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Conserved domains on  [gi|26349115|dbj|BAC38197|]
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unnamed protein product [Mus musculus]

Protein Classification

CuRO_1_ceruloplasmin and CuRO_2_ceruloplasmin domain-containing protein( domain architecture ID 10136062)

protein containing domains CuRO_1_ceruloplasmin, CuRO_2_ceruloplasmin, and Cupredoxin

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 1.38e-121

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


:

Pssm-ID: 259884 [Multi-domain]  Cd Length: 183  Bit Score: 364.43  E-value: 1.38e-121
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26349115  26 RNYYLGIQDMQWNYAPKGRNVITNQTLNNDTVASSFLKSGKNRIGSSYKKTVYKEYSDGTYTEEIAKPAWLGFLGPLLQA 105
Cdd:cd04222   1 REYYIGIRETQWDYAPSGKNLITNQTFDDDEHASVFLKRGPDRIGRVYKKAVYLQYTDDTYRTEIEKPVWLGFLGPILKA 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26349115 106 EVGDVILIHLKNFASRPYTIHPHGVFYEKDSEGSLYPDGSSGYLKADDSVPPGGSHVYNWSIPESHAPTEADPACLTWIY 185
Cdd:cd04222  81 EVGDVIVVHLKNFASRPYSLHPHGVFYNKENEGALYPDNTSGFEKADDAVPPGGSYTYTWTVPEEQAPTKADANCLTRIY 160

                       170       180
                ....*....|....*....|...
gi 26349115 186 HSHVDAPRDIATGLIGPLITCKR 208
Cdd:cd04222 161 HSHIDAPKDIASGLIGPLIICKK 183
CuRO_2_ceruloplasmin cd11021
The second cupredoxin domain of Ceruloplasmin; Ceruloplasmin is a multicopper oxidase ...
 223-363 3.16e-89

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: 278.20  E-value: 3.16e-89
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26349115 223 DHNFFLLFSVIDENLSWHLDDNIATYCSDPASVDKEDGAFQDSNRMHAINGFVFGNLPELSMCAQKHVAWHLFGMGNEID 302
Cdd:cd11021   1 DREFVLMFSVVDENLSWYLDENIKTYCSEPAKVDKDDEDFQESNKMHSINGYTFGNLPGLSMCAGDRVKWHLFGMGNEVD 80

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 26349115 303 VHTAFFHGQMLSIRGHHTDVANIFPATFVTAEMVPQKSGTWLISCEVNSHLRSGMQAFYKV 363
Cdd:cd11021  81 IHSAFFHGQTLTDRGHRTDTINLFPATFVTAEMVAQNPGKWLLSCQVNDHLKAGMQAFYEV 141
Cupredoxin super family cl19115
Cupredoxin superfamily; Cupredoxins contain type I copper centers and are involved in ...
 377-529 1.11e-85

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


The actual alignment was detected with superfamily member cd04224:

Pssm-ID: 473140 [Multi-domain]  Cd Length: 197  Bit Score: 271.27  E-value: 1.11e-85
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26349115 377 GKVRQYFIQAHEIQWDYGPIGYDGRTGKSLREPGSGPDKYFQKSSSRIGGTYWKVRYEAFQDETFQERVHQ-EEETHLGI 455
Cdd:cd04224   1 GKVRHYFIAAEEIMWDYAPSGKNLFTGQNLTAPGSDSEVFFQRNETRIGGTYWKVRYVEYTDATFTTRKHRsKEEEHLGI 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26349115 456 LGPVIRAEVGDTIQVVFYNRASQPFSIQPHGVFYEKNSEGTVYND----------------------------------- 500
Cdd:cd04224  81 LGPVIRAEVGDTIKVTFRNKASRPFSIQPHGVFYEKNYEGAMYRDgdpspgshvspgetftyewtvpegvgptnqdppcl 160

                       170       180       190
                ....*....|....*....|....*....|....*..
gi 26349115 501 --------DPTRDTNSGLVGPLLVCKAGALGADGKQK 529
Cdd:cd04224 161 tylyfsavDPVRDTNSGLVGPLLVCKKGSLNANGRQK 197
Cupredoxin super family cl19115
Cupredoxin superfamily; Cupredoxins contain type I copper centers and are involved in ...
 532-675 3.84e-85

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: 267.81  E-value: 3.84e-85
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26349115 532 DKEFFLLFTVFDENESWYNNANQAAGMLDSRLLSEDVEGFQDSNRMHAINGFLFSNLPRLDMCKGDTVAWHLLGLGTETD 611
Cdd:cd11022   1 DKEFFLLFTVFDENESWYLDENIQQFTLDPRSVDKEDEDFQESNKMHSINGYMYGNQPGLDMCKGDTVSWHLFGLGTETD 80

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 26349115 612 VHGVMFEGNTVQLQGMRKGAVMLFPHTFVTAIMQPDNPGIFEIYCQAGSHREEGMQAIYNVSQC 675
Cdd:cd11022  81 VHGIYFSGNTFLLQGTRRDTANLFPHTSVTAIMQPDNEGTFEVNCQTTDHYSAGMRQIYTVSQC 144
Cupredoxin super family cl19115
Cupredoxin superfamily; Cupredoxins contain type I copper centers and are involved in ...
 690-813 7.17e-67

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


The actual alignment was detected with superfamily member cd04225:

Pssm-ID: 473140 [Multi-domain]  Cd Length: 171  Bit Score: 220.03  E-value: 7.17e-67
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26349115 690 RVYYIMAEEIEWDYCPDRSWELEWHNTSEKdSYGHVFLSNKDGLLGSKYKKAVFREYTDGTFRIPRPRSGPEEHLGILGP 769
Cdd:cd04225   1 RTYYIAAEEVEWDYSPQRTWEQELHNTHEE-SPGNAFLNKGDKFIGSKYKKVVYREYTDDTFSVPKERTAEEEHLGILGP 79

                        90       100       110       120
                ....*....|....*....|....*....|....*....|....
gi 26349115 770 LIRGEVGDILTVVFKNKASRPYSIHAHGVLESNTgGPQAAEPGE 813
Cdd:cd04225  80 LIHAEVGEKVKIVFKNMASRPYSIHAHGVKTDSS-WVAPTEPGE 122
 
Name Accession Description Interval E-value
CuRO_1_ceruloplasmin cd04222
The first cupredoxin domain of Ceruloplasmin; Ceruloplasmin is a multicopper oxidase essential ...
 26-208 1.38e-121

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


Pssm-ID: 259884 [Multi-domain]  Cd Length: 183  Bit Score: 364.43  E-value: 1.38e-121
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26349115  26 RNYYLGIQDMQWNYAPKGRNVITNQTLNNDTVASSFLKSGKNRIGSSYKKTVYKEYSDGTYTEEIAKPAWLGFLGPLLQA 105
Cdd:cd04222   1 REYYIGIRETQWDYAPSGKNLITNQTFDDDEHASVFLKRGPDRIGRVYKKAVYLQYTDDTYRTEIEKPVWLGFLGPILKA 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26349115 106 EVGDVILIHLKNFASRPYTIHPHGVFYEKDSEGSLYPDGSSGYLKADDSVPPGGSHVYNWSIPESHAPTEADPACLTWIY 185
Cdd:cd04222  81 EVGDVIVVHLKNFASRPYSLHPHGVFYNKENEGALYPDNTSGFEKADDAVPPGGSYTYTWTVPEEQAPTKADANCLTRIY 160

                       170       180
                ....*....|....*....|...
gi 26349115 186 HSHVDAPRDIATGLIGPLITCKR 208
Cdd:cd04222 161 HSHIDAPKDIASGLIGPLIICKK 183
CuRO_2_ceruloplasmin cd11021
The second cupredoxin domain of Ceruloplasmin; Ceruloplasmin is a multicopper oxidase ...
 223-363 3.16e-89

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: 278.20  E-value: 3.16e-89
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26349115 223 DHNFFLLFSVIDENLSWHLDDNIATYCSDPASVDKEDGAFQDSNRMHAINGFVFGNLPELSMCAQKHVAWHLFGMGNEID 302
Cdd:cd11021   1 DREFVLMFSVVDENLSWYLDENIKTYCSEPAKVDKDDEDFQESNKMHSINGYTFGNLPGLSMCAGDRVKWHLFGMGNEVD 80

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 26349115 303 VHTAFFHGQMLSIRGHHTDVANIFPATFVTAEMVPQKSGTWLISCEVNSHLRSGMQAFYKV 363
Cdd:cd11021  81 IHSAFFHGQTLTDRGHRTDTINLFPATFVTAEMVAQNPGKWLLSCQVNDHLKAGMQAFYEV 141
CuRO_3_ceruloplasmin cd04224
The third cupredoxin domain of Ceruloplasmin; Ceruloplasmin is a multicopper oxidase essential ...
 377-529 1.11e-85

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: 271.27  E-value: 1.11e-85
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26349115 377 GKVRQYFIQAHEIQWDYGPIGYDGRTGKSLREPGSGPDKYFQKSSSRIGGTYWKVRYEAFQDETFQERVHQ-EEETHLGI 455
Cdd:cd04224   1 GKVRHYFIAAEEIMWDYAPSGKNLFTGQNLTAPGSDSEVFFQRNETRIGGTYWKVRYVEYTDATFTTRKHRsKEEEHLGI 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26349115 456 LGPVIRAEVGDTIQVVFYNRASQPFSIQPHGVFYEKNSEGTVYND----------------------------------- 500
Cdd:cd04224  81 LGPVIRAEVGDTIKVTFRNKASRPFSIQPHGVFYEKNYEGAMYRDgdpspgshvspgetftyewtvpegvgptnqdppcl 160

                       170       180       190
                ....*....|....*....|....*....|....*..
gi 26349115 501 --------DPTRDTNSGLVGPLLVCKAGALGADGKQK 529
Cdd:cd04224 161 tylyfsavDPVRDTNSGLVGPLLVCKKGSLNANGRQK 197
CuRO_4_ceruloplasmin cd11022
The fourth cupredoxin domain of Ceruloplasmin; Ceruloplasmin is a multicopper oxidase ...
 532-675 3.84e-85

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: 267.81  E-value: 3.84e-85
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26349115 532 DKEFFLLFTVFDENESWYNNANQAAGMLDSRLLSEDVEGFQDSNRMHAINGFLFSNLPRLDMCKGDTVAWHLLGLGTETD 611
Cdd:cd11022   1 DKEFFLLFTVFDENESWYLDENIQQFTLDPRSVDKEDEDFQESNKMHSINGYMYGNQPGLDMCKGDTVSWHLFGLGTETD 80

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 26349115 612 VHGVMFEGNTVQLQGMRKGAVMLFPHTFVTAIMQPDNPGIFEIYCQAGSHREEGMQAIYNVSQC 675
Cdd:cd11022  81 VHGIYFSGNTFLLQGTRRDTANLFPHTSVTAIMQPDNEGTFEVNCQTTDHYSAGMRQIYTVSQC 144
CuRO_5_ceruloplasmin cd04225
The fifth cupredoxin domain of Ceruloplasmin; Ceruloplasmin is a multicopper oxidase essential ...
 690-813 7.17e-67

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: 220.03  E-value: 7.17e-67
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26349115 690 RVYYIMAEEIEWDYCPDRSWELEWHNTSEKdSYGHVFLSNKDGLLGSKYKKAVFREYTDGTFRIPRPRSGPEEHLGILGP 769
Cdd:cd04225   1 RTYYIAAEEVEWDYSPQRTWEQELHNTHEE-SPGNAFLNKGDKFIGSKYKKVVYREYTDDTFSVPKERTAEEEHLGILGP 79

                        90       100       110       120
                ....*....|....*....|....*....|....*....|....
gi 26349115 770 LIRGEVGDILTVVFKNKASRPYSIHAHGVLESNTgGPQAAEPGE 813
Cdd:cd04225  80 LIHAEVGEKVKIVFKNMASRPYSIHAHGVKTDSS-WVAPTEPGE 122
SufI COG2132
Multicopper oxidase with three cupredoxin domains (includes cell division protein FtsP and ...
 98-204 5.48e-09

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


Pssm-ID: 441735 [Multi-domain]  Cd Length: 423  Bit Score: 59.18  E-value: 5.48e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26349115  98 FLGPLLQAEVGDVILIHLKNFASRPYTIHPHGVfyekdsegsLYPDGSSGYlkADDSVPPGGSHVYNWSIPeshapteaD 177
Cdd:COG2132  42 YPGPTIRVREGDRVRVRVTNRLPEPTTVHWHGL---------RVPNAMDGV--PGDPIAPGETFTYEFPVP--------Q 102

                        90       100
                ....*....|....*....|....*....
gi 26349115 178 PACLTWiYHSHVDA--PRDIATGLIGPLI 204
Cdd:COG2132 103 PAGTYW-YHPHTHGstAEQVYRGLAGALI 130
Cu-oxidase_3 pfam07732
Multicopper oxidase; This entry contains many divergent copper oxidase-like domains that are ...
 98-204 6.02e-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: 54.56  E-value: 6.02e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26349115    98 FLGPLLQAEVGDVILIHLKNFASRPYTIHPHGVFyekdSEGSLYPDGSSGYlkADDSVPPGGSHVYNWSIPeshapteaD 177
Cdd:pfam07732  24 FPGPTIRVREGDTVVVNVTNNLDEPTSIHWHGLQ----QRGTPWMDGVPGV--TQCPIPPGQSFTYRFQVK--------Q 89

