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Conserved domains on  [gi|6679731|ref|NP_032002|]
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coagulation factor V preproprotein [Mus musculus]

Protein Classification

multicopper oxidase( domain architecture ID 10363155)

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

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
Cupredoxin super family cl19115
Cupredoxin superfamily; Cupredoxins contain type I copper centers and are involved in ...
 1539-1714 2.39e-109

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 cd14451:

Pssm-ID: 473140 [Multi-domain]  Cd Length: 173  Bit Score: 345.29  E-value: 2.39e-109
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6679731  1539 KKFYYIAAEEITWNYAEFAQSEMDHEdtgHTPKDTTYKKVVFRKYLDSTFTSRDPRAEYEEHLGILGPVIRAEVDDVIQV 1618
Cdd:cd14451    1 KRRYYIAAEEEEWDYAGYGKSRLDKT---QNERDTVFKKVVFRRYLDSTFSTPDIQGEYEEHLGILGPVIRAEVDDVIQV 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6679731  1619 RFKNLASRPYSLHAHGLSYEKSSEGKTYEDESPEWFQEDDAVQPNSSYTYVWHATKRSGPENPGSACRAWAYYSAVNVER 1698
Cdd:cd14451   78 FFKNLASRPYSLHAHGLSYEKSSEGLSYDDESPDWFKKDDAVQPNGTYTYVWYANPRSGPENNGSDCRTWAYYSAVNPEK 157

                        170
                 ....*....|....*.
gi 6679731  1699 DIHSGLIGPLLICRKG 1714
Cdd:cd14451  158 DIHSGLIGPLLICRKG 173
CuRO_3_FV_like cd14450
The third cupredoxin domain of coagulation factor V and similar proteins; Factor V is an ...
 347-526 1.74e-104

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: 331.84  E-value: 1.74e-104
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6679731   347 KRWEYFIAAEEVIWNYAPVIPANMDKIYRSQHLDNFSNQIGKHYKKVIYRQYEEETFTKRTDNPSIKQSGILGPVIRAQV 426
Cdd:cd14450    1 KNWEYFIAAEEVIWDYAPSIPENMDKRYRSQYLDNFSNNIGKKYKKAVFTQYEDGSFTKRLENPRPKEEGILGPVIRAQV 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6679731   427 RDTLKIVFKNMASRPYSIYPHGVTFSPYEDGINSSSTSGS-HTTIRPVQPGETFTYKWNILEFDEPTENDAQCLTRPYYS 505
Cdd:cd14450   81 RDTIKIVFKNKASRPYSIYPHGVTVSKAAEGASYPPDPRGnETQNKAVQPGETYTYKWNILETDEPTARDPRCLTRMYHS 160

                        170       180
                 ....*....|....*....|.
gi 6679731   506 DVDVTRDIASGLIGLLLICKS 526
Cdd:cd14450  161 AVDITRDIASGLIGPLLICKS 181
Cupredoxin super family cl19115
Cupredoxin superfamily; Cupredoxins contain type I copper centers and are involved in ...
 32-195 5.98e-94

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 cd04226:

Pssm-ID: 473140 [Multi-domain]  Cd Length: 165  Bit Score: 301.01  E-value: 5.98e-94
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6679731    32 RQFYVAAQGILWNYHPEPTDPSLNSI-PSFKKIVYREYEQYFKKEKPRSSNSGLLGPTLYAEVGDVIKVHFRNKADKPLS 110
Cdd:cd04226    1 REYYIAAQNIDWDYTPQSEELRLKRSeQSFKKIVYREYEEGFKKEKPADLSSGLLGPTLRAEVGDTLIVHFKNMADKPLS 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6679731   111 IHPQGIKYSKFSEGASYADHTFPAERKDDAVAPGEEYTYEWIVSEDSGPTPDDPPCLTHIYYSYENLTQDFNSGLIGPLL 190
Cdd:cd04226   81 IHPQGIAYGKKSEGSLYSDNTSPVEKLDDAVQPGQEYTYVWDITEEVGPTEADPPCLTYIYYSHVNMVRDFNSGLIGALL 160


                 ....*
gi 6679731   191 ICKKG 195
Cdd:cd04226  161 ICKKG 165
CuRO_4_FV_like cd14454
The fourth cupredoxin domain of coagulation factor V and similar proteins; Factor V is an ...
 539-682 1.14e-85

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: 276.37  E-value: 1.14e-85
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6679731   539 DIEQQAVFAVFDENKSWYIEDNINKFCENPDEVKRDDPKFYESNIMSTINGYVPESISTLGFCFDDTVQWHFCSVGTHDD 618
Cdd:cd14454    1 DLEQHAVFAVFDENKSWYLEENINKYCSNPNNVKKDDPKFYKSNIMPTINGYAYESSAPLGFCHSEVVQWHISSVGTQDE 80

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 6679731   619 ILTIHFTGHSFIYGRRHEDTLTLFPMRGESVTVTMDNVGTWMLTTMNSNPKRRNLRLRFRDVKC 682
Cdd:cd14454   81 IITVHLSGHTFRYKGKHEDTLNLFPMSGESITVTMDNLGTWLLGSFGSSKKSKGLRVRFTDVIC 144
Cupredoxin super family cl19115
Cupredoxin superfamily; Cupredoxins contain type I copper centers and are involved in ...
 1726-1861 1.05e-78

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 cd14455:

Pssm-ID: 473140 [Multi-domain]  Cd Length: 140  Bit Score: 256.33  E-value: 1.05e-78
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6679731  1726 MREFVLLFMVFDEKKSWYYEKSKGS----RRIESPEEKNAHKFYAINGMIYNLPGLRMYEQEWVRLHLLNMGGSRDIHVV 1801
Cdd:cd14455    1 RREFVLLFMTFDEEKSWYYEKNRKRtcreNRVKDPNVQDNHTFHAINGIIYNLKGLRMYTNELVRWHLINMGGPKDLHVV 80

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 6679731  1802 HFHGQTLLDNRTKQHQLGVWPLLPGSFKTLEMKASKPGWWLLDTEVGENQVAGMQTPFLI 1861
Cdd:cd14455   81 HFHGQTFTEKGLKDHQLGVYPLLPGSFATLEMKPSKPGLWLLETEVGESQQRGMQTLFLV 140
Cupredoxin super family cl19115
Cupredoxin superfamily; Cupredoxins contain type I copper centers and are involved in ...
 207-325 1.38e-70

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 cd14453:

Pssm-ID: 473140 [Multi-domain]  Cd Length: 123  Bit Score: 232.44  E-value: 1.38e-70
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6679731   207 DKQHVLLFAVFDESKS----RSQSPSLMYTINGFVNKTMPDITVCAHDHVSWHLIGMSSGPELFSIHFNGQVLEQNQHKV 282
Cdd:cd14453    1 YKEYVLMFGVFDENKSwykqNASVDSVKYTINGYTNGTLPDVSICAYDHVSWHLLGMSSEPELFSVHFNGQVLEQNGHKV 80

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|...
gi 6679731   283 STVTLVSATSTTANMTMSPEGRWIVSSLIPKHYQAGMQAYIDI 325
Cdd:cd14453   81 SAVGLVSGSSTTASMTVVHTGRWLISSLIMKHLQAGMYGYLNI 123
FA58C cd00057
Coagulation factor 5/8 C-terminal domain, discoidin domain; Cell surface-attached ...
 2027-2179 6.00e-56

Coagulation factor 5/8 C-terminal domain, discoidin domain; Cell surface-attached carbohydrate-binding domain, present in eukaryotes and assumed to have horizontally transferred to eubacterial genomes.


:

Pssm-ID: 238014 [Multi-domain]  Cd Length: 143  Bit Score: 191.03  E-value: 6.00e-56
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6679731  2027 TPLGLEDGRiQDKQITASSfkksWWGDYWEPSLARLNaqgRVNAWQAKANNNKQWLQVDLLKIKKVTAIVTQGCKSLSSE 2106
Cdd:cd00057    1 EPLGMESGL-ADDQITASS----SYSSGWEASRARLN---SDNAWTPAVNDPPQWLQVDLGKTRRVTGIQTQGRKGGGSS 72

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 6679731  2107 MYVKSYSIQYSDQGVAWKPYRQKssMVDKIFEGNSNTKGHMKNFFNPPIISRFIRIIPKTWNQSIALRLELFG 2179
Cdd:cd00057   73 EWVTSYKVQYSLDGETWTTYKDK--GEEKVFTGNSDGSTPVTNDFPPPIVARYIRILPTTWNGNISLRLELYG 143
FA58C cd00057
Coagulation factor 5/8 C-terminal domain, discoidin domain; Cell surface-attached ...
 1868-2019 2.25e-47

Coagulation factor 5/8 C-terminal domain, discoidin domain; Cell surface-attached carbohydrate-binding domain, present in eukaryotes and assumed to have horizontally transferred to eubacterial genomes.


:

Pssm-ID: 238014 [Multi-domain]  Cd Length: 143  Bit Score: 166.76  E-value: 2.25e-47
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6679731  1868 MPMGLSTGvISDSQIKA-SEYLTYWEPRLARLNnagSYNAWSIEKTALdfpiKPWIQVDMQKEVVVTGIQTQGAKHYLKS 1946
Cdd:cd00057    1 EPLGMESG-LADDQITAsSSYSSGWEASRARLN---SDNAWTPAVNDP----PQWLQVDLGKTRRVTGIQTQGRKGGGSS 72

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 6679731  1947 CFTTEFQVAYSSDQTNWQIFRGKSGksVMYFTGNSDGSTIKENRLDPPIVARYIRIHPTKSYNRPTLRLELQG 2019
Cdd:cd00057   73 EWVTSYKVQYSLDGETWTTYKDKGE--EKVFTGNSDGSTPVTNDFPPPIVARYIRILPTTWNGNISLRLELYG 143
 
Name Accession Description Interval E-value
CuRO_5_FV_like cd14451
The fifth cupredoxin domain of coagulation factor V and similar proteins; Factor V is an ...
 1539-1714 2.39e-109

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: 345.29  E-value: 2.39e-109
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6679731  1539 KKFYYIAAEEITWNYAEFAQSEMDHEdtgHTPKDTTYKKVVFRKYLDSTFTSRDPRAEYEEHLGILGPVIRAEVDDVIQV 1618
Cdd:cd14451    1 KRRYYIAAEEEEWDYAGYGKSRLDKT---QNERDTVFKKVVFRRYLDSTFSTPDIQGEYEEHLGILGPVIRAEVDDVIQV 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6679731  1619 RFKNLASRPYSLHAHGLSYEKSSEGKTYEDESPEWFQEDDAVQPNSSYTYVWHATKRSGPENPGSACRAWAYYSAVNVER 1698
Cdd:cd14451   78 FFKNLASRPYSLHAHGLSYEKSSEGLSYDDESPDWFKKDDAVQPNGTYTYVWYANPRSGPENNGSDCRTWAYYSAVNPEK 157

                        170
                 ....*....|....*.
gi 6679731  1699 DIHSGLIGPLLICRKG 1714
Cdd:cd14451  158 DIHSGLIGPLLICRKG 173
CuRO_3_FV_like cd14450
The third cupredoxin domain of coagulation factor V and similar proteins; Factor V is an ...
 347-526 1.74e-104

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: 331.84  E-value: 1.74e-104
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6679731   347 KRWEYFIAAEEVIWNYAPVIPANMDKIYRSQHLDNFSNQIGKHYKKVIYRQYEEETFTKRTDNPSIKQSGILGPVIRAQV 426
Cdd:cd14450    1 KNWEYFIAAEEVIWDYAPSIPENMDKRYRSQYLDNFSNNIGKKYKKAVFTQYEDGSFTKRLENPRPKEEGILGPVIRAQV 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6679731   427 RDTLKIVFKNMASRPYSIYPHGVTFSPYEDGINSSSTSGS-HTTIRPVQPGETFTYKWNILEFDEPTENDAQCLTRPYYS 505
Cdd:cd14450   81 RDTIKIVFKNKASRPYSIYPHGVTVSKAAEGASYPPDPRGnETQNKAVQPGETYTYKWNILETDEPTARDPRCLTRMYHS 160

                        170       180
                 ....*....|....*....|.
gi 6679731   506 DVDVTRDIASGLIGLLLICKS 526
Cdd:cd14450  161 AVDITRDIASGLIGPLLICKS 181
CuRO_1_FV_like cd04226
The first cupredoxin domain of coagulation factor VIII and similar proteins; Factor V is an ...
 32-195 5.98e-94

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: 301.01  E-value: 5.98e-94
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6679731    32 RQFYVAAQGILWNYHPEPTDPSLNSI-PSFKKIVYREYEQYFKKEKPRSSNSGLLGPTLYAEVGDVIKVHFRNKADKPLS 110
Cdd:cd04226    1 REYYIAAQNIDWDYTPQSEELRLKRSeQSFKKIVYREYEEGFKKEKPADLSSGLLGPTLRAEVGDTLIVHFKNMADKPLS 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6679731   111 IHPQGIKYSKFSEGASYADHTFPAERKDDAVAPGEEYTYEWIVSEDSGPTPDDPPCLTHIYYSYENLTQDFNSGLIGPLL 190
Cdd:cd04226   81 IHPQGIAYGKKSEGSLYSDNTSPVEKLDDAVQPGQEYTYVWDITEEVGPTEADPPCLTYIYYSHVNMVRDFNSGLIGALL 160


                 ....*
gi 6679731   191 ICKKG 195
Cdd:cd04226  161 ICKKG 165
CuRO_4_FV_like cd14454
The fourth cupredoxin domain of coagulation factor V and similar proteins; Factor V is an ...
 539-682 1.14e-85

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: 276.37  E-value: 1.14e-85
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6679731   539 DIEQQAVFAVFDENKSWYIEDNINKFCENPDEVKRDDPKFYESNIMSTINGYVPESISTLGFCFDDTVQWHFCSVGTHDD 618
Cdd:cd14454    1 DLEQHAVFAVFDENKSWYLEENINKYCSNPNNVKKDDPKFYKSNIMPTINGYAYESSAPLGFCHSEVVQWHISSVGTQDE 80

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 6679731   619 ILTIHFTGHSFIYGRRHEDTLTLFPMRGESVTVTMDNVGTWMLTTMNSNPKRRNLRLRFRDVKC 682
Cdd:cd14454   81 IITVHLSGHTFRYKGKHEDTLNLFPMSGESITVTMDNLGTWLLGSFGSSKKSKGLRVRFTDVIC 144
CuRO_6_FV_like cd14455
The sixth cupredoxin domain of coagulation factor V and similar proteins; Factor V is an ...
 1726-1861 1.05e-78

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: 256.33  E-value: 1.05e-78
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6679731  1726 MREFVLLFMVFDEKKSWYYEKSKGS----RRIESPEEKNAHKFYAINGMIYNLPGLRMYEQEWVRLHLLNMGGSRDIHVV 1801
Cdd:cd14455    1 RREFVLLFMTFDEEKSWYYEKNRKRtcreNRVKDPNVQDNHTFHAINGIIYNLKGLRMYTNELVRWHLINMGGPKDLHVV 80

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 6679731  1802 HFHGQTLLDNRTKQHQLGVWPLLPGSFKTLEMKASKPGWWLLDTEVGENQVAGMQTPFLI 1861
Cdd:cd14455   81 HFHGQTFTEKGLKDHQLGVYPLLPGSFATLEMKPSKPGLWLLETEVGESQQRGMQTLFLV 140
CuRO_2_FV_like cd14453
The second cupredoxin domain of coagulation factor V and similar proteins; Factor V is an ...
 207-325 1.38e-70

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: 232.44  E-value: 1.38e-70
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6679731   207 DKQHVLLFAVFDESKS----RSQSPSLMYTINGFVNKTMPDITVCAHDHVSWHLIGMSSGPELFSIHFNGQVLEQNQHKV 282
Cdd:cd14453    1 YKEYVLMFGVFDENKSwykqNASVDSVKYTINGYTNGTLPDVSICAYDHVSWHLLGMSSEPELFSVHFNGQVLEQNGHKV 80

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|...
gi 6679731   283 STVTLVSATSTTANMTMSPEGRWIVSSLIPKHYQAGMQAYIDI 325
Cdd:cd14453   81 SAVGLVSGSSTTASMTVVHTGRWLISSLIMKHLQAGMYGYLNI 123
FA58C cd00057
Coagulation factor 5/8 C-terminal domain, discoidin domain; Cell surface-attached ...
 2027-2179 6.00e-56

Coagulation factor 5/8 C-terminal domain, discoidin domain; Cell surface-attached carbohydrate-binding domain, present in eukaryotes and assumed to have horizontally transferred to eubacterial genomes.


Pssm-ID: 238014 [Multi-domain]  Cd Length: 143  Bit Score: 191.03  E-value: 6.00e-56
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6679731  2027 TPLGLEDGRiQDKQITASSfkksWWGDYWEPSLARLNaqgRVNAWQAKANNNKQWLQVDLLKIKKVTAIVTQGCKSLSSE 2106
Cdd:cd00057    1 EPLGMESGL-ADDQITASS----SYSSGWEASRARLN---SDNAWTPAVNDPPQWLQVDLGKTRRVTGIQTQGRKGGGSS 72

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 6679731  2107 MYVKSYSIQYSDQGVAWKPYRQKssMVDKIFEGNSNTKGHMKNFFNPPIISRFIRIIPKTWNQSIALRLELFG 2179
Cdd:cd00057   73 EWVTSYKVQYSLDGETWTTYKDK--GEEKVFTGNSDGSTPVTNDFPPPIVARYIRILPTTWNGNISLRLELYG 143
FA58C cd00057
Coagulation factor 5/8 C-terminal domain, discoidin domain; Cell surface-attached ...
 1868-2019 2.25e-47

Coagulation factor 5/8 C-terminal domain, discoidin domain; Cell surface-attached carbohydrate-binding domain, present in eukaryotes and assumed to have horizontally transferred to eubacterial genomes.


Pssm-ID: 238014 [Multi-domain]  Cd Length: 143  Bit Score: 166.76  E-value: 2.25e-47
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6679731  1868 MPMGLSTGvISDSQIKA-SEYLTYWEPRLARLNnagSYNAWSIEKTALdfpiKPWIQVDMQKEVVVTGIQTQGAKHYLKS 1946
Cdd:cd00057    1 EPLGMESG-LADDQITAsSSYSSGWEASRARLN---SDNAWTPAVNDP----PQWLQVDLGKTRRVTGIQTQGRKGGGSS 72

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 6679731  1947 CFTTEFQVAYSSDQTNWQIFRGKSGksVMYFTGNSDGSTIKENRLDPPIVARYIRIHPTKSYNRPTLRLELQG 2019
Cdd:cd00057   73 EWVTSYKVQYSLDGETWTTYKDKGE--EKVFTGNSDGSTPVTNDFPPPIVARYIRILPTTWNGNISLRLELYG 143
FA58C smart00231
Coagulation factor 5/8 C-terminal domain, discoidin domain; Cell surface-attached ...
 1865-2020 2.47e-34

Coagulation factor 5/8 C-terminal domain, discoidin domain; Cell surface-attached carbohydrate-binding domain, present in eukaryotes and assumed to have horizontally transferred to eubacterial genomes.


