGYTFGNLPGLSMCAGDRVKWHLFGMGNEVD 80

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 564399494  303 VHTAFFHGQTLSIRGHRTDVAHIFPATFVTAEMVPQKSGTWLISCVVNSHLKSGMQAFYKV 363
Cdd:cd11021    81 IHSAFFHGQTLTDRGHRTDTINLFPATFVTAEMVAQNPGKWLLSCQVNDHLKAGMQAFYEV 141
Cupredoxin super family cl19115
Cupredoxin superfamily; Cupredoxins contain type I copper centers and are involved in ...
 574-717 6.42e-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 cd11022:

Pssm-ID: 473140 [Multi-domain]  Cd Length: 144  Bit Score: 260.49  E-value: 6.42e-81
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564399494  574 DKEFFLLFTIFDENESWYNNANQAAGMLDSRLLSEDVEGFEDSNRMHAINGFLFSNLPRLDICKGDTVAWHLLGLGTEND 653
Cdd:cd11022     1 DKEFFLLFTVFDENESWYLDENIQQFTLDPRSVDKEDEDFQESNKMHSINGYMYGNQPGLDMCKGDTVSWHLFGLGTETD 80

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 564399494  654 VHGVMFEGNTLQLQGMRKSAAMLFPHTFVTAIMQPDNPGIFEIYCQAGSHREAGMQAIYNVSQC 717
Cdd:cd11022    81 VHGIYFSGNTFLLQGTRRDTANLFPHTSVTAIMQPDNEGTFEVNCQTTDHYSAGMRQIYTVSQC 144
Cupredoxin super family cl19115
Cupredoxin superfamily; Cupredoxins contain type I copper centers and are involved in ...
 919-1062 8.83e-65

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: 215.50  E-value: 8.83e-65
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564399494  919 EFALLFLIFDENQSWYLKENIATYGpQETSHVNLQDATFLESNKMHAINGKLYANLRGLTVYQGERVAWYMLAMGQDTDI 998
Cdd:cd11012     3 EFALLFLVFDENESWYLDENIKTYS-DHPEKVNKEDEEFIESNKMHAINGKVFGNLQGLTMHVGDEVYWYLMGMGNEIDI 81

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 564399494  999 HTVHFHAESFLYQNGHSYRADVVDLFPGTFEVVEMVASNPGAWLMHCHVTDHVHAGMETIFTVL 1062
Cdd:cd11012    82 HTAHFHGHSFDYKHRGVYRSDVFDLFPGTFQTVEMIPRTPGTWLLHCHVTDHIHAGMETTYTVL 145
 
Name Accession Description Interval E-value
CuRO_1_ceruloplasmin cd04222
The first cupredoxin domain of Ceruloplasmin; Ceruloplasmin is a multicopper oxidase essential ...
 26-208 3.47e-119

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: 365.20  E-value: 3.47e-119
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564399494   26 RNYYLGIQDIQWNYAPKGRNVITNQTLNNDTVASSFLKSGKNRIGGTYKKTVYKEYSDGTYTNEIAKPAWLGFLGPLLKA 105
Cdd:cd04222     1 REYYIGIRETQWDYAPSGKNLITNQTFDDDEHASVFLKRGPDRIGRVYKKAVYLQYTDDTYRTEIEKPVWLGFLGPILKA 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564399494  106 EMGDVILIHLKNFASRPYTIHPHGVFYEKDSEGSLYPDGSSGYLKADDSVPPGGSHVYNWSIPEGHAPTEADPACLTWIY 185
Cdd:cd04222    81 EVGDVIVVHLKNFASRPYSLHPHGVFYNKENEGALYPDNTSGFEKADDAVPPGGSYTYTWTVPEEQAPTKADANCLTRIY 160

                         170       180
                  ....*....|....*....|...
gi 564399494  186 HSHVDAPRDIATGLIGPLITCKR 208
Cdd:cd04222   161 HSHIDAPKDIASGLIGPLIICKK 183
CuRO_3_ceruloplasmin cd04224
The third cupredoxin domain of Ceruloplasmin; Ceruloplasmin is a multicopper oxidase essential ...
 377-571 2.22e-116

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: 358.32  E-value: 2.22e-116
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564399494  377 GKVRQYFIQAHEIQWDYGPIGHDGRTGKSLREPGSGPDKYFQKSSSRIGGTYWKVRYEAFQDETFQERLHQ-EEETHLGI 455
Cdd:cd04224     1 GKVRHYFIAAEEIMWDYAPSGKNLFTGQNLTAPGSDSEVFFQRNETRIGGTYWKVRYVEYTDATFTTRKHRsKEEEHLGI 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564399494  456 LGPVIRAEVGDTIQVVFYNRASQPFSIQPHGVFYEKSSEGTVYNDGTSYPK-VAKSFEKVTYYWTVPPHAGPTAEDPACL 534
Cdd:cd04224    81 LGPVIRAEVGDTIKVTFRNKASRPFSIQPHGVFYEKNYEGAMYRDGDPSPGsHVSPGETFTYEWTVPEGVGPTNQDPPCL 160

                         170       180       190
                  ....*....|....*....|....*....|....*..
gi 564399494  535 TWMYFSAADPTRDTNSGLVGPLLVCKAGALGEDGKQK 571
Cdd:cd04224   161 TYLYFSAVDPVRDTNSGLVGPLLVCKKGSLNANGRQK 197
CuRO_5_ceruloplasmin cd04225
The fifth cupredoxin domain of Ceruloplasmin; Ceruloplasmin is a multicopper oxidase essential ...
 732-903 1.04e-103

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: 323.65  E-value: 1.04e-103
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564399494  732 RVYYIMAEEIEWDYCPDRSWELEWYNTSEKdSYGHVFLSNKDGLLGSKYKKAVFREYTDGTFRIPQPRSGPEEHLGILGP 811
Cdd:cd04225     1 RTYYIAAEEVEWDYSPQRTWEQELHNTHEE-SPGNAFLNKGDKFIGSKYKKVVYREYTDDTFSVPKERTAEEEHLGILGP 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564399494  812 LIRGEVGDILTVVFKNKASRPYSIHAHGVLESSTgWPQAAEPGEVLTYQWNIPERSGPGPSDSACVSWIYYSAVDPIKDM 891
Cdd:cd04225    80 LIHAEVGEKVKIVFKNMASRPYSIHAHGVKTDSS-WVAPTEPGETQTYTWKIPERSGPGVEDSNCISWAYYSTVDQIKDL 158

                         170
                  ....*....|..
gi 564399494  892 YSGLVGPLVICR 903
Cdd:cd04225   159 YSGLIGPLVICR 170
CuRO_2_ceruloplasmin cd11021
The second cupredoxin domain of Ceruloplasmin; Ceruloplasmin is a multicopper oxidase ...
 223-363 6.23e-86

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: 274.35  E-value: 6.23e-86
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564399494  223 DHNFFLLFSVIDENLSWHLDDNIATYCSDPASVDKEDGPFQDSNRMHAINGFVFGNLPELSMCAQKHVAWHLFGMGNEID 302
Cdd:cd11021     1 DREFVLMFSVVDENLSWYLDENIKTYCSEPAKVDKDDEDFQESNKMHSINGYTFGNLPGLSMCAGDRVKWHLFGMGNEVD 80

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 564399494  303 VHTAFFHGQTLSIRGHRTDVAHIFPATFVTAEMVPQKSGTWLISCVVNSHLKSGMQAFYKV 363
Cdd:cd11021    81 IHSAFFHGQTLTDRGHRTDTINLFPATFVTAEMVAQNPGKWLLSCQVNDHLKAGMQAFYEV 141
CuRO_4_ceruloplasmin cd11022
The fourth cupredoxin domain of Ceruloplasmin; Ceruloplasmin is a multicopper oxidase ...
 574-717 6.42e-81

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: 260.49  E-value: 6.42e-81
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564399494  574 DKEFFLLFTIFDENESWYNNANQAAGMLDSRLLSEDVEGFEDSNRMHAINGFLFSNLPRLDICKGDTVAWHLLGLGTEND 653
Cdd:cd11022     1 DKEFFLLFTVFDENESWYLDENIQQFTLDPRSVDKEDEDFQESNKMHSINGYMYGNQPGLDMCKGDTVSWHLFGLGTETD 80

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 564399494  654 VHGVMFEGNTLQLQGMRKSAAMLFPHTFVTAIMQPDNPGIFEIYCQAGSHREAGMQAIYNVSQC 717
Cdd:cd11022    81 VHGIYFSGNTFLLQGTRRDTANLFPHTSVTAIMQPDNEGTFEVNCQTTDHYSAGMRQIYTVSQC 144
CuRO_6_ceruloplasmin cd11012
The sixth cupredoxin domain of Ceruloplasmin; Ceruloplasmin is a multicopper oxidase essential ...
 919-1062 8.83e-65

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: 215.50  E-value: 8.83e-65
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564399494  919 EFALLFLIFDENQSWYLKENIATYGpQETSHVNLQDATFLESNKMHAINGKLYANLRGLTVYQGERVAWYMLAMGQDTDI 998
Cdd:cd11012     3 EFALLFLVFDENESWYLDENIKTYS-DHPEKVNKEDEEFIESNKMHAINGKVFGNLQGLTMHVGDEVYWYLMGMGNEIDI 81

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 564399494  999 HTVHFHAESFLYQNGHSYRADVVDLFPGTFEVVEMVASNPGAWLMHCHVTDHVHAGMETIFTVL 1062
Cdd:cd11012    82 HTAHFHGHSFDYKHRGVYRSDVFDLFPGTFQTVEMIPRTPGTWLLHCHVTDHIHAGMETTYTVL 145
Cu-oxidase_2 pfam07731
Multicopper oxidase; This entry contains many divergent copper oxidase-like domains that are ...
 961-1065 1.93e-15

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


Pssm-ID: 462246 [Multi-domain]  Cd Length: 138  Bit Score: 74.39  E-value: 1.93e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564399494   961 NKMHAINGKLY-ANLRGLTVYQGERVAWYMLAMgqDTDIHTVHFHAESF----------LYQNGHSY------RADVVDL 1023
Cdd:pfam07731   19 RNDWAINGLLFpPNTNVITLPYGTVVEWVLQNT--TTGVHPFHLHGHSFqvlgrgggpwPEEDPKTYnlvdpvRRDTVQV 96

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|..
gi 564399494  1024 FPGTFEVVEMVASNPGAWLMHCHVTDHVHAGMETIFTVLSHE 1065
Cdd:pfam07731   97 PPGGWVAIRFRADNPGVWLFHCHILWHLDQGMMGQFVVRPGD 138
SufI COG2132
Multicopper oxidase with three cupredoxin domains (includes cell division protein FtsP and ...
 963-1061 2.34e-11

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: 67.27  E-value: 2.34e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564399494  963 MHAINGKLYANLR-GLTVYQGERVAWYMLAMGQDTdiHTVHFHAESF--LYQNG----HSYRADVVDLFPGTFEVVEMVA 1035
Cdd:COG2132   317 VWTINGKAFDPDRpDLTVKLGERERWTLVNDTMMP--HPFHLHGHQFqvLSRNGkpppEGGWKDTVLVPPGETVRILFRF 394

                          90       100
                  ....*....|....*....|....*..
gi 564399494 1036 SN-PGAWLMHCHVTDHVHAGMETIFTV 1061
Cdd:COG2132   395 DNyPGDWMFHCHILEHEDAGMMGQFEV 421
Cu-oxidase_3 pfam07732
Multicopper oxidase; This entry contains many divergent copper oxidase-like domains that are ...
 98-204 3.28e-09

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: 55.71  E-value: 3.28e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564399494    98 FLGPLLKAEMGDVILIHLKNFASRPYTIHPHGVFyekdSEGSLYPDGSSGYlkADDSVPPGGSHVYNWSIPeghapteaD 177
Cdd:pfam07732   24 FPGPTIRVREGDTVVVNVTNNLDEPTSIHWHGLQ----QRGTPWMDGVPGV--TQCPIPPGQSFTYRFQVK--------Q 89

                           90       100
                   ....*....|....*....|....*..
gi 564399494   178 PACLTWiYHSHVDAPRdiATGLIGPLI 204
Cdd:pfam07732   90 QAGTYW-YHSHTSGQQ--AAGLAGAII 113
SufI COG2132
Multicopper oxidase with three cupredoxin domains (includes cell division protein FtsP and ...
 98-204 1.57e-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: 58.41  E-value: 1.57e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564399494   98 FLGPLLKAEMGDVILIHLKNFASRPYTIHPHGVfyekdsegsLYPDGSSGYlkADDSVPPGGSHVYNWSIPeghapteaD 177
Cdd:COG2132    42 YPGPTIRVREGDRVRVRVTNRLPEPTTVHWHGL---------RVPNAMDGV--PGDPIAPGETFTYEFPVP--------Q 102

                          90       100
                  ....*....|....*....|....*....
gi 564399494  178 PACLTWiYHSHVDA--PRDIATGLIGPLI 204
Cdd:COG2132   103 PAGTYW-YHPHTHGstAEQVYRGLAGALI 130
PLN02191 PLN02191
L-ascorbate oxidase
 98-231 8.70e-07

L-ascorbate oxidase


Pssm-ID: 177843 [Multi-domain]  Cd Length: 574  Bit Score: 53.09  E-value: 8.70e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564399494   98 FLGPLLKAEMGDVILIHLKN-FASRPYTIHPHGVfyekDSEGSLYPDGSSGYLKAddSVPPGGSHVYNWSIPEGHaptea 176
Cdd:PLN02191   51 FPGPTIDAVAGDTIVVHLTNkLTTEGLVIHWHGI----RQKGSPWADGAAGVTQC--AINPGETFTYKFTVEKPG----- 119

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 564399494  177 dpaclTWIYHSHVDAPRdiATGLIGPLITCKrgtldGNSPPQRKDVDHNFFLLFS 231
Cdd:PLN02191  120 -----THFYHGHYGMQR--SAGLYGSLIVDV-----AKGPKERLRYDGEFNLLLS 162
SufI COG2132
Multicopper oxidase with three cupredoxin domains (includes cell division protein FtsP and ...
 455-646 1.05e-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: 52.63  E-value: 1.05e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564399494  455 ILGPVIRAEVGDTIQVVFYNRASQPFSIQPHGVFYekSSEgtvyNDGTSYPKVA--KSFekvTYYWTVPPHAGptaedpa 532
Cdd:COG2132    42 YPGPTIRVREGDRVRVRVTNRLPEPTTVHWHGLRV--PNA----MDGVPGDPIApgETF---TYEFPVPQPAG------- 105

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564399494  533 clTWMYFSAADPTRDTN--SGLVGPLLVckagaLGEDGKQKGVDKEFFLLFT--IFDENESW-YNNANQAAGMLDSRLLs 607
Cdd:COG2132   106 --TYWYHPHTHGSTAEQvyRGLAGALIV-----EDPEEDLPRYDRDIPLVLQdwRLDDDGQLlYPMDAAMGGRLGDTLL- 177

                         170       180       190
                  ....*....|....*....|....*....|....*....
gi 564399494  608 edvegfedsnrmhaINGFLfsnLPRLDICKGDTVAWHLL 646
Cdd:COG2132   178 --------------VNGRP---NPTLEVRPGERVRLRLL 199
Cu-oxidase pfam00394
Multicopper oxidase; Many of the proteins in this family contain multiple similar copies of ...
 230-367 3.79e-06

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


Pssm-ID: 395317 [Multi-domain]  Cd Length: 146  Bit Score: 47.70  E-value: 3.79e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564399494   230 FSVIDENLSWHlDDNIATYCSDPASVDKED---GPFQDSnrmHAINGFVFGNLPELSMCAQKHVAWHLFgMGNEIDVHTA 306
Cdd:pfam00394    1 EDYVITLSDWY-HKDAKDLEKELLASGKAPtdfPPVPDA---VLINGKDGASLATLTVTPGKTYRLRII-NVALDDSLNF 75

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 564399494   307 FFHGQTLSIRG--------HRTDVAHIFPATF----VTAemvPQKSGTWLISC-VVNSHLKSGMQAFYKVDSCS 367
Cdd:pfam00394   76 SIEGHKMTVVEvdgvyvnpFTVDSLDIFPGQRysvlVTA---NQDPGNYWIVAsPNIPAFDNGTAAAILRYSGA 146
Cu-oxidase_3 pfam07732
Multicopper oxidase; This entry contains many divergent copper oxidase-like domains that are ...
 808-868 5.71e-06

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


Pssm-ID: 462247 [Multi-domain]  Cd Length: 119  Bit Score: 46.47  E-value: 5.71e-06
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 564399494   808 ILGPLIRGEVGDILTVVFKNKASRPYSIHAHGVLESSTGW-------PQAA-EPGEVLTYQWNIPERSG 868
Cdd:pfam07732   24 FPGPTIRVREGDTVVVNVTNNLDEPTSIHWHGLQQRGTPWmdgvpgvTQCPiPPGQSFTYRFQVKQQAG 92
ascorbOXfungal TIGR03390
L-ascorbate oxidase, fungal type; This model describes a family of fungal ascorbate oxidases, ...
 1016-1061 6.78e-06

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: 50.22  E-value: 6.78e-06
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*.
gi 564399494  1016 YRADVVDLFPGTFEVVEMVASNPGAWLMHCHVTDHVHAGMETIFTV 1061
Cdd:TIGR03390  486 YAVKVVPGAPAGWRAWRIRVTNPGVWMMHCHILQHMVMGMQTVWVF 531
PLN02191 PLN02191
L-ascorbate oxidase
 996-1059 9.64e-06

L-ascorbate oxidase


Pssm-ID: 177843 [Multi-domain]  Cd Length: 574  Bit Score: 49.63  E-value: 9.64e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564399494  996 TDIHTVHFHAESFL---YQNGH---------------SYRADVVdLFPGTFEVVEMVASNPGAWLMHCHVTDHVHAGMET 1057
Cdd:PLN02191  464 SEIHPWHLHGHDFWvlgYGDGKfkpgidektynlknpPLRNTAI-LYPYGWTAIRFVTDNPGVWFFHCHIEPHLHMGMGV 542


                  ..
gi 564399494 1058 IF 1059
Cdd:PLN02191  543 VF 544
Cu-oxidase_3 pfam07732
Multicopper oxidase; This entry contains many divergent copper oxidase-like domains that are ...
 455-558 4.66e-05

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


Pssm-ID: 462247 [Multi-domain]  Cd Length: 119  Bit Score: 43.77  E-value: 4.66e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564399494   455 ILGPVIRAEVGDTIQVVFYNRASQPFSIQPHGVFyeksSEGTVYNDG----TSYPkvAKSFEKVTYYWTVPPHAGptaed 530
Cdd:pfam07732   24 FPGPTIRVREGDTVVVNVTNNLDEPTSIHWHGLQ----QRGTPWMDGvpgvTQCP--IPPGQSFTYRFQVKQQAG----- 92

                           90       100
                   ....*....|....*....|....*...
gi 564399494   531 paclTWMYFSAADPTRdtNSGLVGPLLV 558
Cdd:pfam07732   93 ----TYWYHSHTSGQQ--AAGLAGAIII 114
ascorbase TIGR03388
L-ascorbate oxidase, plant type; Members of this protein family are the copper-containing ...
 810-868 1.33e-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: 1.33e-03
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 564399494   810 GPLIRGEVGDILTVVFKNK-ASRPYSIHAHGVLESSTGWPQAAE--------PGEVLTYQWNIpERSG 868
Cdd:TIGR03388   31 GPTIRAQAGDTIVVELTNKlHTEGVVIHWHGIRQIGTPWADGTAgvtqcainPGETFIYNFVV-DRPG 97
 
Name Accession Description Interval E-value
CuRO_1_ceruloplasmin cd04222
The first cupredoxin domain of Ceruloplasmin; Ceruloplasmin is a multicopper oxidase essential ...
 26-208 3.47e-119