                          90       100
                  ....*....|....*....|....*..
gi 26349115   178 PACLTWiYHSHVDAPRdiATGLIGPLI 204
Cdd:pfam07732  90 QAGTYW-YHSHTSGQQ--AAGLAGAII 113
PLN02191 PLN02191
L-ascorbate oxidase
 98-231 8.00e-07

L-ascorbate oxidase


Pssm-ID: 177843 [Multi-domain]  Cd Length: 574  Bit Score: 52.71  E-value: 8.00e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26349115   98 FLGPLLQAEVGDVILIHLKN-FASRPYTIHPHGVfyekDSEGSLYPDGSSGYLKAddSVPPGGSHVYNWSIPESHaptea 176
Cdd:PLN02191  51 FPGPTIDAVAGDTIVVHLTNkLTTEGLVIHWHGI----RQKGSPWADGAAGVTQC--AINPGETFTYKFTVEKPG----- 119

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 26349115  177 dpaclTWIYHSHVDAPRdiATGLIGPLITCKrgtldGNSPPQRKDVDHNFFLLFS 231
Cdd:PLN02191 120 -----THFYHGHYGMQR--SAGLYGSLIVDV-----AKGPKERLRYDGEFNLLLS 162
Cu-oxidase pfam00394
Multicopper oxidase; Many of the proteins in this family contain multiple similar copies of ...
 230-367 1.66e-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: 48.47  E-value: 1.66e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26349115   230 FSVIDENLSWHlDDNIATYCSDPASVDKEDGAF---QDSnrmHAINGFVFGNLPELSMCAQKHVAWHLFgMGNEIDVHTA 306
Cdd:pfam00394   1 EDYVITLSDWY-HKDAKDLEKELLASGKAPTDFppvPDA---VLINGKDGASLATLTVTPGKTYRLRII-NVALDDSLNF 75

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 26349115   307 FFHGQMLSI---RGHHT-----DVANIFPATF----VTAemvPQKSGTWLISCEVN-SHLRSGMQAFYKVDSCS 367
Cdd:pfam00394  76 SIEGHKMTVvevDGVYVnpftvDSLDIFPGQRysvlVTA---NQDPGNYWIVASPNiPAFDNGTAAAILRYSGA 146
ascorbase TIGR03388
L-ascorbate oxidase, plant type; Members of this protein family are the copper-containing ...
 98-228 6.42e-06

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


Pssm-ID: 274555 [Multi-domain]  Cd Length: 541  Bit Score: 49.75  E-value: 6.42e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26349115    98 FLGPLLQAEVGDVILIHLKN-FASRPYTIHPHGVfyekDSEGSLYPDGSSGYLKAddSVPPGGSHVYNWSIPESHaptea 176
Cdd:TIGR03388  29 FPGPTIRAQAGDTIVVELTNkLHTEGVVIHWHGI----RQIGTPWADGTAGVTQC--AINPGETFIYNFVVDRPG----- 97

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|..
gi 26349115   177 dpaclTWIYHSHVDAPRdiATGLIGPLITCKRgtlDGNSPPQRKDVDHNFFL 228
Cdd:TIGR03388  98 -----TYFYHGHYGMQR--SAGLYGSLIVDVP---DGEKEPFHYDGEFNLLL 139
SufI COG2132
Multicopper oxidase with three cupredoxin domains (includes cell division protein FtsP and ...
 766-813 1.32e-03

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


Pssm-ID: 441735 [Multi-domain]  Cd Length: 423  Bit Score: 42.23  E-value: 1.32e-03
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|.
gi 26349115 766 ILGPLIRGEVGDILTVVFKNKASRPYSIHAHGVLESNT--GGPQAA-EPGE 813
Cdd:COG2132  42 YPGPTIRVREGDRVRVRVTNRLPEPTTVHWHGLRVPNAmdGVPGDPiAPGE 92
Cu-oxidase_3 pfam07732
Multicopper oxidase; This entry contains many divergent copper oxidase-like domains that are ...
 766-845 3.84e-03

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


Pssm-ID: 462247 [Multi-domain]  Cd Length: 119  Bit Score: 38.00  E-value: 3.84e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26349115   766 ILGPLIRGEVGDILTVVFKNKASRPYSIHAHGVLESNT-------GGPQAA-EPGElehlmkrQRLYNpFTLV-----FW 832
Cdd:pfam07732  24 FPGPTIRVREGDTVVVNVTNNLDEPTSIHWHGLQQRGTpwmdgvpGVTQCPiPPGQ-------SFTYR-FQVKqqagtYW 95

                          90
                  ....*....|...
gi 26349115   833 FIPFNILHSWAGQ 845
Cdd:pfam07732  96 YHSHTSGQQAAGL 108
Cu-oxidase_3 pfam07732
Multicopper oxidase; This entry contains many divergent copper oxidase-like domains that are ...
 455-494 3.99e-03

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


Pssm-ID: 462247 [Multi-domain]  Cd Length: 119  Bit Score: 38.00  E-value: 3.99e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|
gi 26349115   455 ILGPVIRAEVGDTIQVVFYNRASQPFSIQPHGVFYEKNSE 494
Cdd:pfam07732  24 FPGPTIRVREGDTVVVNVTNNLDEPTSIHWHGLQQRGTPW 63
 
Name Accession Description Interval E-value
CuRO_1_ceruloplasmin cd04222
The first cupredoxin domain of Ceruloplasmin; Ceruloplasmin is a multicopper oxidase essential ...
 26-208 1.38e-121

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


Pssm-ID: 259884 [Multi-domain]  Cd Length: 183  Bit Score: 364.43  E-value: 1.38e-121
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26349115  26 RNYYLGIQDMQWNYAPKGRNVITNQTLNNDTVASSFLKSGKNRIGSSYKKTVYKEYSDGTYTEEIAKPAWLGFLGPLLQA 105
Cdd:cd04222   1 REYYIGIRETQWDYAPSGKNLITNQTFDDDEHASVFLKRGPDRIGRVYKKAVYLQYTDDTYRTEIEKPVWLGFLGPILKA 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26349115 106 EVGDVILIHLKNFASRPYTIHPHGVFYEKDSEGSLYPDGSSGYLKADDSVPPGGSHVYNWSIPESHAPTEADPACLTWIY 185
Cdd:cd04222  81 EVGDVIVVHLKNFASRPYSLHPHGVFYNKENEGALYPDNTSGFEKADDAVPPGGSYTYTWTVPEEQAPTKADANCLTRIY 160

                       170       180
                ....*....|....*....|...
gi 26349115 186 HSHVDAPRDIATGLIGPLITCKR 208
Cdd:cd04222 161 HSHIDAPKDIASGLIGPLIICKK 183
CuRO_2_ceruloplasmin cd11021
The second cupredoxin domain of Ceruloplasmin; Ceruloplasmin is a multicopper oxidase ...
 223-363 3.16e-89

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: 278.20  E-value: 3.16e-89
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26349115 223 DHNFFLLFSVIDENLSWHLDDNIATYCSDPASVDKEDGAFQDSNRMHAINGFVFGNLPELSMCAQKHVAWHLFGMGNEID 302
Cdd:cd11021   1 DREFVLMFSVVDENLSWYLDENIKTYCSEPAKVDKDDEDFQESNKMHSINGYTFGNLPGLSMCAGDRVKWHLFGMGNEVD 80

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 26349115 303 VHTAFFHGQMLSIRGHHTDVANIFPATFVTAEMVPQKSGTWLISCEVNSHLRSGMQAFYKV 363
Cdd:cd11021  81 IHSAFFHGQTLTDRGHRTDTINLFPATFVTAEMVAQNPGKWLLSCQVNDHLKAGMQAFYEV 141
CuRO_3_ceruloplasmin cd04224
The third cupredoxin domain of Ceruloplasmin; Ceruloplasmin is a multicopper oxidase essential ...
 377-529 1.11e-85

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: 271.27  E-value: 1.11e-85
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26349115 377 GKVRQYFIQAHEIQWDYGPIGYDGRTGKSLREPGSGPDKYFQKSSSRIGGTYWKVRYEAFQDETFQERVHQ-EEETHLGI 455
Cdd:cd04224   1 GKVRHYFIAAEEIMWDYAPSGKNLFTGQNLTAPGSDSEVFFQRNETRIGGTYWKVRYVEYTDATFTTRKHRsKEEEHLGI 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26349115 456 LGPVIRAEVGDTIQVVFYNRASQPFSIQPHGVFYEKNSEGTVYND----------------------------------- 500
Cdd:cd04224  81 LGPVIRAEVGDTIKVTFRNKASRPFSIQPHGVFYEKNYEGAMYRDgdpspgshvspgetftyewtvpegvgptnqdppcl 160

                       170       180       190
                ....*....|....*....|....*....|....*..
gi 26349115 501 --------DPTRDTNSGLVGPLLVCKAGALGADGKQK 529
Cdd:cd04224 161 tylyfsavDPVRDTNSGLVGPLLVCKKGSLNANGRQK 197
CuRO_4_ceruloplasmin cd11022
The fourth cupredoxin domain of Ceruloplasmin; Ceruloplasmin is a multicopper oxidase ...
 532-675 3.84e-85

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: 267.81  E-value: 3.84e-85
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26349115 532 DKEFFLLFTVFDENESWYNNANQAAGMLDSRLLSEDVEGFQDSNRMHAINGFLFSNLPRLDMCKGDTVAWHLLGLGTETD 611
Cdd:cd11022   1 DKEFFLLFTVFDENESWYLDENIQQFTLDPRSVDKEDEDFQESNKMHSINGYMYGNQPGLDMCKGDTVSWHLFGLGTETD 80

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 26349115 612 VHGVMFEGNTVQLQGMRKGAVMLFPHTFVTAIMQPDNPGIFEIYCQAGSHREEGMQAIYNVSQC 675
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 2.18e-78

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


Pssm-ID: 259862 [Multi-domain]  Cd Length: 177  Bit Score: 251.17  E-value: 2.18e-78
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26349115  26 RNYYLGIQDMQWNYAPKGRNVITNQTLNndtvasSFLKSGKNRIGSSYKKTVYKEYSDGTYTEEIAKPAWLGFLGPLLQA 105
Cdd:cd04199   1 RHYYIAAEEIDWDYAPSGLAEKDLSYRN------QYLDNGPFRIGRSYKKVVYREYTDESFTTPGPQPEHLGILGPTIRA 74

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26349115 106 EVGDVILIHLKNFASRPYTIHPHGVFYEKDSEGSLYPDGSSGYLKADDSVPPGGSHVYNWSIPESHAPTEADPACLTWIY 185
Cdd:cd04199  75 EVGDTIKVHFKNKASRPYSIHPHGVSYEKDSEGASYSDQTGPDEKKDDAVAPGETYTYVWIVTEESGPTKGDPACLTWAY 154

                       170       180
                ....*....|....*....|...
gi 26349115 186 HSHVDAPRDIATGLIGPLITCKR 208
Cdd:cd04199 155 YSHVDLEKDINSGLIGPLLICKK 177
CuRO_3_ceruloplasmin cd04224
The third cupredoxin domain of Ceruloplasmin; Ceruloplasmin is a multicopper oxidase essential ...
 23-214 6.39e-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: 223.89  E-value: 6.39e-68
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26349115  23 GAIRNYYLGIQDMQWNYAPKGRNVITNQTLNN-DTVASSFLKSGKNRIGSSYKKTVYKEYSDGTYTEE---IAKPAWLGF 98
Cdd:cd04224   1 GKVRHYFIAAEEIMWDYAPSGKNLFTGQNLTApGSDSEVFFQRNETRIGGTYWKVRYVEYTDATFTTRkhrSKEEEHLGI 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26349115  99 LGPLLQAEVGDVILIHLKNFASRPYTIHPHGVFYEKDSEGSLYPDGSSgylKADDSVPPGGSHVYNWSIPESHAPTEADP 178
Cdd:cd04224  81 LGPVIRAEVGDTIKVTFRNKASRPFSIQPHGVFYEKNYEGAMYRDGDP---SPGSHVSPGETFTYEWTVPEGVGPTNQDP 157

                       170       180       190
                ....*....|....*....|....*....|....*.
gi 26349115 179 ACLTWIYHSHVDAPRDIATGLIGPLITCKRGTLDGN 214
Cdd:cd04224 158 PCLTYLYFSAVDPVRDTNSGLVGPLLVCKKGSLNAN 193
CuRO_5_ceruloplasmin cd04225
The fifth cupredoxin domain of Ceruloplasmin; Ceruloplasmin is a multicopper oxidase essential ...
 690-813 7.17e-67