Pssm-ID: 214572  Cd Length: 139  Bit Score: 129.17  E-value: 2.47e-34
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6679731     1865 ECKMPMGLStgviSDSQIKASEylTYWEPRLARLNnAGSYNAWSIEKTALdfpiKPWIQVDMQKEVVVTGIQTQGAKHYL 1944
Cdd:smart00231    1 PCNEPLGLE----SDSQITASS--SYWAAKIARLN-GGSDGGWCPAKNDL----PPWIQVDLGRLRTVTGVITGRRHGNG 69

                            90       100       110       120       130       140       150
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 6679731     1945 KscFTTEFQVaYSSDQTNWQIFRGKSGksvMYFTGNSDGSTIKENRLDPPIVARYIRIHPTKSYNRPTLRLELQGC 2020
Cdd:smart00231   70 D--WVTYKLE-YSDDGVNWTTYKDGNS---KVFPGNSDAGTVVLNDFPPPIVARYVRILPTGWNGNIILRVELLGC 139
FA58C smart00231
Coagulation factor 5/8 C-terminal domain, discoidin domain; Cell surface-attached ...
 2024-2180 9.15e-34

Coagulation factor 5/8 C-terminal domain, discoidin domain; Cell surface-attached carbohydrate-binding domain, present in eukaryotes and assumed to have horizontally transferred to eubacterial genomes.


Pssm-ID: 214572  Cd Length: 139  Bit Score: 127.63  E-value: 9.15e-34
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6679731     2024 GCSTPLGLEDgriqDKQITASSfkkswwgDYWEPSLARLNaQGRVNAWQAKANNNKQWLQVDLLKIKKVTAIVTQGCKSL 2103
Cdd:smart00231    1 PCNEPLGLES----DSQITASS-------SYWAAKIARLN-GGSDGGWCPAKNDLPPWIQVDLGRLRTVTGVITGRRHGN 68

                            90       100       110       120       130       140       150
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 6679731     2104 SSEMYVKsysIQYSDQGVAWKPYRQKSSMVdkiFEGNSNTKGHMKNFFNPPIISRFIRIIPKTWNQSIALRLELFGC 2180
Cdd:smart00231   69 GDWVTYK---LEYSDDGVNWTTYKDGNSKV---FPGNSDAGTVVLNDFPPPIVARYVRILPTGWNGNIILRVELLGC 139
F5_F8_type_C pfam00754
F5/8 type C domain; This domain is also known as the discoidin (DS) domain family.
 2040-2177 5.94e-33

F5/8 type C domain; This domain is also known as the discoidin (DS) domain family.


Pssm-ID: 459925 [Multi-domain]  Cd Length: 127  Bit Score: 124.87  E-value: 5.94e-33
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6679731    2040 QITASSfkkSWWGDYwePSLARLNaqGRVN-AWQAKANNNKQWLQVDLLKIKKVTAIVTQGCKSLSSeMYVKSYSIQYSD 2118
Cdd:pfam00754    1 QITASS---SYSGEG--PAAAALD--GDPNtAWSAWSGDDPQWIQVDLGKPKKITGVVTQGRQDGSN-GYVTSYKIEYSL 72

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 6679731    2119 QGVAWKPYRqkssmvDKIFEGNSNTKGHMKNFFNPPIISRFIRIIPKTWN--QSIALRLEL 2177
Cdd:pfam00754   73 DGENWTTVK------DEKIPGNNDNNTPVTNTFDPPIKARYVRIVPTSWNggNGIALRAEL 127
F5_F8_type_C pfam00754
F5/8 type C domain; This domain is also known as the discoidin (DS) domain family.
 1881-2017 8.20e-26

F5/8 type C domain; This domain is also known as the discoidin (DS) domain family.


Pssm-ID: 459925 [Multi-domain]  Cd Length: 127  Bit Score: 104.45  E-value: 8.20e-26
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6679731    1881 QIKASEYLTYWEPRLARLNNAGSyNAWSiektALDFPIKPWIQVDMQKEVVVTGIQTQGAKHyLKSCFTTEFQVAYSSDQ 1960
Cdd:pfam00754    1 QITASSSYSGEGPAAAALDGDPN-TAWS----AWSGDDPQWIQVDLGKPKKITGVVTQGRQD-GSNGYVTSYKIEYSLDG 74

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 6679731    1961 TNWQIFRGKsgksvmYFTGNSDGSTIKENRLDPPIVARYIRIHPTK--SYNRPTLRLEL 2017
Cdd:pfam00754   75 ENWTTVKDE------KIPGNNDNNTPVTNTFDPPIKARYVRIVPTSwnGGNGIALRAEL 127
Cu-oxidase_3 pfam07732
Multicopper oxidase; This entry contains many divergent copper oxidase-like domains that are ...
 81-191 6.35e-09

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


Pssm-ID: 462247 [Multi-domain]  Cd Length: 119  Bit Score: 55.71  E-value: 6.35e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6679731      81 NSGLLGPTLYAEVGDVIKVHFRNKADKPLSIHPQGIkyskFSEGASYAD----HTFpaerkdDAVAPGEEYTYEWIVSED 156
Cdd:pfam07732   21 NGQFPGPTIRVREGDTVVVNVTNNLDEPTSIHWHGL----QQRGTPWMDgvpgVTQ------CPIPPGQSFTYRFQVKQQ 90

                           90       100       110
                   ....*....|....*....|....*....|....*
gi 6679731     157 SGptpddppclTHIYYSYENLTQdfNSGLIGPLLI 191
Cdd:pfam07732   91 AG---------TYWYHSHTSGQQ--AAGLAGAIII 114
SufI COG2132
Multicopper oxidase with three cupredoxin domains (includes cell division protein FtsP and ...
 1603-1826 9.48e-08

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


Pssm-ID: 441735 [Multi-domain]  Cd Length: 423  Bit Score: 56.87  E-value: 9.48e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6679731  1603 ILGPVIRAEVDDVIQVRFKNLASRPYSLHAHGL--SYEkssegktyEDESPEwfqedDAVQPNSSYTYVWHATKRSG--- 1677
Cdd:COG2132   42 YPGPTIRVREGDRVRVRVTNRLPEPTTVHWHGLrvPNA--------MDGVPG-----DPIAPGETFTYEFPVPQPAGtyw 108

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6679731  1678 --PENPGSacrawayySAVNVERdihsGLIGPLLIcRKGtlhmERNLPMDMREFVLLF--MVFDEKKSWYYEKSKGSRRI 1753
Cdd:COG2132  109 yhPHTHGS--------TAEQVYR----GLAGALIV-EDP----EEDLPRYDRDIPLVLqdWRLDDDGQLLYPMDAAMGGR 171

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6679731  1754 ESPeeknahkFYAINGMIynLPGLRMYEQEWVRLHLLNMGGSR----------DIHVVHFHGQTLldnrTKQHQLGVWPL 1823
Cdd:COG2132  172 LGD-------TLLVNGRP--NPTLEVRPGERVRLRLLNASNARiyrlalsdgrPFTVIATDGGLL----PAPVEVDELLL 238


                 ...
gi 6679731  1824 LPG 1826
Cdd:COG2132  239 APG 241
SufI COG2132
Multicopper oxidase with three cupredoxin domains (includes cell division protein FtsP and ...
 81-257 1.16e-07

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


Pssm-ID: 441735 [Multi-domain]  Cd Length: 423  Bit Score: 56.48  E-value: 1.16e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6679731    81 NSGLLGPTLYAEVGDVIKVHFRNKADKPLSIHPQGIKYSkfsegASYADHTFPaerkddAVAPGEEYTYEWivsedsgpT 160
Cdd:COG2132   39 NGQYPGPTIRVREGDRVRVRVTNRLPEPTTVHWHGLRVP-----NAMDGVPGD------PIAPGETFTYEF--------P 99

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6679731   161 PDDPPClTHIYYSYENLTQDFN--SGLIGPLLIckkgtltEDG---------------TQKMFDKQHVLLFAVFDESKSR 223
Cdd:COG2132  100 VPQPAG-TYWYHPHTHGSTAEQvyRGLAGALIV-------EDPeedlprydrdiplvlQDWRLDDDGQLLYPMDAAMGGR 171

                        170       180       190
                 ....*....|....*....|....*....|....
gi 6679731   224 SQSpslMYTINGfvnKTMPDITVCAHDHVSWHLI 257
Cdd:COG2132  172 LGD---TLLVNG---RPNPTLEVRPGERVRLRLL 199
PLN02191 PLN02191
L-ascorbate oxidase
 81-201 4.20e-05

L-ascorbate oxidase


Pssm-ID: 177843 [Multi-domain]  Cd Length: 574  Bit Score: 48.86  E-value: 4.20e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6679731     81 NSGLLGPTLYAEVGDVIKVHFRNK-ADKPLSIHPQGIKyskfSEGASYADHTfpAERKDDAVAPGEEYTYEWIVsEDSGp 159
Cdd:PLN02191   48 NGQFPGPTIDAVAGDTIVVHLTNKlTTEGLVIHWHGIR----QKGSPWADGA--AGVTQCAINPGETFTYKFTV-EKPG- 119

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 6679731    160 tpddppclTHIYYSYENLTQdfNSGLIGPLLIC----KKGTLTEDG 201
Cdd:PLN02191  120 --------THFYHGHYGMQR--SAGLYGSLIVDvakgPKERLRYDG 155
Cu-oxidase_3 pfam07732
Multicopper oxidase; This entry contains many divergent copper oxidase-like domains that are ...
 417-485 5.78e-05

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


Pssm-ID: 462247 [Multi-domain]  Cd Length: 119  Bit Score: 44.54  E-value: 5.78e-05
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 6679731     417 ILGPVIRAQVRDTLKIVFKNMASRPYSIYPHG--VTFSPYEDGINSSSTsgshttiRPVQPGETFTYKWNI 485
Cdd:pfam07732   24 FPGPTIRVREGDTVVVNVTNNLDEPTSIHWHGlqQRGTPWMDGVPGVTQ-------CPIPPGQSFTYRFQV 87
Cu-oxidase_3 pfam07732
Multicopper oxidase; This entry contains many divergent copper oxidase-like domains that are ...
 1603-1677 1.81e-04

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


Pssm-ID: 462247 [Multi-domain]  Cd Length: 119  Bit Score: 43.00  E-value: 1.81e-04
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 6679731    1603 ILGPVIRAEVDDVIQVRFKNLASRPYSLHAHGLSYEKSSegktYEDESPEWFQedDAVQPNSSYTYVWHATKRSG 1677
Cdd:pfam07732   24 FPGPTIRVREGDTVVVNVTNNLDEPTSIHWHGLQQRGTP----WMDGVPGVTQ--CPIPPGQSFTYRFQVKQQAG 92
SufI COG2132
Multicopper oxidase with three cupredoxin domains (includes cell division protein FtsP and ...
 417-485 1.21e-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: 43.77  E-value: 1.21e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 6679731   417 ILGPVIRAQVRDTLKIVFKNMASRPYSIYPHGVTFSPYEDGINSsstsgshttiRPVQPGETFTYKWNI 485
Cdd:COG2132   42 YPGPTIRVREGDRVRVRVTNRLPEPTTVHWHGLRVPNAMDGVPG----------DPIAPGETFTYEFPV 100
ascorbase TIGR03388
L-ascorbate oxidase, plant type; Members of this protein family are the copper-containing ...
 86-191 1.87e-03

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


Pssm-ID: 274555 [Multi-domain]  Cd Length: 541  Bit Score: 43.20  E-value: 1.87e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6679731      86 GPTLYAEVGDVIKVHFRNK-ADKPLSIHPQGIKyskfSEGASYADHTfpAERKDDAVAPGEEYTYEWIVsedsgptpDDP 164
Cdd:TIGR03388   31 GPTIRAQAGDTIVVELTNKlHTEGVVIHWHGIR----QIGTPWADGT--AGVTQCAINPGETFIYNFVV--------DRP 96

                           90       100
                   ....*....|....*....|....*..
gi 6679731     165 PclTHIYYSYENLTQdfNSGLIGPLLI 191
Cdd:TIGR03388   97 G--TYFYHGHYGMQR--SAGLYGSLIV 119
PLN02191 PLN02191
L-ascorbate oxidase
 419-532 2.23e-03

L-ascorbate oxidase


Pssm-ID: 177843 [Multi-domain]  Cd Length: 574  Bit Score: 43.08  E-value: 2.23e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6679731    419 GPVIRAQVRDTLKIVFKN-MASRPYSIYPHGVT--FSPYEDGINSSSTSgshttirPVQPGETFTYKWNIlefDEPTend 495
Cdd:PLN02191   53 GPTIDAVAGDTIVVHLTNkLTTEGLVIHWHGIRqkGSPWADGAAGVTQC-------AINPGETFTYKFTV---EKPG--- 119

                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 6679731    496 aqclTRPYYSDVDVTRdiASGLIGLLLICKSRSLDQR 532
Cdd:PLN02191  120 ----THFYHGHYGMQR--SAGLYGSLIVDVAKGPKER 150
Cu-oxidase_2 pfam07731
Multicopper oxidase; This entry contains many divergent copper oxidase-like domains that are ...
 1762-1865 2.34e-03

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


Pssm-ID: 462246 [Multi-domain]  Cd Length: 138  Bit Score: 40.50  E-value: 2.34e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6679731    1762 HKFYAINGMIY--NLPGLRMYEQEWVRLHLLNMGGsrDIHVVHFHG------------QTLLDNRTKQHQLGVW----PL 1823
Cdd:pfam07731   19 RNDWAINGLLFppNTNVITLPYGTVVEWVLQNTTT--GVHPFHLHGhsfqvlgrgggpWPEEDPKTYNLVDPVRrdtvQV 96

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|..
gi 6679731    1824 LPGSFKTLEMKASKPGWWLLDTEVGENQVAGMQTPFLIIDKE 1865
Cdd:pfam07731   97 PPGGWVAIRFRADNPGVWLFHCHILWHLDQGMMGQFVVRPGD 138
 
Name Accession Description Interval E-value
CuRO_5_FV_like cd14451
The fifth cupredoxin domain of coagulation factor V and similar proteins; Factor V is an ...
 1539-1714 2.39e-109

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: 345.29  E-value: 2.39e-109
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6679731  1539 KKFYYIAAEEITWNYAEFAQSEMDHEdtgHTPKDTTYKKVVFRKYLDSTFTSRDPRAEYEEHLGILGPVIRAEVDDVIQV 1618
Cdd:cd14451    1 KRRYYIAAEEEEWDYAGYGKSRLDKT---QNERDTVFKKVVFRRYLDSTFSTPDIQGEYEEHLGILGPVIRAEVDDVIQV 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6679731  1619 RFKNLASRPYSLHAHGLSYEKSSEGKTYEDESPEWFQEDDAVQPNSSYTYVWHATKRSGPENPGSACRAWAYYSAVNVER 1698
Cdd:cd14451   78 FFKNLASRPYSLHAHGLSYEKSSEGLSYDDESPDWFKKDDAVQPNGTYTYVWYANPRSGPENNGSDCRTWAYYSAVNPEK 157

                        170
                 ....*....|....*.
gi 6679731  1699 DIHSGLIGPLLICRKG 1714
Cdd:cd14451  158 DIHSGLIGPLLICRKG 173
CuRO_3_FV_like cd14450
The third cupredoxin domain of coagulation factor V and similar proteins; Factor V is an ...
 347-526 1.74e-104

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: 331.84  E-value: 1.74e-104
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6679731   347 KRWEYFIAAEEVIWNYAPVIPANMDKIYRSQHLDNFSNQIGKHYKKVIYRQYEEETFTKRTDNPSIKQSGILGPVIRAQV 426
Cdd:cd14450    1 KNWEYFIAAEEVIWDYAPSIPENMDKRYRSQYLDNFSNNIGKKYKKAVFTQYEDGSFTKRLENPRPKEEGILGPVIRAQV 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6679731   427 RDTLKIVFKNMASRPYSIYPHGVTFSPYEDGINSSSTSGS-HTTIRPVQPGETFTYKWNILEFDEPTENDAQCLTRPYYS 505
Cdd:cd14450   81 RDTIKIVFKNKASRPYSIYPHGVTVSKAAEGASYPPDPRGnETQNKAVQPGETYTYKWNILETDEPTARDPRCLTRMYHS 160

                        170       180
                 ....*....|....*....|.
gi 6679731   506 DVDVTRDIASGLIGLLLICKS 526
Cdd:cd14450  161 AVDITRDIASGLIGPLLICKS 181
CuRO_1_FV_like cd04226
The first cupredoxin domain of coagulation factor VIII and similar proteins; Factor V is an ...
 32-195 5.98e-94

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: 301.01  E-value: 5.98e-94
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6679731    32 RQFYVAAQGILWNYHPEPTDPSLNSI-PSFKKIVYREYEQYFKKEKPRSSNSGLLGPTLYAEVGDVIKVHFRNKADKPLS 110
Cdd:cd04226    1 REYYIAAQNIDWDYTPQSEELRLKRSeQSFKKIVYREYEEGFKKEKPADLSSGLLGPTLRAEVGDTLIVHFKNMADKPLS 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6679731   111 IHPQGIKYSKFSEGASYADHTFPAERKDDAVAPGEEYTYEWIVSEDSGPTPDDPPCLTHIYYSYENLTQDFNSGLIGPLL 190
Cdd:cd04226   81 IHPQGIAYGKKSEGSLYSDNTSPVEKLDDAVQPGQEYTYVWDITEEVGPTEADPPCLTYIYYSHVNMVRDFNSGLIGALL 160


                 ....*
gi 6679731   191 ICKKG 195
Cdd:cd04226  161 ICKKG 165
CuRO_4_FV_like cd14454
The fourth cupredoxin domain of coagulation factor V and similar proteins; Factor V is an ...
 539-682 1.14e-85

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: 276.37  E-value: 1.14e-85
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6679731   539 DIEQQAVFAVFDENKSWYIEDNINKFCENPDEVKRDDPKFYESNIMSTINGYVPESISTLGFCFDDTVQWHFCSVGTHDD 618
Cdd:cd14454    1 DLEQHAVFAVFDENKSWYLEENINKYCSNPNNVKKDDPKFYKSNIMPTINGYAYESSAPLGFCHSEVVQWHISSVGTQDE 80

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 6679731   619 ILTIHFTGHSFIYGRRHEDTLTLFPMRGESVTVTMDNVGTWMLTTMNSNPKRRNLRLRFRDVKC 682
Cdd:cd14454   81 IITVHLSGHTFRYKGKHEDTLNLFPMSGESITVTMDNLGTWLLGSFGSSKKSKGLRVRFTDVIC 144
CuRO_1_ceruloplasmin_like cd04199
Cupredoxin domains 1, 3, and 5 of ceruloplasmin and similar proteins; This family includes the ...
 1540-1713 1.52e-85