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: 365.20  E-value: 3.47e-119
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564399494   26 RNYYLGIQDIQWNYAPKGRNVITNQTLNNDTVASSFLKSGKNRIGGTYKKTVYKEYSDGTYTNEIAKPAWLGFLGPLLKA 105
Cdd:cd04222     1 REYYIGIRETQWDYAPSGKNLITNQTFDDDEHASVFLKRGPDRIGRVYKKAVYLQYTDDTYRTEIEKPVWLGFLGPILKA 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564399494  106 EMGDVILIHLKNFASRPYTIHPHGVFYEKDSEGSLYPDGSSGYLKADDSVPPGGSHVYNWSIPEGHAPTEADPACLTWIY 185
Cdd:cd04222    81 EVGDVIVVHLKNFASRPYSLHPHGVFYNKENEGALYPDNTSGFEKADDAVPPGGSYTYTWTVPEEQAPTKADANCLTRIY 160

                         170       180
                  ....*....|....*....|...
gi 564399494  186 HSHVDAPRDIATGLIGPLITCKR 208
Cdd:cd04222   161 HSHIDAPKDIASGLIGPLIICKK 183
CuRO_3_ceruloplasmin cd04224
The third cupredoxin domain of Ceruloplasmin; Ceruloplasmin is a multicopper oxidase essential ...
 377-571 2.22e-116

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: 358.32  E-value: 2.22e-116
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564399494  377 GKVRQYFIQAHEIQWDYGPIGHDGRTGKSLREPGSGPDKYFQKSSSRIGGTYWKVRYEAFQDETFQERLHQ-EEETHLGI 455
Cdd:cd04224     1 GKVRHYFIAAEEIMWDYAPSGKNLFTGQNLTAPGSDSEVFFQRNETRIGGTYWKVRYVEYTDATFTTRKHRsKEEEHLGI 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564399494  456 LGPVIRAEVGDTIQVVFYNRASQPFSIQPHGVFYEKSSEGTVYNDGTSYPK-VAKSFEKVTYYWTVPPHAGPTAEDPACL 534
Cdd:cd04224    81 LGPVIRAEVGDTIKVTFRNKASRPFSIQPHGVFYEKNYEGAMYRDGDPSPGsHVSPGETFTYEWTVPEGVGPTNQDPPCL 160

                         170       180       190
                  ....*....|....*....|....*....|....*..
gi 564399494  535 TWMYFSAADPTRDTNSGLVGPLLVCKAGALGEDGKQK 571
Cdd:cd04224   161 TYLYFSAVDPVRDTNSGLVGPLLVCKKGSLNANGRQK 197
CuRO_5_ceruloplasmin cd04225
The fifth cupredoxin domain of Ceruloplasmin; Ceruloplasmin is a multicopper oxidase essential ...
 732-903 1.04e-103

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: 323.65  E-value: 1.04e-103
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564399494  732 RVYYIMAEEIEWDYCPDRSWELEWYNTSEKdSYGHVFLSNKDGLLGSKYKKAVFREYTDGTFRIPQPRSGPEEHLGILGP 811
Cdd:cd04225     1 RTYYIAAEEVEWDYSPQRTWEQELHNTHEE-SPGNAFLNKGDKFIGSKYKKVVYREYTDDTFSVPKERTAEEEHLGILGP 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564399494  812 LIRGEVGDILTVVFKNKASRPYSIHAHGVLESSTgWPQAAEPGEVLTYQWNIPERSGPGPSDSACVSWIYYSAVDPIKDM 891
Cdd:cd04225    80 LIHAEVGEKVKIVFKNMASRPYSIHAHGVKTDSS-WVAPTEPGETQTYTWKIPERSGPGVEDSNCISWAYYSTVDQIKDL 158

                         170
                  ....*....|..
gi 564399494  892 YSGLVGPLVICR 903
Cdd:cd04225   159 YSGLIGPLVICR 170
CuRO_2_ceruloplasmin cd11021
The second cupredoxin domain of Ceruloplasmin; Ceruloplasmin is a multicopper oxidase ...
 223-363 6.23e-86

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: 274.35  E-value: 6.23e-86
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564399494  223 DHNFFLLFSVIDENLSWHLDDNIATYCSDPASVDKEDGPFQDSNRMHAINGFVFGNLPELSMCAQKHVAWHLFGMGNEID 302
Cdd:cd11021     1 DREFVLMFSVVDENLSWYLDENIKTYCSEPAKVDKDDEDFQESNKMHSINGYTFGNLPGLSMCAGDRVKWHLFGMGNEVD 80

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 564399494  303 VHTAFFHGQTLSIRGHRTDVAHIFPATFVTAEMVPQKSGTWLISCVVNSHLKSGMQAFYKV 363
Cdd:cd11021    81 IHSAFFHGQTLTDRGHRTDTINLFPATFVTAEMVAQNPGKWLLSCQVNDHLKAGMQAFYEV 141
CuRO_4_ceruloplasmin cd11022
The fourth cupredoxin domain of Ceruloplasmin; Ceruloplasmin is a multicopper oxidase ...
 574-717 6.42e-81

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: 260.49  E-value: 6.42e-81
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564399494  574 DKEFFLLFTIFDENESWYNNANQAAGMLDSRLLSEDVEGFEDSNRMHAINGFLFSNLPRLDICKGDTVAWHLLGLGTEND 653
Cdd:cd11022     1 DKEFFLLFTVFDENESWYLDENIQQFTLDPRSVDKEDEDFQESNKMHSINGYMYGNQPGLDMCKGDTVSWHLFGLGTETD 80

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 564399494  654 VHGVMFEGNTLQLQGMRKSAAMLFPHTFVTAIMQPDNPGIFEIYCQAGSHREAGMQAIYNVSQC 717
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 ...
 26-208 3.26e-76

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: 248.86  E-value: 3.26e-76
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564399494   26 RNYYLGIQDIQWNYAPKGRNVITNQTLNndtvasSFLKSGKNRIGGTYKKTVYKEYSDGTYTNEIAKPAWLGFLGPLLKA 105
Cdd:cd04199     1 RHYYIAAEEIDWDYAPSGLAEKDLSYRN------QYLDNGPFRIGRSYKKVVYREYTDESFTTPGPQPEHLGILGPTIRA 74

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564399494  106 EMGDVILIHLKNFASRPYTIHPHGVFYEKDSEGSLYPDGSSGYLKADDSVPPGGSHVYNWSIPEGHAPTEADPACLTWIY 185
Cdd:cd04199    75 EVGDTIKVHFKNKASRPYSIHPHGVSYEKDSEGASYSDQTGPDEKKDDAVAPGETYTYVWIVTEESGPTKGDPACLTWAY 154

                         170       180
                  ....*....|....*....|...
gi 564399494  186 HSHVDAPRDIATGLIGPLITCKR 208
Cdd:cd04199   155 YSHVDLEKDINSGLIGPLLICKK 177
CuRO_1_ceruloplasmin_like cd04199
Cupredoxin domains 1, 3, and 5 of ceruloplasmin and similar proteins; This family includes the ...
 732-903 1.46e-68

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: 227.67  E-value: 1.46e-68
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564399494  732 RVYYIMAEEIEWDYCPDRSWELEwyntsekDSYGHVFLSNKDGLLGSKYKKAVFREYTDGTFRIPQPRsgpEEHLGILGP 811
Cdd:cd04199     1 RHYYIAAEEIDWDYAPSGLAEKD-------LSYRNQYLDNGPFRIGRSYKKVVYREYTDESFTTPGPQ---PEHLGILGP 70

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564399494  812 LIRGEVGDILTVVFKNKASRPYSIHAHGV-----LESSTGWPQAAE---------PGEVLTYQWNIPERSGPGPSDSACV 877
Cdd:cd04199    71 TIRAEVGDTIKVHFKNKASRPYSIHPHGVsyekdSEGASYSDQTGPdekkddavaPGETYTYVWIVTEESGPTKGDPACL 150

                         170       180
                  ....*....|....*....|....*.
gi 564399494  878 SWIYYSAVDPIKDMYSGLVGPLVICR 903
Cdd:cd04199   151 TWAYYSHVDLEKDINSGLIGPLLICK 176
CuRO_3_ceruloplasmin cd04224
The third cupredoxin domain of Ceruloplasmin; Ceruloplasmin is a multicopper oxidase essential ...
 23-214 1.74e-68

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: 228.13  E-value: 1.74e-68
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564399494   23 GAIRNYYLGIQDIQWNYAPKGRNVITNQTLNN-DTVASSFLKSGKNRIGGTYKKTVYKEYSDGTYTNE---IAKPAWLGF 98
Cdd:cd04224     1 GKVRHYFIAAEEIMWDYAPSGKNLFTGQNLTApGSDSEVFFQRNETRIGGTYWKVRYVEYTDATFTTRkhrSKEEEHLGI 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564399494   99 LGPLLKAEMGDVILIHLKNFASRPYTIHPHGVFYEKDSEGSLYPDGSSgylKADDSVPPGGSHVYNWSIPEGHAPTEADP 178
Cdd:cd04224    81 LGPVIRAEVGDTIKVTFRNKASRPFSIQPHGVFYEKNYEGAMYRDGDP---SPGSHVSPGETFTYEWTVPEGVGPTNQDP 157

                         170       180       190
                  ....*....|....*....|....*....|....*.
gi 564399494  179 ACLTWIYHSHVDAPRDIATGLIGPLITCKRGTLDGN 214
Cdd:cd04224   158 PCLTYLYFSAVDPVRDTNSGLVGPLLVCKKGSLNAN 193
CuRO_3_ceruloplasmin cd04224
The third cupredoxin domain of Ceruloplasmin; Ceruloplasmin is a multicopper oxidase essential ...
 732-911 1.69e-66

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: 222.35  E-value: 1.69e-66
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564399494  732 RVYYIMAEEIEWDYCPDRSWELEWYNTSEKDSYGHVFLSNKDGLLGSKYKKAVFREYTDGTFRIPQPRSGPEEHLGILGP 811
Cdd:cd04224     4 RHYFIAAEEIMWDYAPSGKNLFTGQNLTAPGSDSEVFFQRNETRIGGTYWKVRYVEYTDATFTTRKHRSKEEEHLGILGP 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564399494  812 LIRGEVGDILTVVFKNKASRPYSIHAHGVL----------ESSTGWPQA-AEPGEVLTYQWNIPERSGPGPSDSACVSWI 880
Cdd:cd04224    84 VIRAEVGDTIKVTFRNKASRPFSIQPHGVFyeknyegamyRDGDPSPGShVSPGETFTYEWTVPEGVGPTNQDPPCLTYL 163

                         170       180       190
                  ....*....|....*....|....*....|.
gi 564399494  881 YYSAVDPIKDMYSGLVGPLVICRNGILEPNG 911
Cdd:cd04224   164 YFSAVDPVRDTNSGLVGPLLVCKKGSLNANG 194
CuRO_6_ceruloplasmin cd11012
The sixth cupredoxin domain of Ceruloplasmin; Ceruloplasmin is a multicopper oxidase essential ...
 919-1062 8.83e-65

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: 215.50  E-value: 8.83e-65
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564399494  919 EFALLFLIFDENQSWYLKENIATYGpQETSHVNLQDATFLESNKMHAINGKLYANLRGLTVYQGERVAWYMLAMGQDTDI 998
Cdd:cd11012     3 EFALLFLVFDENESWYLDENIKTYS-DHPEKVNKEDEEFIESNKMHAINGKVFGNLQGLTMHVGDEVYWYLMGMGNEIDI 81

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 564399494  999 HTVHFHAESFLYQNGHSYRADVVDLFPGTFEVVEMVASNPGAWLMHCHVTDHVHAGMETIFTVL 1062
Cdd:cd11012    82 HTAHFHGHSFDYKHRGVYRSDVFDLFPGTFQTVEMIPRTPGTWLLHCHVTDHIHAGMETTYTVL 145
CuRO_1_ceruloplasmin_like cd04199
Cupredoxin domains 1, 3, and 5 of ceruloplasmin and similar proteins; This family includes the ...
 380-561 1.02e-64

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


Pssm-ID: 259862 [Multi-domain]  Cd Length: 177  Bit Score: 216.50  E-value: 1.02e-64
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564399494  380 RQYFIQAHEIQWDYGPIGhdgrTGKSLREPGSgpdKYFQKSSSRIGGTYWKVRYEAFQDETFQERLHQEEetHLGILGPV 459
Cdd:cd04199     1 RHYYIAAEEIDWDYAPSG----LAEKDLSYRN---QYLDNGPFRIGRSYKKVVYREYTDESFTTPGPQPE--HLGILGPT 71

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564399494  460 IRAEVGDTIQVVFYNRASQPFSIQPHGVFYEKSSEGTVYNDGTSYPKVAKSF----EKVTYYWTVPPHAGPTAEDPACLT 535
Cdd:cd04199    72 IRAEVGDTIKVHFKNKASRPYSIHPHGVSYEKDSEGASYSDQTGPDEKKDDAvapgETYTYVWIVTEESGPTKGDPACLT 151

                         170       180
                  ....*....|....*....|....*.
gi 564399494  536 WMYFSAADPTRDTNSGLVGPLLVCKA 561
Cdd:cd04199   152 WAYYSHVDLEKDINSGLIGPLLICKK 177
CuRO_2_ceruloplasmin_like cd04200
Cupredoxin domains 2, 4, and 6 of ceruloplasmin and similar proteins; This family includes the ...
 223-363 2.84e-64

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: 213.81  E-value: 2.84e-64
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564399494  223 DHNFFLLFSVIDENLSWHLDDNIATYCSDPASVDKEDGPFQDSNRMHAINGFVFGNLPELSMCAQKHVAWHLFGMGNEID 302
Cdd:cd04200     1 DKEFVLLFAVFDENKSWYLEDNIKRFCDNPEKVDKDDEEFQESNKMHAINGYVFGNLPGLTMCAGDRVRWHLLGMGNEVD 80

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 564399494  303 VHTAFFHGQTLSIRGHRTDVAHIFPATFVTAEMVPQKSGTWLISCVVNSHLKSGMQAFYKV 363
Cdd:cd04200    81 VHSIHFHGQTFLYKGYRIDTLTLFPATFETVEMVPSNPGTWLLHCHNSDHRHAGMQAYFLV 141
CuRO_4_ceruloplasmin cd11022
The fourth cupredoxin domain of Ceruloplasmin; Ceruloplasmin is a multicopper oxidase ...
 223-366 8.81e-59

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: 198.48  E-value: 8.81e-59
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564399494  223 DHNFFLLFSVIDENLSWHLDDNIATYCSDPASVDKEDGPFQDSNRMHAINGFVFGNLPELSMCAQKHVAWHLFGMGNEID 302
Cdd:cd11022     1 DKEFFLLFTVFDENESWYLDENIQQFTLDPRSVDKEDEDFQESNKMHSINGYMYGNQPGLDMCKGDTVSWHLFGLGTETD 80

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 564399494  303 VHTAFFHGQTLSIRGHRTDVAHIFPATFVTAEMVPQKSGTWLISCVVNSHLKSGMQAFYKVDSC 366
Cdd:cd11022    81 VHGIYFSGNTFLLQGTRRDTANLFPHTSVTAIMQPDNEGTFEVNCQTTDHYSAGMRQIYTVSQC 144
CuRO_2_ceruloplasmin_like cd04200
Cupredoxin domains 2, 4, and 6 of ceruloplasmin and similar proteins; This family includes the ...
 917-1061 9.75e-57

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


Pssm-ID: 259863 [Multi-domain]  Cd Length: 141  Bit Score: 192.62  E-value: 9.75e-57
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564399494  917 DREFALLFLIFDENQSWYLKENIATYGPqETSHVNLQDATFLESNKMHAINGKLYANLRGLTVYQGERVAWYMLAMGQDT 996
Cdd:cd04200     1 DKEFVLLFAVFDENKSWYLEDNIKRFCD-NPEKVDKDDEEFQESNKMHAINGYVFGNLPGLTMCAGDRVRWHLLGMGNEV 79

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 564399494  997 DIHTVHFHAESFLYQNghsYRADVVDLFPGTFEVVEMVASNPGAWLMHCHVTDHVHAGMETIFTV 1061
Cdd:cd04200    80 DVHSIHFHGQTFLYKG---YRIDTLTLFPATFETVEMVPSNPGTWLLHCHNSDHRHAGMQAYFLV 141
CuRO_5_FV_like cd14451
The fifth cupredoxin domain of coagulation factor V and similar proteins; Factor V is an ...
 732-905 9.81e-57

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


Pssm-ID: 259993 [Multi-domain]  Cd Length: 173  Bit Score: 193.90  E-value: 9.81e-57
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564399494  732 RVYYIMAEEIEWDYCPDRSWELEwYNTSEKDSyghvflsnkdgllgsKYKKAVFREYTDGTFRIPQPRSGPEEHLGILGP 811
Cdd:cd14451     2 RRYYIAAEEEEWDYAGYGKSRLD-KTQNERDT---------------VFKKVVFRRYLDSTFSTPDIQGEYEEHLGILGP 65

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564399494  812 LIRGEVGDILTVVFKNKASRPYSIHAHGV--LESSTG---------W---PQAAEPGEVLTYQWNIPERSGPGPSDSACV 877
Cdd:cd14451    66 VIRAEVDDVIQVFFKNLASRPYSLHAHGLsyEKSSEGlsyddespdWfkkDDAVQPNGTYTYVWYANPRSGPENNGSDCR 145

                         170       180
                  ....*....|....*....|....*...
gi 564399494  878 SWIYYSAVDPIKDMYSGLVGPLVICRNG 905
Cdd:cd14451   146 TWAYYSAVNPEKDIHSGLIGPLLICRKG 173
CuRO_5_FV_like cd14451
The fifth cupredoxin domain of coagulation factor V and similar proteins; Factor V is an ...
 380-562 2.17e-55

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: 190.05  E-value: 2.17e-55
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564399494  380 RQYFIQAHEIQWDYGPIGHDGRTGKSLREPGsgpdkyfqksssriggTYWKVRYEAFQDETFQERLHQ-EEETHLGILGP 458
Cdd:cd14451     2 RRYYIAAEEEEWDYAGYGKSRLDKTQNERDT----------------VFKKVVFRRYLDSTFSTPDIQgEYEEHLGILGP 65

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564399494  459 VIRAEVGDTIQVVFYNRASQPFSIQPHGVFYEKSSEGTVYNDGTSY----PKVAKSFEKVTYYWTVPPHAGPTAEDPACL 534
Cdd:cd14451    66 VIRAEVDDVIQVFFKNLASRPYSLHAHGLSYEKSSEGLSYDDESPDwfkkDDAVQPNGTYTYVWYANPRSGPENNGSDCR 145

                         170       180
                  ....*....|....*....|....*...
gi 564399494  535 TWMYFSAADPTRDTNSGLVGPLLVCKAG 562
Cdd:cd14451   146 TWAYYSAVNPEKDIHSGLIGPLLICRKG 173
CuRO_1_FV_like cd04226
The first cupredoxin domain of coagulation factor VIII and similar proteins; Factor V is an ...
 26-209 6.06e-55

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: 188.53  E-value: 6.06e-55
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564399494   26 RNYYLGIQDIQWNYAPKgrnvitnqtlnndtvaSSFLKSgkNRIGGTYKKTVYKEYSDGtYTNEIAKPAWLGFLGPLLKA 105
Cdd:cd04226     1 REYYIAAQNIDWDYTPQ----------------SEELRL--KRSEQSFKKIVYREYEEG-FKKEKPADLSSGLLGPTLRA 61