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: 220.03  E-value: 7.17e-67
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26349115 690 RVYYIMAEEIEWDYCPDRSWELEWHNTSEKdSYGHVFLSNKDGLLGSKYKKAVFREYTDGTFRIPRPRSGPEEHLGILGP 769
Cdd:cd04225   1 RTYYIAAEEVEWDYSPQRTWEQELHNTHEE-SPGNAFLNKGDKFIGSKYKKVVYREYTDDTFSVPKERTAEEEHLGILGP 79

                        90       100       110       120
                ....*....|....*....|....*....|....*....|....
gi 26349115 770 LIRGEVGDILTVVFKNKASRPYSIHAHGVLESNTgGPQAAEPGE 813
Cdd:cd04225  80 LIHAEVGEKVKIVFKNMASRPYSIHAHGVKTDSS-WVAPTEPGE 122
CuRO_2_ceruloplasmin_like cd04200
Cupredoxin domains 2, 4, and 6 of ceruloplasmin and similar proteins; This family includes the ...
 223-363 2.88e-65

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


Pssm-ID: 259863 [Multi-domain]  Cd Length: 141  Bit Score: 214.20  E-value: 2.88e-65
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26349115 223 DHNFFLLFSVIDENLSWHLDDNIATYCSDPASVDKEDGAFQDSNRMHAINGFVFGNLPELSMCAQKHVAWHLFGMGNEID 302
Cdd:cd04200   1 DKEFVLLFAVFDENKSWYLEDNIKRFCDNPEKVDKDDEEFQESNKMHAINGYVFGNLPGLTMCAGDRVRWHLLGMGNEVD 80

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 26349115 303 VHTAFFHGQMLSIRGHHTDVANIFPATFVTAEMVPQKSGTWLISCEVNSHLRSGMQAFYKV 363
Cdd:cd04200  81 VHSIHFHGQTFLYKGYRIDTLTLFPATFETVEMVPSNPGTWLLHCHNSDHRHAGMQAYFLV 141
CuRO_4_ceruloplasmin cd11022
The fourth cupredoxin domain of Ceruloplasmin; Ceruloplasmin is a multicopper oxidase ...
 223-366 2.60e-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: 198.09  E-value: 2.60e-59
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26349115 223 DHNFFLLFSVIDENLSWHLDDNIATYCSDPASVDKEDGAFQDSNRMHAINGFVFGNLPELSMCAQKHVAWHLFGMGNEID 302
Cdd:cd11022   1 DKEFFLLFTVFDENESWYLDENIQQFTLDPRSVDKEDEDFQESNKMHSINGYMYGNQPGLDMCKGDTVSWHLFGLGTETD 80

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 26349115 303 VHTAFFHGQMLSIRGHHTDVANIFPATFVTAEMVPQKSGTWLISCEVNSHLRSGMQAFYKVDSC 366
Cdd:cd11022  81 VHGIYFSGNTFLLQGTRRDTANLFPHTSVTAIMQPDNEGTFEVNCQTTDHYSAGMRQIYTVSQC 144
CuRO_1_FV_like cd04226
The first cupredoxin domain of coagulation factor VIII and similar proteins; Factor V is an ...
 26-209 2.47e-56

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: 190.84  E-value: 2.47e-56
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26349115  26 RNYYLGIQDMQWNYAPKgrnvitnqtlnndtvaSSFLKSgkNRIGSSYKKTVYKEYSDGtYTEEIAKPAWLGFLGPLLQA 105
Cdd:cd04226   1 REYYIAAQNIDWDYTPQ----------------SEELRL--KRSEQSFKKIVYREYEEG-FKKEKPADLSSGLLGPTLRA 61

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26349115 106 EVGDVILIHLKNFASRPYTIHPHGVFYEKDSEGSLYPDGSSGYLKADDSVPPGGSHVYNWSIPESHAPTEADPACLTWIY 185
Cdd:cd04226  62 EVGDTLIVHFKNMADKPLSIHPQGIAYGKKSEGSLYSDNTSPVEKLDDAVQPGQEYTYVWDITEEVGPTEADPPCLTYIY 141

                       170       180
                ....*....|....*....|....
gi 26349115 186 HSHVDAPRDIATGLIGPLITCKRG 209
Cdd:cd04226 142 YSHVNMVRDFNSGLIGALLICKKG 165
CuRO_3_FV_like cd14450
The third cupredoxin domain of coagulation factor V and similar proteins; Factor V is an ...
 28-207 1.94e-54

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


Pssm-ID: 259992 [Multi-domain]  Cd Length: 181  Bit Score: 186.24  E-value: 1.94e-54
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26349115  28 YYLGIQDMQWNYAPkgrNVITNQtlnNDTVASSFLKSGKNRIGSSYKKTVYKEYSDGTYTE--EIAKPAWLGFLGPLLQA 105
Cdd:cd14450   5 YFIAAEEVIWDYAP---SIPENM---DKRYRSQYLDNFSNNIGKKYKKAVFTQYEDGSFTKrlENPRPKEEGILGPVIRA 78

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26349115 106 EVGDVILIHLKNFASRPYTIHPHGVFYEKDSEGSLYPDGSSGYLKADDSVPPGGSHVYNWSIPESHAPTEADPACLTWIY 185
Cdd:cd14450  79 QVRDTIKIVFKNKASRPYSIYPHGVTVSKAAEGASYPPDPRGNETQNKAVQPGETYTYKWNILETDEPTARDPRCLTRMY 158

                       170       180
                ....*....|....*....|..
gi 26349115 186 HSHVDAPRDIATGLIGPLITCK 207
Cdd:cd14450 159 HSAVDITRDIASGLIGPLLICK 180
CuRO_1_Ceruloplasmin_like_1 cd04229
cupredoxin domain of ceruloplasmin homologs; Uncharacterized subfamily of ceruloplasmin ...
 26-209 2.05e-54

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


Pssm-ID: 259891 [Multi-domain]  Cd Length: 175  Bit Score: 186.08  E-value: 2.05e-54
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26349115  26 RNYYLGIQDMQWNYAPKGRNVIT-NQTLNNDTVASSflkSGKNRIGSSYKKTVYKEYSDGTYTEEIAKPAWLGFLGPLLQ 104
Cdd:cd04229   1 RTYYIAAEEVDWDYAPSGKNKCClGDDLEVSTLDSQ---PGPYTIGSTYTKARYREYTDNSFSTPKPTPAYLGILGPVIR 77

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26349115 105 AEVGDVILIHLKN-FASRPYTIHPHGVFYEKDSEGSLYpdgssgylKADDSVPPGGSHVYNWSIPESHAPTEADPACLTW 183
Cdd:cd04229  78 AEVGDTIKVVFKNnLDEFPVNMHPHGGLYSKDNEGTTD--------GAGDVVAPGETYTYRWIVPEDAGPGPGDPSSRLW 149

                       170       180
                ....*....|....*....|....*.
gi 26349115 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 3.75e-54

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


Pssm-ID: 259993 [Multi-domain]  Cd Length: 173  Bit Score: 185.04  E-value: 3.75e-54
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26349115  26 RNYYLGIQDMQWNYAPKGRNVITNQTLNNDTVassflksgknrigssYKKTVYKEYSDGTYTEEIAKPAW---LGFLGPL 102
Cdd:cd14451   2 RRYYIAAEEEEWDYAGYGKSRLDKTQNERDTV---------------FKKVVFRRYLDSTFSTPDIQGEYeehLGILGPV 66

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26349115 103 LQAEVGDVILIHLKNFASRPYTIHPHGVFYEKDSEGSLYPDGSSGYLKADDSVPPGGSHVYNWSIPESHAPTEADPACLT 182
Cdd:cd14451  67 IRAEVDDVIQVFFKNLASRPYSLHAHGLSYEKSSEGLSYDDESPDWFKKDDAVQPNGTYTYVWYANPRSGPENNGSDCRT 146

                       170       180
                ....*....|....*....|....*..
gi 26349115 183 WIYHSHVDAPRDIATGLIGPLITCKRG 209
Cdd:cd14451 147 WAYYSAVNPEKDIHSGLIGPLLICRKG 173
CuRO_1_FVIII_like cd14452
The first cupredoxin domain of coagulation factor VIII and similar proteins; Factor VIII ...
 26-209 1.19e-53

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: 183.64  E-value: 1.19e-53
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26349115  26 RNYYLGIQDMQWNYapkgrnvitnqTLNNDTVASSFLKSGKNRIGSSYKKTVYKEYSDGTYTEEIAKPAWLGFLGPLLQA 105
Cdd:cd14452   1 RRYYIAAVEIGWDY-----------IHSDLGDPASEQRKKPKDIPQKYIKAVFVEYLDATFTVPKPRPAWMGLLGPTIVA 69

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26349115 106 EVGDVILIHLKNFASRPYTIHPHGVFYEKDSEGSLYPDGSSGYLKADDSVPPGGSHVYNWSIPESHAPTEADPACLTWIY 185
Cdd:cd14452  70 EVGDTVVITFKNLASQPYSLHAVGVSYWKASEGAGYDDSTSQHEKEDDAVYPGGYHTYVWDISPKDGPTGSDPECLTYSY 149

                       170       180
                ....*....|....*....|....
gi 26349115 186 HSHVDAPRDIATGLIGPLITCKRG 209
Cdd:cd14452 150 SSQVDPVKDVNSGLIGALLVCRMG 173
CuRO_2_ceruloplasmin cd11021
The second cupredoxin domain of Ceruloplasmin; Ceruloplasmin is a multicopper oxidase ...
 532-672 1.51e-49

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: 171.11  E-value: 1.51e-49
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26349115 532 DKEFFLLFTVFDENESWYNNANQAAGMLDSRLLSEDVEGFQDSNRMHAINGFLFSNLPRLDMCKGDTVAWHLLGLGTETD 611
Cdd:cd11021   1 DREFVLMFSVVDENLSWYLDENIKTYCSEPAKVDKDDEDFQESNKMHSINGYTFGNLPGLSMCAGDRVKWHLFGMGNEVD 80

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 26349115 612 VHGVMFEGNTVQLQGMRKGAVMLFPHTFVTAIMQPDNPGIFEIYCQAGSHREEGMQAIYNV 672
Cdd:cd11021  81 IHSAFFHGQTLTDRGHRTDTINLFPATFVTAEMVAQNPGKWLLSCQVNDHLKAGMQAFYEV 141
CuRO_6_ceruloplasmin cd11012
The sixth cupredoxin domain of Ceruloplasmin; Ceruloplasmin is a multicopper oxidase essential ...
 226-363 6.19e-47

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: 163.89  E-value: 6.19e-47
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26349115 226 FFLLFSVIDENLSWHLDDNIATYCSDPASVDKEDGAFQDSNRMHAINGFVFGNLPELSMCAQKHVAWHLFGMGNEIDVHT 305
Cdd:cd11012   4 FALLFLVFDENESWYLDENIKTYSDHPEKVNKEDEEFIESNKMHAINGKVFGNLQGLTMHVGDEVYWYLMGMGNEIDIHT 83

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 26349115 306 AFFHGQMLSIR---GHHTDVANIFPATFVTAEMVPQKSGTWLISCEVNSHLRSGMQAFYKV 363
Cdd:cd11012  84 AHFHGHSFDYKhrgVYRSDVFDLFPGTFQTVEMIPRTPGTWLLHCHVTDHIHAGMETTYTV 144
CuRO_5_ceruloplasmin cd04225
The fifth cupredoxin domain of Ceruloplasmin; Ceruloplasmin is a multicopper oxidase essential ...
 26-208 2.65e-46

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


Pssm-ID: 259887 [Multi-domain]  Cd Length: 171  Bit Score: 163.02  E-value: 2.65e-46
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26349115  26 RNYYLGIQDMQWNYAPKGRNVITNQTLNNDTVASSFLKSGKNRIGSSYKKTVYKEYSDGTYT---EEIAKPAWLGFLGPL 102
Cdd:cd04225   1 RTYYIAAEEVEWDYSPQRTWEQELHNTHEESPGNAFLNKGDKFIGSKYKKVVYREYTDDTFSvpkERTAEEEHLGILGPL 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26349115 103 LQAEVGDVILIHLKNFASRPYTIHPHGVfyekdsegslypdgssgylKADDSVP----PGGSHVYNWSIPESHAPTEADP 178
Cdd:cd04225  81 IHAEVGEKVKIVFKNMASRPYSIHAHGV-------------------KTDSSWVaptePGETQTYTWKIPERSGPGVEDS 141

                       170       180       190
                ....*....|....*....|....*....|
gi 26349115 179 ACLTWIYHSHVDAPRDIATGLIGPLITCKR 208
Cdd:cd04225 142 NCISWAYYSTVDQIKDLYSGLIGPLVICRR 171
CuRO_2_ceruloplasmin_like cd04200
Cupredoxin domains 2, 4, and 6 of ceruloplasmin and similar proteins; This family includes the ...
 532-672 1.19e-45

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: 160.27  E-value: 1.19e-45
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26349115 532 DKEFFLLFTVFDENESWYNNANQAAGMLDSRLLSEDVEGFQDSNRMHAINGFLFSNLPRLDMCKGDTVAWHLLGLGTETD 611
Cdd:cd04200   1 DKEFVLLFAVFDENKSWYLEDNIKRFCDNPEKVDKDDEEFQESNKMHAINGYVFGNLPGLTMCAGDRVRWHLLGMGNEVD 80