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: 277.36  E-value: 1.52e-85
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6679731  1540 KFYYIAAEEITWNYAEFAQSEMD------HEDTGHTPKDTTYKKVVFRKYLDSTFTSRDPraeYEEHLGILGPVIRAEVD 1613
Cdd:cd04199    1 RHYYIAAEEIDWDYAPSGLAEKDlsyrnqYLDNGPFRIGRSYKKVVYREYTDESFTTPGP---QPEHLGILGPTIRAEVG 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6679731  1614 DVIQVRFKNLASRPYSLHAHGLSYEKSSEGKTYEDESPEWFQEDDAVQPNSSYTYVWHATKRSGPENPGSACRAWAYYSA 1693
Cdd:cd04199   78 DTIKVHFKNKASRPYSIHPHGVSYEKDSEGASYSDQTGPDEKKDDAVAPGETYTYVWIVTEESGPTKGDPACLTWAYYSH 157

                        170       180
                 ....*....|....*....|
gi 6679731  1694 VNVERDIHSGLIGPLLICRK 1713
Cdd:cd04199  158 VDLEKDINSGLIGPLLICKK 177
CuRO_1_ceruloplasmin_like cd04199
Cupredoxin domains 1, 3, and 5 of ceruloplasmin and similar proteins; This family includes the ...
 349-526 1.24e-84

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: 274.67  E-value: 1.24e-84
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6679731   349 WEYFIAAEEVIWNYAPVIPANMDKIYRSQHLDNFSNQIGKHYKKVIYRQYEEETFTKRTDNPsiKQSGILGPVIRAQVRD 428
Cdd:cd04199    1 RHYYIAAEEIDWDYAPSGLAEKDLSYRNQYLDNGPFRIGRSYKKVVYREYTDESFTTPGPQP--EHLGILGPTIRAEVGD 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6679731   429 TLKIVFKNMASRPYSIYPHGVTFSPYEDGINSSSTSGSHTT-IRPVQPGETFTYKWNILEFDEPTENDAQCLTRPYYSDV 507
Cdd:cd04199   79 TIKVHFKNKASRPYSIHPHGVSYEKDSEGASYSDQTGPDEKkDDAVAPGETYTYVWIVTEESGPTKGDPACLTWAYYSHV 158

                        170
                 ....*....|....*....
gi 6679731   508 DVTRDIASGLIGLLLICKS 526
Cdd:cd04199  159 DLEKDINSGLIGPLLICKK 177
CuRO_6_FV_like cd14455
The sixth cupredoxin domain of coagulation factor V and similar proteins; Factor V is an ...
 1726-1861 1.05e-78

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: 256.33  E-value: 1.05e-78
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6679731  1726 MREFVLLFMVFDEKKSWYYEKSKGS----RRIESPEEKNAHKFYAINGMIYNLPGLRMYEQEWVRLHLLNMGGSRDIHVV 1801
Cdd:cd14455    1 RREFVLLFMTFDEEKSWYYEKNRKRtcreNRVKDPNVQDNHTFHAINGIIYNLKGLRMYTNELVRWHLINMGGPKDLHVV 80

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 6679731  1802 HFHGQTLLDNRTKQHQLGVWPLLPGSFKTLEMKASKPGWWLLDTEVGENQVAGMQTPFLI 1861
Cdd:cd14455   81 HFHGQTFTEKGLKDHQLGVYPLLPGSFATLEMKPSKPGLWLLETEVGESQQRGMQTLFLV 140
CuRO_1_ceruloplasmin_like cd04199
Cupredoxin domains 1, 3, and 5 of ceruloplasmin and similar proteins; This family includes the ...
 32-194 3.60e-76

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


Pssm-ID: 259862 [Multi-domain]  Cd Length: 177  Bit Score: 250.40  E-value: 3.60e-76
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6679731    32 RQFYVAAQGILWNYHPEPTDPSLNSI-------------PSFKKIVYREYEQY-FKKEKPRSSNSGLLGPTLYAEVGDVI 97
Cdd:cd04199    1 RHYYIAAEEIDWDYAPSGLAEKDLSYrnqyldngpfrigRSYKKVVYREYTDEsFTTPGPQPEHLGILGPTIRAEVGDTI 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6679731    98 KVHFRNKADKPLSIHPQGIKYSKFSEGASYADHTFPAERKDDAVAPGEEYTYEWIVSEDSGPTPDDPPCLTHIYYSYENL 177
Cdd:cd04199   81 KVHFKNKASRPYSIHPHGVSYEKDSEGASYSDQTGPDEKKDDAVAPGETYTYVWIVTEESGPTKGDPACLTWAYYSHVDL 160

                        170
                 ....*....|....*..
gi 6679731   178 TQDFNSGLIGPLLICKK 194
Cdd:cd04199  161 EKDINSGLIGPLLICKK 177
CuRO_2_FV_like cd14453
The second cupredoxin domain of coagulation factor V and similar proteins; Factor V is an ...
 207-325 1.38e-70

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: 232.44  E-value: 1.38e-70
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6679731   207 DKQHVLLFAVFDESKS----RSQSPSLMYTINGFVNKTMPDITVCAHDHVSWHLIGMSSGPELFSIHFNGQVLEQNQHKV 282
Cdd:cd14453    1 YKEYVLMFGVFDENKSwykqNASVDSVKYTINGYTNGTLPDVSICAYDHVSWHLLGMSSEPELFSVHFNGQVLEQNGHKV 80

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|...
gi 6679731   283 STVTLVSATSTTANMTMSPEGRWIVSSLIPKHYQAGMQAYIDI 325
Cdd:cd14453   81 SAVGLVSGSSTTASMTVVHTGRWLISSLIMKHLQAGMYGYLNI 123
CuRO_2_ceruloplasmin_like cd04200
Cupredoxin domains 2, 4, and 6 of ceruloplasmin and similar proteins; This family includes the ...
 539-679 1.04e-63

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


Pssm-ID: 259863 [Multi-domain]  Cd Length: 141  Bit Score: 213.43  E-value: 1.04e-63
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6679731   539 DIEQQAVFAVFDENKSWYIEDNINKFCENPDEVKRDDPKFYESNIMSTINGYVPESISTLGFCFDDTVQWHFCSVGTHDD 618
Cdd:cd04200    1 DKEFVLLFAVFDENKSWYLEDNIKRFCDNPEKVDKDDEEFQESNKMHAINGYVFGNLPGLTMCAGDRVRWHLLGMGNEVD 80

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 6679731   619 ILTIHFTGHSFIYGRRHEDTLTLFPMRGESVTVTMDNVGTWMLTTMNSNPKRRNLRLRFRD 679
Cdd:cd04200   81 VHSIHFHGQTFLYKGYRIDTLTLFPATFETVEMVPSNPGTWLLHCHNSDHRHAGMQAYFLV 141
CuRO_3_ceruloplasmin cd04224
The third cupredoxin domain of Ceruloplasmin; Ceruloplasmin is a multicopper oxidase essential ...
 1537-1717 3.20e-62

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


Pssm-ID: 259886 [Multi-domain]  Cd Length: 197  Bit Score: 211.56  E-value: 3.20e-62
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6679731  1537 GHKKFYYIAAEEITWNYAEFAQSEMDHEDTGHTPKDT-------------TYKKVVFRKYLDSTFTSRDPRAEYEEHLGI 1603
Cdd:cd04224    1 GKVRHYFIAAEEIMWDYAPSGKNLFTGQNLTAPGSDSevffqrnetriggTYWKVRYVEYTDATFTTRKHRSKEEEHLGI 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6679731  1604 LGPVIRAEVDDVIQVRFKNLASRPYSLHAHGLSYEKSSEGKTYEDESPewfQEDDAVQPNSSYTYVWHATKRSGPENPGS 1683
Cdd:cd04224   81 LGPVIRAEVGDTIKVTFRNKASRPFSIQPHGVFYEKNYEGAMYRDGDP---SPGSHVSPGETFTYEWTVPEGVGPTNQDP 157

                        170       180       190
                 ....*....|....*....|....*....|....
gi 6679731  1684 ACRAWAYYSAVNVERDIHSGLIGPLLICRKGTLH 1717
Cdd:cd04224  158 PCLTYLYFSAVDPVRDTNSGLVGPLLVCKKGSLN 191
CuRO_3_ceruloplasmin cd04224
The third cupredoxin domain of Ceruloplasmin; Ceruloplasmin is a multicopper oxidase essential ...
 30-204 1.55e-59

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


Pssm-ID: 259886 [Multi-domain]  Cd Length: 197  Bit Score: 203.86  E-value: 1.55e-59
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6679731    30 QLRQFYVAAQGILWNYHPEPTD---------PSLNSIP-----------SFKKIVYREY-EQYFKKEKPRSSNS---GLL 85
Cdd:cd04224    2 KVRHYFIAAEEIMWDYAPSGKNlftgqnltaPGSDSEVffqrnetriggTYWKVRYVEYtDATFTTRKHRSKEEehlGIL 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6679731    86 GPTLYAEVGDVIKVHFRNKADKPLSIHPQGIKYSKFSEGASYADHT-FPAERkddaVAPGEEYTYEWIVSEDSGPTPDDP 164
Cdd:cd04224   82 GPVIRAEVGDTIKVTFRNKASRPFSIQPHGVFYEKNYEGAMYRDGDpSPGSH----VSPGETFTYEWTVPEGVGPTNQDP 157

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|
gi 6679731   165 PCLTHIYYSYENLTQDFNSGLIGPLLICKKGTLTEDGTQK 204
Cdd:cd04224  158 PCLTYLYFSAVDPVRDTNSGLVGPLLVCKKGSLNANGRQK 197
CuRO_3_FVIII_like cd04227
The third cupredoxin domain of coagulation factor VIII and similar proteins; Factor VIII ...
 347-525 4.08e-58

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: 199.00  E-value: 4.08e-58
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6679731   347 KRWEYFIAAEEVIWNYAPVIPANMDKIYRSQHLDNFSNQIGKHYKKVIYRQYEEETFTKRTDNPSikQSGILGPVIRAQV 426
Cdd:cd04227    1 QTWEHYIAAEELDWDYAPLLSSTDDRELQSRYLPTGPQRIGYKYKKVAFVEYTDKTFKRREAKQT--EKGILGPLLKGEV 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6679731   427 RDTLKIVFKNMASRPYSIYPHGVT-FSPYEDGINSSSTSGSHTTirPVQPGETFTYKWNILEFDEPTENDAQCLTRPYYS 505
Cdd:cd04227   79 GDQIHIMFKNTASRPYNIYPHGLTsVRPMYRSRNPAGEKDLKTM--PIGPGETFGYMWELTAEDGPTEEDPRCLTRLYQS 156

                        170       180
                 ....*....|....*....|
gi 6679731   506 DVDVTRDIASGLIGLLLICK 525
Cdd:cd04227  157 TVDPERDLASGLIGPLLICK 176
FA58C cd00057
Coagulation factor 5/8 C-terminal domain, discoidin domain; Cell surface-attached ...
 2027-2179 6.00e-56

Coagulation factor 5/8 C-terminal domain, discoidin domain; Cell surface-attached carbohydrate-binding domain, present in eukaryotes and assumed to have horizontally transferred to eubacterial genomes.


Pssm-ID: 238014 [Multi-domain]  Cd Length: 143  Bit Score: 191.03  E-value: 6.00e-56
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6679731  2027 TPLGLEDGRiQDKQITASSfkksWWGDYWEPSLARLNaqgRVNAWQAKANNNKQWLQVDLLKIKKVTAIVTQGCKSLSSE 2106
Cdd:cd00057    1 EPLGMESGL-ADDQITASS----SYSSGWEASRARLN---SDNAWTPAVNDPPQWLQVDLGKTRRVTGIQTQGRKGGGSS 72

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 6679731  2107 MYVKSYSIQYSDQGVAWKPYRQKssMVDKIFEGNSNTKGHMKNFFNPPIISRFIRIIPKTWNQSIALRLELFG 2179
Cdd:cd00057   73 EWVTSYKVQYSLDGETWTTYKDK--GEEKVFTGNSDGSTPVTNDFPPPIVARYIRILPTTWNGNISLRLELYG 143
CuRO_3_ceruloplasmin cd04224
The third cupredoxin domain of Ceruloplasmin; Ceruloplasmin is a multicopper oxidase essential ...
 351-536 1.14e-54

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: 189.61  E-value: 1.14e-54
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6679731   351 YFIAAEEVIWNYAPvipANMDKIYRSQHL------DNF----SNQIGKHYKKVIYRQYEEETFTKRTD-NPSIKQSGILG 419
Cdd:cd04224    6 YFIAAEEIMWDYAP---SGKNLFTGQNLTapgsdsEVFfqrnETRIGGTYWKVRYVEYTDATFTTRKHrSKEEEHLGILG 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6679731   420 PVIRAQVRDTLKIVFKNMASRPYSIYPHGVTFSPYEDGINSSSTSGSHTTirPVQPGETFTYKWNILEFDEPTENDAQCL 499
Cdd:cd04224   83 PVIRAEVGDTIKVTFRNKASRPFSIQPHGVFYEKNYEGAMYRDGDPSPGS--HVSPGETFTYEWTVPEGVGPTNQDPPCL 160

                        170       180       190
                 ....*....|....*....|....*....|....*..
gi 6679731   500 TRPYYSDVDVTRDIASGLIGLLLICKSRSLDQRGVQR 536
Cdd:cd04224  161 TYLYFSAVDPVRDTNSGLVGPLLVCKKGSLNANGRQK 197
CuRO_5_FVIII_like cd04228
The fifth cupredoxin domain of coagulation factor VIII and similar proteins; Factor VIII ...
 1542-1714 1.95e-53

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: 185.09  E-value: 1.95e-53
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6679731  1542 YYIAAEEITWNYAE------FAQSEMDHEDTGHTPKdttYKKVVFRKYLDSTFTSRDPRAEYEEHLGILGPVIRAEVDDV 1615
Cdd:cd04228    4 YFIAAVEVLWDYGMqrpqhfLRARDPNRGRRKSVPQ---YKKVVFREYLDGSFTQPVYRGELDEHLGILGPYIRAEVEDN 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6679731  1616 IQVRFKNLASRPYSLHAHGLSYEkssegktyEDESPEwfQEDDAVQPNSSYTYVWHATKRSGPENPGSACRAWAYYSAVN 1695
Cdd:cd04228   81 IMVTFKNLASRPYSFHSSLISYE--------EDQRAE--PRGNFVQPGEVQTYSWKVLHQMAPTKQEFDCKAWAYFSNVD 150

                        170
                 ....*....|....*....
gi 6679731  1696 VERDIHSGLIGPLLICRKG 1714
Cdd:cd04228  151 LEKDLHSGLIGPLIICKTG 169
CuRO_2_ceruloplasmin_like cd04200
Cupredoxin domains 2, 4, and 6 of ceruloplasmin and similar proteins; This family includes the ...
 1726-1861 1.32e-52

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: 181.45  E-value: 1.32e-52
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6679731  1726 MREFVLLFMVFDEKKSWYYEK-------SKGSRRIESPEEKNAHKFYAINGMIY-NLPGLRMYEQEWVRLHLLNMGGSRD 1797
Cdd:cd04200    1 DKEFVLLFAVFDENKSWYLEDnikrfcdNPEKVDKDDEEFQESNKMHAINGYVFgNLPGLTMCAGDRVRWHLLGMGNEVD 80

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 6679731  1798 IHVVHFHGQTLLDnrtKQHQLGVWPLLPGSFKTLEMKASKPGWWLLDTEVGENQVAGMQTPFLI 1861
Cdd:cd04200   81 VHSIHFHGQTFLY---KGYRIDTLTLFPATFETVEMVPSNPGTWLLHCHNSDHRHAGMQAYFLV 141
CuRO_5_ceruloplasmin cd04225
The fifth cupredoxin domain of Ceruloplasmin; Ceruloplasmin is a multicopper oxidase essential ...
 1540-1713 2.36e-51

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: 179.20  E-value: 2.36e-51
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6679731  1540 KFYYIAAEEITWNYAEFAQSEMD-HEDTGHTPKD-----------TTYKKVVFRKYLDSTFTSRDPRAEYEEHLGILGPV 1607
Cdd:cd04225    1 RTYYIAAEEVEWDYSPQRTWEQElHNTHEESPGNaflnkgdkfigSKYKKVVYREYTDDTFSVPKERTAEEEHLGILGPL 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6679731  1608 IRAEVDDVIQVRFKNLASRPYSLHAHGLSYEKSSEGKTyedespewfqeddavQPNSSYTYVWHATKRSGPENPGSACRA 1687
Cdd:cd04225   81 IHAEVGEKVKIVFKNMASRPYSIHAHGVKTDSSWVAPT---------------EPGETQTYTWKIPERSGPGVEDSNCIS 145

                        170       180
                 ....*....|....*....|....*.
gi 6679731  1688 WAYYSAVNVERDIHSGLIGPLLICRK 1713
Cdd:cd04225  146 WAYYSTVDQIKDLYSGLIGPLVICRR 171
CuRO_3_FV_like cd14450
The third cupredoxin domain of coagulation factor V and similar proteins; Factor V is an ...
 1542-1712 3.13e-51

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


Pssm-ID: 259992 [Multi-domain]  Cd Length: 181  Bit Score: 179.30  E-value: 3.13e-51
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6679731  1542 YYIAAEEITWNYAEFAQSEMD------HEDTGHTPKDTTYKKVVFRKYLDSTFTSR--DPRAEyeeHLGILGPVIRAEVD 1613
Cdd:cd14450    5 YFIAAEEVIWDYAPSIPENMDkryrsqYLDNFSNNIGKKYKKAVFTQYEDGSFTKRleNPRPK---EEGILGPVIRAQVR 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6679731  1614 DVIQVRFKNLASRPYSLHAHGLSYEKSSEGKTYEDESPEWFQEDDAVQPNSSYTYVWHATKRSGPENPGSACRAWAYYSA 1693
Cdd:cd14450   82 DTIKIVFKNKASRPYSIYPHGVTVSKAAEGASYPPDPRGNETQNKAVQPGETYTYKWNILETDEPTARDPRCLTRMYHSA 161

                        170
                 ....*....|....*....
gi 6679731  1694 VNVERDIHSGLIGPLLICR 1712
Cdd:cd14450  162 VDITRDIASGLIGPLLICK 180
CuRO_1_FVIII_like cd14452
The first cupredoxin domain of coagulation factor VIII and similar proteins; Factor VIII ...
 1542-1714 1.62e-50

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


Pssm-ID: 259994 [Multi-domain]  Cd Length: 173  Bit Score: 177.09  E-value: 1.62e-50
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6679731  1542 YYIAAEEITWNYAEFAQSEMDhEDTGHTPKDTT--YKKVVFRKYLDSTFTSRDPRAEYeehLGILGPVIRAEVDDVIQVR 1619
Cdd:cd14452    3 YYIAAVEIGWDYIHSDLGDPA-SEQRKKPKDIPqkYIKAVFVEYLDATFTVPKPRPAW---MGLLGPTIVAEVGDTVVIT 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6679731  1620 FKNLASRPYSLHAHGLSYEKSSEGKTYEDESPEWFQEDDAVQPNSSYTYVWHATKRSGPENPGSACRAWAYYSAVNVERD 1699
Cdd:cd14452   79 FKNLASQPYSLHAVGVSYWKASEGAGYDDSTSQHEKEDDAVYPGGYHTYVWDISPKDGPTGSDPECLTYSYSSQVDPVKD 158