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564399494  106 EMGDVILIHLKNFASRPYTIHPHGVFYEKDSEGSLYPDGSSGYLKADDSVPPGGSHVYNWSIPEGHAPTEADPACLTWIY 185
Cdd:cd04226    62 EVGDTLIVHFKNMADKPLSIHPQGIAYGKKSEGSLYSDNTSPVEKLDDAVQPGQEYTYVWDITEEVGPTEADPPCLTYIY 141

                         170       180
                  ....*....|....*....|....
gi 564399494  186 HSHVDAPRDIATGLIGPLITCKRG 209
Cdd:cd04226   142 YSHVNMVRDFNSGLIGALLICKKG 165
CuRO_1_Ceruloplasmin_like_1 cd04229
cupredoxin domain of ceruloplasmin homologs; Uncharacterized subfamily of ceruloplasmin ...
 26-209 7.55e-54

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


Pssm-ID: 259891 [Multi-domain]  Cd Length: 175  Bit Score: 185.70  E-value: 7.55e-54
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564399494   26 RNYYLGIQDIQWNYAPKGRNVIT-NQTLNNDTVASSflkSGKNRIGGTYKKTVYKEYSDGTYTNEIAKPAWLGFLGPLLK 104
Cdd:cd04229     1 RTYYIAAEEVDWDYAPSGKNKCClGDDLEVSTLDSQ---PGPYTIGSTYTKARYREYTDNSFSTPKPTPAYLGILGPVIR 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564399494  105 AEMGDVILIHLKN-FASRPYTIHPHGVFYEKDSEGSLYpdgssgylKADDSVPPGGSHVYNWSIPEGHAPTEADPACLTW 183
Cdd:cd04229    78 AEVGDTIKVVFKNnLDEFPVNMHPHGGLYSKDNEGTTD--------GAGDVVAPGETYTYRWIVPEDAGPGPGDPSSRLW 149

                         170       180
                  ....*....|....*....|....*.
gi 564399494  184 IYHSHVDAPRDIATGLIGPLITCKRG 209
Cdd:cd04229   150 LYHSHVDVFAHTNAGLVGPIIVTSKG 175
CuRO_5_FV_like cd14451
The fifth cupredoxin domain of coagulation factor V and similar proteins; Factor V is an ...
 26-209 1.16e-53

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


Pssm-ID: 259993 [Multi-domain]  Cd Length: 173  Bit Score: 185.04  E-value: 1.16e-53
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564399494   26 RNYYLGIQDIQWNYAPKGRNVITNQTLNNDTVassflksgknriggtYKKTVYKEYSDGTYTNEIAKPAW---LGFLGPL 102
Cdd:cd14451     2 RRYYIAAEEEEWDYAGYGKSRLDKTQNERDTV---------------FKKVVFRRYLDSTFSTPDIQGEYeehLGILGPV 66

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564399494  103 LKAEMGDVILIHLKNFASRPYTIHPHGVFYEKDSEGSLYPDGSSGYLKADDSVPPGGSHVYNWSIPEGHAPTEADPACLT 182
Cdd:cd14451    67 IRAEVDDVIQVFFKNLASRPYSLHAHGLSYEKSSEGLSYDDESPDWFKKDDAVQPNGTYTYVWYANPRSGPENNGSDCRT 146

                         170       180
                  ....*....|....*....|....*..
gi 564399494  183 WIYHSHVDAPRDIATGLIGPLITCKRG 209
Cdd:cd14451   147 WAYYSAVNPEKDIHSGLIGPLLICRKG 173
CuRO_3_FV_like cd14450
The third cupredoxin domain of coagulation factor V and similar proteins; Factor V is an ...
 28-207 4.94e-53

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: 183.54  E-value: 4.94e-53
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564399494   28 YYLGIQDIQWNYAPkgrNVITNQtlnNDTVASSFLKSGKNRIGGTYKKTVYKEYSDGTYTN--EIAKPAWLGFLGPLLKA 105
Cdd:cd14450     5 YFIAAEEVIWDYAP---SIPENM---DKRYRSQYLDNFSNNIGKKYKKAVFTQYEDGSFTKrlENPRPKEEGILGPVIRA 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564399494  106 EMGDVILIHLKNFASRPYTIHPHGVFYEKDSEGSLYPDGSSGYLKADDSVPPGGSHVYNWSIPEGHAPTEADPACLTWIY 185
Cdd:cd14450    79 QVRDTIKIVFKNKASRPYSIYPHGVTVSKAAEGASYPPDPRGNETQNKAVQPGETYTYKWNILETDEPTARDPRCLTRMY 158

                         170       180
                  ....*....|....*....|..
gi 564399494  186 HSHVDAPRDIATGLIGPLITCK 207
Cdd:cd14450   159 HSAVDITRDIASGLIGPLLICK 180
CuRO_1_FVIII_like cd14452
The first cupredoxin domain of coagulation factor VIII and similar proteins; Factor VIII ...
 26-209 5.53e-52

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: 180.17  E-value: 5.53e-52
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564399494   26 RNYYLGIQDIQWNYapkgrnvitnqTLNNDTVASSFLKSGKNRIGGTYKKTVYKEYSDGTYTNEIAKPAWLGFLGPLLKA 105
Cdd:cd14452     1 RRYYIAAVEIGWDY-----------IHSDLGDPASEQRKKPKDIPQKYIKAVFVEYLDATFTVPKPRPAWMGLLGPTIVA 69

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564399494  106 EMGDVILIHLKNFASRPYTIHPHGVFYEKDSEGSLYPDGSSGYLKADDSVPPGGSHVYNWSIPEGHAPTEADPACLTWIY 185
Cdd:cd14452    70 EVGDTVVITFKNLASQPYSLHAVGVSYWKASEGAGYDDSTSQHEKEDDAVYPGGYHTYVWDISPKDGPTGSDPECLTYSY 149

                         170       180
                  ....*....|....*....|....
gi 564399494  186 HSHVDAPRDIATGLIGPLITCKRG 209
Cdd:cd14452   150 SSQVDPVKDVNSGLIGALLVCRMG 173
CuRO_3_FV_like cd14450
The third cupredoxin domain of coagulation factor V and similar proteins; Factor V is an ...
 734-903 2.31e-51

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: 178.92  E-value: 2.31e-51
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564399494  734 YYIMAEEIEWDYCPDRSwelewynTSEKDSYGHVFLSNKDGLLGSKYKKAVFREYTDGTFRIPQPRSGPEEhLGILGPLI 813
Cdd:cd14450     5 YFIAAEEVIWDYAPSIP-------ENMDKRYRSQYLDNFSNNIGKKYKKAVFTQYEDGSFTKRLENPRPKE-EGILGPVI 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564399494  814 RGEVGDILTVVFKNKASRPYSIHAHGVL----ESSTGWP----------QAAEPGEVLTYQWNIPERSGPGPSDSACVSW 879
Cdd:cd14450    77 RAQVRDTIKIVFKNKASRPYSIYPHGVTvskaAEGASYPpdprgnetqnKAVQPGETYTYKWNILETDEPTARDPRCLTR 156

                         170       180
                  ....*....|....*....|....
gi 564399494  880 IYYSAVDPIKDMYSGLVGPLVICR 903
Cdd:cd14450   157 MYHSAVDITRDIASGLIGPLLICK 180
CuRO_2_ceruloplasmin cd11021
The second cupredoxin domain of Ceruloplasmin; Ceruloplasmin is a multicopper oxidase ...
 917-1061 3.29e-51

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: 176.89  E-value: 3.29e-51
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564399494  917 DREFALLFLIFDENQSWYLKENIATYGpQETSHVNLQDATFLESNKMHAINGKLYANLRGLTVYQGERVAWYMLAMGQDT 996
Cdd:cd11021     1 DREFVLMFSVVDENLSWYLDENIKTYC-SEPAKVDKDDEDFQESNKMHSINGYTFGNLPGLSMCAGDRVKWHLFGMGNEV 79

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 564399494  997 DIHTVHFHAESFLYQNghsYRADVVDLFPGTFEVVEMVASNPGAWLMHCHVTDHVHAGMETIFTV 1061
Cdd:cd11021    80 DIHSAFFHGQTLTDRG---HRTDTINLFPATFVTAEMVAQNPGKWLLSCQVNDHLKAGMQAFYEV 141
CuRO_1_ceruloplasmin cd04222
The first cupredoxin domain of Ceruloplasmin; Ceruloplasmin is a multicopper oxidase essential ...
 732-903 5.38e-51

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: 177.61  E-value: 5.38e-51
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564399494  732 RVYYIMAEEIEWDYCPDRSwELEWYNTSEKDSYGHVFLSNKDGLLGSKYKKAVFREYTDGTFR--IPQPrsgpeEHLGIL 809
Cdd:cd04222     1 REYYIGIRETQWDYAPSGK-NLITNQTFDDDEHASVFLKRGPDRIGRVYKKAVYLQYTDDTYRteIEKP-----VWLGFL 74

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564399494  810 GPLIRGEVGDILTVVFKNKASRPYSIHAHGVL-----------ESSTGWPQ---AAEPGEVLTYQWNIPERSGPGPSDSA 875
Cdd:cd04222    75 GPILKAEVGDVIVVHLKNFASRPYSLHPHGVFynkenegalypDNTSGFEKaddAVPPGGSYTYTWTVPEEQAPTKADAN 154

                         170       180
                  ....*....|....*....|....*...
gi 564399494  876 CVSWIYYSAVDPIKDMYSGLVGPLVICR 903
Cdd:cd04222   155 CLTRIYHSHIDAPKDIASGLIGPLIICK 182
CuRO_1_ceruloplasmin cd04222
The first cupredoxin domain of Ceruloplasmin; Ceruloplasmin is a multicopper oxidase essential ...
 380-560 8.90e-51

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: 177.23  E-value: 8.90e-51
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564399494  380 RQYFIQAHEIQWDYGPIGHDGRTGKSLREpgsgpDK----YFQKSSSRIGGTYWKVRYEAFQDETFQERLhqEEETHLGI 455
Cdd:cd04222     1 REYYIGIRETQWDYAPSGKNLITNQTFDD-----DEhasvFLKRGPDRIGRVYKKAVYLQYTDDTYRTEI--EKPVWLGF 73

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564399494  456 LGPVIRAEVGDTIQVVFYNRASQPFSIQPHGVFYEKSSEGTVYNDGTSypKVAKSFEKV------TYYWTVPPHAGPTAE 529
Cdd:cd04222    74 LGPILKAEVGDVIVVHLKNFASRPYSLHPHGVFYNKENEGALYPDNTS--GFEKADDAVppggsyTYTWTVPEEQAPTKA 151

                         170       180       190
                  ....*....|....*....|....*....|.
gi 564399494  530 DPACLTWMYFSAADPTRDTNSGLVGPLLVCK 560
Cdd:cd04222   152 DANCLTRIYHSHIDAPKDIASGLIGPLIICK 182
CuRO_3_FV_like cd14450
The third cupredoxin domain of coagulation factor V and similar proteins; Factor V is an ...
 378-561 2.25e-50

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: 175.84  E-value: 2.25e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564399494  378 KVRQYFIQAHEIQWDYGPIGHDGRTGKSlrepgsgPDKYFQKSSSRIGGTYWKVRYEAFQDETFQERLHQEEETHLGILG 457
Cdd:cd14450     1 KNWEYFIAAEEVIWDYAPSIPENMDKRY-------RSQYLDNFSNNIGKKYKKAVFTQYEDGSFTKRLENPRPKEEGILG 73

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564399494  458 PVIRAEVGDTIQVVFYNRASQPFSIQPHGVFYEKSSEGTVY----NDGTSYPKVAKSFEKVTYYWTVPPHAGPTAEDPAC 533
Cdd:cd14450    74 PVIRAQVRDTIKIVFKNKASRPYSIYPHGVTVSKAAEGASYppdpRGNETQNKAVQPGETYTYKWNILETDEPTARDPRC 153

                         170       180
                  ....*....|....*....|....*...
gi 564399494  534 LTWMYFSAADPTRDTNSGLVGPLLVCKA 561
Cdd:cd14450   154 LTRMYHSAVDITRDIASGLIGPLLICKS 181
CuRO_1_Ceruloplasmin_like_1 cd04229
cupredoxin domain of ceruloplasmin homologs; Uncharacterized subfamily of ceruloplasmin ...
 380-562 9.72e-50

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


Pssm-ID: 259891 [Multi-domain]  Cd Length: 175  Bit Score: 173.76  E-value: 9.72e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564399494  380 RQYFIQAHEIQWDYGPIGHDGRTGKSLREPGSGpdkYFQKSSSRIGGTYWKVRYEAFQDETFQERLHQEEetHLGILGPV 459
Cdd:cd04229     1 RTYYIAAEEVDWDYAPSGKNKCCLGDDLEVSTL---DSQPGPYTIGSTYTKARYREYTDNSFSTPKPTPA--YLGILGPV 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564399494  460 IRAEVGDTIQVVFYNRASQ-PFSIQPHGVFYEKSSEGTvyNDGTSypKVAKSFEKVTYYWTVPPHAGPTAEDPACLTWMY 538
Cdd:cd04229    76 IRAEVGDTIKVVFKNNLDEfPVNMHPHGGLYSKDNEGT--TDGAG--DVVAPGETYTYRWIVPEDAGPGPGDPSSRLWLY 151

                         170       180
                  ....*....|....*....|....
gi 564399494  539 FSAADPTRDTNSGLVGPLLVCKAG 562
Cdd:cd04229   152 HSHVDVFAHTNAGLVGPIIVTSKG 175
CuRO_1_Ceruloplasmin_like_1 cd04229
cupredoxin domain of ceruloplasmin homologs; Uncharacterized subfamily of ceruloplasmin ...
 732-905 1.04e-48

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: 171.06  E-value: 1.04e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564399494  732 RVYYIMAEEIEWDY---------CPDRSW-ELEWyntSEKDSYGhvflsnkdglLGSKYKKAVFREYTDGTFRIPQPRsg 801
Cdd:cd04229     1 RTYYIAAEEVDWDYapsgknkccLGDDLEvSTLD---SQPGPYT----------IGSTYTKARYREYTDNSFSTPKPT-- 65

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564399494  802 pEEHLGILGPLIRGEVGDILTVVFKNKASR-PYSIHAHGVLESSTGWPQAAE------PGEVLTYQWNIPERSGPGPSDS 874
Cdd:cd04229    66 -PAYLGILGPVIRAEVGDTIKVVFKNNLDEfPVNMHPHGGLYSKDNEGTTDGagdvvaPGETYTYRWIVPEDAGPGPGDP 144

                         170       180       190
                  ....*....|....*....|....*....|.
gi 564399494  875 ACVSWIYYSAVDPIKDMYSGLVGPLVICRNG 905
Cdd:cd04229   145 SSRLWLYHSHVDVFAHTNAGLVGPIIVTSKG 175
CuRO_5_ceruloplasmin cd04225
The fifth cupredoxin domain of Ceruloplasmin; Ceruloplasmin is a multicopper oxidase essential ...
 380-560 6.38e-48

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: 168.41  E-value: 6.38e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564399494  380 RQYFIQAHEIQWDYGPIGHDGRTGKSLREPGSGpDKYFQKSSSRIGGTYWKVRYEAFQDETF---QERlhQEEETHLGIL 456
Cdd:cd04225     1 RTYYIAAEEVEWDYSPQRTWEQELHNTHEESPG-NAFLNKGDKFIGSKYKKVVYREYTDDTFsvpKER--TAEEEHLGIL 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564399494  457 GPVIRAEVGDTIQVVFYNRASQPFSIQPHGVfyeKSSegtvyndgTSYPKVAKSFEKVTYYWTVPPHAGPTAEDPACLTW 536
Cdd:cd04225    78 GPLIHAEVGEKVKIVFKNMASRPYSIHAHGV---KTD--------SSWVAPTEPGETQTYTWKIPERSGPGVEDSNCISW 146

                         170       180
                  ....*....|....*....|....
gi 564399494  537 MYFSAADPTRDTNSGLVGPLLVCK 560
Cdd:cd04225   147 AYYSTVDQIKDLYSGLIGPLVICR 170
CuRO_2_ceruloplasmin cd11021
The second cupredoxin domain of Ceruloplasmin; Ceruloplasmin is a multicopper oxidase ...
 574-714 9.97e-48

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: 166.88  E-value: 9.97e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564399494  574 DKEFFLLFTIFDENESWYNNANQAAGMLDSRLLSEDVEGFEDSNRMHAINGFLFSNLPRLDICKGDTVAWHLLGLGTEND 653
Cdd:cd11021     1 DREFVLMFSVVDENLSWYLDENIKTYCSEPAKVDKDDEDFQESNKMHSINGYTFGNLPGLSMCAGDRVKWHLFGMGNEVD 80

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 564399494  654 VHGVMFEGNTLQLQGMRKSAAMLFPHTFVTAIMQPDNPGIFEIYCQAGSHREAGMQAIYNV 714
Cdd:cd11021    81 IHSAFFHGQTLTDRGHRTDTINLFPATFVTAEMVAQNPGKWLLSCQVNDHLKAGMQAFYEV 141
CuRO_5_FVIII_like cd04228
The fifth cupredoxin domain of coagulation factor VIII and similar proteins; Factor VIII ...
 732-905 2.11e-47

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: 166.99  E-value: 2.11e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564399494  732 RVYYIMAEEIEWDYCPDRSWELEWYNTSEKDSYGHVflsnkdgllgSKYKKAVFREYTDGTFRIPQPRSGPEEHLGILGP 811
Cdd:cd04228     2 RHYFIAAVEVLWDYGMQRPQHFLRARDPNRGRRKSV----------PQYKKVVFREYLDGSFTQPVYRGELDEHLGILGP 71

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564399494  812 LIRGEVGDILTVVFKNKASRPYSIHAHGVLESSTGWP----QAAEPGEVLTYQWNIPERSGPGPSDSACVSWIYYSAVDP 887
Cdd:cd04228    72 YIRAEVEDNIMVTFKNLASRPYSFHSSLISYEEDQRAeprgNFVQPGEVQTYSWKVLHQMAPTKQEFDCKAWAYFSNVDL 151

                         170
                  ....*....|....*...
gi 564399494  888 IKDMYSGLVGPLVICRNG 905
Cdd:cd04228   152 EKDLHSGLIGPLIICKTG 169
CuRO_6_ceruloplasmin cd11012
The sixth cupredoxin domain of Ceruloplasmin; Ceruloplasmin is a multicopper oxidase essential ...
 226-363 3.48e-46

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: 162.35  E-value: 3.48e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564399494  226 FFLLFSVIDENLSWHLDDNIATYCSDPASVDKEDGPFQDSNRMHAINGFVFGNLPELSMCAQKHVAWHLFGMGNEIDVHT 305
Cdd:cd11012     4 FALLFLVFDENESWYLDENIKTYSDHPEKVNKEDEEFIESNKMHAINGKVFGNLQGLTMHVGDEVYWYLMGMGNEIDIHT 83

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 564399494  306 AFFHGQTLSIR---GHRTDVAHIFPATFVTAEMVPQKSGTWLISCVVNSHLKSGMQAFYKV 363
Cdd:cd11012    84 AHFHGHSFDYKhrgVYRSDVFDLFPGTFQTVEMIPRTPGTWLLHCHVTDHIHAGMETTYTV 144
CuRO_4_ceruloplasmin cd11022
The fourth cupredoxin domain of Ceruloplasmin; Ceruloplasmin is a multicopper oxidase ...
 917-1061 9.70e-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: 158.41  E-value: 9.70e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564399494  917 DREFALLFLIFDENQSWYLKENIATYGPQETShVNLQDATFLESNKMHAINGKLYANLRGLTVYQGERVAWYMLAMGQDT 996
Cdd:cd11022     1 DKEFFLLFTVFDENESWYLDENIQQFTLDPRS-VDKEDEDFQESNKMHSINGYMYGNQPGLDMCKGDTVSWHLFGLGTET 79