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 26349115 612 VHGVMFEGNTVQLQGMRKGAVMLFPHTFVTAIMQPDNPGIFEIYCQAGSHREEGMQAIYNV 672
Cdd:cd04200  81 VHSIHFHGQTFLYKGYRIDTLTLFPATFETVEMVPSNPGTWLLHCHNSDHRHAGMQAYFLV 141
CuRO_3_FVIII_like cd04227
The third cupredoxin domain of coagulation factor VIII and similar proteins; Factor VIII ...
 28-208 1.95e-43

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


Pssm-ID: 259889 [Multi-domain]  Cd Length: 177  Bit Score: 155.47  E-value: 1.95e-43
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26349115  28 YYLGIQDMQWNYAPkgrnvITNQTLNNDtVASSFLKSGKNRIGSSYKKTVYKEYSDGTYTEEIAKPAWLGFLGPLLQAEV 107
Cdd:cd04227   5 HYIAAEELDWDYAP-----LLSSTDDRE-LQSRYLPTGPQRIGYKYKKVAFVEYTDKTFKRREAKQTEKGILGPLLKGEV 78

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26349115 108 GDVILIHLKNFASRPYTIHPHGVFYEKDSEGSLYPDGSSgYLKaDDSVPPGGSHVYNWSIPESHAPTEADPACLTWIYHS 187
Cdd:cd04227  79 GDQIHIMFKNTASRPYNIYPHGLTSVRPMYRSRNPAGEK-DLK-TMPIGPGETFGYMWELTAEDGPTEEDPRCLTRLYQS 156

                       170       180
                ....*....|....*....|.
gi 26349115 188 HVDAPRDIATGLIGPLITCKR 208
Cdd:cd04227 157 TVDPERDLASGLIGPLLICKK 177
CuRO_1_ceruloplasmin_like cd04199
Cupredoxin domains 1, 3, and 5 of ceruloplasmin and similar proteins; This family includes the ...
 380-519 4.61e-42

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: 151.40  E-value: 4.61e-42
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26349115 380 RQYFIQAHEIQWDYGPIGydgrTGKSLREPGSgpdKYFQKSSSRIGGTYWKVRYEAFQDETFqeRVHQEEETHLGILGPV 459
Cdd:cd04199   1 RHYYIAAEEIDWDYAPSG----LAEKDLSYRN---QYLDNGPFRIGRSYKKVVYREYTDESF--TTPGPQPEHLGILGPT 71

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26349115 460 IRAEVGDTIQVVFYNRASQPFSIQPHGVFYEKNSEGTVYND--------------------------------------- 500
Cdd:cd04199  72 IRAEVGDTIKVHFKNKASRPYSIHPHGVSYEKDSEGASYSDqtgpdekkddavapgetytyvwivteesgptkgdpaclt 151

                       170       180
                ....*....|....*....|....*.
gi 26349115 501 -------DPTRDTNSGLVGPLLVCKA 519
Cdd:cd04199 152 wayyshvDLEKDINSGLIGPLLICKK 177
CuRO_1_ceruloplasmin_like cd04199
Cupredoxin domains 1, 3, and 5 of ceruloplasmin and similar proteins; This family includes the ...
 690-798 1.03e-40

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: 147.55  E-value: 1.03e-40
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26349115 690 RVYYIMAEEIEWDYCPDRSWELEWHNTSekdsyghVFLSNKDGLLGSKYKKAVFREYTDGTFRIPRPRsgpEEHLGILGP 769
Cdd:cd04199   1 RHYYIAAEEIDWDYAPSGLAEKDLSYRN-------QYLDNGPFRIGRSYKKVVYREYTDESFTTPGPQ---PEHLGILGP 70

                        90       100
                ....*....|....*....|....*....
gi 26349115 770 LIRGEVGDILTVVFKNKASRPYSIHAHGV 798
Cdd:cd04199  71 TIRAEVGDTIKVHFKNKASRPYSIHPHGV 99
CuRO_3_ceruloplasmin cd04224
The third cupredoxin domain of Ceruloplasmin; Ceruloplasmin is a multicopper oxidase essential ...
 690-805 3.21e-38

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: 141.07  E-value: 3.21e-38
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26349115 690 RVYYIMAEEIEWDYCPDRSWELEWHNTSEKDSYGHVFLSNKDGLLGSKYKKAVFREYTDGTFRIPRPRSGPEEHLGILGP 769
Cdd:cd04224   4 RHYFIAAEEIMWDYAPSGKNLFTGQNLTAPGSDSEVFFQRNETRIGGTYWKVRYVEYTDATFTTRKHRSKEEEHLGILGP 83

                        90       100       110
                ....*....|....*....|....*....|....*..
gi 26349115 770 LIRGEVGDILTVVFKNKASRPYSIHAHGVL-ESNTGG 805
Cdd:cd04224  84 VIRAEVGDTIKVTFRNKASRPFSIQPHGVFyEKNYEG 120
CuRO_5_FV_like cd14451
The fifth cupredoxin domain of coagulation factor V and similar proteins; Factor V is an ...
 380-520 2.35e-36

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: 134.97  E-value: 2.35e-36
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26349115 380 RQYFIQAHEIQWDYGPIGYDGRTGKSLREPGsgpdkyfqksssriggTYWKVRYEAFQDETFQER-VHQEEETHLGILGP 458
Cdd:cd14451   2 RRYYIAAEEEEWDYAGYGKSRLDKTQNERDT----------------VFKKVVFRRYLDSTFSTPdIQGEYEEHLGILGP 65

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26349115 459 VIRAEVGDTIQVVFYNRASQPFSIQPHGVFYEKNSEGTVYNDD------------------------------------- 501
Cdd:cd14451  66 VIRAEVDDVIQVFFKNLASRPYSLHAHGLSYEKSSEGLSYDDEspdwfkkddavqpngtytyvwyanprsgpenngsdcr 145

                       170       180
                ....*....|....*....|....*...
gi 26349115 502 ---------PTRDTNSGLVGPLLVCKAG 520
Cdd:cd14451 146 twayysavnPEKDIHSGLIGPLLICRKG 173
CuRO_6_FVIII_like cd11018
The sixth cupredoxin domain of coagulation factor VIII and similar proteins; Factor VIII ...
 226-363 4.10e-36

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: 133.08  E-value: 4.10e-36
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26349115 226 FFLLFSVIDENLSWHLDDNIATYCSDPASVDKEDGAFQDSNRMHAINGFVFGNLPELSMCAQKHVAWHLFGMGNEIDVHT 305
Cdd:cd11018   4 FALLFTIFDETKSWYFEENMRRNCRPPCHIQTQDPWFHINNKFHAINGYVADTLPGLVMAQHQRIRWHLLNMGSDEEIHS 83

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 26349115 306 AFFHGQMLSIRG---HHTDVANIFPATFVTAEMVPQKSGTWLISCEVNSHLRSGMQAFYKV 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 3.02e-35

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: 131.55  E-value: 3.02e-35
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26349115  25 IRNYYLGIQDMQWNYA-PKGRNVITNQTLNndtvassflkSGKNRIGSSYKKTVYKEYSDGTYTEEIAK---PAWLGFLG 100
Cdd:cd04228   1 IRHYFIAAVEVLWDYGmQRPQHFLRARDPN----------RGRRKSVPQYKKVVFREYLDGSFTQPVYRgelDEHLGILG 70

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26349115 101 PLLQAEVGDVILIHLKNFASRPYTIHPHGVFYEKDsegslypdGSSGYLKadDSVPPGGSHVYNWSIPESHAPTEADPAC 180
Cdd:cd04228  71 PYIRAEVEDNIMVTFKNLASRPYSFHSSLISYEED--------QRAEPRG--NFVQPGEVQTYSWKVLHQMAPTKQEFDC 140

                       170       180
                ....*....|....*....|....*....
gi 26349115 181 LTWIYHSHVDAPRDIATGLIGPLITCKRG 209
Cdd:cd04228 141 KAWAYFSNVDLEKDLHSGLIGPLIICKTG 169
CuRO_1_Ceruloplasmin_like_1 cd04229
cupredoxin domain of ceruloplasmin homologs; Uncharacterized subfamily of ceruloplasmin ...
 380-520 8.52e-34

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: 127.92  E-value: 8.52e-34
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26349115 380 RQYFIQAHEIQWDYGPIGYDGRTGKSLREPGSGpdkYFQKSSSRIGGTYWKVRYEAFQDETFQERVHQEEetHLGILGPV 459
Cdd:cd04229   1 RTYYIAAEEVDWDYAPSGKNKCCLGDDLEVSTL---DSQPGPYTIGSTYTKARYREYTDNSFSTPKPTPA--YLGILGPV 75

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26349115 460 IRAEVGDTIQVVFYNRASQ-PFSIQPHGVFYEKNSEGT------------------------------------VYND-- 500
Cdd:cd04229  76 IRAEVGDTIKVVFKNNLDEfPVNMHPHGGLYSKDNEGTtdgagdvvapgetytyrwivpedagpgpgdpssrlwLYHShv 155

                       170       180
                ....*....|....*....|
gi 26349115 501 DPTRDTNSGLVGPLLVCKAG 520
Cdd:cd04229 156 DVFAHTNAGLVGPIIVTSKG 175
CuRO_3_FV_like cd14450
The third cupredoxin domain of coagulation factor V and similar proteins; Factor V is an ...
 378-519 3.27e-33

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: 126.15  E-value: 3.27e-33
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26349115 378 KVRQYFIQAHEIQWDYGPIGYDGRTGKSlrepgsgPDKYFQKSSSRIGGTYWKVRYEAFQDETFQERVHQEEETHLGILG 457
Cdd:cd14450   1 KNWEYFIAAEEVIWDYAPSIPENMDKRY-------RSQYLDNFSNNIGKKYKKAVFTQYEDGSFTKRLENPRPKEEGILG 73

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26349115 458 PVIRAEVGDTIQVVFYNRASQPFSIQPHGVFYEKNSEGTVYNDDP----------------------------------- 502
Cdd:cd14450  74 PVIRAQVRDTIKIVFKNKASRPYSIYPHGVTVSKAAEGASYPPDPrgnetqnkavqpgetytykwniletdeptardprc 153

                       170       180
                ....*....|....*....|....*...
gi 26349115 503 -----------TRDTNSGLVGPLLVCKA 519
Cdd:cd14450 154 ltrmyhsavdiTRDIASGLIGPLLICKS 181
CuRO_6_ceruloplasmin cd11012
The sixth cupredoxin domain of Ceruloplasmin; Ceruloplasmin is a multicopper oxidase essential ...
 533-672 1.00e-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: 120.74  E-value: 1.00e-31
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26349115 533 KEFFLLFTVFDENESWYNNANQAAGMLDSRLLSEDVEGFQDSNRMHAINGFLFSNLPRLDMCKGDTVAWHLLGLGTETDV 612
Cdd:cd11012   2 LEFALLFLVFDENESWYLDENIKTYSDHPEKVNKEDEEFIESNKMHAINGKVFGNLQGLTMHVGDEVYWYLMGMGNEIDI 81

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 26349115 613 HGVMFEGNTVQLQ--GMRKGAVM-LFPHTFVTAIMQPDNPGIFEIYCQAGSHREEGMQAIYNV 672
Cdd:cd11012  82 HTAHFHGHSFDYKhrGVYRSDVFdLFPGTFQTVEMIPRTPGTWLLHCHVTDHIHAGMETTYTV 144
CuRO_1_ceruloplasmin cd04222
The first cupredoxin domain of Ceruloplasmin; Ceruloplasmin is a multicopper oxidase essential ...
 380-518 1.63e-31

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: 121.37  E-value: 1.63e-31
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26349115 380 RQYFIQAHEIQWDYGPIGYDGRTGKSLREpgsgpDK----YFQKSSSRIGGTYWKVRYEAFQDETFQERVhqEEETHLGI 455
Cdd:cd04222   1 REYYIGIRETQWDYAPSGKNLITNQTFDD-----DEhasvFLKRGPDRIGRVYKKAVYLQYTDDTYRTEI--EKPVWLGF 73

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26349115 456 LGPVIRAEVGDTIQVVFYNRASQPFSIQPHGVFYEKNSEGTVY---------NDD-------------------PT---- 503
Cdd:cd04222  74 LGPILKAEVGDVIVVHLKNFASRPYSLHPHGVFYNKENEGALYpdntsgfekADDavppggsytytwtvpeeqaPTkada 153

                       170       180
                ....*....|....*....|....*....
gi 26349115 504 --------------RDTNSGLVGPLLVCK 518
Cdd:cd04222 154 ncltriyhshidapKDIASGLIGPLIICK 182
CuRO_5_ceruloplasmin cd04225
The fifth cupredoxin domain of Ceruloplasmin; Ceruloplasmin is a multicopper oxidase essential ...
 380-518 2.08e-31