                        170
                 ....*....|....*
gi 6679731  1700 IHSGLIGPLLICRKG 1714
Cdd:cd14452  159 VNSGLIGALLVCRMG 173
CuRO_1_ceruloplasmin cd04222
The first cupredoxin domain of Ceruloplasmin; Ceruloplasmin is a multicopper oxidase essential ...
 1540-1713 2.47e-50

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: 176.84  E-value: 2.47e-50
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6679731  1540 KFYYIAAEEITWNYAEfaqsemDHED--TGHTPKDT----------------TYKKVVFRKYLDSTFTSRDPRAEYeehL 1601
Cdd:cd04222    1 REYYIGIRETQWDYAP------SGKNliTNQTFDDDehasvflkrgpdrigrVYKKAVYLQYTDDTYRTEIEKPVW---L 71

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6679731  1602 GILGPVIRAEVDDVIQVRFKNLASRPYSLHAHGLSYEKSSEGKTYEDESPEWFQEDDAVQPNSSYTYVWHATKRSGPENP 1681
Cdd:cd04222   72 GFLGPILKAEVGDVIVVHLKNFASRPYSLHPHGVFYNKENEGALYPDNTSGFEKADDAVPPGGSYTYTWTVPEEQAPTKA 151

                        170       180       190
                 ....*....|....*....|....*....|..
gi 6679731  1682 GSACRAWAYYSAVNVERDIHSGLIGPLLICRK 1713
Cdd:cd04222  152 DANCLTRIYHSHIDAPKDIASGLIGPLIICKK 183
CuRO_1_FV_like cd04226
The first cupredoxin domain of coagulation factor VIII and similar proteins; Factor V is an ...
 1542-1714 4.26e-50

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: 175.43  E-value: 4.26e-50
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6679731  1542 YYIAAEEITWNYAEfaqsemDHEDTGHTPKDTTYKKVVFRKYlDSTFTSRDPRAEYEehlGILGPVIRAEVDDVIQVRFK 1621
Cdd:cd04226    3 YYIAAQNIDWDYTP------QSEELRLKRSEQSFKKIVYREY-EEGFKKEKPADLSS---GLLGPTLRAEVGDTLIVHFK 72

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6679731  1622 NLASRPYSLHAHGLSYEKSSEGKTYEDESPEWFQEDDAVQPNSSYTYVWHATKRSGPENPGSACRAWAYYSAVNVERDIH 1701
Cdd:cd04226   73 NMADKPLSIHPQGIAYGKKSEGSLYSDNTSPVEKLDDAVQPGQEYTYVWDITEEVGPTEADPPCLTYIYYSHVNMVRDFN 152

                        170
                 ....*....|...
gi 6679731  1702 SGLIGPLLICRKG 1714
Cdd:cd04226  153 SGLIGALLICKKG 165
CuRO_1_ceruloplasmin cd04222
The first cupredoxin domain of Ceruloplasmin; Ceruloplasmin is a multicopper oxidase essential ...
 32-194 1.03e-48

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


Pssm-ID: 259884 [Multi-domain]  Cd Length: 183  Bit Score: 172.22  E-value: 1.03e-48
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6679731    32 RQFYVAAQGILWNYHPEPTDPSLNSI--------------PS-----FKKIVYREY-EQYFKKEKPRSSNSGLLGPTLYA 91
Cdd:cd04222    1 REYYIGIRETQWDYAPSGKNLITNQTfdddehasvflkrgPDrigrvYKKAVYLQYtDDTYRTEIEKPVWLGFLGPILKA 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6679731    92 EVGDVIKVHFRNKADKPLSIHPQGIKYSKFSEGASYADHTFPAERKDDAVAPGEEYTYEWIVSEDSGPTPDDPPCLTHIY 171
Cdd:cd04222   81 EVGDVIVVHLKNFASRPYSLHPHGVFYNKENEGALYPDNTSGFEKADDAVPPGGSYTYTWTVPEEQAPTKADANCLTRIY 160

                        170       180
                 ....*....|....*....|...
gi 6679731   172 YSYENLTQDFNSGLIGPLLICKK 194
Cdd:cd04222  161 HSHIDAPKDIASGLIGPLIICKK 183
CuRO_1_FVIII_like cd14452
The first cupredoxin domain of coagulation factor VIII and similar proteins; Factor VIII ...
 32-195 1.75e-48

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: 170.93  E-value: 1.75e-48
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6679731    32 RQFYVAAQGILWNY-HPEPTDPSLN--SIPS-----FKKIVYREY-EQYFKKEKPRSSNSGLLGPTLYAEVGDVIKVHFR 102
Cdd:cd14452    1 RRYYIAAVEIGWDYiHSDLGDPASEqrKKPKdipqkYIKAVFVEYlDATFTVPKPRPAWMGLLGPTIVAEVGDTVVITFK 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6679731   103 NKADKPLSIHPQGIKYSKFSEGASYADHTFPAERKDDAVAPGEEYTYEWIVSEDSGPTPDDPPCLTHIYYSYENLTQDFN 182
Cdd:cd14452   81 NLASQPYSLHAVGVSYWKASEGAGYDDSTSQHEKEDDAVYPGGYHTYVWDISPKDGPTGSDPECLTYSYSSQVDPVKDVN 160

                        170
                 ....*....|...
gi 6679731   183 SGLIGPLLICKKG 195
Cdd:cd14452  161 SGLIGALLVCRMG 173
FA58C cd00057
Coagulation factor 5/8 C-terminal domain, discoidin domain; Cell surface-attached ...
 1868-2019 2.25e-47

Coagulation factor 5/8 C-terminal domain, discoidin domain; Cell surface-attached carbohydrate-binding domain, present in eukaryotes and assumed to have horizontally transferred to eubacterial genomes.


Pssm-ID: 238014 [Multi-domain]  Cd Length: 143  Bit Score: 166.76  E-value: 2.25e-47
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6679731  1868 MPMGLSTGvISDSQIKA-SEYLTYWEPRLARLNnagSYNAWSIEKTALdfpiKPWIQVDMQKEVVVTGIQTQGAKHYLKS 1946
Cdd:cd00057    1 EPLGMESG-LADDQITAsSSYSSGWEASRARLN---SDNAWTPAVNDP----PQWLQVDLGKTRRVTGIQTQGRKGGGSS 72

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 6679731  1947 CFTTEFQVAYSSDQTNWQIFRGKSGksVMYFTGNSDGSTIKENRLDPPIVARYIRIHPTKSYNRPTLRLELQG 2019
Cdd:cd00057   73 EWVTSYKVQYSLDGETWTTYKDKGE--EKVFTGNSDGSTPVTNDFPPPIVARYIRILPTTWNGNISLRLELYG 143
CuRO_5_ceruloplasmin cd04225
The fifth cupredoxin domain of Ceruloplasmin; Ceruloplasmin is a multicopper oxidase essential ...
 351-525 1.76e-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: 165.33  E-value: 1.76e-46
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6679731   351 YFIAAEEVIWNYAPV------IPANMDKIYRSQHLDNFSNQIGKHYKKVIYRQYEEETFTKRTD-NPSIKQSGILGPVIR 423
Cdd:cd04225    3 YYIAAEEVEWDYSPQrtweqeLHNTHEESPGNAFLNKGDKFIGSKYKKVVYREYTDDTFSVPKErTAEEEHLGILGPLIH 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6679731   424 AQVRDTLKIVFKNMASRPYSIYPHGVTfspyEDGinssstsgshTTIRPVQPGETFTYKWNILEFDEPTENDAQCLTRPY 503
Cdd:cd04225   83 AEVGEKVKIVFKNMASRPYSIHAHGVK----TDS----------SWVAPTEPGETQTYTWKIPERSGPGVEDSNCISWAY 148

                        170       180
                 ....*....|....*....|..
gi 6679731   504 YSDVDVTRDIASGLIGLLLICK 525
Cdd:cd04225  149 YSTVDQIKDLYSGLIGPLVICR 170
CuRO_2_ceruloplasmin_like cd04200
Cupredoxin domains 2, 4, and 6 of ceruloplasmin and similar proteins; This family includes the ...
 207-325 5.42e-46

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: 162.58  E-value: 5.42e-46
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6679731   207 DKQHVLLFAVFDESKS----------------------RSQSPSLMYTINGFVNKTMPDITVCAHDHVSWHLIGMSSGPE 264
Cdd:cd04200    1 DKEFVLLFAVFDENKSwylednikrfcdnpekvdkddeEFQESNKMHAINGYVFGNLPGLTMCAGDRVRWHLLGMGNEVD 80

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 6679731   265 LFSIHFNGQVLEQNQHKVSTVTLVSATSTTANMTMSPEGRWIVSSLIPKHYQAGMQAYIDI 325
Cdd:cd04200   81 VHSIHFHGQTFLYKGYRIDTLTLFPATFETVEMVPSNPGTWLLHCHNSDHRHAGMQAYFLV 141
CuRO_1_ceruloplasmin cd04222
The first cupredoxin domain of Ceruloplasmin; Ceruloplasmin is a multicopper oxidase essential ...
 350-525 8.49e-46

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


Pssm-ID: 259884 [Multi-domain]  Cd Length: 183  Bit Score: 163.74  E-value: 8.49e-46
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6679731   350 EYFIAAEEVIWNYAP----VIPANM--DKIYRSQHLDNFSNQIGKHYKKVIYRQYEEETFTKRTDNPsiKQSGILGPVIR 423
Cdd:cd04222    2 EYYIGIRETQWDYAPsgknLITNQTfdDDEHASVFLKRGPDRIGRVYKKAVYLQYTDDTYRTEIEKP--VWLGFLGPILK 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6679731   424 AQVRDTLKIVFKNMASRPYSIYPHGVTF------SPYEDGINSSSTSGSHttirpVQPGETFTYKWNILEFDEPTENDAQ 497
Cdd:cd04222   80 AEVGDVIVVHLKNFASRPYSLHPHGVFYnkenegALYPDNTSGFEKADDA-----VPPGGSYTYTWTVPEEQAPTKADAN 154

                        170       180
                 ....*....|....*....|....*...
gi 6679731   498 CLTRPYYSDVDVTRDIASGLIGLLLICK 525
Cdd:cd04222  155 CLTRIYHSHIDAPKDIASGLIGPLIICK 182
CuRO_5_FV_like cd14451
The fifth cupredoxin domain of coagulation factor V and similar proteins; Factor V is an ...
 32-195 1.31e-44

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: 160.01  E-value: 1.31e-44
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6679731    32 RQFYVAAQGILWNYHP----EPTDPSLNSIPSFKKIVYREY-EQYFKKEKPR---SSNSGLLGPTLYAEVGDVIKVHFRN 103
Cdd:cd14451    2 RRYYIAAEEEEWDYAGygksRLDKTQNERDTVFKKVVFRRYlDSTFSTPDIQgeyEEHLGILGPVIRAEVDDVIQVFFKN 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6679731   104 KADKPLSIHPQGIKYSKFSEGASYADHTFPAERKDDAVAPGEEYTYEWIVSEDSGPTPDDPPCLTHIYYSYENLTQDFNS 183
Cdd:cd14451   82 LASRPYSLHAHGLSYEKSSEGLSYDDESPDWFKKDDAVQPNGTYTYVWYANPRSGPENNGSDCRTWAYYSAVNPEKDIHS 161

                        170
                 ....*....|..
gi 6679731   184 GLIGPLLICKKG 195
Cdd:cd14451  162 GLIGPLLICRKG 173
CuRO_1_Ceruloplasmin_like_1 cd04229
cupredoxin domain of ceruloplasmin homologs; Uncharacterized subfamily of ceruloplasmin ...
 1542-1714 4.98e-44

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: 158.35  E-value: 4.98e-44
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6679731  1542 YYIAAEEITWNYA----------EFAQSEMDHEDTGHTPKDTTYKKVVFRKYLDSTFTSRDPRaeyEEHLGILGPVIRAE 1611
Cdd:cd04229    3 YYIAAEEVDWDYApsgknkcclgDDLEVSTLDSQPGPYTIGSTYTKARYREYTDNSFSTPKPT---PAYLGILGPVIRAE 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6679731  1612 VDDVIQVRFKN-LASRPYSLHAHGLSYEKSSEGKTYEdespewfqEDDAVQPNSSYTYVWHATKRSGPENPGSACRAWAY 1690
Cdd:cd04229   80 VGDTIKVVFKNnLDEFPVNMHPHGGLYSKDNEGTTDG--------AGDVVAPGETYTYRWIVPEDAGPGPGDPSSRLWLY 151

                        170       180
                 ....*....|....*....|....
gi 6679731  1691 YSAVNVERDIHSGLIGPLLICRKG 1714
Cdd:cd04229  152 HSHVDVFAHTNAGLVGPIIVTSKG 175
CuRO_5_FV_like cd14451
The fifth cupredoxin domain of coagulation factor V and similar proteins; Factor V is an ...
 351-526 5.19e-43

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


Pssm-ID: 259993 [Multi-domain]  Cd Length: 173  Bit Score: 155.38  E-value: 5.19e-43
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6679731   351 YFIAAEEVIWNYAPVIPANMDKIYRSQHldnfsnqigKHYKKVIYRQYEEETFTKRTDNPSIKQS-GILGPVIRAQVRDT 429
Cdd:cd14451    4 YYIAAEEEEWDYAGYGKSRLDKTQNERD---------TVFKKVVFRRYLDSTFSTPDIQGEYEEHlGILGPVIRAEVDDV 74

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6679731   430 LKIVFKNMASRPYSIYPHGVTF------SPYEDGINSSSTSGSHttirpVQPGETFTYKWNILEFDEPTENDAQCLTRPY 503
Cdd:cd14451   75 IQVFFKNLASRPYSLHAHGLSYekssegLSYDDESPDWFKKDDA-----VQPNGTYTYVWYANPRSGPENNGSDCRTWAY 149

                        170       180
                 ....*....|....*....|...
gi 6679731   504 YSDVDVTRDIASGLIGLLLICKS 526
Cdd:cd14451  150 YSAVNPEKDIHSGLIGPLLICRK 172
CuRO_3_FV_like cd14450
The third cupredoxin domain of coagulation factor V and similar proteins; Factor V is an ...
 33-193 1.60e-42

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


Pssm-ID: 259992 [Multi-domain]  Cd Length: 181  Bit Score: 154.26  E-value: 1.60e-42
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6679731    33 QFYVAAQGILWNYHP---EPTDPSLNSI----------PSFKKIVYREYE-QYFKK--EKPRSSNSGLLGPTLYAEVGDV 96
Cdd:cd14450    4 EYFIAAEEVIWDYAPsipENMDKRYRSQyldnfsnnigKKYKKAVFTQYEdGSFTKrlENPRPKEEGILGPVIRAQVRDT 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6679731    97 IKVHFRNKADKPLSIHPQGIKYSKFSEGASYADHTFPAERKDDAVAPGEEYTYEWIVSEDSGPTPDDPPCLTHIYYSYEN 176
Cdd:cd14450   84 IKIVFKNKASRPYSIYPHGVTVSKAAEGASYPPDPRGNETQNKAVQPGETYTYKWNILETDEPTARDPRCLTRMYHSAVD 163

                        170
                 ....*....|....*..
gi 6679731   177 LTQDFNSGLIGPLLICK 193
Cdd:cd14450  164 ITRDIASGLIGPLLICK 180
CuRO_1_FV_like cd04226
The first cupredoxin domain of coagulation factor VIII and similar proteins; Factor V is an ...
 350-525 3.15e-42

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


Pssm-ID: 259888 [Multi-domain]  Cd Length: 165  Bit Score: 152.71  E-value: 3.15e-42
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6679731   350 EYFIAAEEVIWNYAPvipanmdkiyRSQHLDnfSNQIGKHYKKVIYRQYEEEtFTKrtDNPSIKQSGILGPVIRAQVRDT 429
Cdd:cd04226    2 EYYIAAQNIDWDYTP----------QSEELR--LKRSEQSFKKIVYREYEEG-FKK--EKPADLSSGLLGPTLRAEVGDT 66

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6679731   430 LKIVFKNMASRPYSIYPHGVTFSPYEDGINSSSTSGSHTTIR-PVQPGETFTYKWNILEFDEPTENDAQCLTRPYYSDVD 508
Cdd:cd04226   67 LIVHFKNMADKPLSIHPQGIAYGKKSEGSLYSDNTSPVEKLDdAVQPGQEYTYVWDITEEVGPTEADPPCLTYIYYSHVN 146

                        170
                 ....*....|....*..
gi 6679731   509 VTRDIASGLIGLLLICK 525
Cdd:cd04226  147 MVRDFNSGLIGALLICK 163
CuRO_1_Ceruloplasmin_like_1 cd04229
cupredoxin domain of ceruloplasmin homologs; Uncharacterized subfamily of ceruloplasmin ...
 32-195 3.28e-40

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: 147.56  E-value: 3.28e-40
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6679731    32 RQFYVAAQGILWNYHP----------------EPTDPSLNSIPS-FKKIVYREY-EQYFKKEKPRSSNSGLLGPTLYAEV 93
Cdd:cd04229    1 RTYYIAAEEVDWDYAPsgknkcclgddlevstLDSQPGPYTIGStYTKARYREYtDNSFSTPKPTPAYLGILGPVIRAEV 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6679731    94 GDVIKVHFRNKADK-PLSIHPQGIKYSKFSEGAsyadhtfpAERKDDAVAPGEEYTYEWIVSEDSGPTPDDPPCLTHIYY 172
Cdd:cd04229   81 GDTIKVVFKNNLDEfPVNMHPHGGLYSKDNEGT--------TDGAGDVVAPGETYTYRWIVPEDAGPGPGDPSSRLWLYH 152

                        170       180
                 ....*....|....*....|...
gi 6679731   173 SYENLTQDFNSGLIGPLLICKKG 195
Cdd:cd04229  153 SHVDVFAHTNAGLVGPIIVTSKG 175
CuRO_4_FVIII_like cd11016
The fourth cupredoxin domain of coagulation factor VIII and similar proteins; Factor VIII ...
 545-682 2.36e-39

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: 143.86  E-value: 2.36e-39
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6679731   545 VFAVFDENKSWYIEDNINKFCENPDEVKRDDPKFYESNIMSTINGYVPESISTLgFCFDDTVQWHFCSVGTHDDILTIHF 624
Cdd:cd11016    7 LFSVFDENNSWYLKENIHRFTQTPAGVNDTDPDFYASNVMHTINGIVFDRRQFV-ICLTDVAYWYVLSVGAQTDFLSVFF 85

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 6679731   625 TGHSFIYGRRHEDTLTLFPMRGESVTVTMDNVGTWMLTTMNSNPKRRNLRLRFRDVKC 682
Cdd:cd11016   86 SGNTFKHQMVYEDVLTLFPFSGETVSMSPEVPGEWELGCFNGDFRSRGMSAQYTVSTC 143
CuRO_5_FVIII_like cd04228
The fifth cupredoxin domain of coagulation factor VIII and similar proteins; Factor VIII ...
 350-525 1.99e-38