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 564399494  997 DIHTVHFHAESFLYQnghSYRADVVDLFPGTFEVVEMVASNPGAWLMHCHVTDHVHAGMETIFTV 1061
Cdd:cd11022    80 DVHGIYFSGNTFLLQ---GTRRDTANLFPHTSVTAIMQPDNEGTFEVNCQTTDHYSAGMRQIYTV 141
CuRO_3_FVIII_like cd04227
The third cupredoxin domain of coagulation factor VIII and similar proteins; Factor VIII ...
 733-904 1.52e-44

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


Pssm-ID: 259889 [Multi-domain]  Cd Length: 177  Bit Score: 158.94  E-value: 1.52e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564399494  733 VYYIMAEEIEWDYCPDRSwelewynTSEKDSYGHVFLSNKDGLLGSKYKKAVFREYTDGTFRipqPRSGPEEHLGILGPL 812
Cdd:cd04227     4 EHYIAAEELDWDYAPLLS-------STDDRELQSRYLPTGPQRIGYKYKKVAFVEYTDKTFK---RREAKQTEKGILGPL 73

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564399494  813 IRGEVGDILTVVFKNKASRPYSIHAHGV-----LESSTgwPQAAE---------PGEVLTYQWNIPERSGPGPSDSACVS 878
Cdd:cd04227    74 LKGEVGDQIHIMFKNTASRPYNIYPHGLtsvrpMYRSR--NPAGEkdlktmpigPGETFGYMWELTAEDGPTEEDPRCLT 151

                         170       180
                  ....*....|....*....|....*.
gi 564399494  879 WIYYSAVDPIKDMYSGLVGPLVICRN 904
Cdd:cd04227   152 RLYQSTVDPERDLASGLIGPLLICKK 177
CuRO_2_ceruloplasmin_like cd04200
Cupredoxin domains 2, 4, and 6 of ceruloplasmin and similar proteins; This family includes the ...
 574-714 1.53e-44

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: 157.57  E-value: 1.53e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564399494  574 DKEFFLLFTIFDENESWYNNANQAAGMLDSRLLSEDVEGFEDSNRMHAINGFLFSNLPRLDICKGDTVAWHLLGLGTEND 653
Cdd:cd04200     1 DKEFVLLFAVFDENKSWYLEDNIKRFCDNPEKVDKDDEEFQESNKMHAINGYVFGNLPGLTMCAGDRVRWHLLGMGNEVD 80

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 564399494  654 VHGVMFEGNTLQLQGMRKSAAMLFPHTFVTAIMQPDNPGIFEIYCQAGSHREAGMQAIYNV 714
Cdd:cd04200    81 VHSIHFHGQTFLYKGYRIDTLTLFPATFETVEMVPSNPGTWLLHCHNSDHRHAGMQAYFLV 141
CuRO_5_ceruloplasmin cd04225
The fifth cupredoxin domain of Ceruloplasmin; Ceruloplasmin is a multicopper oxidase essential ...
 26-208 4.02e-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: 157.63  E-value: 4.02e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564399494   26 RNYYLGIQDIQWNYAPKGRNVITNQTLNNDTVASSFLKSGKNRIGGTYKKTVYKEYSDGTYTNEIAKPA---WLGFLGPL 102
Cdd:cd04225     1 RTYYIAAEEVEWDYSPQRTWEQELHNTHEESPGNAFLNKGDKFIGSKYKKVVYREYTDDTFSVPKERTAeeeHLGILGPL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564399494  103 LKAEMGDVILIHLKNFASRPYTIHPHGVfyekdsegslypdgssgylKADDSVP----PGGSHVYNWSIPEGHAPTEADP 178
Cdd:cd04225    81 IHAEVGEKVKIVFKNMASRPYSIHAHGV-------------------KTDSSWVaptePGETQTYTWKIPERSGPGVEDS 141

                         170       180       190
                  ....*....|....*....|....*....|
gi 564399494  179 ACLTWIYHSHVDAPRDIATGLIGPLITCKR 208
Cdd:cd04225   142 NCISWAYYSTVDQIKDLYSGLIGPLVICRR 171
CuRO_1_FV_like cd04226
The first cupredoxin domain of coagulation factor VIII and similar proteins; Factor V is an ...
 380-562 5.21e-43

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: 154.25  E-value: 5.21e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564399494  380 RQYFIQAHEIQWDYGPighdgrtgkslrepgsgpdKYFQKSSSRIGGTYWKVRYEAFQDETFQERLHQEEEthlGILGPV 459
Cdd:cd04226     1 REYYIAAQNIDWDYTP-------------------QSEELRLKRSEQSFKKIVYREYEEGFKKEKPADLSS---GLLGPT 58

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564399494  460 IRAEVGDTIQVVFYNRASQPFSIQPHGVFYEKSSEGTVYNDGTS-YPKVAKSF---EKVTYYWTVPPHAGPTAEDPACLT 535
Cdd:cd04226    59 LRAEVGDTLIVHFKNMADKPLSIHPQGIAYGKKSEGSLYSDNTSpVEKLDDAVqpgQEYTYVWDITEEVGPTEADPPCLT 138

                         170       180
                  ....*....|....*....|....*..
gi 564399494  536 WMYFSAADPTRDTNSGLVGPLLVCKAG 562
Cdd:cd04226   139 YIYYSHVNMVRDFNSGLIGALLICKKG 165
CuRO_5_FVIII_like cd04228
The fifth cupredoxin domain of coagulation factor VIII and similar proteins; Factor VIII ...
 379-562 6.08e-42

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


Pssm-ID: 259890 [Multi-domain]  Cd Length: 169  Bit Score: 151.19  E-value: 6.08e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564399494  379 VRQYFIQAHEIQWDYGpighDGRTGKSLR--EPGSGPDKYFQKsssriggtYWKVRYEAFQDETFQERLHQEE-ETHLGI 455
Cdd:cd04228     1 IRHYFIAAVEVLWDYG----MQRPQHFLRarDPNRGRRKSVPQ--------YKKVVFREYLDGSFTQPVYRGElDEHLGI 68

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564399494  456 LGPVIRAEVGDTIQVVFYNRASQPFSIQPHGVFYEkssegtvyNDGTSYP--KVAKSFEKVTYYWTVPPHAGPTAEDPAC 533
Cdd:cd04228    69 LGPYIRAEVEDNIMVTFKNLASRPYSFHSSLISYE--------EDQRAEPrgNFVQPGEVQTYSWKVLHQMAPTKQEFDC 140

                         170       180
                  ....*....|....*....|....*....
gi 564399494  534 LTWMYFSAADPTRDTNSGLVGPLLVCKAG 562
Cdd:cd04228   141 KAWAYFSNVDLEKDLHSGLIGPLIICKTG 169
CuRO_6_FVIII_like cd11018
The sixth cupredoxin domain of coagulation factor VIII and similar proteins; Factor VIII ...
 918-1061 9.56e-42

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


Pssm-ID: 259904 [Multi-domain]  Cd Length: 144  Bit Score: 149.65  E-value: 9.56e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564399494  918 REFALLFLIFDENQSWYLKENIATYGpQETSHVNLQDATFLESNKMHAINGKLYANLRGLTVYQGERVAWYMLAMGQDTD 997
Cdd:cd11018     2 QEFALLFTIFDETKSWYFEENMRRNC-RPPCHIQTQDPWFHINNKFHAINGYVADTLPGLVMAQHQRIRWHLLNMGSDEE 80

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 564399494  998 IHTVHFHAESFLYQNGHSYRADVVDLFPGTFEVVEMVASNPGAWLMHCHVTDHVHAGMETIFTV 1061
Cdd:cd11018    81 IHSVHFHGLPFTVRAKKEYRMGVYNLYPGVFGTVEMRPSTAGIWLVECTVGEHLLAGMSALFLV 144
CuRO_3_FVIII_like cd04227
The third cupredoxin domain of coagulation factor VIII and similar proteins; Factor VIII ...
 28-208 1.21e-41

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: 150.85  E-value: 1.21e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564399494   28 YYLGIQDIQWNYAPkgrnvITNQTLNNDtVASSFLKSGKNRIGGTYKKTVYKEYSDGTYTNEIAKPAWLGFLGPLLKAEM 107
Cdd:cd04227     5 HYIAAEELDWDYAP-----LLSSTDDRE-LQSRYLPTGPQRIGYKYKKVAFVEYTDKTFKRREAKQTEKGILGPLLKGEV 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564399494  108 GDVILIHLKNFASRPYTIHPHGVFYEKDSEGSLYPDGSSgYLKaDDSVPPGGSHVYNWSIPEGHAPTEADPACLTWIYHS 187
Cdd:cd04227    79 GDQIHIMFKNTASRPYNIYPHGLTSVRPMYRSRNPAGEK-DLK-TMPIGPGETFGYMWELTAEDGPTEEDPRCLTRLYQS 156

                         170       180
                  ....*....|....*....|.
gi 564399494  188 HVDAPRDIATGLIGPLITCKR 208
Cdd:cd04227   157 TVDPERDLASGLIGPLLICKK 177
CuRO_3_FVIII_like cd04227
The third cupredoxin domain of coagulation factor VIII and similar proteins; Factor VIII ...
 378-560 1.70e-41

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: 150.47  E-value: 1.70e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564399494  378 KVRQYFIQAHEIQWDYGPI--GHDGRTGKSLrepgsgpdkYFQKSSSRIGGTYWKVRYEAFQDETFQERLHQEEEThlGI 455
Cdd:cd04227     1 QTWEHYIAAEELDWDYAPLlsSTDDRELQSR---------YLPTGPQRIGYKYKKVAFVEYTDKTFKRREAKQTEK--GI 69

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564399494  456 LGPVIRAEVGDTIQVVFYNRASQPFSIQPHGVF----YEKSSEGTVYNDGTSYPkVAKSfEKVTYYWTVPPHAGPTAEDP 531
Cdd:cd04227    70 LGPLLKGEVGDQIHIMFKNTASRPYNIYPHGLTsvrpMYRSRNPAGEKDLKTMP-IGPG-ETFGYMWELTAEDGPTEEDP 147

                         170       180
                  ....*....|....*....|....*....
gi 564399494  532 ACLTWMYFSAADPTRDTNSGLVGPLLVCK 560
Cdd:cd04227   148 RCLTRLYQSTVDPERDLASGLIGPLLICK 176
CuRO_1_FVIII_like cd14452
The first cupredoxin domain of coagulation factor VIII and similar proteins; Factor VIII ...
 380-562 3.41e-40

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: 146.66  E-value: 3.41e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564399494  380 RQYFIQAHEIQWDYgpighdgrTGKSLREPGSGPDKYfqksSSRIGGTYWKVRYEAFQDETFQerLHQEEETHLGILGPV 459
Cdd:cd14452     1 RRYYIAAVEIGWDY--------IHSDLGDPASEQRKK----PKDIPQKYIKAVFVEYLDATFT--VPKPRPAWMGLLGPT 66

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564399494  460 IRAEVGDTIQVVFYNRASQPFSIQPHGVFYEKSSEGTVYNDGTSYPKvaKSFEKV------TYYWTVPPHAGPTAEDPAC 533
Cdd:cd14452    67 IVAEVGDTVVITFKNLASQPYSLHAVGVSYWKASEGAGYDDSTSQHE--KEDDAVypggyhTYVWDISPKDGPTGSDPEC 144

                         170       180
                  ....*....|....*....|....*....
gi 564399494  534 LTWMYFSAADPTRDTNSGLVGPLLVCKAG 562
Cdd:cd14452   145 LTYSYSSQVDPVKDVNSGLIGALLVCRMG 173
CuRO_1_FVIII_like cd14452
The first cupredoxin domain of coagulation factor VIII and similar proteins; Factor VIII ...
 732-905 2.08e-39

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: 144.35  E-value: 2.08e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564399494  732 RVYYIMAEEIEWDYcpdrswelewynTSEKDSYGHVFLSNKDGLLGSKYKKAVFREYTDGTFRIPQPRSGpeeHLGILGP 811
Cdd:cd14452     1 RRYYIAAVEIGWDY------------IHSDLGDPASEQRKKPKDIPQKYIKAVFVEYLDATFTVPKPRPA---WMGLLGP 65

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564399494  812 LIRGEVGDILTVVFKNKASRPYSIHAHGV----------LESSTGWPQ----AAEPGEVLTYQWNIPERSGPGPSDSACV 877
Cdd:cd14452    66 TIVAEVGDTVVITFKNLASQPYSLHAVGVsywkasegagYDDSTSQHEkeddAVYPGGYHTYVWDISPKDGPTGSDPECL 145

                         170       180
                  ....*....|....*....|....*...
gi 564399494  878 SWIYYSAVDPIKDMYSGLVGPLVICRNG 905
Cdd:cd14452   146 TYSYSSQVDPVKDVNSGLIGALLVCRMG 173
CuRO_1_FV_like cd04226
The first cupredoxin domain of coagulation factor VIII and similar proteins; Factor V is an ...
 732-905 3.38e-39

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: 143.46  E-value: 3.38e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564399494  732 RVYYIMAEEIEWDYCPDrswelewyntSEKDSYGHvflsnkdglLGSKYKKAVFREYTDGtFRIPQPRSgpeEHLGILGP 811
Cdd:cd04226     1 REYYIAAQNIDWDYTPQ----------SEELRLKR---------SEQSFKKIVYREYEEG-FKKEKPAD---LSSGLLGP 57

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564399494  812 LIRGEVGDILTVVFKNKASRPYSIHAHGVLES--STG------------WPQAAEPGEVLTYQWNIPERSGPGPSDSACV 877
Cdd:cd04226    58 TLRAEVGDTLIVHFKNMADKPLSIHPQGIAYGkkSEGslysdntspvekLDDAVQPGQEYTYVWDITEEVGPTEADPPCL 137

                         170       180
                  ....*....|....*....|....*...
gi 564399494  878 SWIYYSAVDPIKDMYSGLVGPLVICRNG 905
Cdd:cd04226   138 TYIYYSHVNMVRDFNSGLIGALLICKKG 165
CuRO_6_FV_like cd14455
The sixth cupredoxin domain of coagulation factor V and similar proteins; Factor V is an ...
 918-1061 1.60e-36

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: 134.61  E-value: 1.60e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564399494  918 REFALLFLIFDENQSWYLKENiatygPQET-SHVNLQDATFLESNKMHAINGKLYaNLRGLTVYQGERVAWYMLAMGQDT 996
Cdd:cd14455     2 REFVLLFMTFDEEKSWYYEKN-----RKRTcRENRVKDPNVQDNHTFHAINGIIY-NLKGLRMYTNELVRWHLINMGGPK 75

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 564399494  997 DIHTVHFHAESFLYQNGHSYRADVVDLFPGTFEVVEMVASNPGAWLMHCHVTDHVHAGMETIFTV 1061
Cdd:cd14455    76 DLHVVHFHGQTFTEKGLKDHQLGVYPLLPGSFATLEMKPSKPGLWLLETEVGESQQRGMQTLFLV 140
CuRO_6_FVIII_like cd11018
The sixth cupredoxin domain of coagulation factor VIII and similar proteins; Factor VIII ...
 226-363 2.60e-35

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: 131.54  E-value: 2.60e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564399494  226 FFLLFSVIDENLSWHLDDNIATYCSDPASVDKEDGPFQDSNRMHAINGFVFGNLPELSMCAQKHVAWHLFGMGNEIDVHT 305
Cdd:cd11018     4 FALLFTIFDETKSWYFEENMRRNCRPPCHIQTQDPWFHINNKFHAINGYVADTLPGLVMAQHQRIRWHLLNMGSDEEIHS 83

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 564399494  306 AFFHGQTLSIRG---HRTDVAHIFPATFVTAEMVPQKSGTWLISCVVNSHLKSGMQAFYKV 363
Cdd:cd11018    84 VHFHGLPFTVRAkkeYRMGVYNLYPGVFGTVEMRPSTAGIWLVECTVGEHLLAGMSALFLV 144
CuRO_5_FVIII_like cd04228
The fifth cupredoxin domain of coagulation factor VIII and similar proteins; Factor VIII ...
 25-209 1.04e-34

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


Pssm-ID: 259890 [Multi-domain]  Cd Length: 169  Bit Score: 130.78  E-value: 1.04e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564399494   25 IRNYYLGIQDIQWNYA-PKGRNVITNQTLNndtvassflkSGKNRIGGTYKKTVYKEYSDGTYTNEIAK---PAWLGFLG 100
Cdd:cd04228     1 IRHYFIAAVEVLWDYGmQRPQHFLRARDPN----------RGRRKSVPQYKKVVFREYLDGSFTQPVYRgelDEHLGILG 70

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564399494  101 PLLKAEMGDVILIHLKNFASRPYTIHPHGVFYEKDsegslypdGSSGYLKadDSVPPGGSHVYNWSIPEGHAPTEADPAC 180
Cdd:cd04228    71 PYIRAEVEDNIMVTFKNLASRPYSFHSSLISYEED--------QRAEPRG--NFVQPGEVQTYSWKVLHQMAPTKQEFDC 140

                         170       180
                  ....*....|....*....|....*....
gi 564399494  181 LTWIYHSHVDAPRDIATGLIGPLITCKRG 209
Cdd:cd04228   141 KAWAYFSNVDLEKDLHSGLIGPLIICKTG 169
CuRO_2_ceruloplasmin_like_2 cd11023
cupredoxin domain of ceruloplasmin homologs; Uncharacterized subfamily of ceruloplasmin ...
 917-1061 1.74e-33

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


Pssm-ID: 259909 [Multi-domain]  Cd Length: 118  Bit Score: 125.03  E-value: 1.74e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564399494  917 DREFALLFLIFDEnqswylkENIAtygpqetshvnlqdatflESNKMHAINGKLYANLRGLTVYQGERVAWYMLAMGQDT 996
Cdd:cd11023     1 DQEFIENSSIFLD-------LNVE------------------EAGLMHSINGYVFGNLPGVTIAKGKRVRWHLVAYGNEV 55

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 564399494  997 DIHTVHFHAESFLyqNGHSYRADVVDLFPGTFEVVEMVASNPGAWLMHCHVTDHVHAGMETIFTV 1061
Cdd:cd11023    56 DFHTPHWHGQTVE--ADKSRRTDVAELMPASMRVADMTAADVGTWLLHCHVHDHYMAGMMTQFAV 118
CuRO_2_FVIII_like cd11015
The second cupredoxin domain of coagulation factor VIII and similar proteins; Factor VIII ...
 224-363 2.03e-32

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


Pssm-ID: 259901 [Multi-domain]  Cd Length: 134  Bit Score: 122.71  E-value: 2.03e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564399494  224 HNFFLLFSVIDENLSWHLDDniatycSDPASVDKEdGPFQDSNRMHAINGFVFGNLPELSMCAQKHVAWHLFGMGNEIDV 303
Cdd:cd11015     2 QAFVLLFAVFDEGKSWYSEV------GERKSRDKF-KRADSRKEFHTINGYINASLPGLKICQRKPVIWHVIGMGTAPEV 74

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 564399494  304 HTAFFHGQTLSIRGHRTDVAHIFPATFVTAEMVPQKSGTWLISCVVNSHLKSGMQAFYKV 363
Cdd:cd11015    75 HSIFFEGHTFLVRTHRKVSLEISPMTFLTAQTKPATVGSFLIFCQIHSHQHDGMEAMVKV 134
CuRO_6_ceruloplasmin cd11012
The sixth cupredoxin domain of Ceruloplasmin; Ceruloplasmin is a multicopper oxidase essential ...
 575-714 5.08e-31

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: 119.20  E-value: 5.08e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564399494  575 KEFFLLFTIFDENESWYNNANQAAGMLDSRLLSEDVEGFEDSNRMHAINGFLFSNLPRLDICKGDTVAWHLLGLGTENDV 654
Cdd:cd11012     2 LEFALLFLVFDENESWYLDENIKTYSDHPEKVNKEDEEFIESNKMHAINGKVFGNLQGLTMHVGDEVYWYLMGMGNEIDI 81