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: 120.65  E-value: 2.08e-31
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26349115 380 RQYFIQAHEIQWDYGPigydGRTGKSLREPGSGP---DKYFQKSSSRIGGTYWKVRYEAFQDETFQERV-HQEEETHLGI 455
Cdd:cd04225   1 RTYYIAAEEVEWDYSP----QRTWEQELHNTHEEspgNAFLNKGDKFIGSKYKKVVYREYTDDTFSVPKeRTAEEEHLGI 76

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26349115 456 LGPVIRAEVGDTIQVVFYNRASQPFSIQPHGV-------------------FYEKNSEGTVYND------------DPTR 504
Cdd:cd04225  77 LGPLIHAEVGEKVKIVFKNMASRPYSIHAHGVktdsswvaptepgetqtytWKIPERSGPGVEDsnciswayystvDQIK 156

                       170
                ....*....|....
gi 26349115 505 DTNSGLVGPLLVCK 518
Cdd:cd04225 157 DLYSGLIGPLVICR 170
CuRO_5_FV_like cd14451
The fifth cupredoxin domain of coagulation factor V and similar proteins; Factor V is an ...
 690-799 2.13e-31

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: 120.72  E-value: 2.13e-31
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26349115 690 RVYYIMAEEIEWDYCPDRSWELEWHNTSEKDSYghvflsnkdgllgskyKKAVFREYTDGTFRIPRPRSGPEEHLGILGP 769
Cdd:cd14451   2 RRYYIAAEEEEWDYAGYGKSRLDKTQNERDTVF----------------KKVVFRRYLDSTFSTPDIQGEYEEHLGILGP 65

                        90       100       110
                ....*....|....*....|....*....|
gi 26349115 770 LIRGEVGDILTVVFKNKASRPYSIHAHGVL 799
Cdd:cd14451  66 VIRAEVDDVIQVFFKNLASRPYSLHAHGLS 95
CuRO_4_FVIII_like cd11016
The fourth cupredoxin domain of coagulation factor VIII and similar proteins; Factor VIII ...
 223-366 3.46e-31

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


Pssm-ID: 259902 [Multi-domain]  Cd Length: 143  Bit Score: 119.20  E-value: 3.46e-31
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26349115 223 DHNFFLLFSVIDENLSWHLDDNIATYCSDPASVDKEDGAFQDSNRMHAINGFVFGNLpELSMCAQKHVAWHLFGMGNEID 302
Cdd:cd11016   1 DKDWSLLFSVFDENNSWYLKENIHRFTQTPAGVNDTDPDFYASNVMHTINGIVFDRR-QFVICLTDVAYWYVLSVGAQTD 79

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 26349115 303 VHTAFFHGQMLSIRGHHTDVANIFPATFVTAEMVPQKSGTWLISCeVNSHLRS-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 ...
 532-675 3.57e-31

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


Pssm-ID: 259902 [Multi-domain]  Cd Length: 143  Bit Score: 119.20  E-value: 3.57e-31
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26349115 532 DKEFFLLFTVFDENESWYNNAN------QAAGMLDsrllsEDVEgFQDSNRMHAINGFLFSNLpRLDMCKGDTVAWHLLG 605
Cdd:cd11016   1 DKDWSLLFSVFDENNSWYLKENihrftqTPAGVND-----TDPD-FYASNVMHTINGIVFDRR-QFVICLTDVAYWYVLS 73

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26349115 606 LGTETDVHGVMFEGNTVQLQGMRKGAVMLFPHTFVTAIMQPDNPGIFEIYCQAGSHREEGMQAIYNVSQC 675
Cdd:cd11016  74 VGAQTDFLSVFFSGNTFKHQMVYEDVLTLFPFSGETVSMSPEVPGEWELGCFNGDFRSRGMSAQYTVSTC 143
CuRO_2_FVIII_like cd11015
The second cupredoxin domain of coagulation factor VIII and similar proteins; Factor VIII ...
 224-363 3.73e-31

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: 118.85  E-value: 3.73e-31
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26349115 224 HNFFLLFSVIDENLSWHLDDniatycSDPASVDKEDGAfQDSNRMHAINGFVFGNLPELSMCAQKHVAWHLFGMGNEIDV 303
Cdd:cd11015   2 QAFVLLFAVFDEGKSWYSEV------GERKSRDKFKRA-DSRKEFHTINGYINASLPGLKICQRKPVIWHVIGMGTAPEV 74

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|
gi 26349115 304 HTAFFHGQMLSIRGHHTDVANIFPATFVTAEMVPQKSGTWLISCEVNSHLRSGMQAFYKV 363
Cdd:cd11015  75 HSIFFEGHTFLVRTHRKVSLEISPMTFLTAQTKPATVGSFLIFCQIHSHQHDGMEAMVKV 134
CuRO_3_FV_like cd14450
The third cupredoxin domain of coagulation factor V and similar proteins; Factor V is an ...
 692-813 4.27e-31

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: 120.37  E-value: 4.27e-31
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26349115 692 YYIMAEEIEWDYCPDRSwelewHNTSEKdsYGHVFLSNKDGLLGSKYKKAVFREYTDGTFRIPRPRSGPEEhLGILGPLI 771
Cdd:cd14450   5 YFIAAEEVIWDYAPSIP-----ENMDKR--YRSQYLDNFSNNIGKKYKKAVFTQYEDGSFTKRLENPRPKE-EGILGPVI 76

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*.
gi 26349115 772 RGEVGDILTVVFKNKASRPYSIHAHGVLES--------------NTGGPQAAEPGE 813
Cdd:cd14450  77 RAQVRDTIKIVFKNKASRPYSIYPHGVTVSkaaegasyppdprgNETQNKAVQPGE 132
CuRO_1_ceruloplasmin cd04222
The first cupredoxin domain of Ceruloplasmin; Ceruloplasmin is a multicopper oxidase essential ...
 690-813 1.34e-29

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: 115.98  E-value: 1.34e-29
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26349115 690 RVYYIMAEEIEWDYCPDRSwELEWHNTSEKDSYGHVFLSNKDGLLGSKYKKAVFREYTDGTFR--IPRPrsgpeEHLGIL 767
Cdd:cd04222   1 REYYIGIRETQWDYAPSGK-NLITNQTFDDDEHASVFLKRGPDRIGRVYKKAVYLQYTDDTYRteIEKP-----VWLGFL 74

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|
gi 26349115 768 GPLIRGEVGDILTVVFKNKASRPYSIHAHGVL---ES-------NTGGPQ----AAEPGE 813
Cdd:cd04222  75 GPILKAEVGDVIVVHLKNFASRPYSLHPHGVFynkENegalypdNTSGFEkaddAVPPGG 134
CuRO_2_FVIII_like cd11015
The second cupredoxin domain of coagulation factor VIII and similar proteins; Factor VIII ...
 533-672 1.35e-29

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: 114.23  E-value: 1.35e-29
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26349115 533 KEFFLLFTVFDENESWYnnanqaaGMLDSRLLSEDVEGFQDSNRMHAINGFLFSNLPRLDMCKGDTVAWHLLGLGTETDV 612
Cdd:cd11015   2 QAFVLLFAVFDEGKSWY-------SEVGERKSRDKFKRADSRKEFHTINGYINASLPGLKICQRKPVIWHVIGMGTAPEV 74

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|
gi 26349115 613 HGVMFEGNTVQLQGMRKGAVMLFPHTFVTAIMQPDNPGIFEIYCQAGSHREEGMQAIYNV 672
Cdd:cd11015  75 HSIFFEGHTFLVRTHRKVSLEISPMTFLTAQTKPATVGSFLIFCQIHSHQHDGMEAMVKV 134
CuRO_1_Ceruloplasmin_like_1 cd04229
cupredoxin domain of ceruloplasmin homologs; Uncharacterized subfamily of ceruloplasmin ...
 690-813 3.79e-29

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: 114.44  E-value: 3.79e-29
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26349115 690 RVYYIMAEEIEWDY---------CPDRSW-ELEWhntSEKDSYGhvflsnkdglLGSKYKKAVFREYTDGTFRIPRPRsg 759
Cdd:cd04229   1 RTYYIAAEEVDWDYapsgknkccLGDDLEvSTLD---SQPGPYT----------IGSTYTKARYREYTDNSFSTPKPT-- 65

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 26349115 760 pEEHLGILGPLIRGEVGDILTVVFKNKASR-PYSIHAHGVL--ESNTGGPQAA----EPGE 813
Cdd:cd04229  66 -PAYLGILGPVIRAEVGDTIKVVFKNNLDEfPVNMHPHGGLysKDNEGTTDGAgdvvAPGE 125
CuRO_2_ceruloplasmin_like_2 cd11023
cupredoxin domain of ceruloplasmin homologs; Uncharacterized subfamily of ceruloplasmin ...
 256-363 6.13e-29

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: 111.93  E-value: 6.13e-29
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26349115 256 DKEDGafQDSNRMHAINGFVFGNLPELSMCAQKHVAWHLFGMGNEIDVHTAFFHGQMLSIRGH-HTDVANIFPATFVTAE 334
Cdd:cd11023  12 LDLNV--EEAGLMHSINGYVFGNLPGVTIAKGKRVRWHLVAYGNEVDFHTPHWHGQTVEADKSrRTDVAELMPASMRVAD 89

                        90       100
                ....*....|....*....|....*....
gi 26349115 335 MVPQKSGTWLISCEVNSHLRSGMQAFYKV 363
Cdd:cd11023  90 MTAADVGTWLLHCHVHDHYMAGMMTQFAV 118
CuRO_5_FVIII_like cd04228
The fifth cupredoxin domain of coagulation factor VIII and similar proteins; Factor VIII ...
 690-815 1.99e-28

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: 112.29  E-value: 1.99e-28
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26349115 690 RVYYIMAEEIEWDYCPDRSWELEWHNTSEKDSYGHVflsnkdgllgSKYKKAVFREYTDGTFRIPRPRSGPEEHLGILGP 769
Cdd:cd04228   2 RHYFIAAVEVLWDYGMQRPQHFLRARDPNRGRRKSV----------PQYKKVVFREYLDGSFTQPVYRGELDEHLGILGP 71

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|
gi 26349115 770 LIRGEVGDILTVVFKNKASRPYSIHAHGVLESNTG----GPQAAEPGELE 815
Cdd:cd04228  72 YIRAEVEDNIMVTFKNLASRPYSFHSSLISYEEDQraepRGNFVQPGEVQ 121
CuRO_5_FVIII_like cd04228
The fifth cupredoxin domain of coagulation factor VIII and similar proteins; Factor VIII ...
 379-520 6.24e-28

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: 110.75  E-value: 6.24e-28
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26349115 379 VRQYFIQAHEIQWDYGpigyDGRTGKSLR--EPGSGPDKYFQKsssriggtYWKVRYEAFQDETFQERVHQEE-ETHLGI 455
Cdd:cd04228   1 IRHYFIAAVEVLWDYG----MQRPQHFLRarDPNRGRRKSVPQ--------YKKVVFREYLDGSFTQPVYRGElDEHLGI 68

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26349115 456 LGPVIRAEVGDTIQVVFYNRASQPFSIQPHGVFYEKNSE-----------------------------------GTVYND 500
Cdd:cd04228  69 LGPYIRAEVEDNIMVTFKNLASRPYSFHSSLISYEEDQRaeprgnfvqpgevqtyswkvlhqmaptkqefdckaWAYFSN 148

                       170       180
                ....*....|....*....|.
gi 26349115 501 -DPTRDTNSGLVGPLLVCKAG 520
Cdd:cd04228 149 vDLEKDLHSGLIGPLIICKTG 169
CuRO_6_FV_like cd14455
The sixth cupredoxin domain of coagulation factor V and similar proteins; Factor V is an ...
 226-363 1.34e-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: 1.34e-27
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26349115 226 FFLLFSVIDENLSWHLDDNIATYCSDPASVDKEdgaFQDSNRMHAINGFVFgNLPELSMCAQKHVAWHLFGMGNEIDVHT 305
Cdd:cd14455   4 FVLLFMTFDEEKSWYYEKNRKRTCRENRVKDPN---VQDNHTFHAINGIIY-NLKGLRMYTNELVRWHLINMGGPKDLHV 79

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 26349115 306 AFFHGQMLSIRG---HHTDVANIFPATFVTAEMVPQKSGTWLISCEVNSHLRSGMQAFYKV 363
Cdd:cd14455  80 VHFHGQTFTEKGlkdHQLGVYPLLPGSFATLEMKPSKPGLWLLETEVGESQQRGMQTLFLV 140
CuRO_3_FVIII_like cd04227
The third cupredoxin domain of coagulation factor VIII and similar proteins; Factor VIII ...
 378-518 4.30e-27

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: 108.48  E-value: 4.30e-27
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26349115 378 KVRQYFIQAHEIQWDYGPI--GYDGRTGKSLrepgsgpdkYFQKSSSRIGGTYWKVRYEAFQDETFQERVHQEEEThlGI 455
Cdd:cd04227   1 QTWEHYIAAEELDWDYAPLlsSTDDRELQSR---------YLPTGPQRIGYKYKKVAFVEYTDKTFKRREAKQTEK--GI 69