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: 141.95  E-value: 1.99e-38
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6679731   350 EYFIAAEEVIWNYApvipanmdkIYRSQHL---DNFSNQIGKH---YKKVIYRQYEEETFTKRTDNPSIKQS-GILGPVI 422
Cdd:cd04228    3 HYFIAAVEVLWDYG---------MQRPQHFlraRDPNRGRRKSvpqYKKVVFREYLDGSFTQPVYRGELDEHlGILGPYI 73

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6679731   423 RAQVRDTLKIVFKNMASRPYSIYPHGVTFSpyEDGINSSSTsgshttiRPVQPGETFTYKWNILEFDEPTENDAQCLTRP 502
Cdd:cd04228   74 RAEVEDNIMVTFKNLASRPYSFHSSLISYE--EDQRAEPRG-------NFVQPGEVQTYSWKVLHQMAPTKQEFDCKAWA 144

                        170       180
                 ....*....|....*....|...
gi 6679731   503 YYSDVDVTRDIASGLIGLLLICK 525
Cdd:cd04228  145 YFSNVDLEKDLHSGLIGPLIICK 167
CuRO_6_FVIII_like cd11018
The sixth cupredoxin domain of coagulation factor VIII and similar proteins; Factor VIII ...
 1726-1861 1.18e-37

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


Pssm-ID: 259904 [Multi-domain]  Cd Length: 144  Bit Score: 138.86  E-value: 1.18e-37
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6679731  1726 MREFVLLFMVFDEKKSWYYEKSKgsRR---------IESPEEKNAHKFYAINGMIYN-LPGLRMYEQEWVRLHLLNMGGS 1795
Cdd:cd11018    1 VQEFALLFTIFDETKSWYFEENM--RRncrppchiqTQDPWFHINNKFHAINGYVADtLPGLVMAQHQRIRWHLLNMGSD 78

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 6679731  1796 RDIHVVHFHGQTLLDNRTKQHQLGVWPLLPGSFKTLEMKASKPGWWLLDTEVGENQVAGMQTPFLI 1861
Cdd:cd11018   79 EEIHSVHFHGLPFTVRAKKEYRMGVYNLYPGVFGTVEMRPSTAGIWLVECTVGEHLLAGMSALFLV 144
CuRO_3_FVIII_like cd04227
The third cupredoxin domain of coagulation factor VIII and similar proteins; Factor VIII ...
 1542-1713 1.04e-36

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: 137.37  E-value: 1.04e-36
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6679731  1542 YYIAAEEITWNYAEFAQSEMDHE------DTGHTPKDTTYKKVVFRKYLDSTFTSRDPRaeyEEHLGILGPVIRAEVDDV 1615
Cdd:cd04227    5 HYIAAEELDWDYAPLLSSTDDRElqsrylPTGPQRIGYKYKKVAFVEYTDKTFKRREAK---QTEKGILGPLLKGEVGDQ 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6679731  1616 IQVRFKNLASRPYSLHAHGLS----YEKSSEGKTYEDespewfQEDDAVQPNSSYTYVWHATKRSGPENPGSACRAWAYY 1691
Cdd:cd04227   82 IHIMFKNTASRPYNIYPHGLTsvrpMYRSRNPAGEKD------LKTMPIGPGETFGYMWELTAEDGPTEEDPRCLTRLYQ 155

                        170       180
                 ....*....|....*....|..
gi 6679731  1692 SAVNVERDIHSGLIGPLLICRK 1713
Cdd:cd04227  156 STVDPERDLASGLIGPLLICKK 177
CuRO_5_ceruloplasmin cd04225
The fifth cupredoxin domain of Ceruloplasmin; Ceruloplasmin is a multicopper oxidase essential ...
 32-194 2.03e-36

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: 136.44  E-value: 2.03e-36
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6679731    32 RQFYVAAQGILWNYHPE--------------PTDPSLNS----IPS-FKKIVYREY-EQYFKKEKPRSSNS---GLLGPT 88
Cdd:cd04225    1 RTYYIAAEEVEWDYSPQrtweqelhntheesPGNAFLNKgdkfIGSkYKKVVYREYtDDTFSVPKERTAEEehlGILGPL 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6679731    89 LYAEVGDVIKVHFRNKADKPLSIHPQGIKyskfsegasyADHTFPAerkddAVAPGEEYTYEWIVSEDSGPTPDDPPCLT 168
Cdd:cd04225   81 IHAEVGEKVKIVFKNMASRPYSIHAHGVK----------TDSSWVA-----PTEPGETQTYTWKIPERSGPGVEDSNCIS 145

                        170       180
                 ....*....|....*....|....*.
gi 6679731   169 HIYYSYENLTQDFNSGLIGPLLICKK 194
Cdd:cd04225  146 WAYYSTVDQIKDLYSGLIGPLVICRR 171
CuRO_3_FVIII_like cd04227
The third cupredoxin domain of coagulation factor VIII and similar proteins; Factor VIII ...
 34-194 3.91e-35

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: 133.13  E-value: 3.91e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6679731    34 FYVAAQGILWNYHP---EPTDPSLNSI-----PS-----FKKIVYREYE-QYFKKEKPRSSNSGLLGPTLYAEVGDVIKV 99
Cdd:cd04227    5 HYIAAEELDWDYAPllsSTDDRELQSRylptgPQrigykYKKVAFVEYTdKTFKRREAKQTEKGILGPLLKGEVGDQIHI 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6679731   100 HFRNKADKPLSIHPQGI------KYSKFSEGASyadhtfpaERKDDAVAPGEEYTYEWIVSEDSGPTPDDPPCLTHIYYS 173
Cdd:cd04227   85 MFKNTASRPYNIYPHGLtsvrpmYRSRNPAGEK--------DLKTMPIGPGETFGYMWELTAEDGPTEEDPRCLTRLYQS 156

                        170       180
                 ....*....|....*....|.
gi 6679731   174 YENLTQDFNSGLIGPLLICKK 194
Cdd:cd04227  157 TVDPERDLASGLIGPLLICKK 177
CuRO_1_Ceruloplasmin_like_1 cd04229
cupredoxin domain of ceruloplasmin homologs; Uncharacterized subfamily of ceruloplasmin ...
 350-523 5.51e-35

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: 132.54  E-value: 5.51e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6679731   350 EYFIAAEEVIWNYAPvipANMDKIYRSQHLDNFS-------NQIGKHYKKVIYRQYEEETFTKRTDNPsiKQSGILGPVI 422
Cdd:cd04229    2 TYYIAAEEVDWDYAP---SGKNKCCLGDDLEVSTldsqpgpYTIGSTYTKARYREYTDNSFSTPKPTP--AYLGILGPVI 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6679731   423 RAQVRDTLKIVFKN-MASRPYSIYPHGVTFSPYEDGINssstsgsHTTIRPVQPGETFTYKWNILEFDEPTENDAQCLTR 501
Cdd:cd04229   77 RAEVGDTIKVVFKNnLDEFPVNMHPHGGLYSKDNEGTT-------DGAGDVVAPGETYTYRWIVPEDAGPGPGDPSSRLW 149

                        170       180
                 ....*....|....*....|..
gi 6679731   502 PYYSDVDVTRDIASGLIGLLLI 523
Cdd:cd04229  150 LYHSHVDVFAHTNAGLVGPIIV 171
CuRO_1_FVIII_like cd14452
The first cupredoxin domain of coagulation factor VIII and similar proteins; Factor VIII ...
 350-525 6.79e-35

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


Pssm-ID: 259994 [Multi-domain]  Cd Length: 173  Bit Score: 132.02  E-value: 6.79e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6679731   350 EYFIAAEEVIWNYAPVipanmDKIYRSQHLDNFSNQIGKHYKKVIYRQYEEETFTKRTDNPSikQSGILGPVIRAQVRDT 429
Cdd:cd14452    2 RYYIAAVEIGWDYIHS-----DLGDPASEQRKKPKDIPQKYIKAVFVEYLDATFTVPKPRPA--WMGLLGPTIVAEVGDT 74

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6679731   430 LKIVFKNMASRPYSIYPHGVTF------SPYEDGINSSSTSGSHttirpVQPGETFTYKWNILEFDEPTENDAQCLTRPY 503
Cdd:cd14452   75 VVITFKNLASQPYSLHAVGVSYwkasegAGYDDSTSQHEKEDDA-----VYPGGYHTYVWDISPKDGPTGSDPECLTYSY 149

                        170       180
                 ....*....|....*....|..
gi 6679731   504 YSDVDVTRDIASGLIGLLLICK 525
Cdd:cd14452  150 SSQVDPVKDVNSGLIGALLVCR 171
FA58C smart00231
Coagulation factor 5/8 C-terminal domain, discoidin domain; Cell surface-attached ...
 1865-2020 2.47e-34

Coagulation factor 5/8 C-terminal domain, discoidin domain; Cell surface-attached carbohydrate-binding domain, present in eukaryotes and assumed to have horizontally transferred to eubacterial genomes.


Pssm-ID: 214572  Cd Length: 139  Bit Score: 129.17  E-value: 2.47e-34
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6679731     1865 ECKMPMGLStgviSDSQIKASEylTYWEPRLARLNnAGSYNAWSIEKTALdfpiKPWIQVDMQKEVVVTGIQTQGAKHYL 1944
Cdd:smart00231    1 PCNEPLGLE----SDSQITASS--SYWAAKIARLN-GGSDGGWCPAKNDL----PPWIQVDLGRLRTVTGVITGRRHGNG 69

                            90       100       110       120       130       140       150
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 6679731     1945 KscFTTEFQVaYSSDQTNWQIFRGKSGksvMYFTGNSDGSTIKENRLDPPIVARYIRIHPTKSYNRPTLRLELQGC 2020
Cdd:smart00231   70 D--WVTYKLE-YSDDGVNWTTYKDGNS---KVFPGNSDAGTVVLNDFPPPIVARYVRILPTGWNGNIILRVELLGC 139
FA58C smart00231
Coagulation factor 5/8 C-terminal domain, discoidin domain; Cell surface-attached ...
 2024-2180 9.15e-34

Coagulation factor 5/8 C-terminal domain, discoidin domain; Cell surface-attached carbohydrate-binding domain, present in eukaryotes and assumed to have horizontally transferred to eubacterial genomes.


Pssm-ID: 214572  Cd Length: 139  Bit Score: 127.63  E-value: 9.15e-34
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6679731     2024 GCSTPLGLEDgriqDKQITASSfkkswwgDYWEPSLARLNaQGRVNAWQAKANNNKQWLQVDLLKIKKVTAIVTQGCKSL 2103
Cdd:smart00231    1 PCNEPLGLES----DSQITASS-------SYWAAKIARLN-GGSDGGWCPAKNDLPPWIQVDLGRLRTVTGVITGRRHGN 68

                            90       100       110       120       130       140       150
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 6679731     2104 SSEMYVKsysIQYSDQGVAWKPYRQKSSMVdkiFEGNSNTKGHMKNFFNPPIISRFIRIIPKTWNQSIALRLELFGC 2180
Cdd:smart00231   69 GDWVTYK---LEYSDDGVNWTTYKDGNSKV---FPGNSDAGTVVLNDFPPPIVARYVRILPTGWNGNIILRVELLGC 139
F5_F8_type_C pfam00754
F5/8 type C domain; This domain is also known as the discoidin (DS) domain family.
 2040-2177 5.94e-33

F5/8 type C domain; This domain is also known as the discoidin (DS) domain family.


Pssm-ID: 459925 [Multi-domain]  Cd Length: 127  Bit Score: 124.87  E-value: 5.94e-33
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6679731    2040 QITASSfkkSWWGDYwePSLARLNaqGRVN-AWQAKANNNKQWLQVDLLKIKKVTAIVTQGCKSLSSeMYVKSYSIQYSD 2118
Cdd:pfam00754    1 QITASS---SYSGEG--PAAAALD--GDPNtAWSAWSGDDPQWIQVDLGKPKKITGVVTQGRQDGSN-GYVTSYKIEYSL 72

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 6679731    2119 QGVAWKPYRqkssmvDKIFEGNSNTKGHMKNFFNPPIISRFIRIIPKTWN--QSIALRLEL 2177
Cdd:pfam00754   73 DGENWTTVK------DEKIPGNNDNNTPVTNTFDPPIKARYVRIVPTSWNggNGIALRAEL 127
CuRO_5_FVIII_like cd04228
The fifth cupredoxin domain of coagulation factor VIII and similar proteins; Factor VIII ...
 32-195 2.67e-31

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


Pssm-ID: 259890 [Multi-domain]  Cd Length: 169  Bit Score: 121.53  E-value: 2.67e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6679731    32 RQFYVAAQGILWNY---HPE----PTDPSL---NSIPSFKKIVYREY-EQYFKKEKPR---SSNSGLLGPTLYAEVGDVI 97
Cdd:cd04228    2 RHYFIAAVEVLWDYgmqRPQhflrARDPNRgrrKSVPQYKKVVFREYlDGSFTQPVYRgelDEHLGILGPYIRAEVEDNI 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6679731    98 KVHFRNKADKPLSIHPQGIKYskfsegasyaDHTFPAERKDDAVAPGEEYTYEWIVSEDSGPTPDDPPCLTHIYYSYENL 177
Cdd:cd04228   82 MVTFKNLASRPYSFHSSLISY----------EEDQRAEPRGNFVQPGEVQTYSWKVLHQMAPTKQEFDCKAWAYFSNVDL 151

                        170
                 ....*....|....*...
gi 6679731   178 TQDFNSGLIGPLLICKKG 195
Cdd:cd04228  152 EKDLHSGLIGPLIICKTG 169
CuRO_2_ceruloplasmin cd11021
The second cupredoxin domain of Ceruloplasmin; Ceruloplasmin is a multicopper oxidase ...
 546-667 4.66e-31

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: 119.88  E-value: 4.66e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6679731   546 FAVFDENKSWYIEDNINKFCENPDEVKRDDPKFYESNIMSTINGYVPESISTLGFCFDDTVQWHFCSVGTHDDILTIHFT 625
Cdd:cd11021    8 FSVVDENLSWYLDENIKTYCSEPAKVDKDDEDFQESNKMHSINGYTFGNLPGLSMCAGDRVKWHLFGMGNEVDIHSAFFH 87

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|..
gi 6679731   626 GHSFIYGRRHEDTLTLFPMRGESVTVTMDNVGTWMLTTMNSN 667
Cdd:cd11021   88 GQTLTDRGHRTDTINLFPATFVTAEMVAQNPGKWLLSCQVND 129
CuRO_4_ceruloplasmin cd11022
The fourth cupredoxin domain of Ceruloplasmin; Ceruloplasmin is a multicopper oxidase ...
 546-682 2.81e-30

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: 117.97  E-value: 2.81e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6679731   546 FAVFDENKSWYIEDNINKFCENPDEVKRDDPKFYESNIMSTINGYVPESISTLGFCFDDTVQWHFCSVGTHDDILTIHFT 625
Cdd:cd11022    8 FTVFDENESWYLDENIQQFTLDPRSVDKEDEDFQESNKMHSINGYMYGNQPGLDMCKGDTVSWHLFGLGTETDVHGIYFS 87

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 6679731   626 GHSFIYGRRHEDTLTLFPMrgESVTVTM--DNVGTWMLTTMNSNPKRRNLRLRFRDVKC 682
Cdd:cd11022   88 GNTFLLQGTRRDTANLFPH--TSVTAIMqpDNEGTFEVNCQTTDHYSAGMRQIYTVSQC 144
CuRO_6_ceruloplasmin cd11012
The sixth cupredoxin domain of Ceruloplasmin; Ceruloplasmin is a multicopper oxidase essential ...
 1728-1862 2.93e-27

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: 109.19  E-value: 2.93e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6679731  1728 EFVLLFMVFDEKKSWYYEK-----SKGSRRIESPEEK--NAHKFYAINGMIY-NLPGLRMYEQEWVRLHLLNMGGSRDIH 1799
Cdd:cd11012    3 EFALLFLVFDENESWYLDEniktySDHPEKVNKEDEEfiESNKMHAINGKVFgNLQGLTMHVGDEVYWYLMGMGNEIDIH 82

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 6679731  1800 VVHFHGQTLLDNRTKQHQLGVWPLLPGSFKTLEMKASKPGWWLLDTEVGENQVAGMQTPFLII 1862
Cdd:cd11012   83 TAHFHGHSFDYKHRGVYRSDVFDLFPGTFQTVEMIPRTPGTWLLHCHVTDHIHAGMETTYTVL 145
CuRO_2_ceruloplasmin cd11021
The second cupredoxin domain of Ceruloplasmin; Ceruloplasmin is a multicopper oxidase ...
 1727-1859 9.87e-27

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: 107.56  E-value: 9.87e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6679731  1727 REFVLLFMVFDEKKSWY---------YEKSKGSRRIESPEEKNahKFYAINGMIY-NLPGLRMYEQEWVRLHLLNMGGSR 1796
Cdd:cd11021    2 REFVLMFSVVDENLSWYldeniktycSEPAKVDKDDEDFQESN--KMHSINGYTFgNLPGLSMCAGDRVKWHLFGMGNEV 79

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 6679731  1797 DIHVVHFHGQTLLDnrtKQHQLGVWPLLPGSFKTLEMKASKPGWWLLDTEVGENQVAGMQTPF 1859
Cdd:cd11021   80 DIHSAFFHGQTLTD---RGHRTDTINLFPATFVTAEMVAQNPGKWLLSCQVNDHLKAGMQAFY 139
CuRO_6_ceruloplasmin cd11012
The sixth cupredoxin domain of Ceruloplasmin; Ceruloplasmin is a multicopper oxidase essential ...
 545-661 5.97e-26

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: 105.34  E-value: 5.97e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6679731   545 VFAVFDENKSWYIEDNINKFCENPDEVKRDDPKFYESNIMSTINGYVPESISTLGFCFDDTVQWHFCSVGTHDDILTIHF 624
Cdd:cd11012    7 LFLVFDENESWYLDENIKTYSDHPEKVNKEDEEFIESNKMHAINGKVFGNLQGLTMHVGDEVYWYLMGMGNEIDIHTAHF 86

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|
gi 6679731   625 TGHSFIYGRR---HEDTLTLFPMRGESVTVTMDNVGTWML 661
Cdd:cd11012   87 HGHSFDYKHRgvyRSDVFDLFPGTFQTVEMIPRTPGTWLL 126
F5_F8_type_C pfam00754
F5/8 type C domain; This domain is also known as the discoidin (DS) domain family.
 1881-2017 8.20e-26

F5/8 type C domain; This domain is also known as the discoidin (DS) domain family.