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 564399494  655 HGVMFEGNTLQLQ---GMRKSAAMLFPHTFVTAIMQPDNPGIFEIYCQAGSHREAGMQAIYNV 714
Cdd:cd11012    82 HTAHFHGHSFDYKhrgVYRSDVFDLFPGTFQTVEMIPRTPGTWLLHCHVTDHIHAGMETTYTV 144
CuRO_4_FVIII_like cd11016
The fourth cupredoxin domain of coagulation factor VIII and similar proteins; Factor VIII ...
 223-366 9.70e-31

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


Pssm-ID: 259902 [Multi-domain]  Cd Length: 143  Bit Score: 118.43  E-value: 9.70e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564399494  223 DHNFFLLFSVIDENLSWHLDDNIATYCSDPASVDKEDGPFQDSNRMHAINGFVFGNLpELSMCAQKHVAWHLFGMGNEID 302
Cdd:cd11016     1 DKDWSLLFSVFDENNSWYLKENIHRFTQTPAGVNDTDPDFYASNVMHTINGIVFDRR-QFVICLTDVAYWYVLSVGAQTD 79

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 564399494  303 VHTAFFHGQTLSIRGHRTDVAHIFPATFVTAEMVPQKSGTWLISCvVNSHLKS-GMQAFYKVDSC 366
Cdd:cd11016    80 FLSVFFSGNTFKHQMVYEDVLTLFPFSGETVSMSPEVPGEWELGC-FNGDFRSrGMSAQYTVSTC 143
CuRO_4_FVIII_like cd11016
The fourth cupredoxin domain of coagulation factor VIII and similar proteins; Factor VIII ...
 574-717 6.73e-30

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: 115.74  E-value: 6.73e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564399494  574 DKEFFLLFTIFDENESWYNNAN------QAAGMLDsrllsEDVEgFEDSNRMHAINGFLFSNLpRLDICKGDTVAWHLLG 647
Cdd:cd11016     1 DKDWSLLFSVFDENNSWYLKENihrftqTPAGVND-----TDPD-FYASNVMHTINGIVFDRR-QFVICLTDVAYWYVLS 73

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564399494  648 LGTENDVHGVMFEGNTLQLQGMRKSAAMLFPHTFVTAIMQPDNPGIFEIYCQAGSHREAGMQAIYNVSQC 717
Cdd:cd11016    74 VGAQTDFLSVFFSGNTFKHQMVYEDVLTLFPFSGETVSMSPEVPGEWELGCFNGDFRSRGMSAQYTVSTC 143
CuRO_2_ceruloplasmin_like_2 cd11023
cupredoxin domain of ceruloplasmin homologs; Uncharacterized subfamily of ceruloplasmin ...
 256-363 6.99e-30

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


Pssm-ID: 259909 [Multi-domain]  Cd Length: 118  Bit Score: 115.01  E-value: 6.99e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564399494  256 DKEDGpfQDSNRMHAINGFVFGNLPELSMCAQKHVAWHLFGMGNEIDVHTAFFHGQTLSIRGH-RTDVAHIFPATFVTAE 334
Cdd:cd11023    12 LDLNV--EEAGLMHSINGYVFGNLPGVTIAKGKRVRWHLVAYGNEVDFHTPHWHGQTVEADKSrRTDVAELMPASMRVAD 89

                          90       100
                  ....*....|....*....|....*....
gi 564399494  335 MVPQKSGTWLISCVVNSHLKSGMQAFYKV 363
Cdd:cd11023    90 MTAADVGTWLLHCHVHDHYMAGMMTQFAV 118
CuRO_2_FVIII_like cd11015
The second cupredoxin domain of coagulation factor VIII and similar proteins; Factor VIII ...
 575-714 1.97e-28

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: 111.15  E-value: 1.97e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564399494  575 KEFFLLFTIFDENESWYnnanqaaGMLDSRLLSEDVEGFEDSNRMHAINGFLFSNLPRLDICKGDTVAWHLLGLGTENDV 654
Cdd:cd11015     2 QAFVLLFAVFDEGKSWY-------SEVGERKSRDKFKRADSRKEFHTINGYINASLPGLKICQRKPVIWHVIGMGTAPEV 74

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 564399494  655 HGVMFEGNTLQLQGMRKSAAMLFPHTFVTAIMQPDNPGIFEIYCQAGSHREAGMQAIYNV 714
Cdd:cd11015    75 HSIFFEGHTFLVRTHRKVSLEISPMTFLTAQTKPATVGSFLIFCQIHSHQHDGMEAMVKV 134
CuRO_6_FV_like cd14455
The sixth cupredoxin domain of coagulation factor V and similar proteins; Factor V is an ...
 226-363 1.56e-27

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


Pssm-ID: 259997 [Multi-domain]  Cd Length: 140  Bit Score: 108.80  E-value: 1.56e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564399494  226 FFLLFSVIDENLSWHLDDNIATYCSDPASVDKEdgpFQDSNRMHAINGFVFgNLPELSMCAQKHVAWHLFGMGNEIDVHT 305
Cdd:cd14455     4 FVLLFMTFDEEKSWYYEKNRKRTCRENRVKDPN---VQDNHTFHAINGIIY-NLKGLRMYTNELVRWHLINMGGPKDLHV 79

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 564399494  306 AFFHGQTLSIRG---HRTDVAHIFPATFVTAEMVPQKSGTWLISCVVNSHLKSGMQAFYKV 363
Cdd:cd14455    80 VHFHGQTFTEKGlkdHQLGVYPLLPGSFATLEMKPSKPGLWLLETEVGESQQRGMQTLFLV 140
CuRO_2_FV_like cd14453
The second cupredoxin domain of coagulation factor V and similar proteins; Factor V is an ...
 223-363 3.75e-27

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: 107.25  E-value: 3.75e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564399494  223 DHNFFLLFSVIDENLSWHLDDNiatycsdpasvdkedgpfQDSNRMHAINGFVFGNLPELSMCAQKHVAWHLFGMGNEID 302
Cdd:cd14453     1 YKEYVLMFGVFDENKSWYKQNA------------------SVDSVKYTINGYTNGTLPDVSICAYDHVSWHLLGMSSEPE 62

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 564399494  303 VHTAFFHGQTLSIRGHRTDVAHIFPATFVTAEMVPQKSGTWLISCVVNSHLKSGMQAFYKV 363
Cdd:cd14453    63 LFSVHFNGQVLEQNGHKVSAVGLVSGSSTTASMTVVHTGRWLISSLIMKHLQAGMYGYLNI 123
CuRO_4_FVIII_like cd11016
The fourth cupredoxin domain of coagulation factor VIII and similar proteins; Factor VIII ...
 917-1063 1.14e-26

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: 106.49  E-value: 1.14e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564399494  917 DREFALLFLIFDENQSWYLKENIATYGPQETsHVNLQDATFLESNKMHAINGKLYANLRgLTVYQGERVAWYMLAMGQDT 996
Cdd:cd11016     1 DKDWSLLFSVFDENNSWYLKENIHRFTQTPA-GVNDTDPDFYASNVMHTINGIVFDRRQ-FVICLTDVAYWYVLSVGAQT 78

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 564399494  997 DIHTVHFHAESFLYQNGHSyraDVVDLFPGTFEVVEMVASNPGAWLMHCHVTDHVHAGMETIFTVLS 1063
Cdd:cd11016    79 DFLSVFFSGNTFKHQMVYE---DVLTLFPFSGETVSMSPEVPGEWELGCFNGDFRSRGMSAQYTVST 142
CuRO_4_FV_like cd14454
The fourth cupredoxin domain of coagulation factor V and similar proteins; Factor V is an ...
 229-366 3.19e-26

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


Pssm-ID: 259996 [Multi-domain]  Cd Length: 144  Bit Score: 105.34  E-value: 3.19e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564399494  229 LFSVIDENLSWHLDDNIATYCSDPASVDKEDGPFQDSNRMHAINGFVFGNLPELSMCAQKHVAWHLFGMGNEIDVHTAFF 308
Cdd:cd14454     7 VFAVFDENKSWYLEENINKYCSNPNNVKKDDPKFYKSNIMPTINGYAYESSAPLGFCHSEVVQWHISSVGTQDEIITVHL 86

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 564399494  309 HGQTLSIRGHRTDVAHIFPATFVTAEMVPQKSGTWLIScVVNSHLKS-GMQAFYKVDSC 366
Cdd:cd14454    87 SGHTFRYKGKHEDTLNLFPMSGESITVTMDNLGTWLLG-SFGSSKKSkGLRVRFTDVIC 144
CuRO_6_FVIII_like cd11018
The sixth cupredoxin domain of coagulation factor VIII and similar proteins; Factor VIII ...
 575-714 1.67e-23

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: 97.64  E-value: 1.67e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564399494  575 KEFFLLFTIFDENESWYNNANQAAGMLDSRLLSEDVEGFEDSNRMHAINGFLFSNLPRLDICKGDTVAWHLLGLGTENDV 654
Cdd:cd11018     2 QEFALLFTIFDETKSWYFEENMRRNCRPPCHIQTQDPWFHINNKFHAINGYVADTLPGLVMAQHQRIRWHLLNMGSDEEI 81

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 564399494  655 HGVMFEGNTLQL---QGMRKSAAMLFPHTFVTAIMQPDNPGIFEIYCQAGSHREAGMQAIYNV 714
Cdd:cd11018    82 HSVHFHGLPFTVrakKEYRMGVYNLYPGVFGTVEMRPSTAGIWLVECTVGEHLLAGMSALFLV 144
CuRO_6_FV_like cd14455
The sixth cupredoxin domain of coagulation factor V and similar proteins; Factor V is an ...
 575-714 4.21e-23

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: 96.47  E-value: 4.21e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564399494  575 KEFFLLFTIFDENESWYNNANQAAGMLDSRLLSEdveGFEDSNRMHAINGFLFsNLPRLDICKGDTVAWHLLGLGTENDV 654
Cdd:cd14455     2 REFVLLFMTFDEEKSWYYEKNRKRTCRENRVKDP---NVQDNHTFHAINGIIY-NLKGLRMYTNELVRWHLINMGGPKDL 77

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 564399494  655 HGVMFEGNTLQLQGMRKS---AAMLFPHTFVTAIMQPDNPGIFEIYCQAGSHREAGMQAIYNV 714
Cdd:cd14455    78 HVVHFHGQTFTEKGLKDHqlgVYPLLPGSFATLEMKPSKPGLWLLETEVGESQQRGMQTLFLV 140
CuRO_2_ceruloplasmin_like_2 cd11023
cupredoxin domain of ceruloplasmin homologs; Uncharacterized subfamily of ceruloplasmin ...
 574-714 4.40e-23

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: 95.37  E-value: 4.40e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564399494  574 DKEFFLLFTIFDENESwynnanqaagmldsrllsedvegfEDSNRMHAINGFLFSNLPRLDICKGDTVAWHLLGLGTEND 653
Cdd:cd11023     1 DQEFIENSSIFLDLNV------------------------EEAGLMHSINGYVFGNLPGVTIAKGKRVRWHLVAYGNEVD 56

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 564399494  654 VHGVMFEGNTLQLQGMRKS-AAMLFPHTFVTAIMQPDNPGIFEIYCQAGSHREAGMQAIYNV 714
Cdd:cd11023    57 FHTPHWHGQTVEADKSRRTdVAELMPASMRVADMTAADVGTWLLHCHVHDHYMAGMMTQFAV 118
CuRO_2_FV_like cd14453
The second cupredoxin domain of coagulation factor V and similar proteins; Factor V is an ...
 574-714 1.13e-22

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: 94.54  E-value: 1.13e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564399494  574 DKEFFLLFTIFDENESWYNNANQAagmldsrllsedvegfedSNRMHAINGFLFSNLPRLDICKGDTVAWHLLGLGTEND 653
Cdd:cd14453     1 YKEYVLMFGVFDENKSWYKQNASV------------------DSVKYTINGYTNGTLPDVSICAYDHVSWHLLGMSSEPE 62

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 564399494  654 VHGVMFEGNTLQLQGMRKSAAMLFPHTFVTAIMQPDNPGIFEIYCQAGSHREAGMQAIYNV 714
Cdd:cd14453    63 LFSVHFNGQVLEQNGHKVSAVGLVSGSSTTASMTVVHTGRWLISSLIMKHLQAGMYGYLNI 123
CuRO_4_FV_like cd14454
The fourth cupredoxin domain of coagulation factor V and similar proteins; Factor V is an ...
 917-1043 2.06e-22

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: 94.55  E-value: 2.06e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564399494  917 DREFALLFLIFDENQSWYLKENIATYGpQETSHVNLQDATFLESNKMHAINGKLYANLRGLTVYQGERVAWYMLAMGQDT 996
Cdd:cd14454     1 DLEQHAVFAVFDENKSWYLEENINKYC-SNPNNVKKDDPKFYKSNIMPTINGYAYESSAPLGFCHSEVVQWHISSVGTQD 79

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*..
gi 564399494  997 DIHTVHFHAESFLYQNGHSyraDVVDLFPGTFEVVEMVASNPGAWLM 1043
Cdd:cd14454    80 EIITVHLSGHTFRYKGKHE---DTLNLFPMSGESITVTMDNLGTWLL 123
CuRO_2_FVIII_like cd11015
The second cupredoxin domain of coagulation factor VIII and similar proteins; Factor VIII ...
 918-1061 3.45e-20

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


Pssm-ID: 259901 [Multi-domain]  Cd Length: 134  Bit Score: 87.65  E-value: 3.45e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564399494  918 REFALLFLIFDENQSWYlkeniatygpQETSHVNLQDATFLESN--KMHAINGKLYANLRGLTVYQGERVAWYMLAMGQD 995
Cdd:cd11015     2 QAFVLLFAVFDEGKSWY----------SEVGERKSRDKFKRADSrkEFHTINGYINASLPGLKICQRKPVIWHVIGMGTA 71

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 564399494  996 TDIHTVHFHAESFLYQNghsYRADVVDLFPGTFEVVEMVASNPGAWLMHCHVTDHVHAGMETIFTV 1061
Cdd:cd11015    72 PEVHSIFFEGHTFLVRT---HRKVSLEISPMTFLTAQTKPATVGSFLIFCQIHSHQHDGMEAMVKV 134
CuRO_4_FV_like cd14454
The fourth cupredoxin domain of coagulation factor V and similar proteins; Factor V is an ...
 574-709 1.14e-19

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: 86.46  E-value: 1.14e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564399494  574 DKEFFLLFTIFDENESWYNNANQAAGMLDSRLLSEDVEGFEDSNRMHAINGFLFSNLPRLDICKGDTVAWHLLGLGTEND 653
Cdd:cd14454     1 DLEQHAVFAVFDENKSWYLEENINKYCSNPNNVKKDDPKFYKSNIMPTINGYAYESSAPLGFCHSEVVQWHISSVGTQDE 80

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 564399494  654 VHGVMFEGNTLQLQGMRKSAAMLFPHTFVTAIMQPDNPGIFEIYCQAGSHREAGMQ 709
Cdd:cd14454    81 IITVHLSGHTFRYKGKHEDTLNLFPMSGESITVTMDNLGTWLLGSFGSSKKSKGLR 136
CuRO_2_FV_like cd14453
The second cupredoxin domain of coagulation factor V and similar proteins; Factor V is an ...
 917-1055 2.14e-18

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


Pssm-ID: 259995 [Multi-domain]  Cd Length: 123  Bit Score: 82.21  E-value: 2.14e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564399494  917 DREFALLFLIFDENQSWYlkeniaTYGPQEtshvnlqdatfleSNKMHAINGKLYANLRGLTVYQGERVAWYMLAMGQDT 996
Cdd:cd14453     1 YKEYVLMFGVFDENKSWY------KQNASV-------------DSVKYTINGYTNGTLPDVSICAYDHVSWHLLGMSSEP 61

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 564399494  997 DIHTVHFHAESfLYQNGHsyRADVVDLFPGTFEVVEMVASNPGAWLMHCHVTDHVHAGM 1055
Cdd:cd14453    62 ELFSVHFNGQV-LEQNGH--KVSAVGLVSGSSTTASMTVVHTGRWLISSLIMKHLQAGM 117
CuRO_1_LCC_like cd04206
Cupredoxin domain 1 of laccase-like multicopper oxidases; including laccase, CueO, spore coat ...
 97-204 1.65e-15

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


Pssm-ID: 259869 [Multi-domain]  Cd Length: 120  Bit Score: 73.86  E-value: 1.65e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564399494   97 GFLGPLLKAEMGDVILIHLKN-FASRPYTIHPHGVFYEKDSEGslypDGSSGYLKadDSVPPGGSHVYNWsipeghaptE 175
Cdd:cd04206    27 QFPGPTIRVKEGDTVEVTVTNnLPNEPTSIHWHGLRQPGTNDG----DGVAGLTQ--CPIPPGESFTYRF---------T 91

                          90       100
                  ....*....|....*....|....*....
gi 564399494  176 ADPACLTWIYHSHVDAprDIATGLIGPLI 204
Cdd:cd04206    92 VDDQAGTFWYHSHVGG--QRADGLYGPLI 118
Cu-oxidase_2 pfam07731
Multicopper oxidase; This entry contains many divergent copper oxidase-like domains that are ...
 961-1065 1.93e-15

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


Pssm-ID: 462246 [Multi-domain]  Cd Length: 138  Bit Score: 74.39  E-value: 1.93e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564399494   961 NKMHAINGKLY-ANLRGLTVYQGERVAWYMLAMgqDTDIHTVHFHAESF----------LYQNGHSY------RADVVDL 1023
Cdd:pfam07731   19 RNDWAINGLLFpPNTNVITLPYGTVVEWVLQNT--TTGVHPFHLHGHSFqvlgrgggpwPEEDPKTYnlvdpvRRDTVQV 96

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|..
gi 564399494  1024 FPGTFEVVEMVASNPGAWLMHCHVTDHVHAGMETIFTVLSHE 1065
Cdd:pfam07731   97 PPGGWVAIRFRADNPGVWLFHCHILWHLDQGMMGQFVVRPGD 138
CuRO_3_LCC_like cd04207
Cupredoxin domain 3 of laccase-like multicopper oxidases; including laccase, CueO, spore coat ...
 965-1060 2.32e-15

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


Pssm-ID: 259870 [Multi-domain]  Cd Length: 132  Bit Score: 74.03  E-value: 2.32e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564399494  965 AINGK----LYANLRGLTVYQGERVAWYMLAMGQDTDIHTVHFHAESF--LYQNGHSYRA----------DVVDLFPGTF 1028
Cdd:cd04207    21 VINGMpfkeGDANTDIFSVEAGDVVEIVLINAGNHDMQHPFHLHGHSFwvLGSGGGPFDAplnltnppwrDTVLVPPGGW 100

                          90       100       110
                  ....*....|....*....|....*....|..
gi 564399494 1029 EVVEMVASNPGAWLMHCHVTDHVHAGMETIFT 1060
Cdd:cd04207   101 VVIRFKADNPGVWMLHCHILEHEDAGMMTVFE 132
CuRO_1_LCC_like cd04206
Cupredoxin domain 1 of laccase-like multicopper oxidases; including laccase, CueO, spore coat ...
 454-559 6.49e-14

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: 69.24  E-value: 6.49e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564399494  454 GILGPVIRAEVGDTIQVVFYNR-ASQPFSIQPHGVFYEKSSEGtVYNDGTSYPKVAKsFEKVTYYWTVPPHAGptaedpa 532
Cdd:cd04206    27 QFPGPTIRVKEGDTVEVTVTNNlPNEPTSIHWHGLRQPGTNDG-DGVAGLTQCPIPP-GESFTYRFTVDDQAG------- 97