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26349115 456 LGPVIRAEVGDTIQVVFYNRASQPFSIQPHGV------FYEKNSEGT--------------------VYND--------- 500
Cdd:cd04227  70 LGPLLKGEVGDQIHIMFKNTASRPYNIYPHGLtsvrpmYRSRNPAGEkdlktmpigpgetfgymwelTAEDgpteedprc 149

                       170       180
                ....*....|....*....|....*..
gi 26349115 501 ---------DPTRDTNSGLVGPLLVCK 518
Cdd:cd04227 150 ltrlyqstvDPERDLASGLIGPLLICK 176
CuRO_4_FV_like cd14454
The fourth cupredoxin domain of coagulation factor V and similar proteins; Factor V is an ...
 229-366 5.06e-27

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


Pssm-ID: 259996 [Multi-domain]  Cd Length: 144  Bit Score: 107.26  E-value: 5.06e-27
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26349115 229 LFSVIDENLSWHLDDNIATYCSDPASVDKEDGAFQDSNRMHAINGFVFGNLPELSMCAQKHVAWHLFGMGNEIDVHTAFF 308
Cdd:cd14454   7 VFAVFDENKSWYLEENINKYCSNPNNVKKDDPKFYKSNIMPTINGYAYESSAPLGFCHSEVVQWHISSVGTQDEIITVHL 86

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*....
gi 26349115 309 HGQMLSIRGHHTDVANIFPATFVTAEMVPQKSGTWLIScEVNSHLRS-GMQAFYKVDSC 366
Cdd:cd14454  87 SGHTFRYKGKHEDTLNLFPMSGESITVTMDNLGTWLLG-SFGSSKKSkGLRVRFTDVIC 144
CuRO_2_FV_like cd14453
The second cupredoxin domain of coagulation factor V and similar proteins; Factor V is an ...
 223-363 5.56e-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: 106.48  E-value: 5.56e-27
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26349115 223 DHNFFLLFSVIDENLSWHLDDNiatycsdpasvdkedgafQDSNRMHAINGFVFGNLPELSMCAQKHVAWHLFGMGNEID 302
Cdd:cd14453   1 YKEYVLMFGVFDENKSWYKQNA------------------SVDSVKYTINGYTNGTLPDVSICAYDHVSWHLLGMSSEPE 62

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 26349115 303 VHTAFFHGQMLSIRGHHTDVANIFPATFVTAEMVPQKSGTWLISCEVNSHLRSGMQAFYKV 363
Cdd:cd14453  63 LFSVHFNGQVLEQNGHKVSAVGLVSGSSTTASMTVVHTGRWLISSLIMKHLQAGMYGYLNI 123
CuRO_3_FVIII_like cd04227
The third cupredoxin domain of coagulation factor VIII and similar proteins; Factor VIII ...
 691-798 9.69e-27

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: 107.71  E-value: 9.69e-27
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26349115 691 VYYIMAEEIEWDYCPDRSwelewhnTSEKDSYGHVFLSNKDGLLGSKYKKAVFREYTDGTFRiprPRSGPEEHLGILGPL 770
Cdd:cd04227   4 EHYIAAEELDWDYAPLLS-------STDDRELQSRYLPTGPQRIGYKYKKVAFVEYTDKTFK---RREAKQTEKGILGPL 73

                        90       100
                ....*....|....*....|....*...
gi 26349115 771 IRGEVGDILTVVFKNKASRPYSIHAHGV 798
Cdd:cd04227  74 LKGEVGDQIHIMFKNTASRPYNIYPHGL 101
CuRO_6_FV_like cd14455
The sixth cupredoxin domain of coagulation factor V and similar proteins; Factor V is an ...
 533-672 3.31e-25

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: 101.87  E-value: 3.31e-25
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26349115 533 KEFFLLFTVFDENESWYNNANQAAGMLDSRLLSEdveGFQDSNRMHAINGFLFsNLPRLDMCKGDTVAWHLLGLGTETDV 612
Cdd:cd14455   2 REFVLLFMTFDEEKSWYYEKNRKRTCRENRVKDP---NVQDNHTFHAINGIIY-NLKGLRMYTNELVRWHLINMGGPKDL 77

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 26349115 613 HGVMFEGNTV---QLQGMRKGAVMLFPHTFVTAIMQPDNPGIFEIYCQAGSHREEGMQAIYNV 672
Cdd:cd14455  78 HVVHFHGQTFtekGLKDHQLGVYPLLPGSFATLEMKPSKPGLWLLETEVGESQQRGMQTLFLV 140
CuRO_1_FV_like cd04226
The first cupredoxin domain of coagulation factor VIII and similar proteins; Factor V is an ...
 380-520 9.15e-25

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: 101.47  E-value: 9.15e-25
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26349115 380 RQYFIQAHEIQWDYGPigydgrtgkslrepgsgpdKYFQKSSSRIGGTYWKVRYEAFQDETFQERVHQEEEthlGILGPV 459
Cdd:cd04226   1 REYYIAAQNIDWDYTP-------------------QSEELRLKRSEQSFKKIVYREYEEGFKKEKPADLSS---GLLGPT 58

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26349115 460 IRAEVGDTIQVVFYNRASQPFSIQPHGVFYEKNSEGTVYND---------------------------------DP---- 502
Cdd:cd04226  59 LRAEVGDTLIVHFKNMADKPLSIHPQGIAYGKKSEGSLYSDntspveklddavqpgqeytyvwditeevgpteaDPpclt 138

                       170       180
                ....*....|....*....|....*..
gi 26349115 503 ---------TRDTNSGLVGPLLVCKAG 520
Cdd:cd04226 139 yiyyshvnmVRDFNSGLIGALLICKKG 165
CuRO_6_FVIII_like cd11018
The sixth cupredoxin domain of coagulation factor VIII and similar proteins; Factor VIII ...
 533-672 1.31e-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: 1.31e-23
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26349115 533 KEFFLLFTVFDENESWYNNANQAAGMLDSRLLSEDVEGFQDSNRMHAINGFLFSNLPRLDMCKGDTVAWHLLGLGTETDV 612
Cdd:cd11018   2 QEFALLFTIFDETKSWYFEENMRRNCRPPCHIQTQDPWFHINNKFHAINGYVADTLPGLVMAQHQRIRWHLLNMGSDEEI 81

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 26349115 613 HGVMFEGNTVQL---QGMRKGAVMLFPHTFVTAIMQPDNPGIFEIYCQAGSHREEGMQAIYNV 672
Cdd:cd11018  82 HSVHFHGLPFTVrakKEYRMGVYNLYPGVFGTVEMRPSTAGIWLVECTVGEHLLAGMSALFLV 144
CuRO_1_FVIII_like cd14452
The first cupredoxin domain of coagulation factor VIII and similar proteins; Factor VIII ...
 380-520 9.52e-22

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: 93.12  E-value: 9.52e-22
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26349115 380 RQYFIQAHEIQWDYgpigydgrTGKSLREPGSGPDKYfqksSSRIGGTYWKVRYEAFQDETFQerVHQEEETHLGILGPV 459
Cdd:cd14452   1 RRYYIAAVEIGWDY--------IHSDLGDPASEQRKK----PKDIPQKYIKAVFVEYLDATFT--VPKPRPAWMGLLGPT 66

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26349115 460 IRAEVGDTIQVVFYNRASQPFSIQPHGVFYEKNSEGTVYND--------------------------------------- 500
Cdd:cd14452  67 IVAEVGDTVVITFKNLASQPYSLHAVGVSYWKASEGAGYDDstsqhekeddavypggyhtyvwdispkdgptgsdpeclt 146

                       170       180
                ....*....|....*....|....*..
gi 26349115 501 -------DPTRDTNSGLVGPLLVCKAG 520
Cdd:cd14452 147 ysyssqvDPVKDVNSGLIGALLVCRMG 173
CuRO_2_FV_like cd14453
The second cupredoxin domain of coagulation factor V and similar proteins; Factor V is an ...
 532-672 1.17e-21

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: 91.07  E-value: 1.17e-21
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26349115 532 DKEFFLLFTVFDENESWYNnanqaagmldsrllsedvEGFQDSNRMHAINGFLFSNLPRLDMCKGDTVAWHLLGLGTETD 611
Cdd:cd14453   1 YKEYVLMFGVFDENKSWYK------------------QNASVDSVKYTINGYTNGTLPDVSICAYDHVSWHLLGMSSEPE 62

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 26349115 612 VHGVMFEGNTVQLQGMRKGAVMLFPHTFVTAIMQPDNPGIFEIYCQAGSHREEGMQAIYNV 672
Cdd:cd14453  63 LFSVHFNGQVLEQNGHKVSAVGLVSGSSTTASMTVVHTGRWLISSLIMKHLQAGMYGYLNI 123
CuRO_1_FVIII_like cd14452
The first cupredoxin domain of coagulation factor VIII and similar proteins; Factor VIII ...
 690-798 3.18e-21

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: 91.58  E-value: 3.18e-21
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26349115 690 RVYYIMAEEIEWDYcpdrswelewhnTSEKDSYGHVFLSNKDGLLGSKYKKAVFREYTDGTFRIPRPRSGpeeHLGILGP 769
Cdd:cd14452   1 RRYYIAAVEIGWDY------------IHSDLGDPASEQRKKPKDIPQKYIKAVFVEYLDATFTVPKPRPA---WMGLLGP 65

                        90       100
                ....*....|....*....|....*....
gi 26349115 770 LIRGEVGDILTVVFKNKASRPYSIHAHGV 798
Cdd:cd14452  66 TIVAEVGDTVVITFKNLASQPYSLHAVGV 94
CuRO_2_ceruloplasmin_like_2 cd11023
cupredoxin domain of ceruloplasmin homologs; Uncharacterized subfamily of ceruloplasmin ...
 572-672 3.50e-21

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: 89.59  E-value: 3.50e-21
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26349115 572 QDSNRMHAINGFLFSNLPRLDMCKGDTVAWHLLGLGTETDVHGVMFEGNTVQLQGMRKGAVM-LFPHTFVTAIMQPDNPG 650
Cdd:cd11023  17 EEAGLMHSINGYVFGNLPGVTIAKGKRVRWHLVAYGNEVDFHTPHWHGQTVEADKSRRTDVAeLMPASMRVADMTAADVG 96

                        90       100
                ....*....|....*....|..
gi 26349115 651 IFEIYCQAGSHREEGMQAIYNV 672
Cdd:cd11023  97 TWLLHCHVHDHYMAGMMTQFAV 118
CuRO_4_FV_like cd14454
The fourth cupredoxin domain of coagulation factor V and similar proteins; Factor V is an ...
 532-667 7.48e-20

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: 86.85  E-value: 7.48e-20
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26349115 532 DKEFFLLFTVFDENESWYNNANQAAGMLDSRLLSEDVEGFQDSNRMHAINGFLFSNLPRLDMCKGDTVAWHLLGLGTETD 611
Cdd:cd14454   1 DLEQHAVFAVFDENKSWYLEENINKYCSNPNNVKKDDPKFYKSNIMPTINGYAYESSAPLGFCHSEVVQWHISSVGTQDE 80

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*.
gi 26349115 612 VHGVMFEGNTVQLQGMRKGAVMLFPHTFVTAIMQPDNPGIFEIYCQAGSHREEGMQ 667
Cdd:cd14454  81 IITVHLSGHTFRYKGKHEDTLNLFPMSGESITVTMDNLGTWLLGSFGSSKKSKGLR 136
CuRO_1_FV_like cd04226
The first cupredoxin domain of coagulation factor VIII and similar proteins; Factor V is an ...
 690-798 1.23e-19

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: 86.84  E-value: 1.23e-19
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26349115 690 RVYYIMAEEIEWDYCPdrswelEWHNTSEKDSyghvflsnkdgllGSKYKKAVFREYTDGtFRIPRPRSgpeEHLGILGP 769
Cdd:cd04226   1 REYYIAAQNIDWDYTP------QSEELRLKRS-------------EQSFKKIVYREYEEG-FKKEKPAD---LSSGLLGP 57

                        90       100
                ....*....|....*....|....*....
gi 26349115 770 LIRGEVGDILTVVFKNKASRPYSIHAHGV 798
Cdd:cd04226  58 TLRAEVGDTLIVHFKNMADKPLSIHPQGI 86
CuRO_1_LCC_like cd04206
Cupredoxin domain 1 of laccase-like multicopper oxidases; including laccase, CueO, spore coat ...
 97-204 1.24e-16

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


Pssm-ID: 259869 [Multi-domain]  Cd Length: 120  Bit Score: 76.56  E-value: 1.24e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26349115  97 GFLGPLLQAEVGDVILIHLKN-FASRPYTIHPHGVFYEKDSEGslypDGSSGYLKadDSVPPGGSHVYNWsipeshaptE 175
Cdd:cd04206  27 QFPGPTIRVKEGDTVEVTVTNnLPNEPTSIHWHGLRQPGTNDG----DGVAGLTQ--CPIPPGESFTYRF---------T 91