Pssm-ID: 459925 [Multi-domain]  Cd Length: 127  Bit Score: 104.45  E-value: 8.20e-26
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6679731    1881 QIKASEYLTYWEPRLARLNNAGSyNAWSiektALDFPIKPWIQVDMQKEVVVTGIQTQGAKHyLKSCFTTEFQVAYSSDQ 1960
Cdd:pfam00754    1 QITASSSYSGEGPAAAALDGDPN-TAWS----AWSGDDPQWIQVDLGKPKKITGVVTQGRQD-GSNGYVTSYKIEYSLDG 74

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 6679731    1961 TNWQIFRGKsgksvmYFTGNSDGSTIKENRLDPPIVARYIRIHPTK--SYNRPTLRLEL 2017
Cdd:pfam00754   75 ENWTTVKDE------KIPGNNDNNTPVTNTFDPPIKARYVRIVPTSwnGGNGIALRAEL 127
CuRO_2_FVIII_like cd11015
The second cupredoxin domain of coagulation factor VIII and similar proteins; Factor VIII ...
 208-325 1.25e-25

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


Pssm-ID: 259901 [Multi-domain]  Cd Length: 134  Bit Score: 104.22  E-value: 1.25e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6679731   208 KQHVLLFAVFDESKS---------------RSQSPSLMYTINGFVNKTMPDITVCAHDHVSWHLIGMSSGPELFSIHFNG 272
Cdd:cd11015    2 QAFVLLFAVFDEGKSwysevgerksrdkfkRADSRKEFHTINGYINASLPGLKICQRKPVIWHVIGMGTAPEVHSIFFEG 81

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|...
gi 6679731   273 QVLEQNQHKVSTVTLVSATSTTANMTMSPEGRWIVSSLIPKHYQAGMQAYIDI 325
Cdd:cd11015   82 HTFLVRTHRKVSLEISPMTFLTAQTKPATVGSFLIFCQIHSHQHDGMEAMVKV 134
CuRO_2_ceruloplasmin cd11021
The second cupredoxin domain of Ceruloplasmin; Ceruloplasmin is a multicopper oxidase ...
 207-325 1.11e-22

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: 96.00  E-value: 1.11e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6679731   207 DKQHVLLFAVFDESKS----------------------RSQSPSLMYTINGFVNKTMPDITVCAHDHVSWHLIGMSSGPE 264
Cdd:cd11021    1 DREFVLMFSVVDENLSwyldeniktycsepakvdkddeDFQESNKMHSINGYTFGNLPGLSMCAGDRVKWHLFGMGNEVD 80

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 6679731   265 LFSIHFNGQVLEQNQHKVSTVTLVSATSTTANMTMSPEGRWIVSSLIPKHYQAGMQAYIDI 325
Cdd:cd11021   81 IHSAFFHGQTLTDRGHRTDTINLFPATFVTAEMVAQNPGKWLLSCQVNDHLKAGMQAFYEV 141
CuRO_6_FVIII_like cd11018
The sixth cupredoxin domain of coagulation factor VIII and similar proteins; Factor VIII ...
 546-661 1.11e-21

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: 93.41  E-value: 1.11e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6679731   546 FAVFDENKSWYIEDNINKFCENPDEVKRDDPKFYESNIMSTINGYVPESISTLGFCFDDTVQWHFCSVGTHDDILTIHFT 625
Cdd:cd11018    8 FTIFDETKSWYFEENMRRNCRPPCHIQTQDPWFHINNKFHAINGYVADTLPGLVMAQHQRIRWHLLNMGSDEEIHSVHFH 87

                         90       100       110
                 ....*....|....*....|....*....|....*....
gi 6679731   626 GHSFIYGRRHEDTL---TLFPMRGESVTVTMDNVGTWML 661
Cdd:cd11018   88 GLPFTVRAKKEYRMgvyNLYPGVFGTVEMRPSTAGIWLV 126
CuRO_2_FVIII_like cd11015
The second cupredoxin domain of coagulation factor VIII and similar proteins; Factor VIII ...
 1727-1861 1.45e-21

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


Pssm-ID: 259901 [Multi-domain]  Cd Length: 134  Bit Score: 92.66  E-value: 1.45e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6679731  1727 REFVLLFMVFDEKKSWYYEKSKGSRRIESPEEKNAHKFYAINGMI-YNLPGLRMYEQEWVRLHLLNMGGSRDIHVVHFHG 1805
Cdd:cd11015    2 QAFVLLFAVFDEGKSWYSEVGERKSRDKFKRADSRKEFHTINGYInASLPGLKICQRKPVIWHVIGMGTAPEVHSIFFEG 81

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 6679731  1806 QTLLdnrTKQHQLGVWPLLPGSFKTLEMKASKPGWWLLDTEVGENQVAGMQTPFLI 1861
Cdd:cd11015   82 HTFL---VRTHRKVSLEISPMTFLTAQTKPATVGSFLIFCQIHSHQHDGMEAMVKV 134
CuRO_2_ceruloplasmin_like_2 cd11023
cupredoxin domain of ceruloplasmin homologs; Uncharacterized subfamily of ceruloplasmin ...
 1727-1861 1.99e-20

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


Pssm-ID: 259909 [Multi-domain]  Cd Length: 118  Bit Score: 88.82  E-value: 1.99e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6679731  1727 REFVLLFMVFDEkkswyyekskgsrriESPEEknAHKFYAINGMIY-NLPGLRMYEQEWVRLHLLNMGGSRDIHVVHFHG 1805
Cdd:cd11023    2 QEFIENSSIFLD---------------LNVEE--AGLMHSINGYVFgNLPGVTIAKGKRVRWHLVAYGNEVDFHTPHWHG 64

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 6679731  1806 QTLLDNRTKQHQlgVWPLLPGSFKTLEMKASKPGWWLLDTEVGENQVAGMQTPFLI 1861
Cdd:cd11023   65 QTVEADKSRRTD--VAELMPASMRVADMTAADVGTWLLHCHVHDHYMAGMMTQFAV 118
CuRO_2_FV_like cd14453
The second cupredoxin domain of coagulation factor V and similar proteins; Factor V is an ...
 1727-1856 1.43e-18

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


Pssm-ID: 259995 [Multi-domain]  Cd Length: 123  Bit Score: 83.75  E-value: 1.43e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6679731  1727 REFVLLFMVFDEKKSWYyekskgsrrieSPEEKNAHKFYAINGMIY-NLPGLRMYEQEWVRLHLLNMGGSRDIHVVHFHG 1805
Cdd:cd14453    2 KEYVLMFGVFDENKSWY-----------KQNASVDSVKYTINGYTNgTLPDVSICAYDHVSWHLLGMSSEPELFSVHFNG 70

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|.
gi 6679731  1806 QTLLDNrtkQHQLGVWPLLPGSFKTLEMKASKPGWWLLDTEVGENQVAGMQ 1856
Cdd:cd14453   71 QVLEQN---GHKVSAVGLVSGSSTTASMTVVHTGRWLISSLIMKHLQAGMY 118
CuRO_4_ceruloplasmin cd11022
The fourth cupredoxin domain of Ceruloplasmin; Ceruloplasmin is a multicopper oxidase ...
 207-328 4.33e-17

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: 80.22  E-value: 4.33e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6679731   207 DKQHVLLFAVFDESKSRS----------------------QSPSLMYTINGFVNKTMPDITVCAHDHVSWHLIGMSSGPE 264
Cdd:cd11022    1 DKEFFLLFTVFDENESWYldeniqqftldprsvdkededfQESNKMHSINGYMYGNQPGLDMCKGDTVSWHLFGLGTETD 80

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 6679731   265 LFSIHFNGQVLEQNQHKVSTVTLVSATSTTANMTMSPEGRWIVSSLIPKHYQAGMQAYIDIKNC 328
Cdd:cd11022   81 VHGIYFSGNTFLLQGTRRDTANLFPHTSVTAIMQPDNEGTFEVNCQTTDHYSAGMRQIYTVSQC 144
CuRO_4_ceruloplasmin cd11022
The fourth cupredoxin domain of Ceruloplasmin; Ceruloplasmin is a multicopper oxidase ...
 1727-1855 3.47e-16

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: 77.52  E-value: 3.47e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6679731  1727 REFVLLFMVFDEKKSWY-------YEKSKGSRRIESPEEKNAHKFYAINGMIY-NLPGLRMYEQEWVRLHLLNMGGSRDI 1798
Cdd:cd11022    2 KEFFLLFTVFDENESWYldeniqqFTLDPRSVDKEDEDFQESNKMHSINGYMYgNQPGLDMCKGDTVSWHLFGLGTETDV 81

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 6679731  1799 HVVHFHGQTLLDNRTKQHQLGvwpLLPGSFKTLEMKASKPGWWLLDTEVGENQVAGM 1855
Cdd:cd11022   82 HGIYFSGNTFLLQGTRRDTAN---LFPHTSVTAIMQPDNEGTFEVNCQTTDHYSAGM 135
CuRO_6_FVIII_like cd11018
The sixth cupredoxin domain of coagulation factor VIII and similar proteins; Factor VIII ...
 212-321 1.20e-14

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: 72.99  E-value: 1.20e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6679731   212 LLFAVFDESKS-----------------RSQSPSL-----MYTINGFVNKTMPDITVCAHDHVSWHLIGMSSGPELFSIH 269
Cdd:cd11018    6 LLFTIFDETKSwyfeenmrrncrppchiQTQDPWFhinnkFHAINGYVADTLPGLVMAQHQRIRWHLLNMGSDEEIHSVH 85

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 6679731   270 FNGQVL---EQNQHKVSTVTLVSATSTTANMTMSPEGRWIVSSLIPKHYQAGMQA 321
Cdd:cd11018   86 FHGLPFtvrAKKEYRMGVYNLYPGVFGTVEMRPSTAGIWLVECTVGEHLLAGMSA 140
CuRO_1_LCC_like cd04206
Cupredoxin domain 1 of laccase-like multicopper oxidases; including laccase, CueO, spore coat ...
 1591-1711 1.07e-13

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


Pssm-ID: 259869 [Multi-domain]  Cd Length: 120  Bit Score: 69.62  E-value: 1.07e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6679731  1591 RDPRAEYEEHLGILGPVIRAEVDDVIQVRFKN-LASRPYSLHAHGLSYEKSSEGktyedeSPEWFQEDDAVQPNSSYTYV 1669
Cdd:cd04206   16 GVLRQVITVNGQFPGPTIRVKEGDTVEVTVTNnLPNEPTSIHWHGLRQPGTNDG------DGVAGLTQCPIPPGESFTYR 89

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|..
gi 6679731  1670 WHATKRSGpenpgsacrAWAYYSAVNVERDihSGLIGPLLIC 1711
Cdd:cd04206   90 FTVDDQAG---------TFWYHSHVGGQRA--DGLYGPLIVE 120
CuRO_1_LCC_like cd04206
Cupredoxin domain 1 of laccase-like multicopper oxidases; including laccase, CueO, spore coat ...
 81-192 2.46e-13

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


Pssm-ID: 259869 [Multi-domain]  Cd Length: 120  Bit Score: 68.47  E-value: 2.46e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6679731    81 NSGLLGPTLYAEVGDVIKVHFRNKAD-KPLSIHPQGIkyskFSEGASYADhtFPAERKDDAVAPGEEYTYEWIVSEDSGp 159
Cdd:cd04206   25 NGQFPGPTIRVKEGDTVEVTVTNNLPnEPTSIHWHGL----RQPGTNDGD--GVAGLTQCPIPPGESFTYRFTVDDQAG- 97

                         90       100       110
                 ....*....|....*....|....*....|...
gi 6679731   160 tpddppclTHIYYSYENLtqDFNSGLIGPLLIC 192
Cdd:cd04206   98 --------TFWYHSHVGG--QRADGLYGPLIVE 120
CuRO_6_FV_like cd14455
The sixth cupredoxin domain of coagulation factor V and similar proteins; Factor V is an ...
 546-677 3.65e-13

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: 68.74  E-value: 3.65e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6679731   546 FAVFDENKSWYIEDNINKFCEnpdEVKRDDPKFYESNIMSTINGyVPESISTLGFCFDDTVQWHFCSVGTHDDILTIHFT 625
Cdd:cd14455    8 FMTFDEEKSWYYEKNRKRTCR---ENRVKDPNVQDNHTFHAING-IIYNLKGLRMYTNELVRWHLINMGGPKDLHVVHFH 83

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 6679731   626 GHSFIYGRRHEDTLTLFP-MRGESVTVTM--DNVGTWMLTTMNSNPKRRNLRLRF 677
Cdd:cd14455   84 GQTFTEKGLKDHQLGVYPlLPGSFATLEMkpSKPGLWLLETEVGESQQRGMQTLF 138
CuRO_2_ceruloplasmin_like_2 cd11023
cupredoxin domain of ceruloplasmin homologs; Uncharacterized subfamily of ceruloplasmin ...
 207-319 5.30e-13

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: 67.63  E-value: 5.30e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6679731   207 DKQHVLLFAVFDESKSrsQSPSLMYTINGFVNKTMPDITVCAHDHVSWHLIGMSSGPELFSIHFNGQVLEQNQHKVSTV- 285
Cdd:cd11023    1 DQEFIENSSIFLDLNV--EEAGLMHSINGYVFGNLPGVTIAKGKRVRWHLVAYGNEVDFHTPHWHGQTVEADKSRRTDVa 78

                         90       100       110
                 ....*....|....*....|....*....|....
gi 6679731   286 TLVSATSTTANMTMSPEGRWIVSSLIPKHYQAGM 319
Cdd:cd11023   79 ELMPASMRVADMTAADVGTWLLHCHVHDHYMAGM 112
CuRO_1_2DMCO_NIR_like cd11024
The cupredoxin domain 1 of a two-domain laccase related to nitrite reductase; The two-domain ...
 86-152 9.22e-13

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: 66.91  E-value: 9.22e-13
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 6679731    86 GPTLYAEVGDVIKVHFRNKADKPLSIHPQGIKYSKFsegasyaDHTFPAErkddaVAPGEEYTYEWI 152
Cdd:cd11024   32 GPTLRATEGDLVRIHFINTGDHPHTIHFHGIHDAAM-------DGTGLGP-----IMPGESFTYEFV 86
CuRO_2_FV_like cd14453
The second cupredoxin domain of coagulation factor V and similar proteins; Factor V is an ...
 541-664 1.08e-12

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: 66.81  E-value: 1.08e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6679731   541 EQQAV--FAVFDENKSWYiedninkfcenpdevkRDDPKfyESNIMSTINGYVPESISTLGFCFDDTVQWHFCSVGTHDD 618
Cdd:cd14453    1 YKEYVlmFGVFDENKSWY----------------KQNAS--VDSVKYTINGYTNGTLPDVSICAYDHVSWHLLGMSSEPE 62

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*...
gi 6679731   619 ILTIHFTGHSFIYGRRHEDTLTLfpMRGESVTVTMDNV--GTWMLTTM 664
Cdd:cd14453   63 LFSVHFNGQVLEQNGHKVSAVGL--VSGSSTTASMTVVhtGRWLISSL 108
CuRO_4_FVIII_like cd11016
The fourth cupredoxin domain of coagulation factor VIII and similar proteins; Factor VIII ...
 207-328 4.40e-12

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: 65.66  E-value: 4.40e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6679731   207 DKQHVLLFAVFDESKS----------------------RSQSPSLMYTINGFVNKTMpDITVCAHDHVSWHLIGMSSGPE 264
Cdd:cd11016    1 DKDWSLLFSVFDENNSwylkenihrftqtpagvndtdpDFYASNVMHTINGIVFDRR-QFVICLTDVAYWYVLSVGAQTD 79

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 6679731   265 LFSIHFNGQVLEQNQHKVSTVTLVSATSTTANMTMSPEGRWIVSSLIPKHYQAGMQAYIDIKNC 328
Cdd:cd11016   80 FLSVFFSGNTFKHQMVYEDVLTLFPFSGETVSMSPEVPGEWELGCFNGDFRSRGMSAQYTVSTC 143
CuRO_2_FVIII_like cd11015
The second cupredoxin domain of coagulation factor VIII and similar proteins; Factor VIII ...
 545-669 1.35e-11

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: 64.16  E-value: 1.35e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6679731   545 VFAVFDENKSWYIEDNINKfceNPDEVKRDD--PKFYesnimsTINGYVPESISTLGFCFDDTVQWHFCSVGTHDDILTI 622
Cdd:cd11015    7 LFAVFDEGKSWYSEVGERK---SRDKFKRADsrKEFH------TINGYINASLPGLKICQRKPVIWHVIGMGTAPEVHSI 77

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*..
gi 6679731   623 HFTGHSFIYGRRHEDTLTLFPMRGESVTVTMDNVGTWMLTTMNSNPK 669
Cdd:cd11015   78 FFEGHTFLVRTHRKVSLEISPMTFLTAQTKPATVGSFLIFCQIHSHQ 124
CuRO_1_LCC_like cd04206
Cupredoxin domain 1 of laccase-like multicopper oxidases; including laccase, CueO, spore coat ...
 416-524 8.71e-11

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


Pssm-ID: 259869 [Multi-domain]  Cd Length: 120  Bit Score: 61.15  E-value: 8.71e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6679731   416 GILGPVIRAQVRDTLKIVFKN-MASRPYSIYPHGVTF--SPYEDGINSSSTSgshttirPVQPGETFTYKWNIlefdept 492
Cdd:cd04206   27 QFPGPTIRVKEGDTVEVTVTNnLPNEPTSIHWHGLRQpgTNDGDGVAGLTQC-------PIPPGESFTYRFTV------- 92

                         90       100       110
                 ....*....|....*....|....*....|..
gi 6679731   493 enDAQCLTRPYYSDVDVtrDIASGLIGLLLIC 524
Cdd:cd04206   93 --DDQAGTFWYHSHVGG--QRADGLYGPLIVE 120
CuRO_6_FV_like cd14455
The sixth cupredoxin domain of coagulation factor V and similar proteins; Factor V is an ...
 208-321 1.01e-10

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: 61.80  E-value: 1.01e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6679731   208 KQHVLLFAVFDESKS-------------------RSQSPSLMYTINGFVnKTMPDITVCAHDHVSWHLIGMSSGPELFSI 268
Cdd:cd14455    2 REFVLLFMTFDEEKSwyyeknrkrtcrenrvkdpNVQDNHTFHAINGII-YNLKGLRMYTNELVRWHLINMGGPKDLHVV 80

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 6679731   269 HFNGQVLEQN---QHKVSTVTLVSATSTTANMTMSPEGRWIVSSLIPKHYQAGMQA 321
Cdd:cd14455   81 HFHGQTFTEKglkDHQLGVYPLLPGSFATLEMKPSKPGLWLLETEVGESQQRGMQT 136
CuRO_4_FV_like cd14454
The fourth cupredoxin domain of coagulation factor V and similar proteins; Factor V is an ...
 207-310 1.65e-10

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: 61.04  E-value: 1.65e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6679731   207 DKQHVLLFAVFDESKS-----------------RSQSPS-----LMYTINGFVNKTMPDITVCAHDHVSWHLIGMSSGPE 264
Cdd:cd14454    1 DLEQHAVFAVFDENKSwyleeninkycsnpnnvKKDDPKfyksnIMPTINGYAYESSAPLGFCHSEVVQWHISSVGTQDE 80

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*.
gi 6679731   265 LFSIHFNGQVLEQNQHKVSTVTLVSATSTTANMTMSPEGRWIVSSL 310
Cdd:cd14454   81 IITVHLSGHTFRYKGKHEDTLNLFPMSGESITVTMDNLGTWLLGSF 126
CuRO_1_Diphenol_Ox cd13857
The first cupredoxin domain of fungal laccase, diphenol oxidase; Diphenol oxidase belongs to ...
 86-191 2.26e-10