                          90       100
                  ....*....|....*....|....*..
gi 564399494  533 clTWMYFSAADPTRDTnsGLVGPLLVC 559
Cdd:cd04206    98 --TFWYHSHVGGQRAD--GLYGPLIVE 120
CuRO_3_CopA cd13896
The third cupredoxin domain of CopA copper resistance protein family; CopA is a multicopper ...
 966-1061 2.41e-13

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: 67.67  E-value: 2.41e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564399494  966 INGKLYANLRGLTVYQGERVAwymLAMGQDTDI-HTVHFHAESFLYQNGH---SYRADVVDLFPGTFEVVEMVASNPGAW 1041
Cdd:cd13896    19 INGKAYPDADPLRVREGERVR---IVFVNDTMMaHPMHLHGHFFQVENGNgeyGPRKDTVLVPPGETVSVDFDADNPGRW 95

                          90       100
                  ....*....|....*....|
gi 564399494 1042 LMHCHVTDHVHAGMETIFTV 1061
Cdd:cd13896    96 AFHCHNLYHMEAGMMRVVEY 115
CuRO_1_Diphenol_Ox cd13857
The first cupredoxin domain of fungal laccase, diphenol oxidase; Diphenol oxidase belongs to ...
 98-204 8.85e-13

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: 66.13  E-value: 8.85e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564399494   98 FLGPLLKAEMGDVILIHLKNFASRPYTIHPHGVFyekdSEGSLYPDGSSGYLKAddSVPPGGSHVYNWSIpEGHAPTead 177
Cdd:cd13857    28 FPGPLIEANQGDRIVVHVTNELDEPTSIHWHGLF----QNGTNWMDGTAGITQC--PIPPGGSFTYNFTV-DGQYGT--- 97

                          90       100
                  ....*....|....*....|....*..
gi 564399494  178 paclTWiYHSHVDAprDIATGLIGPLI 204
Cdd:cd13857    98 ----YW-YHSHYST--QYADGLVGPLI 117
CuRO_D2_2dMcoN_like cd04202
The second cupredoxin domain of bacterial two domain multicopper oxidase McoN and similar ...
 917-1062 9.44e-12

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


Pssm-ID: 259865 [Multi-domain]  Cd Length: 138  Bit Score: 63.81  E-value: 9.44e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564399494  917 DREFALLFlifdenQSWyLKENIATYGPQETSHVNlqdatflesnkMHAINGKLYANLRGLTVYQGERVAWYMLAMGQDt 996
Cdd:cd04202     1 DRDYTLVL------QEW-FVDPGTTPMPPEGMDFN-----------YFTINGKSFPATPPLVVKEGDRVRIRLINLSMD- 61

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 564399494  997 dIHTVHFHAESFLY--QNGH------SYRADVVDLFPGTFEVVEMVASNPGAWLMHCHVTDHV-HAGMETIFTVL 1062
Cdd:cd04202    62 -HHPMHLHGHFFLVtaTDGGpipgsaPWPKDTLNVAPGERYDIEFVADNPGDWMFHCHKLHHAmNGMGGGMMTLI 135
SufI COG2132
Multicopper oxidase with three cupredoxin domains (includes cell division protein FtsP and ...
 963-1061 2.34e-11

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: 67.27  E-value: 2.34e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564399494  963 MHAINGKLYANLR-GLTVYQGERVAWYMLAMGQDTdiHTVHFHAESF--LYQNG----HSYRADVVDLFPGTFEVVEMVA 1035
Cdd:COG2132   317 VWTINGKAFDPDRpDLTVKLGERERWTLVNDTMMP--HPFHLHGHQFqvLSRNGkpppEGGWKDTVLVPPGETVRILFRF 394

                          90       100
                  ....*....|....*....|....*..
gi 564399494 1036 SN-PGAWLMHCHVTDHVHAGMETIFTV 1061
Cdd:COG2132   395 DNyPGDWMFHCHILEHEDAGMMGQFEV 421
CuRO_3_CumA_like cd13906
The third cupredoxin domain of CumA like multicopper oxidase; This multicopper oxidase (MCO) ...
 983-1061 4.29e-11

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


Pssm-ID: 259973 [Multi-domain]  Cd Length: 138  Bit Score: 62.02  E-value: 4.29e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564399494  983 ERVAWYMLAMGQDTD-IHTVHFHAESF--LYQNG----HSYRADVVDLFPGtfEVVE--MVASNPGAWLMHCHVTDHVHA 1053
Cdd:cd13906    52 KRGRSYVLRLVNETAfLHPMHLHGHFFrvLSRNGrpvpEPFWRDTVLLGPK--ETVDiaFVADNPGDWMFHCHILEHQET 129


                  ....*...
gi 564399494 1054 GMETIFTV 1061
Cdd:cd13906   130 GMMGVIRV 137
CuRO_1_LCC_like cd04206
Cupredoxin domain 1 of laccase-like multicopper oxidases; including laccase, CueO, spore coat ...
 807-902 4.90e-11

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: 61.15  E-value: 4.90e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564399494  807 GILGPLIRGEVGDILTVVFKNK-ASRPYSIHAHGVLESSTGWPQAA--------EPGEVLTYQWNIPERSGpgpsdsacv 877
Cdd:cd04206    27 QFPGPTIRVKEGDTVEVTVTNNlPNEPTSIHWHGLRQPGTNDGDGVagltqcpiPPGESFTYRFTVDDQAG--------- 97

                          90       100
                  ....*....|....*....|....*
gi 564399494  878 SWIYYSAVDPikDMYSGLVGPLVIC 902
Cdd:cd04206    98 TFWYHSHVGG--QRADGLYGPLIVE 120
CuRO_1_2DMCO_NIR_like cd11024
The cupredoxin domain 1 of a two-domain laccase related to nitrite reductase; The two-domain ...
 100-204 7.19e-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. 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: 60.75  E-value: 7.19e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564399494  100 GPLLKAEMGDVILIHLKNFASRPYTIHPHGVFYEKDsegslypDGSSGylkadDSVPPGGSHVYNWsipeghaptEADPA 179
Cdd:cd11024    32 GPTLRATEGDLVRIHFINTGDHPHTIHFHGIHDAAM-------DGTGL-----GPIMPGESFTYEF---------VAEPA 90

                          90       100
                  ....*....|....*....|....*..
gi 564399494  180 ClTWIYHSHVdAP--RDIATGLIGPLI 204
Cdd:cd11024    91 G-THLYHCHV-QPlkEHIAMGLYGAFI 115
CuRO_1_2DMCO_NIR_like_2 cd14449
The cupredoxin domain 1 of a two-domain laccase related to nitrite reductase; The two-domain ...
 100-204 1.21e-10

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


Pssm-ID: 259991 [Multi-domain]  Cd Length: 135  Bit Score: 60.36  E-value: 1.21e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564399494  100 GPLLKAEMGDVILIHLKNFASRPYTIHPHGVFYEKDSEGSLYPdgssgylkaDDSVPPGGSHVYNWSIPEGHAPTEADPA 179
Cdd:cd14449    29 GPVIEVREGDTLKILFRNTLDVPASLHPHGVDYTTASDGTGMN---------ASIVAPGDTRIYTWRTHGGYRRADGSWA 99

                          90       100       110
                  ....*....|....*....|....*....|..
gi 564399494  180 CLT---WIYHSHV----DAPRDIATGLIGPLI 204
Cdd:cd14449   100 EGTagyWHYHDHVfgteHGTEGLSRGLYGALI 131
CuRO_1_CumA_like cd13861
The first cupredoxin domain of CumA like multicopper oxidase; This multicopper oxidase (MCO) ...
 93-204 3.73e-10

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


Pssm-ID: 259930 [Multi-domain]  Cd Length: 119  Bit Score: 58.40  E-value: 3.73e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564399494   93 PAWL---GFLGPLLKAEMGDVILIHLKNFASRPYTIHPHGVFYEKDSEGSlyPDGSSgylkadDSVPPGGSHVYNWSIPe 169
Cdd:cd13861    21 RTWGyngQVPGPELRVRQGDTLRVRLTNRLPEPTTIHWHGLRLPNAMDGV--PGLTQ------PPVPPGESFTYEFTPP- 91

                          90       100       110
                  ....*....|....*....|....*....|....*
gi 564399494  170 ghapteaDPAclTWIYHSHVDAPRDIATGLIGPLI 204
Cdd:cd13861    92 -------DAG--TYWYHPHVGSQEQLDRGLYGPLI 117
CuRO_3_MaLCC_like cd13901
The third cupredoxin domain of the fungal laccases similar to Ma-LCC from Melanocarpus ...
 1017-1055 4.08e-10

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: 59.55  E-value: 4.08e-10
                          10        20        30
                  ....*....|....*....|....*....|....*....
gi 564399494 1017 RADVVDLFPGTFEVVEMVASNPGAWLMHCHVTDHVHAGM 1055
Cdd:cd13901   114 RRDVAMLPAGGYLVIAFKTDNPGAWLMHCHIAWHASGGL 152
CuRO_D1_2dMcoN_like cd13859
The first cupredoxin domain of bacterial two domain multicopper oxidase McoN and similar ...
 100-204 4.90e-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: 58.26  E-value: 4.90e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564399494  100 GPLLKAEMGDVILIHLKNFASRPYTIHPHGVFyekdSEGSLYPDGSSGYLKadDSVPPGGSHVYNWsipeghaptEADPA 179
Cdd:cd13859    31 GPLIHVKEGDDLVVHVTNNTTLPHTIHWHGVL----QMGSWKMDGVPGVTQ--PAIEPGESFTYKF---------KAERP 95

                          90       100
                  ....*....|....*....|....*.
gi 564399494  180 CLTWiYHSHVDAPRDIAT-GLIGPLI 204
Cdd:cd13859    96 GTLW-YHCHVNVNEHVGMrGMWGPLI 120
Cu-oxidase_3 pfam07732
Multicopper oxidase; This entry contains many divergent copper oxidase-like domains that are ...
 98-204 3.28e-09

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: 55.71  E-value: 3.28e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564399494    98 FLGPLLKAEMGDVILIHLKNFASRPYTIHPHGVFyekdSEGSLYPDGSSGYlkADDSVPPGGSHVYNWSIPeghapteaD 177
Cdd:pfam07732   24 FPGPTIRVREGDTVVVNVTNNLDEPTSIHWHGLQ----QRGTPWMDGVPGV--TQCPIPPGQSFTYRFQVK--------Q 89

                           90       100
                   ....*....|....*....|....*..
gi 564399494   178 PACLTWiYHSHVDAPRdiATGLIGPLI 204
Cdd:pfam07732   90 QAGTYW-YHSHTSGQQ--AAGLAGAII 113
CuRO_3_Fet3p cd13899
The third Cupredoxin domain of multicopper oxidase Fet3p; Fet3p catalyzes the ferroxidase ...
 994-1059 9.89e-09

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


Pssm-ID: 259966 [Multi-domain]  Cd Length: 160  Bit Score: 55.72  E-value: 9.89e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564399494  994 QDTDIHTVHFHAESF-------------LYQNGHSY-----RADVVDLFPGTFEVVEMVASNPGAWLMHCHVTDHVHAGM 1055
Cdd:cd13899    73 WDAGKHPFHLHGHKFqvvqrspdvasddPNPPINEFpenpmRRDTVMVPPGGSVVIRFRADNPGVWFFHCHIEWHLEAGL 152


                  ....
gi 564399494 1056 ETIF 1059
Cdd:cd13899   153 AATF 156
CuRO_1_McoC_like cd13855
The first cupredoxin domain of a multicopper oxidase McoC and similar proteins; This family ...
 100-204 1.22e-08

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: 54.40  E-value: 1.22e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564399494  100 GPLLKAEMGDVILIHLKNFASRPYTIHPHGVFYEKDSEGSlypdgssgylkADDSVPPGGSHVYNWSIPEGHAPTeadpa 179
Cdd:cd13855    32 GPLIEVFEGDTVEITFRNRLPEPTTVHWHGLPVPPDQDGN-----------PHDPVAPGNDRVYRFTLPQDSAGT----- 95

                          90       100
                  ....*....|....*....|....*.
gi 564399494  180 clTWIY-HSHVDAPRDIATGLIGPLI 204
Cdd:cd13855    96 --YWYHpHPHGHTAEQVYRGLAGAFV 119
SufI COG2132
Multicopper oxidase with three cupredoxin domains (includes cell division protein FtsP and ...
 98-204 1.57e-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: 58.41  E-value: 1.57e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564399494   98 FLGPLLKAEMGDVILIHLKNFASRPYTIHPHGVfyekdsegsLYPDGSSGYlkADDSVPPGGSHVYNWSIPeghapteaD 177
Cdd:COG2132    42 YPGPTIRVREGDRVRVRVTNRLPEPTTVHWHGL---------RVPNAMDGV--PGDPIAPGETFTYEFPVP--------Q 102

                          90       100
                  ....*....|....*....|....*....
gi 564399494  178 PACLTWiYHSHVDA--PRDIATGLIGPLI 204
Cdd:COG2132   103 PAGTYW-YHPHTHGstAEQVYRGLAGALI 130
CuRO_3_MCO_like_2 cd13908
The third cupredoxin domain of uncharacterized multicopper oxidase; Multicopper Oxidases (MCOs) ...
 966-1059 1.99e-08

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


Pssm-ID: 259975 [Multi-domain]  Cd Length: 122  Bit Score: 53.61  E-value: 1.99e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564399494  966 INGKLYANL-RGLTVYQGERvawYMLAM-GQDTDIHTVHFHAESF-LYQNG----HSYRADVVDLFPGTFEVVEMVASNP 1038
Cdd:cd13908    23 INGKSYPDEdPPLVVQQGRR---YRLVFrNASDDAHPMHLHRHTFeVTRIDgkptSGLRKDVVMLGGYQRVEVDFVADNP 99

                          90       100
                  ....*....|....*....|.
gi 564399494 1039 GAWLMHCHVTDHVHAGMETIF 1059
Cdd:cd13908   100 GLTLFHCHQQLHMDYGFMALF 120
CuRO_3_MCO_like_3 cd13909
The third cupredoxin domain of uncharacterized multicopper oxidase; Multicopper Oxidases (MCOs) ...
 940-1062 4.55e-08

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


Pssm-ID: 259976 [Multi-domain]  Cd Length: 137  Bit Score: 53.29  E-value: 4.55e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564399494  940 ATYGPQETSHVNLqdatfLESNKMHAINGKlyANlRGLT-VYQGERVAWYMLAMGQDTDI-HTVHFHaesflyqnGHSYR 1017
Cdd:cd13909    18 ATMGGQEMSMREL-----IQLGQFWAFNGV--AG-RPDDpLLEARRGETVRIEMVNNTGFpHGMHLH--------GHHFR 81

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 564399494 1018 A-----------DVVDLFPGTFEVVEMVASNPGAWLMHCHVTDHVHAGMETIFTVL 1062
Cdd:cd13909    82 AilpngalgpwrDTLLMDRGETREIAFVADNPGDWLLHCHMLEHAAAGMMSWFRVT 137
CuRO_1_Fet3p cd13851
The first Cupredoxin domain of multicopper oxidase Fet3P; Fet3p catalyzes the ferroxidase ...
 101-204 4.56e-08

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: 52.65  E-value: 4.56e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564399494  101 PLLKAEMGDVILIHLKN-FASRPYTIHPHGVFYekdsEGSLYPDGSSGYLKADdsVPPGGSHVYNWSIPEGHApteadpa 179
Cdd:cd13851    32 PPIEVNKGDTVVIHATNsLGDQPTSLHFHGLFQ----NGTNYMDGPVGVTQCP--IPPGQSFTYEFTVDTQVG------- 98

                          90       100
                  ....*....|....*....|....*
gi 564399494  180 clTWIYHSHVDAprDIATGLIGPLI 204
Cdd:cd13851    99 --TYWYHSHDGG--QYPDGLRGPFI 119
CuRO_1_2DMCO_NIR_like cd11024
The cupredoxin domain 1 of a two-domain laccase related to nitrite reductase; The two-domain ...
 810-861 5.68e-08

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


Pssm-ID: 259910 [Multi-domain]  Cd Length: 119  Bit Score: 52.27  E-value: 5.68e-08
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 564399494  810 GPLIRGEVGDILTVVFKNKASRPYSIHAHGV---LESSTGWPQAAePGEVLTYQW 861
Cdd:cd11024    32 GPTLRATEGDLVRIHFINTGDHPHTIHFHGIhdaAMDGTGLGPIM-PGESFTYEF 85
CuRO_1_CumA_like cd13861
The first cupredoxin domain of CumA like multicopper oxidase; This multicopper oxidase (MCO) ...
 454-558 1.30e-07

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


Pssm-ID: 259930 [Multi-domain]  Cd Length: 119  Bit Score: 51.08  E-value: 1.30e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564399494  454 GILGPVIRAEVGDTIQVVFYNRASQPFSIQPHGVFYEKSSEGTvynDGTSYPKVA--KSFEkvtyYWTVPPHAGptaedp 531
Cdd:cd13861    28 QVPGPELRVRQGDTLRVRLTNRLPEPTTIHWHGLRLPNAMDGV---PGLTQPPVPpgESFT----YEFTPPDAG------ 94

                          90       100
                  ....*....|....*....|....*..
gi 564399494  532 aclTWMYFSAADPTRDTNSGLVGPLLV 558
Cdd:cd13861    95 ---TYWYHPHVGSQEQLDRGLYGPLIV 118
CuRO_1_2DMCO_NIR_like cd11024
The cupredoxin domain 1 of a two-domain laccase related to nitrite reductase; The two-domain ...
 457-558 2.90e-07

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


Pssm-ID: 259910 [Multi-domain]  Cd Length: 119  Bit Score: 50.35  E-value: 2.90e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564399494  457 GPVIRAEVGDTIQVVFYNRASQPFSIQPHGVFYEkssegtvYNDGTSYPKVAkSFEKVTYYWTVPPhAGptaedpaclTW 536
Cdd:cd11024    32 GPTLRATEGDLVRIHFINTGDHPHTIHFHGIHDA-------AMDGTGLGPIM-PGESFTYEFVAEP-AG---------TH 93

                          90       100
                  ....*....|....*....|...
gi 564399494  537 MYFSAADPTRD-TNSGLVGPLLV 558
Cdd:cd11024    94 LYHCHVQPLKEhIAMGLYGAFIV 116
CuRO_D1_2dMcoN_like cd13859
The first cupredoxin domain of bacterial two domain multicopper oxidase McoN and similar ...
 810-901 2.96e-07

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: 50.55  E-value: 2.96e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564399494  810 GPLIRGEVGDILTVVFKNKASRPYSIHAHGVLESST----GWP----QAAEPGEVLTYQWnIPERSGpgpsdsacVSWIY 881
Cdd:cd13859    31 GPLIHVKEGDDLVVHVTNNTTLPHTIHWHGVLQMGSwkmdGVPgvtqPAIEPGESFTYKF-KAERPG--------TLWYH 101

                          90       100
                  ....*....|....*....|
gi 564399494  882 YSAVDPIKDMYSGLVGPLVI 901
Cdd:cd13859   102 CHVNVNEHVGMRGMWGPLIV 121
CuRO_3_LCC_plant cd13897
The third cupredoxin domain of the plant laccases; Laccase is a blue multicopper oxidase (MCO) ...
 1030-1061 6.20e-07

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: 49.95  E-value: 6.20e-07
                          10        20        30
                  ....*....|....*....|....*....|..
gi 564399494 1030 VVEMVASNPGAWLMHCHVTDHVHAGMETIFTV 1061
Cdd:cd13897   105 AIRFVADNPGVWFMHCHFERHTSWGMATVFIV 136
CuRO_3_tcLLC2_insect_like cd13905
The third cupredoxin domain of the insect laccases similar to laccase 2 in Tribolium castaneum; ...
 1030-1067 6.65e-07