                        90       100
                ....*....|....*....|....*....
gi 26349115 176 ADPACLTWIYHSHVDAprDIATGLIGPLI 204
Cdd:cd04206  92 VDDQAGTFWYHSHVGG--QRADGLYGPLI 118
CuRO_1_Diphenol_Ox cd13857
The first cupredoxin domain of fungal laccase, diphenol oxidase; Diphenol oxidase belongs to ...
 98-204 2.86e-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: 66.90  E-value: 2.86e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26349115  98 FLGPLLQAEVGDVILIHLKNFASRPYTIHPHGVFyekdSEGSLYPDGSSGYLKAddSVPPGGSHVYNWSIPESHAptead 177
Cdd:cd13857  28 FPGPLIEANQGDRIVVHVTNELDEPTSIHWHGLF----QNGTNWMDGTAGITQC--PIPPGGSFTYNFTVDGQYG----- 96

                        90       100
                ....*....|....*....|....*..
gi 26349115 178 paclTWIYHSHVDAprDIATGLIGPLI 204
Cdd:cd13857  97 ----TYWYHSHYST--QYADGLVGPLI 117
CuRO_1_2DMCO_NIR_like cd11024
The cupredoxin domain 1 of a two-domain laccase related to nitrite reductase; The two-domain ...
 100-204 3.43e-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: 61.13  E-value: 3.43e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26349115 100 GPLLQAEVGDVILIHLKNFASRPYTIHPHGVFYEKDsegslypDGSSGylkadDSVPPGGSHVYNWsipeshaptEADPA 179
Cdd:cd11024  32 GPTLRATEGDLVRIHFINTGDHPHTIHFHGIHDAAM-------DGTGL-----GPIMPGESFTYEF---------VAEPA 90

                        90       100
                ....*....|....*....|....*..
gi 26349115 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 1.09e-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: 1.09e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26349115 100 GPLLQAEVGDVILIHLKNFASRPYTIHPHGVFYEKDSEGSLYPdgssgylkaDDSVPPGGSHVYNWsipESHAPTEADPA 179
Cdd:cd14449  29 GPVIEVREGDTLKILFRNTLDVPASLHPHGVDYTTASDGTGMN---------ASIVAPGDTRIYTW---RTHGGYRRADG 96

                        90       100       110
                ....*....|....*....|....*....|....*
gi 26349115 180 CL------TWIYHSHV----DAPRDIATGLIGPLI 204
Cdd:cd14449  97 SWaegtagYWHYHDHVfgteHGTEGLSRGLYGALI 131
CuRO_1_CumA_like cd13861
The first cupredoxin domain of CumA like multicopper oxidase; This multicopper oxidase (MCO) ...
 93-204 2.00e-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: 58.79  E-value: 2.00e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26349115  93 PAWL---GFLGPLLQAEVGDVILIHLKNFASRPYTIHPHGVFYEKDSEGSlyPDGSSgylkadDSVPPGGSHVYNWSIPe 169
Cdd:cd13861  21 RTWGyngQVPGPELRVRQGDTLRVRLTNRLPEPTTIHWHGLRLPNAMDGV--PGLTQ------PPVPPGESFTYEFTPP- 91

                        90       100       110
                ....*....|....*....|....*....|....*
gi 26349115 170 shapteaDPAclTWIYHSHVDAPRDIATGLIGPLI 204
Cdd:cd13861  92 -------DAG--TYWYHPHVGSQEQLDRGLYGPLI 117
CuRO_D1_2dMcoN_like cd13859
The first cupredoxin domain of bacterial two domain multicopper oxidase McoN and similar ...
 100-204 3.69e-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: 3.69e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26349115 100 GPLLQAEVGDVILIHLKNFASRPYTIHPHGVFyekdSEGSLYPDGSSGYLKadDSVPPGGSHVYNWsipeshaptEADPA 179
Cdd:cd13859  31 GPLIHVKEGDDLVVHVTNNTTLPHTIHWHGVL----QMGSWKMDGVPGVTQ--PAIEPGESFTYKF---------KAERP 95

                        90       100
                ....*....|....*....|....*.
gi 26349115 180 CLTWiYHSHVDAPRDIAT-GLIGPLI 204
Cdd:cd13859  96 GTLW-YHCHVNVNEHVGMrGMWGPLI 120
SufI COG2132
Multicopper oxidase with three cupredoxin domains (includes cell division protein FtsP and ...
 98-204 5.48e-09

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


Pssm-ID: 441735 [Multi-domain]  Cd Length: 423  Bit Score: 59.18  E-value: 5.48e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26349115  98 FLGPLLQAEVGDVILIHLKNFASRPYTIHPHGVfyekdsegsLYPDGSSGYlkADDSVPPGGSHVYNWSIPeshapteaD 177
Cdd:COG2132  42 YPGPTIRVREGDRVRVRVTNRLPEPTTVHWHGL---------RVPNAMDGV--PGDPIAPGETFTYEFPVP--------Q 102

                        90       100
                ....*....|....*....|....*....
gi 26349115 178 PACLTWiYHSHVDA--PRDIATGLIGPLI 204
Cdd:COG2132 103 PAGTYW-YHPHTHGstAEQVYRGLAGALI 130
Cu-oxidase_3 pfam07732
Multicopper oxidase; This entry contains many divergent copper oxidase-like domains that are ...
 98-204 6.02e-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: 54.56  E-value: 6.02e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26349115    98 FLGPLLQAEVGDVILIHLKNFASRPYTIHPHGVFyekdSEGSLYPDGSSGYlkADDSVPPGGSHVYNWSIPeshapteaD 177
Cdd:pfam07732  24 FPGPTIRVREGDTVVVNVTNNLDEPTSIHWHGLQ----QRGTPWMDGVPGV--TQCPIPPGQSFTYRFQVK--------Q 89

                          90       100
                  ....*....|....*....|....*..
gi 26349115   178 PACLTWiYHSHVDAPRdiATGLIGPLI 204
Cdd:pfam07732  90 QAGTYW-YHSHTSGQQ--AAGLAGAII 113
CuRO_1_Fet3p cd13851
The first Cupredoxin domain of multicopper oxidase Fet3P; Fet3p catalyzes the ferroxidase ...
 101-204 2.28e-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: 53.04  E-value: 2.28e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26349115 101 PLLQAEVGDVILIHLKN-FASRPYTIHPHGVFYekdsEGSLYPDGSSGYLKADdsVPPGGSHVYNWSIPESHApteadpa 179
Cdd:cd13851  32 PPIEVNKGDTVVIHATNsLGDQPTSLHFHGLFQ----NGTNYMDGPVGVTQCP--IPPGQSFTYEFTVDTQVG------- 98

                        90       100
                ....*....|....*....|....*
gi 26349115 180 clTWIYHSHVDAprDIATGLIGPLI 204
Cdd:cd13851  99 --TYWYHSHDGG--QYPDGLRGPFI 119
CuRO_1_McoC_like cd13855
The first cupredoxin domain of a multicopper oxidase McoC and similar proteins; This family ...
 100-204 3.20e-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: 52.86  E-value: 3.20e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26349115 100 GPLLQAEVGDVILIHLKNFASRPYTIHPHGVFYEKDSEGSlypdgssgylkADDSVPPGGSHVYNWSIPESHAPTeadpa 179
Cdd:cd13855  32 GPLIEVFEGDTVEITFRNRLPEPTTVHWHGLPVPPDQDGN-----------PHDPVAPGNDRVYRFTLPQDSAGT----- 95

                        90       100
                ....*....|....*....|....*.
gi 26349115 180 clTWIY-HSHVDAPRDIATGLIGPLI 204
Cdd:cd13855  96 --YWYHpHPHGHTAEQVYRGLAGAFV 119
CuRO_1_2dMco_1 cd13860
The first cupredoxin domain of bacteria two domain multicopper oxidase; This subfamily ...
 100-204 2.68e-07

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


Pssm-ID: 259929 [Multi-domain]  Cd Length: 119  Bit Score: 49.89  E-value: 2.68e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26349115 100 GPLLQAEVGDVILIHLKNFASRPYTIHPHGVfyekdsegsLYP---DGSSGYlkADDSVPPGGSHVYNWSIPESHaptea 176
Cdd:cd13860  31 GPTIEVTEGDRVRILVTNELPEPTTVHWHGL---------PVPngmDGVPGI--TQPPIQPGETFTYEFTAKQAG----- 94

                        90       100
                ....*....|....*....|....*...
gi 26349115 177 dpaclTWIYHSHVDAPRDIATGLIGPLI 204
Cdd:cd13860  95 -----TYMYHSHVDEAKQEDMGLYGAFI 117
PLN02191 PLN02191
L-ascorbate oxidase
 98-231 8.00e-07

L-ascorbate oxidase


Pssm-ID: 177843 [Multi-domain]  Cd Length: 574  Bit Score: 52.71  E-value: 8.00e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26349115   98 FLGPLLQAEVGDVILIHLKN-FASRPYTIHPHGVfyekDSEGSLYPDGSSGYLKAddSVPPGGSHVYNWSIPESHaptea 176
Cdd:PLN02191  51 FPGPTIDAVAGDTIVVHLTNkLTTEGLVIHWHGI----RQKGSPWADGAAGVTQC--AINPGETFTYKFTVEKPG----- 119

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 26349115  177 dpaclTWIYHSHVDAPRdiATGLIGPLITCKrgtldGNSPPQRKDVDHNFFLLFS 231
Cdd:PLN02191 120 -----THFYHGHYGMQR--SAGLYGSLIVDV-----AKGPKERLRYDGEFNLLLS 162
Cu-oxidase pfam00394
Multicopper oxidase; Many of the proteins in this family contain multiple similar copies of ...
 230-367 1.66e-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: 48.47  E-value: 1.66e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26349115   230 FSVIDENLSWHlDDNIATYCSDPASVDKEDGAF---QDSnrmHAINGFVFGNLPELSMCAQKHVAWHLFgMGNEIDVHTA 306
Cdd:pfam00394   1 EDYVITLSDWY-HKDAKDLEKELLASGKAPTDFppvPDA---VLINGKDGASLATLTVTPGKTYRLRII-NVALDDSLNF 75

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 26349115   307 FFHGQMLSI---RGHHT-----DVANIFPATF----VTAemvPQKSGTWLISCEVN-SHLRSGMQAFYKVDSCS 367
Cdd:pfam00394  76 SIEGHKMTVvevDGVYVnpftvDSLDIFPGQRysvlVTA---NQDPGNYWIVASPNiPAFDNGTAAAILRYSGA 146
CuRO_1_LCC_like cd04206
Cupredoxin domain 1 of laccase-like multicopper oxidases; including laccase, CueO, spore coat ...
 454-496 4.61e-06

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: 46.51  E-value: 4.61e-06
                        10        20        30        40
                ....*....|....*....|....*....|....*....|....
gi 26349115 454 GILGPVIRAEVGDTIQVVFYNR-ASQPFSIQPHGVFYEKNSEGT 496
Cdd:cd04206  27 QFPGPTIRVKEGDTVEVTVTNNlPNEPTSIHWHGLRQPGTNDGD 70
CuRO_1_Abr2_like cd13850
The first cupredoxin domain of a group of fungal Laccases similar to Abr2 from Aspergillus ...
 83-203 4.63e-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: 46.52  E-value: 4.63e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26349115  83 DGTYTEeiaKPAWLG---FLGPLLQAEVGDVILIHLKNFASRPYTIHPHGVFyekdSEGSLYPDGSSGYLKAddSVPPGG 159
Cdd:cd13850  11 DGDGGE---REVILIngqFPGPPIILDEGDEVEILVTNNLPVNTTIHFHGIL----QRGTPWSDGVPGVTQW--PIQPGG 81

                        90       100       110       120
                ....*....|....*....|....*....|....*....|....
gi 26349115 160 SHVYNWsipeshapTEADPACLTWiYHSHVDAprDIATGLIGPL 203
Cdd:cd13850  82 SFTYRW--------KAEDQYGLYW-YHSHYRG--YYMDGLYGPI 114
ascorbase TIGR03388
L-ascorbate oxidase, plant type; Members of this protein family are the copper-containing ...
 98-228 6.42e-06

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


Pssm-ID: 274555 [Multi-domain]  Cd Length: 541  Bit Score: 49.75  E-value: 6.42e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26349115    98 FLGPLLQAEVGDVILIHLKN-FASRPYTIHPHGVfyekDSEGSLYPDGSSGYLKAddSVPPGGSHVYNWSIPESHaptea 176
Cdd:TIGR03388  29 FPGPTIRAQAGDTIVVELTNkLHTEGVVIHWHGI----RQIGTPWADGTAGVTQC--AINPGETFIYNFVVDRPG----- 97