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


Pssm-ID: 259926 [Multi-domain]  Cd Length: 119  Bit Score: 59.96  E-value: 2.26e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6679731    86 GPTLYAEVGDVIKVHFRNKADKPLSIHPQGIkyskFSEGASYADHTfpAERKDDAVAPGEEYTYEWIVSEDSGptpddpp 165
Cdd:cd13857   30 GPLIEANQGDRIVVHVTNELDEPTSIHWHGL----FQNGTNWMDGT--AGITQCPIPPGGSFTYNFTVDGQYG------- 96

                         90       100
                 ....*....|....*....|....*..
gi 6679731   166 clTHIYYS-YENLTQDfnsGLIGPLLI 191
Cdd:cd13857   97 --TYWYHShYSTQYAD---GLVGPLIV 118
CuRO_1_CumA_like cd13861
The first cupredoxin domain of CumA like multicopper oxidase; This multicopper oxidase (MCO) ...
 81-191 2.33e-09

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


Pssm-ID: 259930 [Multi-domain]  Cd Length: 119  Bit Score: 57.24  E-value: 2.33e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6679731    81 NSGLLGPTLYAEVGDVIKVHFRNKADKPLSIHPQGIKYSKFSEGAsyADHTFPaerkddAVAPGEEYTYEWivsedsgpT 160
Cdd:cd13861   26 NGQVPGPELRVRQGDTLRVRLTNRLPEPTTIHWHGLRLPNAMDGV--PGLTQP------PVPPGESFTYEF--------T 89

                         90       100       110
                 ....*....|....*....|....*....|.
gi 6679731   161 PDDPPclTHIYYSYENLTQDFNSGLIGPLLI 191
Cdd:cd13861   90 PPDAG--TYWYHPHVGSQEQLDRGLYGPLIV 118
CuRO_1_2DMCO_NIR_like_2 cd14449
The cupredoxin domain 1 of a two-domain laccase related to nitrite reductase; The two-domain ...
 61-191 4.49e-09

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


Pssm-ID: 259991 [Multi-domain]  Cd Length: 135  Bit Score: 56.89  E-value: 4.49e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6679731    61 KKIVYREYEQYFKKEKPRssnsgLLGPTLYAEVGDVIKVHFRNKADKPLSIHPQGIKYSKFSEGASyadhtfpaeRKDDA 140
Cdd:cd14449    9 EKLTDDAWGYGLKGGVAT-----VPGPVIEVREGDTLKILFRNTLDVPASLHPHGVDYTTASDGTG---------MNASI 74

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 6679731   141 VAPGEEYTYEW----IVSEDSGPTPDDPPCLTHiYYSY----ENLTQDFNSGLIGPLLI 191
Cdd:cd14449   75 VAPGDTRIYTWrthgGYRRADGSWAEGTAGYWH-YHDHvfgtEHGTEGLSRGLYGALIV 132
CuRO_4_FVIII_like cd11016
The fourth cupredoxin domain of coagulation factor VIII and similar proteins; Factor VIII ...
 1730-1861 4.66e-09

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: 56.80  E-value: 4.66e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6679731  1730 VLLFMVFDEKKSWYYEK-------SKGSRRIESPEEKNAHKFYAINGMIYNLPGLRMYEQEWVRLHLLNMGGSRDIHVVH 1802
Cdd:cd11016    5 SLLFSVFDENNSWYLKEnihrftqTPAGVNDTDPDFYASNVMHTINGIVFDRRQFVICLTDVAYWYVLSVGAQTDFLSVF 84

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 6679731  1803 FHGQTLldnrtkQHQL---GVWPLLPGSFKTLEMKASKPGWWLLDTEVGENQVAGMQTPFLI 1861
Cdd:cd11016   85 FSGNTF------KHQMvyeDVLTLFPFSGETVSMSPEVPGEWELGCFNGDFRSRGMSAQYTV 140
Cu-oxidase_3 pfam07732
Multicopper oxidase; This entry contains many divergent copper oxidase-like domains that are ...
 81-191 6.35e-09

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


Pssm-ID: 462247 [Multi-domain]  Cd Length: 119  Bit Score: 55.71  E-value: 6.35e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6679731      81 NSGLLGPTLYAEVGDVIKVHFRNKADKPLSIHPQGIkyskFSEGASYAD----HTFpaerkdDAVAPGEEYTYEWIVSED 156
Cdd:pfam07732   21 NGQFPGPTIRVREGDTVVVNVTNNLDEPTSIHWHGL----QQRGTPWMDgvpgVTQ------CPIPPGQSFTYRFQVKQQ 90

                           90       100       110
                   ....*....|....*....|....*....|....*
gi 6679731     157 SGptpddppclTHIYYSYENLTQdfNSGLIGPLLI 191
Cdd:pfam07732   91 AG---------TYWYHSHTSGQQ--AAGLAGAIII 114
CuRO_1_2DMCO_NIR_like cd11024
The cupredoxin domain 1 of a two-domain laccase related to nitrite reductase; The two-domain ...
 419-523 8.19e-09

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


Pssm-ID: 259910 [Multi-domain]  Cd Length: 119  Bit Score: 55.35  E-value: 8.19e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6679731   419 GPVIRAQVRDTLKIVFKNMASRPYSIYPHGVtFSPYEDGINSsstsgshttiRPVQPGETFTYKWnilefdeptenDAQC 498
Cdd:cd11024   32 GPTLRATEGDLVRIHFINTGDHPHTIHFHGI-HDAAMDGTGL----------GPIMPGESFTYEF-----------VAEP 89

                         90       100
                 ....*....|....*....|....*..
gi 6679731   499 L-TRPYYSDV-DVTRDIASGLIGLLLI 523
Cdd:cd11024   90 AgTHLYHCHVqPLKEHIAMGLYGAFIV 116
CuRO_2_ceruloplasmin_like_2 cd11023
cupredoxin domain of ceruloplasmin homologs; Uncharacterized subfamily of ceruloplasmin ...
 580-661 1.45e-08

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: 54.92  E-value: 1.45e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6679731   580 ESNIMSTINGYVPESISTLGFCFDDTVQWHFCSVGTHDDILTIHFTGHSF-IYGRRHEDTLTLFPMRGESVTVTMDNVGT 658
Cdd:cd11023   18 EAGLMHSINGYVFGNLPGVTIAKGKRVRWHLVAYGNEVDFHTPHWHGQTVeADKSRRTDVAELMPASMRVADMTAADVGT 97


                 ...
gi 6679731   659 WML 661
Cdd:cd11023   98 WLL 100
CuRO_6_ceruloplasmin cd11012
The sixth cupredoxin domain of Ceruloplasmin; Ceruloplasmin is a multicopper oxidase essential ...
 208-321 2.62e-08

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: 54.87  E-value: 2.62e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6679731   208 KQHVLLFAVFDES---------KSRSQSPSL-------------MYTINGFVNKTMPDITVCAHDHVSWHLIGMSSGPEL 265
Cdd:cd11012    2 LEFALLFLVFDENeswyldeniKTYSDHPEKvnkedeefiesnkMHAINGKVFGNLQGLTMHVGDEVYWYLMGMGNEIDI 81

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 6679731   266 FSIHFNGQVLEQNQ---HKVSTVTLVSATSTTANMTMSPEGRWIVSSLIPKHYQAGMQA 321
Cdd:cd11012   82 HTAHFHGHSFDYKHrgvYRSDVFDLFPGTFQTVEMIPRTPGTWLLHCHVTDHIHAGMET 140
CuRO_1_2dMco_1 cd13860
The first cupredoxin domain of bacteria two domain multicopper oxidase; This subfamily ...
 419-523 5.94e-08

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


Pssm-ID: 259929 [Multi-domain]  Cd Length: 119  Bit Score: 52.97  E-value: 5.94e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6679731   419 GPVIRAQVRDTLKIVFKNMASRPYSIYPHGVTFSPYEDGINSSSTsgshttiRPVQPGETFTYkwnilEFDeptendaqc 498
Cdd:cd13860   31 GPTIEVTEGDRVRILVTNELPEPTTVHWHGLPVPNGMDGVPGITQ-------PPIQPGETFTY-----EFT--------- 89

                         90       100
                 ....*....|....*....|....*....
gi 6679731   499 LTRP----YYSDVDVTRDIASGLIGLLLI 523
Cdd:cd13860   90 AKQAgtymYHSHVDEAKQEDMGLYGAFIV 118
SufI COG2132
Multicopper oxidase with three cupredoxin domains (includes cell division protein FtsP and ...
 1603-1826 9.48e-08

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


Pssm-ID: 441735 [Multi-domain]  Cd Length: 423  Bit Score: 56.87  E-value: 9.48e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6679731  1603 ILGPVIRAEVDDVIQVRFKNLASRPYSLHAHGL--SYEkssegktyEDESPEwfqedDAVQPNSSYTYVWHATKRSG--- 1677
Cdd:COG2132   42 YPGPTIRVREGDRVRVRVTNRLPEPTTVHWHGLrvPNA--------MDGVPG-----DPIAPGETFTYEFPVPQPAGtyw 108

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6679731  1678 --PENPGSacrawayySAVNVERdihsGLIGPLLIcRKGtlhmERNLPMDMREFVLLF--MVFDEKKSWYYEKSKGSRRI 1753
Cdd:COG2132  109 yhPHTHGS--------TAEQVYR----GLAGALIV-EDP----EEDLPRYDRDIPLVLqdWRLDDDGQLLYPMDAAMGGR 171

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6679731  1754 ESPeeknahkFYAINGMIynLPGLRMYEQEWVRLHLLNMGGSR----------DIHVVHFHGQTLldnrTKQHQLGVWPL 1823
Cdd:COG2132  172 LGD-------TLLVNGRP--NPTLEVRPGERVRLRLLNASNARiyrlalsdgrPFTVIATDGGLL----PAPVEVDELLL 238


                 ...
gi 6679731  1824 LPG 1826
Cdd:COG2132  239 APG 241
CuRO_4_FV_like cd14454
The fourth cupredoxin domain of coagulation factor V and similar proteins; Factor V is an ...
 1732-1866 9.85e-08

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: 53.34  E-value: 9.85e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6679731  1732 LFMVFDEKKSWYYEKSKgSRRIESPEE--KNAHKFY------AINGMIY-NLPGLRMYEQEWVRLHLLNMGGSRDIHVVH 1802
Cdd:cd14454    7 VFAVFDENKSWYLEENI-NKYCSNPNNvkKDDPKFYksnimpTINGYAYeSSAPLGFCHSEVVQWHISSVGTQDEIITVH 85

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 6679731  1803 FHGQTLLDNRTKQHQLGVWPLlpgSFKTLEMKASKPGWWLLDTEVGENQVAGMQTPFLiiDKEC 1866
Cdd:cd14454   86 LSGHTFRYKGKHEDTLNLFPM---SGESITVTMDNLGTWLLGSFGSSKKSKGLRVRFT--DVIC 144
CuRO_1_2DMCO_NIR_like_2 cd14449
The cupredoxin domain 1 of a two-domain laccase related to nitrite reductase; The two-domain ...
 1605-1713 1.03e-07

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


Pssm-ID: 259991 [Multi-domain]  Cd Length: 135  Bit Score: 53.04  E-value: 1.03e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6679731  1605 GPVIRAEVDDVIQVRFKNLASRPYSLHAHGLSYEKSSEGkTYEDESpewfqeddAVQPNSSYTYVW--HATKR--SGPEN 1680
Cdd:cd14449   29 GPVIEVREGDTLKILFRNTLDVPASLHPHGVDYTTASDG-TGMNAS--------IVAPGDTRIYTWrtHGGYRraDGSWA 99

                         90       100       110
                 ....*....|....*....|....*....|....*...
gi 6679731  1681 PGSAcRAWAYYSAVnVERD-----IHSGLIGPLLICRK 1713
Cdd:cd14449  100 EGTA-GYWHYHDHV-FGTEhgtegLSRGLYGALIVRRV 135
SufI COG2132
Multicopper oxidase with three cupredoxin domains (includes cell division protein FtsP and ...
 81-257 1.16e-07

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


Pssm-ID: 441735 [Multi-domain]  Cd Length: 423  Bit Score: 56.48  E-value: 1.16e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6679731    81 NSGLLGPTLYAEVGDVIKVHFRNKADKPLSIHPQGIKYSkfsegASYADHTFPaerkddAVAPGEEYTYEWivsedsgpT 160
Cdd:COG2132   39 NGQYPGPTIRVREGDRVRVRVTNRLPEPTTVHWHGLRVP-----NAMDGVPGD------PIAPGETFTYEF--------P 99

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6679731   161 PDDPPClTHIYYSYENLTQDFN--SGLIGPLLIckkgtltEDG---------------TQKMFDKQHVLLFAVFDESKSR 223
Cdd:COG2132  100 VPQPAG-TYWYHPHTHGSTAEQvyRGLAGALIV-------EDPeedlprydrdiplvlQDWRLDDDGQLLYPMDAAMGGR 171

                        170       180       190
                 ....*....|....*....|....*....|....
gi 6679731   224 SQSpslMYTINGfvnKTMPDITVCAHDHVSWHLI 257
Cdd:COG2132  172 LGD---TLLVNG---RPNPTLEVRPGERVRLRLL 199
CuRO_1_AAO cd13845
The first cupredoxin domain of plant Ascorbate oxidase; Ascorbate oxidase catalyzes the ...
 81-191 2.17e-06

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


Pssm-ID: 259914 [Multi-domain]  Cd Length: 120  Bit Score: 48.60  E-value: 2.17e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6679731    81 NSGLLGPTLYAEVGDVIKVHFRNK-ADKPLSIHPQGIKyskfSEGASYADHTfpAERKDDAVAPGEEYTYEWIVsedsgp 159
Cdd:cd13845   25 NGQFPGPTIRATAGDTIVVELENKlPTEGVAIHWHGIR----QRGTPWADGT--ASVSQCPINPGETFTYQFVV------ 92

                         90       100       110
                 ....*....|....*....|....*....|..
gi 6679731   160 tpDDPPclTHIYYSYENLTQdfNSGLIGPLLI 191
Cdd:cd13845   93 --DRPG--TYFYHGHYGMQR--SAGLYGSLIV 118
CuRO_D1_2dMcoN_like cd13859
The first cupredoxin domain of bacterial two domain multicopper oxidase McoN and similar ...
 419-483 4.55e-06

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: 47.86  E-value: 4.55e-06
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 6679731   419 GPVIRAQVRDTLKIVFKNMASRPYSIYPHGV--TFSPYEDGINSSSTsgshttiRPVQPGETFTYKW 483
Cdd:cd13859   31 GPLIHVKEGDDLVVHVTNNTTLPHTIHWHGVlqMGSWKMDGVPGVTQ-------PAIEPGESFTYKF 90
CuRO_1_2DMCO_NIR_like_2 cd14449
The cupredoxin domain 1 of a two-domain laccase related to nitrite reductase; The two-domain ...
 419-483 6.76e-06

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


Pssm-ID: 259991 [Multi-domain]  Cd Length: 135  Bit Score: 47.65  E-value: 6.76e-06
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 6679731   419 GPVIRAQVRDTLKIVFKNMASRPYSIYPHGVTFSPYEDGINSSSTSgshttirpVQPGETFTYKW 483
Cdd:cd14449   29 GPVIEVREGDTLKILFRNTLDVPASLHPHGVDYTTASDGTGMNASI--------VAPGDTRIYTW 85
CuRO_1_Diphenol_Ox cd13857
The first cupredoxin domain of fungal laccase, diphenol oxidase; Diphenol oxidase belongs to ...
 419-485 8.19e-06

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


Pssm-ID: 259926 [Multi-domain]  Cd Length: 119  Bit Score: 46.87  E-value: 8.19e-06
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 6679731   419 GPVIRAQVRDTLKIVFKNMASRPYSIYPHGVTF--SPYEDGINSSSTSgshttirPVQPGETFTYKWNI 485
Cdd:cd13857   30 GPLIEANQGDRIVVHVTNELDEPTSIHWHGLFQngTNWMDGTAGITQC-------PIPPGGSFTYNFTV 91
CuRO_1_CumA_like cd13861
The first cupredoxin domain of CumA like multicopper oxidase; This multicopper oxidase (MCO) ...
 1602-1710 1.05e-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: 46.46  E-value: 1.05e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6679731  1602 GILGPVIRAEVDDVIQVRFKNLASRPYSLHAHGLSYEKSSEGktyedeSPEWFQedDAVQPNSSYTYvwhatkRSGPENP 1681
Cdd:cd13861   28 QVPGPELRVRQGDTLRVRLTNRLPEPTTIHWHGLRLPNAMDG------VPGLTQ--PPVPPGESFTY------EFTPPDA 93

                         90       100
                 ....*....|....*....|....*....
gi 6679731  1682 GSACrawaYYSAVNVERDIHSGLIGPLLI 1710
Cdd:cd13861   94 GTYW----YHPHVGSQEQLDRGLYGPLIV 118
CuRO_1_2DMCO_NIR_like cd11024
The cupredoxin domain 1 of a two-domain laccase related to nitrite reductase; The two-domain ...
 1605-1710 1.73e-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: 46.11  E-value: 1.73e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6679731  1605 GPVIRAEVDDVIQVRFKNLASRPYSLHAHGLSYEKssegktyedespewfqEDDA----VQPNSSYTYVWHATKrsgpen 1680
Cdd:cd11024   32 GPTLRATEGDLVRIHFINTGDHPHTIHFHGIHDAA----------------MDGTglgpIMPGESFTYEFVAEP------ 89

                         90       100       110
                 ....*....|....*....|....*....|.
gi 6679731  1681 PGsacrAWAYYSAVN-VERDIHSGLIGPLLI 1710
Cdd:cd11024   90 AG----THLYHCHVQpLKEHIAMGLYGAFIV 116
CuRO_1_2dMco_1 cd13860
The first cupredoxin domain of bacteria two domain multicopper oxidase; This subfamily ...
 86-191 2.50e-05

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: 45.65  E-value: 2.50e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6679731    86 GPTLYAEVGDVIKVHFRNKADKPLSIHPQGIKYSKFSEGasyadhtfPAERKDDAVAPGEEYTYEWIVsEDSGptpddpp 165
Cdd:cd13860   31 GPTIEVTEGDRVRILVTNELPEPTTVHWHGLPVPNGMDG--------VPGITQPPIQPGETFTYEFTA-KQAG------- 94

                         90       100
                 ....*....|....*....|....*.
gi 6679731   166 clTHIYYSYENLTQDFNSGLIGPLLI 191
Cdd:cd13860   95 --TYMYHSHVDEAKQEDMGLYGAFIV 118
CuRO_1_CumA_like cd13861
The first cupredoxin domain of CumA like multicopper oxidase; This multicopper oxidase (MCO) ...
 416-523 2.82e-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: 45.30  E-value: 2.82e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6679731   416 GILGPVIRAQVRDTLKIVFKNMASRPYSIYPHGVTFSPYEDGINSSSTSgshttirPVQPGETFTYkwnilEFDEPtenD 495
Cdd:cd13861   28 QVPGPELRVRQGDTLRVRLTNRLPEPTTIHWHGLRLPNAMDGVPGLTQP-------PVPPGESFTY-----EFTPP---D 92