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: 50.76  E-value: 6.65e-07
                          10        20        30
                  ....*....|....*....|....*....|....*...
gi 564399494 1030 VVEMVASNPGAWLMHCHVTDHVHAGMETIFTVLSHEEH 1067
Cdd:cd13905   134 VIRFRADNPGYWLLHCHIEFHLLEGMALVLKVGEPSDP 171
CuRO_3_AAO cd13893
The third cupredoxin domain of plant Ascorbate oxidase; Ascorbate oxidase catalyzes the ...
 1019-1059 7.22e-07

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: 50.11  E-value: 7.22e-07
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|.
gi 564399494 1019 DVVDLFPGTFEVVEMVASNPGAWLMHCHVTDHVHAGMETIF 1059
Cdd:cd13893   104 NTVTIFPYGWTALRFKADNPGVWAFHCHIEWHFHMGMGVVF 144
CuRO_1_CumA_like cd13861
The first cupredoxin domain of CumA like multicopper oxidase; This multicopper oxidase (MCO) ...
 807-901 7.53e-07

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


Pssm-ID: 259930 [Multi-domain]  Cd Length: 119  Bit Score: 49.16  E-value: 7.53e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564399494  807 GILGPLIRGEVGDILTVVFKNKASRPYSIHAHGV-LES-STGWP---QAA-EPGEVLTYQWNIPErsgPGpsdsacVSWi 880
Cdd:cd13861    28 QVPGPELRVRQGDTLRVRLTNRLPEPTTIHWHGLrLPNaMDGVPgltQPPvPPGESFTYEFTPPD---AG------TYW- 97

                          90       100
                  ....*....|....*....|.
gi 564399494  881 YYSAVDPIKDMYSGLVGPLVI 901
Cdd:cd13861    98 YHPHVGSQEQLDRGLYGPLIV 118
PLN02191 PLN02191
L-ascorbate oxidase
 98-231 8.70e-07

L-ascorbate oxidase


Pssm-ID: 177843 [Multi-domain]  Cd Length: 574  Bit Score: 53.09  E-value: 8.70e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564399494   98 FLGPLLKAEMGDVILIHLKN-FASRPYTIHPHGVfyekDSEGSLYPDGSSGYLKAddSVPPGGSHVYNWSIPEGHaptea 176
Cdd:PLN02191   51 FPGPTIDAVAGDTIVVHLTNkLTTEGLVIHWHGI----RQKGSPWADGAAGVTQC--AINPGETFTYKFTVEKPG----- 119

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 564399494  177 dpaclTWIYHSHVDAPRdiATGLIGPLITCKrgtldGNSPPQRKDVDHNFFLLFS 231
Cdd:PLN02191  120 -----THFYHGHYGMQR--SAGLYGSLIVDV-----AKGPKERLRYDGEFNLLLS 162
SufI COG2132
Multicopper oxidase with three cupredoxin domains (includes cell division protein FtsP and ...
 455-646 1.05e-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: 52.63  E-value: 1.05e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564399494  455 ILGPVIRAEVGDTIQVVFYNRASQPFSIQPHGVFYekSSEgtvyNDGTSYPKVA--KSFekvTYYWTVPPHAGptaedpa 532
Cdd:COG2132    42 YPGPTIRVREGDRVRVRVTNRLPEPTTVHWHGLRV--PNA----MDGVPGDPIApgETF---TYEFPVPQPAG------- 105

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564399494  533 clTWMYFSAADPTRDTN--SGLVGPLLVckagaLGEDGKQKGVDKEFFLLFT--IFDENESW-YNNANQAAGMLDSRLLs 607
Cdd:COG2132   106 --TYWYHPHTHGSTAEQvyRGLAGALIV-----EDPEEDLPRYDRDIPLVLQdwRLDDDGQLlYPMDAAMGGRLGDTLL- 177

                         170       180       190
                  ....*....|....*....|....*....|....*....
gi 564399494  608 edvegfedsnrmhaINGFLfsnLPRLDICKGDTVAWHLL 646
Cdd:COG2132   178 --------------VNGRP---NPTLEVRPGERVRLRLL 199
CuRO_1_2DMCO_NIR_like_2 cd14449
The cupredoxin domain 1 of a two-domain laccase related to nitrite reductase; The two-domain ...
 457-558 1.14e-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. Laccase is a blue multi-copper enzyme that catalyzes the oxidation of a variety of organic substrates coupled to the reduction of molecular oxygen to water. It displays broad substrate specificity, catalyzing the oxidation of a wide variety of aromatic, notably phenolic, and inorganic substances. Laccase has been implicated in a wide spectrum of biological activities. This subfamily has lost the type 1 (T1) copper binding site in domain 1 that is present in other two-domain laccases.


Pssm-ID: 259991 [Multi-domain]  Cd Length: 135  Bit Score: 49.19  E-value: 1.14e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564399494  457 GPVIRAEVGDTIQVVFYNRASQPFSIQPHGVFYEKSSEGTVYNDGTSYPKVAKSFEKVTYYWTVPPHAGPTAEDPAclTW 536
Cdd:cd14449    29 GPVIEVREGDTLKILFRNTLDVPASLHPHGVDYTTASDGTGMNASIVAPGDTRIYTWRTHGGYRRADGSWAEGTAG--YW 106

                          90       100
                  ....*....|....*....|....*.
gi 564399494  537 MY----FSAADPTRDTNSGLVGPLLV 558
Cdd:cd14449   107 HYhdhvFGTEHGTEGLSRGLYGALIV 132
CuRO_1_2dMco_1 cd13860
The first cupredoxin domain of bacteria two domain multicopper oxidase; This subfamily ...
 100-204 1.41e-06

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


Pssm-ID: 259929 [Multi-domain]  Cd Length: 119  Bit Score: 48.35  E-value: 1.41e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564399494  100 GPLLKAEMGDVILIHLKNFASRPYTIHPHGVfyekdsegsLYP---DGSSGYlkADDSVPPGGSHVYNWSI-PEGhapte 175
Cdd:cd13860    31 GPTIEVTEGDRVRILVTNELPEPTTVHWHGL---------PVPngmDGVPGI--TQPPIQPGETFTYEFTAkQAG----- 94

                          90       100
                  ....*....|....*....|....*....
gi 564399494  176 adpaclTWIYHSHVDAPRDIATGLIGPLI 204
Cdd:cd13860    95 ------TYMYHSHVDEAKQEDMGLYGAFI 117
CuRO_1_Diphenol_Ox cd13857
The first cupredoxin domain of fungal laccase, diphenol oxidase; Diphenol oxidase belongs to ...
 810-901 2.11e-06

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: 47.64  E-value: 2.11e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564399494  810 GPLIRGEVGDILTVVFKNKASRPYSIHAHGVLESSTGWPQAAE--------PGEVLTYQWNIPERSGpgpsdsacVSWiY 881
Cdd:cd13857    30 GPLIEANQGDRIVVHVTNELDEPTSIHWHGLFQNGTNWMDGTAgitqcpipPGGSFTYNFTVDGQYG--------TYW-Y 100

                          90       100
                  ....*....|....*....|.
gi 564399494  882 YSAVDPikdMYS-GLVGPLVI 901
Cdd:cd13857   101 HSHYST---QYAdGLVGPLIV 118
CuRO_1_Diphenol_Ox cd13857
The first cupredoxin domain of fungal laccase, diphenol oxidase; Diphenol oxidase belongs to ...
 457-558 2.25e-06

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: 47.64  E-value: 2.25e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564399494  457 GPVIRAEVGDTIQVVFYNRASQPFSIQPHGVFyeksSEGTVYNDGTsyPKVAK----SFEKVTYYWTVPPHAGptaedpa 532
Cdd:cd13857    30 GPLIEANQGDRIVVHVTNELDEPTSIHWHGLF----QNGTNWMDGT--AGITQcpipPGGSFTYNFTVDGQYG------- 96

                          90       100
                  ....*....|....*....|....*.
gi 564399494  533 clTWMYFSAADPTrdTNSGLVGPLLV 558
Cdd:cd13857    97 --TYWYHSHYSTQ--YADGLVGPLIV 118
Cu-oxidase pfam00394
Multicopper oxidase; Many of the proteins in this family contain multiple similar copies of ...
 230-367 3.79e-06

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


Pssm-ID: 395317 [Multi-domain]  Cd Length: 146  Bit Score: 47.70  E-value: 3.79e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564399494   230 FSVIDENLSWHlDDNIATYCSDPASVDKED---GPFQDSnrmHAINGFVFGNLPELSMCAQKHVAWHLFgMGNEIDVHTA 306
Cdd:pfam00394    1 EDYVITLSDWY-HKDAKDLEKELLASGKAPtdfPPVPDA---VLINGKDGASLATLTVTPGKTYRLRII-NVALDDSLNF 75

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 564399494   307 FFHGQTLSIRG--------HRTDVAHIFPATF----VTAemvPQKSGTWLISC-VVNSHLKSGMQAFYKVDSCS 367
Cdd:pfam00394   76 SIEGHKMTVVEvdgvyvnpFTVDSLDIFPGQRysvlVTA---NQDPGNYWIVAsPNIPAFDNGTAAAILRYSGA 146
Cu-oxidase_3 pfam07732
Multicopper oxidase; This entry contains many divergent copper oxidase-like domains that are ...
 808-868 5.71e-06

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


Pssm-ID: 462247 [Multi-domain]  Cd Length: 119  Bit Score: 46.47  E-value: 5.71e-06
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 564399494   808 ILGPLIRGEVGDILTVVFKNKASRPYSIHAHGVLESSTGW-------PQAA-EPGEVLTYQWNIPERSG 868
Cdd:pfam07732   24 FPGPTIRVREGDTVVVNVTNNLDEPTSIHWHGLQQRGTPWmdgvpgvTQCPiPPGQSFTYRFQVKQQAG 92
ascorbOXfungal TIGR03390
L-ascorbate oxidase, fungal type; This model describes a family of fungal ascorbate oxidases, ...
 1016-1061 6.78e-06

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: 50.22  E-value: 6.78e-06
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*.
gi 564399494  1016 YRADVVDLFPGTFEVVEMVASNPGAWLMHCHVTDHVHAGMETIFTV 1061
Cdd:TIGR03390  486 YAVKVVPGAPAGWRAWRIRVTNPGVWMMHCHILQHMVMGMQTVWVF 531
CuRO_1_McoC_like cd13855
The first cupredoxin domain of a multicopper oxidase McoC and similar proteins; This family ...
 810-901 7.42e-06

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: 46.31  E-value: 7.42e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564399494  810 GPLIRGEVGDILTVVFKNKASRPYSIHAHG--VLESSTGWP-QAAEPGEVLTYQWNIPErsgpgpsDSACVSWI-----Y 881
Cdd:cd13855    32 GPLIEVFEGDTVEITFRNRLPEPTTVHWHGlpVPPDQDGNPhDPVAPGNDRVYRFTLPQ-------DSAGTYWYhphphG 104

                          90       100
                  ....*....|....*....|
gi 564399494  882 YSAvdpiKDMYSGLVGPLVI 901
Cdd:cd13855   105 HTA----EQVYRGLAGAFVV 120
CuRO_1_Abr2_like cd13850
The first cupredoxin domain of a group of fungal Laccases similar to Abr2 from Aspergillus ...
 92-203 7.75e-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: 7.75e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564399494   92 KPAWLG---FLGPLLKAEMGDVILIHLKNFASRPYTIHPHGVFyekdSEGSLYPDGSSGYLKAddSVPPGGSHVYNWsip 168
Cdd:cd13850    17 REVILIngqFPGPPIILDEGDEVEILVTNNLPVNTTIHFHGIL----QRGTPWSDGVPGVTQW--PIQPGGSFTYRW--- 87

                          90       100       110
                  ....*....|....*....|....*....|....*
gi 564399494  169 eghapTEADPACLTWiYHSHVDAprDIATGLIGPL 203
Cdd:cd13850    88 -----KAEDQYGLYW-YHSHYRG--YYMDGLYGPI 114
PLN02191 PLN02191
L-ascorbate oxidase
 996-1059 9.64e-06

L-ascorbate oxidase


Pssm-ID: 177843 [Multi-domain]  Cd Length: 574  Bit Score: 49.63  E-value: 9.64e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564399494  996 TDIHTVHFHAESFL---YQNGH---------------SYRADVVdLFPGTFEVVEMVASNPGAWLMHCHVTDHVHAGMET 1057
Cdd:PLN02191  464 SEIHPWHLHGHDFWvlgYGDGKfkpgidektynlknpPLRNTAI-LYPYGWTAIRFVTDNPGVWFFHCHIEPHLHMGMGV 542


                  ..
gi 564399494 1058 IF 1059
Cdd:PLN02191  543 VF 544
CuRO_1_Tv-LCC_like cd13856
The first cupredoxin domain of fungal laccases similar to Tv-LCC from Trametes versicolor; ...
 98-204 2.41e-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: 45.02  E-value: 2.41e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564399494   98 FLGPLLKAEMGDVILIHLKNFAS-----RPYTIHPHGVFYEKDSegslYPDGSSGYLKAddSVPPGGSHVYNWSIPEgha 172
Cdd:cd13856    28 FPGPLITANKGDTFRITVVNQLTdptmrRSTSIHWHGIFQHGTN----YADGPAFVTQC--PIAPNHSFTYDFTAGD--- 98

                          90       100       110
                  ....*....|....*....|....*....|..
gi 564399494  173 ptEADpaclTWIYHSHVDAprDIATGLIGPLI 204
Cdd:cd13856    99 --QAG----TFWYHSHLST--QYCDGLRGPLV 122
CuRO_1_Abr2_like cd13850
The first cupredoxin domain of a group of fungal Laccases similar to Abr2 from Aspergillus ...
 810-901 2.68e-05

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: 44.60  E-value: 2.68e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564399494  810 GPLIRGEVGDILTVVFKNKASRPYSIHAHGVLESSTGW----P----QAAEPGEVLTYQWNIPERSGpgpsdsacvSWIY 881
Cdd:cd13850    28 GPPIILDEGDEVEILVTNNLPVNTTIHFHGILQRGTPWsdgvPgvtqWPIQPGGSFTYRWKAEDQYG---------LYWY 98

                          90       100
                  ....*....|....*....|.
gi 564399494  882 YSAvdpIKDMYS-GLVGPLVI 901
Cdd:cd13850    99 HSH---YRGYYMdGLYGPIYI 116
CuRO_3_McoC_like cd13902
The third cupredoxin domain of a multicopper oxidase McoC and similar proteins; This family ...
 945-1061 3.63e-05

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: 44.31  E-value: 3.63e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564399494  945 QETSHVNLQDATFLesnkmhaINGKLYANLR-GLTVYQGERVAWYMlamgqDTDIHTVH-FHAESFLYQ----NGH---- 1014
Cdd:cd13902     9 SEGMSMGAGGMMFL-------INGKTFDMNRiDFVAKVGEVEVWEV-----TNTSHMDHpFHLHGTQFQvleiDGNpqkp 76

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*....
gi 564399494 1015 SYRA--DVVDLFPGTFEVVEMVASNPGAWLMHCHVTDHVHAGMETIFTV 1061
Cdd:cd13902    77 EYRAwkDTVNLPPGEAVRIATRQDDPGMWMYHCHILEHEDAGMMGMLHV 125
CuRO_1_MCO_like_1 cd13862
The first cupredoxin domain of uncharacterized multicopper oxidase; Multicopper Oxidases (MCOs) ...
 100-204 3.71e-05

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: 44.43  E-value: 3.71e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564399494  100 GPLLKAEMGDVILIHLKNFASRPYTIHPHGVFYEKDSEGSLyPDGSSgylkaddSVPPGGSHVYNWSipeghapteADPA 179
Cdd:cd13862    31 GPLLRMRQGVSVTVDVFNDTDIPEYVHWHGLPLPADVDGAM-EEGTP-------SVPPHGHRRYRMT---------PRPA 93

                          90       100
                  ....*....|....*....|....*....
gi 564399494  180 CLTWiYHSHVDAPRDIA----TGLIGPLI 204
Cdd:cd13862    94 GFRW-YHTHVMTMDDLTrgqySGLFGFVY 121
CuRO_3_Tv-LCC_like cd13903
The third cupredoxin domain of the fungal laccases similar to Tv-LCC from Trametes Versicolor; ...
 993-1059 3.94e-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: 44.96  E-value: 3.94e-05
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 564399494  993 GQDTDIHTVHFHAESF---LYQNGHSY------RADVVDL-FPGTFEVVEMVASNPGAWLMHCHVTDHVHAGMETIF 1059
Cdd:cd13903    67 GAIGGPHPFHLHGHAFsvvRSAGSNTYnyvnpvRRDVVSVgTPGDGVTIRFVTDNPGPWFLHCHIDWHLEAGLAVVF 143
CuRO_3_AAO_like_2 cd13895
The third cupredoxin domain of Ascorbate oxidase homologs; This family includes fungal ...
 996-1059 4.16e-05

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: 45.77  E-value: 4.16e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564399494  996 TDIHTVHFHAESFLY-------------------QNGHSYRADVVDLFPGTFE-------------VVEMVASNPGAWLM 1043
Cdd:cd13895    90 LDAHPWHAHGAHYYDlgsglgtysatalaneeklRGYNPIRRDTTMLYRYGGKgyypppgtgsgwrAWRLRVDDPGVWML 169

                          90
                  ....*....|....*.
gi 564399494 1044 HCHVTDHVHAGMETIF 1059
Cdd:cd13895   170 HCHILQHMIMGMQTVW 185
Cu-oxidase_3 pfam07732
Multicopper oxidase; This entry contains many divergent copper oxidase-like domains that are ...
 455-558 4.66e-05

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


Pssm-ID: 462247 [Multi-domain]  Cd Length: 119  Bit Score: 43.77  E-value: 4.66e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564399494   455 ILGPVIRAEVGDTIQVVFYNRASQPFSIQPHGVFyeksSEGTVYNDG----TSYPkvAKSFEKVTYYWTVPPHAGptaed 530
Cdd:pfam07732   24 FPGPTIRVREGDTVVVNVTNNLDEPTSIHWHGLQ----QRGTPWMDGvpgvTQCP--IPPGQSFTYRFQVKQQAG----- 92

                           90       100
                   ....*....|....*....|....*...
gi 564399494   531 paclTWMYFSAADPTRdtNSGLVGPLLV 558
Cdd:pfam07732   93 ----TYWYHSHTSGQQ--AAGLAGAIII 114
CuRO_1_2DMCO_NIR_like_2 cd14449
The cupredoxin domain 1 of a two-domain laccase related to nitrite reductase; The two-domain ...
 810-903 6.58e-05

The cupredoxin domain 1 of a two-domain laccase related to nitrite reductase; The two-domain laccase (small laccase) in this family differs significantly from all laccases. It resembles the two domain nitrite reductase in both sequence and structure. It consists of two cupredoxin domains and forms trimers, and hence resembles the quaternary structure of nitrite reductases more than that of large laccases. There are three trinuclear copper clusters in the enzyme localized between domains 1 and 2 of each pair of neighbor chains. 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: 44.18  E-value: 6.58e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564399494  810 GPLIRGEVGDILTVVFKNKASRPYSIHAHGV----LESSTGWPQAA-EPGEVLTYQWN--IPERSGPGP-SDSACVSWIY 881
Cdd:cd14449    29 GPVIEVREGDTLKILFRNTLDVPASLHPHGVdyttASDGTGMNASIvAPGDTRIYTWRthGGYRRADGSwAEGTAGYWHY 108

                          90       100
                  ....*....|....*....|....*.
gi 564399494  882 YSAV----DPIKDMYSGLVGPLVICR 903
Cdd:cd14449   109 HDHVfgteHGTEGLSRGLYGALIVRR 134
ascorbase TIGR03388
L-ascorbate oxidase, plant type; Members of this protein family are the copper-containing ...
 993-1059 8.91e-05