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|..
gi 26349115   177 dpaclTWIYHSHVDAPRdiATGLIGPLITCKRgtlDGNSPPQRKDVDHNFFL 228
Cdd:TIGR03388  98 -----TYFYHGHYGMQR--SAGLYGSLIVDVP---DGEKEPFHYDGEFNLLL 139
CuRO_1_2DMCO_NIR_like_2 cd14449
The cupredoxin domain 1 of a two-domain laccase related to nitrite reductase; The two-domain ...
 457-499 1.80e-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: 45.34  E-value: 1.80e-05
                        10        20        30        40
                ....*....|....*....|....*....|....*....|...
gi 26349115 457 GPVIRAEVGDTIQVVFYNRASQPFSIQPHGVFYEKNSEGTVYN 499
Cdd:cd14449  29 GPVIEVREGDTLKILFRNTLDVPASLHPHGVDYTTASDGTGMN 71
CuRO_1_2DMCO_NIR_like cd11024
The cupredoxin domain 1 of a two-domain laccase related to nitrite reductase; The two-domain ...
 768-813 3.48e-05

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


Pssm-ID: 259910 [Multi-domain]  Cd Length: 119  Bit Score: 43.80  E-value: 3.48e-05
                        10        20        30        40
                ....*....|....*....|....*....|....*....|....*...
gi 26349115 768 GPLIRGEVGDILTVVFKNKASRPYSIHAHGV--LESNTGGPQAAEPGE 813
Cdd:cd11024  32 GPTLRATEGDLVRIHFINTGDHPHTIHFHGIhdAAMDGTGLGPIMPGE 79
CuRO_1_CumA_like cd13861
The first cupredoxin domain of CumA like multicopper oxidase; This multicopper oxidase (MCO) ...
 454-487 4.17e-05

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


Pssm-ID: 259930 [Multi-domain]  Cd Length: 119  Bit Score: 43.76  E-value: 4.17e-05
                        10        20        30
                ....*....|....*....|....*....|....
gi 26349115 454 GILGPVIRAEVGDTIQVVFYNRASQPFSIQPHGV 487
Cdd:cd13861  28 QVPGPELRVRQGDTLRVRLTNRLPEPTTIHWHGL 61
CuRO_1_Tv-LCC_like cd13856
The first cupredoxin domain of fungal laccases similar to Tv-LCC from Trametes versicolor; ...
 98-204 4.53e-05

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


Pssm-ID: 259925 [Multi-domain]  Cd Length: 125  Bit Score: 43.87  E-value: 4.53e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26349115  98 FLGPLLQAEVGDVILIHLKNFAS-----RPYTIHPHGVFYEKDSegslYPDGSSGYLKAddSVPPGGSHVYNWSIPEsha 172
Cdd:cd13856  28 FPGPLITANKGDTFRITVVNQLTdptmrRSTSIHWHGIFQHGTN----YADGPAFVTQC--PIAPNHSFTYDFTAGD--- 98

                        90       100       110
                ....*....|....*....|....*....|..
gi 26349115 173 ptEADpaclTWIYHSHVDAprDIATGLIGPLI 204
Cdd:cd13856  99 --QAG----TFWYHSHLST--QYCDGLRGPLV 122
CuRO_1_MaLCC_like cd13854
The first cupredoxin domain of the fungal laccases similar to Ma-LCC from Melanocarpus ...
 100-204 5.01e-05

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


Pssm-ID: 259923 [Multi-domain]  Cd Length: 122  Bit Score: 43.39  E-value: 5.01e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26349115 100 GPLLQAEVGDVILIHLKNfaSRPY---TIHPHGVfyekDSEGSLYPDGSSGYLKAddSVPPGGSHVYNWsipeshaptEA 176
Cdd:cd13854  33 GPLIEANWGDTIEVTVIN--KLQDngtSIHWHGI----RQLNTNWQDGVPGVTEC--PIAPGDTRTYRF---------RA 95

                        90       100
                ....*....|....*....|....*...
gi 26349115 177 DPACLTWiYHSHVDAprDIATGLIGPLI 204
Cdd:cd13854  96 TQYGTSW-YHSHYSA--QYGDGVVGPIV 120
CuRO_1_MCO_like_1 cd13862
The first cupredoxin domain of uncharacterized multicopper oxidase; Multicopper Oxidases (MCOs) ...
 100-204 6.33e-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: 43.28  E-value: 6.33e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26349115 100 GPLLQAEVGDVILIHLKNFASRPYTIHPHGVFYEKDSEGSLyPDGSSgylkaddSVPPGGSHVYNWSipeshapteADPA 179
Cdd:cd13862  31 GPLLRMRQGVSVTVDVFNDTDIPEYVHWHGLPLPADVDGAM-EEGTP-------SVPPHGHRRYRMT---------PRPA 93

                        90       100
                ....*....|....*....|....*....
gi 26349115 180 CLTWiYHSHVDAPRDIA----TGLIGPLI 204
Cdd:cd13862  94 GFRW-YHTHVMTMDDLTrgqySGLFGFVY 121
CuRO_1_2DMCO_NIR_like cd11024
The cupredoxin domain 1 of a two-domain laccase related to nitrite reductase; The two-domain ...
 457-492 9.61e-05

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


Pssm-ID: 259910 [Multi-domain]  Cd Length: 119  Bit Score: 42.64  E-value: 9.61e-05
                        10        20        30
                ....*....|....*....|....*....|....*.
gi 26349115 457 GPVIRAEVGDTIQVVFYNRASQPFSIQPHGVFYEKN 492
Cdd:cd11024  32 GPTLRATEGDLVRIHFINTGDHPHTIHFHGIHDAAM 67
CuRO_D1_2dMcoN_like cd13859
The first cupredoxin domain of bacterial two domain multicopper oxidase McoN and similar ...
 768-813 1.18e-04

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


Pssm-ID: 259928 [Multi-domain]  Cd Length: 122  Bit Score: 42.47  E-value: 1.18e-04
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|....
gi 26349115 768 GPLIRGEVGDILTVVFKNKASRPYSIHAHGVLESNT----GGP----QAAEPGE 813
Cdd:cd13859  31 GPLIHVKEGDDLVVHVTNNTTLPHTIHWHGVLQMGSwkmdGVPgvtqPAIEPGE 84
CuRO_1_AAO cd13845
The first cupredoxin domain of plant Ascorbate oxidase; Ascorbate oxidase catalyzes the ...
 97-204 1.57e-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: 42.05  E-value: 1.57e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26349115  97 GFLGPLLQAEVGDVILIHLKN-FASRPYTIHPHGVfyekDSEGSLYPDGSSGYLKAddSVPPGGSHVYNWSIPESHapte 175
Cdd:cd13845  27 QFPGPTIRATAGDTIVVELENkLPTEGVAIHWHGI----RQRGTPWADGTASVSQC--PINPGETFTYQFVVDRPG---- 96

                        90       100
                ....*....|....*....|....*....
gi 26349115 176 adpaclTWIYHSHVDAPRdiATGLIGPLI 204
Cdd:cd13845  97 ------TYFYHGHYGMQR--SAGLYGSLI 117
CuRO_1_CumA_like cd13861
The first cupredoxin domain of CumA like multicopper oxidase; This multicopper oxidase (MCO) ...
 765-798 4.63e-04

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


Pssm-ID: 259930 [Multi-domain]  Cd Length: 119  Bit Score: 40.68  E-value: 4.63e-04
                        10        20        30
                ....*....|....*....|....*....|....
gi 26349115 765 GILGPLIRGEVGDILTVVFKNKASRPYSIHAHGV 798
Cdd:cd13861  28 QVPGPELRVRQGDTLRVRLTNRLPEPTTIHWHGL 61
CuRO_1_LCC_like cd04206
Cupredoxin domain 1 of laccase-like multicopper oxidases; including laccase, CueO, spore coat ...
 765-803 5.91e-04

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


Pssm-ID: 259869 [Multi-domain]  Cd Length: 120  Bit Score: 40.35  E-value: 5.91e-04
                        10        20        30        40
                ....*....|....*....|....*....|....*....|
gi 26349115 765 GILGPLIRGEVGDILTVVFKNK-ASRPYSIHAHGVLESNT 803
Cdd:cd04206  27 QFPGPTIRVKEGDTVEVTVTNNlPNEPTSIHWHGLRQPGT 66
SufI COG2132
Multicopper oxidase with three cupredoxin domains (includes cell division protein FtsP and ...
 766-813 1.32e-03

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


Pssm-ID: 441735 [Multi-domain]  Cd Length: 423  Bit Score: 42.23  E-value: 1.32e-03
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|.
gi 26349115 766 ILGPLIRGEVGDILTVVFKNKASRPYSIHAHGVLESNT--GGPQAA-EPGE 813
Cdd:COG2132  42 YPGPTIRVREGDRVRVRVTNRLPEPTTVHWHGLRVPNAmdGVPGDPiAPGE 92
CuRO_1_Diphenol_Ox cd13857
The first cupredoxin domain of fungal laccase, diphenol oxidase; Diphenol oxidase belongs to ...
 457-503 1.44e-03

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


Pssm-ID: 259926 [Multi-domain]  Cd Length: 119  Bit Score: 39.16  E-value: 1.44e-03
                        10        20        30        40
                ....*....|....*....|....*....|....*....|....*..
gi 26349115 457 GPVIRAEVGDTIQVVFYNRASQPFSIQPHGVFyeknSEGTVYNDDPT 503
Cdd:cd13857  30 GPLIEANQGDRIVVHVTNELDEPTSIHWHGLF----QNGTNWMDGTA 72
CuRO_1_tcLCC2_insect_like cd13858
The first cupredoxin domain of insect laccases similar to laccase 2 in Tribolium castaneum; ...
 100-204 2.24e-03

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


Pssm-ID: 259927 [Multi-domain]  Cd Length: 105  Bit Score: 38.29  E-value: 2.24e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26349115 100 GPLLQAEVGDVILIHLKN-FASRPYTIHPHGVFyekdSEGSLYPDGssgylkaddsVP--------PGGSHVYNWSipes 170
Cdd:cd13858  16 GPSIEVCEGDTVVVDVKNrLPGESTTIHWHGIH----QRGTPYMDG----------VPmvtqcpilPGQTFRYKFK---- 77

                        90       100       110
                ....*....|....*....|....*....|....
gi 26349115 171 hapteADPAClTWIYHSHVDAPRdiATGLIGPLI 204
Cdd:cd13858  78 -----ADPAG-THWYHSHSGTQR--ADGLFGALI 103
Cu-oxidase_3 pfam07732
Multicopper oxidase; This entry contains many divergent copper oxidase-like domains that are ...
 766-845 3.84e-03

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


Pssm-ID: 462247 [Multi-domain]  Cd Length: 119  Bit Score: 38.00  E-value: 3.84e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26349115   766 ILGPLIRGEVGDILTVVFKNKASRPYSIHAHGVLESNT-------GGPQAA-EPGElehlmkrQRLYNpFTLV-----FW 832
Cdd:pfam07732  24 FPGPTIRVREGDTVVVNVTNNLDEPTSIHWHGLQQRGTpwmdgvpGVTQCPiPPGQ-------SFTYR-FQVKqqagtYW 95

                          90
                  ....*....|...
gi 26349115   833 FIPFNILHSWAGQ 845
Cdd:pfam07732  96 YHSHTSGQQAAGL 108
Cu-oxidase_3 pfam07732
Multicopper oxidase; This entry contains many divergent copper oxidase-like domains that are ...
 455-494 3.99e-03

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


Pssm-ID: 462247 [Multi-domain]  Cd Length: 119  Bit Score: 38.00  E-value: 3.99e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|
gi 26349115   455 ILGPVIRAEVGDTIQVVFYNRASQPFSIQPHGVFYEKNSE 494
Cdd:pfam07732  24 FPGPTIRVREGDTVVVNVTNNLDEPTSIHWHGLQQRGTPW 63
CuRO_1_CueO_FtsP cd04232
The first Cupredoxin domain of the multicopper oxidase CueO, the cell division protein FtsP, ...
 98-204 4.48e-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: 37.94  E-value: 4.48e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26349115  98 FLGPLLQAEVGDVILIHLKNFASRPYTIHPHGVFYEKDSEGSLYpdgssgylkadDSVPPGGSHVYNWSIpeshapteAD 177
Cdd:cd04232  29 YLGPTIRVKKGDTVRINVTNNLDEETTVHWHGLHVPGEMDGGPH-----------QPIAPGQTWSPTFTI--------DQ 89

                        90       100
                ....*....|....*....|....*....
gi 26349115 178 PACLTWiYHSHVDA--PRDIATGLIGPLI 204
Cdd:cd04232  90 PAATLW-YHPHTHGktAEQVYRGLAGLFI 117
CuRO_1_CuNIR_like cd04201
Cupredoxin domain 1 of Copper-containing nitrite reductase and two-domain laccase; ...
 100-204 5.83e-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: 37.47  E-value: 5.83e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26349115 100 GPLLQAEVGDVILIHLKNfasRPYTIHPHGVfyekDSEGSLYPDGSSGYlkadDSVPPGGSHVYNWsipeshaptEADPA 179
Cdd:cd04201  32 GPMLRVREGDTVELHFSN---NPSSTMPHNI----DFHAATGAGGGAGA----TFIAPGETSTFSF---------KATQP 91

                        90       100
                ....*....|....*....|....*.
gi 26349115 180 ClTWIYHSHVDA-PRDIATGLIGPLI 204
Cdd:cd04201  92 G-LYVYHCAVAPvPMHIANGMYGLIL 116
 
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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