                         90       100
                 ....*....|....*....|....*...
gi 6679731   496 AQclTRPYYSDVDVTRDIASGLIGLLLI 523
Cdd:cd13861   93 AG--TYWYHPHVGSQEQLDRGLYGPLIV 118
CuRO_3_LCC_like cd04207
Cupredoxin domain 3 of laccase-like multicopper oxidases; including laccase, CueO, spore coat ...
 1753-1859 4.06e-05

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


Pssm-ID: 259870 [Multi-domain]  Cd Length: 132  Bit Score: 45.14  E-value: 4.06e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6679731  1753 IESPEEKNAHKFYAINGMIY-----NLPGLRMYEQEWVRLHLLNMGGSRDIHVVHFHGQT---------------LLDNR 1812
Cdd:cd04207    8 LSQTGAPDGTTRWVINGMPFkegdaNTDIFSVEAGDVVEIVLINAGNHDMQHPFHLHGHSfwvlgsgggpfdaplNLTNP 87

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*..
gi 6679731  1813 TKQHqlgVWPLLPGSFKTLEMKASKPGWWLLDTEVGENQVAGMQTPF 1859
Cdd:cd04207   88 PWRD---TVLVPPGGWVVIRFKADNPGVWMLHCHILEHEDAGMMTVF 131
PLN02191 PLN02191
L-ascorbate oxidase
 81-201 4.20e-05

L-ascorbate oxidase


Pssm-ID: 177843 [Multi-domain]  Cd Length: 574  Bit Score: 48.86  E-value: 4.20e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6679731     81 NSGLLGPTLYAEVGDVIKVHFRNK-ADKPLSIHPQGIKyskfSEGASYADHTfpAERKDDAVAPGEEYTYEWIVsEDSGp 159
Cdd:PLN02191   48 NGQFPGPTIDAVAGDTIVVHLTNKlTTEGLVIHWHGIR----QKGSPWADGA--AGVTQCAINPGETFTYKFTV-EKPG- 119

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 6679731    160 tpddppclTHIYYSYENLTQdfNSGLIGPLLIC----KKGTLTEDG 201
Cdd:PLN02191  120 --------THFYHGHYGMQR--SAGLYGSLIVDvakgPKERLRYDG 155
Cu-oxidase_3 pfam07732
Multicopper oxidase; This entry contains many divergent copper oxidase-like domains that are ...
 417-485 5.78e-05

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


Pssm-ID: 462247 [Multi-domain]  Cd Length: 119  Bit Score: 44.54  E-value: 5.78e-05
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 6679731     417 ILGPVIRAQVRDTLKIVFKNMASRPYSIYPHG--VTFSPYEDGINSSSTsgshttiRPVQPGETFTYKWNI 485
Cdd:pfam07732   24 FPGPTIRVREGDTVVVNVTNNLDEPTSIHWHGlqQRGTPWMDGVPGVTQ-------CPIPPGQSFTYRFQV 87
CuRO_D1_2dMcoN_like cd13859
The first cupredoxin domain of bacterial two domain multicopper oxidase McoN and similar ...
 1605-1710 6.32e-05

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


Pssm-ID: 259928 [Multi-domain]  Cd Length: 122  Bit Score: 44.39  E-value: 6.32e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6679731  1605 GPVIRA-EVDDVIqVRFKNLASRPYSLHAHGLsYEKSSegkTYEDESPEWFQEddAVQPNSSYTYVWHAtkrsgpENPGS 1683
Cdd:cd13859   31 GPLIHVkEGDDLV-VHVTNNTTLPHTIHWHGV-LQMGS---WKMDGVPGVTQP--AIEPGESFTYKFKA------ERPGT 97

                         90       100
                 ....*....|....*....|....*...
gi 6679731  1684 acrAWaYYSAVNV-ERDIHSGLIGPLLI 1710
Cdd:cd13859   98 ---LW-YHCHVNVnEHVGMRGMWGPLIV 121
CuRO_1_Diphenol_Ox cd13857
The first cupredoxin domain of fungal laccase, diphenol oxidase; Diphenol oxidase belongs to ...
 1605-1710 7.66e-05

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: 44.17  E-value: 7.66e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6679731  1605 GPVIRAEVDDVIQVRFKNLASRPYSLHAHGLsYEkssEGKTYEDESPEWFQedDAVQPNSSYTYVWHATKRSGPenpgsa 1684
Cdd:cd13857   30 GPLIEANQGDRIVVHVTNELDEPTSIHWHGL-FQ---NGTNWMDGTAGITQ--CPIPPGGSFTYNFTVDGQYGT------ 97

                         90       100
                 ....*....|....*....|....*...
gi 6679731  1685 crAW--AYYSAVNVErdihsGLIGPLLI 1710
Cdd:cd13857   98 --YWyhSHYSTQYAD-----GLVGPLIV 118
CuRO_1_AAO cd13845
The first cupredoxin domain of plant Ascorbate oxidase; Ascorbate oxidase catalyzes the ...
 419-523 8.93e-05

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


Pssm-ID: 259914 [Multi-domain]  Cd Length: 120  Bit Score: 43.97  E-value: 8.93e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6679731   419 GPVIRAQVRDTLKIVFKN-MASRPYSIYPHGV--TFSPYEDGINSSSTSgshttirPVQPGETFTYKWNIlefDEPTend 495
Cdd:cd13845   30 GPTIRATAGDTIVVELENkLPTEGVAIHWHGIrqRGTPWADGTASVSQC-------PINPGETFTYQFVV---DRPG--- 96

                         90       100
                 ....*....|....*....|....*...
gi 6679731   496 aqclTRPYYSDVDVTRdiASGLIGLLLI 523
Cdd:cd13845   97 ----TYFYHGHYGMQR--SAGLYGSLIV 118
Cu-oxidase_3 pfam07732
Multicopper oxidase; This entry contains many divergent copper oxidase-like domains that are ...
 1603-1677 1.81e-04

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


Pssm-ID: 462247 [Multi-domain]  Cd Length: 119  Bit Score: 43.00  E-value: 1.81e-04
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 6679731    1603 ILGPVIRAEVDDVIQVRFKNLASRPYSLHAHGLSYEKSSegktYEDESPEWFQedDAVQPNSSYTYVWHATKRSG 1677
Cdd:pfam07732   24 FPGPTIRVREGDTVVVNVTNNLDEPTSIHWHGLQQRGTP----WMDGVPGVTQ--CPIPPGQSFTYRFQVKQQAG 92
CuRO_1_Fet3p cd13851
The first Cupredoxin domain of multicopper oxidase Fet3P; Fet3p catalyzes the ferroxidase ...
 87-191 2.49e-04

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: 42.64  E-value: 2.49e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6679731    87 PTLYAEVGDVIKVHFRNK-ADKPLSIHPQGIkyskFSEGASYADHtfPAERKDDAVAPGEEYTYEWIVSEDSGptpddpp 165
Cdd:cd13851   32 PPIEVNKGDTVVIHATNSlGDQPTSLHFHGL----FQNGTNYMDG--PVGVTQCPIPPGQSFTYEFTVDTQVG------- 98

                         90       100
                 ....*....|....*....|....*.
gi 6679731   166 clTHIYYSYeNLTQdFNSGLIGPLLI 191
Cdd:cd13851   99 --TYWYHSH-DGGQ-YPDGLRGPFII 120
CuRO_1_LCC_plant cd13849
The first cupredoxin domain of plant laccases; Laccase is a blue multicopper oxidase (MCO) ...
 81-158 2.81e-04

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


Pssm-ID: 259918 [Multi-domain]  Cd Length: 117  Bit Score: 42.63  E-value: 2.81e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6679731    81 NSGLLGPTLYAEVGDVIKVHFRNKADKPLSIHPQGIK--YSKFSEGASYADHTfPAErkddavaPGEEYTYEWIVSEDSG 158
Cdd:cd13849   23 NGQFPGPTIRVHEGDTVVVNVTNRSPYNITIHWHGIRqlRSGWADGPAYITQC-PIQ-------PGQSYTYRFTVTGQEG 94
CuRO_1_Abr2_like cd13850
The first cupredoxin domain of a group of fungal Laccases similar to Abr2 from Aspergillus ...
 1605-1677 3.11e-04

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: 42.29  E-value: 3.11e-04
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 6679731  1605 GPVIRAEVDDVIQVRFKNLASRPYSLHAHGLsyekSSEGKTYEDESPEWFQEddAVQPNSSYTYVWHATKRSG 1677
Cdd:cd13850   28 GPPIILDEGDEVEILVTNNLPVNTTIHFHGI----LQRGTPWSDGVPGVTQW--PIQPGGSFTYRWKAEDQYG 94
CuRO_1_LCC_plant cd13849
The first cupredoxin domain of plant laccases; Laccase is a blue multicopper oxidase (MCO) ...
 419-485 5.43e-04

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


Pssm-ID: 259918 [Multi-domain]  Cd Length: 117  Bit Score: 41.86  E-value: 5.43e-04
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 6679731   419 GPVIRAQVRDTLKIVFKNMASRPYSIYPHGV--TFSPYEDGINSSSTsgshttiRPVQPGETFTYKWNI 485
Cdd:cd13849   28 GPTIRVHEGDTVVVNVTNRSPYNITIHWHGIrqLRSGWADGPAYITQ-------CPIQPGQSYTYRFTV 89
CuRO_1_Abr2_like cd13850
The first cupredoxin domain of a group of fungal Laccases similar to Abr2 from Aspergillus ...
 419-485 8.66e-04

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: 41.13  E-value: 8.66e-04
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 6679731   419 GPVIRAQVRDTLKIVFKNMASRPYSIYPHGV--TFSPYEDGINSSSTsgshttiRPVQPGETFTYKWNI 485
Cdd:cd13850   28 GPPIILDEGDEVEILVTNNLPVNTTIHFHGIlqRGTPWSDGVPGVTQ-------WPIQPGGSFTYRWKA 89
CuRO_1_CopA cd13848
The first cupredoxin domain of CopA copper resistance protein family; CopA is a multicopper ...
 81-191 8.92e-04

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


Pssm-ID: 259917 [Multi-domain]  Cd Length: 116  Bit Score: 41.11  E-value: 8.92e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6679731    81 NSGLLGPTLYAEVGDVIKVHFRNKADKPLSIHPQGIKYSKFSEGASYAdhTFPaerkddAVAPGEEYTYEWIVSEdSGpt 160
Cdd:cd13848   25 NGQVPGPLLRFKEGDDATIRVHNRLDEDTSIHWHGLLLPNDMDGVPGL--SFP------GIKPGETFTYRFPVRQ-SG-- 93

                         90       100       110
                 ....*....|....*....|....*....|.
gi 6679731   161 pddppclTHIYYSYENLtQDfNSGLIGPLLI 191
Cdd:cd13848   94 -------TYWYHSHSGL-QE-QTGLYGPIII 115
SufI COG2132
Multicopper oxidase with three cupredoxin domains (includes cell division protein FtsP and ...
 417-485 1.21e-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: 43.77  E-value: 1.21e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 6679731   417 ILGPVIRAQVRDTLKIVFKNMASRPYSIYPHGVTFSPYEDGINSsstsgshttiRPVQPGETFTYKWNI 485
Cdd:COG2132   42 YPGPTIRVREGDRVRVRVTNRLPEPTTVHWHGLRVPNAMDGVPG----------DPIAPGETFTYEFPV 100
CuRO_1_McoC_like cd13855
The first cupredoxin domain of a multicopper oxidase McoC and similar proteins; This family ...
 419-485 1.56e-03

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


Pssm-ID: 259924 [Multi-domain]  Cd Length: 121  Bit Score: 40.54  E-value: 1.56e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 6679731   419 GPVIRAQVRDTLKIVFKNMASRPYSIYPHGVTFSPYEDGinssstsgshTTIRPVQPGETFTYKWNI 485
Cdd:cd13855   32 GPLIEVFEGDTVEITFRNRLPEPTTVHWHGLPVPPDQDG----------NPHDPVAPGNDRVYRFTL 88
CuRO_1_2dMco_1 cd13860
The first cupredoxin domain of bacteria two domain multicopper oxidase; This subfamily ...
 1605-1710 1.66e-03

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


Pssm-ID: 259929 [Multi-domain]  Cd Length: 119  Bit Score: 40.26  E-value: 1.66e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6679731  1605 GPVIRAEVDDVIQVRFKNLASRPYSLHAHGLSYEKSSEGktyedeSPEWFQedDAVQPNSSYTYVWHATKrsgpenPGSa 1684
Cdd:cd13860   31 GPTIEVTEGDRVRILVTNELPEPTTVHWHGLPVPNGMDG------VPGITQ--PPIQPGETFTYEFTAKQ------AGT- 95

                         90       100
                 ....*....|....*....|....*.
gi 6679731  1685 craWAYYSAVNVERDIHSGLIGPLLI 1710
Cdd:cd13860   96 ---YMYHSHVDEAKQEDMGLYGAFIV 118
CuRO_1_MaLCC_like cd13854
The first cupredoxin domain of the fungal laccases similar to Ma-LCC from Melanocarpus ...
 419-488 1.83e-03

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


Pssm-ID: 259923 [Multi-domain]  Cd Length: 122  Bit Score: 40.30  E-value: 1.83e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 6679731   419 GPVIRAQVRDTLKI-VFKNMASRPYSIYPHGVT--FSPYEDGINSSSTSgshttirPVQPGETFTYKWNILEF 488
Cdd:cd13854   33 GPLIEANWGDTIEVtVINKLQDNGTSIHWHGIRqlNTNWQDGVPGVTEC-------PIAPGDTRTYRFRATQY 98
ascorbase TIGR03388
L-ascorbate oxidase, plant type; Members of this protein family are the copper-containing ...
 86-191 1.87e-03

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


Pssm-ID: 274555 [Multi-domain]  Cd Length: 541  Bit Score: 43.20  E-value: 1.87e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6679731      86 GPTLYAEVGDVIKVHFRNK-ADKPLSIHPQGIKyskfSEGASYADHTfpAERKDDAVAPGEEYTYEWIVsedsgptpDDP 164
Cdd:TIGR03388   31 GPTIRAQAGDTIVVELTNKlHTEGVVIHWHGIR----QIGTPWADGT--AGVTQCAINPGETFIYNFVV--------DRP 96

                           90       100
                   ....*....|....*....|....*..
gi 6679731     165 PclTHIYYSYENLTQdfNSGLIGPLLI 191
Cdd:TIGR03388   97 G--TYFYHGHYGMQR--SAGLYGSLIV 119
CuRO_1_Tv-LCC_like cd13856
The first cupredoxin domain of fungal laccases similar to Tv-LCC from Trametes versicolor; ...
 81-191 2.17e-03

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


Pssm-ID: 259925 [Multi-domain]  Cd Length: 125  Bit Score: 40.01  E-value: 2.17e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6679731    81 NSGLLGPTLYAEVGDVIKVHFRNK-----ADKPLSIHPQGIkyskFSEGASYADHtfPAERKDDAVAPGEEYTYEWIVSE 155
Cdd:cd13856   25 NGQFPGPLITANKGDTFRITVVNQltdptMRRSTSIHWHGI----FQHGTNYADG--PAFVTQCPIAPNHSFTYDFTAGD 98

                         90       100       110
                 ....*....|....*....|....*....|....*.
gi 6679731   156 DSGptpddppclTHIYYSYenLTQDFNSGLIGPLLI 191
Cdd:cd13856   99 QAG---------TFWYHSH--LSTQYCDGLRGPLVI 123
PLN02191 PLN02191
L-ascorbate oxidase
 419-532 2.23e-03

L-ascorbate oxidase


Pssm-ID: 177843 [Multi-domain]  Cd Length: 574  Bit Score: 43.08  E-value: 2.23e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6679731    419 GPVIRAQVRDTLKIVFKN-MASRPYSIYPHGVT--FSPYEDGINSSSTSgshttirPVQPGETFTYKWNIlefDEPTend 495
Cdd:PLN02191   53 GPTIDAVAGDTIVVHLTNkLTTEGLVIHWHGIRqkGSPWADGAAGVTQC-------AINPGETFTYKFTV---EKPG--- 119

                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 6679731    496 aqclTRPYYSDVDVTRdiASGLIGLLLICKSRSLDQR 532
Cdd:PLN02191  120 ----THFYHGHYGMQR--SAGLYGSLIVDVAKGPKER 150
Cu-oxidase_2 pfam07731
Multicopper oxidase; This entry contains many divergent copper oxidase-like domains that are ...
 1762-1865 2.34e-03

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


Pssm-ID: 462246 [Multi-domain]  Cd Length: 138  Bit Score: 40.50  E-value: 2.34e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6679731    1762 HKFYAINGMIY--NLPGLRMYEQEWVRLHLLNMGGsrDIHVVHFHG------------QTLLDNRTKQHQLGVW----PL 1823
Cdd:pfam07731   19 RNDWAINGLLFppNTNVITLPYGTVVEWVLQNTTT--GVHPFHLHGhsfqvlgrgggpWPEEDPKTYNLVDPVRrdtvQV 96

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|..
gi 6679731    1824 LPGSFKTLEMKASKPGWWLLDTEVGENQVAGMQTPFLIIDKE 1865
Cdd:pfam07731   97 PPGGWVAIRFRADNPGVWLFHCHILWHLDQGMMGQFVVRPGD 138
CuRO_1_CuNIR_like cd04201
Cupredoxin domain 1 of Copper-containing nitrite reductase and two-domain laccase; ...
 1769-1839 2.42e-03

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


Pssm-ID: 259864 [Multi-domain]  Cd Length: 120  Bit Score: 39.78  E-value: 2.42e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 6679731  1769 GMIYN--LPG--LRMYEQEWVRLHLLNMGGSRDIHVVHFHGQTlldnrTKQHQLGVWPLLPGSFKTLEMKASKPG 1839
Cdd:cd04201   23 YWTFDgdIPGpmLRVREGDTVELHFSNNPSSTMPHNIDFHAAT-----GAGGGAGATFIAPGETSTFSFKATQPG 92
CuRO_1_McoP_like cd13852
The first cupredoxin domain of multicopper oxidase McoP and similar proteins; This family ...
 85-158 4.58e-03

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


Pssm-ID: 259921 [Multi-domain]  Cd Length: 114  Bit Score: 38.81  E-value: 4.58e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 6679731    85 LGPTLYAEVGDVIKVHFRNKADKPLSIHPQGIKYSKFSEGasyadHtfPAerkdDAVAPGEEYTYEWIVSEDSG 158
Cdd:cd13852   23 LGPILRLRKGQKVRITFKNNLPEPTIIHWHGLHVPAAMDG-----H--PR----YAIDPGETYVYEFEVLNRAG 85
CuRO_1_McoC_like cd13855
The first cupredoxin domain of a multicopper oxidase McoC and similar proteins; This family ...
 81-160 4.72e-03

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


Pssm-ID: 259924 [Multi-domain]  Cd Length: 121  Bit Score: 39.00  E-value: 4.72e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6679731    81 NSGLLGPTLYAEVGDVIKVHFRNKADKPLSIHPQGIKYSKFSEGASYadhtfpaerkdDAVAPGEEYTYEWIVSEDSGPT 160
Cdd:cd13855   27 NGSVPGPLIEVFEGDTVEITFRNRLPEPTTVHWHGLPVPPDQDGNPH-----------DPVAPGNDRVYRFTLPQDSAGT 95
 
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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