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


Pssm-ID: 274555 [Multi-domain]  Cd Length: 541  Bit Score: 46.67  E-value: 8.91e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564399494   993 GQDTDIHTVHFHAESFL---YQNGhSYRADV---------------VDLFPGTFEVVEMVASNPGAWLMHCHVTDHVHAG 1054
Cdd:TIGR03388  438 GNNSETHPWHLHGHDFWvlgYGEG-KFRPGVdeksynlknpplrntVVIFPYGWTALRFVADNPGVWAFHCHIEPHLHMG 516


                   ....*
gi 564399494  1055 METIF 1059
Cdd:TIGR03388  517 MGVVF 521
CuRO_1_AAO cd13845
The first cupredoxin domain of plant Ascorbate oxidase; Ascorbate oxidase catalyzes the ...
 97-204 1.13e-04

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: 42.82  E-value: 1.13e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564399494   97 GFLGPLLKAEMGDVILIHLKN-FASRPYTIHPHGVfyekDSEGSLYPDGSSGYLKAddSVPPGGSHVYNWSIPEghapte 175
Cdd:cd13845    27 QFPGPTIRATAGDTIVVELENkLPTEGVAIHWHGI----RQRGTPWADGTASVSQC--PINPGETFTYQFVVDR------ 94

                          90       100
                  ....*....|....*....|....*....
gi 564399494  176 adPAclTWIYHSHVDAPRdiATGLIGPLI 204
Cdd:cd13845    95 --PG--TYFYHGHYGMQR--SAGLYGSLI 117
CuRO_1_Tv-LCC_like cd13856
The first cupredoxin domain of fungal laccases similar to Tv-LCC from Trametes versicolor; ...
 810-901 1.24e-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: 43.09  E-value: 1.24e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564399494  810 GPLIRGEVGDILTVVFKNKAS-----RPYSIHAHGVLESSTGW----------PQAaePGEVLTYQWNIPERSGpgpsds 874
Cdd:cd13856    30 GPLITANKGDTFRITVVNQLTdptmrRSTSIHWHGIFQHGTNYadgpafvtqcPIA--PNHSFTYDFTAGDQAG------ 101

                          90       100
                  ....*....|....*....|....*...
gi 564399494  875 acVSWiYYSAVDPikdMY-SGLVGPLVI 901
Cdd:cd13856   102 --TFW-YHSHLST---QYcDGLRGPLVI 123
CuRO_3_Abr2_like cd13898
The third cupredoxin domain of a group of fungal Laccases similar to Abr2 from Aspergillus ...
 1030-1055 1.29e-04

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


Pssm-ID: 259965 [Multi-domain]  Cd Length: 164  Bit Score: 43.79  E-value: 1.29e-04
                          10        20
                  ....*....|....*....|....*.
gi 564399494 1030 VVEMVASNPGAWLMHCHVTDHVHAGM 1055
Cdd:cd13898   132 VIRYHVVNPGAWLLHCHIQSHLAGGM 157
CuRO_1_MaLCC_like cd13854
The first cupredoxin domain of the fungal laccases similar to Ma-LCC from Melanocarpus ...
 100-204 1.40e-04

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: 42.61  E-value: 1.40e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564399494  100 GPLLKAEMGDVILIHLKNfaSRPY---TIHPHGVfyekDSEGSLYPDGSSGYLKAddSVPPGGSHVYNWsipeghaptEA 176
Cdd:cd13854    33 GPLIEANWGDTIEVTVIN--KLQDngtSIHWHGI----RQLNTNWQDGVPGVTEC--PIAPGDTRTYRF---------RA 95

                          90       100
                  ....*....|....*....|....*...
gi 564399494  177 DPACLTWiYHSHVDAprDIATGLIGPLI 204
Cdd:cd13854    96 TQYGTSW-YHSHYSA--QYGDGVVGPIV 120
CuRO_1_2dMco_1 cd13860
The first cupredoxin domain of bacteria two domain multicopper oxidase; This subfamily ...
 810-901 1.42e-04

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


Pssm-ID: 259929 [Multi-domain]  Cd Length: 119  Bit Score: 42.57  E-value: 1.42e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564399494  810 GPLIRGEVGDILTVVFKNKASRPYSIHAHGVLESST-----GWPQAA-EPGEVLTYQWNIpERSGpgpsdsacvSWIYYS 883
Cdd:cd13860    31 GPTIEVTEGDRVRILVTNELPEPTTVHWHGLPVPNGmdgvpGITQPPiQPGETFTYEFTA-KQAG---------TYMYHS 100

                          90
                  ....*....|....*...
gi 564399494  884 AVDPIKDMYSGLVGPLVI 901
Cdd:cd13860   101 HVDEAKQEDMGLYGAFIV 118
CuRO_1_2DMCO_NIR_like cd11024
The cupredoxin domain 1 of a two-domain laccase related to nitrite reductase; The two-domain ...
 999-1061 1.74e-04

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


Pssm-ID: 259910 [Multi-domain]  Cd Length: 119  Bit Score: 42.26  E-value: 1.74e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 564399494  999 HTVHFHAESFLYQNGHSYRadvvDLFPGTFEVVEMVASNPGAWLMHCHV---TDHVHAGMETIFTV 1061
Cdd:cd11024    55 HTIHFHGIHDAAMDGTGLG----PIMPGESFTYEFVAEPAGTHLYHCHVqplKEHIAMGLYGAFIV 116
CuRO_3_BOD cd13889
The third cupredoxin domain of Bilirubin oxidase (BOD); Bilirubin oxidase (BOD) catalyzes the ...
 956-1061 1.77e-04

The third cupredoxin domain of Bilirubin oxidase (BOD); Bilirubin oxidase (BOD) catalyzes the oxidation of bilirubin to biliverdin and the four-electron reduction of molecular oxygen to water. It is used in diagnosing jaundice through the determination of bilirubin in serum. BOD is a member of the multicopper oxidase (MCO) family that also includes laccase, ascorbate oxidase and ceruloplasmin. 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: 259956 [Multi-domain]  Cd Length: 124  Bit Score: 42.30  E-value: 1.77e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564399494  956 TFLESNKMHAINGKLYANLRGL--TVYQGERVAWYmLAMGQDTDIHTVHFHAESF--LYQNG-----HSY---RADVVDL 1023
Cdd:cd13889     7 RFGRGNGMWTINGKTWADPNRIdaAPQLGTVEIWT-LINGGGGWSHPIHIHLEDFqiLSRNGgsravPPYergRKDVVYL 85

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|.
gi 564399494 1024 FPGtfEVVEMVA---SNPGAWLMHCHVTDHVHAGMETIFTV 1061
Cdd:cd13889    86 GPG--EEVRVLMrfrPFRGKYMMHCHNLVHEDHDMMLRFEV 124
CuRO_3_MCO_like_4 cd13910
The third cupredoxin domain of uncharacterized multicopper oxidase; Multicopper Oxidases (MCOs) ...
 1030-1055 2.46e-04

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


Pssm-ID: 259977 [Multi-domain]  Cd Length: 166  Bit Score: 43.05  E-value: 2.46e-04
                          10        20
                  ....*....|....*....|....*.
gi 564399494 1030 VVEMVASNPGAWLMHCHVTDHVHAGM 1055
Cdd:cd13910   135 VLRFVADNPGLWAFHCHILWHMAAGM 160
laccase TIGR03389
laccase, plant; Members of this protein family include the copper-containing enzyme laccase ...
 1030-1061 2.55e-04

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


Pssm-ID: 274556 [Multi-domain]  Cd Length: 539  Bit Score: 45.11  E-value: 2.55e-04
                           10        20        30
                   ....*....|....*....|....*....|..
gi 564399494  1030 VVEMVASNPGAWLMHCHVTDHVHAGMETIFTV 1061
Cdd:TIGR03389  488 AIRFVADNPGVWFMHCHLEVHTTWGLKMAFLV 519
CuRO_3_Diphenol_Ox cd13904
The third cupredoxin domain of fungal laccase, diphenol oxidase; Diphenol oxidase belongs to ...
 1017-1054 5.83e-04

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


Pssm-ID: 259971 [Multi-domain]  Cd Length: 158  Bit Score: 41.51  E-value: 5.83e-04
                          10        20        30
                  ....*....|....*....|....*....|....*...
gi 564399494 1017 RADVVDLFPGTFEVVEMVASNPGAWLMHCHVTDHVHAG 1054
Cdd:cd13904   114 RRDTIVIPGGSWAVLRIPADNPGVWALHCHIGWHLAAG 151
CuRO_1_AAO cd13845
The first cupredoxin domain of plant Ascorbate oxidase; Ascorbate oxidase catalyzes the ...
 810-861 7.38e-04

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: 40.51  E-value: 7.38e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 564399494  810 GPLIRGEVGDILTVVFKNK-ASRPYSIHAHGVLESSTGWPQ--------AAEPGEVLTYQW 861
Cdd:cd13845    30 GPTIRATAGDTIVVELENKlPTEGVAIHWHGIRQRGTPWADgtasvsqcPINPGETFTYQF 90
CuRO_1_LCC_plant cd13849
The first cupredoxin domain of plant laccases; Laccase is a blue multicopper oxidase (MCO) ...
 810-868 1.19e-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: 39.94  E-value: 1.19e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 564399494  810 GPLIRGEVGDILTVVFKNKASRPYSIHAHGVLESSTGWPQAAE--------PGEVLTYQWNIPERSG 868
Cdd:cd13849    28 GPTIRVHEGDTVVVNVTNRSPYNITIHWHGIRQLRSGWADGPAyitqcpiqPGQSYTYRFTVTGQEG 94
ascorbase TIGR03388
L-ascorbate oxidase, plant type; Members of this protein family are the copper-containing ...
 810-868 1.33e-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: 1.33e-03
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 564399494   810 GPLIRGEVGDILTVVFKNK-ASRPYSIHAHGVLESSTGWPQAAE--------PGEVLTYQWNIpERSG 868
Cdd:TIGR03388   31 GPTIRAQAGDTIVVELTNKlHTEGVVIHWHGIRQIGTPWADGTAgvtqcainPGETFIYNFVV-DRPG 97
CuRO_1_CuNIR_like cd04201
Cupredoxin domain 1 of Copper-containing nitrite reductase and two-domain laccase; ...
 977-1062 2.32e-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: 39.01  E-value: 2.32e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564399494  977 LTVYQGERVAWYMLAMGQDTDIHTVHFHAESflyqnGHSYRADVVDLFPGTFEVVEMVASNPGAWLMHCHVTD---HVHA 1053
Cdd:cd04201    35 LRVREGDTVELHFSNNPSSTMPHNIDFHAAT-----GAGGGAGATFIAPGETSTFSFKATQPGLYVYHCAVAPvpmHIAN 109


                  ....*....
gi 564399494 1054 GMETIFTVL 1062
Cdd:cd04201   110 GMYGLILVE 118
CuRO_1_CueO_FtsP cd04232
The first Cupredoxin domain of the multicopper oxidase CueO, the cell division protein FtsP, ...
 98-204 2.36e-03

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: 39.09  E-value: 2.36e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564399494   98 FLGPLLKAEMGDVILIHLKNFASRPYTIHPHGVFYEKDSEGSLYpdgssgylkadDSVPPGGSHVYNWSIpeghapteAD 177
Cdd:cd04232    29 YLGPTIRVKKGDTVRINVTNNLDEETTVHWHGLHVPGEMDGGPH-----------QPIAPGQTWSPTFTI--------DQ 89

                          90       100
                  ....*....|....*....|....*....
gi 564399494  178 PACLTWiYHSHVDA--PRDIATGLIGPLI 204
Cdd:cd04232    90 PAATLW-YHPHTHGktAEQVYRGLAGLFI 117
CuRO_1_CuNIR cd11020
Cupredoxin domain 1 of Copper-containing nitrite reductase; Copper-containing nitrite ...
 810-888 2.84e-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: 38.73  E-value: 2.84e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564399494  810 GPLIRGEVGDILTVVFKNKASR--PYSIHAHGVLESSTGWPQAAEPGEVLTYQWnIPERSGpgpsdsacvSWIYYSAVDP 887
Cdd:cd11020    32 GPVIRVREGDTVELTLTNPGTNtmPHSIDFHAATGPGGGEFTTIAPGETKTFSF-KALYPG---------VFMYHCATAP 101


                  .
gi 564399494  888 I 888
Cdd:cd11020   102 V 102
CuRO_1_LCC_plant cd13849
The first cupredoxin domain of plant laccases; Laccase is a blue multicopper oxidase (MCO) ...
 457-504 2.88e-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: 2.88e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*...
gi 564399494  457 GPVIRAEVGDTIQVVFYNRASQPFSIQPHGVFYEKSsegtVYNDGTSY 504
Cdd:cd13849    28 GPTIRVHEGDTVVVNVTNRSPYNITIHWHGIRQLRS----GWADGPAY 71
CuRO_3_LCC_like cd04207
Cupredoxin domain 3 of laccase-like multicopper oxidases; including laccase, CueO, spore coat ...
 258-361 4.61e-03

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: 38.60  E-value: 4.61e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564399494  258 EDGPFQDSNRMHAINGFVF----GNLPELSMCAQKHVAWHLFGMGNEIDVHTAFFHG---QTLSIRGH------------ 318
Cdd:cd04207     9 SQTGAPDGTTRWVINGMPFkegdANTDIFSVEAGDVVEIVLINAGNHDMQHPFHLHGhsfWVLGSGGGpfdaplnltnpp 88

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|...
gi 564399494  319 RTDVAHIFPATFVTAEMVPQKSGTWLISCVVNSHLKSGMQAFY 361
Cdd:cd04207    89 WRDTVLVPPGGWVVIRFKADNPGVWMLHCHILEHEDAGMMTVF 131
CuRO_1_LCC_plant cd13849
The first cupredoxin domain of plant laccases; Laccase is a blue multicopper oxidase (MCO) ...
 98-204 4.81e-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: 38.01  E-value: 4.81e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564399494   98 FLGPLLKAEMGDVILIHLKNFASRPYTIHPHGVFYEKdsegSLYPDGSSGYLKAddSVPPGGSHVYNWSIpEGHAPTead 177
Cdd:cd13849    26 FPGPTIRVHEGDTVVVNVTNRSPYNITIHWHGIRQLR----SGWADGPAYITQC--PIQPGQSYTYRFTV-TGQEGT--- 95

                          90       100
                  ....*....|....*....|....*..
gi 564399494  178 pacLTWiyHSHVDAPRdiATgLIGPLI 204
Cdd:cd13849    96 ---LWW--HAHISWLR--AT-VYGAFI 114
CuRO_1_tcLCC2_insect_like cd13858
The first cupredoxin domain of insect laccases similar to laccase 2 in Tribolium castaneum; ...
 100-204 5.01e-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: 37.90  E-value: 5.01e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564399494  100 GPLLKAEMGDVILIHLKN-FASRPYTIHPHGVFyekdSEGSLYPDGssgylkaddsVP--------PGGSHVYNWSipeg 170
Cdd:cd13858    16 GPSIEVCEGDTVVVDVKNrLPGESTTIHWHGIH----QRGTPYMDG----------VPmvtqcpilPGQTFRYKFK---- 77

                          90       100       110
                  ....*....|....*....|....*....|....
gi 564399494  171 hapteADPAClTWIYHSHVDAPRdiATGLIGPLI 204
Cdd:cd13858    78 -----ADPAG-THWYHSHSGTQR--ADGLFGALI 103
PLN02604 PLN02604
oxidoreductase
 1035-1059 5.48e-03

oxidoreductase


Pssm-ID: 215324 [Multi-domain]  Cd Length: 566  Bit Score: 40.61  E-value: 5.48e-03
                          10        20
                  ....*....|....*....|....*
gi 564399494 1035 ASNPGAWLMHCHVTDHVHAGMETIF 1059
Cdd:PLN02604  520 ADNPGVWAFHCHIESHFFMGMGVVF 544
CuRO_1_McoP_like cd13852
The first cupredoxin domain of multicopper oxidase McoP and similar proteins; This family ...
 809-868 6.23e-03

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


Pssm-ID: 259921 [Multi-domain]  Cd Length: 114  Bit Score: 37.65  E-value: 6.23e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 564399494  809 LGPLIRGEVGDILTVVFKNKASRPYSIHAHG--VLESSTGWPQAA-EPGEVLTYQWNIPERSG 868
Cdd:cd13852    23 LGPILRLRKGQKVRITFKNNLPEPTIIHWHGlhVPAAMDGHPRYAiDPGETYVYEFEVLNRAG 85
CuRO_1_CopA cd13848
The first cupredoxin domain of CopA copper resistance protein family; CopA is a multicopper ...
 807-863 6.77e-03

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: 37.65  E-value: 6.77e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 564399494  807 GILGPLIRGEVGDILTVVFKNKASRPYSIHAHGVL--ESSTGWP----QAAEPGEVLTYQWNI 863
Cdd:cd13848    27 QVPGPLLRFKEGDDATIRVHNRLDEDTSIHWHGLLlpNDMDGVPglsfPGIKPGETFTYRFPV 89
CuRO_1_AAO cd13845
The first cupredoxin domain of plant Ascorbate oxidase; Ascorbate oxidase catalyzes the ...
 429-558 8.46e-03

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


Pssm-ID: 259914 [Multi-domain]  Cd Length: 120  Bit Score: 37.43  E-value: 8.46e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564399494  429 WKVRYEAFQDETFqerlhqeEETHLGI----LGPVIRAEVGDTIQVVFYNR-ASQPFSIQPHGVfyekSSEGTVYNDGTS 503
Cdd:cd13845     5 WKVEYMFWAPDCV-------EKLVIGIngqfPGPTIRATAGDTIVVELENKlPTEGVAIHWHGI----RQRGTPWADGTA 73

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 564399494  504 YPK--VAKSFEKVTYYWTVpPHAGptaedpaclTWMYFSAADPTRdtNSGLVGPLLV 558
Cdd:cd13845    74 SVSqcPINPGETFTYQFVV-DRPG---------TYFYHGHYGMQR--SAGLYGSLIV 118
CuRO_1_MCO_like_1 cd13862
The first cupredoxin domain of uncharacterized multicopper oxidase; Multicopper Oxidases (MCOs) ...
 810-901 9.19e-03

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: 37.50  E-value: 9.19e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564399494  810 GPLIRGEVGDILTVVFKNKASRPYSIHAHGVLESST-------GWPQAAePGEVLTYqwnipeRSGPGPSDSacvSWiYY 882
Cdd:cd13862    31 GPLLRMRQGVSVTVDVFNDTDIPEYVHWHGLPLPADvdgameeGTPSVP-PHGHRRY------RMTPRPAGF---RW-YH 99

                          90       100
                  ....*....|....*....|...
gi 564399494  883 SAVDPIKDM----YSGLVGPLVI 901
Cdd:cd13862   100 THVMTMDDLtrgqYSGLFGFVYI 122
CuRO_1_MCO_like_1 cd13862
The first cupredoxin domain of uncharacterized multicopper oxidase; Multicopper Oxidases (MCOs) ...
 457-558 9.37e-03

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: 37.50  E-value: 9.37e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564399494  457 GPVIRAEVGDTIQVVFYNRASQPFSIQPHGVFYEKSSEGTVyNDGTSYpkvaksfekvtyywtVPPHAGPT---AEDPAC 533
Cdd:cd13862    31 GPLLRMRQGVSVTVDVFNDTDIPEYVHWHGLPLPADVDGAM-EEGTPS---------------VPPHGHRRyrmTPRPAG 94

                          90       100
                  ....*....|....*....|....*...
gi 564399494  534 LTWMY---FSAADPTRDTNSGLVGPLLV 558
Cdd:cd13862    95 FRWYHthvMTMDDLTRGQYSGLFGFVYI 122
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

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